data_9BZF
# 
_entry.id   9BZF 
# 
_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   9BZF         pdb_00009bzf 10.2210/pdb9bzf/pdb 
WWPDB D_1000284446 ?            ?                   
EMDB  EMD-45066    ?            ?                   
# 
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                        9BZF 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        
'Class 28 model for combined refinement of Bacillus subtilis ribonucleotide reductase complex' 
_pdbx_database_related.db_id          EMD-45066 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              nozomi.ando@cornell.edu 
_pdbx_contact_author.name_first         Nozomi 
_pdbx_contact_author.name_last          Ando 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7062-1644 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, D.'       1 0000-0002-3879-039X 
'Thomas, W.C.' 2 0000-0001-5490-4900 
'Burnim, A.A.' 3 0000-0002-9962-1397 
'Ando, N.'     4 0000-0001-7062-1644 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                2458 
_citation.page_last                 2458 
_citation.title                     
'Conformational landscapes of a class I ribonucleotide reductase complex during turnover reveal intrinsic dynamics and asymmetry.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57735-4 
_citation.pdbx_database_id_PubMed   40075098 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xu, D.'       1 ? 
primary 'Thomas, W.C.' 2 ? 
primary 'Burnim, A.A.' 3 ? 
primary 'Ando, N.'     4 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Ribonucleoside-diphosphate reductase subunit alpha' 80791.469 2 1.17.4.1 ? ? ? 
2 polymer     man 'Ribonucleoside-diphosphate reductase subunit beta'  40720.992 2 1.17.4.1 ? ? ? 
3 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"                          507.181   2 ?        ? ? ? 
4 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE"                           443.201   2 ?        ? ? ? 
5 non-polymer syn "THYMIDINE-5'-TRIPHOSPHATE"                          482.168   2 ?        ? ? ? 
6 non-polymer syn 'MAGNESIUM ION'                                      24.305    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 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
4 "GUANOSINE-5'-DIPHOSPHATE"  GDP 
5 "THYMIDINE-5'-TRIPHOSPHATE" TTP 
6 'MAGNESIUM ION'             MG  
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 
GDP 'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O11 P2' 443.201 
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 GDP ? ? GDP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ATP ? ? ATP ? ? '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 ATP 1 801 701 ATP ATP A . 
F 4 GDP 1 802 702 GDP GDP A . 
G 5 TTP 1 803 703 TTP TTP A . 
H 6 MG  1 804 704 MG  MG  A . 
I 5 TTP 1 801 701 TTP TTP B . 
J 6 MG  1 802 702 MG  MG  B . 
K 3 ATP 1 803 703 ATP ATP B . 
L 4 GDP 1 804 704 GDP GDP 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                   9BZF 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BZF 
_struct.title                        'Class 28 model for combined refinement 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        9BZF 
_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 5 ? 
J N N 6 ? 
K N N 3 ? 
L N N 4 ? 
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 9BZF A 1  ? 700 ? P50620 1 ? 700 ? 1 700 
2 1 9BZF B 1  ? 700 ? P50620 1 ? 700 ? 1 700 
3 2 9BZF C 22 ? 350 ? P50621 1 ? 329 ? 1 329 
4 2 9BZF 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 9BZF MET C 1  ? UNP P50621 ? ? 'initiating methionine' -20 1  
3 9BZF GLY C 2  ? UNP P50621 ? ? 'expression tag'        -19 2  
3 9BZF SER C 3  ? UNP P50621 ? ? 'expression tag'        -18 3  
3 9BZF SER C 4  ? UNP P50621 ? ? 'expression tag'        -17 4  
3 9BZF HIS C 5  ? UNP P50621 ? ? 'expression tag'        -16 5  
3 9BZF HIS C 6  ? UNP P50621 ? ? 'expression tag'        -15 6  
3 9BZF HIS C 7  ? UNP P50621 ? ? 'expression tag'        -14 7  
3 9BZF HIS C 8  ? UNP P50621 ? ? 'expression tag'        -13 8  
3 9BZF HIS C 9  ? UNP P50621 ? ? 'expression tag'        -12 9  
3 9BZF HIS C 10 ? UNP P50621 ? ? 'expression tag'        -11 10 
3 9BZF SER C 11 ? UNP P50621 ? ? 'expression tag'        -10 11 
3 9BZF SER C 12 ? UNP P50621 ? ? 'expression tag'        -9  12 
3 9BZF GLY C 13 ? UNP P50621 ? ? 'expression tag'        -8  13 
3 9BZF LEU C 14 ? UNP P50621 ? ? 'expression tag'        -7  14 
3 9BZF VAL C 15 ? UNP P50621 ? ? 'expression tag'        -6  15 
3 9BZF PRO C 16 ? UNP P50621 ? ? 'expression tag'        -5  16 
3 9BZF ARG C 17 ? UNP P50621 ? ? 'expression tag'        -4  17 
3 9BZF GLY C 18 ? UNP P50621 ? ? 'expression tag'        -3  18 
3 9BZF SER C 19 ? UNP P50621 ? ? 'expression tag'        -2  19 
3 9BZF HIS C 20 ? UNP P50621 ? ? 'expression tag'        -1  20 
3 9BZF MET C 21 ? UNP P50621 ? ? 'expression tag'        0   21 
4 9BZF MET D 1  ? UNP P50621 ? ? 'initiating methionine' -20 22 
4 9BZF GLY D 2  ? UNP P50621 ? ? 'expression tag'        -19 23 
4 9BZF SER D 3  ? UNP P50621 ? ? 'expression tag'        -18 24 
4 9BZF SER D 4  ? UNP P50621 ? ? 'expression tag'        -17 25 
4 9BZF HIS D 5  ? UNP P50621 ? ? 'expression tag'        -16 26 
4 9BZF HIS D 6  ? UNP P50621 ? ? 'expression tag'        -15 27 
4 9BZF HIS D 7  ? UNP P50621 ? ? 'expression tag'        -14 28 
4 9BZF HIS D 8  ? UNP P50621 ? ? 'expression tag'        -13 29 
4 9BZF HIS D 9  ? UNP P50621 ? ? 'expression tag'        -12 30 
4 9BZF HIS D 10 ? UNP P50621 ? ? 'expression tag'        -11 31 
4 9BZF SER D 11 ? UNP P50621 ? ? 'expression tag'        -10 32 
4 9BZF SER D 12 ? UNP P50621 ? ? 'expression tag'        -9  33 
4 9BZF GLY D 13 ? UNP P50621 ? ? 'expression tag'        -8  34 
4 9BZF LEU D 14 ? UNP P50621 ? ? 'expression tag'        -7  35 
4 9BZF VAL D 15 ? UNP P50621 ? ? 'expression tag'        -6  36 
4 9BZF PRO D 16 ? UNP P50621 ? ? 'expression tag'        -5  37 
4 9BZF ARG D 17 ? UNP P50621 ? ? 'expression tag'        -4  38 
4 9BZF GLY D 18 ? UNP P50621 ? ? 'expression tag'        -3  39 
4 9BZF SER D 19 ? UNP P50621 ? ? 'expression tag'        -2  40 
4 9BZF HIS D 20 ? UNP P50621 ? ? 'expression tag'        -1  41 
4 9BZF 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   ? GLU A 15  ? PRO A 7   GLU A 15  1 ? 9  
HELX_P HELX_P2  AA2 GLN A 25  ? ASP A 39  ? GLN A 25  ASP A 39  1 ? 15 
HELX_P HELX_P3  AA3 ASN A 50  ? ASN A 61  ? ASN A 50  ASN A 61  1 ? 12 
HELX_P HELX_P4  AA4 GLU A 65  ? LEU A 71  ? GLU A 65  LEU A 71  1 ? 7  
HELX_P HELX_P5  AA5 SER A 73  ? LYS A 87  ? SER A 73  LYS A 87  1 ? 15 
HELX_P HELX_P6  AA6 SER A 93  ? TYR A 104 ? SER A 93  TYR A 104 1 ? 12 
HELX_P HELX_P7  AA7 ARG A 117 ? ASN A 131 ? ARG A 117 ASN A 131 1 ? 15 
HELX_P HELX_P8  AA8 ASP A 133 ? ASN A 146 ? ASP A 133 ASN A 146 1 ? 14 
HELX_P HELX_P9  AA9 SER A 152 ? ALA A 159 ? SER A 152 ALA A 159 1 ? 8  
HELX_P HELX_P10 AB1 SER A 178 ? LEU A 195 ? SER A 178 LEU A 195 1 ? 18 
HELX_P HELX_P11 AB2 LYS A 221 ? ALA A 237 ? LYS A 221 ALA A 237 1 ? 17 
HELX_P HELX_P12 AB3 ASP A 257 ? THR A 264 ? ASP A 257 THR A 264 1 ? 8  
HELX_P HELX_P13 AB4 PRO A 285 ? GLU A 294 ? PRO A 285 GLU A 294 1 ? 10 
HELX_P HELX_P14 AB5 TYR A 302 ? GLY A 311 ? TYR A 302 GLY A 311 1 ? 10 
HELX_P HELX_P15 AB6 HIS A 313 ? MET A 317 ? HIS A 313 MET A 317 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 318 ? ASN A 329 ? ASP A 318 ASN A 329 1 ? 12 
HELX_P HELX_P17 AB8 ASN A 338 ? GLY A 354 ? ASN A 338 GLY A 354 1 ? 17 
HELX_P HELX_P18 AB9 GLN A 361 ? LYS A 366 ? GLN A 361 LYS A 366 1 ? 6  
HELX_P HELX_P19 AC1 ILE A 416 ? HIS A 422 ? ILE A 416 HIS A 422 1 ? 7  
HELX_P HELX_P20 AC2 SER A 424 ? THR A 442 ? SER A 424 THR A 442 1 ? 19 
HELX_P HELX_P21 AC3 ALA A 448 ? LYS A 459 ? ALA A 448 LYS A 459 1 ? 12 
HELX_P HELX_P22 AC4 ASN A 467 ? ASN A 475 ? ASN A 467 ASN A 475 1 ? 9  
HELX_P HELX_P23 AC5 SER A 481 ? GLY A 511 ? SER A 481 GLY A 511 1 ? 31 
HELX_P HELX_P24 AC6 SER A 520 ? GLY A 525 ? SER A 520 GLY A 525 1 ? 6  
HELX_P HELX_P25 AC7 PHE A 528 ? THR A 534 ? PHE A 528 THR A 534 1 ? 7  
HELX_P HELX_P26 AC8 TYR A 540 ? PHE A 547 ? TYR A 540 PHE A 547 1 ? 8  
HELX_P HELX_P27 AC9 THR A 554 ? GLY A 569 ? THR A 554 GLY A 569 1 ? 16 
HELX_P HELX_P28 AD1 SER A 583 ? GLN A 588 ? SER A 583 GLN A 588 1 ? 6  
HELX_P HELX_P29 AD2 ASP A 633 ? GLN A 646 ? ASP A 633 GLN A 646 1 ? 14 
HELX_P HELX_P30 AD3 THR A 663 ? GLY A 678 ? THR A 663 GLY A 678 1 ? 16 
HELX_P HELX_P31 AD4 PRO B 7   ? GLU B 15  ? PRO B 7   GLU B 15  1 ? 9  
HELX_P HELX_P32 AD5 GLN B 25  ? TYR B 40  ? GLN B 25  TYR B 40  1 ? 16 
HELX_P HELX_P33 AD6 TYR B 40  ? THR B 45  ? TYR B 40  THR B 45  1 ? 6  
HELX_P HELX_P34 AD7 ASN B 50  ? ASN B 61  ? ASN B 50  ASN B 61  1 ? 12 
HELX_P HELX_P35 AD8 GLU B 65  ? LEU B 71  ? GLU B 65  LEU B 71  1 ? 7  
HELX_P HELX_P36 AD9 SER B 73  ? LYS B 87  ? SER B 73  LYS B 87  1 ? 15 
HELX_P HELX_P37 AE1 SER B 93  ? TYR B 104 ? SER B 93  TYR B 104 1 ? 12 
HELX_P HELX_P38 AE2 ARG B 117 ? ASN B 131 ? ARG B 117 ASN B 131 1 ? 15 
HELX_P HELX_P39 AE3 ASP B 133 ? ASN B 146 ? ASP B 133 ASN B 146 1 ? 14 
HELX_P HELX_P40 AE4 SER B 152 ? ALA B 159 ? SER B 152 ALA B 159 1 ? 8  
HELX_P HELX_P41 AE5 SER B 178 ? LEU B 195 ? SER B 178 LEU B 195 1 ? 18 
HELX_P HELX_P42 AE6 LYS B 221 ? ALA B 237 ? LYS B 221 ALA B 237 1 ? 17 
HELX_P HELX_P43 AE7 ASP B 238 ? GLN B 242 ? ASP B 238 GLN B 242 5 ? 5  
HELX_P HELX_P44 AE8 ASP B 257 ? THR B 264 ? ASP B 257 THR B 264 1 ? 8  
HELX_P HELX_P45 AE9 PRO B 285 ? ASP B 295 ? PRO B 285 ASP B 295 1 ? 11 
HELX_P HELX_P46 AF1 TYR B 302 ? GLY B 311 ? TYR B 302 GLY B 311 1 ? 10 
HELX_P HELX_P47 AF2 HIS B 313 ? MET B 317 ? HIS B 313 MET B 317 5 ? 5  
HELX_P HELX_P48 AF3 ASP B 318 ? ASN B 329 ? ASP B 318 ASN B 329 1 ? 12 
HELX_P HELX_P49 AF4 ASN B 338 ? GLY B 354 ? ASN B 338 GLY B 354 1 ? 17 
HELX_P HELX_P50 AF5 GLN B 361 ? LYS B 366 ? GLN B 361 LYS B 366 1 ? 6  
HELX_P HELX_P51 AF6 ILE B 416 ? HIS B 422 ? ILE B 416 HIS B 422 1 ? 7  
HELX_P HELX_P52 AF7 SER B 424 ? THR B 442 ? SER B 424 THR B 442 1 ? 19 
HELX_P HELX_P53 AF8 ALA B 448 ? LYS B 459 ? ALA B 448 LYS B 459 1 ? 12 
HELX_P HELX_P54 AF9 ASN B 467 ? ASN B 475 ? ASN B 467 ASN B 475 1 ? 9  
HELX_P HELX_P55 AG1 SER B 481 ? GLY B 511 ? SER B 481 GLY B 511 1 ? 31 
HELX_P HELX_P56 AG2 GLN B 516 ? GLY B 519 ? GLN B 516 GLY B 519 5 ? 4  
HELX_P HELX_P57 AG3 SER B 520 ? GLY B 525 ? SER B 520 GLY B 525 1 ? 6  
HELX_P HELX_P58 AG4 PHE B 528 ? THR B 534 ? PHE B 528 THR B 534 1 ? 7  
HELX_P HELX_P59 AG5 TYR B 540 ? PHE B 547 ? TYR B 540 PHE B 547 1 ? 8  
HELX_P HELX_P60 AG6 THR B 554 ? GLY B 569 ? THR B 554 GLY B 569 1 ? 16 
HELX_P HELX_P61 AG7 SER B 583 ? GLN B 588 ? SER B 583 GLN B 588 1 ? 6  
HELX_P HELX_P62 AG8 ASP B 633 ? GLN B 646 ? ASP B 633 GLN B 646 1 ? 14 
HELX_P HELX_P63 AG9 THR B 663 ? GLY B 678 ? THR B 663 GLY B 678 1 ? 16 
HELX_P HELX_P64 AH1 PHE C 38  ? GLN C 49  ? PHE C 17  GLN C 28  1 ? 12 
HELX_P HELX_P65 AH2 LEU C 52  ? ILE C 56  ? LEU C 31  ILE C 35  5 ? 5  
HELX_P HELX_P66 AH3 LEU C 58  ? GLY C 60  ? LEU C 37  GLY C 39  5 ? 3  
HELX_P HELX_P67 AH4 ASP C 61  ? TYR C 67  ? ASP C 40  TYR C 46  1 ? 7  
HELX_P HELX_P68 AH5 GLY C 69  ? THR C 93  ? GLY C 48  THR C 72  1 ? 25 
HELX_P HELX_P69 AH6 THR C 93  ? VAL C 102 ? THR C 72  VAL C 81  1 ? 10 
HELX_P HELX_P70 AH7 GLY C 104 ? VAL C 121 ? GLY C 83  VAL C 100 1 ? 18 
HELX_P HELX_P71 AH8 VAL C 121 ? ALA C 134 ? VAL C 100 ALA C 113 1 ? 14 
HELX_P HELX_P72 AH9 PRO C 135 ? ASN C 149 ? PRO C 114 ASN C 128 1 ? 15 
HELX_P HELX_P73 AI1 ASN C 149 ? ALA C 165 ? ASN C 128 ALA C 144 1 ? 17 
HELX_P HELX_P74 AI2 ASP C 170 ? PHE C 187 ? ASP C 149 PHE C 166 1 ? 18 
HELX_P HELX_P75 AI3 PHE C 189 ? GLY C 201 ? PHE C 168 GLY C 180 1 ? 13 
HELX_P HELX_P76 AI4 LEU C 205 ? ASN C 235 ? LEU C 184 ASN C 214 1 ? 31 
HELX_P HELX_P77 AI5 THR C 238 ? ASP C 269 ? THR C 217 ASP C 248 1 ? 32 
HELX_P HELX_P78 AI6 GLN C 270 ? GLY C 272 ? GLN C 249 GLY C 251 5 ? 3  
HELX_P HELX_P79 AI7 LEU C 273 ? LEU C 292 ? LEU C 252 LEU C 271 1 ? 20 
HELX_P HELX_P80 AI8 ASN C 304 ? GLY C 310 ? ASN C 283 GLY C 289 1 ? 7  
HELX_P HELX_P81 AI9 LYS C 337 ? TYR C 342 ? LYS C 316 TYR C 321 5 ? 6  
HELX_P HELX_P82 AJ1 PHE D 38  ? GLN D 49  ? PHE D 17  GLN D 28  1 ? 12 
HELX_P HELX_P83 AJ2 LEU D 52  ? ILE D 56  ? LEU D 31  ILE D 35  5 ? 5  
HELX_P HELX_P84 AJ3 LEU D 58  ? GLY D 60  ? LEU D 37  GLY D 39  5 ? 3  
HELX_P HELX_P85 AJ4 ASP D 61  ? LYS D 66  ? ASP D 40  LYS D 45  1 ? 6  
HELX_P HELX_P86 AJ5 GLY D 69  ? THR D 93  ? GLY D 48  THR D 72  1 ? 25 
HELX_P HELX_P87 AJ6 THR D 93  ? VAL D 102 ? THR D 72  VAL D 81  1 ? 10 
HELX_P HELX_P88 AJ7 GLY D 104 ? VAL D 121 ? GLY D 83  VAL D 100 1 ? 18 
HELX_P HELX_P89 AJ8 VAL D 121 ? ALA D 134 ? VAL D 100 ALA D 113 1 ? 14 
HELX_P HELX_P90 AJ9 PRO D 135 ? ASN D 149 ? PRO D 114 ASN D 128 1 ? 15 
HELX_P HELX_P91 AK1 ASN D 149 ? ALA D 165 ? ASN D 128 ALA D 144 1 ? 17 
HELX_P HELX_P92 AK2 ASP D 170 ? PHE D 187 ? ASP D 149 PHE D 166 1 ? 18 
HELX_P HELX_P93 AK3 PHE D 189 ? GLY D 201 ? PHE D 168 GLY D 180 1 ? 13 
HELX_P HELX_P94 AK4 LEU D 205 ? ASN D 235 ? LEU D 184 ASN D 214 1 ? 31 
HELX_P HELX_P95 AK5 THR D 238 ? ASP D 269 ? THR D 217 ASP D 248 1 ? 32 
HELX_P HELX_P96 AK6 GLN D 270 ? GLY D 272 ? GLN D 249 GLY D 251 5 ? 3  
HELX_P HELX_P97 AK7 LEU D 273 ? LEU D 292 ? LEU D 252 LEU D 271 1 ? 20 
HELX_P HELX_P98 AK8 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 ? ? G TTP .   O2A ? ? ? 1_555 H MG . MG ? ? A TTP 803 A MG 804 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
metalc2  metalc ? ? G TTP .   O1B ? ? ? 1_555 H MG . MG ? ? A TTP 803 A MG 804 1_555 ? ? ? ? ? ? ? 2.849 ? ? 
metalc3  metalc ? ? G TTP .   O1G ? ? ? 1_555 H MG . MG ? ? A TTP 803 A MG 804 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc4  metalc ? ? I TTP .   O2A ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc5  metalc ? ? I TTP .   O1B ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.501 ? ? 
metalc6  metalc ? ? I TTP .   O3G ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.179 ? ? 
metalc7  metalc ? ? C ASP 87  OD1 ? ? ? 1_555 N MN . MN ? ? C ASP 66  C MN 402 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc8  metalc ? ? C GLU 118 OE2 ? ? ? 1_555 M MN . MN ? ? C GLU 97  C MN 401 1_555 ? ? ? ? ? ? ? 1.960 ? ? 
metalc9  metalc ? ? C GLU 118 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 97  C MN 402 1_555 ? ? ? ? ? ? ? 2.113 ? ? 
metalc10 metalc ? ? C HIS 122 ND1 ? ? ? 1_555 N MN . MN ? ? C HIS 101 C MN 402 1_555 ? ? ? ? ? ? ? 2.177 ? ? 
metalc11 metalc ? ? C GLU 185 OE1 ? ? ? 1_555 M MN . MN ? ? C GLU 164 C MN 401 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
metalc12 metalc ? ? C GLU 185 OE2 ? ? ? 1_555 M MN . MN ? ? C GLU 164 C MN 401 1_555 ? ? ? ? ? ? ? 1.966 ? ? 
metalc13 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 M MN . MN ? ? C GLU 198 C MN 401 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc14 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.711 ? ? 
metalc15 metalc ? ? C GLU 219 OE2 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc16 metalc ? ? C HIS 222 ND1 ? ? ? 1_555 M MN . MN ? ? C HIS 201 C MN 401 1_555 ? ? ? ? ? ? ? 2.408 ? ? 
metalc17 metalc ? ? D ASP 87  OD1 ? ? ? 1_555 P MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc18 metalc ? ? D ASP 87  OD2 ? ? ? 1_555 P MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.156 ? ? 
metalc19 metalc ? ? D GLU 118 OE2 ? ? ? 1_555 O MN . MN ? ? D GLU 97  D MN 401 1_555 ? ? ? ? ? ? ? 1.912 ? ? 
metalc20 metalc ? ? D GLU 118 OE1 ? ? ? 1_555 P MN . MN ? ? D GLU 97  D MN 402 1_555 ? ? ? ? ? ? ? 1.990 ? ? 
metalc21 metalc ? ? D HIS 122 ND1 ? ? ? 1_555 P MN . MN ? ? D HIS 101 D MN 402 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc22 metalc ? ? D GLU 185 OE1 ? ? ? 1_555 O MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc23 metalc ? ? D GLU 185 OE2 ? ? ? 1_555 O MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc24 metalc ? ? D GLU 219 OE1 ? ? ? 1_555 O MN . MN ? ? D GLU 198 D MN 401 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc25 metalc ? ? D GLU 219 OE2 ? ? ? 1_555 P MN . MN ? ? D GLU 198 D MN 402 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc26 metalc ? ? D HIS 222 ND1 ? ? ? 1_555 O MN . MN ? ? D HIS 201 D MN 401 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O2A ? G TTP .   ? A TTP 803 ? 1_555 MG ? H MG . ? A MG 804 ? 1_555 O1B ? G TTP .   ? A TTP 803 ? 1_555 65.7  ? 
2  O2A ? G TTP .   ? A TTP 803 ? 1_555 MG ? H MG . ? A MG 804 ? 1_555 O1G ? G TTP .   ? A TTP 803 ? 1_555 111.2 ? 
3  O1B ? G TTP .   ? A TTP 803 ? 1_555 MG ? H MG . ? A MG 804 ? 1_555 O1G ? G TTP .   ? A TTP 803 ? 1_555 64.8  ? 
4  O2A ? I TTP .   ? B TTP 801 ? 1_555 MG ? J MG . ? B MG 802 ? 1_555 O1B ? I TTP .   ? B TTP 801 ? 1_555 71.7  ? 
5  O2A ? I TTP .   ? B TTP 801 ? 1_555 MG ? J MG . ? B MG 802 ? 1_555 O3G ? I TTP .   ? B TTP 801 ? 1_555 88.0  ? 
6  O1B ? I TTP .   ? B TTP 801 ? 1_555 MG ? J MG . ? B MG 802 ? 1_555 O3G ? I TTP .   ? B TTP 801 ? 1_555 74.3  ? 
7  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  ? 
8  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 ? 
9  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  ? 
10 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 ? 
11 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  ? 
12 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 ? 
13 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 ? 
14 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 ? 
15 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 ? 
16 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  ? 
17 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 ? 
18 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  ? 
19 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 64.7  ? 
20 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 ? 
21 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  ? 
22 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 ? 
23 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 97.1  ? 
24 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 ? 
25 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_555 104.0 ? 
26 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  ? 
27 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  ? 
28 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 93.3  ? 
29 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 ? 
30 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 165.7 ? 
31 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 ? 
32 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  ? 
33 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  ? 
34 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 ? 
35 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_555 122.0 ? 
36 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  ? 
37 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 ? 
38 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  ? 
39 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  ? 
40 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_555 121.6 ? 
41 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  ? 
42 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_555 136.8 ? 
43 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  ? 
44 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 ? 
45 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 ? 
46 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 0.33 
2 TYR 355 B . ? TYR 355 B PRO 356 B ? PRO 356 B 1 0.74 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 6 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 3 ? 
AA8 ? 8 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA8 5 6 ? parallel      
AA8 6 7 ? parallel      
AA8 7 8 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 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 GLN A 19  ? LYS A 20  ? GLN A 19  LYS A 20  
AA1 2 LYS A 23  ? PHE A 24  ? LYS A 23  PHE A 24  
AA2 1 TYR A 149 ? PRO A 151 ? TYR A 149 PRO A 151 
AA2 2 LEU A 411 ? ASN A 415 ? LEU A 411 ASN A 415 
AA2 3 GLY A 462 ? MET A 466 ? GLY A 462 MET A 466 
AA3 1 CYS A 170 ? GLU A 174 ? CYS A 170 GLU A 174 
AA3 2 GLY A 198 ? ASN A 202 ? GLY A 198 ASN A 202 
AA3 3 GLY A 247 ? ASN A 252 ? GLY A 247 ASN A 252 
AA3 4 LEU A 278 ? ILE A 284 ? LEU A 278 ILE A 284 
AA3 5 TYR A 357 ? PHE A 360 ? TYR A 357 PHE A 360 
AA3 6 THR A 681 ? ILE A 682 ? THR A 681 ILE A 682 
AA4 1 ALA A 298 ? PHE A 301 ? ALA A 298 PHE A 301 
AA4 2 LYS A 334 ? ILE A 337 ? LYS A 334 ILE A 337 
AA5 1 ILE A 601 ? TYR A 606 ? ILE A 601 TYR A 606 
AA5 2 SER A 609 ? PRO A 614 ? SER A 609 PRO A 614 
AA6 1 LEU A 656 ? LEU A 658 ? LEU A 656 LEU A 658 
AA6 2 ALA A 685 ? THR A 687 ? ALA A 685 THR A 687 
AA7 1 TYR B 149 ? PRO B 151 ? TYR B 149 PRO B 151 
AA7 2 SER B 408 ? ASN B 415 ? SER B 408 ASN B 415 
AA7 3 ILE B 461 ? MET B 466 ? ILE B 461 MET B 466 
AA8 1 TYR B 149 ? PRO B 151 ? TYR B 149 PRO B 151 
AA8 2 SER B 408 ? ASN B 415 ? SER B 408 ASN B 415 
AA8 3 CYS B 170 ? GLU B 174 ? CYS B 170 GLU B 174 
AA8 4 GLY B 198 ? ASN B 202 ? GLY B 198 ASN B 202 
AA8 5 GLY B 247 ? ASN B 252 ? GLY B 247 ASN B 252 
AA8 6 LEU B 278 ? ILE B 284 ? LEU B 278 ILE B 284 
AA8 7 TYR B 357 ? PHE B 360 ? TYR B 357 PHE B 360 
AA8 8 THR B 681 ? ILE B 682 ? THR B 681 ILE B 682 
AA9 1 ALA B 298 ? PHE B 301 ? ALA B 298 PHE B 301 
AA9 2 LYS B 334 ? ILE B 337 ? LYS B 334 ILE B 337 
AB1 1 ILE B 601 ? TYR B 606 ? ILE B 601 TYR B 606 
AB1 2 SER B 609 ? PRO B 614 ? SER B 609 PRO B 614 
AB2 1 LEU B 656 ? LYS B 659 ? LEU B 656 LYS B 659 
AB2 2 ALA B 685 ? LYS B 688 ? ALA B 685 LYS B 688 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 20  ? N LYS A 20  O LYS A 23  ? O LYS A 23  
AA2 1 2 N GLN A 150 ? N GLN A 150 O SER A 413 ? O SER A 413 
AA2 2 3 N GLY A 412 ? N GLY A 412 O GLY A 464 ? O GLY A 464 
AA3 1 2 N LEU A 173 ? N LEU A 173 O SER A 200 ? O SER A 200 
AA3 2 3 N LEU A 201 ? N LEU A 201 O TYR A 250 ? O TYR A 250 
AA3 3 4 N GLY A 247 ? N GLY A 247 O SER A 279 ? O SER A 279 
AA3 4 5 N VAL A 282 ? N VAL A 282 O TYR A 357 ? O TYR A 357 
AA3 5 6 N ILE A 358 ? N ILE A 358 O ILE A 682 ? O ILE A 682 
AA4 1 2 N ALA A 298 ? N ALA A 298 O ILE A 337 ? O ILE A 337 
AA5 1 2 N GLU A 602 ? N GLU A 602 O TYR A 613 ? O TYR A 613 
AA6 1 2 N LEU A 656 ? N LEU A 656 O ARG A 686 ? O ARG A 686 
AA7 1 2 N GLN B 150 ? N GLN B 150 O SER B 413 ? O SER B 413 
AA7 2 3 N GLY B 412 ? N GLY B 412 O GLY B 464 ? O GLY B 464 
AA8 1 2 N GLN B 150 ? N GLN B 150 O SER B 413 ? O SER B 413 
AA8 2 3 O CYS B 409 ? O CYS B 409 N CYS B 170 ? N CYS B 170 
AA8 3 4 N LEU B 173 ? N LEU B 173 O SER B 200 ? O SER B 200 
AA8 4 5 N LEU B 201 ? N LEU B 201 O TYR B 250 ? O TYR B 250 
AA8 5 6 N GLY B 247 ? N GLY B 247 O SER B 279 ? O SER B 279 
AA8 6 7 N VAL B 282 ? N VAL B 282 O TYR B 357 ? O TYR B 357 
AA8 7 8 N ILE B 358 ? N ILE B 358 O ILE B 682 ? O ILE B 682 
AA9 1 2 N ALA B 298 ? N ALA B 298 O ILE B 337 ? O ILE B 337 
AB1 1 2 N ARG B 604 ? N ARG B 604 O THR B 611 ? O THR B 611 
AB2 1 2 N LEU B 658 ? N LEU B 658 O ARG B 686 ? O ARG B 686 
# 
_pdbx_entry_details.entry_id                   9BZF 
_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 OG1 A THR 108 ? ? OD1 A ASP 110 ? ? 2.01 
2 1 O   A PRO 616 ? ? OH  A TYR 626 ? ? 2.13 
3 1 O   B PRO 616 ? ? OH  B TYR 626 ? ? 2.14 
4 1 NH2 D ARG 86  ? ? OE1 D GLU 211 ? ? 2.18 
5 1 NE2 B HIS 372 ? ? O   B GLN 516 ? ? 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 ASP A 257 ? ? -69.47  2.76    
2  1 ASP A 398 ? ? 39.40   35.67   
3  1 SER A 593 ? ? 56.66   -153.80 
4  1 ASP B 215 ? ? 74.81   -2.83   
5  1 SER B 593 ? ? 60.64   -154.17 
6  1 THR C 72  ? ? -128.06 -59.08  
7  1 ASP C 148 ? ? 58.11   15.68   
8  1 PHE C 166 ? ? -125.63 -60.85  
9  1 THR D 72  ? ? -128.12 -58.52  
10 1 PHE D 166 ? ? -144.12 -61.21  
11 1 ASP D 317 ? ? 64.26   164.49  
12 1 ASP D 318 ? ? 66.26   -1.32   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BZF 
_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 9BYH ? ?      'Rigid-body docking of consensus model 9BYH containing alpha subunits and beta C-terminal tails' ? ?      PDB 
'experimental model' 9BYH 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                    9BZF 
_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                  4.4 
_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               28000 
_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                        9BZF 
_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              9BZF 
_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                9BZF 
_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              9BZF 
_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 
GDP PB     P  N N 135 
GDP O1B    O  N N 136 
GDP O2B    O  N N 137 
GDP O3B    O  N N 138 
GDP O3A    O  N N 139 
GDP PA     P  N N 140 
GDP O1A    O  N N 141 
GDP O2A    O  N N 142 
GDP "O5'"  O  N N 143 
GDP "C5'"  C  N N 144 
GDP "C4'"  C  N R 145 
GDP "O4'"  O  N N 146 
GDP "C3'"  C  N S 147 
GDP "O3'"  O  N N 148 
GDP "C2'"  C  N R 149 
GDP "O2'"  O  N N 150 
GDP "C1'"  C  N R 151 
GDP N9     N  Y N 152 
GDP C8     C  Y N 153 
GDP N7     N  Y N 154 
GDP C5     C  Y N 155 
GDP C6     C  N N 156 
GDP O6     O  N N 157 
GDP N1     N  N N 158 
GDP C2     C  N N 159 
GDP N2     N  N N 160 
GDP N3     N  N N 161 
GDP C4     C  Y N 162 
GDP HOB2   H  N N 163 
GDP HOB3   H  N N 164 
GDP HOA2   H  N N 165 
GDP "H5'"  H  N N 166 
GDP "H5''" H  N N 167 
GDP "H4'"  H  N N 168 
GDP "H3'"  H  N N 169 
GDP "HO3'" H  N N 170 
GDP "H2'"  H  N N 171 
GDP "HO2'" H  N N 172 
GDP "H1'"  H  N N 173 
GDP H8     H  N N 174 
GDP HN1    H  N N 175 
GDP HN21   H  N N 176 
GDP HN22   H  N N 177 
GLN N      N  N N 178 
GLN CA     C  N S 179 
GLN C      C  N N 180 
GLN O      O  N N 181 
GLN CB     C  N N 182 
GLN CG     C  N N 183 
GLN CD     C  N N 184 
GLN OE1    O  N N 185 
GLN NE2    N  N N 186 
GLN OXT    O  N N 187 
GLN H      H  N N 188 
GLN H2     H  N N 189 
GLN HA     H  N N 190 
GLN HB2    H  N N 191 
GLN HB3    H  N N 192 
GLN HG2    H  N N 193 
GLN HG3    H  N N 194 
GLN HE21   H  N N 195 
GLN HE22   H  N N 196 
GLN HXT    H  N N 197 
GLU N      N  N N 198 
GLU CA     C  N S 199 
GLU C      C  N N 200 
GLU O      O  N N 201 
GLU CB     C  N N 202 
GLU CG     C  N N 203 
GLU CD     C  N N 204 
GLU OE1    O  N N 205 
GLU OE2    O  N N 206 
GLU OXT    O  N N 207 
GLU H      H  N N 208 
GLU H2     H  N N 209 
GLU HA     H  N N 210 
GLU HB2    H  N N 211 
GLU HB3    H  N N 212 
GLU HG2    H  N N 213 
GLU HG3    H  N N 214 
GLU HE2    H  N N 215 
GLU HXT    H  N N 216 
GLY N      N  N N 217 
GLY CA     C  N N 218 
GLY C      C  N N 219 
GLY O      O  N N 220 
GLY OXT    O  N N 221 
GLY H      H  N N 222 
GLY H2     H  N N 223 
GLY HA2    H  N N 224 
GLY HA3    H  N N 225 
GLY HXT    H  N N 226 
HIS N      N  N N 227 
HIS CA     C  N S 228 
HIS C      C  N N 229 
HIS O      O  N N 230 
HIS CB     C  N N 231 
HIS CG     C  Y N 232 
HIS ND1    N  Y N 233 
HIS CD2    C  Y N 234 
HIS CE1    C  Y N 235 
HIS NE2    N  Y N 236 
HIS OXT    O  N N 237 
HIS H      H  N N 238 
HIS H2     H  N N 239 
HIS HA     H  N N 240 
HIS HB2    H  N N 241 
HIS HB3    H  N N 242 
HIS HD1    H  N N 243 
HIS HD2    H  N N 244 
HIS HE1    H  N N 245 
HIS HE2    H  N N 246 
HIS HXT    H  N N 247 
ILE N      N  N N 248 
ILE CA     C  N S 249 
ILE C      C  N N 250 
ILE O      O  N N 251 
ILE CB     C  N S 252 
ILE CG1    C  N N 253 
ILE CG2    C  N N 254 
ILE CD1    C  N N 255 
ILE OXT    O  N N 256 
ILE H      H  N N 257 
ILE H2     H  N N 258 
ILE HA     H  N N 259 
ILE HB     H  N N 260 
ILE HG12   H  N N 261 
ILE HG13   H  N N 262 
ILE HG21   H  N N 263 
ILE HG22   H  N N 264 
ILE HG23   H  N N 265 
ILE HD11   H  N N 266 
ILE HD12   H  N N 267 
ILE HD13   H  N N 268 
ILE HXT    H  N N 269 
LEU N      N  N N 270 
LEU CA     C  N S 271 
LEU C      C  N N 272 
LEU O      O  N N 273 
LEU CB     C  N N 274 
LEU CG     C  N N 275 
LEU CD1    C  N N 276 
LEU CD2    C  N N 277 
LEU OXT    O  N N 278 
LEU H      H  N N 279 
LEU H2     H  N N 280 
LEU HA     H  N N 281 
LEU HB2    H  N N 282 
LEU HB3    H  N N 283 
LEU HG     H  N N 284 
LEU HD11   H  N N 285 
LEU HD12   H  N N 286 
LEU HD13   H  N N 287 
LEU HD21   H  N N 288 
LEU HD22   H  N N 289 
LEU HD23   H  N N 290 
LEU HXT    H  N N 291 
LYS N      N  N N 292 
LYS CA     C  N S 293 
LYS C      C  N N 294 
LYS O      O  N N 295 
LYS CB     C  N N 296 
LYS CG     C  N N 297 
LYS CD     C  N N 298 
LYS CE     C  N N 299 
LYS NZ     N  N N 300 
LYS OXT    O  N N 301 
LYS H      H  N N 302 
LYS H2     H  N N 303 
LYS HA     H  N N 304 
LYS HB2    H  N N 305 
LYS HB3    H  N N 306 
LYS HG2    H  N N 307 
LYS HG3    H  N N 308 
LYS HD2    H  N N 309 
LYS HD3    H  N N 310 
LYS HE2    H  N N 311 
LYS HE3    H  N N 312 
LYS HZ1    H  N N 313 
LYS HZ2    H  N N 314 
LYS HZ3    H  N N 315 
LYS HXT    H  N N 316 
MET N      N  N N 317 
MET CA     C  N S 318 
MET C      C  N N 319 
MET O      O  N N 320 
MET CB     C  N N 321 
MET CG     C  N N 322 
MET SD     S  N N 323 
MET CE     C  N N 324 
MET OXT    O  N N 325 
MET H      H  N N 326 
MET H2     H  N N 327 
MET HA     H  N N 328 
MET HB2    H  N N 329 
MET HB3    H  N N 330 
MET HG2    H  N N 331 
MET HG3    H  N N 332 
MET HE1    H  N N 333 
MET HE2    H  N N 334 
MET HE3    H  N N 335 
MET HXT    H  N N 336 
MG  MG     MG N N 337 
MN  MN     MN N N 338 
PHE N      N  N N 339 
PHE CA     C  N S 340 
PHE C      C  N N 341 
PHE O      O  N N 342 
PHE CB     C  N N 343 
PHE CG     C  Y N 344 
PHE CD1    C  Y N 345 
PHE CD2    C  Y N 346 
PHE CE1    C  Y N 347 
PHE CE2    C  Y N 348 
PHE CZ     C  Y N 349 
PHE OXT    O  N N 350 
PHE H      H  N N 351 
PHE H2     H  N N 352 
PHE HA     H  N N 353 
PHE HB2    H  N N 354 
PHE HB3    H  N N 355 
PHE HD1    H  N N 356 
PHE HD2    H  N N 357 
PHE HE1    H  N N 358 
PHE HE2    H  N N 359 
PHE HZ     H  N N 360 
PHE HXT    H  N N 361 
PRO N      N  N N 362 
PRO CA     C  N S 363 
PRO C      C  N N 364 
PRO O      O  N N 365 
PRO CB     C  N N 366 
PRO CG     C  N N 367 
PRO CD     C  N N 368 
PRO OXT    O  N N 369 
PRO H      H  N N 370 
PRO HA     H  N N 371 
PRO HB2    H  N N 372 
PRO HB3    H  N N 373 
PRO HG2    H  N N 374 
PRO HG3    H  N N 375 
PRO HD2    H  N N 376 
PRO HD3    H  N N 377 
PRO HXT    H  N N 378 
SER N      N  N N 379 
SER CA     C  N S 380 
SER C      C  N N 381 
SER O      O  N N 382 
SER CB     C  N N 383 
SER OG     O  N N 384 
SER OXT    O  N N 385 
SER H      H  N N 386 
SER H2     H  N N 387 
SER HA     H  N N 388 
SER HB2    H  N N 389 
SER HB3    H  N N 390 
SER HG     H  N N 391 
SER HXT    H  N N 392 
THR N      N  N N 393 
THR CA     C  N S 394 
THR C      C  N N 395 
THR O      O  N N 396 
THR CB     C  N R 397 
THR OG1    O  N N 398 
THR CG2    C  N N 399 
THR OXT    O  N N 400 
THR H      H  N N 401 
THR H2     H  N N 402 
THR HA     H  N N 403 
THR HB     H  N N 404 
THR HG1    H  N N 405 
THR HG21   H  N N 406 
THR HG22   H  N N 407 
THR HG23   H  N N 408 
THR HXT    H  N N 409 
TRP N      N  N N 410 
TRP CA     C  N S 411 
TRP C      C  N N 412 
TRP O      O  N N 413 
TRP CB     C  N N 414 
TRP CG     C  Y N 415 
TRP CD1    C  Y N 416 
TRP CD2    C  Y N 417 
TRP NE1    N  Y N 418 
TRP CE2    C  Y N 419 
TRP CE3    C  Y N 420 
TRP CZ2    C  Y N 421 
TRP CZ3    C  Y N 422 
TRP CH2    C  Y N 423 
TRP OXT    O  N N 424 
TRP H      H  N N 425 
TRP H2     H  N N 426 
TRP HA     H  N N 427 
TRP HB2    H  N N 428 
TRP HB3    H  N N 429 
TRP HD1    H  N N 430 
TRP HE1    H  N N 431 
TRP HE3    H  N N 432 
TRP HZ2    H  N N 433 
TRP HZ3    H  N N 434 
TRP HH2    H  N N 435 
TRP HXT    H  N N 436 
TTP PA     P  N S 437 
TTP O1A    O  N N 438 
TTP O2A    O  N N 439 
TTP O3A    O  N N 440 
TTP PB     P  N S 441 
TTP O1B    O  N N 442 
TTP O2B    O  N N 443 
TTP O3B    O  N N 444 
TTP PG     P  N N 445 
TTP O1G    O  N N 446 
TTP O2G    O  N N 447 
TTP O3G    O  N N 448 
TTP "O5'"  O  N N 449 
TTP "C5'"  C  N N 450 
TTP "C4'"  C  N R 451 
TTP "O4'"  O  N N 452 
TTP "C3'"  C  N S 453 
TTP "O3'"  O  N N 454 
TTP "C2'"  C  N N 455 
TTP "C1'"  C  N R 456 
TTP N1     N  N N 457 
TTP C2     C  N N 458 
TTP O2     O  N N 459 
TTP N3     N  N N 460 
TTP C4     C  N N 461 
TTP O4     O  N N 462 
TTP C5     C  N N 463 
TTP C5M    C  N N 464 
TTP C6     C  N N 465 
TTP HOA2   H  N N 466 
TTP HOB2   H  N N 467 
TTP HOG2   H  N N 468 
TTP HOG3   H  N N 469 
TTP "H5'1" H  N N 470 
TTP "H5'2" H  N N 471 
TTP "H4'"  H  N N 472 
TTP "H3'"  H  N N 473 
TTP "HO3'" H  N N 474 
TTP "H2'1" H  N N 475 
TTP "H2'2" H  N N 476 
TTP "H1'"  H  N N 477 
TTP HN3    H  N N 478 
TTP HM51   H  N N 479 
TTP HM52   H  N N 480 
TTP HM53   H  N N 481 
TTP H6     H  N N 482 
TYR N      N  N N 483 
TYR CA     C  N S 484 
TYR C      C  N N 485 
TYR O      O  N N 486 
TYR CB     C  N N 487 
TYR CG     C  Y N 488 
TYR CD1    C  Y N 489 
TYR CD2    C  Y N 490 
TYR CE1    C  Y N 491 
TYR CE2    C  Y N 492 
TYR CZ     C  Y N 493 
TYR OH     O  N N 494 
TYR OXT    O  N N 495 
TYR H      H  N N 496 
TYR H2     H  N N 497 
TYR HA     H  N N 498 
TYR HB2    H  N N 499 
TYR HB3    H  N N 500 
TYR HD1    H  N N 501 
TYR HD2    H  N N 502 
TYR HE1    H  N N 503 
TYR HE2    H  N N 504 
TYR HH     H  N N 505 
TYR HXT    H  N N 506 
VAL N      N  N N 507 
VAL CA     C  N S 508 
VAL C      C  N N 509 
VAL O      O  N N 510 
VAL CB     C  N N 511 
VAL CG1    C  N N 512 
VAL CG2    C  N N 513 
VAL OXT    O  N N 514 
VAL H      H  N N 515 
VAL H2     H  N N 516 
VAL HA     H  N N 517 
VAL HB     H  N N 518 
VAL HG11   H  N N 519 
VAL HG12   H  N N 520 
VAL HG13   H  N N 521 
VAL HG21   H  N N 522 
VAL HG22   H  N N 523 
VAL HG23   H  N N 524 
VAL HXT    H  N N 525 
# 
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 
GDP PB    O1B    doub N N 132 
GDP PB    O2B    sing N N 133 
GDP PB    O3B    sing N N 134 
GDP PB    O3A    sing N N 135 
GDP O2B   HOB2   sing N N 136 
GDP O3B   HOB3   sing N N 137 
GDP O3A   PA     sing N N 138 
GDP PA    O1A    doub N N 139 
GDP PA    O2A    sing N N 140 
GDP PA    "O5'"  sing N N 141 
GDP O2A   HOA2   sing N N 142 
GDP "O5'" "C5'"  sing N N 143 
GDP "C5'" "C4'"  sing N N 144 
GDP "C5'" "H5'"  sing N N 145 
GDP "C5'" "H5''" sing N N 146 
GDP "C4'" "O4'"  sing N N 147 
GDP "C4'" "C3'"  sing N N 148 
GDP "C4'" "H4'"  sing N N 149 
GDP "O4'" "C1'"  sing N N 150 
GDP "C3'" "O3'"  sing N N 151 
GDP "C3'" "C2'"  sing N N 152 
GDP "C3'" "H3'"  sing N N 153 
GDP "O3'" "HO3'" sing N N 154 
GDP "C2'" "O2'"  sing N N 155 
GDP "C2'" "C1'"  sing N N 156 
GDP "C2'" "H2'"  sing N N 157 
GDP "O2'" "HO2'" sing N N 158 
GDP "C1'" N9     sing N N 159 
GDP "C1'" "H1'"  sing N N 160 
GDP N9    C8     sing Y N 161 
GDP N9    C4     sing Y N 162 
GDP C8    N7     doub Y N 163 
GDP C8    H8     sing N N 164 
GDP N7    C5     sing Y N 165 
GDP C5    C6     sing N N 166 
GDP C5    C4     doub Y N 167 
GDP C6    O6     doub N N 168 
GDP C6    N1     sing N N 169 
GDP N1    C2     sing N N 170 
GDP N1    HN1    sing N N 171 
GDP C2    N2     sing N N 172 
GDP C2    N3     doub N N 173 
GDP N2    HN21   sing N N 174 
GDP N2    HN22   sing N N 175 
GDP N3    C4     sing N N 176 
GLN N     CA     sing N N 177 
GLN N     H      sing N N 178 
GLN N     H2     sing N N 179 
GLN CA    C      sing N N 180 
GLN CA    CB     sing N N 181 
GLN CA    HA     sing N N 182 
GLN C     O      doub N N 183 
GLN C     OXT    sing N N 184 
GLN CB    CG     sing N N 185 
GLN CB    HB2    sing N N 186 
GLN CB    HB3    sing N N 187 
GLN CG    CD     sing N N 188 
GLN CG    HG2    sing N N 189 
GLN CG    HG3    sing N N 190 
GLN CD    OE1    doub N N 191 
GLN CD    NE2    sing N N 192 
GLN NE2   HE21   sing N N 193 
GLN NE2   HE22   sing N N 194 
GLN OXT   HXT    sing N N 195 
GLU N     CA     sing N N 196 
GLU N     H      sing N N 197 
GLU N     H2     sing N N 198 
GLU CA    C      sing N N 199 
GLU CA    CB     sing N N 200 
GLU CA    HA     sing N N 201 
GLU C     O      doub N N 202 
GLU C     OXT    sing N N 203 
GLU CB    CG     sing N N 204 
GLU CB    HB2    sing N N 205 
GLU CB    HB3    sing N N 206 
GLU CG    CD     sing N N 207 
GLU CG    HG2    sing N N 208 
GLU CG    HG3    sing N N 209 
GLU CD    OE1    doub N N 210 
GLU CD    OE2    sing N N 211 
GLU OE2   HE2    sing N N 212 
GLU OXT   HXT    sing N N 213 
GLY N     CA     sing N N 214 
GLY N     H      sing N N 215 
GLY N     H2     sing N N 216 
GLY CA    C      sing N N 217 
GLY CA    HA2    sing N N 218 
GLY CA    HA3    sing N N 219 
GLY C     O      doub N N 220 
GLY C     OXT    sing N N 221 
GLY OXT   HXT    sing N N 222 
HIS N     CA     sing N N 223 
HIS N     H      sing N N 224 
HIS N     H2     sing N N 225 
HIS CA    C      sing N N 226 
HIS CA    CB     sing N N 227 
HIS CA    HA     sing N N 228 
HIS C     O      doub N N 229 
HIS C     OXT    sing N N 230 
HIS CB    CG     sing N N 231 
HIS CB    HB2    sing N N 232 
HIS CB    HB3    sing N N 233 
HIS CG    ND1    sing Y N 234 
HIS CG    CD2    doub Y N 235 
HIS ND1   CE1    doub Y N 236 
HIS ND1   HD1    sing N N 237 
HIS CD2   NE2    sing Y N 238 
HIS CD2   HD2    sing N N 239 
HIS CE1   NE2    sing Y N 240 
HIS CE1   HE1    sing N N 241 
HIS NE2   HE2    sing N N 242 
HIS OXT   HXT    sing N N 243 
ILE N     CA     sing N N 244 
ILE N     H      sing N N 245 
ILE N     H2     sing N N 246 
ILE CA    C      sing N N 247 
ILE CA    CB     sing N N 248 
ILE CA    HA     sing N N 249 
ILE C     O      doub N N 250 
ILE C     OXT    sing N N 251 
ILE CB    CG1    sing N N 252 
ILE CB    CG2    sing N N 253 
ILE CB    HB     sing N N 254 
ILE CG1   CD1    sing N N 255 
ILE CG1   HG12   sing N N 256 
ILE CG1   HG13   sing N N 257 
ILE CG2   HG21   sing N N 258 
ILE CG2   HG22   sing N N 259 
ILE CG2   HG23   sing N N 260 
ILE CD1   HD11   sing N N 261 
ILE CD1   HD12   sing N N 262 
ILE CD1   HD13   sing N N 263 
ILE OXT   HXT    sing N N 264 
LEU N     CA     sing N N 265 
LEU N     H      sing N N 266 
LEU N     H2     sing N N 267 
LEU CA    C      sing N N 268 
LEU CA    CB     sing N N 269 
LEU CA    HA     sing N N 270 
LEU C     O      doub N N 271 
LEU C     OXT    sing N N 272 
LEU CB    CG     sing N N 273 
LEU CB    HB2    sing N N 274 
LEU CB    HB3    sing N N 275 
LEU CG    CD1    sing N N 276 
LEU CG    CD2    sing N N 277 
LEU CG    HG     sing N N 278 
LEU CD1   HD11   sing N N 279 
LEU CD1   HD12   sing N N 280 
LEU CD1   HD13   sing N N 281 
LEU CD2   HD21   sing N N 282 
LEU CD2   HD22   sing N N 283 
LEU CD2   HD23   sing N N 284 
LEU OXT   HXT    sing N N 285 
LYS N     CA     sing N N 286 
LYS N     H      sing N N 287 
LYS N     H2     sing N N 288 
LYS CA    C      sing N N 289 
LYS CA    CB     sing N N 290 
LYS CA    HA     sing N N 291 
LYS C     O      doub N N 292 
LYS C     OXT    sing N N 293 
LYS CB    CG     sing N N 294 
LYS CB    HB2    sing N N 295 
LYS CB    HB3    sing N N 296 
LYS CG    CD     sing N N 297 
LYS CG    HG2    sing N N 298 
LYS CG    HG3    sing N N 299 
LYS CD    CE     sing N N 300 
LYS CD    HD2    sing N N 301 
LYS CD    HD3    sing N N 302 
LYS CE    NZ     sing N N 303 
LYS CE    HE2    sing N N 304 
LYS CE    HE3    sing N N 305 
LYS NZ    HZ1    sing N N 306 
LYS NZ    HZ2    sing N N 307 
LYS NZ    HZ3    sing N N 308 
LYS OXT   HXT    sing N N 309 
MET N     CA     sing N N 310 
MET N     H      sing N N 311 
MET N     H2     sing N N 312 
MET CA    C      sing N N 313 
MET CA    CB     sing N N 314 
MET CA    HA     sing N N 315 
MET C     O      doub N N 316 
MET C     OXT    sing N N 317 
MET CB    CG     sing N N 318 
MET CB    HB2    sing N N 319 
MET CB    HB3    sing N N 320 
MET CG    SD     sing N N 321 
MET CG    HG2    sing N N 322 
MET CG    HG3    sing N N 323 
MET SD    CE     sing N N 324 
MET CE    HE1    sing N N 325 
MET CE    HE2    sing N N 326 
MET CE    HE3    sing N N 327 
MET OXT   HXT    sing N N 328 
PHE N     CA     sing N N 329 
PHE N     H      sing N N 330 
PHE N     H2     sing N N 331 
PHE CA    C      sing N N 332 
PHE CA    CB     sing N N 333 
PHE CA    HA     sing N N 334 
PHE C     O      doub N N 335 
PHE C     OXT    sing N N 336 
PHE CB    CG     sing N N 337 
PHE CB    HB2    sing N N 338 
PHE CB    HB3    sing N N 339 
PHE CG    CD1    doub Y N 340 
PHE CG    CD2    sing Y N 341 
PHE CD1   CE1    sing Y N 342 
PHE CD1   HD1    sing N N 343 
PHE CD2   CE2    doub Y N 344 
PHE CD2   HD2    sing N N 345 
PHE CE1   CZ     doub Y N 346 
PHE CE1   HE1    sing N N 347 
PHE CE2   CZ     sing Y N 348 
PHE CE2   HE2    sing N N 349 
PHE CZ    HZ     sing N N 350 
PHE OXT   HXT    sing N N 351 
PRO N     CA     sing N N 352 
PRO N     CD     sing N N 353 
PRO N     H      sing N N 354 
PRO CA    C      sing N N 355 
PRO CA    CB     sing N N 356 
PRO CA    HA     sing N N 357 
PRO C     O      doub N N 358 
PRO C     OXT    sing N N 359 
PRO CB    CG     sing N N 360 
PRO CB    HB2    sing N N 361 
PRO CB    HB3    sing N N 362 
PRO CG    CD     sing N N 363 
PRO CG    HG2    sing N N 364 
PRO CG    HG3    sing N N 365 
PRO CD    HD2    sing N N 366 
PRO CD    HD3    sing N N 367 
PRO OXT   HXT    sing N N 368 
SER N     CA     sing N N 369 
SER N     H      sing N N 370 
SER N     H2     sing N N 371 
SER CA    C      sing N N 372 
SER CA    CB     sing N N 373 
SER CA    HA     sing N N 374 
SER C     O      doub N N 375 
SER C     OXT    sing N N 376 
SER CB    OG     sing N N 377 
SER CB    HB2    sing N N 378 
SER CB    HB3    sing N N 379 
SER OG    HG     sing N N 380 
SER OXT   HXT    sing N N 381 
THR N     CA     sing N N 382 
THR N     H      sing N N 383 
THR N     H2     sing N N 384 
THR CA    C      sing N N 385 
THR CA    CB     sing N N 386 
THR CA    HA     sing N N 387 
THR C     O      doub N N 388 
THR C     OXT    sing N N 389 
THR CB    OG1    sing N N 390 
THR CB    CG2    sing N N 391 
THR CB    HB     sing N N 392 
THR OG1   HG1    sing N N 393 
THR CG2   HG21   sing N N 394 
THR CG2   HG22   sing N N 395 
THR CG2   HG23   sing N N 396 
THR OXT   HXT    sing N N 397 
TRP N     CA     sing N N 398 
TRP N     H      sing N N 399 
TRP N     H2     sing N N 400 
TRP CA    C      sing N N 401 
TRP CA    CB     sing N N 402 
TRP CA    HA     sing N N 403 
TRP C     O      doub N N 404 
TRP C     OXT    sing N N 405 
TRP CB    CG     sing N N 406 
TRP CB    HB2    sing N N 407 
TRP CB    HB3    sing N N 408 
TRP CG    CD1    doub Y N 409 
TRP CG    CD2    sing Y N 410 
TRP CD1   NE1    sing Y N 411 
TRP CD1   HD1    sing N N 412 
TRP CD2   CE2    doub Y N 413 
TRP CD2   CE3    sing Y N 414 
TRP NE1   CE2    sing Y N 415 
TRP NE1   HE1    sing N N 416 
TRP CE2   CZ2    sing Y N 417 
TRP CE3   CZ3    doub Y N 418 
TRP CE3   HE3    sing N N 419 
TRP CZ2   CH2    doub Y N 420 
TRP CZ2   HZ2    sing N N 421 
TRP CZ3   CH2    sing Y N 422 
TRP CZ3   HZ3    sing N N 423 
TRP CH2   HH2    sing N N 424 
TRP OXT   HXT    sing N N 425 
TTP PA    O1A    doub N N 426 
TTP PA    O2A    sing N N 427 
TTP PA    O3A    sing N N 428 
TTP PA    "O5'"  sing N N 429 
TTP O2A   HOA2   sing N N 430 
TTP O3A   PB     sing N N 431 
TTP PB    O1B    doub N N 432 
TTP PB    O2B    sing N N 433 
TTP PB    O3B    sing N N 434 
TTP O2B   HOB2   sing N N 435 
TTP O3B   PG     sing N N 436 
TTP PG    O1G    doub N N 437 
TTP PG    O2G    sing N N 438 
TTP PG    O3G    sing N N 439 
TTP O2G   HOG2   sing N N 440 
TTP O3G   HOG3   sing N N 441 
TTP "O5'" "C5'"  sing N N 442 
TTP "C5'" "C4'"  sing N N 443 
TTP "C5'" "H5'1" sing N N 444 
TTP "C5'" "H5'2" sing N N 445 
TTP "C4'" "O4'"  sing N N 446 
TTP "C4'" "C3'"  sing N N 447 
TTP "C4'" "H4'"  sing N N 448 
TTP "O4'" "C1'"  sing N N 449 
TTP "C3'" "O3'"  sing N N 450 
TTP "C3'" "C2'"  sing N N 451 
TTP "C3'" "H3'"  sing N N 452 
TTP "O3'" "HO3'" sing N N 453 
TTP "C2'" "C1'"  sing N N 454 
TTP "C2'" "H2'1" sing N N 455 
TTP "C2'" "H2'2" sing N N 456 
TTP "C1'" N1     sing N N 457 
TTP "C1'" "H1'"  sing N N 458 
TTP N1    C2     sing N N 459 
TTP N1    C6     sing N N 460 
TTP C2    O2     doub N N 461 
TTP C2    N3     sing N N 462 
TTP N3    C4     sing N N 463 
TTP N3    HN3    sing N N 464 
TTP C4    O4     doub N N 465 
TTP C4    C5     sing N N 466 
TTP C5    C5M    sing N N 467 
TTP C5    C6     doub N N 468 
TTP C5M   HM51   sing N N 469 
TTP C5M   HM52   sing N N 470 
TTP C5M   HM53   sing N N 471 
TTP C6    H6     sing N N 472 
TYR N     CA     sing N N 473 
TYR N     H      sing N N 474 
TYR N     H2     sing N N 475 
TYR CA    C      sing N N 476 
TYR CA    CB     sing N N 477 
TYR CA    HA     sing N N 478 
TYR C     O      doub N N 479 
TYR C     OXT    sing N N 480 
TYR CB    CG     sing N N 481 
TYR CB    HB2    sing N N 482 
TYR CB    HB3    sing N N 483 
TYR CG    CD1    doub Y N 484 
TYR CG    CD2    sing Y N 485 
TYR CD1   CE1    sing Y N 486 
TYR CD1   HD1    sing N N 487 
TYR CD2   CE2    doub Y N 488 
TYR CD2   HD2    sing N N 489 
TYR CE1   CZ     doub Y N 490 
TYR CE1   HE1    sing N N 491 
TYR CE2   CZ     sing Y N 492 
TYR CE2   HE2    sing N N 493 
TYR CZ    OH     sing N N 494 
TYR OH    HH     sing N N 495 
TYR OXT   HXT    sing N N 496 
VAL N     CA     sing N N 497 
VAL N     H      sing N N 498 
VAL N     H2     sing N N 499 
VAL CA    C      sing N N 500 
VAL CA    CB     sing N N 501 
VAL CA    HA     sing N N 502 
VAL C     O      doub N N 503 
VAL C     OXT    sing N N 504 
VAL CB    CG1    sing N N 505 
VAL CB    CG2    sing N N 506 
VAL CB    HB     sing N N 507 
VAL CG1   HG11   sing N N 508 
VAL CG1   HG12   sing N N 509 
VAL CG1   HG13   sing N N 510 
VAL CG2   HG21   sing N N 511 
VAL CG2   HG22   sing N N 512 
VAL CG2   HG23   sing N N 513 
VAL OXT   HXT    sing N N 514 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-24 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BZF 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'Class 28 model for combined refinement 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 9BYH 
2 'experimental model' PDB 4DR0 
# 
_atom_sites.entry_id                    9BZF 
_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   ? 106.919 112.994 100.111 1.00 61.20 ?  6   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 6   ? 108.065 113.526 99.387  1.00 61.32 ?  6   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 6   ? 107.601 114.334 98.174  1.00 62.07 ?  6   VAL A C     1 
ATOM   4     O  O     . VAL A 1 6   ? 106.802 113.858 97.367  1.00 60.69 ?  6   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 6   ? 109.036 112.393 98.977  1.00 61.34 ?  6   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 6   ? 108.312 111.306 98.191  1.00 61.29 ?  6   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 6   ? 110.203 112.948 98.179  1.00 59.53 ?  6   VAL A CG2   1 
ATOM   8     N  N     . PRO A 1 7   ? 108.083 115.569 98.060  1.00 58.51 ?  7   PRO A N     1 
ATOM   9     C  CA    . PRO A 1 7   ? 107.684 116.416 96.930  1.00 54.85 ?  7   PRO A CA    1 
ATOM   10    C  C     . PRO A 1 7   ? 108.291 115.932 95.623  1.00 54.57 ?  7   PRO A C     1 
ATOM   11    O  O     . PRO A 1 7   ? 109.312 115.243 95.592  1.00 55.81 ?  7   PRO A O     1 
ATOM   12    C  CB    . PRO A 1 7   ? 108.206 117.808 97.301  1.00 53.42 ?  7   PRO A CB    1 
ATOM   13    C  CG    . PRO A 1 7   ? 108.911 117.679 98.599  1.00 53.02 ?  7   PRO A CG    1 
ATOM   14    C  CD    . PRO A 1 7   ? 108.981 116.250 99.006  1.00 55.87 ?  7   PRO A CD    1 
ATOM   15    N  N     . LYS A 1 8   ? 107.638 116.322 94.524  1.00 54.03 ?  8   LYS A N     1 
ATOM   16    C  CA    . LYS A 1 8   ? 108.028 115.830 93.205  1.00 53.45 ?  8   LYS A CA    1 
ATOM   17    C  C     . LYS A 1 8   ? 109.444 116.259 92.840  1.00 55.16 ?  8   LYS A C     1 
ATOM   18    O  O     . LYS A 1 8   ? 110.216 115.467 92.284  1.00 57.31 ?  8   LYS A O     1 
ATOM   19    C  CB    . LYS A 1 8   ? 107.032 116.318 92.153  1.00 55.50 ?  8   LYS A CB    1 
ATOM   20    C  CG    . LYS A 1 8   ? 107.427 115.992 90.722  1.00 55.15 ?  8   LYS A CG    1 
ATOM   21    C  CD    . LYS A 1 8   ? 106.578 116.766 89.727  1.00 55.42 ?  8   LYS A CD    1 
ATOM   22    C  CE    . LYS A 1 8   ? 107.064 116.552 88.303  1.00 55.63 ?  8   LYS A CE    1 
ATOM   23    N  NZ    . LYS A 1 8   ? 106.445 117.518 87.353  1.00 56.86 1  8   LYS A NZ    1 
ATOM   24    N  N     . TRP A 1 9   ? 109.804 117.511 93.136  1.00 54.44 ?  9   TRP A N     1 
ATOM   25    C  CA    . TRP A 1 9   ? 111.144 117.979 92.803  1.00 52.69 ?  9   TRP A CA    1 
ATOM   26    C  C     . TRP A 1 9   ? 112.205 117.222 93.588  1.00 51.63 ?  9   TRP A C     1 
ATOM   27    O  O     . TRP A 1 9   ? 113.300 116.972 93.073  1.00 53.76 ?  9   TRP A O     1 
ATOM   28    C  CB    . TRP A 1 9   ? 111.266 119.483 93.050  1.00 52.54 ?  9   TRP A CB    1 
ATOM   29    C  CG    . TRP A 1 9   ? 111.000 119.910 94.461  1.00 49.94 ?  9   TRP A CG    1 
ATOM   30    C  CD1   . TRP A 1 9   ? 111.901 119.959 95.483  1.00 49.74 ?  9   TRP A CD1   1 
ATOM   31    C  CD2   . TRP A 1 9   ? 109.756 120.371 95.002  1.00 51.38 ?  9   TRP A CD2   1 
ATOM   32    N  NE1   . TRP A 1 9   ? 111.295 120.411 96.630  1.00 49.45 ?  9   TRP A NE1   1 
ATOM   33    C  CE2   . TRP A 1 9   ? 109.979 120.672 96.361  1.00 51.17 ?  9   TRP A CE2   1 
ATOM   34    C  CE3   . TRP A 1 9   ? 108.477 120.553 94.472  1.00 49.58 ?  9   TRP A CE3   1 
ATOM   35    C  CZ2   . TRP A 1 9   ? 108.969 121.146 97.194  1.00 49.84 ?  9   TRP A CZ2   1 
ATOM   36    C  CZ3   . TRP A 1 9   ? 107.476 121.021 95.301  1.00 51.27 ?  9   TRP A CZ3   1 
ATOM   37    C  CH2   . TRP A 1 9   ? 107.727 121.310 96.648  1.00 51.47 ?  9   TRP A CH2   1 
ATOM   38    N  N     . ILE A 1 10  ? 111.896 116.828 94.824  1.00 54.01 ?  10  ILE A N     1 
ATOM   39    C  CA    . ILE A 1 10  ? 112.856 116.066 95.614  1.00 53.77 ?  10  ILE A CA    1 
ATOM   40    C  C     . ILE A 1 10  ? 113.039 114.667 95.034  1.00 53.66 ?  10  ILE A C     1 
ATOM   41    O  O     . ILE A 1 10  ? 114.154 114.135 95.009  1.00 56.41 ?  10  ILE A O     1 
ATOM   42    C  CB    . ILE A 1 10  ? 112.423 116.030 97.090  1.00 54.66 ?  10  ILE A CB    1 
ATOM   43    C  CG1   . ILE A 1 10  ? 112.591 117.418 97.711  1.00 54.34 ?  10  ILE A CG1   1 
ATOM   44    C  CG2   . ILE A 1 10  ? 113.236 115.006 97.865  1.00 54.60 ?  10  ILE A CG2   1 
ATOM   45    C  CD1   . ILE A 1 10  ? 112.490 117.441 99.215  1.00 55.93 ?  10  ILE A CD1   1 
ATOM   46    N  N     . GLN A 1 11  ? 111.957 114.049 94.552  1.00 57.00 ?  11  GLN A N     1 
ATOM   47    C  CA    . GLN A 1 11  ? 112.102 112.765 93.869  1.00 57.95 ?  11  GLN A CA    1 
ATOM   48    C  C     . GLN A 1 11  ? 112.934 112.907 92.601  1.00 57.73 ?  11  GLN A C     1 
ATOM   49    O  O     . GLN A 1 11  ? 113.805 112.074 92.324  1.00 59.00 ?  11  GLN A O     1 
ATOM   50    C  CB    . GLN A 1 11  ? 110.731 112.170 93.541  1.00 57.52 ?  11  GLN A CB    1 
ATOM   51    C  CG    . GLN A 1 11  ? 109.701 112.297 94.645  1.00 58.92 ?  11  GLN A CG    1 
ATOM   52    C  CD    . GLN A 1 11  ? 108.282 112.352 94.112  1.00 60.78 ?  11  GLN A CD    1 
ATOM   53    O  OE1   . GLN A 1 11  ? 108.050 112.191 92.915  1.00 58.86 ?  11  GLN A OE1   1 
ATOM   54    N  NE2   . GLN A 1 11  ? 107.325 112.581 95.004  1.00 58.93 ?  11  GLN A NE2   1 
ATOM   55    N  N     . LEU A 1 12  ? 112.685 113.962 91.821  1.00 53.91 ?  12  LEU A N     1 
ATOM   56    C  CA    . LEU A 1 12  ? 113.462 114.176 90.605  1.00 52.66 ?  12  LEU A CA    1 
ATOM   57    C  C     . LEU A 1 12  ? 114.930 114.438 90.917  1.00 54.69 ?  12  LEU A C     1 
ATOM   58    O  O     . LEU A 1 12  ? 115.807 114.083 90.122  1.00 56.24 ?  12  LEU A O     1 
ATOM   59    C  CB    . LEU A 1 12  ? 112.871 115.333 89.800  1.00 52.80 ?  12  LEU A CB    1 
ATOM   60    C  CG    . LEU A 1 12  ? 111.727 114.977 88.848  1.00 53.51 ?  12  LEU A CG    1 
ATOM   61    C  CD1   . LEU A 1 12  ? 111.041 116.233 88.336  1.00 55.35 ?  12  LEU A CD1   1 
ATOM   62    C  CD2   . LEU A 1 12  ? 112.237 114.132 87.693  1.00 52.97 ?  12  LEU A CD2   1 
ATOM   63    N  N     . ASN A 1 13  ? 115.216 115.061 92.061  1.00 53.32 ?  13  ASN A N     1 
ATOM   64    C  CA    . ASN A 1 13  ? 116.599 115.292 92.462  1.00 51.61 ?  13  ASN A CA    1 
ATOM   65    C  C     . ASN A 1 13  ? 117.268 114.008 92.941  1.00 53.33 ?  13  ASN A C     1 
ATOM   66    O  O     . ASN A 1 13  ? 118.426 113.746 92.601  1.00 57.21 ?  13  ASN A O     1 
ATOM   67    C  CB    . ASN A 1 13  ? 116.654 116.363 93.552  1.00 52.13 ?  13  ASN A CB    1 
ATOM   68    C  CG    . ASN A 1 13  ? 118.069 116.671 93.995  1.00 51.95 ?  13  ASN A CG    1 
ATOM   69    O  OD1   . ASN A 1 13  ? 118.542 116.152 95.004  1.00 52.22 ?  13  ASN A OD1   1 
ATOM   70    N  ND2   . ASN A 1 13  ? 118.752 117.521 93.237  1.00 53.37 ?  13  ASN A ND2   1 
ATOM   71    N  N     . ASN A 1 14  ? 116.559 113.199 93.731  1.00 56.37 ?  14  ASN A N     1 
ATOM   72    C  CA    . ASN A 1 14  ? 117.106 111.924 94.182  1.00 55.27 ?  14  ASN A CA    1 
ATOM   73    C  C     . ASN A 1 14  ? 117.229 110.914 93.052  1.00 55.96 ?  14  ASN A C     1 
ATOM   74    O  O     . ASN A 1 14  ? 117.954 109.924 93.198  1.00 59.84 ?  14  ASN A O     1 
ATOM   75    C  CB    . ASN A 1 14  ? 116.250 111.348 95.311  1.00 55.43 ?  14  ASN A CB    1 
ATOM   76    C  CG    . ASN A 1 14  ? 116.250 112.226 96.547  1.00 58.93 ?  14  ASN A CG    1 
ATOM   77    O  OD1   . ASN A 1 14  ? 116.338 113.449 96.455  1.00 59.21 ?  14  ASN A OD1   1 
ATOM   78    N  ND2   . ASN A 1 14  ? 116.148 111.601 97.714  1.00 59.70 ?  14  ASN A ND2   1 
ATOM   79    N  N     . GLU A 1 15  ? 116.544 111.138 91.930  1.00 57.11 ?  15  GLU A N     1 
ATOM   80    C  CA    . GLU A 1 15  ? 116.713 110.268 90.774  1.00 58.53 ?  15  GLU A CA    1 
ATOM   81    C  C     . GLU A 1 15  ? 118.079 110.418 90.115  1.00 58.60 ?  15  GLU A C     1 
ATOM   82    O  O     . GLU A 1 15  ? 118.400 109.632 89.217  1.00 61.66 ?  15  GLU A O     1 
ATOM   83    C  CB    . GLU A 1 15  ? 115.607 110.530 89.749  1.00 58.15 ?  15  GLU A CB    1 
ATOM   84    C  CG    . GLU A 1 15  ? 114.285 109.858 90.088  1.00 58.81 ?  15  GLU A CG    1 
ATOM   85    C  CD    . GLU A 1 15  ? 113.158 110.273 89.163  1.00 61.24 ?  15  GLU A CD    1 
ATOM   86    O  OE1   . GLU A 1 15  ? 113.439 110.610 87.995  1.00 60.87 ?  15  GLU A OE1   1 
ATOM   87    O  OE2   . GLU A 1 15  ? 111.990 110.264 89.604  1.00 59.03 -1 15  GLU A OE2   1 
ATOM   88    N  N     . ILE A 1 16  ? 118.878 111.407 90.524  1.00 58.15 ?  16  ILE A N     1 
ATOM   89    C  CA    . ILE A 1 16  ? 120.225 111.562 89.973  1.00 58.69 ?  16  ILE A CA    1 
ATOM   90    C  C     . ILE A 1 16  ? 121.076 110.343 90.302  1.00 57.58 ?  16  ILE A C     1 
ATOM   91    O  O     . ILE A 1 16  ? 121.768 109.793 89.437  1.00 58.61 ?  16  ILE A O     1 
ATOM   92    C  CB    . ILE A 1 16  ? 120.876 112.852 90.503  1.00 57.30 ?  16  ILE A CB    1 
ATOM   93    C  CG1   . ILE A 1 16  ? 120.242 114.085 89.865  1.00 56.73 ?  16  ILE A CG1   1 
ATOM   94    C  CG2   . ILE A 1 16  ? 122.378 112.838 90.253  1.00 57.89 ?  16  ILE A CG2   1 
ATOM   95    C  CD1   . ILE A 1 16  ? 120.400 115.326 90.700  1.00 56.64 ?  16  ILE A CD1   1 
ATOM   96    N  N     . MET A 1 17  ? 121.038 109.903 91.563  1.00 57.91 ?  17  MET A N     1 
ATOM   97    C  CA    . MET A 1 17  ? 121.877 108.786 91.985  1.00 60.77 ?  17  MET A CA    1 
ATOM   98    C  C     . MET A 1 17  ? 121.473 107.486 91.307  1.00 60.83 ?  17  MET A C     1 
ATOM   99    O  O     . MET A 1 17  ? 122.308 106.590 91.144  1.00 61.69 ?  17  MET A O     1 
ATOM   100   C  CB    . MET A 1 17  ? 121.816 108.629 93.504  1.00 60.42 ?  17  MET A CB    1 
ATOM   101   C  CG    . MET A 1 17  ? 122.238 109.866 94.276  1.00 59.88 ?  17  MET A CG    1 
ATOM   102   S  SD    . MET A 1 17  ? 123.393 110.943 93.407  1.00 62.45 ?  17  MET A SD    1 
ATOM   103   C  CE    . MET A 1 17  ? 124.910 110.007 93.571  1.00 58.33 ?  17  MET A CE    1 
ATOM   104   N  N     . ILE A 1 18  ? 120.207 107.358 90.915  1.00 63.10 ?  18  ILE A N     1 
ATOM   105   C  CA    . ILE A 1 18  ? 119.749 106.169 90.202  1.00 63.93 ?  18  ILE A CA    1 
ATOM   106   C  C     . ILE A 1 18  ? 120.462 106.142 88.854  1.00 64.49 ?  18  ILE A C     1 
ATOM   107   O  O     . ILE A 1 18  ? 120.293 107.047 88.032  1.00 66.32 ?  18  ILE A O     1 
ATOM   108   C  CB    . ILE A 1 18  ? 118.222 106.151 90.034  1.00 63.43 ?  18  ILE A CB    1 
ATOM   109   C  CG1   . ILE A 1 18  ? 117.502 105.645 91.297  1.00 64.00 ?  18  ILE A CG1   1 
ATOM   110   C  CG2   . ILE A 1 18  ? 117.823 105.279 88.852  1.00 63.67 ?  18  ILE A CG2   1 
ATOM   111   C  CD1   . ILE A 1 18  ? 118.006 106.173 92.627  1.00 63.77 ?  18  ILE A CD1   1 
ATOM   112   N  N     . GLN A 1 19  ? 121.274 105.113 88.631  1.00 67.59 ?  19  GLN A N     1 
ATOM   113   C  CA    . GLN A 1 19  ? 122.139 105.072 87.462  1.00 69.12 ?  19  GLN A CA    1 
ATOM   114   C  C     . GLN A 1 19  ? 121.427 104.409 86.289  1.00 70.12 ?  19  GLN A C     1 
ATOM   115   O  O     . GLN A 1 19  ? 120.893 103.304 86.418  1.00 70.79 ?  19  GLN A O     1 
ATOM   116   C  CB    . GLN A 1 19  ? 123.433 104.326 87.788  1.00 70.18 ?  19  GLN A CB    1 
ATOM   117   C  CG    . GLN A 1 19  ? 124.407 105.129 88.636  1.00 68.31 ?  19  GLN A CG    1 
ATOM   118   C  CD    . GLN A 1 19  ? 125.830 104.618 88.534  1.00 70.65 ?  19  GLN A CD    1 
ATOM   119   O  OE1   . GLN A 1 19  ? 126.146 103.800 87.670  1.00 71.53 ?  19  GLN A OE1   1 
ATOM   120   N  NE2   . GLN A 1 19  ? 126.696 105.100 89.416  1.00 69.08 ?  19  GLN A NE2   1 
ATOM   121   N  N     . LYS A 1 20  ? 121.422 105.091 85.149  1.00 72.27 ?  20  LYS A N     1 
ATOM   122   C  CA    . LYS A 1 20  ? 120.887 104.557 83.905  1.00 73.91 ?  20  LYS A CA    1 
ATOM   123   C  C     . LYS A 1 20  ? 122.035 104.366 82.926  1.00 76.01 ?  20  LYS A C     1 
ATOM   124   O  O     . LYS A 1 20  ? 122.785 105.310 82.653  1.00 75.81 ?  20  LYS A O     1 
ATOM   125   C  CB    . LYS A 1 20  ? 119.823 105.490 83.320  1.00 71.70 ?  20  LYS A CB    1 
ATOM   126   C  CG    . LYS A 1 20  ? 119.593 105.328 81.825  1.00 73.05 ?  20  LYS A CG    1 
ATOM   127   C  CD    . LYS A 1 20  ? 120.160 106.503 81.044  1.00 74.70 ?  20  LYS A CD    1 
ATOM   128   C  CE    . LYS A 1 20  ? 120.473 106.113 79.608  1.00 74.77 ?  20  LYS A CE    1 
ATOM   129   N  NZ    . LYS A 1 20  ? 120.531 107.301 78.711  1.00 74.65 1  20  LYS A NZ    1 
ATOM   130   N  N     . ASP A 1 21  ? 122.171 103.144 82.408  1.00 77.71 ?  21  ASP A N     1 
ATOM   131   C  CA    . ASP A 1 21  ? 123.278 102.776 81.524  1.00 78.08 ?  21  ASP A CA    1 
ATOM   132   C  C     . ASP A 1 21  ? 124.627 103.035 82.195  1.00 78.21 ?  21  ASP A C     1 
ATOM   133   O  O     . ASP A 1 21  ? 125.596 103.445 81.551  1.00 77.84 ?  21  ASP A O     1 
ATOM   134   C  CB    . ASP A 1 21  ? 123.185 103.506 80.181  1.00 78.03 ?  21  ASP A CB    1 
ATOM   135   C  CG    . ASP A 1 21  ? 123.976 102.817 79.086  1.00 79.20 ?  21  ASP A CG    1 
ATOM   136   O  OD1   . ASP A 1 21  ? 123.920 101.571 79.006  1.00 77.85 ?  21  ASP A OD1   1 
ATOM   137   O  OD2   . ASP A 1 21  ? 124.654 103.520 78.307  1.00 77.64 -1 21  ASP A OD2   1 
ATOM   138   N  N     . GLY A 1 22  ? 124.688 102.799 83.502  1.00 74.06 ?  22  GLY A N     1 
ATOM   139   C  CA    . GLY A 1 22  ? 125.917 103.004 84.241  1.00 72.25 ?  22  GLY A CA    1 
ATOM   140   C  C     . GLY A 1 22  ? 126.342 104.446 84.384  1.00 73.50 ?  22  GLY A C     1 
ATOM   141   O  O     . GLY A 1 22  ? 127.519 104.710 84.643  1.00 74.68 ?  22  GLY A O     1 
ATOM   142   N  N     . LYS A 1 23  ? 125.419 105.392 84.225  1.00 69.34 ?  23  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 23  ? 125.730 106.809 84.322  1.00 67.22 ?  23  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 23  ? 124.708 107.506 85.207  1.00 68.95 ?  23  LYS A C     1 
ATOM   145   O  O     . LYS A 1 23  ? 123.530 107.141 85.232  1.00 70.38 ?  23  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 23  ? 125.756 107.478 82.940  1.00 68.25 ?  23  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 23  ? 126.858 106.978 82.025  1.00 68.58 ?  23  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 23  ? 126.696 107.530 80.620  1.00 68.77 ?  23  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 23  ? 127.657 106.865 79.651  1.00 71.00 ?  23  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 23  ? 127.373 107.241 78.240  1.00 69.00 1  23  LYS A NZ    1 
ATOM   151   N  N     . PHE A 1 24  ? 125.175 108.515 85.936  1.00 62.03 ?  24  PHE A N     1 
ATOM   152   C  CA    . PHE A 1 24  ? 124.284 109.311 86.767  1.00 59.31 ?  24  PHE A CA    1 
ATOM   153   C  C     . PHE A 1 24  ? 123.373 110.165 85.896  1.00 59.62 ?  24  PHE A C     1 
ATOM   154   O  O     . PHE A 1 24  ? 123.800 110.718 84.879  1.00 59.64 ?  24  PHE A O     1 
ATOM   155   C  CB    . PHE A 1 24  ? 125.091 110.199 87.712  1.00 57.58 ?  24  PHE A CB    1 
ATOM   156   C  CG    . PHE A 1 24  ? 125.873 109.437 88.741  1.00 59.16 ?  24  PHE A CG    1 
ATOM   157   C  CD1   . PHE A 1 24  ? 125.252 108.931 89.867  1.00 60.30 ?  24  PHE A CD1   1 
ATOM   158   C  CD2   . PHE A 1 24  ? 127.233 109.229 88.581  1.00 60.20 ?  24  PHE A CD2   1 
ATOM   159   C  CE1   . PHE A 1 24  ? 125.971 108.228 90.813  1.00 61.28 ?  24  PHE A CE1   1 
ATOM   160   C  CE2   . PHE A 1 24  ? 127.957 108.530 89.526  1.00 58.77 ?  24  PHE A CE2   1 
ATOM   161   C  CZ    . PHE A 1 24  ? 127.324 108.030 90.644  1.00 59.24 ?  24  PHE A CZ    1 
ATOM   162   N  N     . GLN A 1 25  ? 122.107 110.269 86.299  1.00 59.49 ?  25  GLN A N     1 
ATOM   163   C  CA    . GLN A 1 25  ? 121.127 111.072 85.569  1.00 61.28 ?  25  GLN A CA    1 
ATOM   164   C  C     . GLN A 1 25  ? 121.244 112.521 86.034  1.00 60.68 ?  25  GLN A C     1 
ATOM   165   O  O     . GLN A 1 25  ? 120.420 113.042 86.789  1.00 62.38 ?  25  GLN A O     1 
ATOM   166   C  CB    . GLN A 1 25  ? 119.721 110.523 85.774  1.00 61.69 ?  25  GLN A CB    1 
ATOM   167   C  CG    . GLN A 1 25  ? 119.494 109.155 85.157  1.00 60.60 ?  25  GLN A CG    1 
ATOM   168   C  CD    . GLN A 1 25  ? 118.173 108.542 85.573  1.00 61.28 ?  25  GLN A CD    1 
ATOM   169   O  OE1   . GLN A 1 25  ? 117.141 108.782 84.948  1.00 60.75 ?  25  GLN A OE1   1 
ATOM   170   N  NE2   . GLN A 1 25  ? 118.200 107.744 86.633  1.00 60.63 ?  25  GLN A NE2   1 
ATOM   171   N  N     . PHE A 1 26  ? 122.309 113.178 85.570  1.00 56.32 ?  26  PHE A N     1 
ATOM   172   C  CA    . PHE A 1 26  ? 122.537 114.574 85.930  1.00 54.81 ?  26  PHE A CA    1 
ATOM   173   C  C     . PHE A 1 26  ? 121.451 115.478 85.360  1.00 56.40 ?  26  PHE A C     1 
ATOM   174   O  O     . PHE A 1 26  ? 120.983 116.400 86.042  1.00 56.54 ?  26  PHE A O     1 
ATOM   175   C  CB    . PHE A 1 26  ? 123.915 115.020 85.442  1.00 51.71 ?  26  PHE A CB    1 
ATOM   176   C  CG    . PHE A 1 26  ? 125.055 114.324 86.129  1.00 54.69 ?  26  PHE A CG    1 
ATOM   177   C  CD1   . PHE A 1 26  ? 125.135 114.296 87.510  1.00 52.92 ?  26  PHE A CD1   1 
ATOM   178   C  CD2   . PHE A 1 26  ? 126.045 113.698 85.392  1.00 52.64 ?  26  PHE A CD2   1 
ATOM   179   C  CE1   . PHE A 1 26  ? 126.183 113.658 88.144  1.00 52.85 ?  26  PHE A CE1   1 
ATOM   180   C  CE2   . PHE A 1 26  ? 127.094 113.056 86.020  1.00 50.88 ?  26  PHE A CE2   1 
ATOM   181   C  CZ    . PHE A 1 26  ? 127.164 113.038 87.397  1.00 52.70 ?  26  PHE A CZ    1 
ATOM   182   N  N     . ASP A 1 27  ? 121.035 115.225 84.116  1.00 58.64 ?  27  ASP A N     1 
ATOM   183   C  CA    . ASP A 1 27  ? 120.031 116.069 83.475  1.00 58.79 ?  27  ASP A CA    1 
ATOM   184   C  C     . ASP A 1 27  ? 118.723 116.087 84.255  1.00 59.03 ?  27  ASP A C     1 
ATOM   185   O  O     . ASP A 1 27  ? 117.989 117.083 84.212  1.00 59.44 ?  27  ASP A O     1 
ATOM   186   C  CB    . ASP A 1 27  ? 119.793 115.598 82.038  1.00 59.79 ?  27  ASP A CB    1 
ATOM   187   C  CG    . ASP A 1 27  ? 119.359 114.144 81.960  1.00 62.16 ?  27  ASP A CG    1 
ATOM   188   O  OD1   . ASP A 1 27  ? 118.243 113.821 82.417  1.00 62.25 ?  27  ASP A OD1   1 
ATOM   189   O  OD2   . ASP A 1 27  ? 120.139 113.321 81.439  1.00 62.20 -1 27  ASP A OD2   1 
ATOM   190   N  N     . LYS A 1 28  ? 118.422 115.005 84.981  1.00 56.53 ?  28  LYS A N     1 
ATOM   191   C  CA    . LYS A 1 28  ? 117.212 114.972 85.795  1.00 58.97 ?  28  LYS A CA    1 
ATOM   192   C  C     . LYS A 1 28  ? 117.175 116.127 86.784  1.00 59.60 ?  28  LYS A C     1 
ATOM   193   O  O     . LYS A 1 28  ? 116.095 116.653 87.080  1.00 59.48 ?  28  LYS A O     1 
ATOM   194   C  CB    . LYS A 1 28  ? 117.111 113.637 86.532  1.00 58.52 ?  28  LYS A CB    1 
ATOM   195   C  CG    . LYS A 1 28  ? 116.572 112.500 85.683  1.00 60.37 ?  28  LYS A CG    1 
ATOM   196   C  CD    . LYS A 1 28  ? 115.081 112.315 85.893  1.00 59.68 ?  28  LYS A CD    1 
ATOM   197   C  CE    . LYS A 1 28  ? 114.425 111.695 84.673  1.00 58.32 ?  28  LYS A CE    1 
ATOM   198   N  NZ    . LYS A 1 28  ? 114.628 112.525 83.454  1.00 59.76 1  28  LYS A NZ    1 
ATOM   199   N  N     . ASP A 1 29  ? 118.343 116.546 87.282  1.00 57.46 ?  29  ASP A N     1 
ATOM   200   C  CA    . ASP A 1 29  ? 118.396 117.696 88.181  1.00 54.95 ?  29  ASP A CA    1 
ATOM   201   C  C     . ASP A 1 29  ? 117.710 118.903 87.563  1.00 53.98 ?  29  ASP A C     1 
ATOM   202   O  O     . ASP A 1 29  ? 116.918 119.581 88.229  1.00 56.72 ?  29  ASP A O     1 
ATOM   203   C  CB    . ASP A 1 29  ? 119.846 118.031 88.526  1.00 55.38 ?  29  ASP A CB    1 
ATOM   204   C  CG    . ASP A 1 29  ? 119.985 118.676 89.891  1.00 56.18 ?  29  ASP A CG    1 
ATOM   205   O  OD1   . ASP A 1 29  ? 119.122 118.429 90.759  1.00 55.71 ?  29  ASP A OD1   1 
ATOM   206   O  OD2   . ASP A 1 29  ? 120.961 119.427 90.098  1.00 55.40 -1 29  ASP A OD2   1 
ATOM   207   N  N     . LYS A 1 30  ? 117.973 119.164 86.279  1.00 54.92 ?  30  LYS A N     1 
ATOM   208   C  CA    . LYS A 1 30  ? 117.313 120.272 85.597  1.00 56.30 ?  30  LYS A CA    1 
ATOM   209   C  C     . LYS A 1 30  ? 115.800 120.147 85.707  1.00 55.88 ?  30  LYS A C     1 
ATOM   210   O  O     . LYS A 1 30  ? 115.111 121.104 86.079  1.00 58.29 ?  30  LYS A O     1 
ATOM   211   C  CB    . LYS A 1 30  ? 117.746 120.318 84.131  1.00 57.24 ?  30  LYS A CB    1 
ATOM   212   C  CG    . LYS A 1 30  ? 119.234 120.556 83.930  1.00 59.30 ?  30  LYS A CG    1 
ATOM   213   C  CD    . LYS A 1 30  ? 119.598 120.566 82.453  1.00 59.58 ?  30  LYS A CD    1 
ATOM   214   C  CE    . LYS A 1 30  ? 121.104 120.519 82.256  1.00 58.77 ?  30  LYS A CE    1 
ATOM   215   N  NZ    . LYS A 1 30  ? 121.482 119.914 80.949  1.00 58.18 1  30  LYS A NZ    1 
ATOM   216   N  N     . GLU A 1 31  ? 115.273 118.949 85.435  1.00 57.35 ?  31  GLU A N     1 
ATOM   217   C  CA    . GLU A 1 31  ? 113.837 118.732 85.567  1.00 56.70 ?  31  GLU A CA    1 
ATOM   218   C  C     . GLU A 1 31  ? 113.367 119.072 86.973  1.00 56.29 ?  31  GLU A C     1 
ATOM   219   O  O     . GLU A 1 31  ? 112.339 119.738 87.147  1.00 58.26 ?  31  GLU A O     1 
ATOM   220   C  CB    . GLU A 1 31  ? 113.486 117.284 85.216  1.00 56.01 ?  31  GLU A CB    1 
ATOM   221   C  CG    . GLU A 1 31  ? 114.243 116.681 84.024  1.00 58.50 ?  31  GLU A CG    1 
ATOM   222   C  CD    . GLU A 1 31  ? 113.952 117.357 82.685  1.00 61.13 ?  31  GLU A CD    1 
ATOM   223   O  OE1   . GLU A 1 31  ? 114.056 118.596 82.576  1.00 60.18 ?  31  GLU A OE1   1 
ATOM   224   O  OE2   . GLU A 1 31  ? 113.613 116.628 81.729  1.00 59.93 -1 31  GLU A OE2   1 
ATOM   225   N  N     . ALA A 1 32  ? 114.139 118.663 87.984  1.00 50.08 ?  32  ALA A N     1 
ATOM   226   C  CA    . ALA A 1 32  ? 113.793 118.984 89.363  1.00 48.71 ?  32  ALA A CA    1 
ATOM   227   C  C     . ALA A 1 32  ? 113.585 120.481 89.532  1.00 52.68 ?  32  ALA A C     1 
ATOM   228   O  O     . ALA A 1 32  ? 112.583 120.917 90.114  1.00 55.36 ?  32  ALA A O     1 
ATOM   229   C  CB    . ALA A 1 32  ? 114.882 118.476 90.310  1.00 47.76 ?  32  ALA A CB    1 
ATOM   230   N  N     . VAL A 1 33  ? 114.496 121.286 88.974  1.00 50.76 ?  33  VAL A N     1 
ATOM   231   C  CA    . VAL A 1 33  ? 114.364 122.736 89.084  1.00 49.52 ?  33  VAL A CA    1 
ATOM   232   C  C     . VAL A 1 33  ? 113.009 123.170 88.552  1.00 50.65 ?  33  VAL A C     1 
ATOM   233   O  O     . VAL A 1 33  ? 112.265 123.901 89.217  1.00 52.98 ?  33  VAL A O     1 
ATOM   234   C  CB    . VAL A 1 33  ? 115.505 123.449 88.337  1.00 50.41 ?  33  VAL A CB    1 
ATOM   235   C  CG1   . VAL A 1 33  ? 115.683 124.864 88.869  1.00 48.62 ?  33  VAL A CG1   1 
ATOM   236   C  CG2   . VAL A 1 33  ? 116.786 122.665 88.441  1.00 50.88 ?  33  VAL A CG2   1 
ATOM   237   N  N     . HIS A 1 34  ? 112.649 122.675 87.365  1.00 47.66 ?  34  HIS A N     1 
ATOM   238   C  CA    . HIS A 1 34  ? 111.352 123.004 86.789  1.00 47.52 ?  34  HIS A CA    1 
ATOM   239   C  C     . HIS A 1 34  ? 110.238 122.661 87.764  1.00 50.23 ?  34  HIS A C     1 
ATOM   240   O  O     . HIS A 1 34  ? 109.383 123.501 88.072  1.00 54.05 ?  34  HIS A O     1 
ATOM   241   C  CB    . HIS A 1 34  ? 111.171 122.264 85.465  1.00 50.92 ?  34  HIS A CB    1 
ATOM   242   C  CG    . HIS A 1 34  ? 110.340 123.007 84.466  1.00 50.54 ?  34  HIS A CG    1 
ATOM   243   N  ND1   . HIS A 1 34  ? 109.051 123.415 84.727  1.00 53.04 ?  34  HIS A ND1   1 
ATOM   244   C  CD2   . HIS A 1 34  ? 110.618 123.419 83.207  1.00 51.78 ?  34  HIS A CD2   1 
ATOM   245   C  CE1   . HIS A 1 34  ? 108.569 124.043 83.670  1.00 54.94 ?  34  HIS A CE1   1 
ATOM   246   N  NE2   . HIS A 1 34  ? 109.499 124.060 82.734  1.00 54.28 ?  34  HIS A NE2   1 
ATOM   247   N  N     . SER A 1 35  ? 110.276 121.446 88.318  1.00 48.83 ?  35  SER A N     1 
ATOM   248   C  CA    . SER A 1 35  ? 109.276 121.060 89.304  1.00 49.75 ?  35  SER A CA    1 
ATOM   249   C  C     . SER A 1 35  ? 109.311 122.006 90.493  1.00 50.04 ?  35  SER A C     1 
ATOM   250   O  O     . SER A 1 35  ? 108.271 122.516 90.927  1.00 52.60 ?  35  SER A O     1 
ATOM   251   C  CB    . SER A 1 35  ? 109.507 119.616 89.748  1.00 50.64 ?  35  SER A CB    1 
ATOM   252   O  OG    . SER A 1 35  ? 108.659 119.272 90.830  1.00 52.65 ?  35  SER A OG    1 
ATOM   253   N  N     . TYR A 1 36  ? 110.516 122.306 90.990  1.00 47.40 ?  36  TYR A N     1 
ATOM   254   C  CA    . TYR A 1 36  ? 110.640 123.183 92.148  1.00 48.30 ?  36  TYR A CA    1 
ATOM   255   C  C     . TYR A 1 36  ? 110.043 124.553 91.868  1.00 46.43 ?  36  TYR A C     1 
ATOM   256   O  O     . TYR A 1 36  ? 109.637 125.255 92.799  1.00 46.71 ?  36  TYR A O     1 
ATOM   257   C  CB    . TYR A 1 36  ? 112.106 123.311 92.558  1.00 46.66 ?  36  TYR A CB    1 
ATOM   258   C  CG    . TYR A 1 36  ? 112.321 124.091 93.834  1.00 45.89 ?  36  TYR A CG    1 
ATOM   259   C  CD1   . TYR A 1 36  ? 111.749 123.676 95.029  1.00 46.40 ?  36  TYR A CD1   1 
ATOM   260   C  CD2   . TYR A 1 36  ? 113.102 125.238 93.847  1.00 45.04 ?  36  TYR A CD2   1 
ATOM   261   C  CE1   . TYR A 1 36  ? 111.946 124.383 96.199  1.00 44.74 ?  36  TYR A CE1   1 
ATOM   262   C  CE2   . TYR A 1 36  ? 113.304 125.951 95.011  1.00 44.92 ?  36  TYR A CE2   1 
ATOM   263   C  CZ    . TYR A 1 36  ? 112.725 125.520 96.184  1.00 45.50 ?  36  TYR A CZ    1 
ATOM   264   O  OH    . TYR A 1 36  ? 112.925 126.230 97.345  1.00 47.43 ?  36  TYR A OH    1 
ATOM   265   N  N     . PHE A 1 37  ? 109.964 124.941 90.597  1.00 48.48 ?  37  PHE A N     1 
ATOM   266   C  CA    . PHE A 1 37  ? 109.320 126.192 90.232  1.00 49.98 ?  37  PHE A CA    1 
ATOM   267   C  C     . PHE A 1 37  ? 107.874 126.010 89.804  1.00 52.80 ?  37  PHE A C     1 
ATOM   268   O  O     . PHE A 1 37  ? 107.070 126.929 89.979  1.00 56.29 ?  37  PHE A O     1 
ATOM   269   C  CB    . PHE A 1 37  ? 110.104 126.886 89.114  1.00 51.07 ?  37  PHE A CB    1 
ATOM   270   C  CG    . PHE A 1 37  ? 111.308 127.634 89.604  1.00 51.02 ?  37  PHE A CG    1 
ATOM   271   C  CD1   . PHE A 1 37  ? 111.200 128.948 90.025  1.00 50.72 ?  37  PHE A CD1   1 
ATOM   272   C  CD2   . PHE A 1 37  ? 112.544 127.018 89.662  1.00 50.97 ?  37  PHE A CD2   1 
ATOM   273   C  CE1   . PHE A 1 37  ? 112.305 129.634 90.484  1.00 50.45 ?  37  PHE A CE1   1 
ATOM   274   C  CE2   . PHE A 1 37  ? 113.651 127.699 90.119  1.00 50.90 ?  37  PHE A CE2   1 
ATOM   275   C  CZ    . PHE A 1 37  ? 113.532 129.008 90.533  1.00 49.87 ?  37  PHE A CZ    1 
ATOM   276   N  N     . VAL A 1 38  ? 107.518 124.843 89.263  1.00 54.56 ?  38  VAL A N     1 
ATOM   277   C  CA    . VAL A 1 38  ? 106.142 124.644 88.820  1.00 53.41 ?  38  VAL A CA    1 
ATOM   278   C  C     . VAL A 1 38  ? 105.244 124.302 90.001  1.00 53.94 ?  38  VAL A C     1 
ATOM   279   O  O     . VAL A 1 38  ? 104.075 124.706 90.041  1.00 55.77 ?  38  VAL A O     1 
ATOM   280   C  CB    . VAL A 1 38  ? 106.092 123.567 87.720  1.00 53.67 ?  38  VAL A CB    1 
ATOM   281   C  CG1   . VAL A 1 38  ? 104.756 122.838 87.720  1.00 56.03 ?  38  VAL A CG1   1 
ATOM   282   C  CG2   . VAL A 1 38  ? 106.341 124.199 86.365  1.00 52.77 ?  38  VAL A CG2   1 
ATOM   283   N  N     . ASP A 1 39  ? 105.771 123.586 90.991  1.00 52.80 ?  39  ASP A N     1 
ATOM   284   C  CA    . ASP A 1 39  ? 104.977 123.109 92.114  1.00 53.63 ?  39  ASP A CA    1 
ATOM   285   C  C     . ASP A 1 39  ? 105.061 124.007 93.341  1.00 57.33 ?  39  ASP A C     1 
ATOM   286   O  O     . ASP A 1 39  ? 104.055 124.186 94.034  1.00 58.77 ?  39  ASP A O     1 
ATOM   287   C  CB    . ASP A 1 39  ? 105.409 121.691 92.497  1.00 55.81 ?  39  ASP A CB    1 
ATOM   288   C  CG    . ASP A 1 39  ? 105.510 120.770 91.298  1.00 57.71 ?  39  ASP A CG    1 
ATOM   289   O  OD1   . ASP A 1 39  ? 104.689 120.910 90.368  1.00 56.94 ?  39  ASP A OD1   1 
ATOM   290   O  OD2   . ASP A 1 39  ? 106.412 119.907 91.285  1.00 58.02 -1 39  ASP A OD2   1 
ATOM   291   N  N     . TYR A 1 40  ? 106.229 124.578 93.638  1.00 55.98 ?  40  TYR A N     1 
ATOM   292   C  CA    . TYR A 1 40  ? 106.435 125.281 94.898  1.00 53.64 ?  40  TYR A CA    1 
ATOM   293   C  C     . TYR A 1 40  ? 106.674 126.775 94.724  1.00 58.23 ?  40  TYR A C     1 
ATOM   294   O  O     . TYR A 1 40  ? 105.945 127.583 95.303  1.00 60.63 ?  40  TYR A O     1 
ATOM   295   C  CB    . TYR A 1 40  ? 107.606 124.647 95.659  1.00 53.89 ?  40  TYR A CB    1 
ATOM   296   C  CG    . TYR A 1 40  ? 107.707 125.095 97.100  1.00 54.81 ?  40  TYR A CG    1 
ATOM   297   C  CD1   . TYR A 1 40  ? 108.442 126.221 97.448  1.00 53.49 ?  40  TYR A CD1   1 
ATOM   298   C  CD2   . TYR A 1 40  ? 107.063 124.395 98.111  1.00 55.81 ?  40  TYR A CD2   1 
ATOM   299   C  CE1   . TYR A 1 40  ? 108.534 126.635 98.761  1.00 55.23 ?  40  TYR A CE1   1 
ATOM   300   C  CE2   . TYR A 1 40  ? 107.151 124.802 99.427  1.00 57.31 ?  40  TYR A CE2   1 
ATOM   301   C  CZ    . TYR A 1 40  ? 107.887 125.922 99.747  1.00 58.22 ?  40  TYR A CZ    1 
ATOM   302   O  OH    . TYR A 1 40  ? 107.976 126.330 101.057 1.00 57.01 ?  40  TYR A OH    1 
ATOM   303   N  N     . ILE A 1 41  ? 107.684 127.170 93.946  1.00 55.03 ?  41  ILE A N     1 
ATOM   304   C  CA    . ILE A 1 41  ? 108.130 128.562 93.967  1.00 51.74 ?  41  ILE A CA    1 
ATOM   305   C  C     . ILE A 1 41  ? 107.047 129.486 93.425  1.00 50.75 ?  41  ILE A C     1 
ATOM   306   O  O     . ILE A 1 41  ? 106.713 130.503 94.044  1.00 53.01 ?  41  ILE A O     1 
ATOM   307   C  CB    . ILE A 1 41  ? 109.449 128.721 93.192  1.00 49.42 ?  41  ILE A CB    1 
ATOM   308   C  CG1   . ILE A 1 41  ? 110.593 128.037 93.942  1.00 48.58 ?  41  ILE A CG1   1 
ATOM   309   C  CG2   . ILE A 1 41  ? 109.772 130.190 92.996  1.00 48.07 ?  41  ILE A CG2   1 
ATOM   310   C  CD1   . ILE A 1 41  ? 110.721 128.469 95.384  1.00 46.20 ?  41  ILE A CD1   1 
ATOM   311   N  N     . ASN A 1 42  ? 106.471 129.145 92.270  1.00 51.13 ?  42  ASN A N     1 
ATOM   312   C  CA    . ASN A 1 42  ? 105.444 130.003 91.687  1.00 51.45 ?  42  ASN A CA    1 
ATOM   313   C  C     . ASN A 1 42  ? 104.179 130.027 92.534  1.00 55.41 ?  42  ASN A C     1 
ATOM   314   O  O     . ASN A 1 42  ? 103.506 131.062 92.610  1.00 56.50 ?  42  ASN A O     1 
ATOM   315   C  CB    . ASN A 1 42  ? 105.128 129.552 90.261  1.00 52.87 ?  42  ASN A CB    1 
ATOM   316   C  CG    . ASN A 1 42  ? 106.306 129.718 89.324  1.00 53.98 ?  42  ASN A CG    1 
ATOM   317   O  OD1   . ASN A 1 42  ? 107.285 130.389 89.651  1.00 57.56 ?  42  ASN A OD1   1 
ATOM   318   N  ND2   . ASN A 1 42  ? 106.220 129.105 88.150  1.00 54.07 ?  42  ASN A ND2   1 
ATOM   319   N  N     . GLN A 1 43  ? 103.836 128.905 93.171  1.00 57.91 ?  43  GLN A N     1 
ATOM   320   C  CA    . GLN A 1 43  ? 102.642 128.863 94.009  1.00 55.47 ?  43  GLN A CA    1 
ATOM   321   C  C     . GLN A 1 43  ? 102.787 129.756 95.236  1.00 55.81 ?  43  GLN A C     1 
ATOM   322   O  O     . GLN A 1 43  ? 101.828 130.422 95.642  1.00 56.47 ?  43  GLN A O     1 
ATOM   323   C  CB    . GLN A 1 43  ? 102.348 127.422 94.426  1.00 55.39 ?  43  GLN A CB    1 
ATOM   324   C  CG    . GLN A 1 43  ? 101.419 126.676 93.482  1.00 57.56 ?  43  GLN A CG    1 
ATOM   325   C  CD    . GLN A 1 43  ? 102.023 126.463 92.107  1.00 58.38 ?  43  GLN A CD    1 
ATOM   326   O  OE1   . GLN A 1 43  ? 103.238 126.542 91.931  1.00 57.94 ?  43  GLN A OE1   1 
ATOM   327   N  NE2   . GLN A 1 43  ? 101.173 126.192 91.124  1.00 56.72 ?  43  GLN A NE2   1 
ATOM   328   N  N     . ASN A 1 44  ? 103.974 129.783 95.839  1.00 54.90 ?  44  ASN A N     1 
ATOM   329   C  CA    . ASN A 1 44  ? 104.212 130.532 97.066  1.00 55.01 ?  44  ASN A CA    1 
ATOM   330   C  C     . ASN A 1 44  ? 104.883 131.879 96.826  1.00 54.27 ?  44  ASN A C     1 
ATOM   331   O  O     . ASN A 1 44  ? 105.370 132.492 97.779  1.00 54.47 ?  44  ASN A O     1 
ATOM   332   C  CB    . ASN A 1 44  ? 105.045 129.695 98.040  1.00 53.41 ?  44  ASN A CB    1 
ATOM   333   C  CG    . ASN A 1 44  ? 104.393 128.367 98.373  1.00 55.83 ?  44  ASN A CG    1 
ATOM   334   O  OD1   . ASN A 1 44  ? 103.901 128.163 99.481  1.00 56.75 ?  44  ASN A OD1   1 
ATOM   335   N  ND2   . ASN A 1 44  ? 104.390 127.453 97.409  1.00 56.44 ?  44  ASN A ND2   1 
ATOM   336   N  N     . THR A 1 45  ? 104.922 132.351 95.584  1.00 54.15 ?  45  THR A N     1 
ATOM   337   C  CA    . THR A 1 45  ? 105.488 133.654 95.261  1.00 55.09 ?  45  THR A CA    1 
ATOM   338   C  C     . THR A 1 45  ? 104.371 134.685 95.181  1.00 55.66 ?  45  THR A C     1 
ATOM   339   O  O     . THR A 1 45  ? 103.406 134.505 94.429  1.00 56.05 ?  45  THR A O     1 
ATOM   340   C  CB    . THR A 1 45  ? 106.261 133.610 93.941  1.00 55.01 ?  45  THR A CB    1 
ATOM   341   O  OG1   . THR A 1 45  ? 107.555 133.034 94.163  1.00 57.88 ?  45  THR A OG1   1 
ATOM   342   C  CG2   . THR A 1 45  ? 106.434 135.011 93.370  1.00 53.39 ?  45  THR A CG2   1 
ATOM   343   N  N     . VAL A 1 46  ? 104.502 135.759 95.958  1.00 55.46 ?  46  VAL A N     1 
ATOM   344   C  CA    . VAL A 1 46  ? 103.498 136.817 95.954  1.00 55.19 ?  46  VAL A CA    1 
ATOM   345   C  C     . VAL A 1 46  ? 103.638 137.621 94.669  1.00 55.73 ?  46  VAL A C     1 
ATOM   346   O  O     . VAL A 1 46  ? 104.722 138.116 94.344  1.00 58.54 ?  46  VAL A O     1 
ATOM   347   C  CB    . VAL A 1 46  ? 103.642 137.715 97.190  1.00 55.20 ?  46  VAL A CB    1 
ATOM   348   C  CG1   . VAL A 1 46  ? 102.693 138.897 97.098  1.00 54.96 ?  46  VAL A CG1   1 
ATOM   349   C  CG2   . VAL A 1 46  ? 103.381 136.922 98.453  1.00 54.62 ?  46  VAL A CG2   1 
ATOM   350   N  N     . PHE A 1 47  ? 102.540 137.756 93.934  1.00 59.11 ?  47  PHE A N     1 
ATOM   351   C  CA    . PHE A 1 47  ? 102.522 138.501 92.687  1.00 59.69 ?  47  PHE A CA    1 
ATOM   352   C  C     . PHE A 1 47  ? 101.671 139.755 92.835  1.00 61.94 ?  47  PHE A C     1 
ATOM   353   O  O     . PHE A 1 47  ? 100.673 139.769 93.561  1.00 63.68 ?  47  PHE A O     1 
ATOM   354   C  CB    . PHE A 1 47  ? 101.990 137.646 91.534  1.00 60.14 ?  47  PHE A CB    1 
ATOM   355   C  CG    . PHE A 1 47  ? 102.445 138.110 90.180  1.00 62.75 ?  47  PHE A CG    1 
ATOM   356   C  CD1   . PHE A 1 47  ? 103.721 137.824 89.728  1.00 61.43 ?  47  PHE A CD1   1 
ATOM   357   C  CD2   . PHE A 1 47  ? 101.596 138.837 89.362  1.00 62.25 ?  47  PHE A CD2   1 
ATOM   358   C  CE1   . PHE A 1 47  ? 104.144 138.252 88.484  1.00 61.54 ?  47  PHE A CE1   1 
ATOM   359   C  CE2   . PHE A 1 47  ? 102.014 139.269 88.116  1.00 61.58 ?  47  PHE A CE2   1 
ATOM   360   C  CZ    . PHE A 1 47  ? 103.288 138.975 87.677  1.00 61.77 ?  47  PHE A CZ    1 
ATOM   361   N  N     . PHE A 1 48  ? 102.081 140.807 92.137  1.00 57.51 ?  48  PHE A N     1 
ATOM   362   C  CA    . PHE A 1 48  ? 101.410 142.095 92.172  1.00 57.86 ?  48  PHE A CA    1 
ATOM   363   C  C     . PHE A 1 48  ? 100.996 142.494 90.762  1.00 58.93 ?  48  PHE A C     1 
ATOM   364   O  O     . PHE A 1 48  ? 101.553 142.016 89.770  1.00 61.11 ?  48  PHE A O     1 
ATOM   365   C  CB    . PHE A 1 48  ? 102.311 143.175 92.784  1.00 57.18 ?  48  PHE A CB    1 
ATOM   366   C  CG    . PHE A 1 48  ? 102.716 142.899 94.206  1.00 56.27 ?  48  PHE A CG    1 
ATOM   367   C  CD1   . PHE A 1 48  ? 103.799 142.084 94.488  1.00 56.87 ?  48  PHE A CD1   1 
ATOM   368   C  CD2   . PHE A 1 48  ? 102.020 143.466 95.260  1.00 58.06 ?  48  PHE A CD2   1 
ATOM   369   C  CE1   . PHE A 1 48  ? 104.176 141.836 95.793  1.00 57.84 ?  48  PHE A CE1   1 
ATOM   370   C  CE2   . PHE A 1 48  ? 102.392 143.219 96.568  1.00 58.40 ?  48  PHE A CE2   1 
ATOM   371   C  CZ    . PHE A 1 48  ? 103.471 142.403 96.834  1.00 57.22 ?  48  PHE A CZ    1 
ATOM   372   N  N     . HIS A 1 49  ? 99.997  143.376 90.686  1.00 63.64 ?  49  HIS A N     1 
ATOM   373   C  CA    . HIS A 1 49  ? 99.503  143.819 89.386  1.00 66.40 ?  49  HIS A CA    1 
ATOM   374   C  C     . HIS A 1 49  ? 100.578 144.555 88.598  1.00 67.18 ?  49  HIS A C     1 
ATOM   375   O  O     . HIS A 1 49  ? 100.619 144.463 87.366  1.00 67.16 ?  49  HIS A O     1 
ATOM   376   C  CB    . HIS A 1 49  ? 98.271  144.706 89.567  1.00 67.54 ?  49  HIS A CB    1 
ATOM   377   C  CG    . HIS A 1 49  ? 97.626  145.114 88.279  1.00 69.46 ?  49  HIS A CG    1 
ATOM   378   N  ND1   . HIS A 1 49  ? 97.230  144.203 87.324  1.00 68.49 ?  49  HIS A ND1   1 
ATOM   379   C  CD2   . HIS A 1 49  ? 97.305  146.335 87.791  1.00 67.80 ?  49  HIS A CD2   1 
ATOM   380   C  CE1   . HIS A 1 49  ? 96.695  144.845 86.301  1.00 68.74 ?  49  HIS A CE1   1 
ATOM   381   N  NE2   . HIS A 1 49  ? 96.728  146.141 86.559  1.00 69.21 ?  49  HIS A NE2   1 
ATOM   382   N  N     . ASN A 1 50  ? 101.452 145.285 89.285  1.00 64.74 ?  50  ASN A N     1 
ATOM   383   C  CA    . ASN A 1 50  ? 102.558 145.977 88.642  1.00 63.49 ?  50  ASN A CA    1 
ATOM   384   C  C     . ASN A 1 50  ? 103.676 146.162 89.658  1.00 62.85 ?  50  ASN A C     1 
ATOM   385   O  O     . ASN A 1 50  ? 103.488 145.968 90.862  1.00 61.77 ?  50  ASN A O     1 
ATOM   386   C  CB    . ASN A 1 50  ? 102.109 147.317 88.038  1.00 62.57 ?  50  ASN A CB    1 
ATOM   387   C  CG    . ASN A 1 50  ? 101.739 148.347 89.092  1.00 64.44 ?  50  ASN A CG    1 
ATOM   388   O  OD1   . ASN A 1 50  ? 101.518 148.016 90.256  1.00 64.51 ?  50  ASN A OD1   1 
ATOM   389   N  ND2   . ASN A 1 50  ? 101.669 149.607 88.681  1.00 63.77 ?  50  ASN A ND2   1 
ATOM   390   N  N     . LEU A 1 51  ? 104.855 146.533 89.155  1.00 57.68 ?  51  LEU A N     1 
ATOM   391   C  CA    . LEU A 1 51  ? 106.012 146.699 90.029  1.00 56.20 ?  51  LEU A CA    1 
ATOM   392   C  C     . LEU A 1 51  ? 105.820 147.848 91.009  1.00 57.94 ?  51  LEU A C     1 
ATOM   393   O  O     . LEU A 1 51  ? 106.398 147.828 92.102  1.00 59.15 ?  51  LEU A O     1 
ATOM   394   C  CB    . LEU A 1 51  ? 107.272 146.920 89.195  1.00 55.60 ?  51  LEU A CB    1 
ATOM   395   C  CG    . LEU A 1 51  ? 108.601 147.040 89.941  1.00 55.06 ?  51  LEU A CG    1 
ATOM   396   C  CD1   . LEU A 1 51  ? 108.945 145.737 90.645  1.00 54.14 ?  51  LEU A CD1   1 
ATOM   397   C  CD2   . LEU A 1 51  ? 109.705 147.447 88.984  1.00 54.35 ?  51  LEU A CD2   1 
ATOM   398   N  N     . LYS A 1 52  ? 105.028 148.857 90.640  1.00 57.99 ?  52  LYS A N     1 
ATOM   399   C  CA    . LYS A 1 52  ? 104.767 149.964 91.553  1.00 57.65 ?  52  LYS A CA    1 
ATOM   400   C  C     . LYS A 1 52  ? 104.069 149.472 92.815  1.00 58.88 ?  52  LYS A C     1 
ATOM   401   O  O     . LYS A 1 52  ? 104.437 149.854 93.932  1.00 59.30 ?  52  LYS A O     1 
ATOM   402   C  CB    . LYS A 1 52  ? 103.930 151.033 90.848  1.00 57.85 ?  52  LYS A CB    1 
ATOM   403   C  CG    . LYS A 1 52  ? 104.325 152.464 91.180  1.00 58.85 ?  52  LYS A CG    1 
ATOM   404   C  CD    . LYS A 1 52  ? 103.895 152.859 92.580  1.00 59.24 ?  52  LYS A CD    1 
ATOM   405   C  CE    . LYS A 1 52  ? 104.163 154.330 92.843  1.00 59.48 ?  52  LYS A CE    1 
ATOM   406   N  NZ    . LYS A 1 52  ? 104.298 154.615 94.298  1.00 59.50 1  52  LYS A NZ    1 
ATOM   407   N  N     . GLU A 1 53  ? 103.065 148.608 92.651  1.00 60.58 ?  53  GLU A N     1 
ATOM   408   C  CA    . GLU A 1 53  ? 102.369 148.049 93.805  1.00 60.45 ?  53  GLU A CA    1 
ATOM   409   C  C     . GLU A 1 53  ? 103.302 147.192 94.650  1.00 60.19 ?  53  GLU A C     1 
ATOM   410   O  O     . GLU A 1 53  ? 103.250 147.238 95.884  1.00 60.00 ?  53  GLU A O     1 
ATOM   411   C  CB    . GLU A 1 53  ? 101.163 147.230 93.344  1.00 61.07 ?  53  GLU A CB    1 
ATOM   412   C  CG    . GLU A 1 53  ? 100.265 146.749 94.471  1.00 62.36 ?  53  GLU A CG    1 
ATOM   413   C  CD    . GLU A 1 53  ? 99.238  145.738 94.003  1.00 63.76 ?  53  GLU A CD    1 
ATOM   414   O  OE1   . GLU A 1 53  ? 99.110  144.675 94.648  1.00 62.97 ?  53  GLU A OE1   1 
ATOM   415   O  OE2   . GLU A 1 53  ? 98.559  146.003 92.989  1.00 62.77 -1 53  GLU A OE2   1 
ATOM   416   N  N     . LYS A 1 54  ? 104.161 146.402 94.003  1.00 58.66 ?  54  LYS A N     1 
ATOM   417   C  CA    . LYS A 1 54  ? 105.105 145.566 94.739  1.00 54.61 ?  54  LYS A CA    1 
ATOM   418   C  C     . LYS A 1 54  ? 106.058 146.414 95.569  1.00 52.64 ?  54  LYS A C     1 
ATOM   419   O  O     . LYS A 1 54  ? 106.293 146.134 96.751  1.00 55.36 ?  54  LYS A O     1 
ATOM   420   C  CB    . LYS A 1 54  ? 105.885 144.682 93.767  1.00 54.10 ?  54  LYS A CB    1 
ATOM   421   C  CG    . LYS A 1 54  ? 107.066 143.968 94.397  1.00 57.14 ?  54  LYS A CG    1 
ATOM   422   C  CD    . LYS A 1 54  ? 107.512 142.791 93.552  1.00 55.57 ?  54  LYS A CD    1 
ATOM   423   C  CE    . LYS A 1 54  ? 108.656 142.045 94.207  1.00 55.37 ?  54  LYS A CE    1 
ATOM   424   N  NZ    . LYS A 1 54  ? 108.793 140.664 93.668  1.00 55.79 1  54  LYS A NZ    1 
ATOM   425   N  N     . LEU A 1 55  ? 106.616 147.463 94.962  1.00 53.92 ?  55  LEU A N     1 
ATOM   426   C  CA    . LEU A 1 55  ? 107.545 148.327 95.680  1.00 55.07 ?  55  LEU A CA    1 
ATOM   427   C  C     . LEU A 1 55  ? 106.846 149.068 96.811  1.00 57.40 ?  55  LEU A C     1 
ATOM   428   O  O     . LEU A 1 55  ? 107.410 149.217 97.900  1.00 58.63 ?  55  LEU A O     1 
ATOM   429   C  CB    . LEU A 1 55  ? 108.201 149.310 94.713  1.00 55.64 ?  55  LEU A CB    1 
ATOM   430   C  CG    . LEU A 1 55  ? 109.129 148.697 93.663  1.00 56.12 ?  55  LEU A CG    1 
ATOM   431   C  CD1   . LEU A 1 55  ? 109.555 149.748 92.654  1.00 56.83 ?  55  LEU A CD1   1 
ATOM   432   C  CD2   . LEU A 1 55  ? 110.341 148.048 94.314  1.00 53.50 ?  55  LEU A CD2   1 
ATOM   433   N  N     . ASP A 1 56  ? 105.616 149.535 96.575  1.00 60.10 ?  56  ASP A N     1 
ATOM   434   C  CA    . ASP A 1 56  ? 104.870 150.207 97.634  1.00 59.38 ?  56  ASP A CA    1 
ATOM   435   C  C     . ASP A 1 56  ? 104.590 149.262 98.794  1.00 57.92 ?  56  ASP A C     1 
ATOM   436   O  O     . ASP A 1 56  ? 104.734 149.642 99.961  1.00 57.64 ?  56  ASP A O     1 
ATOM   437   C  CB    . ASP A 1 56  ? 103.565 150.774 97.078  1.00 60.22 ?  56  ASP A CB    1 
ATOM   438   C  CG    . ASP A 1 56  ? 103.779 152.025 96.254  1.00 62.26 ?  56  ASP A CG    1 
ATOM   439   O  OD1   . ASP A 1 56  ? 102.823 152.464 95.579  1.00 62.19 ?  56  ASP A OD1   1 
ATOM   440   O  OD2   . ASP A 1 56  ? 104.902 152.571 96.281  1.00 61.30 -1 56  ASP A OD2   1 
ATOM   441   N  N     . TYR A 1 57  ? 104.192 148.023 98.496  1.00 52.63 ?  57  TYR A N     1 
ATOM   442   C  CA    . TYR A 1 57  ? 103.920 147.059 99.555  1.00 54.65 ?  57  TYR A CA    1 
ATOM   443   C  C     . TYR A 1 57  ? 105.182 146.723 100.336 1.00 56.13 ?  57  TYR A C     1 
ATOM   444   O  O     . TYR A 1 57  ? 105.143 146.603 101.566 1.00 57.38 ?  57  TYR A O     1 
ATOM   445   C  CB    . TYR A 1 57  ? 103.300 145.792 98.965  1.00 53.46 ?  57  TYR A CB    1 
ATOM   446   C  CG    . TYR A 1 57  ? 103.103 144.684 99.975  1.00 55.24 ?  57  TYR A CG    1 
ATOM   447   C  CD1   . TYR A 1 57  ? 101.993 144.669 100.809 1.00 54.93 ?  57  TYR A CD1   1 
ATOM   448   C  CD2   . TYR A 1 57  ? 104.026 143.652 100.093 1.00 55.44 ?  57  TYR A CD2   1 
ATOM   449   C  CE1   . TYR A 1 57  ? 101.810 143.659 101.734 1.00 55.25 ?  57  TYR A CE1   1 
ATOM   450   C  CE2   . TYR A 1 57  ? 103.851 142.641 101.014 1.00 55.86 ?  57  TYR A CE2   1 
ATOM   451   C  CZ    . TYR A 1 57  ? 102.742 142.647 101.832 1.00 55.58 ?  57  TYR A CZ    1 
ATOM   452   O  OH    . TYR A 1 57  ? 102.564 141.638 102.749 1.00 56.63 ?  57  TYR A OH    1 
ATOM   453   N  N     . LEU A 1 58  ? 106.310 146.559 99.642  1.00 51.42 ?  58  LEU A N     1 
ATOM   454   C  CA    . LEU A 1 58  ? 107.545 146.196 100.328 1.00 50.27 ?  58  LEU A CA    1 
ATOM   455   C  C     . LEU A 1 58  ? 108.075 147.352 101.169 1.00 51.95 ?  58  LEU A C     1 
ATOM   456   O  O     . LEU A 1 58  ? 108.593 147.136 102.271 1.00 52.72 ?  58  LEU A O     1 
ATOM   457   C  CB    . LEU A 1 58  ? 108.588 145.730 99.315  1.00 49.61 ?  58  LEU A CB    1 
ATOM   458   C  CG    . LEU A 1 58  ? 108.267 144.389 98.646  1.00 50.58 ?  58  LEU A CG    1 
ATOM   459   C  CD1   . LEU A 1 58  ? 109.136 144.160 97.423  1.00 51.28 ?  58  LEU A CD1   1 
ATOM   460   C  CD2   . LEU A 1 58  ? 108.417 143.245 99.633  1.00 51.20 ?  58  LEU A CD2   1 
ATOM   461   N  N     . VAL A 1 59  ? 107.953 148.585 100.674 1.00 53.73 ?  59  VAL A N     1 
ATOM   462   C  CA    . VAL A 1 59  ? 108.422 149.738 101.435 1.00 54.61 ?  59  VAL A CA    1 
ATOM   463   C  C     . VAL A 1 59  ? 107.520 149.992 102.638 1.00 57.60 ?  59  VAL A C     1 
ATOM   464   O  O     . VAL A 1 59  ? 107.997 150.223 103.755 1.00 56.54 ?  59  VAL A O     1 
ATOM   465   C  CB    . VAL A 1 59  ? 108.510 150.974 100.524 1.00 54.59 ?  59  VAL A CB    1 
ATOM   466   C  CG1   . VAL A 1 59  ? 108.537 152.243 101.353 1.00 53.14 ?  59  VAL A CG1   1 
ATOM   467   C  CG2   . VAL A 1 59  ? 109.741 150.888 99.638  1.00 54.08 ?  59  VAL A CG2   1 
ATOM   468   N  N     . GLU A 1 60  ? 106.201 149.945 102.428 1.00 60.48 ?  60  GLU A N     1 
ATOM   469   C  CA    . GLU A 1 60  ? 105.262 150.264 103.499 1.00 58.01 ?  60  GLU A CA    1 
ATOM   470   C  C     . GLU A 1 60  ? 105.318 149.233 104.619 1.00 57.85 ?  60  GLU A C     1 
ATOM   471   O  O     . GLU A 1 60  ? 105.220 149.586 105.799 1.00 58.08 ?  60  GLU A O     1 
ATOM   472   C  CB    . GLU A 1 60  ? 103.846 150.374 102.934 1.00 58.23 ?  60  GLU A CB    1 
ATOM   473   C  CG    . GLU A 1 60  ? 103.587 151.659 102.162 1.00 59.63 ?  60  GLU A CG    1 
ATOM   474   C  CD    . GLU A 1 60  ? 102.424 151.537 101.197 1.00 61.74 ?  60  GLU A CD    1 
ATOM   475   O  OE1   . GLU A 1 60  ? 101.709 150.513 101.249 1.00 59.38 ?  60  GLU A OE1   1 
ATOM   476   O  OE2   . GLU A 1 60  ? 102.227 152.463 100.382 1.00 61.31 -1 60  GLU A OE2   1 
ATOM   477   N  N     . ASN A 1 61  ? 105.475 147.956 104.273 1.00 53.71 ?  61  ASN A N     1 
ATOM   478   C  CA    . ASN A 1 61  ? 105.530 146.885 105.261 1.00 52.50 ?  61  ASN A CA    1 
ATOM   479   C  C     . ASN A 1 61  ? 106.919 146.703 105.861 1.00 54.36 ?  61  ASN A C     1 
ATOM   480   O  O     . ASN A 1 61  ? 107.197 145.641 106.434 1.00 54.46 ?  61  ASN A O     1 
ATOM   481   C  CB    . ASN A 1 61  ? 105.049 145.573 104.641 1.00 53.45 ?  61  ASN A CB    1 
ATOM   482   C  CG    . ASN A 1 61  ? 103.542 145.516 104.496 1.00 56.30 ?  61  ASN A CG    1 
ATOM   483   O  OD1   . ASN A 1 61  ? 102.908 146.496 104.110 1.00 54.48 ?  61  ASN A OD1   1 
ATOM   484   N  ND2   . ASN A 1 61  ? 102.960 144.364 104.807 1.00 55.68 ?  61  ASN A ND2   1 
ATOM   485   N  N     . GLN A 1 62  ? 107.786 147.710 105.736 1.00 53.25 ?  62  GLN A N     1 
ATOM   486   C  CA    . GLN A 1 62  ? 109.119 147.713 106.342 1.00 52.66 ?  62  GLN A CA    1 
ATOM   487   C  C     . GLN A 1 62  ? 109.984 146.559 105.843 1.00 52.40 ?  62  GLN A C     1 
ATOM   488   O  O     . GLN A 1 62  ? 110.817 146.030 106.584 1.00 53.31 ?  62  GLN A O     1 
ATOM   489   C  CB    . GLN A 1 62  ? 109.036 147.696 107.872 1.00 51.98 ?  62  GLN A CB    1 
ATOM   490   C  CG    . GLN A 1 62  ? 107.982 148.629 108.451 1.00 51.77 ?  62  GLN A CG    1 
ATOM   491   C  CD    . GLN A 1 62  ? 108.210 150.078 108.070 1.00 54.59 ?  62  GLN A CD    1 
ATOM   492   O  OE1   . GLN A 1 62  ? 109.150 150.716 108.543 1.00 54.15 ?  62  GLN A OE1   1 
ATOM   493   N  NE2   . GLN A 1 62  ? 107.349 150.606 107.210 1.00 54.94 ?  62  GLN A NE2   1 
ATOM   494   N  N     . TYR A 1 63  ? 109.795 146.154 104.588 1.00 50.12 ?  63  TYR A N     1 
ATOM   495   C  CA    . TYR A 1 63  ? 110.684 145.179 103.968 1.00 46.66 ?  63  TYR A CA    1 
ATOM   496   C  C     . TYR A 1 63  ? 111.908 145.850 103.357 1.00 48.34 ?  63  TYR A C     1 
ATOM   497   O  O     . TYR A 1 63  ? 113.035 145.380 103.540 1.00 49.61 ?  63  TYR A O     1 
ATOM   498   C  CB    . TYR A 1 63  ? 109.940 144.377 102.895 1.00 47.01 ?  63  TYR A CB    1 
ATOM   499   C  CG    . TYR A 1 63  ? 108.905 143.420 103.436 1.00 49.24 ?  63  TYR A CG    1 
ATOM   500   C  CD1   . TYR A 1 63  ? 109.268 142.382 104.282 1.00 48.39 ?  63  TYR A CD1   1 
ATOM   501   C  CD2   . TYR A 1 63  ? 107.568 143.550 103.093 1.00 50.04 ?  63  TYR A CD2   1 
ATOM   502   C  CE1   . TYR A 1 63  ? 108.325 141.504 104.775 1.00 48.45 ?  63  TYR A CE1   1 
ATOM   503   C  CE2   . TYR A 1 63  ? 106.619 142.676 103.579 1.00 50.57 ?  63  TYR A CE2   1 
ATOM   504   C  CZ    . TYR A 1 63  ? 107.002 141.657 104.421 1.00 50.75 ?  63  TYR A CZ    1 
ATOM   505   O  OH    . TYR A 1 63  ? 106.054 140.787 104.907 1.00 53.58 ?  63  TYR A OH    1 
ATOM   506   N  N     . TYR A 1 64  ? 111.700 146.945 102.634 1.00 47.25 ?  64  TYR A N     1 
ATOM   507   C  CA    . TYR A 1 64  ? 112.764 147.679 101.966 1.00 43.93 ?  64  TYR A CA    1 
ATOM   508   C  C     . TYR A 1 64  ? 113.049 148.988 102.690 1.00 46.86 ?  64  TYR A C     1 
ATOM   509   O  O     . TYR A 1 64  ? 112.340 149.387 103.616 1.00 49.91 ?  64  TYR A O     1 
ATOM   510   C  CB    . TYR A 1 64  ? 112.397 147.967 100.507 1.00 45.49 ?  64  TYR A CB    1 
ATOM   511   C  CG    . TYR A 1 64  ? 112.510 146.776 99.590  1.00 45.64 ?  64  TYR A CG    1 
ATOM   512   C  CD1   . TYR A 1 64  ? 113.046 145.576 100.038 1.00 42.74 ?  64  TYR A CD1   1 
ATOM   513   C  CD2   . TYR A 1 64  ? 112.085 146.853 98.274  1.00 47.43 ?  64  TYR A CD2   1 
ATOM   514   C  CE1   . TYR A 1 64  ? 113.149 144.487 99.201  1.00 40.32 ?  64  TYR A CE1   1 
ATOM   515   C  CE2   . TYR A 1 64  ? 112.185 145.773 97.430  1.00 46.63 ?  64  TYR A CE2   1 
ATOM   516   C  CZ    . TYR A 1 64  ? 112.716 144.592 97.897  1.00 44.90 ?  64  TYR A CZ    1 
ATOM   517   O  OH    . TYR A 1 64  ? 112.814 143.515 97.051  1.00 44.35 ?  64  TYR A OH    1 
ATOM   518   N  N     . GLU A 1 65  ? 114.109 149.655 102.246 1.00 52.27 ?  65  GLU A N     1 
ATOM   519   C  CA    . GLU A 1 65  ? 114.430 150.996 102.705 1.00 50.80 ?  65  GLU A CA    1 
ATOM   520   C  C     . GLU A 1 65  ? 113.936 152.021 101.693 1.00 53.51 ?  65  GLU A C     1 
ATOM   521   O  O     . GLU A 1 65  ? 114.013 151.802 100.481 1.00 54.80 ?  65  GLU A O     1 
ATOM   522   C  CB    . GLU A 1 65  ? 115.937 151.154 102.917 1.00 50.17 ?  65  GLU A CB    1 
ATOM   523   C  CG    . GLU A 1 65  ? 116.451 150.579 104.225 1.00 51.49 ?  65  GLU A CG    1 
ATOM   524   C  CD    . GLU A 1 65  ? 117.911 150.180 104.152 1.00 52.41 ?  65  GLU A CD    1 
ATOM   525   O  OE1   . GLU A 1 65  ? 118.627 150.697 103.269 1.00 53.30 ?  65  GLU A OE1   1 
ATOM   526   O  OE2   . GLU A 1 65  ? 118.348 149.359 104.984 1.00 52.68 -1 65  GLU A OE2   1 
ATOM   527   N  N     . GLU A 1 66  ? 113.419 153.140 102.201 1.00 54.86 ?  66  GLU A N     1 
ATOM   528   C  CA    . GLU A 1 66  ? 112.934 154.202 101.328 1.00 54.45 ?  66  GLU A CA    1 
ATOM   529   C  C     . GLU A 1 66  ? 114.072 154.996 100.701 1.00 56.09 ?  66  GLU A C     1 
ATOM   530   O  O     . GLU A 1 66  ? 113.921 155.511 99.588  1.00 56.40 ?  66  GLU A O     1 
ATOM   531   C  CB    . GLU A 1 66  ? 112.018 155.149 102.110 1.00 55.78 ?  66  GLU A CB    1 
ATOM   532   C  CG    . GLU A 1 66  ? 110.529 155.158 101.719 1.00 57.32 ?  66  GLU A CG    1 
ATOM   533   C  CD    . GLU A 1 66  ? 110.230 155.522 100.262 1.00 58.41 ?  66  GLU A CD    1 
ATOM   534   O  OE1   . GLU A 1 66  ? 111.141 155.541 99.408  1.00 58.37 ?  66  GLU A OE1   1 
ATOM   535   O  OE2   . GLU A 1 66  ? 109.047 155.796 99.969  1.00 55.35 -1 66  GLU A OE2   1 
ATOM   536   N  N     . GLU A 1 67  ? 115.206 155.108 101.395 1.00 54.76 ?  67  GLU A N     1 
ATOM   537   C  CA    . GLU A 1 67  ? 116.258 156.026 100.967 1.00 55.13 ?  67  GLU A CA    1 
ATOM   538   C  C     . GLU A 1 67  ? 116.854 155.612 99.626  1.00 55.53 ?  67  GLU A C     1 
ATOM   539   O  O     . GLU A 1 67  ? 117.006 156.442 98.721  1.00 55.42 ?  67  GLU A O     1 
ATOM   540   C  CB    . GLU A 1 67  ? 117.347 156.105 102.038 1.00 56.55 ?  67  GLU A CB    1 
ATOM   541   C  CG    . GLU A 1 67  ? 116.819 156.367 103.438 1.00 57.39 ?  67  GLU A CG    1 
ATOM   542   C  CD    . GLU A 1 67  ? 116.693 155.101 104.260 1.00 60.75 ?  67  GLU A CD    1 
ATOM   543   O  OE1   . GLU A 1 67  ? 117.727 154.609 104.759 1.00 59.46 ?  67  GLU A OE1   1 
ATOM   544   O  OE2   . GLU A 1 67  ? 115.560 154.597 104.409 1.00 57.42 -1 67  GLU A OE2   1 
ATOM   545   N  N     . PHE A 1 68  ? 117.196 154.330 99.474  1.00 48.39 ?  68  PHE A N     1 
ATOM   546   C  CA    . PHE A 1 68  ? 117.875 153.905 98.254  1.00 44.87 ?  68  PHE A CA    1 
ATOM   547   C  C     . PHE A 1 68  ? 116.923 153.852 97.066  1.00 44.22 ?  68  PHE A C     1 
ATOM   548   O  O     . PHE A 1 68  ? 117.350 154.065 95.926  1.00 47.66 ?  68  PHE A O     1 
ATOM   549   C  CB    . PHE A 1 68  ? 118.560 152.553 98.474  1.00 46.19 ?  68  PHE A CB    1 
ATOM   550   C  CG    . PHE A 1 68  ? 117.689 151.365 98.181  1.00 44.21 ?  68  PHE A CG    1 
ATOM   551   C  CD1   . PHE A 1 68  ? 116.769 150.917 99.113  1.00 44.39 ?  68  PHE A CD1   1 
ATOM   552   C  CD2   . PHE A 1 68  ? 117.814 150.676 96.986  1.00 39.83 ?  68  PHE A CD2   1 
ATOM   553   C  CE1   . PHE A 1 68  ? 115.974 149.818 98.848  1.00 42.62 ?  68  PHE A CE1   1 
ATOM   554   C  CE2   . PHE A 1 68  ? 117.024 149.577 96.717  1.00 43.07 ?  68  PHE A CE2   1 
ATOM   555   C  CZ    . PHE A 1 68  ? 116.105 149.147 97.650  1.00 45.52 ?  68  PHE A CZ    1 
ATOM   556   N  N     . LEU A 1 69  ? 115.640 153.576 97.305  1.00 46.25 ?  69  LEU A N     1 
ATOM   557   C  CA    . LEU A 1 69  ? 114.672 153.594 96.214  1.00 46.48 ?  69  LEU A CA    1 
ATOM   558   C  C     . LEU A 1 69  ? 114.281 155.011 95.819  1.00 48.21 ?  69  LEU A C     1 
ATOM   559   O  O     . LEU A 1 69  ? 113.914 155.247 94.662  1.00 45.42 ?  69  LEU A O     1 
ATOM   560   C  CB    . LEU A 1 69  ? 113.427 152.793 96.597  1.00 45.84 ?  69  LEU A CB    1 
ATOM   561   C  CG    . LEU A 1 69  ? 113.566 151.271 96.511  1.00 43.33 ?  69  LEU A CG    1 
ATOM   562   C  CD1   . LEU A 1 69  ? 112.301 150.581 96.992  1.00 43.30 ?  69  LEU A CD1   1 
ATOM   563   C  CD2   . LEU A 1 69  ? 113.913 150.838 95.095  1.00 42.58 ?  69  LEU A CD2   1 
ATOM   564   N  N     . SER A 1 70  ? 114.353 155.961 96.754  1.00 50.75 ?  70  SER A N     1 
ATOM   565   C  CA    . SER A 1 70  ? 113.977 157.337 96.455  1.00 49.04 ?  70  SER A CA    1 
ATOM   566   C  C     . SER A 1 70  ? 114.979 158.034 95.546  1.00 49.55 ?  70  SER A C     1 
ATOM   567   O  O     . SER A 1 70  ? 114.646 159.071 94.962  1.00 51.31 ?  70  SER A O     1 
ATOM   568   C  CB    . SER A 1 70  ? 113.816 158.129 97.754  1.00 50.83 ?  70  SER A CB    1 
ATOM   569   O  OG    . SER A 1 70  ? 115.076 158.419 98.332  1.00 52.71 ?  70  SER A OG    1 
ATOM   570   N  N     . LEU A 1 71  ? 116.192 157.495 95.410  1.00 44.06 ?  71  LEU A N     1 
ATOM   571   C  CA    . LEU A 1 71  ? 117.192 158.103 94.543  1.00 43.61 ?  71  LEU A CA    1 
ATOM   572   C  C     . LEU A 1 71  ? 116.877 157.928 93.064  1.00 44.26 ?  71  LEU A C     1 
ATOM   573   O  O     . LEU A 1 71  ? 117.492 158.606 92.234  1.00 44.16 ?  71  LEU A O     1 
ATOM   574   C  CB    . LEU A 1 71  ? 118.574 157.520 94.843  1.00 45.70 ?  71  LEU A CB    1 
ATOM   575   C  CG    . LEU A 1 71  ? 119.012 157.532 96.307  1.00 47.64 ?  71  LEU A CG    1 
ATOM   576   C  CD1   . LEU A 1 71  ? 120.041 156.444 96.563  1.00 47.24 ?  71  LEU A CD1   1 
ATOM   577   C  CD2   . LEU A 1 71  ? 119.563 158.896 96.684  1.00 45.83 ?  71  LEU A CD2   1 
ATOM   578   N  N     . TYR A 1 72  ? 115.946 157.046 92.717  1.00 44.00 ?  72  TYR A N     1 
ATOM   579   C  CA    . TYR A 1 72  ? 115.565 156.805 91.335  1.00 44.48 ?  72  TYR A CA    1 
ATOM   580   C  C     . TYR A 1 72  ? 114.103 157.167 91.130  1.00 46.44 ?  72  TYR A C     1 
ATOM   581   O  O     . TYR A 1 72  ? 113.281 157.047 92.043  1.00 47.83 ?  72  TYR A O     1 
ATOM   582   C  CB    . TYR A 1 72  ? 115.768 155.336 90.931  1.00 43.94 ?  72  TYR A CB    1 
ATOM   583   C  CG    . TYR A 1 72  ? 117.095 154.732 91.323  1.00 41.73 ?  72  TYR A CG    1 
ATOM   584   C  CD1   . TYR A 1 72  ? 117.310 154.253 92.608  1.00 42.19 ?  72  TYR A CD1   1 
ATOM   585   C  CD2   . TYR A 1 72  ? 118.125 154.618 90.401  1.00 40.29 ?  72  TYR A CD2   1 
ATOM   586   C  CE1   . TYR A 1 72  ? 118.518 153.696 92.968  1.00 41.19 ?  72  TYR A CE1   1 
ATOM   587   C  CE2   . TYR A 1 72  ? 119.336 154.058 90.751  1.00 40.28 ?  72  TYR A CE2   1 
ATOM   588   C  CZ    . TYR A 1 72  ? 119.526 153.600 92.036  1.00 40.85 ?  72  TYR A CZ    1 
ATOM   589   O  OH    . TYR A 1 72  ? 120.730 153.043 92.394  1.00 43.51 ?  72  TYR A OH    1 
ATOM   590   N  N     . SER A 1 73  ? 113.786 157.617 89.922  1.00 51.19 ?  73  SER A N     1 
ATOM   591   C  CA    . SER A 1 73  ? 112.395 157.674 89.512  1.00 50.58 ?  73  SER A CA    1 
ATOM   592   C  C     . SER A 1 73  ? 111.870 156.256 89.310  1.00 52.96 ?  73  SER A C     1 
ATOM   593   O  O     . SER A 1 73  ? 112.634 155.310 89.098  1.00 52.97 ?  73  SER A O     1 
ATOM   594   C  CB    . SER A 1 73  ? 112.241 158.492 88.230  1.00 50.80 ?  73  SER A CB    1 
ATOM   595   O  OG    . SER A 1 73  ? 112.631 157.739 87.095  1.00 50.85 ?  73  SER A OG    1 
ATOM   596   N  N     . PHE A 1 74  ? 110.547 156.107 89.392  1.00 55.14 ?  74  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 74  ? 109.964 154.779 89.235  1.00 53.82 ?  74  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 74  ? 110.237 154.206 87.851  1.00 55.08 ?  74  PHE A C     1 
ATOM   599   O  O     . PHE A 1 74  ? 110.340 152.984 87.697  1.00 56.91 ?  74  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 74  ? 108.461 154.812 89.505  1.00 54.87 ?  74  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 74  ? 107.753 153.551 89.097  1.00 56.02 ?  74  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 74  ? 107.934 152.383 89.819  1.00 54.35 ?  74  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 74  ? 106.921 153.527 87.991  1.00 56.03 ?  74  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 74  ? 107.297 151.218 89.449  1.00 56.64 ?  74  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 74  ? 106.278 152.362 87.617  1.00 56.94 ?  74  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 74  ? 106.467 151.207 88.348  1.00 57.05 ?  74  PHE A CZ    1 
ATOM   607   N  N     . GLU A 1 75  ? 110.356 155.065 86.834  1.00 54.57 ?  75  GLU A N     1 
ATOM   608   C  CA    . GLU A 1 75  ? 110.675 154.581 85.495  1.00 55.54 ?  75  GLU A CA    1 
ATOM   609   C  C     . GLU A 1 75  ? 112.051 153.927 85.461  1.00 57.99 ?  75  GLU A C     1 
ATOM   610   O  O     . GLU A 1 75  ? 112.235 152.880 84.833  1.00 58.35 ?  75  GLU A O     1 
ATOM   611   C  CB    . GLU A 1 75  ? 110.595 155.729 84.483  1.00 54.90 ?  75  GLU A CB    1 
ATOM   612   C  CG    . GLU A 1 75  ? 109.263 156.532 84.393  1.00 55.52 ?  75  GLU A CG    1 
ATOM   613   C  CD    . GLU A 1 75  ? 107.962 155.709 84.402  1.00 58.83 ?  75  GLU A CD    1 
ATOM   614   O  OE1   . GLU A 1 75  ? 107.967 154.482 84.614  1.00 59.31 ?  75  GLU A OE1   1 
ATOM   615   O  OE2   . GLU A 1 75  ? 106.890 156.323 84.196  1.00 57.49 -1 75  GLU A OE2   1 
ATOM   616   N  N     . ASP A 1 76  ? 113.028 154.523 86.147  1.00 52.85 ?  76  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 76  ? 114.368 153.945 86.188  1.00 49.88 ?  76  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 76  ? 114.380 152.611 86.931  1.00 49.23 ?  76  ASP A C     1 
ATOM   619   O  O     . ASP A 1 76  ? 115.047 151.664 86.502  1.00 53.95 ?  76  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 76  ? 115.339 154.932 86.831  1.00 52.85 ?  76  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 76  ? 115.594 156.145 85.958  1.00 55.11 ?  76  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 76  ? 114.948 156.261 84.895  1.00 54.60 ?  76  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 76  ? 116.447 156.978 86.328  1.00 53.49 -1 76  ASP A OD2   1 
ATOM   624   N  N     . ILE A 1 77  ? 113.650 152.519 88.046  1.00 44.02 ?  77  ILE A N     1 
ATOM   625   C  CA    . ILE A 1 77  ? 113.573 151.259 88.784  1.00 45.79 ?  77  ILE A CA    1 
ATOM   626   C  C     . ILE A 1 77  ? 112.907 150.185 87.936  1.00 44.53 ?  77  ILE A C     1 
ATOM   627   O  O     . ILE A 1 77  ? 113.344 149.026 87.911  1.00 47.23 ?  77  ILE A O     1 
ATOM   628   C  CB    . ILE A 1 77  ? 112.834 151.467 90.119  1.00 46.81 ?  77  ILE A CB    1 
ATOM   629   C  CG1   . ILE A 1 77  ? 113.589 152.470 90.990  1.00 46.87 ?  77  ILE A CG1   1 
ATOM   630   C  CG2   . ILE A 1 77  ? 112.674 150.147 90.853  1.00 44.75 ?  77  ILE A CG2   1 
ATOM   631   C  CD1   . ILE A 1 77  ? 112.830 152.904 92.220  1.00 45.19 ?  77  ILE A CD1   1 
ATOM   632   N  N     . LYS A 1 78  ? 111.832 150.549 87.233  1.00 48.26 ?  78  LYS A N     1 
ATOM   633   C  CA    . LYS A 1 78  ? 111.162 149.599 86.353  1.00 49.51 ?  78  LYS A CA    1 
ATOM   634   C  C     . LYS A 1 78  ? 112.082 149.154 85.225  1.00 49.50 ?  78  LYS A C     1 
ATOM   635   O  O     . LYS A 1 78  ? 112.076 147.981 84.840  1.00 51.38 ?  78  LYS A O     1 
ATOM   636   C  CB    . LYS A 1 78  ? 109.880 150.218 85.795  1.00 51.36 ?  78  LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 78  ? 109.030 149.269 84.970  1.00 50.07 ?  78  LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 78  ? 107.725 149.924 84.560  1.00 51.85 ?  78  LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 78  ? 107.037 149.138 83.460  1.00 53.23 ?  78  LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 78  ? 106.022 149.967 82.757  1.00 50.53 1  78  LYS A NZ    1 
ATOM   641   N  N     . GLU A 1 79  ? 112.879 150.076 84.680  1.00 50.11 ?  79  GLU A N     1 
ATOM   642   C  CA    . GLU A 1 79  ? 113.830 149.709 83.636  1.00 50.50 ?  79  GLU A CA    1 
ATOM   643   C  C     . GLU A 1 79  ? 114.897 148.759 84.166  1.00 48.79 ?  79  GLU A C     1 
ATOM   644   O  O     . GLU A 1 79  ? 115.302 147.822 83.471  1.00 48.81 ?  79  GLU A O     1 
ATOM   645   C  CB    . GLU A 1 79  ? 114.473 150.964 83.041  1.00 50.57 ?  79  GLU A CB    1 
ATOM   646   C  CG    . GLU A 1 79  ? 114.011 151.367 81.624  1.00 51.59 ?  79  GLU A CG    1 
ATOM   647   C  CD    . GLU A 1 79  ? 114.235 150.311 80.532  1.00 55.08 ?  79  GLU A CD    1 
ATOM   648   O  OE1   . GLU A 1 79  ? 114.296 150.712 79.350  1.00 55.04 ?  79  GLU A OE1   1 
ATOM   649   O  OE2   . GLU A 1 79  ? 114.356 149.103 80.819  1.00 54.19 -1 79  GLU A OE2   1 
ATOM   650   N  N     . VAL A 1 80  ? 115.367 148.987 85.393  1.00 44.57 ?  80  VAL A N     1 
ATOM   651   C  CA    . VAL A 1 80  ? 116.349 148.084 85.988  1.00 41.51 ?  80  VAL A CA    1 
ATOM   652   C  C     . VAL A 1 80  ? 115.749 146.695 86.192  1.00 45.35 ?  80  VAL A C     1 
ATOM   653   O  O     . VAL A 1 80  ? 116.387 145.675 85.894  1.00 46.84 ?  80  VAL A O     1 
ATOM   654   C  CB    . VAL A 1 80  ? 116.881 148.679 87.303  1.00 40.87 ?  80  VAL A CB    1 
ATOM   655   C  CG1   . VAL A 1 80  ? 117.712 147.658 88.054  1.00 41.66 ?  80  VAL A CG1   1 
ATOM   656   C  CG2   . VAL A 1 80  ? 117.701 149.924 87.019  1.00 40.91 ?  80  VAL A CG2   1 
ATOM   657   N  N     . PHE A 1 81  ? 114.515 146.632 86.697  1.00 41.17 ?  81  PHE A N     1 
ATOM   658   C  CA    . PHE A 1 81  ? 113.854 145.341 86.876  1.00 39.00 ?  81  PHE A CA    1 
ATOM   659   C  C     . PHE A 1 81  ? 113.632 144.643 85.539  1.00 43.72 ?  81  PHE A C     1 
ATOM   660   O  O     . PHE A 1 81  ? 113.780 143.419 85.434  1.00 47.44 ?  81  PHE A O     1 
ATOM   661   C  CB    . PHE A 1 81  ? 112.526 145.529 87.609  1.00 40.74 ?  81  PHE A CB    1 
ATOM   662   C  CG    . PHE A 1 81  ? 112.639 145.454 89.106  1.00 39.06 ?  81  PHE A CG    1 
ATOM   663   C  CD1   . PHE A 1 81  ? 113.032 146.560 89.841  1.00 40.39 ?  81  PHE A CD1   1 
ATOM   664   C  CD2   . PHE A 1 81  ? 112.353 144.279 89.778  1.00 38.70 ?  81  PHE A CD2   1 
ATOM   665   C  CE1   . PHE A 1 81  ? 113.135 146.496 91.217  1.00 41.25 ?  81  PHE A CE1   1 
ATOM   666   C  CE2   . PHE A 1 81  ? 112.455 144.210 91.155  1.00 39.22 ?  81  PHE A CE2   1 
ATOM   667   C  CZ    . PHE A 1 81  ? 112.847 145.320 91.874  1.00 39.43 ?  81  PHE A CZ    1 
ATOM   668   N  N     . LYS A 1 82  ? 113.267 145.405 84.506  1.00 45.50 ?  82  LYS A N     1 
ATOM   669   C  CA    . LYS A 1 82  ? 113.081 144.828 83.179  1.00 44.86 ?  82  LYS A CA    1 
ATOM   670   C  C     . LYS A 1 82  ? 114.396 144.300 82.622  1.00 44.10 ?  82  LYS A C     1 
ATOM   671   O  O     . LYS A 1 82  ? 114.419 143.254 81.968  1.00 46.58 ?  82  LYS A O     1 
ATOM   672   C  CB    . LYS A 1 82  ? 112.476 145.869 82.238  1.00 46.41 ?  82  LYS A CB    1 
ATOM   673   C  CG    . LYS A 1 82  ? 110.973 146.029 82.379  1.00 47.69 ?  82  LYS A CG    1 
ATOM   674   C  CD    . LYS A 1 82  ? 110.400 146.856 81.241  1.00 49.23 ?  82  LYS A CD    1 
ATOM   675   C  CE    . LYS A 1 82  ? 109.001 146.390 80.877  1.00 48.47 ?  82  LYS A CE    1 
ATOM   676   N  NZ    . LYS A 1 82  ? 108.831 144.929 81.108  1.00 48.61 1  82  LYS A NZ    1 
ATOM   677   N  N     . THR A 1 83  ? 115.495 145.016 82.858  1.00 41.81 ?  83  THR A N     1 
ATOM   678   C  CA    . THR A 1 83  ? 116.803 144.521 82.442  1.00 42.61 ?  83  THR A CA    1 
ATOM   679   C  C     . THR A 1 83  ? 117.151 143.227 83.165  1.00 44.80 ?  83  THR A C     1 
ATOM   680   O  O     . THR A 1 83  ? 117.722 142.306 82.569  1.00 47.02 ?  83  THR A O     1 
ATOM   681   C  CB    . THR A 1 83  ? 117.874 145.583 82.697  1.00 42.16 ?  83  THR A CB    1 
ATOM   682   O  OG1   . THR A 1 83  ? 117.497 146.807 82.055  1.00 47.88 ?  83  THR A OG1   1 
ATOM   683   C  CG2   . THR A 1 83  ? 119.218 145.131 82.149  1.00 43.17 ?  83  THR A CG2   1 
ATOM   684   N  N     . ALA A 1 84  ? 116.817 143.143 84.455  1.00 38.43 ?  84  ALA A N     1 
ATOM   685   C  CA    . ALA A 1 84  ? 117.059 141.908 85.197  1.00 35.86 ?  84  ALA A CA    1 
ATOM   686   C  C     . ALA A 1 84  ? 116.239 140.752 84.642  1.00 39.07 ?  84  ALA A C     1 
ATOM   687   O  O     . ALA A 1 84  ? 116.744 139.633 84.498  1.00 42.31 ?  84  ALA A O     1 
ATOM   688   C  CB    . ALA A 1 84  ? 116.754 142.117 86.678  1.00 36.56 ?  84  ALA A CB    1 
ATOM   689   N  N     . TYR A 1 85  ? 114.969 141.000 84.324  1.00 44.03 ?  85  TYR A N     1 
ATOM   690   C  CA    . TYR A 1 85  ? 114.089 139.940 83.846  1.00 39.83 ?  85  TYR A CA    1 
ATOM   691   C  C     . TYR A 1 85  ? 114.282 139.608 82.372  1.00 40.48 ?  85  TYR A C     1 
ATOM   692   O  O     . TYR A 1 85  ? 113.821 138.550 81.931  1.00 41.84 ?  85  TYR A O     1 
ATOM   693   C  CB    . TYR A 1 85  ? 112.627 140.320 84.094  1.00 41.64 ?  85  TYR A CB    1 
ATOM   694   C  CG    . TYR A 1 85  ? 112.144 140.022 85.495  1.00 41.09 ?  85  TYR A CG    1 
ATOM   695   C  CD1   . TYR A 1 85  ? 111.592 138.789 85.810  1.00 39.31 ?  85  TYR A CD1   1 
ATOM   696   C  CD2   . TYR A 1 85  ? 112.239 140.972 86.502  1.00 42.16 ?  85  TYR A CD2   1 
ATOM   697   C  CE1   . TYR A 1 85  ? 111.148 138.509 87.085  1.00 41.12 ?  85  TYR A CE1   1 
ATOM   698   C  CE2   . TYR A 1 85  ? 111.796 140.702 87.782  1.00 42.11 ?  85  TYR A CE2   1 
ATOM   699   C  CZ    . TYR A 1 85  ? 111.252 139.469 88.068  1.00 43.05 ?  85  TYR A CZ    1 
ATOM   700   O  OH    . TYR A 1 85  ? 110.810 139.194 89.339  1.00 43.05 ?  85  TYR A OH    1 
ATOM   701   N  N     . ALA A 1 86  ? 114.948 140.472 81.603  1.00 40.35 ?  86  ALA A N     1 
ATOM   702   C  CA    . ALA A 1 86  ? 115.162 140.200 80.188  1.00 40.94 ?  86  ALA A CA    1 
ATOM   703   C  C     . ALA A 1 86  ? 116.144 139.062 79.956  1.00 45.40 ?  86  ALA A C     1 
ATOM   704   O  O     . ALA A 1 86  ? 116.114 138.442 78.889  1.00 45.64 ?  86  ALA A O     1 
ATOM   705   C  CB    . ALA A 1 86  ? 115.654 141.461 79.478  1.00 39.65 ?  86  ALA A CB    1 
ATOM   706   N  N     . LYS A 1 87  ? 117.014 138.780 80.928  1.00 43.91 ?  87  LYS A N     1 
ATOM   707   C  CA    . LYS A 1 87  ? 117.942 137.664 80.787  1.00 41.44 ?  87  LYS A CA    1 
ATOM   708   C  C     . LYS A 1 87  ? 117.211 136.328 80.757  1.00 42.51 ?  87  LYS A C     1 
ATOM   709   O  O     . LYS A 1 87  ? 117.698 135.370 80.145  1.00 44.65 ?  87  LYS A O     1 
ATOM   710   C  CB    . LYS A 1 87  ? 118.968 137.697 81.922  1.00 41.57 ?  87  LYS A CB    1 
ATOM   711   C  CG    . LYS A 1 87  ? 119.840 136.456 82.030  1.00 43.60 ?  87  LYS A CG    1 
ATOM   712   C  CD    . LYS A 1 87  ? 121.291 136.766 81.718  1.00 40.15 ?  87  LYS A CD    1 
ATOM   713   C  CE    . LYS A 1 87  ? 122.153 135.519 81.811  1.00 40.86 ?  87  LYS A CE    1 
ATOM   714   N  NZ    . LYS A 1 87  ? 123.084 135.403 80.655  1.00 42.63 1  87  LYS A NZ    1 
ATOM   715   N  N     . LYS A 1 88  ? 116.031 136.259 81.378  1.00 43.17 ?  88  LYS A N     1 
ATOM   716   C  CA    . LYS A 1 88  ? 115.294 135.006 81.543  1.00 41.87 ?  88  LYS A CA    1 
ATOM   717   C  C     . LYS A 1 88  ? 116.166 133.966 82.240  1.00 40.24 ?  88  LYS A C     1 
ATOM   718   O  O     . LYS A 1 88  ? 116.265 132.812 81.816  1.00 43.96 ?  88  LYS A O     1 
ATOM   719   C  CB    . LYS A 1 88  ? 114.772 134.484 80.200  1.00 43.41 ?  88  LYS A CB    1 
ATOM   720   C  CG    . LYS A 1 88  ? 113.388 134.990 79.828  1.00 44.06 ?  88  LYS A CG    1 
ATOM   721   C  CD    . LYS A 1 88  ? 113.467 136.132 78.826  1.00 44.79 ?  88  LYS A CD    1 
ATOM   722   C  CE    . LYS A 1 88  ? 112.390 137.172 79.084  1.00 45.47 ?  88  LYS A CE    1 
ATOM   723   N  NZ    . LYS A 1 88  ? 112.556 138.374 78.218  1.00 43.81 1  88  LYS A NZ    1 
ATOM   724   N  N     . PHE A 1 89  ? 116.815 134.397 83.320  1.00 39.10 ?  89  PHE A N     1 
ATOM   725   C  CA    . PHE A 1 89  ? 117.735 133.531 84.043  1.00 33.63 ?  89  PHE A CA    1 
ATOM   726   C  C     . PHE A 1 89  ? 117.009 132.314 84.597  1.00 40.27 ?  89  PHE A C     1 
ATOM   727   O  O     . PHE A 1 89  ? 115.915 132.421 85.159  1.00 42.10 ?  89  PHE A O     1 
ATOM   728   C  CB    . PHE A 1 89  ? 118.407 134.301 85.181  1.00 34.46 ?  89  PHE A CB    1 
ATOM   729   C  CG    . PHE A 1 89  ? 119.268 133.445 86.064  1.00 34.23 ?  89  PHE A CG    1 
ATOM   730   C  CD1   . PHE A 1 89  ? 120.567 133.143 85.699  1.00 34.64 ?  89  PHE A CD1   1 
ATOM   731   C  CD2   . PHE A 1 89  ? 118.778 132.938 87.255  1.00 35.69 ?  89  PHE A CD2   1 
ATOM   732   C  CE1   . PHE A 1 89  ? 121.361 132.352 86.505  1.00 37.08 ?  89  PHE A CE1   1 
ATOM   733   C  CE2   . PHE A 1 89  ? 119.567 132.145 88.063  1.00 32.64 ?  89  PHE A CE2   1 
ATOM   734   C  CZ    . PHE A 1 89  ? 120.859 131.854 87.689  1.00 35.02 ?  89  PHE A CZ    1 
ATOM   735   N  N     . ARG A 1 90  ? 117.628 131.149 84.433  1.00 41.70 ?  90  ARG A N     1 
ATOM   736   C  CA    . ARG A 1 90  ? 117.106 129.898 84.960  1.00 40.07 ?  90  ARG A CA    1 
ATOM   737   C  C     . ARG A 1 90  ? 118.183 129.233 85.798  1.00 39.11 ?  90  ARG A C     1 
ATOM   738   O  O     . ARG A 1 90  ? 119.331 129.113 85.358  1.00 40.65 ?  90  ARG A O     1 
ATOM   739   C  CB    . ARG A 1 90  ? 116.657 128.962 83.831  1.00 39.99 ?  90  ARG A CB    1 
ATOM   740   C  CG    . ARG A 1 90  ? 115.653 129.575 82.873  1.00 41.43 ?  90  ARG A CG    1 
ATOM   741   C  CD    . ARG A 1 90  ? 114.296 129.757 83.531  1.00 42.63 ?  90  ARG A CD    1 
ATOM   742   N  NE    . ARG A 1 90  ? 113.414 130.599 82.733  1.00 44.13 ?  90  ARG A NE    1 
ATOM   743   C  CZ    . ARG A 1 90  ? 112.898 131.748 83.149  1.00 45.93 ?  90  ARG A CZ    1 
ATOM   744   N  NH1   . ARG A 1 90  ? 113.147 132.219 84.360  1.00 45.56 1  90  ARG A NH1   1 
ATOM   745   N  NH2   . ARG A 1 90  ? 112.113 132.440 82.330  1.00 43.70 ?  90  ARG A NH2   1 
ATOM   746   N  N     . PHE A 1 91  ? 117.818 128.815 87.002  1.00 36.18 ?  91  PHE A N     1 
ATOM   747   C  CA    . PHE A 1 91  ? 118.747 128.071 87.838  1.00 37.86 ?  91  PHE A CA    1 
ATOM   748   C  C     . PHE A 1 91  ? 119.038 126.722 87.190  1.00 43.33 ?  91  PHE A C     1 
ATOM   749   O  O     . PHE A 1 91  ? 118.104 125.975 86.881  1.00 44.55 ?  91  PHE A O     1 
ATOM   750   C  CB    . PHE A 1 91  ? 118.172 127.878 89.238  1.00 35.06 ?  91  PHE A CB    1 
ATOM   751   C  CG    . PHE A 1 91  ? 118.112 129.142 90.048  1.00 39.65 ?  91  PHE A CG    1 
ATOM   752   C  CD1   . PHE A 1 91  ? 119.225 129.592 90.738  1.00 41.67 ?  91  PHE A CD1   1 
ATOM   753   C  CD2   . PHE A 1 91  ? 116.944 129.881 90.118  1.00 38.52 ?  91  PHE A CD2   1 
ATOM   754   C  CE1   . PHE A 1 91  ? 119.173 130.753 91.484  1.00 39.51 ?  91  PHE A CE1   1 
ATOM   755   C  CE2   . PHE A 1 91  ? 116.887 131.042 90.863  1.00 38.91 ?  91  PHE A CE2   1 
ATOM   756   C  CZ    . PHE A 1 91  ? 118.003 131.479 91.546  1.00 38.48 ?  91  PHE A CZ    1 
ATOM   757   N  N     . PRO A 1 92  ? 120.309 126.374 86.966  1.00 43.39 ?  92  PRO A N     1 
ATOM   758   C  CA    . PRO A 1 92  ? 120.609 125.112 86.277  1.00 42.30 ?  92  PRO A CA    1 
ATOM   759   C  C     . PRO A 1 92  ? 120.462 123.883 87.152  1.00 43.13 ?  92  PRO A C     1 
ATOM   760   O  O     . PRO A 1 92  ? 120.318 122.777 86.615  1.00 44.76 ?  92  PRO A O     1 
ATOM   761   C  CB    . PRO A 1 92  ? 122.063 125.301 85.832  1.00 42.75 ?  92  PRO A CB    1 
ATOM   762   C  CG    . PRO A 1 92  ? 122.645 126.173 86.895  1.00 43.24 ?  92  PRO A CG    1 
ATOM   763   C  CD    . PRO A 1 92  ? 121.535 127.088 87.368  1.00 40.50 ?  92  PRO A CD    1 
ATOM   764   N  N     . SER A 1 93  ? 120.491 124.037 88.473  1.00 42.55 ?  93  SER A N     1 
ATOM   765   C  CA    . SER A 1 93  ? 120.394 122.920 89.397  1.00 41.96 ?  93  SER A CA    1 
ATOM   766   C  C     . SER A 1 93  ? 119.360 123.243 90.466  1.00 44.09 ?  93  SER A C     1 
ATOM   767   O  O     . SER A 1 93  ? 119.089 124.408 90.766  1.00 47.27 ?  93  SER A O     1 
ATOM   768   C  CB    . SER A 1 93  ? 121.748 122.608 90.047  1.00 43.27 ?  93  SER A CB    1 
ATOM   769   O  OG    . SER A 1 93  ? 121.956 123.404 91.200  1.00 45.05 ?  93  SER A OG    1 
ATOM   770   N  N     . PHE A 1 94  ? 118.772 122.185 91.029  1.00 43.75 ?  94  PHE A N     1 
ATOM   771   C  CA    . PHE A 1 94  ? 117.743 122.368 92.047  1.00 40.05 ?  94  PHE A CA    1 
ATOM   772   C  C     . PHE A 1 94  ? 118.306 123.048 93.287  1.00 42.38 ?  94  PHE A C     1 
ATOM   773   O  O     . PHE A 1 94  ? 117.642 123.896 93.894  1.00 44.10 ?  94  PHE A O     1 
ATOM   774   C  CB    . PHE A 1 94  ? 117.114 121.024 92.414  1.00 40.38 ?  94  PHE A CB    1 
ATOM   775   C  CG    . PHE A 1 94  ? 116.489 121.005 93.779  1.00 41.40 ?  94  PHE A CG    1 
ATOM   776   C  CD1   . PHE A 1 94  ? 115.304 121.678 94.021  1.00 41.31 ?  94  PHE A CD1   1 
ATOM   777   C  CD2   . PHE A 1 94  ? 117.088 120.319 94.821  1.00 44.07 ?  94  PHE A CD2   1 
ATOM   778   C  CE1   . PHE A 1 94  ? 114.731 121.669 95.276  1.00 41.35 ?  94  PHE A CE1   1 
ATOM   779   C  CE2   . PHE A 1 94  ? 116.516 120.305 96.078  1.00 45.35 ?  94  PHE A CE2   1 
ATOM   780   C  CZ    . PHE A 1 94  ? 115.336 120.980 96.306  1.00 41.55 ?  94  PHE A CZ    1 
ATOM   781   N  N     . MET A 1 95  ? 119.529 122.685 93.683  1.00 41.51 ?  95  MET A N     1 
ATOM   782   C  CA    . MET A 1 95  ? 120.094 123.228 94.911  1.00 39.30 ?  95  MET A CA    1 
ATOM   783   C  C     . MET A 1 95  ? 120.341 124.727 94.815  1.00 41.31 ?  95  MET A C     1 
ATOM   784   O  O     . MET A 1 95  ? 120.234 125.427 95.823  1.00 42.06 ?  95  MET A O     1 
ATOM   785   C  CB    . MET A 1 95  ? 121.388 122.495 95.268  1.00 40.51 ?  95  MET A CB    1 
ATOM   786   C  CG    . MET A 1 95  ? 121.972 122.842 96.638  1.00 43.89 ?  95  MET A CG    1 
ATOM   787   S  SD    . MET A 1 95  ? 121.004 122.432 98.114  1.00 54.57 ?  95  MET A SD    1 
ATOM   788   C  CE    . MET A 1 95  ? 119.948 121.099 97.550  1.00 45.92 ?  95  MET A CE    1 
ATOM   789   N  N     . SER A 1 96  ? 120.656 125.240 93.624  1.00 38.56 ?  96  SER A N     1 
ATOM   790   C  CA    . SER A 1 96  ? 120.842 126.681 93.471  1.00 34.14 ?  96  SER A CA    1 
ATOM   791   C  C     . SER A 1 96  ? 119.570 127.439 93.835  1.00 38.41 ?  96  SER A C     1 
ATOM   792   O  O     . SER A 1 96  ? 119.583 128.342 94.684  1.00 40.40 ?  96  SER A O     1 
ATOM   793   C  CB    . SER A 1 96  ? 121.262 126.997 92.037  1.00 32.01 ?  96  SER A CB    1 
ATOM   794   O  OG    . SER A 1 96  ? 122.234 126.078 91.576  1.00 36.90 ?  96  SER A OG    1 
ATOM   795   N  N     . ALA A 1 97  ? 118.452 127.061 93.212  1.00 38.59 ?  97  ALA A N     1 
ATOM   796   C  CA    . ALA A 1 97  ? 117.182 127.720 93.490  1.00 34.80 ?  97  ALA A CA    1 
ATOM   797   C  C     . ALA A 1 97  ? 116.735 127.474 94.922  1.00 35.83 ?  97  ALA A C     1 
ATOM   798   O  O     . ALA A 1 97  ? 116.199 128.377 95.574  1.00 41.87 ?  97  ALA A O     1 
ATOM   799   C  CB    . ALA A 1 97  ? 116.118 127.240 92.506  1.00 36.02 ?  97  ALA A CB    1 
ATOM   800   N  N     . PHE A 1 98  ? 116.937 126.255 95.427  1.00 37.46 ?  98  PHE A N     1 
ATOM   801   C  CA    . PHE A 1 98  ? 116.542 125.954 96.797  1.00 37.31 ?  98  PHE A CA    1 
ATOM   802   C  C     . PHE A 1 98  ? 117.307 126.817 97.791  1.00 37.48 ?  98  PHE A C     1 
ATOM   803   O  O     . PHE A 1 98  ? 116.714 127.390 98.710  1.00 46.19 ?  98  PHE A O     1 
ATOM   804   C  CB    . PHE A 1 98  ? 116.760 124.472 97.096  1.00 41.86 ?  98  PHE A CB    1 
ATOM   805   C  CG    . PHE A 1 98  ? 116.423 124.085 98.505  1.00 42.40 ?  98  PHE A CG    1 
ATOM   806   C  CD1   . PHE A 1 98  ? 115.107 123.878 98.881  1.00 42.56 ?  98  PHE A CD1   1 
ATOM   807   C  CD2   . PHE A 1 98  ? 117.418 123.935 99.456  1.00 41.56 ?  98  PHE A CD2   1 
ATOM   808   C  CE1   . PHE A 1 98  ? 114.791 123.525 100.177 1.00 43.31 ?  98  PHE A CE1   1 
ATOM   809   C  CE2   . PHE A 1 98  ? 117.108 123.582 100.754 1.00 42.84 ?  98  PHE A CE2   1 
ATOM   810   C  CZ    . PHE A 1 98  ? 115.792 123.377 101.115 1.00 44.36 ?  98  PHE A CZ    1 
ATOM   811   N  N     . LYS A 1 99  ? 118.623 126.937 97.610  1.00 38.45 ?  99  LYS A N     1 
ATOM   812   C  CA    . LYS A 1 99  ? 119.431 127.747 98.511  1.00 36.82 ?  99  LYS A CA    1 
ATOM   813   C  C     . LYS A 1 99  ? 119.054 129.216 98.418  1.00 38.12 ?  99  LYS A C     1 
ATOM   814   O  O     . LYS A 1 99  ? 118.987 129.906 99.443  1.00 43.28 ?  99  LYS A O     1 
ATOM   815   C  CB    . LYS A 1 99  ? 120.915 127.550 98.204  1.00 37.70 ?  99  LYS A CB    1 
ATOM   816   C  CG    . LYS A 1 99  ? 121.490 126.252 98.746  1.00 39.76 ?  99  LYS A CG    1 
ATOM   817   C  CD    . LYS A 1 99  ? 121.114 126.037 100.199 1.00 41.23 ?  99  LYS A CD    1 
ATOM   818   C  CE    . LYS A 1 99  ? 122.312 125.593 101.019 1.00 39.84 ?  99  LYS A CE    1 
ATOM   819   N  NZ    . LYS A 1 99  ? 122.066 125.751 102.478 1.00 43.67 1  99  LYS A NZ    1 
ATOM   820   N  N     . PHE A 1 100 ? 118.795 129.720 97.208  1.00 33.98 ?  100 PHE A N     1 
ATOM   821   C  CA    . PHE A 1 100 ? 118.404 131.121 97.100  1.00 32.03 ?  100 PHE A CA    1 
ATOM   822   C  C     . PHE A 1 100 ? 117.066 131.378 97.781  1.00 35.49 ?  100 PHE A C     1 
ATOM   823   O  O     . PHE A 1 100 ? 116.932 132.316 98.576  1.00 40.64 ?  100 PHE A O     1 
ATOM   824   C  CB    . PHE A 1 100 ? 118.336 131.572 95.645  1.00 29.77 ?  100 PHE A CB    1 
ATOM   825   C  CG    . PHE A 1 100 ? 117.768 132.950 95.490  1.00 36.38 ?  100 PHE A CG    1 
ATOM   826   C  CD1   . PHE A 1 100 ? 118.517 134.061 95.845  1.00 36.19 ?  100 PHE A CD1   1 
ATOM   827   C  CD2   . PHE A 1 100 ? 116.473 133.137 95.045  1.00 35.11 ?  100 PHE A CD2   1 
ATOM   828   C  CE1   . PHE A 1 100 ? 117.994 135.330 95.730  1.00 35.16 ?  100 PHE A CE1   1 
ATOM   829   C  CE2   . PHE A 1 100 ? 115.944 134.406 94.932  1.00 35.41 ?  100 PHE A CE2   1 
ATOM   830   C  CZ    . PHE A 1 100 ? 116.707 135.504 95.274  1.00 35.14 ?  100 PHE A CZ    1 
ATOM   831   N  N     . TYR A 1 101 ? 116.058 130.558 97.484  1.00 38.04 ?  101 TYR A N     1 
ATOM   832   C  CA    . TYR A 1 101 ? 114.719 130.805 97.997  1.00 37.60 ?  101 TYR A CA    1 
ATOM   833   C  C     . TYR A 1 101 ? 114.540 130.357 99.440  1.00 38.38 ?  101 TYR A C     1 
ATOM   834   O  O     . TYR A 1 101 ? 113.496 130.644 100.034 1.00 44.60 ?  101 TYR A O     1 
ATOM   835   C  CB    . TYR A 1 101 ? 113.683 130.125 97.099  1.00 36.13 ?  101 TYR A CB    1 
ATOM   836   C  CG    . TYR A 1 101 ? 113.469 130.853 95.792  1.00 32.59 ?  101 TYR A CG    1 
ATOM   837   C  CD1   . TYR A 1 101 ? 112.743 132.036 95.746  1.00 36.94 ?  101 TYR A CD1   1 
ATOM   838   C  CD2   . TYR A 1 101 ? 114.006 130.370 94.608  1.00 34.18 ?  101 TYR A CD2   1 
ATOM   839   C  CE1   . TYR A 1 101 ? 112.554 132.710 94.558  1.00 38.04 ?  101 TYR A CE1   1 
ATOM   840   C  CE2   . TYR A 1 101 ? 113.821 131.036 93.415  1.00 36.49 ?  101 TYR A CE2   1 
ATOM   841   C  CZ    . TYR A 1 101 ? 113.094 132.206 93.395  1.00 38.47 ?  101 TYR A CZ    1 
ATOM   842   O  OH    . TYR A 1 101 ? 112.907 132.874 92.207  1.00 41.93 ?  101 TYR A OH    1 
ATOM   843   N  N     . ASN A 1 102 ? 115.525 129.669 100.018 1.00 41.74 ?  102 ASN A N     1 
ATOM   844   C  CA    . ASN A 1 102 ? 115.494 129.332 101.432 1.00 45.03 ?  102 ASN A CA    1 
ATOM   845   C  C     . ASN A 1 102 ? 116.389 130.224 102.280 1.00 45.97 ?  102 ASN A C     1 
ATOM   846   O  O     . ASN A 1 102 ? 116.158 130.333 103.489 1.00 48.30 ?  102 ASN A O     1 
ATOM   847   C  CB    . ASN A 1 102 ? 115.911 127.870 101.636 1.00 42.99 ?  102 ASN A CB    1 
ATOM   848   C  CG    . ASN A 1 102 ? 114.726 126.942 101.803 1.00 46.78 ?  102 ASN A CG    1 
ATOM   849   O  OD1   . ASN A 1 102 ? 113.935 126.752 100.879 1.00 48.92 ?  102 ASN A OD1   1 
ATOM   850   N  ND2   . ASN A 1 102 ? 114.599 126.353 102.986 1.00 44.50 ?  102 ASN A ND2   1 
ATOM   851   N  N     . ASP A 1 103 ? 117.397 130.860 101.683 1.00 41.29 ?  103 ASP A N     1 
ATOM   852   C  CA    . ASP A 1 103 ? 118.351 131.665 102.433 1.00 41.46 ?  103 ASP A CA    1 
ATOM   853   C  C     . ASP A 1 103 ? 118.332 133.142 102.079 1.00 40.82 ?  103 ASP A C     1 
ATOM   854   O  O     . ASP A 1 103 ? 118.518 133.973 102.970 1.00 45.01 ?  103 ASP A O     1 
ATOM   855   C  CB    . ASP A 1 103 ? 119.774 131.134 102.223 1.00 44.47 ?  103 ASP A CB    1 
ATOM   856   C  CG    . ASP A 1 103 ? 119.989 129.777 102.857 1.00 48.51 ?  103 ASP A CG    1 
ATOM   857   O  OD1   . ASP A 1 103 ? 119.077 129.296 103.561 1.00 47.69 ?  103 ASP A OD1   1 
ATOM   858   O  OD2   . ASP A 1 103 ? 121.071 129.189 102.649 1.00 50.67 -1 103 ASP A OD2   1 
ATOM   859   N  N     . TYR A 1 104 ? 118.112 133.497 100.816 1.00 34.75 ?  104 TYR A N     1 
ATOM   860   C  CA    . TYR A 1 104 ? 118.288 134.870 100.366 1.00 38.48 ?  104 TYR A CA    1 
ATOM   861   C  C     . TYR A 1 104 ? 117.016 135.542 99.875  1.00 39.62 ?  104 TYR A C     1 
ATOM   862   O  O     . TYR A 1 104 ? 116.911 136.765 99.978  1.00 43.43 ?  104 TYR A O     1 
ATOM   863   C  CB    . TYR A 1 104 ? 119.344 134.931 99.251  1.00 38.18 ?  104 TYR A CB    1 
ATOM   864   C  CG    . TYR A 1 104 ? 120.689 134.394 99.677  1.00 40.21 ?  104 TYR A CG    1 
ATOM   865   C  CD1   . TYR A 1 104 ? 121.601 135.202 100.344 1.00 37.87 ?  104 TYR A CD1   1 
ATOM   866   C  CD2   . TYR A 1 104 ? 121.044 133.077 99.424  1.00 35.30 ?  104 TYR A CD2   1 
ATOM   867   C  CE1   . TYR A 1 104 ? 122.829 134.713 100.740 1.00 36.61 ?  104 TYR A CE1   1 
ATOM   868   C  CE2   . TYR A 1 104 ? 122.267 132.579 99.818  1.00 35.79 ?  104 TYR A CE2   1 
ATOM   869   C  CZ    . TYR A 1 104 ? 123.157 133.401 100.475 1.00 39.06 ?  104 TYR A CZ    1 
ATOM   870   O  OH    . TYR A 1 104 ? 124.379 132.909 100.868 1.00 40.64 ?  104 TYR A OH    1 
ATOM   871   N  N     . ALA A 1 105 ? 116.056 134.791 99.340  1.00 40.76 ?  105 ALA A N     1 
ATOM   872   C  CA    . ALA A 1 105 ? 114.826 135.402 98.857  1.00 38.14 ?  105 ALA A CA    1 
ATOM   873   C  C     . ALA A 1 105 ? 114.040 136.004 100.014 1.00 42.98 ?  105 ALA A C     1 
ATOM   874   O  O     . ALA A 1 105 ? 113.895 135.390 101.075 1.00 44.65 ?  105 ALA A O     1 
ATOM   875   C  CB    . ALA A 1 105 ? 113.973 134.374 98.117  1.00 37.75 ?  105 ALA A CB    1 
ATOM   876   N  N     . LEU A 1 106 ? 113.536 137.217 99.806  1.00 44.74 ?  106 LEU A N     1 
ATOM   877   C  CA    . LEU A 1 106 ? 112.769 137.894 100.842 1.00 40.94 ?  106 LEU A CA    1 
ATOM   878   C  C     . LEU A 1 106 ? 111.424 137.208 101.035 1.00 45.24 ?  106 LEU A C     1 
ATOM   879   O  O     . LEU A 1 106 ? 110.692 136.964 100.071 1.00 46.46 ?  106 LEU A O     1 
ATOM   880   C  CB    . LEU A 1 106 ? 112.568 139.363 100.480 1.00 44.43 ?  106 LEU A CB    1 
ATOM   881   C  CG    . LEU A 1 106 ? 111.811 140.216 101.501 1.00 43.46 ?  106 LEU A CG    1 
ATOM   882   C  CD1   . LEU A 1 106 ? 112.606 140.347 102.789 1.00 42.46 ?  106 LEU A CD1   1 
ATOM   883   C  CD2   . LEU A 1 106 ? 111.495 141.583 100.921 1.00 43.80 ?  106 LEU A CD2   1 
ATOM   884   N  N     . LYS A 1 107 ? 111.098 136.903 102.286 1.00 50.99 ?  107 LYS A N     1 
ATOM   885   C  CA    . LYS A 1 107 ? 109.847 136.255 102.642 1.00 50.88 ?  107 LYS A CA    1 
ATOM   886   C  C     . LYS A 1 107 ? 109.036 137.166 103.552 1.00 54.09 ?  107 LYS A C     1 
ATOM   887   O  O     . LYS A 1 107 ? 109.565 138.093 104.171 1.00 54.52 ?  107 LYS A O     1 
ATOM   888   C  CB    . LYS A 1 107 ? 110.094 134.907 103.333 1.00 51.63 ?  107 LYS A CB    1 
ATOM   889   C  CG    . LYS A 1 107 ? 111.234 134.100 102.736 1.00 50.31 ?  107 LYS A CG    1 
ATOM   890   C  CD    . LYS A 1 107 ? 110.713 132.966 101.870 1.00 50.99 ?  107 LYS A CD    1 
ATOM   891   C  CE    . LYS A 1 107 ? 111.354 131.642 102.251 1.00 54.46 ?  107 LYS A CE    1 
ATOM   892   N  NZ    . LYS A 1 107 ? 111.088 130.582 101.239 1.00 51.38 1  107 LYS A NZ    1 
ATOM   893   N  N     . THR A 1 108 ? 107.736 136.893 103.620 1.00 58.40 ?  108 THR A N     1 
ATOM   894   C  CA    . THR A 1 108 ? 106.853 137.651 104.490 1.00 57.21 ?  108 THR A CA    1 
ATOM   895   C  C     . THR A 1 108 ? 107.229 137.427 105.956 1.00 59.00 ?  108 THR A C     1 
ATOM   896   O  O     . THR A 1 108 ? 108.039 136.562 106.296 1.00 59.19 ?  108 THR A O     1 
ATOM   897   C  CB    . THR A 1 108 ? 105.398 137.256 104.249 1.00 57.88 ?  108 THR A CB    1 
ATOM   898   O  OG1   . THR A 1 108 ? 105.248 135.844 104.441 1.00 63.02 ?  108 THR A OG1   1 
ATOM   899   C  CG2   . THR A 1 108 ? 104.980 137.614 102.832 1.00 57.15 ?  108 THR A CG2   1 
ATOM   900   N  N     . ASN A 1 109 ? 106.626 138.232 106.834 1.00 60.83 ?  109 ASN A N     1 
ATOM   901   C  CA    . ASN A 1 109 ? 106.901 138.104 108.262 1.00 62.67 ?  109 ASN A CA    1 
ATOM   902   C  C     . ASN A 1 109 ? 106.502 136.733 108.791 1.00 64.04 ?  109 ASN A C     1 
ATOM   903   O  O     . ASN A 1 109 ? 107.100 136.240 109.754 1.00 64.25 ?  109 ASN A O     1 
ATOM   904   C  CB    . ASN A 1 109 ? 106.177 139.203 109.041 1.00 62.17 ?  109 ASN A CB    1 
ATOM   905   C  CG    . ASN A 1 109 ? 106.590 140.593 108.606 1.00 61.16 ?  109 ASN A CG    1 
ATOM   906   O  OD1   . ASN A 1 109 ? 106.844 140.837 107.428 1.00 60.42 ?  109 ASN A OD1   1 
ATOM   907   N  ND2   . ASN A 1 109 ? 106.661 141.515 109.559 1.00 61.63 ?  109 ASN A ND2   1 
ATOM   908   N  N     . ASP A 1 110 ? 105.500 136.107 108.180 1.00 65.81 ?  110 ASP A N     1 
ATOM   909   C  CA    . ASP A 1 110 ? 105.059 134.771 108.554 1.00 64.93 ?  110 ASP A CA    1 
ATOM   910   C  C     . ASP A 1 110 ? 105.862 133.666 107.880 1.00 67.09 ?  110 ASP A C     1 
ATOM   911   O  O     . ASP A 1 110 ? 105.624 132.487 108.165 1.00 67.07 ?  110 ASP A O     1 
ATOM   912   C  CB    . ASP A 1 110 ? 103.569 134.614 108.236 1.00 67.12 ?  110 ASP A CB    1 
ATOM   913   C  CG    . ASP A 1 110 ? 103.270 134.786 106.758 1.00 68.83 ?  110 ASP A CG    1 
ATOM   914   O  OD1   . ASP A 1 110 ? 104.209 135.101 105.996 1.00 68.34 ?  110 ASP A OD1   1 
ATOM   915   O  OD2   . ASP A 1 110 ? 102.102 134.616 106.358 1.00 66.30 -1 110 ASP A OD2   1 
ATOM   916   N  N     . LYS A 1 111 ? 106.803 134.020 106.998 1.00 66.76 ?  111 LYS A N     1 
ATOM   917   C  CA    . LYS A 1 111 ? 107.737 133.071 106.388 1.00 65.22 ?  111 LYS A CA    1 
ATOM   918   C  C     . LYS A 1 111 ? 107.024 131.952 105.631 1.00 67.30 ?  111 LYS A C     1 
ATOM   919   O  O     . LYS A 1 111 ? 107.490 130.810 105.613 1.00 68.62 ?  111 LYS A O     1 
ATOM   920   C  CB    . LYS A 1 111 ? 108.687 132.474 107.431 1.00 66.02 ?  111 LYS A CB    1 
ATOM   921   C  CG    . LYS A 1 111 ? 109.292 133.487 108.391 1.00 66.12 ?  111 LYS A CG    1 
ATOM   922   C  CD    . LYS A 1 111 ? 110.100 134.539 107.649 1.00 67.95 ?  111 LYS A CD    1 
ATOM   923   C  CE    . LYS A 1 111 ? 111.322 133.930 106.981 1.00 68.19 ?  111 LYS A CE    1 
ATOM   924   N  NZ    . LYS A 1 111 ? 112.156 134.962 106.303 1.00 65.71 1  111 LYS A NZ    1 
ATOM   925   N  N     . LYS A 1 112 ? 105.894 132.259 104.995 1.00 65.38 ?  112 LYS A N     1 
ATOM   926   C  CA    . LYS A 1 112 ? 105.180 131.278 104.191 1.00 66.35 ?  112 LYS A CA    1 
ATOM   927   C  C     . LYS A 1 112 ? 105.048 131.679 102.730 1.00 66.89 ?  112 LYS A C     1 
ATOM   928   O  O     . LYS A 1 112 ? 104.664 130.840 101.909 1.00 68.20 ?  112 LYS A O     1 
ATOM   929   C  CB    . LYS A 1 112 ? 103.779 131.023 104.767 1.00 67.22 ?  112 LYS A CB    1 
ATOM   930   C  CG    . LYS A 1 112 ? 102.756 132.078 104.389 1.00 67.45 ?  112 LYS A CG    1 
ATOM   931   C  CD    . LYS A 1 112 ? 101.339 131.599 104.655 1.00 67.24 ?  112 LYS A CD    1 
ATOM   932   C  CE    . LYS A 1 112 ? 101.191 131.072 106.074 1.00 69.30 ?  112 LYS A CE    1 
ATOM   933   N  NZ    . LYS A 1 112 ? 101.640 132.068 107.086 1.00 66.57 1  112 LYS A NZ    1 
ATOM   934   N  N     . LYS A 1 113 ? 105.350 132.927 102.387 1.00 59.81 ?  113 LYS A N     1 
ATOM   935   C  CA    . LYS A 1 113 ? 105.235 133.414 101.023 1.00 58.38 ?  113 LYS A CA    1 
ATOM   936   C  C     . LYS A 1 113 ? 106.556 134.030 100.592 1.00 59.83 ?  113 LYS A C     1 
ATOM   937   O  O     . LYS A 1 113 ? 107.347 134.489 101.421 1.00 60.10 ?  113 LYS A O     1 
ATOM   938   C  CB    . LYS A 1 113 ? 104.107 134.444 100.890 1.00 58.07 ?  113 LYS A CB    1 
ATOM   939   C  CG    . LYS A 1 113 ? 102.727 133.835 100.708 1.00 58.53 ?  113 LYS A CG    1 
ATOM   940   C  CD    . LYS A 1 113 ? 102.558 133.251 99.316  1.00 59.74 ?  113 LYS A CD    1 
ATOM   941   C  CE    . LYS A 1 113 ? 101.141 132.751 99.096  1.00 58.90 ?  113 LYS A CE    1 
ATOM   942   N  NZ    . LYS A 1 113 ? 100.972 132.128 97.755  1.00 60.00 1  113 LYS A NZ    1 
ATOM   943   N  N     . ILE A 1 114 ? 106.788 134.035 99.283  1.00 53.46 ?  114 ILE A N     1 
ATOM   944   C  CA    . ILE A 1 114 ? 108.024 134.538 98.696  1.00 51.44 ?  114 ILE A CA    1 
ATOM   945   C  C     . ILE A 1 114 ? 107.729 135.889 98.064  1.00 49.75 ?  114 ILE A C     1 
ATOM   946   O  O     . ILE A 1 114 ? 106.912 135.988 97.141  1.00 52.17 ?  114 ILE A O     1 
ATOM   947   C  CB    . ILE A 1 114 ? 108.601 133.556 97.666  1.00 51.20 ?  114 ILE A CB    1 
ATOM   948   C  CG1   . ILE A 1 114 ? 109.240 132.361 98.374  1.00 50.03 ?  114 ILE A CG1   1 
ATOM   949   C  CG2   . ILE A 1 114 ? 109.617 134.250 96.775  1.00 48.71 ?  114 ILE A CG2   1 
ATOM   950   C  CD1   . ILE A 1 114 ? 109.344 131.129 97.511  1.00 50.18 ?  114 ILE A CD1   1 
ATOM   951   N  N     . LEU A 1 115 ? 108.390 136.931 98.564  1.00 46.17 ?  115 LEU A N     1 
ATOM   952   C  CA    . LEU A 1 115 ? 108.214 138.274 98.030  1.00 46.36 ?  115 LEU A CA    1 
ATOM   953   C  C     . LEU A 1 115 ? 109.222 138.616 96.944  1.00 47.43 ?  115 LEU A C     1 
ATOM   954   O  O     . LEU A 1 115 ? 108.917 139.424 96.061  1.00 49.19 ?  115 LEU A O     1 
ATOM   955   C  CB    . LEU A 1 115 ? 108.315 139.307 99.155  1.00 47.39 ?  115 LEU A CB    1 
ATOM   956   C  CG    . LEU A 1 115 ? 107.208 139.268 100.208 1.00 48.80 ?  115 LEU A CG    1 
ATOM   957   C  CD1   . LEU A 1 115 ? 107.688 139.904 101.500 1.00 46.26 ?  115 LEU A CD1   1 
ATOM   958   C  CD2   . LEU A 1 115 ? 105.958 139.963 99.695  1.00 45.93 ?  115 LEU A CD2   1 
ATOM   959   N  N     . GLU A 1 116 ? 110.410 138.019 96.985  1.00 45.75 ?  116 GLU A N     1 
ATOM   960   C  CA    . GLU A 1 116 ? 111.490 138.352 96.068  1.00 42.66 ?  116 GLU A CA    1 
ATOM   961   C  C     . GLU A 1 116 ? 111.864 137.138 95.232  1.00 42.32 ?  116 GLU A C     1 
ATOM   962   O  O     . GLU A 1 116 ? 112.112 136.056 95.775  1.00 46.46 ?  116 GLU A O     1 
ATOM   963   C  CB    . GLU A 1 116 ? 112.723 138.848 96.828  1.00 43.84 ?  116 GLU A CB    1 
ATOM   964   C  CG    . GLU A 1 116 ? 112.927 140.347 96.768  1.00 44.60 ?  116 GLU A CG    1 
ATOM   965   C  CD    . GLU A 1 116 ? 114.156 140.793 97.533  1.00 43.95 ?  116 GLU A CD    1 
ATOM   966   O  OE1   . GLU A 1 116 ? 114.783 139.944 98.200  1.00 42.41 ?  116 GLU A OE1   1 
ATOM   967   O  OE2   . GLU A 1 116 ? 114.494 141.993 97.468  1.00 46.49 -1 116 GLU A OE2   1 
ATOM   968   N  N     . ARG A 1 117 ? 111.905 137.322 93.916  1.00 41.40 ?  117 ARG A N     1 
ATOM   969   C  CA    . ARG A 1 117 ? 112.524 136.353 93.030  1.00 42.35 ?  117 ARG A CA    1 
ATOM   970   C  C     . ARG A 1 117 ? 114.022 136.636 92.946  1.00 42.07 ?  117 ARG A C     1 
ATOM   971   O  O     . ARG A 1 117 ? 114.543 137.553 93.586  1.00 45.43 ?  117 ARG A O     1 
ATOM   972   C  CB    . ARG A 1 117 ? 111.870 136.396 91.652  1.00 42.96 ?  117 ARG A CB    1 
ATOM   973   C  CG    . ARG A 1 117 ? 110.379 136.096 91.658  1.00 43.74 ?  117 ARG A CG    1 
ATOM   974   C  CD    . ARG A 1 117 ? 109.923 135.540 90.321  1.00 46.22 ?  117 ARG A CD    1 
ATOM   975   N  NE    . ARG A 1 117 ? 109.952 134.084 90.293  1.00 47.84 ?  117 ARG A NE    1 
ATOM   976   C  CZ    . ARG A 1 117 ? 108.875 133.311 90.333  1.00 44.68 ?  117 ARG A CZ    1 
ATOM   977   N  NH1   . ARG A 1 117 ? 107.658 133.825 90.407  1.00 45.48 1  117 ARG A NH1   1 
ATOM   978   N  NH2   . ARG A 1 117 ? 109.022 131.990 90.295  1.00 45.28 ?  117 ARG A NH2   1 
ATOM   979   N  N     . TYR A 1 118 ? 114.733 135.836 92.150  1.00 35.82 ?  118 TYR A N     1 
ATOM   980   C  CA    . TYR A 1 118 ? 116.149 136.107 91.930  1.00 33.09 ?  118 TYR A CA    1 
ATOM   981   C  C     . TYR A 1 118 ? 116.346 137.441 91.223  1.00 35.83 ?  118 TYR A C     1 
ATOM   982   O  O     . TYR A 1 118 ? 117.220 138.232 91.598  1.00 36.46 ?  118 TYR A O     1 
ATOM   983   C  CB    . TYR A 1 118 ? 116.787 134.973 91.131  1.00 33.04 ?  118 TYR A CB    1 
ATOM   984   C  CG    . TYR A 1 118 ? 118.294 134.949 91.211  1.00 34.61 ?  118 TYR A CG    1 
ATOM   985   C  CD1   . TYR A 1 118 ? 118.945 135.071 92.429  1.00 34.13 ?  118 TYR A CD1   1 
ATOM   986   C  CD2   . TYR A 1 118 ? 119.065 134.811 90.068  1.00 32.57 ?  118 TYR A CD2   1 
ATOM   987   C  CE1   . TYR A 1 118 ? 120.321 135.050 92.507  1.00 32.21 ?  118 TYR A CE1   1 
ATOM   988   C  CE2   . TYR A 1 118 ? 120.442 134.787 90.134  1.00 28.54 ?  118 TYR A CE2   1 
ATOM   989   C  CZ    . TYR A 1 118 ? 121.065 134.907 91.356  1.00 33.42 ?  118 TYR A CZ    1 
ATOM   990   O  OH    . TYR A 1 118 ? 122.437 134.886 91.426  1.00 41.14 ?  118 TYR A OH    1 
ATOM   991   N  N     . GLU A 1 119 ? 115.527 137.713 90.205  1.00 38.05 ?  119 GLU A N     1 
ATOM   992   C  CA    . GLU A 1 119 ? 115.637 138.974 89.483  1.00 33.51 ?  119 GLU A CA    1 
ATOM   993   C  C     . GLU A 1 119 ? 115.284 140.156 90.376  1.00 34.98 ?  119 GLU A C     1 
ATOM   994   O  O     . GLU A 1 119 ? 115.912 141.214 90.283  1.00 41.26 ?  119 GLU A O     1 
ATOM   995   C  CB    . GLU A 1 119 ? 114.748 138.945 88.241  1.00 34.53 ?  119 GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 119 ? 115.212 137.974 87.168  1.00 33.42 ?  119 GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 119 ? 114.593 136.598 87.315  1.00 38.33 ?  119 GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 119 ? 114.269 136.204 88.455  1.00 40.04 ?  119 GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 119 ? 114.431 135.908 86.287  1.00 39.80 -1 119 GLU A OE2   1 
ATOM   1000  N  N     . ASP A 1 120 ? 114.288 139.997 91.251  1.00 38.34 ?  120 ASP A N     1 
ATOM   1001  C  CA    . ASP A 1 120 ? 113.921 141.081 92.158  1.00 35.32 ?  120 ASP A CA    1 
ATOM   1002  C  C     . ASP A 1 120 ? 115.053 141.402 93.125  1.00 36.45 ?  120 ASP A C     1 
ATOM   1003  O  O     . ASP A 1 120 ? 115.396 142.573 93.331  1.00 37.89 ?  120 ASP A O     1 
ATOM   1004  C  CB    . ASP A 1 120 ? 112.652 140.719 92.930  1.00 39.27 ?  120 ASP A CB    1 
ATOM   1005  C  CG    . ASP A 1 120 ? 111.504 140.355 92.021  1.00 44.42 ?  120 ASP A CG    1 
ATOM   1006  O  OD1   . ASP A 1 120 ? 111.312 141.050 91.002  1.00 42.64 ?  120 ASP A OD1   1 
ATOM   1007  O  OD2   . ASP A 1 120 ? 110.789 139.377 92.324  1.00 48.92 -1 120 ASP A OD2   1 
ATOM   1008  N  N     . ARG A 1 121 ? 115.642 140.370 93.733  1.00 35.02 ?  121 ARG A N     1 
ATOM   1009  C  CA    . ARG A 1 121 ? 116.747 140.592 94.659  1.00 32.20 ?  121 ARG A CA    1 
ATOM   1010  C  C     . ARG A 1 121 ? 117.939 141.212 93.945  1.00 33.06 ?  121 ARG A C     1 
ATOM   1011  O  O     . ARG A 1 121 ? 118.578 142.131 94.469  1.00 38.75 ?  121 ARG A O     1 
ATOM   1012  C  CB    . ARG A 1 121 ? 117.143 139.275 95.326  1.00 30.88 ?  121 ARG A CB    1 
ATOM   1013  C  CG    . ARG A 1 121 ? 118.392 139.362 96.191  1.00 30.04 ?  121 ARG A CG    1 
ATOM   1014  C  CD    . ARG A 1 121 ? 118.033 139.406 97.666  1.00 29.75 ?  121 ARG A CD    1 
ATOM   1015  N  NE    . ARG A 1 121 ? 117.346 140.641 98.029  1.00 37.01 ?  121 ARG A NE    1 
ATOM   1016  C  CZ    . ARG A 1 121 ? 117.935 141.698 98.570  1.00 36.31 ?  121 ARG A CZ    1 
ATOM   1017  N  NH1   . ARG A 1 121 ? 119.229 141.704 98.846  1.00 34.61 1  121 ARG A NH1   1 
ATOM   1018  N  NH2   . ARG A 1 121 ? 117.207 142.776 98.846  1.00 33.20 ?  121 ARG A NH2   1 
ATOM   1019  N  N     . ILE A 1 122 ? 118.248 140.726 92.740  1.00 30.77 ?  122 ILE A N     1 
ATOM   1020  C  CA    . ILE A 1 122 ? 119.372 141.273 91.988  1.00 28.80 ?  122 ILE A CA    1 
ATOM   1021  C  C     . ILE A 1 122 ? 119.119 142.732 91.628  1.00 30.77 ?  122 ILE A C     1 
ATOM   1022  O  O     . ILE A 1 122 ? 120.019 143.572 91.734  1.00 34.25 ?  122 ILE A O     1 
ATOM   1023  C  CB    . ILE A 1 122 ? 119.644 140.409 90.743  1.00 30.30 ?  122 ILE A CB    1 
ATOM   1024  C  CG1   . ILE A 1 122 ? 120.417 139.151 91.142  1.00 26.40 ?  122 ILE A CG1   1 
ATOM   1025  C  CG2   . ILE A 1 122 ? 120.405 141.198 89.686  1.00 28.94 ?  122 ILE A CG2   1 
ATOM   1026  C  CD1   . ILE A 1 122 ? 120.848 138.304 89.979  1.00 28.85 ?  122 ILE A CD1   1 
ATOM   1027  N  N     . SER A 1 123 ? 117.895 143.061 91.208  1.00 31.33 ?  123 SER A N     1 
ATOM   1028  C  CA    . SER A 1 123 ? 117.565 144.444 90.878  1.00 32.29 ?  123 SER A CA    1 
ATOM   1029  C  C     . SER A 1 123 ? 117.677 145.344 92.100  1.00 30.43 ?  123 SER A C     1 
ATOM   1030  O  O     . SER A 1 123 ? 118.181 146.468 92.006  1.00 32.18 ?  123 SER A O     1 
ATOM   1031  C  CB    . SER A 1 123 ? 116.155 144.524 90.295  1.00 28.37 ?  123 SER A CB    1 
ATOM   1032  O  OG    . SER A 1 123 ? 115.924 143.481 89.370  1.00 32.84 ?  123 SER A OG    1 
ATOM   1033  N  N     . ILE A 1 124 ? 117.205 144.871 93.254  1.00 30.02 ?  124 ILE A N     1 
ATOM   1034  C  CA    . ILE A 1 124 ? 117.284 145.678 94.467  1.00 32.25 ?  124 ILE A CA    1 
ATOM   1035  C  C     . ILE A 1 124 ? 118.736 145.909 94.864  1.00 32.94 ?  124 ILE A C     1 
ATOM   1036  O  O     . ILE A 1 124 ? 119.125 147.029 95.223  1.00 38.22 ?  124 ILE A O     1 
ATOM   1037  C  CB    . ILE A 1 124 ? 116.475 145.017 95.596  1.00 36.78 ?  124 ILE A CB    1 
ATOM   1038  C  CG1   . ILE A 1 124 ? 114.979 145.192 95.337  1.00 37.74 ?  124 ILE A CG1   1 
ATOM   1039  C  CG2   . ILE A 1 124 ? 116.856 145.598 96.949  1.00 29.38 ?  124 ILE A CG2   1 
ATOM   1040  C  CD1   . ILE A 1 124 ? 114.580 146.612 94.994  1.00 32.41 ?  124 ILE A CD1   1 
ATOM   1041  N  N     . VAL A 1 125 ? 119.564 144.863 94.793  1.00 30.55 ?  125 VAL A N     1 
ATOM   1042  C  CA    . VAL A 1 125 ? 120.974 145.012 95.143  1.00 29.88 ?  125 VAL A CA    1 
ATOM   1043  C  C     . VAL A 1 125 ? 121.670 145.952 94.165  1.00 24.99 ?  125 VAL A C     1 
ATOM   1044  O  O     . VAL A 1 125 ? 122.518 146.760 94.557  1.00 32.24 ?  125 VAL A O     1 
ATOM   1045  C  CB    . VAL A 1 125 ? 121.661 143.635 95.205  1.00 30.99 ?  125 VAL A CB    1 
ATOM   1046  C  CG1   . VAL A 1 125 ? 123.141 143.790 95.481  1.00 30.65 ?  125 VAL A CG1   1 
ATOM   1047  C  CG2   . VAL A 1 125 ? 121.028 142.781 96.283  1.00 25.85 ?  125 VAL A CG2   1 
ATOM   1048  N  N     . ALA A 1 126 ? 121.318 145.869 92.880  1.00 23.57 ?  126 ALA A N     1 
ATOM   1049  C  CA    . ALA A 1 126 ? 121.904 146.765 91.885  1.00 22.17 ?  126 ALA A CA    1 
ATOM   1050  C  C     . ALA A 1 126 ? 121.505 148.214 92.133  1.00 29.36 ?  126 ALA A C     1 
ATOM   1051  O  O     . ALA A 1 126 ? 122.340 149.121 92.027  1.00 33.76 ?  126 ALA A O     1 
ATOM   1052  C  CB    . ALA A 1 126 ? 121.483 146.331 90.484  1.00 29.36 ?  126 ALA A CB    1 
ATOM   1053  N  N     . LEU A 1 127 ? 120.232 148.452 92.452  1.00 31.34 ?  127 LEU A N     1 
ATOM   1054  C  CA    . LEU A 1 127 ? 119.780 149.809 92.741  1.00 27.26 ?  127 LEU A CA    1 
ATOM   1055  C  C     . LEU A 1 127 ? 120.459 150.356 93.989  1.00 30.16 ?  127 LEU A C     1 
ATOM   1056  O  O     . LEU A 1 127 ? 120.792 151.545 94.054  1.00 36.11 ?  127 LEU A O     1 
ATOM   1057  C  CB    . LEU A 1 127 ? 118.260 149.833 92.897  1.00 32.59 ?  127 LEU A CB    1 
ATOM   1058  C  CG    . LEU A 1 127 ? 117.447 149.587 91.626  1.00 30.20 ?  127 LEU A CG    1 
ATOM   1059  C  CD1   . LEU A 1 127 ? 116.039 149.134 91.972  1.00 35.03 ?  127 LEU A CD1   1 
ATOM   1060  C  CD2   . LEU A 1 127 ? 117.411 150.831 90.756  1.00 31.61 ?  127 LEU A CD2   1 
ATOM   1061  N  N     . PHE A 1 128 ? 120.664 149.504 94.994  1.00 29.65 ?  128 PHE A N     1 
ATOM   1062  C  CA    . PHE A 1 128 ? 121.411 149.926 96.173  1.00 27.44 ?  128 PHE A CA    1 
ATOM   1063  C  C     . PHE A 1 128 ? 122.858 150.254 95.822  1.00 27.67 ?  128 PHE A C     1 
ATOM   1064  O  O     . PHE A 1 128 ? 123.416 151.239 96.318  1.00 39.06 ?  128 PHE A O     1 
ATOM   1065  C  CB    . PHE A 1 128 ? 121.349 148.840 97.246  1.00 27.29 ?  128 PHE A CB    1 
ATOM   1066  C  CG    . PHE A 1 128 ? 122.256 149.093 98.412  1.00 32.64 ?  128 PHE A CG    1 
ATOM   1067  C  CD1   . PHE A 1 128 ? 123.458 148.420 98.530  1.00 28.84 ?  128 PHE A CD1   1 
ATOM   1068  C  CD2   . PHE A 1 128 ? 121.900 149.999 99.395  1.00 32.00 ?  128 PHE A CD2   1 
ATOM   1069  C  CE1   . PHE A 1 128 ? 124.293 148.653 99.599  1.00 31.85 ?  128 PHE A CE1   1 
ATOM   1070  C  CE2   . PHE A 1 128 ? 122.731 150.234 100.471 1.00 35.22 ?  128 PHE A CE2   1 
ATOM   1071  C  CZ    . PHE A 1 128 ? 123.928 149.559 100.574 1.00 33.47 ?  128 PHE A CZ    1 
ATOM   1072  N  N     . PHE A 1 129 ? 123.479 149.434 94.971  1.00 24.44 ?  129 PHE A N     1 
ATOM   1073  C  CA    . PHE A 1 129 ? 124.868 149.657 94.584  1.00 22.14 ?  129 PHE A CA    1 
ATOM   1074  C  C     . PHE A 1 129 ? 125.035 150.972 93.833  1.00 28.86 ?  129 PHE A C     1 
ATOM   1075  O  O     . PHE A 1 129 ? 125.973 151.732 94.096  1.00 28.00 ?  129 PHE A O     1 
ATOM   1076  C  CB    . PHE A 1 129 ? 125.362 148.502 93.714  1.00 22.02 ?  129 PHE A CB    1 
ATOM   1077  C  CG    . PHE A 1 129 ? 125.749 147.276 94.482  1.00 23.96 ?  129 PHE A CG    1 
ATOM   1078  C  CD1   . PHE A 1 129 ? 125.931 147.321 95.851  1.00 24.20 ?  129 PHE A CD1   1 
ATOM   1079  C  CD2   . PHE A 1 129 ? 125.944 146.075 93.823  1.00 22.46 ?  129 PHE A CD2   1 
ATOM   1080  C  CE1   . PHE A 1 129 ? 126.290 146.187 96.548  1.00 24.48 ?  129 PHE A CE1   1 
ATOM   1081  C  CE2   . PHE A 1 129 ? 126.307 144.941 94.516  1.00 24.48 ?  129 PHE A CE2   1 
ATOM   1082  C  CZ    . PHE A 1 129 ? 126.481 144.996 95.880  1.00 26.83 ?  129 PHE A CZ    1 
ATOM   1083  N  N     . ALA A 1 130 ? 124.137 151.251 92.886  1.00 30.83 ?  130 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 130 ? 124.336 152.383 91.987  1.00 31.96 ?  130 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 130 ? 124.162 153.720 92.697  1.00 40.33 ?  130 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 130 ? 124.744 154.723 92.268  1.00 42.45 ?  130 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 130 ? 123.379 152.284 90.805  1.00 32.00 ?  130 ALA A CB    1 
ATOM   1088  N  N     . ASN A 1 131 ? 123.366 153.754 93.768  1.00 40.41 ?  131 ASN A N     1 
ATOM   1089  C  CA    . ASN A 1 131 ? 123.178 154.959 94.579  1.00 38.34 ?  131 ASN A CA    1 
ATOM   1090  C  C     . ASN A 1 131 ? 122.631 156.122 93.749  1.00 41.21 ?  131 ASN A C     1 
ATOM   1091  O  O     . ASN A 1 131 ? 123.033 157.274 93.922  1.00 46.33 ?  131 ASN A O     1 
ATOM   1092  C  CB    . ASN A 1 131 ? 124.479 155.359 95.281  1.00 34.85 ?  131 ASN A CB    1 
ATOM   1093  C  CG    . ASN A 1 131 ? 124.237 156.079 96.591  1.00 43.68 ?  131 ASN A CG    1 
ATOM   1094  O  OD1   . ASN A 1 131 ? 123.219 155.871 97.249  1.00 43.08 ?  131 ASN A OD1   1 
ATOM   1095  N  ND2   . ASN A 1 131 ? 125.178 156.933 96.978  1.00 44.19 ?  131 ASN A ND2   1 
ATOM   1096  N  N     . GLY A 1 132 ? 121.706 155.820 92.841  1.00 39.55 ?  132 GLY A N     1 
ATOM   1097  C  CA    . GLY A 1 132 ? 121.008 156.836 92.077  1.00 39.30 ?  132 GLY A CA    1 
ATOM   1098  C  C     . GLY A 1 132 ? 121.297 156.850 90.592  1.00 43.26 ?  132 GLY A C     1 
ATOM   1099  O  O     . GLY A 1 132 ? 120.644 157.611 89.865  1.00 45.37 ?  132 GLY A O     1 
ATOM   1100  N  N     . ASP A 1 133 ? 122.241 156.046 90.111  1.00 43.29 ?  133 ASP A N     1 
ATOM   1101  C  CA    . ASP A 1 133 ? 122.601 156.012 88.697  1.00 41.14 ?  133 ASP A CA    1 
ATOM   1102  C  C     . ASP A 1 133 ? 121.876 154.846 88.032  1.00 42.99 ?  133 ASP A C     1 
ATOM   1103  O  O     . ASP A 1 133 ? 122.188 153.681 88.297  1.00 47.06 ?  133 ASP A O     1 
ATOM   1104  C  CB    . ASP A 1 133 ? 124.113 155.890 88.528  1.00 43.53 ?  133 ASP A CB    1 
ATOM   1105  C  CG    . ASP A 1 133 ? 124.585 156.320 87.153  1.00 46.21 ?  133 ASP A CG    1 
ATOM   1106  O  OD1   . ASP A 1 133 ? 123.732 156.519 86.263  1.00 48.02 ?  133 ASP A OD1   1 
ATOM   1107  O  OD2   . ASP A 1 133 ? 125.812 156.455 86.962  1.00 46.08 -1 133 ASP A OD2   1 
ATOM   1108  N  N     . THR A 1 134 ? 120.911 155.160 87.165  1.00 45.97 ?  134 THR A N     1 
ATOM   1109  C  CA    . THR A 1 134 ? 120.132 154.108 86.518  1.00 41.92 ?  134 THR A CA    1 
ATOM   1110  C  C     . THR A 1 134 ? 120.994 153.264 85.583  1.00 43.76 ?  134 THR A C     1 
ATOM   1111  O  O     . THR A 1 134 ? 120.836 152.040 85.525  1.00 44.74 ?  134 THR A O     1 
ATOM   1112  C  CB    . THR A 1 134 ? 118.945 154.715 85.766  1.00 45.87 ?  134 THR A CB    1 
ATOM   1113  O  OG1   . THR A 1 134 ? 118.310 153.705 84.972  1.00 48.16 ?  134 THR A OG1   1 
ATOM   1114  C  CG2   . THR A 1 134 ? 119.391 155.867 84.872  1.00 46.73 ?  134 THR A CG2   1 
ATOM   1115  N  N     . GLU A 1 135 ? 121.908 153.896 84.841  1.00 42.46 ?  135 GLU A N     1 
ATOM   1116  C  CA    . GLU A 1 135 ? 122.789 153.136 83.958  1.00 43.05 ?  135 GLU A CA    1 
ATOM   1117  C  C     . GLU A 1 135 ? 123.738 152.250 84.754  1.00 43.92 ?  135 GLU A C     1 
ATOM   1118  O  O     . GLU A 1 135 ? 123.978 151.096 84.382  1.00 43.52 ?  135 GLU A O     1 
ATOM   1119  C  CB    . GLU A 1 135 ? 123.570 154.086 83.051  1.00 43.57 ?  135 GLU A CB    1 
ATOM   1120  C  CG    . GLU A 1 135 ? 122.758 154.645 81.893  1.00 44.06 ?  135 GLU A CG    1 
ATOM   1121  C  CD    . GLU A 1 135 ? 121.630 153.723 81.471  1.00 47.86 ?  135 GLU A CD    1 
ATOM   1122  O  OE1   . GLU A 1 135 ? 121.897 152.763 80.720  1.00 47.89 ?  135 GLU A OE1   1 
ATOM   1123  O  OE2   . GLU A 1 135 ? 120.475 153.963 81.883  1.00 48.27 -1 135 GLU A OE2   1 
ATOM   1124  N  N     . LYS A 1 136 ? 124.283 152.770 85.854  1.00 35.81 ?  136 LYS A N     1 
ATOM   1125  C  CA    . LYS A 1 136 ? 125.124 151.952 86.721  1.00 32.22 ?  136 LYS A CA    1 
ATOM   1126  C  C     . LYS A 1 136 ? 124.324 150.810 87.336  1.00 33.99 ?  136 LYS A C     1 
ATOM   1127  O  O     . LYS A 1 136 ? 124.835 149.694 87.487  1.00 39.30 ?  136 LYS A O     1 
ATOM   1128  C  CB    . LYS A 1 136 ? 125.751 152.824 87.809  1.00 38.68 ?  136 LYS A CB    1 
ATOM   1129  C  CG    . LYS A 1 136 ? 126.827 152.137 88.626  1.00 37.05 ?  136 LYS A CG    1 
ATOM   1130  C  CD    . LYS A 1 136 ? 128.184 152.237 87.955  1.00 36.18 ?  136 LYS A CD    1 
ATOM   1131  C  CE    . LYS A 1 136 ? 129.298 151.890 88.927  1.00 38.80 ?  136 LYS A CE    1 
ATOM   1132  N  NZ    . LYS A 1 136 ? 130.642 152.186 88.360  1.00 39.04 1  136 LYS A NZ    1 
ATOM   1133  N  N     . ALA A 1 137 ? 123.066 151.071 87.698  1.00 33.83 ?  137 ALA A N     1 
ATOM   1134  C  CA    . ALA A 1 137 ? 122.212 150.013 88.227  1.00 30.50 ?  137 ALA A CA    1 
ATOM   1135  C  C     . ALA A 1 137 ? 121.972 148.928 87.186  1.00 31.42 ?  137 ALA A C     1 
ATOM   1136  O  O     . ALA A 1 137 ? 121.978 147.736 87.510  1.00 33.06 ?  137 ALA A O     1 
ATOM   1137  C  CB    . ALA A 1 137 ? 120.885 150.599 88.707  1.00 29.01 ?  137 ALA A CB    1 
ATOM   1138  N  N     . LYS A 1 138 ? 121.754 149.320 85.929  1.00 35.80 ?  138 LYS A N     1 
ATOM   1139  C  CA    . LYS A 1 138 ? 121.577 148.331 84.871  1.00 34.99 ?  138 LYS A CA    1 
ATOM   1140  C  C     . LYS A 1 138 ? 122.861 147.546 84.627  1.00 31.55 ?  138 LYS A C     1 
ATOM   1141  O  O     . LYS A 1 138 ? 122.816 146.345 84.340  1.00 33.93 ?  138 LYS A O     1 
ATOM   1142  C  CB    . LYS A 1 138 ? 121.106 149.010 83.586  1.00 39.13 ?  138 LYS A CB    1 
ATOM   1143  C  CG    . LYS A 1 138 ? 119.662 149.478 83.630  1.00 39.27 ?  138 LYS A CG    1 
ATOM   1144  C  CD    . LYS A 1 138 ? 119.443 150.680 82.729  1.00 37.78 ?  138 LYS A CD    1 
ATOM   1145  C  CE    . LYS A 1 138 ? 119.118 150.249 81.308  1.00 37.18 ?  138 LYS A CE    1 
ATOM   1146  N  NZ    . LYS A 1 138 ? 119.202 151.387 80.353  1.00 39.98 1  138 LYS A NZ    1 
ATOM   1147  N  N     . GLU A 1 139 ? 124.015 148.210 84.735  1.00 36.22 ?  139 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 139 ? 125.286 147.497 84.622  1.00 32.63 ?  139 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 139 ? 125.440 146.470 85.737  1.00 32.19 ?  139 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 139 ? 125.877 145.340 85.494  1.00 40.53 ?  139 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 139 ? 126.451 148.485 84.645  1.00 33.71 ?  139 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 139 ? 126.516 149.406 83.442  1.00 36.98 ?  139 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 139 ? 127.690 150.360 83.507  1.00 45.18 ?  139 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 139 ? 128.787 149.925 83.914  1.00 43.35 ?  139 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 139 ? 127.517 151.545 83.151  1.00 41.43 -1 139 GLU A OE2   1 
ATOM   1156  N  N     . TYR A 1 140 ? 125.081 146.843 86.967  1.00 23.52 ?  140 TYR A N     1 
ATOM   1157  C  CA    . TYR A 1 140 ? 125.137 145.896 88.076  1.00 27.69 ?  140 TYR A CA    1 
ATOM   1158  C  C     . TYR A 1 140 ? 124.163 144.743 87.867  1.00 28.10 ?  140 TYR A C     1 
ATOM   1159  O  O     . TYR A 1 140 ? 124.471 143.591 88.195  1.00 33.30 ?  140 TYR A O     1 
ATOM   1160  C  CB    . TYR A 1 140 ? 124.838 146.607 89.394  1.00 28.73 ?  140 TYR A CB    1 
ATOM   1161  C  CG    . TYR A 1 140 ? 125.991 147.398 89.957  1.00 30.16 ?  140 TYR A CG    1 
ATOM   1162  C  CD1   . TYR A 1 140 ? 127.212 146.794 90.216  1.00 28.80 ?  140 TYR A CD1   1 
ATOM   1163  C  CD2   . TYR A 1 140 ? 125.853 148.747 90.242  1.00 30.41 ?  140 TYR A CD2   1 
ATOM   1164  C  CE1   . TYR A 1 140 ? 128.266 147.515 90.734  1.00 29.52 ?  140 TYR A CE1   1 
ATOM   1165  C  CE2   . TYR A 1 140 ? 126.899 149.475 90.762  1.00 30.02 ?  140 TYR A CE2   1 
ATOM   1166  C  CZ    . TYR A 1 140 ? 128.102 148.856 91.006  1.00 25.73 ?  140 TYR A CZ    1 
ATOM   1167  O  OH    . TYR A 1 140 ? 129.142 149.586 91.524  1.00 31.30 ?  140 TYR A OH    1 
ATOM   1168  N  N     . VAL A 1 141 ? 122.973 145.041 87.344  1.00 32.97 ?  141 VAL A N     1 
ATOM   1169  C  CA    . VAL A 1 141 ? 121.988 143.997 87.078  1.00 30.44 ?  141 VAL A CA    1 
ATOM   1170  C  C     . VAL A 1 141 ? 122.514 143.024 86.032  1.00 29.32 ?  141 VAL A C     1 
ATOM   1171  O  O     . VAL A 1 141 ? 122.358 141.806 86.167  1.00 34.54 ?  141 VAL A O     1 
ATOM   1172  C  CB    . VAL A 1 141 ? 120.645 144.624 86.661  1.00 32.31 ?  141 VAL A CB    1 
ATOM   1173  C  CG1   . VAL A 1 141 ? 120.020 143.863 85.507  1.00 28.92 ?  141 VAL A CG1   1 
ATOM   1174  C  CG2   . VAL A 1 141 ? 119.693 144.645 87.839  1.00 32.26 ?  141 VAL A CG2   1 
ATOM   1175  N  N     . ASN A 1 142 ? 123.142 143.542 84.975  1.00 27.50 ?  142 ASN A N     1 
ATOM   1176  C  CA    . ASN A 1 142 ? 123.723 142.661 83.967  1.00 29.40 ?  142 ASN A CA    1 
ATOM   1177  C  C     . ASN A 1 142 ? 124.895 141.869 84.531  1.00 29.06 ?  142 ASN A C     1 
ATOM   1178  O  O     . ASN A 1 142 ? 125.126 140.728 84.116  1.00 36.97 ?  142 ASN A O     1 
ATOM   1179  C  CB    . ASN A 1 142 ? 124.165 143.472 82.752  1.00 29.77 ?  142 ASN A CB    1 
ATOM   1180  C  CG    . ASN A 1 142 ? 123.001 143.903 81.888  1.00 32.97 ?  142 ASN A CG    1 
ATOM   1181  O  OD1   . ASN A 1 142 ? 122.052 143.146 81.682  1.00 32.44 ?  142 ASN A OD1   1 
ATOM   1182  N  ND2   . ASN A 1 142 ? 123.064 145.126 81.375  1.00 33.88 ?  142 ASN A ND2   1 
ATOM   1183  N  N     . LEU A 1 143 ? 125.641 142.455 85.467  1.00 28.20 ?  143 LEU A N     1 
ATOM   1184  C  CA    . LEU A 1 143 ? 126.747 141.744 86.095  1.00 25.80 ?  143 LEU A CA    1 
ATOM   1185  C  C     . LEU A 1 143 ? 126.254 140.579 86.944  1.00 25.05 ?  143 LEU A C     1 
ATOM   1186  O  O     . LEU A 1 143 ? 126.820 139.481 86.892  1.00 28.27 ?  143 LEU A O     1 
ATOM   1187  C  CB    . LEU A 1 143 ? 127.564 142.714 86.944  1.00 23.48 ?  143 LEU A CB    1 
ATOM   1188  C  CG    . LEU A 1 143 ? 128.997 142.312 87.280  1.00 28.00 ?  143 LEU A CG    1 
ATOM   1189  C  CD1   . LEU A 1 143 ? 129.857 142.376 86.036  1.00 28.70 ?  143 LEU A CD1   1 
ATOM   1190  C  CD2   . LEU A 1 143 ? 129.548 143.216 88.365  1.00 29.39 ?  143 LEU A CD2   1 
ATOM   1191  N  N     . MET A 1 144 ? 125.207 140.801 87.735  1.00 28.78 ?  144 MET A N     1 
ATOM   1192  C  CA    . MET A 1 144 ? 124.720 139.781 88.658  1.00 23.13 ?  144 MET A CA    1 
ATOM   1193  C  C     . MET A 1 144 ? 123.785 138.769 88.009  1.00 25.40 ?  144 MET A C     1 
ATOM   1194  O  O     . MET A 1 144 ? 123.715 137.625 88.473  1.00 29.77 ?  144 MET A O     1 
ATOM   1195  C  CB    . MET A 1 144 ? 124.014 140.440 89.843  1.00 23.68 ?  144 MET A CB    1 
ATOM   1196  C  CG    . MET A 1 144 ? 124.840 141.508 90.528  1.00 26.24 ?  144 MET A CG    1 
ATOM   1197  S  SD    . MET A 1 144 ? 124.276 141.852 92.199  1.00 33.43 ?  144 MET A SD    1 
ATOM   1198  C  CE    . MET A 1 144 ? 123.616 143.497 91.965  1.00 28.66 ?  144 MET A CE    1 
ATOM   1199  N  N     . ILE A 1 145 ? 123.064 139.152 86.958  1.00 29.37 ?  145 ILE A N     1 
ATOM   1200  C  CA    . ILE A 1 145 ? 122.194 138.208 86.271  1.00 28.87 ?  145 ILE A CA    1 
ATOM   1201  C  C     . ILE A 1 145 ? 122.982 137.338 85.294  1.00 31.49 ?  145 ILE A C     1 
ATOM   1202  O  O     . ILE A 1 145 ? 122.576 136.207 85.010  1.00 35.53 ?  145 ILE A O     1 
ATOM   1203  C  CB    . ILE A 1 145 ? 121.038 138.945 85.568  1.00 27.96 ?  145 ILE A CB    1 
ATOM   1204  C  CG1   . ILE A 1 145 ? 119.809 138.040 85.467  1.00 30.70 ?  145 ILE A CG1   1 
ATOM   1205  C  CG2   . ILE A 1 145 ? 121.452 139.444 84.189  1.00 32.52 ?  145 ILE A CG2   1 
ATOM   1206  C  CD1   . ILE A 1 145 ? 119.238 137.626 86.802  1.00 28.51 ?  145 ILE A CD1   1 
ATOM   1207  N  N     . ASN A 1 146 ? 124.106 137.840 84.779  1.00 23.60 ?  146 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 146 ? 125.080 136.977 84.127  1.00 26.02 ?  146 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 146 ? 125.859 136.149 85.135  1.00 25.75 ?  146 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 146 ? 126.614 135.258 84.731  1.00 30.46 ?  146 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 146 ? 126.049 137.806 83.282  1.00 25.53 ?  146 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 146 ? 125.383 138.428 82.073  1.00 30.32 ?  146 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 146 ? 124.294 138.023 81.673  1.00 35.31 ?  146 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 146 ? 126.039 139.421 81.483  1.00 30.38 ?  146 ASN A ND2   1 
ATOM   1215  N  N     . GLN A 1 147 ? 125.692 136.435 86.427  1.00 23.38 ?  147 GLN A N     1 
ATOM   1216  C  CA    . GLN A 1 147 ? 126.355 135.712 87.509  1.00 20.38 ?  147 GLN A CA    1 
ATOM   1217  C  C     . GLN A 1 147 ? 127.873 135.791 87.377  1.00 26.35 ?  147 GLN A C     1 
ATOM   1218  O  O     . GLN A 1 147 ? 128.593 134.858 87.733  1.00 35.68 ?  147 GLN A O     1 
ATOM   1219  C  CB    . GLN A 1 147 ? 125.880 134.260 87.579  1.00 24.70 ?  147 GLN A CB    1 
ATOM   1220  C  CG    . GLN A 1 147 ? 124.461 134.111 88.101  1.00 23.57 ?  147 GLN A CG    1 
ATOM   1221  C  CD    . GLN A 1 147 ? 124.200 132.745 88.696  1.00 26.46 ?  147 GLN A CD    1 
ATOM   1222  O  OE1   . GLN A 1 147 ? 123.510 132.617 89.707  1.00 28.11 ?  147 GLN A OE1   1 
ATOM   1223  N  NE2   . GLN A 1 147 ? 124.752 131.713 88.071  1.00 35.92 ?  147 GLN A NE2   1 
ATOM   1224  N  N     . GLU A 1 148 ? 128.361 136.917 86.856  1.00 25.21 ?  148 GLU A N     1 
ATOM   1225  C  CA    . GLU A 1 148 ? 129.798 137.153 86.807  1.00 22.94 ?  148 GLU A CA    1 
ATOM   1226  C  C     . GLU A 1 148 ? 130.337 137.564 88.170  1.00 24.69 ?  148 GLU A C     1 
ATOM   1227  O  O     . GLU A 1 148 ? 131.435 137.152 88.559  1.00 29.83 ?  148 GLU A O     1 
ATOM   1228  C  CB    . GLU A 1 148 ? 130.119 138.223 85.763  1.00 20.80 ?  148 GLU A CB    1 
ATOM   1229  C  CG    . GLU A 1 148 ? 129.681 137.865 84.355  1.00 24.20 ?  148 GLU A CG    1 
ATOM   1230  C  CD    . GLU A 1 148 ? 129.669 139.063 83.429  1.00 33.09 ?  148 GLU A CD    1 
ATOM   1231  O  OE1   . GLU A 1 148 ? 128.695 139.843 83.477  1.00 36.31 ?  148 GLU A OE1   1 
ATOM   1232  O  OE2   . GLU A 1 148 ? 130.633 139.227 82.654  1.00 36.13 -1 148 GLU A OE2   1 
ATOM   1233  N  N     . TYR A 1 149 ? 129.578 138.367 88.907  1.00 18.43 ?  149 TYR A N     1 
ATOM   1234  C  CA    . TYR A 1 149 ? 129.965 138.816 90.235  1.00 20.58 ?  149 TYR A CA    1 
ATOM   1235  C  C     . TYR A 1 149 ? 128.842 138.514 91.212  1.00 22.59 ?  149 TYR A C     1 
ATOM   1236  O  O     . TYR A 1 149 ? 127.661 138.630 90.872  1.00 30.54 ?  149 TYR A O     1 
ATOM   1237  C  CB    . TYR A 1 149 ? 130.285 140.311 90.246  1.00 22.04 ?  149 TYR A CB    1 
ATOM   1238  C  CG    . TYR A 1 149 ? 130.417 140.900 91.630  1.00 21.96 ?  149 TYR A CG    1 
ATOM   1239  C  CD1   . TYR A 1 149 ? 131.448 140.514 92.475  1.00 17.07 ?  149 TYR A CD1   1 
ATOM   1240  C  CD2   . TYR A 1 149 ? 129.508 141.843 92.093  1.00 19.77 ?  149 TYR A CD2   1 
ATOM   1241  C  CE1   . TYR A 1 149 ? 131.570 141.052 93.741  1.00 22.13 ?  149 TYR A CE1   1 
ATOM   1242  C  CE2   . TYR A 1 149 ? 129.623 142.385 93.355  1.00 17.50 ?  149 TYR A CE2   1 
ATOM   1243  C  CZ    . TYR A 1 149 ? 130.656 141.986 94.175  1.00 19.19 ?  149 TYR A CZ    1 
ATOM   1244  O  OH    . TYR A 1 149 ? 130.774 142.523 95.435  1.00 20.73 ?  149 TYR A OH    1 
ATOM   1245  N  N     . GLN A 1 150 ? 129.216 138.125 92.423  1.00 19.43 ?  150 GLN A N     1 
ATOM   1246  C  CA    . GLN A 1 150 ? 128.263 137.790 93.475  1.00 14.05 ?  150 GLN A CA    1 
ATOM   1247  C  C     . GLN A 1 150 ? 128.646 138.562 94.727  1.00 17.22 ?  150 GLN A C     1 
ATOM   1248  O  O     . GLN A 1 150 ? 129.738 138.326 95.284  1.00 18.47 ?  150 GLN A O     1 
ATOM   1249  C  CB    . GLN A 1 150 ? 128.251 136.286 93.733  1.00 19.49 ?  150 GLN A CB    1 
ATOM   1250  C  CG    . GLN A 1 150 ? 127.458 135.849 94.949  1.00 20.50 ?  150 GLN A CG    1 
ATOM   1251  C  CD    . GLN A 1 150 ? 126.022 136.326 94.914  1.00 17.04 ?  150 GLN A CD    1 
ATOM   1252  O  OE1   . GLN A 1 150 ? 125.236 135.907 94.065  1.00 22.92 ?  150 GLN A OE1   1 
ATOM   1253  N  NE2   . GLN A 1 150 ? 125.670 137.205 95.842  1.00 19.47 ?  150 GLN A NE2   1 
ATOM   1254  N  N     . PRO A 1 151 ? 127.819 139.501 95.181  1.00 24.37 ?  151 PRO A N     1 
ATOM   1255  C  CA    . PRO A 1 151 ? 128.053 140.102 96.496  1.00 10.14 ?  151 PRO A CA    1 
ATOM   1256  C  C     . PRO A 1 151 ? 127.959 139.041 97.580  1.00 13.12 ?  151 PRO A C     1 
ATOM   1257  O  O     . PRO A 1 151 ? 127.256 138.039 97.438  1.00 25.36 ?  151 PRO A O     1 
ATOM   1258  C  CB    . PRO A 1 151 ? 126.931 141.140 96.622  1.00 19.55 ?  151 PRO A CB    1 
ATOM   1259  C  CG    . PRO A 1 151 ? 126.485 141.400 95.222  1.00 19.21 ?  151 PRO A CG    1 
ATOM   1260  C  CD    . PRO A 1 151 ? 126.676 140.112 94.485  1.00 19.61 ?  151 PRO A CD    1 
ATOM   1261  N  N     . SER A 1 152 ? 128.695 139.264 98.665  1.00 23.35 ?  152 SER A N     1 
ATOM   1262  C  CA    . SER A 1 152 ? 128.732 138.301 99.752  1.00 19.59 ?  152 SER A CA    1 
ATOM   1263  C  C     . SER A 1 152 ? 127.335 138.088 100.331 1.00 22.03 ?  152 SER A C     1 
ATOM   1264  O  O     . SER A 1 152 ? 126.394 138.837 100.062 1.00 27.11 ?  152 SER A O     1 
ATOM   1265  C  CB    . SER A 1 152 ? 129.689 138.770 100.844 1.00 19.84 ?  152 SER A CB    1 
ATOM   1266  O  OG    . SER A 1 152 ? 129.226 139.967 101.440 1.00 23.90 ?  152 SER A OG    1 
ATOM   1267  N  N     . THR A 1 153 ? 127.212 137.037 101.140 1.00 26.99 ?  153 THR A N     1 
ATOM   1268  C  CA    . THR A 1 153 ? 125.941 136.746 101.795 1.00 21.18 ?  153 THR A CA    1 
ATOM   1269  C  C     . THR A 1 153 ? 125.373 137.936 102.563 1.00 30.64 ?  153 THR A C     1 
ATOM   1270  O  O     . THR A 1 153 ? 124.170 138.209 102.406 1.00 32.29 ?  153 THR A O     1 
ATOM   1271  C  CB    . THR A 1 153 ? 126.102 135.525 102.715 1.00 26.27 ?  153 THR A CB    1 
ATOM   1272  O  OG1   . THR A 1 153 ? 126.254 134.342 101.921 1.00 31.38 ?  153 THR A OG1   1 
ATOM   1273  C  CG2   . THR A 1 153 ? 124.891 135.368 103.624 1.00 25.56 ?  153 THR A CG2   1 
ATOM   1274  N  N     . PRO A 1 154 ? 126.142 138.682 103.367 1.00 28.10 ?  154 PRO A N     1 
ATOM   1275  C  CA    . PRO A 1 154 ? 125.558 139.884 103.993 1.00 20.25 ?  154 PRO A CA    1 
ATOM   1276  C  C     . PRO A 1 154 ? 125.058 140.899 102.981 1.00 20.45 ?  154 PRO A C     1 
ATOM   1277  O  O     . PRO A 1 154 ? 123.912 141.357 103.077 1.00 28.25 ?  154 PRO A O     1 
ATOM   1278  C  CB    . PRO A 1 154 ? 126.718 140.438 104.830 1.00 22.33 ?  154 PRO A CB    1 
ATOM   1279  C  CG    . PRO A 1 154 ? 127.616 139.297 105.044 1.00 18.21 ?  154 PRO A CG    1 
ATOM   1280  C  CD    . PRO A 1 154 ? 127.522 138.451 103.830 1.00 19.76 ?  154 PRO A CD    1 
ATOM   1281  N  N     . THR A 1 155 ? 125.891 141.261 102.004 1.00 21.90 ?  155 THR A N     1 
ATOM   1282  C  CA    . THR A 1 155 ? 125.487 142.254 101.014 1.00 22.24 ?  155 THR A CA    1 
ATOM   1283  C  C     . THR A 1 155 ? 124.319 141.750 100.175 1.00 24.01 ?  155 THR A C     1 
ATOM   1284  O  O     . THR A 1 155 ? 123.322 142.455 99.994  1.00 25.79 ?  155 THR A O     1 
ATOM   1285  C  CB    . THR A 1 155 ? 126.672 142.616 100.119 1.00 20.44 ?  155 THR A CB    1 
ATOM   1286  O  OG1   . THR A 1 155 ? 127.808 142.933 100.933 1.00 26.23 ?  155 THR A OG1   1 
ATOM   1287  C  CG2   . THR A 1 155 ? 126.330 143.812 99.251  1.00 15.83 ?  155 THR A CG2   1 
ATOM   1288  N  N     . PHE A 1 156 ? 124.421 140.523 99.662  1.00 26.18 ?  156 PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 156 ? 123.371 140.000 98.793  1.00 22.55 ?  156 PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 156 ? 122.049 139.863 99.538  1.00 29.74 ?  156 PHE A C     1 
ATOM   1291  O  O     . PHE A 1 156 ? 120.983 140.165 98.987  1.00 25.60 ?  156 PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 156 ? 123.795 138.655 98.207  1.00 21.93 ?  156 PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 156 ? 122.975 138.225 97.027  1.00 27.63 ?  156 PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 156 ? 122.859 139.042 95.916  1.00 24.70 ?  156 PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 156 ? 122.320 137.006 97.029  1.00 23.84 ?  156 PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 156 ? 122.106 138.651 94.828  1.00 24.94 ?  156 PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 156 ? 121.566 136.610 95.944  1.00 25.17 ?  156 PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 156 ? 121.458 137.433 94.843  1.00 29.02 ?  156 PHE A CZ    1 
ATOM   1299  N  N     . LEU A 1 157 ? 122.095 139.406 100.788 1.00 29.89 ?  157 LEU A N     1 
ATOM   1300  C  CA    . LEU A 1 157 ? 120.873 139.171 101.548 1.00 24.18 ?  157 LEU A CA    1 
ATOM   1301  C  C     . LEU A 1 157 ? 120.250 140.468 102.054 1.00 27.71 ?  157 LEU A C     1 
ATOM   1302  O  O     . LEU A 1 157 ? 119.023 140.609 102.045 1.00 38.07 ?  157 LEU A O     1 
ATOM   1303  C  CB    . LEU A 1 157 ? 121.168 138.229 102.716 1.00 29.60 ?  157 LEU A CB    1 
ATOM   1304  C  CG    . LEU A 1 157 ? 120.100 138.097 103.801 1.00 30.16 ?  157 LEU A CG    1 
ATOM   1305  C  CD1   . LEU A 1 157 ? 119.047 137.089 103.391 1.00 31.34 ?  157 LEU A CD1   1 
ATOM   1306  C  CD2   . LEU A 1 157 ? 120.734 137.702 105.125 1.00 25.42 ?  157 LEU A CD2   1 
ATOM   1307  N  N     . ASN A 1 158 ? 121.068 141.426 102.487 1.00 29.43 ?  158 ASN A N     1 
ATOM   1308  C  CA    . ASN A 1 158 ? 120.569 142.559 103.252 1.00 28.29 ?  158 ASN A CA    1 
ATOM   1309  C  C     . ASN A 1 158 ? 120.499 143.863 102.468 1.00 29.21 ?  158 ASN A C     1 
ATOM   1310  O  O     . ASN A 1 158 ? 119.907 144.824 102.967 1.00 35.75 ?  158 ASN A O     1 
ATOM   1311  C  CB    . ASN A 1 158 ? 121.439 142.769 104.496 1.00 28.05 ?  158 ASN A CB    1 
ATOM   1312  C  CG    . ASN A 1 158 ? 121.353 141.614 105.469 1.00 33.65 ?  158 ASN A CG    1 
ATOM   1313  O  OD1   . ASN A 1 158 ? 120.268 141.117 105.765 1.00 37.04 ?  158 ASN A OD1   1 
ATOM   1314  N  ND2   . ASN A 1 158 ? 122.502 141.174 105.965 1.00 34.74 ?  158 ASN A ND2   1 
ATOM   1315  N  N     . ALA A 1 159 ? 121.080 143.932 101.273 1.00 27.74 ?  159 ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 159 ? 121.085 145.188 100.531 1.00 27.63 ?  159 ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 159 ? 119.662 145.608 100.191 1.00 33.43 ?  159 ALA A C     1 
ATOM   1318  O  O     . ALA A 1 159 ? 118.908 144.847 99.578  1.00 39.61 ?  159 ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 159 ? 121.916 145.058 99.257  1.00 29.21 ?  159 ALA A CB    1 
ATOM   1320  N  N     . GLY A 1 160 ? 119.299 146.823 100.593 1.00 36.32 ?  160 GLY A N     1 
ATOM   1321  C  CA    . GLY A 1 160 ? 117.987 147.360 100.317 1.00 36.92 ?  160 GLY A CA    1 
ATOM   1322  C  C     . GLY A 1 160 ? 116.891 146.925 101.263 1.00 39.04 ?  160 GLY A C     1 
ATOM   1323  O  O     . GLY A 1 160 ? 115.727 147.262 101.023 1.00 44.26 ?  160 GLY A O     1 
ATOM   1324  N  N     . ARG A 1 161 ? 117.215 146.194 102.325 1.00 41.42 ?  161 ARG A N     1 
ATOM   1325  C  CA    . ARG A 1 161 ? 116.222 145.695 103.268 1.00 41.58 ?  161 ARG A CA    1 
ATOM   1326  C  C     . ARG A 1 161 ? 116.289 146.493 104.563 1.00 43.09 ?  161 ARG A C     1 
ATOM   1327  O  O     . ARG A 1 161 ? 117.378 146.731 105.093 1.00 45.61 ?  161 ARG A O     1 
ATOM   1328  C  CB    . ARG A 1 161 ? 116.443 144.209 103.555 1.00 37.99 ?  161 ARG A CB    1 
ATOM   1329  C  CG    . ARG A 1 161 ? 116.162 143.300 102.374 1.00 40.07 ?  161 ARG A CG    1 
ATOM   1330  C  CD    . ARG A 1 161 ? 115.988 141.860 102.823 1.00 39.67 ?  161 ARG A CD    1 
ATOM   1331  N  NE    . ARG A 1 161 ? 116.007 140.933 101.698 1.00 42.62 ?  161 ARG A NE    1 
ATOM   1332  C  CZ    . ARG A 1 161 ? 116.101 139.616 101.816 1.00 43.82 ?  161 ARG A CZ    1 
ATOM   1333  N  NH1   . ARG A 1 161 ? 116.174 139.031 103.000 1.00 39.86 1  161 ARG A NH1   1 
ATOM   1334  N  NH2   . ARG A 1 161 ? 116.123 138.867 100.718 1.00 43.40 ?  161 ARG A NH2   1 
ATOM   1335  N  N     . LYS A 1 162 ? 115.123 146.907 105.066 1.00 48.38 ?  162 LYS A N     1 
ATOM   1336  C  CA    . LYS A 1 162 ? 115.085 147.664 106.314 1.00 50.04 ?  162 LYS A CA    1 
ATOM   1337  C  C     . LYS A 1 162 ? 115.395 146.772 107.511 1.00 49.96 ?  162 LYS A C     1 
ATOM   1338  O  O     . LYS A 1 162 ? 116.177 147.146 108.392 1.00 51.28 ?  162 LYS A O     1 
ATOM   1339  C  CB    . LYS A 1 162 ? 113.723 148.339 106.480 1.00 49.53 ?  162 LYS A CB    1 
ATOM   1340  C  CG    . LYS A 1 162 ? 113.676 149.361 107.605 1.00 48.91 ?  162 LYS A CG    1 
ATOM   1341  C  CD    . LYS A 1 162 ? 113.070 150.678 107.144 1.00 49.75 ?  162 LYS A CD    1 
ATOM   1342  C  CE    . LYS A 1 162 ? 111.686 150.475 106.554 1.00 52.02 ?  162 LYS A CE    1 
ATOM   1343  N  NZ    . LYS A 1 162 ? 111.398 151.446 105.462 1.00 52.03 1  162 LYS A NZ    1 
ATOM   1344  N  N     . ARG A 1 163 ? 114.788 145.588 107.560 1.00 49.65 ?  163 ARG A N     1 
ATOM   1345  C  CA    . ARG A 1 163 ? 115.054 144.618 108.622 1.00 51.16 ?  163 ARG A CA    1 
ATOM   1346  C  C     . ARG A 1 163 ? 116.272 143.809 108.202 1.00 52.31 ?  163 ARG A C     1 
ATOM   1347  O  O     . ARG A 1 163 ? 116.165 142.779 107.534 1.00 53.52 ?  163 ARG A O     1 
ATOM   1348  C  CB    . ARG A 1 163 ? 113.836 143.732 108.862 1.00 53.63 ?  163 ARG A CB    1 
ATOM   1349  C  CG    . ARG A 1 163 ? 113.611 143.341 110.317 1.00 52.96 ?  163 ARG A CG    1 
ATOM   1350  C  CD    . ARG A 1 163 ? 114.677 142.383 110.828 1.00 52.96 ?  163 ARG A CD    1 
ATOM   1351  N  NE    . ARG A 1 163 ? 114.942 141.300 109.888 1.00 53.32 ?  163 ARG A NE    1 
ATOM   1352  C  CZ    . ARG A 1 163 ? 116.110 140.683 109.767 1.00 53.85 ?  163 ARG A CZ    1 
ATOM   1353  N  NH1   . ARG A 1 163 ? 117.149 141.021 110.512 1.00 53.22 1  163 ARG A NH1   1 
ATOM   1354  N  NH2   . ARG A 1 163 ? 116.237 139.705 108.876 1.00 52.27 ?  163 ARG A NH2   1 
ATOM   1355  N  N     . ARG A 1 164 ? 117.451 144.283 108.597 1.00 50.24 ?  164 ARG A N     1 
ATOM   1356  C  CA    . ARG A 1 164 ? 118.694 143.715 108.102 1.00 50.56 ?  164 ARG A CA    1 
ATOM   1357  C  C     . ARG A 1 164 ? 119.799 143.910 109.128 1.00 49.30 ?  164 ARG A C     1 
ATOM   1358  O  O     . ARG A 1 164 ? 119.717 144.766 110.011 1.00 50.46 ?  164 ARG A O     1 
ATOM   1359  C  CB    . ARG A 1 164 ? 119.108 144.355 106.774 1.00 46.90 ?  164 ARG A CB    1 
ATOM   1360  C  CG    . ARG A 1 164 ? 119.735 145.733 106.941 1.00 43.57 ?  164 ARG A CG    1 
ATOM   1361  C  CD    . ARG A 1 164 ? 120.523 146.141 105.710 1.00 46.79 ?  164 ARG A CD    1 
ATOM   1362  N  NE    . ARG A 1 164 ? 121.030 147.505 105.797 1.00 46.54 ?  164 ARG A NE    1 
ATOM   1363  C  CZ    . ARG A 1 164 ? 122.078 147.873 106.521 1.00 49.60 ?  164 ARG A CZ    1 
ATOM   1364  N  NH1   . ARG A 1 164 ? 122.758 147.001 107.246 1.00 48.82 1  164 ARG A NH1   1 
ATOM   1365  N  NH2   . ARG A 1 164 ? 122.455 149.148 106.515 1.00 47.91 ?  164 ARG A NH2   1 
ATOM   1366  N  N     . GLY A 1 165 ? 120.840 143.090 108.997 1.00 43.35 ?  165 GLY A N     1 
ATOM   1367  C  CA    . GLY A 1 165 ? 122.092 143.316 109.682 1.00 42.46 ?  165 GLY A CA    1 
ATOM   1368  C  C     . GLY A 1 165 ? 123.026 144.166 108.843 1.00 45.44 ?  165 GLY A C     1 
ATOM   1369  O  O     . GLY A 1 165 ? 122.660 144.703 107.796 1.00 46.28 ?  165 GLY A O     1 
ATOM   1370  N  N     . GLU A 1 166 ? 124.261 144.285 109.317 1.00 39.87 ?  166 GLU A N     1 
ATOM   1371  C  CA    . GLU A 1 166 ? 125.249 145.038 108.564 1.00 37.89 ?  166 GLU A CA    1 
ATOM   1372  C  C     . GLU A 1 166 ? 125.685 144.259 107.325 1.00 38.58 ?  166 GLU A C     1 
ATOM   1373  O  O     . GLU A 1 166 ? 125.627 143.028 107.275 1.00 36.64 ?  166 GLU A O     1 
ATOM   1374  C  CB    . GLU A 1 166 ? 126.461 145.367 109.437 1.00 35.65 ?  166 GLU A CB    1 
ATOM   1375  C  CG    . GLU A 1 166 ? 126.490 146.801 109.953 1.00 38.87 ?  166 GLU A CG    1 
ATOM   1376  C  CD    . GLU A 1 166 ? 126.507 147.841 108.842 1.00 45.97 ?  166 GLU A CD    1 
ATOM   1377  O  OE1   . GLU A 1 166 ? 126.897 147.507 107.702 1.00 48.15 ?  166 GLU A OE1   1 
ATOM   1378  O  OE2   . GLU A 1 166 ? 126.127 149.000 109.111 1.00 43.24 -1 166 GLU A OE2   1 
ATOM   1379  N  N     . LEU A 1 167 ? 126.128 145.003 106.311 1.00 30.76 ?  167 LEU A N     1 
ATOM   1380  C  CA    . LEU A 1 167 ? 126.598 144.396 105.074 1.00 25.60 ?  167 LEU A CA    1 
ATOM   1381  C  C     . LEU A 1 167 ? 128.003 143.826 105.193 1.00 28.67 ?  167 LEU A C     1 
ATOM   1382  O  O     . LEU A 1 167 ? 128.452 143.129 104.277 1.00 30.69 ?  167 LEU A O     1 
ATOM   1383  C  CB    . LEU A 1 167 ? 126.555 145.420 103.939 1.00 26.21 ?  167 LEU A CB    1 
ATOM   1384  C  CG    . LEU A 1 167 ? 125.175 145.944 103.550 1.00 25.34 ?  167 LEU A CG    1 
ATOM   1385  C  CD1   . LEU A 1 167 ? 125.250 146.671 102.230 1.00 27.51 ?  167 LEU A CD1   1 
ATOM   1386  C  CD2   . LEU A 1 167 ? 124.176 144.809 103.472 1.00 27.01 ?  167 LEU A CD2   1 
ATOM   1387  N  N     . VAL A 1 168 ? 128.700 144.107 106.288 1.00 29.92 ?  168 VAL A N     1 
ATOM   1388  C  CA    . VAL A 1 168 ? 130.016 143.544 106.564 1.00 20.10 ?  168 VAL A CA    1 
ATOM   1389  C  C     . VAL A 1 168 ? 129.857 142.501 107.658 1.00 25.75 ?  168 VAL A C     1 
ATOM   1390  O  O     . VAL A 1 168 ? 129.171 142.743 108.660 1.00 33.49 ?  168 VAL A O     1 
ATOM   1391  C  CB    . VAL A 1 168 ? 131.012 144.638 106.985 1.00 24.69 ?  168 VAL A CB    1 
ATOM   1392  C  CG1   . VAL A 1 168 ? 132.391 144.042 107.213 1.00 29.31 ?  168 VAL A CG1   1 
ATOM   1393  C  CG2   . VAL A 1 168 ? 131.068 145.738 105.938 1.00 27.55 ?  168 VAL A CG2   1 
ATOM   1394  N  N     . SER A 1 169 ? 130.470 141.335 107.465 1.00 26.07 ?  169 SER A N     1 
ATOM   1395  C  CA    . SER A 1 169 ? 130.420 140.278 108.463 1.00 29.38 ?  169 SER A CA    1 
ATOM   1396  C  C     . SER A 1 169 ? 131.786 139.766 108.886 1.00 32.50 ?  169 SER A C     1 
ATOM   1397  O  O     . SER A 1 169 ? 131.853 138.832 109.693 1.00 38.92 ?  169 SER A O     1 
ATOM   1398  C  CB    . SER A 1 169 ? 129.570 139.102 107.965 1.00 30.68 ?  169 SER A CB    1 
ATOM   1399  O  OG    . SER A 1 169 ? 128.190 139.394 108.093 1.00 38.06 ?  169 SER A OG    1 
ATOM   1400  N  N     . CYS A 1 170 ? 132.871 140.333 108.373 1.00 26.32 ?  170 CYS A N     1 
ATOM   1401  C  CA    . CYS A 1 170 ? 134.210 140.010 108.845 1.00 24.16 ?  170 CYS A CA    1 
ATOM   1402  C  C     . CYS A 1 170 ? 134.760 141.223 109.585 1.00 23.58 ?  170 CYS A C     1 
ATOM   1403  O  O     . CYS A 1 170 ? 134.901 142.304 109.002 1.00 26.85 ?  170 CYS A O     1 
ATOM   1404  C  CB    . CYS A 1 170 ? 135.121 139.577 107.692 1.00 30.30 ?  170 CYS A CB    1 
ATOM   1405  S  SG    . CYS A 1 170 ? 135.646 140.854 106.526 1.00 48.74 ?  170 CYS A SG    1 
ATOM   1406  N  N     . PHE A 1 171 ? 135.029 141.048 110.874 1.00 23.10 ?  171 PHE A N     1 
ATOM   1407  C  CA    . PHE A 1 171 ? 135.538 142.112 111.727 1.00 10.69 ?  171 PHE A CA    1 
ATOM   1408  C  C     . PHE A 1 171 ? 136.750 141.601 112.481 1.00 15.01 ?  171 PHE A C     1 
ATOM   1409  O  O     . PHE A 1 171 ? 136.719 140.503 113.044 1.00 22.56 ?  171 PHE A O     1 
ATOM   1410  C  CB    . PHE A 1 171 ? 134.470 142.599 112.710 1.00 15.76 ?  171 PHE A CB    1 
ATOM   1411  C  CG    . PHE A 1 171 ? 133.238 143.133 112.047 1.00 17.29 ?  171 PHE A CG    1 
ATOM   1412  C  CD1   . PHE A 1 171 ? 133.253 144.371 111.433 1.00 19.36 ?  171 PHE A CD1   1 
ATOM   1413  C  CD2   . PHE A 1 171 ? 132.065 142.400 112.038 1.00 15.63 ?  171 PHE A CD2   1 
ATOM   1414  C  CE1   . PHE A 1 171 ? 132.126 144.866 110.818 1.00 14.98 ?  171 PHE A CE1   1 
ATOM   1415  C  CE2   . PHE A 1 171 ? 130.932 142.892 111.427 1.00 16.79 ?  171 PHE A CE2   1 
ATOM   1416  C  CZ    . PHE A 1 171 ? 130.964 144.128 110.816 1.00 16.17 ?  171 PHE A CZ    1 
ATOM   1417  N  N     . LEU A 1 172 ? 137.815 142.394 112.486 1.00 14.71 ?  172 LEU A N     1 
ATOM   1418  C  CA    . LEU A 1 172 ? 139.033 142.070 113.210 1.00 9.06  ?  172 LEU A CA    1 
ATOM   1419  C  C     . LEU A 1 172 ? 139.250 143.127 114.280 1.00 13.65 ?  172 LEU A C     1 
ATOM   1420  O  O     . LEU A 1 172 ? 139.308 144.321 113.972 1.00 16.89 ?  172 LEU A O     1 
ATOM   1421  C  CB    . LEU A 1 172 ? 140.238 142.004 112.270 1.00 14.71 ?  172 LEU A CB    1 
ATOM   1422  C  CG    . LEU A 1 172 ? 140.343 140.804 111.330 1.00 6.10  ?  172 LEU A CG    1 
ATOM   1423  C  CD1   . LEU A 1 172 ? 139.436 140.981 110.124 1.00 8.62  ?  172 LEU A CD1   1 
ATOM   1424  C  CD2   . LEU A 1 172 ? 141.780 140.612 110.894 1.00 13.30 ?  172 LEU A CD2   1 
ATOM   1425  N  N     . LEU A 1 173 ? 139.371 142.690 115.527 1.00 16.08 ?  173 LEU A N     1 
ATOM   1426  C  CA    . LEU A 1 173 ? 139.537 143.589 116.657 1.00 12.47 ?  173 LEU A CA    1 
ATOM   1427  C  C     . LEU A 1 173 ? 140.904 143.395 117.291 1.00 11.97 ?  173 LEU A C     1 
ATOM   1428  O  O     . LEU A 1 173 ? 141.368 142.264 117.460 1.00 16.59 ?  173 LEU A O     1 
ATOM   1429  C  CB    . LEU A 1 173 ? 138.450 143.365 117.710 1.00 16.96 ?  173 LEU A CB    1 
ATOM   1430  C  CG    . LEU A 1 173 ? 136.992 143.382 117.258 1.00 20.16 ?  173 LEU A CG    1 
ATOM   1431  C  CD1   . LEU A 1 173 ? 136.082 143.271 118.468 1.00 19.08 ?  173 LEU A CD1   1 
ATOM   1432  C  CD2   . LEU A 1 173 ? 136.680 144.634 116.456 1.00 16.49 ?  173 LEU A CD2   1 
ATOM   1433  N  N     . GLU A 1 174 ? 141.546 144.505 117.631 1.00 25.98 ?  174 GLU A N     1 
ATOM   1434  C  CA    . GLU A 1 174 ? 142.751 144.485 118.444 1.00 23.68 ?  174 GLU A CA    1 
ATOM   1435  C  C     . GLU A 1 174 ? 142.378 144.730 119.898 1.00 20.40 ?  174 GLU A C     1 
ATOM   1436  O  O     . GLU A 1 174 ? 141.650 145.676 120.213 1.00 29.43 ?  174 GLU A O     1 
ATOM   1437  C  CB    . GLU A 1 174 ? 143.742 145.548 117.969 1.00 26.29 ?  174 GLU A CB    1 
ATOM   1438  C  CG    . GLU A 1 174 ? 144.282 145.319 116.570 1.00 22.14 ?  174 GLU A CG    1 
ATOM   1439  C  CD    . GLU A 1 174 ? 145.659 144.692 116.577 1.00 25.00 ?  174 GLU A CD    1 
ATOM   1440  O  OE1   . GLU A 1 174 ? 146.243 144.549 117.670 1.00 28.05 ?  174 GLU A OE1   1 
ATOM   1441  O  OE2   . GLU A 1 174 ? 146.160 144.344 115.489 1.00 28.48 -1 174 GLU A OE2   1 
ATOM   1442  N  N     . VAL A 1 175 ? 142.875 143.873 120.782 1.00 19.84 ?  175 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 175 ? 142.595 143.964 122.211 1.00 20.81 ?  175 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 175 ? 143.876 144.380 122.918 1.00 18.94 ?  175 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 175 ? 144.891 143.676 122.848 1.00 26.83 ?  175 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 175 ? 142.060 142.637 122.771 1.00 22.21 ?  175 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 175 ? 141.485 142.842 124.163 1.00 14.41 ?  175 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 175 ? 141.016 142.050 121.835 1.00 19.87 ?  175 VAL A CG2   1 
ATOM   1449  N  N     . ASN A 1 176 ? 143.830 145.522 123.597 1.00 18.41 ?  176 ASN A N     1 
ATOM   1450  C  CA    . ASN A 1 176 ? 144.973 145.989 124.360 1.00 20.00 ?  176 ASN A CA    1 
ATOM   1451  C  C     . ASN A 1 176 ? 144.997 145.332 125.736 1.00 23.60 ?  176 ASN A C     1 
ATOM   1452  O  O     . ASN A 1 176 ? 143.987 144.825 126.233 1.00 24.22 ?  176 ASN A O     1 
ATOM   1453  C  CB    . ASN A 1 176 ? 144.944 147.510 124.493 1.00 18.83 ?  176 ASN A CB    1 
ATOM   1454  C  CG    . ASN A 1 176 ? 146.325 148.125 124.451 1.00 21.31 ?  176 ASN A CG    1 
ATOM   1455  O  OD1   . ASN A 1 176 ? 147.315 147.480 124.793 1.00 27.96 ?  176 ASN A OD1   1 
ATOM   1456  N  ND2   . ASN A 1 176 ? 146.400 149.380 124.025 1.00 20.44 ?  176 ASN A ND2   1 
ATOM   1457  N  N     . ASP A 1 177 ? 146.176 145.352 126.359 1.00 23.65 ?  177 ASP A N     1 
ATOM   1458  C  CA    . ASP A 1 177 ? 146.410 144.636 127.612 1.00 20.06 ?  177 ASP A CA    1 
ATOM   1459  C  C     . ASP A 1 177 ? 145.906 145.477 128.783 1.00 24.85 ?  177 ASP A C     1 
ATOM   1460  O  O     . ASP A 1 177 ? 146.670 146.095 129.529 1.00 35.39 ?  177 ASP A O     1 
ATOM   1461  C  CB    . ASP A 1 177 ? 147.887 144.298 127.759 1.00 19.80 ?  177 ASP A CB    1 
ATOM   1462  C  CG    . ASP A 1 177 ? 148.155 143.364 128.916 1.00 25.30 ?  177 ASP A CG    1 
ATOM   1463  O  OD1   . ASP A 1 177 ? 147.365 142.417 129.116 1.00 28.44 ?  177 ASP A OD1   1 
ATOM   1464  O  OD2   . ASP A 1 177 ? 149.160 143.575 129.626 1.00 31.09 -1 177 ASP A OD2   1 
ATOM   1465  N  N     . SER A 1 178 ? 144.586 145.492 128.944 1.00 20.57 ?  178 SER A N     1 
ATOM   1466  C  CA    . SER A 1 178 ? 143.962 146.175 130.068 1.00 17.37 ?  178 SER A CA    1 
ATOM   1467  C  C     . SER A 1 178 ? 142.566 145.609 130.269 1.00 17.74 ?  178 SER A C     1 
ATOM   1468  O  O     . SER A 1 178 ? 141.973 145.031 129.355 1.00 27.43 ?  178 SER A O     1 
ATOM   1469  C  CB    . SER A 1 178 ? 143.906 147.691 129.848 1.00 16.60 ?  178 SER A CB    1 
ATOM   1470  O  OG    . SER A 1 178 ? 142.690 148.073 129.234 1.00 20.62 ?  178 SER A OG    1 
ATOM   1471  N  N     . LEU A 1 179 ? 142.049 145.779 131.488 1.00 22.74 ?  179 LEU A N     1 
ATOM   1472  C  CA    . LEU A 1 179 ? 140.688 145.337 131.776 1.00 19.48 ?  179 LEU A CA    1 
ATOM   1473  C  C     . LEU A 1 179 ? 139.665 146.185 131.033 1.00 18.74 ?  179 LEU A C     1 
ATOM   1474  O  O     . LEU A 1 179 ? 138.651 145.666 130.556 1.00 22.22 ?  179 LEU A O     1 
ATOM   1475  C  CB    . LEU A 1 179 ? 140.425 145.379 133.280 1.00 26.25 ?  179 LEU A CB    1 
ATOM   1476  C  CG    . LEU A 1 179 ? 139.129 144.697 133.726 1.00 18.81 ?  179 LEU A CG    1 
ATOM   1477  C  CD1   . LEU A 1 179 ? 139.275 143.186 133.669 1.00 21.68 ?  179 LEU A CD1   1 
ATOM   1478  C  CD2   . LEU A 1 179 ? 138.728 145.151 135.118 1.00 18.45 ?  179 LEU A CD2   1 
ATOM   1479  N  N     . ASN A 1 180 ? 139.912 147.493 130.933 1.00 21.73 ?  180 ASN A N     1 
ATOM   1480  C  CA    . ASN A 1 180 ? 139.030 148.357 130.156 1.00 19.79 ?  180 ASN A CA    1 
ATOM   1481  C  C     . ASN A 1 180 ? 138.994 147.927 128.696 1.00 20.72 ?  180 ASN A C     1 
ATOM   1482  O  O     . ASN A 1 180 ? 137.922 147.851 128.087 1.00 24.18 ?  180 ASN A O     1 
ATOM   1483  C  CB    . ASN A 1 180 ? 139.485 149.811 130.270 1.00 21.19 ?  180 ASN A CB    1 
ATOM   1484  C  CG    . ASN A 1 180 ? 139.037 150.464 131.559 1.00 26.79 ?  180 ASN A CG    1 
ATOM   1485  O  OD1   . ASN A 1 180 ? 138.004 150.107 132.125 1.00 33.12 ?  180 ASN A OD1   1 
ATOM   1486  N  ND2   . ASN A 1 180 ? 139.816 151.427 132.032 1.00 26.38 ?  180 ASN A ND2   1 
ATOM   1487  N  N     . ASP A 1 181 ? 140.161 147.626 128.126 1.00 21.75 ?  181 ASP A N     1 
ATOM   1488  C  CA    . ASP A 1 181 ? 140.219 147.202 126.732 1.00 12.47 ?  181 ASP A CA    1 
ATOM   1489  C  C     . ASP A 1 181 ? 139.582 145.833 126.540 1.00 18.69 ?  181 ASP A C     1 
ATOM   1490  O  O     . ASP A 1 181 ? 138.935 145.587 125.520 1.00 26.03 ?  181 ASP A O     1 
ATOM   1491  C  CB    . ASP A 1 181 ? 141.667 147.201 126.247 1.00 20.67 ?  181 ASP A CB    1 
ATOM   1492  C  CG    . ASP A 1 181 ? 142.251 148.595 126.166 1.00 28.75 ?  181 ASP A CG    1 
ATOM   1493  O  OD1   . ASP A 1 181 ? 141.765 149.394 125.341 1.00 31.69 ?  181 ASP A OD1   1 
ATOM   1494  O  OD2   . ASP A 1 181 ? 143.198 148.892 126.923 1.00 29.88 -1 181 ASP A OD2   1 
ATOM   1495  N  N     . ILE A 1 182 ? 139.744 144.931 127.508 1.00 20.59 ?  182 ILE A N     1 
ATOM   1496  C  CA    . ILE A 1 182 ? 139.120 143.615 127.405 1.00 17.82 ?  182 ILE A CA    1 
ATOM   1497  C  C     . ILE A 1 182 ? 137.600 143.734 127.462 1.00 19.62 ?  182 ILE A C     1 
ATOM   1498  O  O     . ILE A 1 182 ? 136.882 143.098 126.679 1.00 25.76 ?  182 ILE A O     1 
ATOM   1499  C  CB    . ILE A 1 182 ? 139.665 142.684 128.503 1.00 18.58 ?  182 ILE A CB    1 
ATOM   1500  C  CG1   . ILE A 1 182 ? 141.046 142.166 128.106 1.00 20.04 ?  182 ILE A CG1   1 
ATOM   1501  C  CG2   . ILE A 1 182 ? 138.711 141.527 128.761 1.00 21.02 ?  182 ILE A CG2   1 
ATOM   1502  C  CD1   . ILE A 1 182 ? 141.810 141.554 129.241 1.00 21.69 ?  182 ILE A CD1   1 
ATOM   1503  N  N     . SER A 1 183 ? 137.085 144.550 128.383 1.00 20.91 ?  183 SER A N     1 
ATOM   1504  C  CA    . SER A 1 183 ? 135.643 144.752 128.468 1.00 19.31 ?  183 SER A CA    1 
ATOM   1505  C  C     . SER A 1 183 ? 135.104 145.421 127.210 1.00 23.27 ?  183 SER A C     1 
ATOM   1506  O  O     . SER A 1 183 ? 134.032 145.056 126.716 1.00 25.87 ?  183 SER A O     1 
ATOM   1507  C  CB    . SER A 1 183 ? 135.303 145.579 129.707 1.00 19.40 ?  183 SER A CB    1 
ATOM   1508  O  OG    . SER A 1 183 ? 135.845 146.883 129.614 1.00 29.39 ?  183 SER A OG    1 
ATOM   1509  N  N     . ARG A 1 184 ? 135.838 146.401 126.676 1.00 25.20 ?  184 ARG A N     1 
ATOM   1510  C  CA    . ARG A 1 184 ? 135.417 147.040 125.435 1.00 19.46 ?  184 ARG A CA    1 
ATOM   1511  C  C     . ARG A 1 184 ? 135.440 146.058 124.272 1.00 23.51 ?  184 ARG A C     1 
ATOM   1512  O  O     . ARG A 1 184 ? 134.571 146.107 123.399 1.00 28.66 ?  184 ARG A O     1 
ATOM   1513  C  CB    . ARG A 1 184 ? 136.302 148.249 125.139 1.00 15.25 ?  184 ARG A CB    1 
ATOM   1514  C  CG    . ARG A 1 184 ? 135.903 149.009 123.889 1.00 24.35 ?  184 ARG A CG    1 
ATOM   1515  C  CD    . ARG A 1 184 ? 134.445 149.418 123.930 1.00 24.56 ?  184 ARG A CD    1 
ATOM   1516  N  NE    . ARG A 1 184 ? 134.249 150.661 124.665 1.00 32.26 ?  184 ARG A NE    1 
ATOM   1517  C  CZ    . ARG A 1 184 ? 133.139 150.980 125.314 1.00 29.75 ?  184 ARG A CZ    1 
ATOM   1518  N  NH1   . ARG A 1 184 ? 132.098 150.164 125.345 1.00 25.23 1  184 ARG A NH1   1 
ATOM   1519  N  NH2   . ARG A 1 184 ? 133.070 152.146 125.948 1.00 26.89 ?  184 ARG A NH2   1 
ATOM   1520  N  N     . ALA A 1 185 ? 136.429 145.162 124.238 1.00 24.15 ?  185 ALA A N     1 
ATOM   1521  C  CA    . ALA A 1 185 ? 136.477 144.146 123.194 1.00 16.96 ?  185 ALA A CA    1 
ATOM   1522  C  C     . ALA A 1 185 ? 135.290 143.201 123.294 1.00 20.26 ?  185 ALA A C     1 
ATOM   1523  O  O     . ALA A 1 185 ? 134.699 142.829 122.276 1.00 23.61 ?  185 ALA A O     1 
ATOM   1524  C  CB    . ALA A 1 185 ? 137.790 143.369 123.277 1.00 16.52 ?  185 ALA A CB    1 
ATOM   1525  N  N     . ILE A 1 186 ? 134.925 142.803 124.515 1.00 23.68 ?  186 ILE A N     1 
ATOM   1526  C  CA    . ILE A 1 186 ? 133.746 141.959 124.705 1.00 20.75 ?  186 ILE A CA    1 
ATOM   1527  C  C     . ILE A 1 186 ? 132.495 142.681 124.219 1.00 20.06 ?  186 ILE A C     1 
ATOM   1528  O  O     . ILE A 1 186 ? 131.652 142.107 123.516 1.00 27.89 ?  186 ILE A O     1 
ATOM   1529  C  CB    . ILE A 1 186 ? 133.618 141.541 126.182 1.00 26.09 ?  186 ILE A CB    1 
ATOM   1530  C  CG1   . ILE A 1 186 ? 134.756 140.599 126.577 1.00 24.61 ?  186 ILE A CG1   1 
ATOM   1531  C  CG2   . ILE A 1 186 ? 132.269 140.888 126.443 1.00 24.04 ?  186 ILE A CG2   1 
ATOM   1532  C  CD1   . ILE A 1 186 ? 135.044 140.591 128.060 1.00 23.67 ?  186 ILE A CD1   1 
ATOM   1533  N  N     . ASP A 1 187 ? 132.362 143.959 124.581 1.00 21.52 ?  187 ASP A N     1 
ATOM   1534  C  CA    . ASP A 1 187 ? 131.201 144.739 124.164 1.00 19.03 ?  187 ASP A CA    1 
ATOM   1535  C  C     . ASP A 1 187 ? 131.131 144.859 122.646 1.00 23.82 ?  187 ASP A C     1 
ATOM   1536  O  O     . ASP A 1 187 ? 130.066 144.675 122.047 1.00 28.16 ?  187 ASP A O     1 
ATOM   1537  C  CB    . ASP A 1 187 ? 131.245 146.123 124.810 1.00 17.96 ?  187 ASP A CB    1 
ATOM   1538  C  CG    . ASP A 1 187 ? 130.406 147.141 124.065 1.00 28.50 ?  187 ASP A CG    1 
ATOM   1539  O  OD1   . ASP A 1 187 ? 129.196 146.896 123.877 1.00 30.94 ?  187 ASP A OD1   1 
ATOM   1540  O  OD2   . ASP A 1 187 ? 130.958 148.186 123.663 1.00 34.22 -1 187 ASP A OD2   1 
ATOM   1541  N  N     . ILE A 1 188 ? 132.261 145.169 122.008 1.00 22.45 ?  188 ILE A N     1 
ATOM   1542  C  CA    . ILE A 1 188 ? 132.281 145.341 120.559 1.00 21.59 ?  188 ILE A CA    1 
ATOM   1543  C  C     . ILE A 1 188 ? 132.005 144.017 119.859 1.00 23.18 ?  188 ILE A C     1 
ATOM   1544  O  O     . ILE A 1 188 ? 131.317 143.976 118.835 1.00 27.73 ?  188 ILE A O     1 
ATOM   1545  C  CB    . ILE A 1 188 ? 133.621 145.956 120.112 1.00 22.36 ?  188 ILE A CB    1 
ATOM   1546  C  CG1   . ILE A 1 188 ? 133.780 147.367 120.675 1.00 22.66 ?  188 ILE A CG1   1 
ATOM   1547  C  CG2   . ILE A 1 188 ? 133.708 146.013 118.602 1.00 21.91 ?  188 ILE A CG2   1 
ATOM   1548  C  CD1   . ILE A 1 188 ? 135.139 147.972 120.416 1.00 22.60 ?  188 ILE A CD1   1 
ATOM   1549  N  N     . SER A 1 189 ? 132.535 142.916 120.396 1.00 18.21 ?  189 SER A N     1 
ATOM   1550  C  CA    . SER A 1 189 ? 132.240 141.604 119.834 1.00 12.23 ?  189 SER A CA    1 
ATOM   1551  C  C     . SER A 1 189 ? 130.752 141.303 119.911 1.00 19.79 ?  189 SER A C     1 
ATOM   1552  O  O     . SER A 1 189 ? 130.163 140.792 118.952 1.00 28.18 ?  189 SER A O     1 
ATOM   1553  C  CB    . SER A 1 189 ? 133.043 140.530 120.566 1.00 20.99 ?  189 SER A CB    1 
ATOM   1554  O  OG    . SER A 1 189 ? 134.424 140.835 120.567 1.00 27.35 ?  189 SER A OG    1 
ATOM   1555  N  N     . MET A 1 190 ? 130.125 141.623 121.045 1.00 25.42 ?  190 MET A N     1 
ATOM   1556  C  CA    . MET A 1 190 ? 128.686 141.420 121.176 1.00 22.32 ?  190 MET A CA    1 
ATOM   1557  C  C     . MET A 1 190 ? 127.912 142.282 120.188 1.00 18.68 ?  190 MET A C     1 
ATOM   1558  O  O     . MET A 1 190 ? 126.951 141.816 119.565 1.00 22.42 ?  190 MET A O     1 
ATOM   1559  C  CB    . MET A 1 190 ? 128.246 141.730 122.604 1.00 25.23 ?  190 MET A CB    1 
ATOM   1560  C  CG    . MET A 1 190 ? 128.468 140.599 123.580 1.00 18.79 ?  190 MET A CG    1 
ATOM   1561  S  SD    . MET A 1 190 ? 128.471 141.199 125.274 1.00 37.97 ?  190 MET A SD    1 
ATOM   1562  C  CE    . MET A 1 190 ? 127.155 140.209 125.959 1.00 27.75 ?  190 MET A CE    1 
ATOM   1563  N  N     . GLN A 1 191 ? 128.316 143.544 120.030 1.00 21.05 ?  191 GLN A N     1 
ATOM   1564  C  CA    . GLN A 1 191 ? 127.607 144.444 119.126 1.00 22.57 ?  191 GLN A CA    1 
ATOM   1565  C  C     . GLN A 1 191 ? 127.748 144.002 117.675 1.00 24.99 ?  191 GLN A C     1 
ATOM   1566  O  O     . GLN A 1 191 ? 126.798 144.112 116.891 1.00 30.62 ?  191 GLN A O     1 
ATOM   1567  C  CB    . GLN A 1 191 ? 128.111 145.877 119.296 1.00 22.31 ?  191 GLN A CB    1 
ATOM   1568  C  CG    . GLN A 1 191 ? 127.940 146.443 120.694 1.00 21.20 ?  191 GLN A CG    1 
ATOM   1569  C  CD    . GLN A 1 191 ? 126.491 146.689 121.058 1.00 27.26 ?  191 GLN A CD    1 
ATOM   1570  O  OE1   . GLN A 1 191 ? 125.630 146.809 120.188 1.00 28.28 ?  191 GLN A OE1   1 
ATOM   1571  N  NE2   . GLN A 1 191 ? 126.215 146.771 122.354 1.00 25.51 ?  191 GLN A NE2   1 
ATOM   1572  N  N     . LEU A 1 192 ? 128.927 143.509 117.294 1.00 24.46 ?  192 LEU A N     1 
ATOM   1573  C  CA    . LEU A 1 192 ? 129.140 143.083 115.917 1.00 19.42 ?  192 LEU A CA    1 
ATOM   1574  C  C     . LEU A 1 192 ? 128.494 141.735 115.629 1.00 23.47 ?  192 LEU A C     1 
ATOM   1575  O  O     . LEU A 1 192 ? 128.041 141.503 114.502 1.00 33.19 ?  192 LEU A O     1 
ATOM   1576  C  CB    . LEU A 1 192 ? 130.634 143.035 115.605 1.00 20.09 ?  192 LEU A CB    1 
ATOM   1577  C  CG    . LEU A 1 192 ? 131.380 144.369 115.673 1.00 18.88 ?  192 LEU A CG    1 
ATOM   1578  C  CD1   . LEU A 1 192 ? 132.880 144.138 115.652 1.00 18.46 ?  192 LEU A CD1   1 
ATOM   1579  C  CD2   . LEU A 1 192 ? 130.955 145.298 114.550 1.00 16.55 ?  192 LEU A CD2   1 
ATOM   1580  N  N     . SER A 1 193 ? 128.445 140.834 116.613 1.00 19.30 ?  193 SER A N     1 
ATOM   1581  C  CA    . SER A 1 193 ? 127.682 139.603 116.444 1.00 21.10 ?  193 SER A CA    1 
ATOM   1582  C  C     . SER A 1 193 ? 126.191 139.896 116.369 1.00 30.66 ?  193 SER A C     1 
ATOM   1583  O  O     . SER A 1 193 ? 125.448 139.199 115.669 1.00 35.65 ?  193 SER A O     1 
ATOM   1584  C  CB    . SER A 1 193 ? 127.987 138.634 117.585 1.00 23.76 ?  193 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 193 ? 129.379 138.576 117.836 1.00 29.24 ?  193 SER A OG    1 
ATOM   1586  N  N     . LYS A 1 194 ? 125.737 140.921 117.092 1.00 28.35 ?  194 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 194 ? 124.354 141.370 116.971 1.00 26.81 ?  194 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 194 ? 124.056 141.838 115.553 1.00 33.98 ?  194 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 194 ? 122.971 141.578 115.019 1.00 37.52 ?  194 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 194 ? 124.086 142.485 117.982 1.00 25.61 ?  194 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 194 ? 122.785 143.231 117.773 1.00 31.84 ?  194 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 194 ? 122.686 144.432 118.698 1.00 34.30 ?  194 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 194 ? 121.288 145.026 118.681 1.00 30.41 ?  194 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 194 ? 121.191 146.237 119.540 1.00 33.10 1  194 LYS A NZ    1 
ATOM   1595  N  N     . LEU A 1 195 ? 125.010 142.528 114.926 1.00 34.63 ?  195 LEU A N     1 
ATOM   1596  C  CA    . LEU A 1 195 ? 124.869 142.947 113.538 1.00 32.10 ?  195 LEU A CA    1 
ATOM   1597  C  C     . LEU A 1 195 ? 124.968 141.784 112.560 1.00 34.27 ?  195 LEU A C     1 
ATOM   1598  O  O     . LEU A 1 195 ? 124.710 141.978 111.368 1.00 37.81 ?  195 LEU A O     1 
ATOM   1599  C  CB    . LEU A 1 195 ? 125.930 143.995 113.197 1.00 32.31 ?  195 LEU A CB    1 
ATOM   1600  C  CG    . LEU A 1 195 ? 125.802 145.342 113.908 1.00 35.80 ?  195 LEU A CG    1 
ATOM   1601  C  CD1   . LEU A 1 195 ? 126.985 146.235 113.576 1.00 35.62 ?  195 LEU A CD1   1 
ATOM   1602  C  CD2   . LEU A 1 195 ? 124.493 146.018 113.537 1.00 33.64 ?  195 LEU A CD2   1 
ATOM   1603  N  N     . GLY A 1 196 ? 125.339 140.596 113.028 1.00 34.97 ?  196 GLY A N     1 
ATOM   1604  C  CA    . GLY A 1 196 ? 125.459 139.442 112.166 1.00 33.07 ?  196 GLY A CA    1 
ATOM   1605  C  C     . GLY A 1 196 ? 126.847 139.169 111.641 1.00 37.29 ?  196 GLY A C     1 
ATOM   1606  O  O     . GLY A 1 196 ? 126.994 138.343 110.732 1.00 40.02 ?  196 GLY A O     1 
ATOM   1607  N  N     . GLY A 1 197 ? 127.868 139.826 112.179 1.00 34.21 ?  197 GLY A N     1 
ATOM   1608  C  CA    . GLY A 1 197 ? 129.214 139.667 111.676 1.00 24.52 ?  197 GLY A CA    1 
ATOM   1609  C  C     . GLY A 1 197 ? 130.057 138.698 112.483 1.00 23.86 ?  197 GLY A C     1 
ATOM   1610  O  O     . GLY A 1 197 ? 129.873 138.532 113.685 1.00 33.65 ?  197 GLY A O     1 
ATOM   1611  N  N     . GLY A 1 198 ? 130.993 138.051 111.791 1.00 17.12 ?  198 GLY A N     1 
ATOM   1612  C  CA    . GLY A 1 198 ? 131.982 137.223 112.459 1.00 16.73 ?  198 GLY A CA    1 
ATOM   1613  C  C     . GLY A 1 198 ? 133.128 138.084 112.950 1.00 17.59 ?  198 GLY A C     1 
ATOM   1614  O  O     . GLY A 1 198 ? 133.683 138.890 112.195 1.00 18.46 ?  198 GLY A O     1 
ATOM   1615  N  N     . VAL A 1 199 ? 133.486 137.917 114.218 1.00 21.76 ?  199 VAL A N     1 
ATOM   1616  C  CA    . VAL A 1 199 ? 134.431 138.795 114.895 1.00 13.39 ?  199 VAL A CA    1 
ATOM   1617  C  C     . VAL A 1 199 ? 135.694 138.013 115.212 1.00 11.65 ?  199 VAL A C     1 
ATOM   1618  O  O     . VAL A 1 199 ? 135.632 136.940 115.821 1.00 16.01 ?  199 VAL A O     1 
ATOM   1619  C  CB    . VAL A 1 199 ? 133.822 139.388 116.176 1.00 13.59 ?  199 VAL A CB    1 
ATOM   1620  C  CG1   . VAL A 1 199 ? 134.788 140.365 116.815 1.00 15.15 ?  199 VAL A CG1   1 
ATOM   1621  C  CG2   . VAL A 1 199 ? 132.501 140.055 115.867 1.00 18.65 ?  199 VAL A CG2   1 
ATOM   1622  N  N     . SER A 1 200 ? 136.837 138.555 114.807 1.00 15.20 ?  200 SER A N     1 
ATOM   1623  C  CA    . SER A 1 200 ? 138.141 138.004 115.139 1.00 3.66  ?  200 SER A CA    1 
ATOM   1624  C  C     . SER A 1 200 ? 138.861 138.978 116.058 1.00 11.73 ?  200 SER A C     1 
ATOM   1625  O  O     . SER A 1 200 ? 138.885 140.185 115.794 1.00 21.37 ?  200 SER A O     1 
ATOM   1626  C  CB    . SER A 1 200 ? 138.967 137.746 113.881 1.00 9.17  ?  200 SER A CB    1 
ATOM   1627  O  OG    . SER A 1 200 ? 140.109 136.962 114.171 1.00 16.25 ?  200 SER A OG    1 
ATOM   1628  N  N     . LEU A 1 201 ? 139.438 138.458 117.136 1.00 16.66 ?  201 LEU A N     1 
ATOM   1629  C  CA    . LEU A 1 201 ? 140.118 139.270 118.133 1.00 9.22  ?  201 LEU A CA    1 
ATOM   1630  C  C     . LEU A 1 201 ? 141.565 138.819 118.255 1.00 7.69  ?  201 LEU A C     1 
ATOM   1631  O  O     . LEU A 1 201 ? 141.838 137.618 118.349 1.00 9.39  ?  201 LEU A O     1 
ATOM   1632  C  CB    . LEU A 1 201 ? 139.419 139.175 119.492 1.00 16.07 ?  201 LEU A CB    1 
ATOM   1633  C  CG    . LEU A 1 201 ? 137.970 139.662 119.531 1.00 14.03 ?  201 LEU A CG    1 
ATOM   1634  C  CD1   . LEU A 1 201 ? 137.011 138.484 119.512 1.00 14.27 ?  201 LEU A CD1   1 
ATOM   1635  C  CD2   . LEU A 1 201 ? 137.730 140.536 120.747 1.00 15.95 ?  201 LEU A CD2   1 
ATOM   1636  N  N     . ASN A 1 202 ? 142.480 139.782 118.260 1.00 13.18 ?  202 ASN A N     1 
ATOM   1637  C  CA    . ASN A 1 202 ? 143.893 139.514 118.487 1.00 7.05  ?  202 ASN A CA    1 
ATOM   1638  C  C     . ASN A 1 202 ? 144.163 139.561 119.985 1.00 13.85 ?  202 ASN A C     1 
ATOM   1639  O  O     . ASN A 1 202 ? 143.932 140.588 120.631 1.00 25.93 ?  202 ASN A O     1 
ATOM   1640  C  CB    . ASN A 1 202 ? 144.759 140.533 117.749 1.00 8.39  ?  202 ASN A CB    1 
ATOM   1641  C  CG    . ASN A 1 202 ? 146.224 140.153 117.735 1.00 11.78 ?  202 ASN A CG    1 
ATOM   1642  O  OD1   . ASN A 1 202 ? 146.573 138.977 117.829 1.00 17.73 ?  202 ASN A OD1   1 
ATOM   1643  N  ND2   . ASN A 1 202 ? 147.091 141.149 117.614 1.00 14.87 ?  202 ASN A ND2   1 
ATOM   1644  N  N     . LEU A 1 203 ? 144.648 138.450 120.537 1.00 8.33  ?  203 LEU A N     1 
ATOM   1645  C  CA    . LEU A 1 203 ? 144.911 138.343 121.966 1.00 9.55  ?  203 LEU A CA    1 
ATOM   1646  C  C     . LEU A 1 203 ? 146.398 138.320 122.288 1.00 12.58 ?  203 LEU A C     1 
ATOM   1647  O  O     . LEU A 1 203 ? 146.770 138.036 123.431 1.00 14.59 ?  203 LEU A O     1 
ATOM   1648  C  CB    . LEU A 1 203 ? 144.230 137.097 122.535 1.00 15.42 ?  203 LEU A CB    1 
ATOM   1649  C  CG    . LEU A 1 203 ? 142.710 137.012 122.376 1.00 15.72 ?  203 LEU A CG    1 
ATOM   1650  C  CD1   . LEU A 1 203 ? 142.146 135.972 123.322 1.00 14.37 ?  203 LEU A CD1   1 
ATOM   1651  C  CD2   . LEU A 1 203 ? 142.051 138.362 122.609 1.00 12.05 ?  203 LEU A CD2   1 
ATOM   1652  N  N     . SER A 1 204 ? 147.257 138.620 121.311 1.00 17.27 ?  204 SER A N     1 
ATOM   1653  C  CA    . SER A 1 204 ? 148.696 138.553 121.536 1.00 15.28 ?  204 SER A CA    1 
ATOM   1654  C  C     . SER A 1 204 ? 149.192 139.673 122.442 1.00 17.32 ?  204 SER A C     1 
ATOM   1655  O  O     . SER A 1 204 ? 150.160 139.477 123.184 1.00 27.44 ?  204 SER A O     1 
ATOM   1656  C  CB    . SER A 1 204 ? 149.436 138.595 120.200 1.00 12.39 ?  204 SER A CB    1 
ATOM   1657  O  OG    . SER A 1 204 ? 148.954 137.594 119.323 1.00 20.84 ?  204 SER A OG    1 
ATOM   1658  N  N     . LYS A 1 205 ? 148.555 140.844 122.396 1.00 18.64 ?  205 LYS A N     1 
ATOM   1659  C  CA    . LYS A 1 205 ? 148.957 141.938 123.270 1.00 21.79 ?  205 LYS A CA    1 
ATOM   1660  C  C     . LYS A 1 205 ? 148.595 141.678 124.724 1.00 22.02 ?  205 LYS A C     1 
ATOM   1661  O  O     . LYS A 1 205 ? 149.194 142.284 125.617 1.00 28.08 ?  205 LYS A O     1 
ATOM   1662  C  CB    . LYS A 1 205 ? 148.323 143.246 122.803 1.00 22.28 ?  205 LYS A CB    1 
ATOM   1663  C  CG    . LYS A 1 205 ? 148.871 143.746 121.486 1.00 21.54 ?  205 LYS A CG    1 
ATOM   1664  C  CD    . LYS A 1 205 ? 148.242 145.063 121.091 1.00 25.34 ?  205 LYS A CD    1 
ATOM   1665  C  CE    . LYS A 1 205 ? 148.942 145.648 119.880 1.00 28.62 ?  205 LYS A CE    1 
ATOM   1666  N  NZ    . LYS A 1 205 ? 148.846 144.755 118.695 1.00 24.12 1  205 LYS A NZ    1 
ATOM   1667  N  N     . LEU A 1 206 ? 147.634 140.795 124.978 1.00 18.83 ?  206 LEU A N     1 
ATOM   1668  C  CA    . LEU A 1 206 ? 147.251 140.470 126.343 1.00 12.03 ?  206 LEU A CA    1 
ATOM   1669  C  C     . LEU A 1 206 ? 148.369 139.706 127.040 1.00 18.40 ?  206 LEU A C     1 
ATOM   1670  O  O     . LEU A 1 206 ? 148.963 138.788 126.471 1.00 24.65 ?  206 LEU A O     1 
ATOM   1671  C  CB    . LEU A 1 206 ? 145.969 139.644 126.345 1.00 16.39 ?  206 LEU A CB    1 
ATOM   1672  C  CG    . LEU A 1 206 ? 144.724 140.365 125.831 1.00 21.56 ?  206 LEU A CG    1 
ATOM   1673  C  CD1   . LEU A 1 206 ? 143.525 139.441 125.881 1.00 19.17 ?  206 LEU A CD1   1 
ATOM   1674  C  CD2   . LEU A 1 206 ? 144.467 141.626 126.633 1.00 21.52 ?  206 LEU A CD2   1 
ATOM   1675  N  N     . ARG A 1 207 ? 148.652 140.091 128.280 1.00 25.76 ?  207 ARG A N     1 
ATOM   1676  C  CA    . ARG A 1 207 ? 149.725 139.452 129.024 1.00 22.21 ?  207 ARG A CA    1 
ATOM   1677  C  C     . ARG A 1 207 ? 149.326 138.040 129.439 1.00 27.34 ?  207 ARG A C     1 
ATOM   1678  O  O     . ARG A 1 207 ? 148.148 137.733 129.639 1.00 33.02 ?  207 ARG A O     1 
ATOM   1679  C  CB    . ARG A 1 207 ? 150.104 140.293 130.243 1.00 25.46 ?  207 ARG A CB    1 
ATOM   1680  C  CG    . ARG A 1 207 ? 149.016 140.467 131.278 1.00 20.93 ?  207 ARG A CG    1 
ATOM   1681  C  CD    . ARG A 1 207 ? 149.439 141.478 132.329 1.00 21.04 ?  207 ARG A CD    1 
ATOM   1682  N  NE    . ARG A 1 207 ? 149.173 142.846 131.902 1.00 29.59 ?  207 ARG A NE    1 
ATOM   1683  C  CZ    . ARG A 1 207 ? 149.247 143.907 132.693 1.00 23.85 ?  207 ARG A CZ    1 
ATOM   1684  N  NH1   . ARG A 1 207 ? 149.596 143.797 133.964 1.00 28.40 1  207 ARG A NH1   1 
ATOM   1685  N  NH2   . ARG A 1 207 ? 148.961 145.107 132.198 1.00 19.28 ?  207 ARG A NH2   1 
ATOM   1686  N  N     . ALA A 1 208 ? 150.330 137.176 129.565 1.00 28.20 ?  208 ALA A N     1 
ATOM   1687  C  CA    . ALA A 1 208 ? 150.104 135.752 129.756 1.00 25.93 ?  208 ALA A CA    1 
ATOM   1688  C  C     . ALA A 1 208 ? 149.657 135.461 131.187 1.00 31.00 ?  208 ALA A C     1 
ATOM   1689  O  O     . ALA A 1 208 ? 149.547 136.353 132.031 1.00 33.88 ?  208 ALA A O     1 
ATOM   1690  C  CB    . ALA A 1 208 ? 151.364 134.966 129.403 1.00 27.47 ?  208 ALA A CB    1 
ATOM   1691  N  N     . LYS A 1 209 ? 149.383 134.189 131.457 1.00 30.80 ?  209 LYS A N     1 
ATOM   1692  C  CA    . LYS A 1 209 ? 148.963 133.781 132.791 1.00 25.81 ?  209 LYS A CA    1 
ATOM   1693  C  C     . LYS A 1 209 ? 150.149 133.814 133.746 1.00 33.73 ?  209 LYS A C     1 
ATOM   1694  O  O     . LYS A 1 209 ? 151.248 133.363 133.406 1.00 34.47 ?  209 LYS A O     1 
ATOM   1695  C  CB    . LYS A 1 209 ? 148.349 132.384 132.752 1.00 28.85 ?  209 LYS A CB    1 
ATOM   1696  C  CG    . LYS A 1 209 ? 147.797 131.916 134.086 1.00 32.40 ?  209 LYS A CG    1 
ATOM   1697  C  CD    . LYS A 1 209 ? 147.621 130.407 134.131 1.00 32.56 ?  209 LYS A CD    1 
ATOM   1698  C  CE    . LYS A 1 209 ? 148.751 129.684 133.416 1.00 35.58 ?  209 LYS A CE    1 
ATOM   1699  N  NZ    . LYS A 1 209 ? 148.534 128.212 133.392 1.00 35.06 1  209 LYS A NZ    1 
ATOM   1700  N  N     . GLY A 1 210 ? 149.923 134.339 134.946 1.00 37.65 ?  210 GLY A N     1 
ATOM   1701  C  CA    . GLY A 1 210 ? 150.986 134.481 135.917 1.00 32.83 ?  210 GLY A CA    1 
ATOM   1702  C  C     . GLY A 1 210 ? 151.756 135.777 135.839 1.00 35.30 ?  210 GLY A C     1 
ATOM   1703  O  O     . GLY A 1 210 ? 152.869 135.850 136.372 1.00 40.60 ?  210 GLY A O     1 
ATOM   1704  N  N     . GLU A 1 211 ? 151.208 136.798 135.191 1.00 33.92 ?  211 GLU A N     1 
ATOM   1705  C  CA    . GLU A 1 211 ? 151.846 138.101 135.097 1.00 31.71 ?  211 GLU A CA    1 
ATOM   1706  C  C     . GLU A 1 211 ? 151.306 139.033 136.175 1.00 34.75 ?  211 GLU A C     1 
ATOM   1707  O  O     . GLU A 1 211 ? 150.354 138.718 136.892 1.00 36.62 ?  211 GLU A O     1 
ATOM   1708  C  CB    . GLU A 1 211 ? 151.638 138.703 133.705 1.00 30.32 ?  211 GLU A CB    1 
ATOM   1709  C  CG    . GLU A 1 211 ? 152.317 137.916 132.604 1.00 33.60 ?  211 GLU A CG    1 
ATOM   1710  C  CD    . GLU A 1 211 ? 153.188 138.781 131.720 1.00 36.43 ?  211 GLU A CD    1 
ATOM   1711  O  OE1   . GLU A 1 211 ? 154.195 139.321 132.224 1.00 39.07 ?  211 GLU A OE1   1 
ATOM   1712  O  OE2   . GLU A 1 211 ? 152.879 138.910 130.518 1.00 30.88 -1 211 GLU A OE2   1 
ATOM   1713  N  N     . ALA A 1 212 ? 151.931 140.202 136.281 1.00 33.78 ?  212 ALA A N     1 
ATOM   1714  C  CA    . ALA A 1 212 ? 151.637 141.137 137.356 1.00 33.97 ?  212 ALA A CA    1 
ATOM   1715  C  C     . ALA A 1 212 ? 150.586 142.156 136.935 1.00 39.38 ?  212 ALA A C     1 
ATOM   1716  O  O     . ALA A 1 212 ? 150.621 142.680 135.818 1.00 41.12 ?  212 ALA A O     1 
ATOM   1717  C  CB    . ALA A 1 212 ? 152.908 141.859 137.802 1.00 35.82 ?  212 ALA A CB    1 
ATOM   1718  N  N     . ILE A 1 213 ? 149.650 142.428 137.841 1.00 32.09 ?  213 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 148.670 143.497 137.687 1.00 34.78 ?  213 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 148.921 144.494 138.809 1.00 36.14 ?  213 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 148.715 144.174 139.987 1.00 40.58 ?  213 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 147.227 142.976 137.725 1.00 34.49 ?  213 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 147.061 141.781 136.785 1.00 34.39 ?  213 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 146.253 144.083 137.361 1.00 29.79 ?  213 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 145.775 141.017 137.000 1.00 30.50 ?  213 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 149.353 145.703 138.447 1.00 41.13 ?  214 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 149.711 146.740 139.417 1.00 40.28 ?  214 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 150.753 146.231 140.410 1.00 46.68 ?  214 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 150.654 146.455 141.619 1.00 49.91 ?  214 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 148.474 147.275 140.140 1.00 40.44 ?  214 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 147.722 148.343 139.366 1.00 40.01 ?  214 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 146.509 148.841 140.131 1.00 42.30 ?  214 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 145.920 150.080 139.475 1.00 44.11 ?  214 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 144.713 150.572 140.194 1.00 42.67 1  214 LYS A NZ    1 
ATOM   1735  N  N     . ASP A 1 215 ? 151.756 145.526 139.885 1.00 47.70 ?  215 ASP A N     1 
ATOM   1736  C  CA    . ASP A 1 215 ? 152.915 145.076 140.661 1.00 49.79 ?  215 ASP A CA    1 
ATOM   1737  C  C     . ASP A 1 215 ? 152.525 144.114 141.782 1.00 48.44 ?  215 ASP A C     1 
ATOM   1738  O  O     . ASP A 1 215 ? 153.115 144.121 142.863 1.00 48.37 ?  215 ASP A O     1 
ATOM   1739  C  CB    . ASP A 1 215 ? 153.704 146.265 141.215 1.00 48.76 ?  215 ASP A CB    1 
ATOM   1740  C  CG    . ASP A 1 215 ? 154.150 147.226 140.130 1.00 52.47 ?  215 ASP A CG    1 
ATOM   1741  O  OD1   . ASP A 1 215 ? 154.563 146.753 139.051 1.00 51.00 ?  215 ASP A OD1   1 
ATOM   1742  O  OD2   . ASP A 1 215 ? 154.090 148.453 140.355 1.00 51.63 -1 215 ASP A OD2   1 
ATOM   1743  N  N     . VAL A 1 216 ? 151.523 143.275 141.527 1.00 43.69 ?  216 VAL A N     1 
ATOM   1744  C  CA    . VAL A 1 216 ? 151.233 142.116 142.364 1.00 45.86 ?  216 VAL A CA    1 
ATOM   1745  C  C     . VAL A 1 216 ? 151.405 140.875 141.495 1.00 46.94 ?  216 VAL A C     1 
ATOM   1746  O  O     . VAL A 1 216 ? 150.926 140.834 140.357 1.00 49.98 ?  216 VAL A O     1 
ATOM   1747  C  CB    . VAL A 1 216 ? 149.833 142.198 143.015 1.00 44.85 ?  216 VAL A CB    1 
ATOM   1748  C  CG1   . VAL A 1 216 ? 149.363 143.646 143.099 1.00 43.90 ?  216 VAL A CG1   1 
ATOM   1749  C  CG2   . VAL A 1 216 ? 148.799 141.327 142.309 1.00 43.37 ?  216 VAL A CG2   1 
ATOM   1750  N  N     . GLU A 1 217 ? 152.150 139.899 142.004 1.00 48.48 ?  217 GLU A N     1 
ATOM   1751  C  CA    . GLU A 1 217 ? 152.648 138.817 141.168 1.00 48.13 ?  217 GLU A CA    1 
ATOM   1752  C  C     . GLU A 1 217 ? 151.616 137.702 141.017 1.00 49.28 ?  217 GLU A C     1 
ATOM   1753  O  O     . GLU A 1 217 ? 150.733 137.514 141.859 1.00 51.39 ?  217 GLU A O     1 
ATOM   1754  C  CB    . GLU A 1 217 ? 153.947 138.251 141.743 1.00 50.28 ?  217 GLU A CB    1 
ATOM   1755  C  CG    . GLU A 1 217 ? 155.005 139.293 142.090 1.00 50.51 ?  217 GLU A CG    1 
ATOM   1756  C  CD    . GLU A 1 217 ? 155.012 140.476 141.137 1.00 52.26 ?  217 GLU A CD    1 
ATOM   1757  O  OE1   . GLU A 1 217 ? 155.618 140.361 140.052 1.00 53.56 ?  217 GLU A OE1   1 
ATOM   1758  O  OE2   . GLU A 1 217 ? 154.420 141.521 141.478 1.00 49.24 -1 217 GLU A OE2   1 
ATOM   1759  N  N     . ASN A 1 218 ? 151.753 136.954 139.918 1.00 44.02 ?  218 ASN A N     1 
ATOM   1760  C  CA    . ASN A 1 218 ? 150.927 135.777 139.633 1.00 44.04 ?  218 ASN A CA    1 
ATOM   1761  C  C     . ASN A 1 218 ? 149.438 136.114 139.674 1.00 47.82 ?  218 ASN A C     1 
ATOM   1762  O  O     . ASN A 1 218 ? 148.630 135.369 140.230 1.00 46.76 ?  218 ASN A O     1 
ATOM   1763  C  CB    . ASN A 1 218 ? 151.253 134.632 140.592 1.00 43.02 ?  218 ASN A CB    1 
ATOM   1764  C  CG    . ASN A 1 218 ? 151.244 133.279 139.909 1.00 48.15 ?  218 ASN A CG    1 
ATOM   1765  O  OD1   . ASN A 1 218 ? 151.822 133.110 138.834 1.00 50.06 ?  218 ASN A OD1   1 
ATOM   1766  N  ND2   . ASN A 1 218 ? 150.588 132.306 140.530 1.00 47.54 ?  218 ASN A ND2   1 
ATOM   1767  N  N     . ALA A 1 219 ? 149.073 137.246 139.076 1.00 38.03 ?  219 ALA A N     1 
ATOM   1768  C  CA    . ALA A 1 219 ? 147.710 137.753 139.155 1.00 33.65 ?  219 ALA A CA    1 
ATOM   1769  C  C     . ALA A 1 219 ? 146.914 137.572 137.873 1.00 35.31 ?  219 ALA A C     1 
ATOM   1770  O  O     . ALA A 1 219 ? 145.695 137.383 137.939 1.00 36.61 ?  219 ALA A O     1 
ATOM   1771  C  CB    . ALA A 1 219 ? 147.727 139.239 139.522 1.00 35.87 ?  219 ALA A CB    1 
ATOM   1772  N  N     . THR A 1 220 ? 147.563 137.625 136.715 1.00 36.45 ?  220 THR A N     1 
ATOM   1773  C  CA    . THR A 1 220 ? 146.841 137.567 135.453 1.00 30.45 ?  220 THR A CA    1 
ATOM   1774  C  C     . THR A 1 220 ? 146.316 136.160 135.192 1.00 34.14 ?  220 THR A C     1 
ATOM   1775  O  O     . THR A 1 220 ? 146.993 135.165 135.463 1.00 35.22 ?  220 THR A O     1 
ATOM   1776  C  CB    . THR A 1 220 ? 147.747 138.009 134.304 1.00 27.27 ?  220 THR A CB    1 
ATOM   1777  O  OG1   . THR A 1 220 ? 148.348 139.269 134.627 1.00 35.48 ?  220 THR A OG1   1 
ATOM   1778  C  CG2   . THR A 1 220 ? 146.947 138.158 133.022 1.00 29.46 ?  220 THR A CG2   1 
ATOM   1779  N  N     . LYS A 1 221 ? 145.095 136.085 134.661 1.00 35.92 ?  221 LYS A N     1 
ATOM   1780  C  CA    . LYS A 1 221 ? 144.513 134.814 134.255 1.00 30.05 ?  221 LYS A CA    1 
ATOM   1781  C  C     . LYS A 1 221 ? 144.975 134.369 132.875 1.00 33.95 ?  221 LYS A C     1 
ATOM   1782  O  O     . LYS A 1 221 ? 144.673 133.240 132.473 1.00 40.03 ?  221 LYS A O     1 
ATOM   1783  C  CB    . LYS A 1 221 ? 142.986 134.902 134.277 1.00 29.97 ?  221 LYS A CB    1 
ATOM   1784  C  CG    . LYS A 1 221 ? 142.393 134.980 135.667 1.00 32.25 ?  221 LYS A CG    1 
ATOM   1785  C  CD    . LYS A 1 221 ? 141.039 134.299 135.724 1.00 33.02 ?  221 LYS A CD    1 
ATOM   1786  C  CE    . LYS A 1 221 ? 140.625 134.024 137.156 1.00 33.42 ?  221 LYS A CE    1 
ATOM   1787  N  NZ    . LYS A 1 221 ? 139.432 133.136 137.228 1.00 36.29 1  221 LYS A NZ    1 
ATOM   1788  N  N     . GLY A 1 222 ? 145.690 135.218 132.149 1.00 31.76 ?  222 GLY A N     1 
ATOM   1789  C  CA    . GLY A 1 222 ? 146.137 134.881 130.819 1.00 26.99 ?  222 GLY A CA    1 
ATOM   1790  C  C     . GLY A 1 222 ? 145.078 135.158 129.771 1.00 27.61 ?  222 GLY A C     1 
ATOM   1791  O  O     . GLY A 1 222 ? 144.033 135.762 130.026 1.00 33.53 ?  222 GLY A O     1 
ATOM   1792  N  N     . VAL A 1 223 ? 145.370 134.699 128.553 1.00 25.41 ?  223 VAL A N     1 
ATOM   1793  C  CA    . VAL A 1 223 ? 144.424 134.877 127.460 1.00 24.51 ?  223 VAL A CA    1 
ATOM   1794  C  C     . VAL A 1 223 ? 143.292 133.863 127.509 1.00 18.93 ?  223 VAL A C     1 
ATOM   1795  O  O     . VAL A 1 223 ? 142.280 134.055 126.829 1.00 22.69 ?  223 VAL A O     1 
ATOM   1796  C  CB    . VAL A 1 223 ? 145.132 134.808 126.096 1.00 22.73 ?  223 VAL A CB    1 
ATOM   1797  C  CG1   . VAL A 1 223 ? 146.395 135.646 126.112 1.00 20.06 ?  223 VAL A CG1   1 
ATOM   1798  C  CG2   . VAL A 1 223 ? 145.444 133.367 125.726 1.00 20.14 ?  223 VAL A CG2   1 
ATOM   1799  N  N     . VAL A 1 224 ? 143.421 132.795 128.297 1.00 27.29 ?  224 VAL A N     1 
ATOM   1800  C  CA    . VAL A 1 224 ? 142.368 131.786 128.346 1.00 23.25 ?  224 VAL A CA    1 
ATOM   1801  C  C     . VAL A 1 224 ? 141.123 132.315 129.055 1.00 27.16 ?  224 VAL A C     1 
ATOM   1802  O  O     . VAL A 1 224 ? 139.996 132.013 128.643 1.00 29.49 ?  224 VAL A O     1 
ATOM   1803  C  CB    . VAL A 1 224 ? 142.895 130.501 129.005 1.00 30.45 ?  224 VAL A CB    1 
ATOM   1804  C  CG1   . VAL A 1 224 ? 141.793 129.462 129.114 1.00 28.30 ?  224 VAL A CG1   1 
ATOM   1805  C  CG2   . VAL A 1 224 ? 144.062 129.950 128.207 1.00 28.17 ?  224 VAL A CG2   1 
ATOM   1806  N  N     . GLY A 1 225 ? 141.288 133.105 130.116 1.00 26.05 ?  225 GLY A N     1 
ATOM   1807  C  CA    . GLY A 1 225 ? 140.131 133.729 130.742 1.00 23.64 ?  225 GLY A CA    1 
ATOM   1808  C  C     . GLY A 1 225 ? 139.437 134.709 129.817 1.00 21.95 ?  225 GLY A C     1 
ATOM   1809  O  O     . GLY A 1 225 ? 138.204 134.790 129.784 1.00 29.10 ?  225 GLY A O     1 
ATOM   1810  N  N     . VAL A 1 226 ? 140.220 135.465 129.045 1.00 22.04 ?  226 VAL A N     1 
ATOM   1811  C  CA    . VAL A 1 226 ? 139.645 136.366 128.053 1.00 21.14 ?  226 VAL A CA    1 
ATOM   1812  C  C     . VAL A 1 226 ? 138.911 135.573 126.981 1.00 19.41 ?  226 VAL A C     1 
ATOM   1813  O  O     . VAL A 1 226 ? 137.864 135.998 126.483 1.00 22.12 ?  226 VAL A O     1 
ATOM   1814  C  CB    . VAL A 1 226 ? 140.739 137.262 127.447 1.00 19.03 ?  226 VAL A CB    1 
ATOM   1815  C  CG1   . VAL A 1 226 ? 140.120 138.317 126.544 1.00 26.23 ?  226 VAL A CG1   1 
ATOM   1816  C  CG2   . VAL A 1 226 ? 141.557 137.907 128.547 1.00 16.46 ?  226 VAL A CG2   1 
ATOM   1817  N  N     . MET A 1 227 ? 139.450 134.410 126.608 1.00 21.13 ?  227 MET A N     1 
ATOM   1818  C  CA    . MET A 1 227 ? 138.767 133.557 125.640 1.00 23.66 ?  227 MET A CA    1 
ATOM   1819  C  C     . MET A 1 227 ? 137.457 133.029 126.200 1.00 23.17 ?  227 MET A C     1 
ATOM   1820  O  O     . MET A 1 227 ? 136.472 132.913 125.469 1.00 28.48 ?  227 MET A O     1 
ATOM   1821  C  CB    . MET A 1 227 ? 139.663 132.396 125.215 1.00 20.13 ?  227 MET A CB    1 
ATOM   1822  C  CG    . MET A 1 227 ? 140.883 132.803 124.424 1.00 17.73 ?  227 MET A CG    1 
ATOM   1823  S  SD    . MET A 1 227 ? 142.080 131.469 124.330 1.00 36.51 ?  227 MET A SD    1 
ATOM   1824  C  CE    . MET A 1 227 ? 141.192 130.324 123.283 1.00 24.79 ?  227 MET A CE    1 
ATOM   1825  N  N     . LYS A 1 228 ? 137.431 132.680 127.486 1.00 21.26 ?  228 LYS A N     1 
ATOM   1826  C  CA    . LYS A 1 228 ? 136.180 132.254 128.108 1.00 22.96 ?  228 LYS A CA    1 
ATOM   1827  C  C     . LYS A 1 228 ? 135.153 133.379 128.093 1.00 21.81 ?  228 LYS A C     1 
ATOM   1828  O  O     . LYS A 1 228 ? 133.974 133.157 127.782 1.00 24.62 ?  228 LYS A O     1 
ATOM   1829  C  CB    . LYS A 1 228 ? 136.433 131.787 129.541 1.00 24.81 ?  228 LYS A CB    1 
ATOM   1830  C  CG    . LYS A 1 228 ? 136.977 130.376 129.656 1.00 27.57 ?  228 LYS A CG    1 
ATOM   1831  C  CD    . LYS A 1 228 ? 137.452 130.099 131.074 1.00 30.30 ?  228 LYS A CD    1 
ATOM   1832  C  CE    . LYS A 1 228 ? 138.957 130.265 131.197 1.00 31.49 ?  228 LYS A CE    1 
ATOM   1833  N  NZ    . LYS A 1 228 ? 139.374 130.692 132.561 1.00 27.84 1  228 LYS A NZ    1 
ATOM   1834  N  N     . LEU A 1 229 ? 135.588 134.599 128.421 1.00 20.71 ?  229 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 229 ? 134.688 135.748 128.377 1.00 18.79 ?  229 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 229 ? 134.157 135.978 126.968 1.00 20.13 ?  229 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 229 ? 132.960 136.216 126.770 1.00 18.55 ?  229 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 229 ? 135.410 136.995 128.884 1.00 20.16 ?  229 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 229 ? 135.634 137.130 130.388 1.00 18.98 ?  229 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 229 ? 136.551 138.305 130.663 1.00 21.66 ?  229 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 229 ? 134.311 137.306 131.103 1.00 18.33 ?  229 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 230 ? 135.042 135.910 125.971 1.00 24.97 ?  230 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 230 ? 134.632 136.117 124.588 1.00 16.02 ?  230 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 230 ? 133.704 135.009 124.112 1.00 15.64 ?  230 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 230 ? 132.757 135.267 123.366 1.00 30.75 ?  230 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 230 ? 135.861 136.213 123.685 1.00 23.37 ?  230 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 230 ? 136.692 137.488 123.823 1.00 22.41 ?  230 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 230 ? 137.995 137.361 123.048 1.00 23.43 ?  230 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 230 ? 135.899 138.698 123.358 1.00 16.74 ?  230 LEU A CD2   1 
ATOM   1850  N  N     . ASP A 1 231 ? 133.968 133.769 124.522 1.00 23.35 ?  231 ASP A N     1 
ATOM   1851  C  CA    . ASP A 1 231 ? 133.099 132.659 124.151 1.00 23.77 ?  231 ASP A CA    1 
ATOM   1852  C  C     . ASP A 1 231 ? 131.707 132.839 124.738 1.00 22.03 ?  231 ASP A C     1 
ATOM   1853  O  O     . ASP A 1 231 ? 130.705 132.596 124.058 1.00 29.84 ?  231 ASP A O     1 
ATOM   1854  C  CB    . ASP A 1 231 ? 133.718 131.338 124.609 1.00 23.08 ?  231 ASP A CB    1 
ATOM   1855  C  CG    . ASP A 1 231 ? 132.799 130.155 124.391 1.00 36.05 ?  231 ASP A CG    1 
ATOM   1856  O  OD1   . ASP A 1 231 ? 132.366 129.941 123.239 1.00 42.35 ?  231 ASP A OD1   1 
ATOM   1857  O  OD2   . ASP A 1 231 ? 132.514 129.434 125.371 1.00 33.33 -1 231 ASP A OD2   1 
ATOM   1858  N  N     . ASN A 1 232 ? 131.624 133.280 125.995 1.00 27.62 ?  232 ASN A N     1 
ATOM   1859  C  CA    . ASN A 1 232 ? 130.316 133.571 126.577 1.00 25.45 ?  232 ASN A CA    1 
ATOM   1860  C  C     . ASN A 1 232 ? 129.628 134.718 125.847 1.00 21.44 ?  232 ASN A C     1 
ATOM   1861  O  O     . ASN A 1 232 ? 128.415 134.671 125.608 1.00 28.17 ?  232 ASN A O     1 
ATOM   1862  C  CB    . ASN A 1 232 ? 130.457 133.884 128.065 1.00 26.42 ?  232 ASN A CB    1 
ATOM   1863  C  CG    . ASN A 1 232 ? 129.486 133.093 128.915 1.00 32.00 ?  232 ASN A CG    1 
ATOM   1864  O  OD1   . ASN A 1 232 ? 128.276 133.299 128.847 1.00 34.71 ?  232 ASN A OD1   1 
ATOM   1865  N  ND2   . ASN A 1 232 ? 130.009 132.166 129.705 1.00 34.25 ?  232 ASN A ND2   1 
ATOM   1866  N  N     . ALA A 1 233 ? 130.386 135.755 125.487 1.00 17.49 ?  233 ALA A N     1 
ATOM   1867  C  CA    . ALA A 1 233 ? 129.807 136.883 124.766 1.00 19.25 ?  233 ALA A CA    1 
ATOM   1868  C  C     . ALA A 1 233 ? 129.271 136.458 123.404 1.00 27.61 ?  233 ALA A C     1 
ATOM   1869  O  O     . ALA A 1 233 ? 128.210 136.922 122.972 1.00 27.48 ?  233 ALA A O     1 
ATOM   1870  C  CB    . ALA A 1 233 ? 130.845 137.994 124.613 1.00 19.50 ?  233 ALA A CB    1 
ATOM   1871  N  N     . PHE A 1 234 ? 129.998 135.581 122.708 1.00 25.88 ?  234 PHE A N     1 
ATOM   1872  C  CA    . PHE A 1 234 ? 129.562 135.127 121.394 1.00 18.99 ?  234 PHE A CA    1 
ATOM   1873  C  C     . PHE A 1 234 ? 128.395 134.156 121.493 1.00 22.17 ?  234 PHE A C     1 
ATOM   1874  O  O     . PHE A 1 234 ? 127.536 134.131 120.605 1.00 29.06 ?  234 PHE A O     1 
ATOM   1875  C  CB    . PHE A 1 234 ? 130.727 134.486 120.641 1.00 24.21 ?  234 PHE A CB    1 
ATOM   1876  C  CG    . PHE A 1 234 ? 131.698 135.480 120.072 1.00 22.59 ?  234 PHE A CG    1 
ATOM   1877  C  CD1   . PHE A 1 234 ? 131.275 136.451 119.183 1.00 21.43 ?  234 PHE A CD1   1 
ATOM   1878  C  CD2   . PHE A 1 234 ? 133.035 135.441 120.422 1.00 21.36 ?  234 PHE A CD2   1 
ATOM   1879  C  CE1   . PHE A 1 234 ? 132.167 137.367 118.662 1.00 20.43 ?  234 PHE A CE1   1 
ATOM   1880  C  CE2   . PHE A 1 234 ? 133.929 136.355 119.906 1.00 22.33 ?  234 PHE A CE2   1 
ATOM   1881  C  CZ    . PHE A 1 234 ? 133.495 137.318 119.023 1.00 22.81 ?  234 PHE A CZ    1 
ATOM   1882  N  N     . ARG A 1 235 ? 128.345 133.346 122.553 1.00 24.66 ?  235 ARG A N     1 
ATOM   1883  C  CA    . ARG A 1 235 ? 127.171 132.511 122.778 1.00 25.84 ?  235 ARG A CA    1 
ATOM   1884  C  C     . ARG A 1 235 ? 125.943 133.367 123.050 1.00 31.07 ?  235 ARG A C     1 
ATOM   1885  O  O     . ARG A 1 235 ? 124.846 133.063 122.570 1.00 39.35 ?  235 ARG A O     1 
ATOM   1886  C  CB    . ARG A 1 235 ? 127.419 131.547 123.937 1.00 26.56 ?  235 ARG A CB    1 
ATOM   1887  C  CG    . ARG A 1 235 ? 128.433 130.461 123.636 1.00 32.06 ?  235 ARG A CG    1 
ATOM   1888  C  CD    . ARG A 1 235 ? 128.340 129.323 124.635 1.00 31.55 ?  235 ARG A CD    1 
ATOM   1889  N  NE    . ARG A 1 235 ? 129.550 129.214 125.441 1.00 33.93 ?  235 ARG A NE    1 
ATOM   1890  C  CZ    . ARG A 1 235 ? 129.727 129.820 126.607 1.00 35.96 ?  235 ARG A CZ    1 
ATOM   1891  N  NH1   . ARG A 1 235 ? 128.786 130.581 127.139 1.00 35.78 1  235 ARG A NH1   1 
ATOM   1892  N  NH2   . ARG A 1 235 ? 130.878 129.658 127.253 1.00 33.53 ?  235 ARG A NH2   1 
ATOM   1893  N  N     . TYR A 1 236 ? 126.110 134.445 123.819 1.00 25.37 ?  236 TYR A N     1 
ATOM   1894  C  CA    . TYR A 1 236 ? 124.981 135.314 124.130 1.00 21.11 ?  236 TYR A CA    1 
ATOM   1895  C  C     . TYR A 1 236 ? 124.482 136.044 122.888 1.00 24.21 ?  236 TYR A C     1 
ATOM   1896  O  O     . TYR A 1 236 ? 123.274 136.102 122.633 1.00 24.55 ?  236 TYR A O     1 
ATOM   1897  C  CB    . TYR A 1 236 ? 125.375 136.314 125.216 1.00 19.94 ?  236 TYR A CB    1 
ATOM   1898  C  CG    . TYR A 1 236 ? 124.217 137.135 125.722 1.00 23.99 ?  236 TYR A CG    1 
ATOM   1899  C  CD1   . TYR A 1 236 ? 123.269 136.579 126.566 1.00 21.35 ?  236 TYR A CD1   1 
ATOM   1900  C  CD2   . TYR A 1 236 ? 124.070 138.465 125.352 1.00 24.85 ?  236 TYR A CD2   1 
ATOM   1901  C  CE1   . TYR A 1 236 ? 122.209 137.321 127.032 1.00 24.71 ?  236 TYR A CE1   1 
ATOM   1902  C  CE2   . TYR A 1 236 ? 123.010 139.216 125.813 1.00 16.98 ?  236 TYR A CE2   1 
ATOM   1903  C  CZ    . TYR A 1 236 ? 122.083 138.637 126.653 1.00 21.52 ?  236 TYR A CZ    1 
ATOM   1904  O  OH    . TYR A 1 236 ? 121.024 139.373 127.119 1.00 25.78 ?  236 TYR A OH    1 
ATOM   1905  N  N     . ALA A 1 237 ? 125.397 136.608 122.103 1.00 30.61 ?  237 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 237 ? 125.050 137.366 120.901 1.00 30.91 ?  237 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 237 ? 125.081 136.406 119.717 1.00 35.59 ?  237 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 237 ? 126.132 136.142 119.132 1.00 39.55 ?  237 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 237 ? 126.002 138.540 120.707 1.00 30.89 ?  237 ALA A CB    1 
ATOM   1910  N  N     . ASP A 1 238 ? 123.911 135.887 119.357 1.00 50.35 ?  238 ASP A N     1 
ATOM   1911  C  CA    . ASP A 1 238 ? 123.780 134.857 118.331 1.00 54.69 ?  238 ASP A CA    1 
ATOM   1912  C  C     . ASP A 1 238 ? 122.724 135.251 117.303 1.00 59.58 ?  238 ASP A C     1 
ATOM   1913  O  O     . ASP A 1 238 ? 121.847 134.463 116.940 1.00 59.96 ?  238 ASP A O     1 
ATOM   1914  C  CB    . ASP A 1 238 ? 123.451 133.510 118.966 1.00 52.63 ?  238 ASP A CB    1 
ATOM   1915  C  CG    . ASP A 1 238 ? 122.261 133.580 119.899 1.00 55.48 ?  238 ASP A CG    1 
ATOM   1916  O  OD1   . ASP A 1 238 ? 121.829 134.704 120.231 1.00 55.79 ?  238 ASP A OD1   1 
ATOM   1917  O  OD2   . ASP A 1 238 ? 121.755 132.512 120.303 1.00 56.24 -1 238 ASP A OD2   1 
ATOM   1918  N  N     . GLN A 1 239 ? 122.804 136.495 116.820 1.00 65.05 ?  239 GLN A N     1 
ATOM   1919  C  CA    . GLN A 1 239 ? 121.919 137.004 115.768 1.00 64.51 ?  239 GLN A CA    1 
ATOM   1920  C  C     . GLN A 1 239 ? 120.446 136.843 116.136 1.00 64.87 ?  239 GLN A C     1 
ATOM   1921  O  O     . GLN A 1 239 ? 119.633 136.365 115.341 1.00 64.37 ?  239 GLN A O     1 
ATOM   1922  C  CB    . GLN A 1 239 ? 122.214 136.332 114.424 1.00 64.27 ?  239 GLN A CB    1 
ATOM   1923  C  CG    . GLN A 1 239 ? 123.329 136.975 113.627 1.00 63.60 ?  239 GLN A CG    1 
ATOM   1924  C  CD    . GLN A 1 239 ? 123.095 136.878 112.130 1.00 65.72 ?  239 GLN A CD    1 
ATOM   1925  O  OE1   . GLN A 1 239 ? 121.997 137.147 111.644 1.00 65.94 ?  239 GLN A OE1   1 
ATOM   1926  N  NE2   . GLN A 1 239 ? 124.127 136.484 111.393 1.00 64.99 ?  239 GLN A NE2   1 
ATOM   1927  N  N     . MET A 1 240 ? 120.103 137.253 117.359 1.00 68.51 ?  240 MET A N     1 
ATOM   1928  C  CA    . MET A 1 240 ? 118.731 137.165 117.861 1.00 68.14 ?  240 MET A CA    1 
ATOM   1929  C  C     . MET A 1 240 ? 118.212 135.729 117.809 1.00 69.94 ?  240 MET A C     1 
ATOM   1930  O  O     . MET A 1 240 ? 117.058 135.477 117.453 1.00 68.89 ?  240 MET A O     1 
ATOM   1931  C  CB    . MET A 1 240 ? 117.799 138.106 117.092 1.00 66.92 ?  240 MET A CB    1 
ATOM   1932  C  CG    . MET A 1 240 ? 118.027 139.583 117.363 1.00 68.38 ?  240 MET A CG    1 
ATOM   1933  S  SD    . MET A 1 240 ? 119.759 140.069 117.266 1.00 73.97 ?  240 MET A SD    1 
ATOM   1934  C  CE    . MET A 1 240 ? 119.589 141.816 116.916 1.00 65.29 ?  240 MET A CE    1 
ATOM   1935  N  N     . GLY A 1 241 ? 119.071 134.780 118.165 1.00 69.79 ?  241 GLY A N     1 
ATOM   1936  C  CA    . GLY A 1 241 ? 118.691 133.378 118.165 1.00 68.54 ?  241 GLY A CA    1 
ATOM   1937  C  C     . GLY A 1 241 ? 118.411 132.795 116.796 1.00 70.57 ?  241 GLY A C     1 
ATOM   1938  O  O     . GLY A 1 241 ? 117.457 132.023 116.640 1.00 71.99 ?  241 GLY A O     1 
ATOM   1939  N  N     . GLN A 1 242 ? 119.221 133.143 115.797 1.00 72.20 ?  242 GLN A N     1 
ATOM   1940  C  CA    . GLN A 1 242 ? 119.084 132.600 114.452 1.00 72.85 ?  242 GLN A CA    1 
ATOM   1941  C  C     . GLN A 1 242 ? 120.264 131.712 114.077 1.00 73.98 ?  242 GLN A C     1 
ATOM   1942  O  O     . GLN A 1 242 ? 120.071 130.560 113.678 1.00 74.28 ?  242 GLN A O     1 
ATOM   1943  C  CB    . GLN A 1 242 ? 118.923 133.740 113.437 1.00 72.37 ?  242 GLN A CB    1 
ATOM   1944  C  CG    . GLN A 1 242 ? 117.642 134.541 113.606 1.00 73.86 ?  242 GLN A CG    1 
ATOM   1945  C  CD    . GLN A 1 242 ? 117.300 135.360 112.379 1.00 75.01 ?  242 GLN A CD    1 
ATOM   1946  O  OE1   . GLN A 1 242 ? 117.911 135.201 111.322 1.00 75.76 ?  242 GLN A OE1   1 
ATOM   1947  N  NE2   . GLN A 1 242 ? 116.320 136.245 112.513 1.00 73.28 ?  242 GLN A NE2   1 
ATOM   1948  N  N     . ARG A 1 243 ? 121.487 132.220 114.198 1.00 64.01 ?  243 ARG A N     1 
ATOM   1949  C  CA    . ARG A 1 243 ? 122.692 131.450 113.936 1.00 63.58 ?  243 ARG A CA    1 
ATOM   1950  C  C     . ARG A 1 243 ? 123.558 131.426 115.188 1.00 62.97 ?  243 ARG A C     1 
ATOM   1951  O  O     . ARG A 1 243 ? 123.475 132.321 116.033 1.00 61.17 ?  243 ARG A O     1 
ATOM   1952  C  CB    . ARG A 1 243 ? 123.471 132.024 112.724 1.00 62.81 ?  243 ARG A CB    1 
ATOM   1953  C  CG    . ARG A 1 243 ? 124.027 133.456 112.863 1.00 63.98 ?  243 ARG A CG    1 
ATOM   1954  C  CD    . ARG A 1 243 ? 125.315 133.529 113.679 1.00 64.32 ?  243 ARG A CD    1 
ATOM   1955  N  NE    . ARG A 1 243 ? 125.811 134.888 113.852 1.00 65.06 ?  243 ARG A NE    1 
ATOM   1956  C  CZ    . ARG A 1 243 ? 126.817 135.412 113.168 1.00 64.23 ?  243 ARG A CZ    1 
ATOM   1957  N  NH1   . ARG A 1 243 ? 127.457 134.721 112.238 1.00 63.32 1  243 ARG A NH1   1 
ATOM   1958  N  NH2   . ARG A 1 243 ? 127.197 136.660 113.426 1.00 60.04 ?  243 ARG A NH2   1 
ATOM   1959  N  N     . GLN A 1 244 ? 124.390 130.395 115.302 1.00 64.35 ?  244 GLN A N     1 
ATOM   1960  C  CA    . GLN A 1 244 ? 125.297 130.295 116.437 1.00 62.85 ?  244 GLN A CA    1 
ATOM   1961  C  C     . GLN A 1 244 ? 126.375 131.367 116.343 1.00 62.96 ?  244 GLN A C     1 
ATOM   1962  O  O     . GLN A 1 244 ? 127.037 131.504 115.310 1.00 60.03 ?  244 GLN A O     1 
ATOM   1963  C  CB    . GLN A 1 244 ? 125.937 128.909 116.489 1.00 60.75 ?  244 GLN A CB    1 
ATOM   1964  C  CG    . GLN A 1 244 ? 125.029 127.817 117.028 1.00 62.26 ?  244 GLN A CG    1 
ATOM   1965  C  CD    . GLN A 1 244 ? 125.807 126.646 117.596 1.00 64.17 ?  244 GLN A CD    1 
ATOM   1966  O  OE1   . GLN A 1 244 ? 126.812 126.219 117.028 1.00 64.37 ?  244 GLN A OE1   1 
ATOM   1967  N  NE2   . GLN A 1 244 ? 125.345 126.121 118.725 1.00 61.33 ?  244 GLN A NE2   1 
ATOM   1968  N  N     . GLY A 1 245 ? 126.557 132.119 117.427 1.00 50.20 ?  245 GLY A N     1 
ATOM   1969  C  CA    . GLY A 1 245 ? 127.549 133.177 117.456 1.00 46.90 ?  245 GLY A CA    1 
ATOM   1970  C  C     . GLY A 1 245 ? 128.948 132.669 117.176 1.00 45.73 ?  245 GLY A C     1 
ATOM   1971  O  O     . GLY A 1 245 ? 129.451 131.793 117.884 1.00 43.83 ?  245 GLY A O     1 
ATOM   1972  N  N     . SER A 1 246 ? 129.586 133.218 116.147 1.00 40.73 ?  246 SER A N     1 
ATOM   1973  C  CA    . SER A 1 246 ? 130.873 132.737 115.667 1.00 32.62 ?  246 SER A CA    1 
ATOM   1974  C  C     . SER A 1 246 ? 131.939 133.784 115.951 1.00 31.43 ?  246 SER A C     1 
ATOM   1975  O  O     . SER A 1 246 ? 131.808 134.940 115.533 1.00 30.78 ?  246 SER A O     1 
ATOM   1976  C  CB    . SER A 1 246 ? 130.815 132.422 114.173 1.00 32.71 ?  246 SER A CB    1 
ATOM   1977  O  OG    . SER A 1 246 ? 129.929 131.348 113.910 1.00 44.32 ?  246 SER A OG    1 
ATOM   1978  N  N     . GLY A 1 247 ? 132.991 133.375 116.654 1.00 28.96 ?  247 GLY A N     1 
ATOM   1979  C  CA    . GLY A 1 247 ? 134.102 134.257 116.931 1.00 13.13 ?  247 GLY A CA    1 
ATOM   1980  C  C     . GLY A 1 247 ? 135.415 133.514 116.793 1.00 15.41 ?  247 GLY A C     1 
ATOM   1981  O  O     . GLY A 1 247 ? 135.475 132.286 116.886 1.00 23.68 ?  247 GLY A O     1 
ATOM   1982  N  N     . ALA A 1 248 ? 136.469 134.287 116.563 1.00 17.67 ?  248 ALA A N     1 
ATOM   1983  C  CA    . ALA A 1 248 ? 137.812 133.755 116.419 1.00 14.46 ?  248 ALA A CA    1 
ATOM   1984  C  C     . ALA A 1 248 ? 138.761 134.525 117.322 1.00 12.56 ?  248 ALA A C     1 
ATOM   1985  O  O     . ALA A 1 248 ? 138.603 135.728 117.533 1.00 16.39 ?  248 ALA A O     1 
ATOM   1986  C  CB    . ALA A 1 248 ? 138.300 133.828 114.965 1.00 8.12  ?  248 ALA A CB    1 
ATOM   1987  N  N     . ALA A 1 249 ? 139.747 133.814 117.856 1.00 16.30 ?  249 ALA A N     1 
ATOM   1988  C  CA    . ALA A 1 249 ? 140.798 134.407 118.670 1.00 5.45  ?  249 ALA A CA    1 
ATOM   1989  C  C     . ALA A 1 249 ? 142.144 134.026 118.076 1.00 11.13 ?  249 ALA A C     1 
ATOM   1990  O  O     . ALA A 1 249 ? 142.386 132.852 117.784 1.00 19.26 ?  249 ALA A O     1 
ATOM   1991  C  CB    . ALA A 1 249 ? 140.702 133.943 120.126 1.00 13.03 ?  249 ALA A CB    1 
ATOM   1992  N  N     . TYR A 1 250 ? 143.010 135.014 117.891 1.00 15.80 ?  250 TYR A N     1 
ATOM   1993  C  CA    . TYR A 1 250 ? 144.335 134.793 117.335 1.00 9.77  ?  250 TYR A CA    1 
ATOM   1994  C  C     . TYR A 1 250 ? 145.388 135.106 118.386 1.00 6.64  ?  250 TYR A C     1 
ATOM   1995  O  O     . TYR A 1 250 ? 145.315 136.140 119.058 1.00 17.12 ?  250 TYR A O     1 
ATOM   1996  C  CB    . TYR A 1 250 ? 144.560 135.647 116.089 1.00 10.64 ?  250 TYR A CB    1 
ATOM   1997  C  CG    . TYR A 1 250 ? 144.017 135.028 114.824 1.00 17.03 ?  250 TYR A CG    1 
ATOM   1998  C  CD1   . TYR A 1 250 ? 142.662 135.077 114.533 1.00 11.39 ?  250 TYR A CD1   1 
ATOM   1999  C  CD2   . TYR A 1 250 ? 144.859 134.390 113.923 1.00 13.62 ?  250 TYR A CD2   1 
ATOM   2000  C  CE1   . TYR A 1 250 ? 142.160 134.513 113.381 1.00 5.03  ?  250 TYR A CE1   1 
ATOM   2001  C  CE2   . TYR A 1 250 ? 144.364 133.821 112.768 1.00 9.66  ?  250 TYR A CE2   1 
ATOM   2002  C  CZ    . TYR A 1 250 ? 143.015 133.886 112.502 1.00 8.96  ?  250 TYR A CZ    1 
ATOM   2003  O  OH    . TYR A 1 250 ? 142.515 133.326 111.351 1.00 16.52 ?  250 TYR A OH    1 
ATOM   2004  N  N     . LEU A 1 251 ? 146.356 134.210 118.525 1.00 11.05 ?  251 LEU A N     1 
ATOM   2005  C  CA    . LEU A 1 251 ? 147.465 134.385 119.445 1.00 13.94 ?  251 LEU A CA    1 
ATOM   2006  C  C     . LEU A 1 251 ? 148.768 134.112 118.714 1.00 11.63 ?  251 LEU A C     1 
ATOM   2007  O  O     . LEU A 1 251 ? 148.858 133.168 117.925 1.00 16.73 ?  251 LEU A O     1 
ATOM   2008  C  CB    . LEU A 1 251 ? 147.344 133.454 120.654 1.00 17.48 ?  251 LEU A CB    1 
ATOM   2009  C  CG    . LEU A 1 251 ? 148.161 133.852 121.882 1.00 12.99 ?  251 LEU A CG    1 
ATOM   2010  C  CD1   . LEU A 1 251 ? 147.502 135.011 122.602 1.00 18.08 ?  251 LEU A CD1   1 
ATOM   2011  C  CD2   . LEU A 1 251 ? 148.340 132.669 122.812 1.00 13.39 ?  251 LEU A CD2   1 
ATOM   2012  N  N     . ASN A 1 252 ? 149.770 134.944 118.973 1.00 15.94 ?  252 ASN A N     1 
ATOM   2013  C  CA    . ASN A 1 252 ? 151.096 134.691 118.435 1.00 12.87 ?  252 ASN A CA    1 
ATOM   2014  C  C     . ASN A 1 252 ? 151.684 133.440 119.073 1.00 14.42 ?  252 ASN A C     1 
ATOM   2015  O  O     . ASN A 1 252 ? 151.472 133.169 120.258 1.00 25.53 ?  252 ASN A O     1 
ATOM   2016  C  CB    . ASN A 1 252 ? 152.007 135.892 118.674 1.00 15.10 ?  252 ASN A CB    1 
ATOM   2017  C  CG    . ASN A 1 252 ? 153.154 135.953 117.690 1.00 20.40 ?  252 ASN A CG    1 
ATOM   2018  O  OD1   . ASN A 1 252 ? 154.137 135.226 117.819 1.00 25.03 ?  252 ASN A OD1   1 
ATOM   2019  N  ND2   . ASN A 1 252 ? 153.028 136.815 116.690 1.00 17.33 ?  252 ASN A ND2   1 
ATOM   2020  N  N     . ILE A 1 253 ? 152.424 132.667 118.276 1.00 13.59 ?  253 ILE A N     1 
ATOM   2021  C  CA    . ILE A 1 253 ? 152.975 131.413 118.772 1.00 20.79 ?  253 ILE A CA    1 
ATOM   2022  C  C     . ILE A 1 253 ? 154.066 131.643 119.811 1.00 23.63 ?  253 ILE A C     1 
ATOM   2023  O  O     . ILE A 1 253 ? 154.404 130.720 120.561 1.00 25.79 ?  253 ILE A O     1 
ATOM   2024  C  CB    . ILE A 1 253 ? 153.493 130.557 117.600 1.00 19.47 ?  253 ILE A CB    1 
ATOM   2025  C  CG1   . ILE A 1 253 ? 153.512 129.079 117.991 1.00 23.14 ?  253 ILE A CG1   1 
ATOM   2026  C  CG2   . ILE A 1 253 ? 154.869 131.026 117.154 1.00 13.69 ?  253 ILE A CG2   1 
ATOM   2027  C  CD1   . ILE A 1 253 ? 153.336 128.136 116.831 1.00 21.73 ?  253 ILE A CD1   1 
ATOM   2028  N  N     . PHE A 1 254 ? 154.622 132.850 119.886 1.00 22.21 ?  254 PHE A N     1 
ATOM   2029  C  CA    . PHE A 1 254 ? 155.620 133.176 120.895 1.00 15.92 ?  254 PHE A CA    1 
ATOM   2030  C  C     . PHE A 1 254 ? 155.003 133.721 122.175 1.00 21.42 ?  254 PHE A C     1 
ATOM   2031  O  O     . PHE A 1 254 ? 155.729 133.950 123.149 1.00 29.46 ?  254 PHE A O     1 
ATOM   2032  C  CB    . PHE A 1 254 ? 156.634 134.173 120.326 1.00 22.92 ?  254 PHE A CB    1 
ATOM   2033  C  CG    . PHE A 1 254 ? 157.657 133.540 119.426 1.00 26.00 ?  254 PHE A CG    1 
ATOM   2034  C  CD1   . PHE A 1 254 ? 158.606 132.670 119.938 1.00 25.65 ?  254 PHE A CD1   1 
ATOM   2035  C  CD2   . PHE A 1 254 ? 157.658 133.796 118.066 1.00 23.77 ?  254 PHE A CD2   1 
ATOM   2036  C  CE1   . PHE A 1 254 ? 159.543 132.081 119.114 1.00 28.02 ?  254 PHE A CE1   1 
ATOM   2037  C  CE2   . PHE A 1 254 ? 158.592 133.206 117.236 1.00 26.10 ?  254 PHE A CE2   1 
ATOM   2038  C  CZ    . PHE A 1 254 ? 159.537 132.349 117.762 1.00 27.05 ?  254 PHE A CZ    1 
ATOM   2039  N  N     . HIS A 1 255 ? 153.692 133.945 122.192 1.00 26.58 ?  255 HIS A N     1 
ATOM   2040  C  CA    . HIS A 1 255 ? 152.990 134.209 123.439 1.00 17.25 ?  255 HIS A CA    1 
ATOM   2041  C  C     . HIS A 1 255 ? 153.075 132.979 124.331 1.00 19.54 ?  255 HIS A C     1 
ATOM   2042  O  O     . HIS A 1 255 ? 153.004 131.844 123.854 1.00 28.90 ?  255 HIS A O     1 
ATOM   2043  C  CB    . HIS A 1 255 ? 151.531 134.563 123.151 1.00 19.06 ?  255 HIS A CB    1 
ATOM   2044  C  CG    . HIS A 1 255 ? 150.810 135.189 124.304 1.00 23.16 ?  255 HIS A CG    1 
ATOM   2045  N  ND1   . HIS A 1 255 ? 150.448 134.485 125.431 1.00 21.46 ?  255 HIS A ND1   1 
ATOM   2046  C  CD2   . HIS A 1 255 ? 150.361 136.452 124.489 1.00 15.99 ?  255 HIS A CD2   1 
ATOM   2047  C  CE1   . HIS A 1 255 ? 149.820 135.292 126.268 1.00 16.84 ?  255 HIS A CE1   1 
ATOM   2048  N  NE2   . HIS A 1 255 ? 149.753 136.491 125.720 1.00 13.24 ?  255 HIS A NE2   1 
ATOM   2049  N  N     . ARG A 1 256 ? 153.239 133.202 125.637 1.00 21.55 ?  256 ARG A N     1 
ATOM   2050  C  CA    . ARG A 1 256 ? 153.475 132.073 126.529 1.00 21.81 ?  256 ARG A CA    1 
ATOM   2051  C  C     . ARG A 1 256 ? 152.231 131.207 126.670 1.00 27.23 ?  256 ARG A C     1 
ATOM   2052  O  O     . ARG A 1 256 ? 152.333 129.988 126.846 1.00 30.87 ?  256 ARG A O     1 
ATOM   2053  C  CB    . ARG A 1 256 ? 153.927 132.561 127.898 1.00 24.98 ?  256 ARG A CB    1 
ATOM   2054  C  CG    . ARG A 1 256 ? 154.490 131.451 128.752 1.00 29.78 ?  256 ARG A CG    1 
ATOM   2055  C  CD    . ARG A 1 256 ? 153.955 131.496 130.159 1.00 30.42 ?  256 ARG A CD    1 
ATOM   2056  N  NE    . ARG A 1 256 ? 152.509 131.670 130.203 1.00 29.67 ?  256 ARG A NE    1 
ATOM   2057  C  CZ    . ARG A 1 256 ? 151.666 130.726 130.599 1.00 31.62 ?  256 ARG A CZ    1 
ATOM   2058  N  NH1   . ARG A 1 256 ? 152.096 129.540 130.997 1.00 32.60 1  256 ARG A NH1   1 
ATOM   2059  N  NH2   . ARG A 1 256 ? 150.363 130.981 130.605 1.00 33.08 ?  256 ARG A NH2   1 
ATOM   2060  N  N     . ASP A 1 257 ? 151.051 131.814 126.592 1.00 22.54 ?  257 ASP A N     1 
ATOM   2061  C  CA    . ASP A 1 257 ? 149.784 131.096 126.706 1.00 19.25 ?  257 ASP A CA    1 
ATOM   2062  C  C     . ASP A 1 257 ? 149.498 130.199 125.525 1.00 24.96 ?  257 ASP A C     1 
ATOM   2063  O  O     . ASP A 1 257 ? 148.426 129.577 125.539 1.00 32.70 ?  257 ASP A O     1 
ATOM   2064  C  CB    . ASP A 1 257 ? 148.630 132.086 126.871 1.00 21.68 ?  257 ASP A CB    1 
ATOM   2065  C  CG    . ASP A 1 257 ? 148.558 132.678 128.259 1.00 30.64 ?  257 ASP A CG    1 
ATOM   2066  O  OD1   . ASP A 1 257 ? 149.120 132.078 129.196 1.00 28.10 ?  257 ASP A OD1   1 
ATOM   2067  O  OD2   . ASP A 1 257 ? 147.925 133.741 128.415 1.00 34.69 -1 257 ASP A OD2   1 
ATOM   2068  N  N     . ILE A 1 258 ? 150.415 130.105 124.558 1.00 26.12 ?  258 ILE A N     1 
ATOM   2069  C  CA    . ILE A 1 258 ? 150.113 129.444 123.292 1.00 25.64 ?  258 ILE A CA    1 
ATOM   2070  C  C     . ILE A 1 258 ? 149.664 128.007 123.526 1.00 23.84 ?  258 ILE A C     1 
ATOM   2071  O  O     . ILE A 1 258 ? 148.751 127.514 122.857 1.00 32.27 ?  258 ILE A O     1 
ATOM   2072  C  CB    . ILE A 1 258 ? 151.323 129.523 122.339 1.00 22.86 ?  258 ILE A CB    1 
ATOM   2073  C  CG1   . ILE A 1 258 ? 150.955 128.977 120.958 1.00 25.32 ?  258 ILE A CG1   1 
ATOM   2074  C  CG2   . ILE A 1 258 ? 152.536 128.801 122.915 1.00 19.03 ?  258 ILE A CG2   1 
ATOM   2075  C  CD1   . ILE A 1 258 ? 149.817 129.722 120.303 1.00 18.76 ?  258 ILE A CD1   1 
ATOM   2076  N  N     . ASN A 1 259 ? 150.285 127.317 124.484 1.00 23.42 ?  259 ASN A N     1 
ATOM   2077  C  CA    . ASN A 1 259 ? 149.854 125.959 124.796 1.00 23.87 ?  259 ASN A CA    1 
ATOM   2078  C  C     . ASN A 1 259 ? 148.453 125.959 125.394 1.00 27.63 ?  259 ASN A C     1 
ATOM   2079  O  O     . ASN A 1 259 ? 147.561 125.252 124.908 1.00 29.97 ?  259 ASN A O     1 
ATOM   2080  C  CB    . ASN A 1 259 ? 150.853 125.301 125.746 1.00 25.62 ?  259 ASN A CB    1 
ATOM   2081  C  CG    . ASN A 1 259 ? 152.141 124.908 125.052 1.00 30.57 ?  259 ASN A CG    1 
ATOM   2082  O  OD1   . ASN A 1 259 ? 152.158 124.011 124.210 1.00 31.68 ?  259 ASN A OD1   1 
ATOM   2083  N  ND2   . ASN A 1 259 ? 153.228 125.586 125.399 1.00 27.56 ?  259 ASN A ND2   1 
ATOM   2084  N  N     . ASP A 1 260 ? 148.227 126.786 126.418 1.00 26.94 ?  260 ASP A N     1 
ATOM   2085  C  CA    . ASP A 1 260 ? 146.908 126.853 127.039 1.00 26.40 ?  260 ASP A CA    1 
ATOM   2086  C  C     . ASP A 1 260 ? 145.861 127.295 126.026 1.00 21.16 ?  260 ASP A C     1 
ATOM   2087  O  O     . ASP A 1 260 ? 144.769 126.721 125.952 1.00 27.71 ?  260 ASP A O     1 
ATOM   2088  C  CB    . ASP A 1 260 ? 146.939 127.801 128.238 1.00 26.24 ?  260 ASP A CB    1 
ATOM   2089  C  CG    . ASP A 1 260 ? 148.159 127.598 129.112 1.00 36.42 ?  260 ASP A CG    1 
ATOM   2090  O  OD1   . ASP A 1 260 ? 148.638 128.589 129.703 1.00 35.80 ?  260 ASP A OD1   1 
ATOM   2091  O  OD2   . ASP A 1 260 ? 148.636 126.449 129.212 1.00 35.91 -1 260 ASP A OD2   1 
ATOM   2092  N  N     . PHE A 1 261 ? 146.190 128.319 125.235 1.00 26.31 ?  261 PHE A N     1 
ATOM   2093  C  CA    . PHE A 1 261 ? 145.423 128.680 124.050 1.00 23.74 ?  261 PHE A CA    1 
ATOM   2094  C  C     . PHE A 1 261 ? 145.034 127.437 123.259 1.00 20.08 ?  261 PHE A C     1 
ATOM   2095  O  O     . PHE A 1 261 ? 143.847 127.130 123.091 1.00 21.56 ?  261 PHE A O     1 
ATOM   2096  C  CB    . PHE A 1 261 ? 146.264 129.640 123.199 1.00 16.16 ?  261 PHE A CB    1 
ATOM   2097  C  CG    . PHE A 1 261 ? 145.540 130.224 122.022 1.00 22.45 ?  261 PHE A CG    1 
ATOM   2098  C  CD1   . PHE A 1 261 ? 144.654 131.271 122.186 1.00 18.74 ?  261 PHE A CD1   1 
ATOM   2099  C  CD2   . PHE A 1 261 ? 145.782 129.753 120.743 1.00 23.64 ?  261 PHE A CD2   1 
ATOM   2100  C  CE1   . PHE A 1 261 ? 143.998 131.819 121.104 1.00 13.75 ?  261 PHE A CE1   1 
ATOM   2101  C  CE2   . PHE A 1 261 ? 145.132 130.299 119.657 1.00 15.00 ?  261 PHE A CE2   1 
ATOM   2102  C  CZ    . PHE A 1 261 ? 144.240 131.334 119.838 1.00 18.00 ?  261 PHE A CZ    1 
ATOM   2103  N  N     . LEU A 1 262 ? 146.040 126.677 122.818 1.00 26.08 ?  262 LEU A N     1 
ATOM   2104  C  CA    . LEU A 1 262 ? 145.770 125.462 122.059 1.00 23.94 ?  262 LEU A CA    1 
ATOM   2105  C  C     . LEU A 1 262 ? 144.992 124.458 122.897 1.00 29.96 ?  262 LEU A C     1 
ATOM   2106  O  O     . LEU A 1 262 ? 144.119 123.748 122.383 1.00 28.96 ?  262 LEU A O     1 
ATOM   2107  C  CB    . LEU A 1 262 ? 147.081 124.855 121.566 1.00 23.93 ?  262 LEU A CB    1 
ATOM   2108  C  CG    . LEU A 1 262 ? 147.859 125.669 120.534 1.00 25.30 ?  262 LEU A CG    1 
ATOM   2109  C  CD1   . LEU A 1 262 ? 149.148 124.960 120.164 1.00 27.68 ?  262 LEU A CD1   1 
ATOM   2110  C  CD2   . LEU A 1 262 ? 147.011 125.933 119.304 1.00 23.46 ?  262 LEU A CD2   1 
ATOM   2111  N  N     . ASP A 1 263 ? 145.270 124.413 124.203 1.00 35.28 ?  263 ASP A N     1 
ATOM   2112  C  CA    . ASP A 1 263 ? 144.571 123.482 125.078 1.00 29.88 ?  263 ASP A CA    1 
ATOM   2113  C  C     . ASP A 1 263 ? 143.081 123.775 125.148 1.00 31.41 ?  263 ASP A C     1 
ATOM   2114  O  O     . ASP A 1 263 ? 142.316 122.923 125.611 1.00 39.37 ?  263 ASP A O     1 
ATOM   2115  C  CB    . ASP A 1 263 ? 145.177 123.520 126.481 1.00 33.59 ?  263 ASP A CB    1 
ATOM   2116  C  CG    . ASP A 1 263 ? 146.523 122.828 126.551 1.00 38.24 ?  263 ASP A CG    1 
ATOM   2117  O  OD1   . ASP A 1 263 ? 146.833 122.034 125.639 1.00 38.59 ?  263 ASP A OD1   1 
ATOM   2118  O  OD2   . ASP A 1 263 ? 147.270 123.077 127.521 1.00 38.50 -1 263 ASP A OD2   1 
ATOM   2119  N  N     . THR A 1 264 ? 142.650 124.958 124.704 1.00 34.25 ?  264 THR A N     1 
ATOM   2120  C  CA    . THR A 1 264 ? 141.223 125.246 124.682 1.00 32.61 ?  264 THR A CA    1 
ATOM   2121  C  C     . THR A 1 264 ? 140.483 124.425 123.635 1.00 37.29 ?  264 THR A C     1 
ATOM   2122  O  O     . THR A 1 264 ? 139.254 124.327 123.702 1.00 40.05 ?  264 THR A O     1 
ATOM   2123  C  CB    . THR A 1 264 ? 140.987 126.735 124.432 1.00 35.07 ?  264 THR A CB    1 
ATOM   2124  O  OG1   . THR A 1 264 ? 141.586 127.112 123.186 1.00 39.96 ?  264 THR A OG1   1 
ATOM   2125  C  CG2   . THR A 1 264 ? 141.591 127.562 125.555 1.00 31.28 ?  264 THR A CG2   1 
ATOM   2126  N  N     . LYS A 1 265 ? 141.193 123.833 122.674 1.00 36.99 ?  265 LYS A N     1 
ATOM   2127  C  CA    . LYS A 1 265 ? 140.558 123.050 121.623 1.00 36.97 ?  265 LYS A CA    1 
ATOM   2128  C  C     . LYS A 1 265 ? 140.724 121.549 121.797 1.00 39.83 ?  265 LYS A C     1 
ATOM   2129  O  O     . LYS A 1 265 ? 140.202 120.785 120.978 1.00 43.53 ?  265 LYS A O     1 
ATOM   2130  C  CB    . LYS A 1 265 ? 141.094 123.469 120.250 1.00 37.82 ?  265 LYS A CB    1 
ATOM   2131  C  CG    . LYS A 1 265 ? 140.441 124.717 119.693 1.00 37.62 ?  265 LYS A CG    1 
ATOM   2132  C  CD    . LYS A 1 265 ? 138.934 124.661 119.840 1.00 39.31 ?  265 LYS A CD    1 
ATOM   2133  C  CE    . LYS A 1 265 ? 138.287 125.942 119.353 1.00 36.10 ?  265 LYS A CE    1 
ATOM   2134  N  NZ    . LYS A 1 265 ? 136.844 125.997 119.707 1.00 37.78 1  265 LYS A NZ    1 
ATOM   2135  N  N     . LYS A 1 266 ? 141.431 121.102 122.829 1.00 45.49 ?  266 LYS A N     1 
ATOM   2136  C  CA    . LYS A 1 266 ? 141.559 119.673 123.070 1.00 46.34 ?  266 LYS A CA    1 
ATOM   2137  C  C     . LYS A 1 266 ? 140.253 119.104 123.612 1.00 50.98 ?  266 LYS A C     1 
ATOM   2138  O  O     . LYS A 1 266 ? 139.526 119.759 124.363 1.00 50.36 ?  266 LYS A O     1 
ATOM   2139  C  CB    . LYS A 1 266 ? 142.704 119.391 124.041 1.00 44.07 ?  266 LYS A CB    1 
ATOM   2140  C  CG    . LYS A 1 266 ? 144.074 119.400 123.387 1.00 47.04 ?  266 LYS A CG    1 
ATOM   2141  C  CD    . LYS A 1 266 ? 145.166 118.994 124.362 1.00 48.02 ?  266 LYS A CD    1 
ATOM   2142  C  CE    . LYS A 1 266 ? 146.492 118.800 123.644 1.00 48.71 ?  266 LYS A CE    1 
ATOM   2143  N  NZ    . LYS A 1 266 ? 147.633 118.685 124.594 1.00 47.04 1  266 LYS A NZ    1 
ATOM   2144  N  N     . ILE A 1 267 ? 139.953 117.868 123.209 1.00 57.94 ?  267 ILE A N     1 
ATOM   2145  C  CA    . ILE A 1 267 ? 138.738 117.209 123.678 1.00 59.55 ?  267 ILE A CA    1 
ATOM   2146  C  C     . ILE A 1 267 ? 138.836 116.906 125.168 1.00 59.12 ?  267 ILE A C     1 
ATOM   2147  O  O     . ILE A 1 267 ? 137.840 116.980 125.898 1.00 57.17 ?  267 ILE A O     1 
ATOM   2148  C  CB    . ILE A 1 267 ? 138.469 115.936 122.856 1.00 59.00 ?  267 ILE A CB    1 
ATOM   2149  C  CG1   . ILE A 1 267 ? 138.171 116.294 121.397 1.00 59.81 ?  267 ILE A CG1   1 
ATOM   2150  C  CG2   . ILE A 1 267 ? 137.319 115.147 123.462 1.00 57.14 ?  267 ILE A CG2   1 
ATOM   2151  C  CD1   . ILE A 1 267 ? 139.353 116.114 120.468 1.00 59.86 ?  267 ILE A CD1   1 
ATOM   2152  N  N     . SER A 1 268 ? 140.034 116.562 125.643 1.00 60.20 ?  268 SER A N     1 
ATOM   2153  C  CA    . SER A 1 268 ? 140.236 116.242 127.051 1.00 63.53 ?  268 SER A CA    1 
ATOM   2154  C  C     . SER A 1 268 ? 140.191 117.469 127.954 1.00 64.19 ?  268 SER A C     1 
ATOM   2155  O  O     . SER A 1 268 ? 140.215 117.311 129.179 1.00 63.68 ?  268 SER A O     1 
ATOM   2156  C  CB    . SER A 1 268 ? 141.571 115.519 127.236 1.00 63.60 ?  268 SER A CB    1 
ATOM   2157  O  OG    . SER A 1 268 ? 142.649 116.314 126.774 1.00 62.10 ?  268 SER A OG    1 
ATOM   2158  N  N     . ALA A 1 269 ? 140.137 118.672 127.387 1.00 66.10 ?  269 ALA A N     1 
ATOM   2159  C  CA    . ALA A 1 269 ? 140.116 119.884 128.193 1.00 65.74 ?  269 ALA A CA    1 
ATOM   2160  C  C     . ALA A 1 269 ? 138.858 119.943 129.053 1.00 66.79 ?  269 ALA A C     1 
ATOM   2161  O  O     . ALA A 1 269 ? 137.778 119.504 128.650 1.00 64.71 ?  269 ALA A O     1 
ATOM   2162  C  CB    . ALA A 1 269 ? 140.195 121.122 127.298 1.00 61.65 ?  269 ALA A CB    1 
ATOM   2163  N  N     . ASP A 1 270 ? 139.011 120.496 130.254 1.00 73.17 ?  270 ASP A N     1 
ATOM   2164  C  CA    . ASP A 1 270 ? 137.900 120.605 131.184 1.00 73.06 ?  270 ASP A CA    1 
ATOM   2165  C  C     . ASP A 1 270 ? 136.931 121.700 130.738 1.00 73.22 ?  270 ASP A C     1 
ATOM   2166  O  O     . ASP A 1 270 ? 137.181 122.446 129.787 1.00 73.93 ?  270 ASP A O     1 
ATOM   2167  C  CB    . ASP A 1 270 ? 138.408 120.888 132.597 1.00 73.27 ?  270 ASP A CB    1 
ATOM   2168  C  CG    . ASP A 1 270 ? 139.620 120.052 132.959 1.00 74.95 ?  270 ASP A CG    1 
ATOM   2169  O  OD1   . ASP A 1 270 ? 139.730 118.915 132.455 1.00 74.46 ?  270 ASP A OD1   1 
ATOM   2170  O  OD2   . ASP A 1 270 ? 140.461 120.532 133.748 1.00 73.37 -1 270 ASP A OD2   1 
ATOM   2171  N  N     . GLU A 1 271 ? 135.805 121.788 131.450 1.00 74.54 ?  271 GLU A N     1 
ATOM   2172  C  CA    . GLU A 1 271 ? 134.779 122.766 131.100 1.00 75.66 ?  271 GLU A CA    1 
ATOM   2173  C  C     . GLU A 1 271 ? 135.244 124.195 131.355 1.00 75.28 ?  271 GLU A C     1 
ATOM   2174  O  O     . GLU A 1 271 ? 134.775 125.124 130.689 1.00 74.37 ?  271 GLU A O     1 
ATOM   2175  C  CB    . GLU A 1 271 ? 133.494 122.479 131.876 1.00 74.59 ?  271 GLU A CB    1 
ATOM   2176  C  CG    . GLU A 1 271 ? 132.926 121.087 131.644 1.00 75.40 ?  271 GLU A CG    1 
ATOM   2177  C  CD    . GLU A 1 271 ? 132.904 120.699 130.178 1.00 76.58 ?  271 GLU A CD    1 
ATOM   2178  O  OE1   . GLU A 1 271 ? 132.391 121.489 129.356 1.00 75.75 ?  271 GLU A OE1   1 
ATOM   2179  O  OE2   . GLU A 1 271 ? 133.401 119.602 129.844 1.00 74.84 -1 271 GLU A OE2   1 
ATOM   2180  N  N     . ASP A 1 272 ? 136.154 124.392 132.305 1.00 69.39 ?  272 ASP A N     1 
ATOM   2181  C  CA    . ASP A 1 272 ? 136.697 125.713 132.594 1.00 70.33 ?  272 ASP A CA    1 
ATOM   2182  C  C     . ASP A 1 272 ? 137.885 126.067 131.710 1.00 70.67 ?  272 ASP A C     1 
ATOM   2183  O  O     . ASP A 1 272 ? 138.475 127.137 131.888 1.00 68.52 ?  272 ASP A O     1 
ATOM   2184  C  CB    . ASP A 1 272 ? 137.101 125.810 134.070 1.00 70.43 ?  272 ASP A CB    1 
ATOM   2185  C  CG    . ASP A 1 272 ? 138.261 124.898 134.421 1.00 71.48 ?  272 ASP A CG    1 
ATOM   2186  O  OD1   . ASP A 1 272 ? 138.451 123.879 133.727 1.00 70.47 ?  272 ASP A OD1   1 
ATOM   2187  O  OD2   . ASP A 1 272 ? 138.984 125.204 135.391 1.00 70.07 -1 272 ASP A OD2   1 
ATOM   2188  N  N     . VAL A 1 273 ? 138.255 125.192 130.773 1.00 65.21 ?  273 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 273 ? 139.368 125.427 129.867 1.00 64.67 ?  273 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 273 ? 138.910 125.516 128.417 1.00 62.53 ?  273 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 273 ? 139.378 126.378 127.665 1.00 65.25 ?  273 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 273 ? 140.450 124.336 130.028 1.00 66.28 ?  273 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 273 ? 141.475 124.415 128.906 1.00 63.57 ?  273 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 273 ? 141.126 124.454 131.384 1.00 64.79 ?  273 VAL A CG2   1 
ATOM   2195  N  N     . ARG A 1 274 ? 137.982 124.655 128.010 1.00 60.44 ?  274 ARG A N     1 
ATOM   2196  C  CA    . ARG A 1 274 ? 137.588 124.554 126.613 1.00 59.82 ?  274 ARG A CA    1 
ATOM   2197  C  C     . ARG A 1 274 ? 136.587 125.644 126.246 1.00 58.10 ?  274 ARG A C     1 
ATOM   2198  O  O     . ARG A 1 274 ? 135.634 125.900 126.988 1.00 58.12 ?  274 ARG A O     1 
ATOM   2199  C  CB    . ARG A 1 274 ? 136.988 123.176 126.334 1.00 59.95 ?  274 ARG A CB    1 
ATOM   2200  C  CG    . ARG A 1 274 ? 136.104 123.114 125.099 1.00 58.60 ?  274 ARG A CG    1 
ATOM   2201  C  CD    . ARG A 1 274 ? 136.070 121.715 124.506 1.00 58.80 ?  274 ARG A CD    1 
ATOM   2202  N  NE    . ARG A 1 274 ? 135.901 120.687 125.527 1.00 62.16 ?  274 ARG A NE    1 
ATOM   2203  C  CZ    . ARG A 1 274 ? 134.753 120.413 126.134 1.00 63.53 ?  274 ARG A CZ    1 
ATOM   2204  N  NH1   . ARG A 1 274 ? 133.642 121.071 125.841 1.00 62.50 1  274 ARG A NH1   1 
ATOM   2205  N  NH2   . ARG A 1 274 ? 134.718 119.453 127.053 1.00 63.03 ?  274 ARG A NH2   1 
ATOM   2206  N  N     . VAL A 1 275 ? 136.808 126.282 125.098 1.00 47.64 ?  275 VAL A N     1 
ATOM   2207  C  CA    . VAL A 1 275 ? 135.860 127.216 124.503 1.00 44.89 ?  275 VAL A CA    1 
ATOM   2208  C  C     . VAL A 1 275 ? 135.290 126.563 123.251 1.00 45.72 ?  275 VAL A C     1 
ATOM   2209  O  O     . VAL A 1 275 ? 136.043 126.083 122.395 1.00 47.61 ?  275 VAL A O     1 
ATOM   2210  C  CB    . VAL A 1 275 ? 136.520 128.571 124.184 1.00 44.54 ?  275 VAL A CB    1 
ATOM   2211  C  CG1   . VAL A 1 275 ? 136.744 129.361 125.463 1.00 42.69 ?  275 VAL A CG1   1 
ATOM   2212  C  CG2   . VAL A 1 275 ? 137.839 128.374 123.455 1.00 44.81 ?  275 VAL A CG2   1 
ATOM   2213  N  N     . LYS A 1 276 ? 133.962 126.529 123.150 1.00 46.73 ?  276 LYS A N     1 
ATOM   2214  C  CA    . LYS A 1 276 ? 133.300 125.760 122.104 1.00 47.97 ?  276 LYS A CA    1 
ATOM   2215  C  C     . LYS A 1 276 ? 132.891 126.587 120.894 1.00 47.05 ?  276 LYS A C     1 
ATOM   2216  O  O     . LYS A 1 276 ? 132.980 126.091 119.766 1.00 52.80 ?  276 LYS A O     1 
ATOM   2217  C  CB    . LYS A 1 276 ? 132.061 125.056 122.672 1.00 49.01 ?  276 LYS A CB    1 
ATOM   2218  C  CG    . LYS A 1 276 ? 131.126 125.967 123.452 1.00 52.48 ?  276 LYS A CG    1 
ATOM   2219  C  CD    . LYS A 1 276 ? 130.082 125.170 124.222 1.00 50.48 ?  276 LYS A CD    1 
ATOM   2220  C  CE    . LYS A 1 276 ? 130.715 124.017 124.986 1.00 49.46 ?  276 LYS A CE    1 
ATOM   2221  N  NZ    . LYS A 1 276 ? 131.767 124.485 125.931 1.00 48.12 1  276 LYS A NZ    1 
ATOM   2222  N  N     . THR A 1 277 ? 132.447 127.826 121.089 1.00 38.15 ?  277 THR A N     1 
ATOM   2223  C  CA    . THR A 1 277 ? 132.015 128.676 119.989 1.00 38.69 ?  277 THR A CA    1 
ATOM   2224  C  C     . THR A 1 277 ? 133.063 129.707 119.595 1.00 42.36 ?  277 THR A C     1 
ATOM   2225  O  O     . THR A 1 277 ? 132.750 130.641 118.852 1.00 41.83 ?  277 THR A O     1 
ATOM   2226  C  CB    . THR A 1 277 ? 130.701 129.377 120.343 1.00 41.43 ?  277 THR A CB    1 
ATOM   2227  O  OG1   . THR A 1 277 ? 130.960 130.454 121.254 1.00 35.00 ?  277 THR A OG1   1 
ATOM   2228  C  CG2   . THR A 1 277 ? 129.732 128.393 120.980 1.00 41.22 ?  277 THR A CG2   1 
ATOM   2229  N  N     . LEU A 1 278 ? 134.293 129.562 120.076 1.00 33.87 ?  278 LEU A N     1 
ATOM   2230  C  CA    . LEU A 1 278 ? 135.378 130.487 119.770 1.00 31.20 ?  278 LEU A CA    1 
ATOM   2231  C  C     . LEU A 1 278 ? 136.434 129.749 118.960 1.00 25.43 ?  278 LEU A C     1 
ATOM   2232  O  O     . LEU A 1 278 ? 137.170 128.919 119.502 1.00 34.43 ?  278 LEU A O     1 
ATOM   2233  C  CB    . LEU A 1 278 ? 135.978 131.067 121.048 1.00 28.77 ?  278 LEU A CB    1 
ATOM   2234  C  CG    . LEU A 1 278 ? 136.853 132.309 120.881 1.00 25.02 ?  278 LEU A CG    1 
ATOM   2235  C  CD1   . LEU A 1 278 ? 135.996 133.549 120.714 1.00 24.11 ?  278 LEU A CD1   1 
ATOM   2236  C  CD2   . LEU A 1 278 ? 137.794 132.462 122.061 1.00 31.95 ?  278 LEU A CD2   1 
ATOM   2237  N  N     . SER A 1 279 ? 136.504 130.049 117.668 1.00 26.11 ?  279 SER A N     1 
ATOM   2238  C  CA    . SER A 1 279 ? 137.587 129.541 116.841 1.00 21.19 ?  279 SER A CA    1 
ATOM   2239  C  C     . SER A 1 279 ? 138.911 130.141 117.293 1.00 20.60 ?  279 SER A C     1 
ATOM   2240  O  O     . SER A 1 279 ? 138.959 131.235 117.862 1.00 33.10 ?  279 SER A O     1 
ATOM   2241  C  CB    . SER A 1 279 ? 137.337 129.868 115.371 1.00 17.65 ?  279 SER A CB    1 
ATOM   2242  O  OG    . SER A 1 279 ? 136.247 129.122 114.860 1.00 25.68 ?  279 SER A OG    1 
ATOM   2243  N  N     . ILE A 1 280 ? 139.995 129.412 117.054 1.00 18.70 ?  280 ILE A N     1 
ATOM   2244  C  CA    . ILE A 1 280 ? 141.321 129.864 117.450 1.00 22.67 ?  280 ILE A CA    1 
ATOM   2245  C  C     . ILE A 1 280 ? 142.241 129.838 116.240 1.00 23.14 ?  280 ILE A C     1 
ATOM   2246  O  O     . ILE A 1 280 ? 142.147 128.944 115.391 1.00 26.18 ?  280 ILE A O     1 
ATOM   2247  C  CB    . ILE A 1 280 ? 141.908 129.022 118.603 1.00 17.83 ?  280 ILE A CB    1 
ATOM   2248  C  CG1   . ILE A 1 280 ? 142.098 127.565 118.186 1.00 23.84 ?  280 ILE A CG1   1 
ATOM   2249  C  CG2   . ILE A 1 280 ? 141.025 129.120 119.834 1.00 20.13 ?  280 ILE A CG2   1 
ATOM   2250  C  CD1   . ILE A 1 280 ? 143.190 126.861 118.963 1.00 18.96 ?  280 ILE A CD1   1 
ATOM   2251  N  N     . GLY A 1 281 ? 143.103 130.839 116.149 1.00 13.73 ?  281 GLY A N     1 
ATOM   2252  C  CA    . GLY A 1 281 ? 144.144 130.860 115.145 1.00 4.47  ?  281 GLY A CA    1 
ATOM   2253  C  C     . GLY A 1 281 ? 145.473 131.200 115.782 1.00 10.46 ?  281 GLY A C     1 
ATOM   2254  O  O     . GLY A 1 281 ? 145.544 131.930 116.769 1.00 18.34 ?  281 GLY A O     1 
ATOM   2255  N  N     . VAL A 1 282 ? 146.535 130.650 115.204 1.00 15.23 ?  282 VAL A N     1 
ATOM   2256  C  CA    . VAL A 1 282 ? 147.890 130.839 115.705 1.00 12.71 ?  282 VAL A CA    1 
ATOM   2257  C  C     . VAL A 1 282 ? 148.696 131.580 114.651 1.00 13.55 ?  282 VAL A C     1 
ATOM   2258  O  O     . VAL A 1 282 ? 148.689 131.204 113.473 1.00 17.64 ?  282 VAL A O     1 
ATOM   2259  C  CB    . VAL A 1 282 ? 148.551 129.498 116.070 1.00 14.51 ?  282 VAL A CB    1 
ATOM   2260  C  CG1   . VAL A 1 282 ? 150.037 129.681 116.301 1.00 19.00 ?  282 VAL A CG1   1 
ATOM   2261  C  CG2   . VAL A 1 282 ? 147.899 128.922 117.309 1.00 19.47 ?  282 VAL A CG2   1 
ATOM   2262  N  N     . VAL A 1 283 ? 149.376 132.640 115.073 1.00 12.13 ?  283 VAL A N     1 
ATOM   2263  C  CA    . VAL A 1 283 ? 150.253 133.411 114.201 1.00 11.66 ?  283 VAL A CA    1 
ATOM   2264  C  C     . VAL A 1 283 ? 151.673 132.896 114.386 1.00 16.58 ?  283 VAL A C     1 
ATOM   2265  O  O     . VAL A 1 283 ? 152.210 132.919 115.498 1.00 25.42 ?  283 VAL A O     1 
ATOM   2266  C  CB    . VAL A 1 283 ? 150.161 134.911 114.512 1.00 11.36 ?  283 VAL A CB    1 
ATOM   2267  C  CG1   . VAL A 1 283 ? 150.895 135.714 113.460 1.00 9.15  ?  283 VAL A CG1   1 
ATOM   2268  C  CG2   . VAL A 1 283 ? 148.705 135.335 114.598 1.00 14.54 ?  283 VAL A CG2   1 
ATOM   2269  N  N     . ILE A 1 284 ? 152.279 132.432 113.302 1.00 14.52 ?  284 ILE A N     1 
ATOM   2270  C  CA    . ILE A 1 284 ? 153.583 131.787 113.336 1.00 14.52 ?  284 ILE A CA    1 
ATOM   2271  C  C     . ILE A 1 284 ? 154.570 132.647 112.560 1.00 18.20 ?  284 ILE A C     1 
ATOM   2272  O  O     . ILE A 1 284 ? 154.578 132.645 111.329 1.00 20.15 ?  284 ILE A O     1 
ATOM   2273  C  CB    . ILE A 1 284 ? 153.521 130.360 112.763 1.00 16.43 ?  284 ILE A CB    1 
ATOM   2274  C  CG1   . ILE A 1 284 ? 152.507 129.520 113.541 1.00 16.93 ?  284 ILE A CG1   1 
ATOM   2275  C  CG2   . ILE A 1 284 ? 154.893 129.709 112.799 1.00 17.23 ?  284 ILE A CG2   1 
ATOM   2276  C  CD1   . ILE A 1 284 ? 152.491 128.061 113.147 1.00 19.37 ?  284 ILE A CD1   1 
ATOM   2277  N  N     . PRO A 1 285 ? 155.420 133.404 113.249 1.00 27.08 ?  285 PRO A N     1 
ATOM   2278  C  CA    . PRO A 1 285 ? 156.480 134.142 112.556 1.00 25.81 ?  285 PRO A CA    1 
ATOM   2279  C  C     . PRO A 1 285 ? 157.528 133.197 111.989 1.00 23.52 ?  285 PRO A C     1 
ATOM   2280  O  O     . PRO A 1 285 ? 157.611 132.021 112.350 1.00 25.24 ?  285 PRO A O     1 
ATOM   2281  C  CB    . PRO A 1 285 ? 157.072 135.036 113.652 1.00 19.49 ?  285 PRO A CB    1 
ATOM   2282  C  CG    . PRO A 1 285 ? 156.048 135.052 114.744 1.00 17.59 ?  285 PRO A CG    1 
ATOM   2283  C  CD    . PRO A 1 285 ? 155.377 133.721 114.684 1.00 21.54 ?  285 PRO A CD    1 
ATOM   2284  N  N     . ASP A 1 286 ? 158.337 133.736 111.073 1.00 26.51 ?  286 ASP A N     1 
ATOM   2285  C  CA    . ASP A 1 286 ? 159.399 132.937 110.468 1.00 24.40 ?  286 ASP A CA    1 
ATOM   2286  C  C     . ASP A 1 286 ? 160.408 132.464 111.504 1.00 29.80 ?  286 ASP A C     1 
ATOM   2287  O  O     . ASP A 1 286 ? 161.066 131.438 111.300 1.00 32.08 ?  286 ASP A O     1 
ATOM   2288  C  CB    . ASP A 1 286 ? 160.108 133.736 109.376 1.00 24.91 ?  286 ASP A CB    1 
ATOM   2289  C  CG    . ASP A 1 286 ? 159.587 133.419 107.992 1.00 36.92 ?  286 ASP A CG    1 
ATOM   2290  O  OD1   . ASP A 1 286 ? 158.505 132.805 107.890 1.00 36.04 ?  286 ASP A OD1   1 
ATOM   2291  O  OD2   . ASP A 1 286 ? 160.257 133.787 107.004 1.00 39.10 -1 286 ASP A OD2   1 
ATOM   2292  N  N     . LYS A 1 287 ? 160.549 133.195 112.613 1.00 30.46 ?  287 LYS A N     1 
ATOM   2293  C  CA    . LYS A 1 287 ? 161.505 132.801 113.642 1.00 28.00 ?  287 LYS A CA    1 
ATOM   2294  C  C     . LYS A 1 287 ? 161.141 131.453 114.250 1.00 29.31 ?  287 LYS A C     1 
ATOM   2295  O  O     . LYS A 1 287 ? 162.021 130.625 114.511 1.00 36.10 ?  287 LYS A O     1 
ATOM   2296  C  CB    . LYS A 1 287 ? 161.582 133.875 114.727 1.00 31.50 ?  287 LYS A CB    1 
ATOM   2297  C  CG    . LYS A 1 287 ? 162.738 133.685 115.691 1.00 27.46 ?  287 LYS A CG    1 
ATOM   2298  C  CD    . LYS A 1 287 ? 164.037 133.456 114.937 1.00 30.56 ?  287 LYS A CD    1 
ATOM   2299  C  CE    . LYS A 1 287 ? 165.231 133.465 115.870 1.00 31.46 ?  287 LYS A CE    1 
ATOM   2300  N  NZ    . LYS A 1 287 ? 166.514 133.353 115.124 1.00 34.93 1  287 LYS A NZ    1 
ATOM   2301  N  N     . PHE A 1 288 ? 159.849 131.214 114.486 1.00 24.06 ?  288 PHE A N     1 
ATOM   2302  C  CA    . PHE A 1 288 ? 159.425 129.923 115.022 1.00 24.02 ?  288 PHE A CA    1 
ATOM   2303  C  C     . PHE A 1 288 ? 159.739 128.794 114.048 1.00 24.75 ?  288 PHE A C     1 
ATOM   2304  O  O     . PHE A 1 288 ? 160.177 127.713 114.459 1.00 36.24 ?  288 PHE A O     1 
ATOM   2305  C  CB    . PHE A 1 288 ? 157.932 129.953 115.345 1.00 25.06 ?  288 PHE A CB    1 
ATOM   2306  C  CG    . PHE A 1 288 ? 157.425 128.686 115.973 1.00 26.56 ?  288 PHE A CG    1 
ATOM   2307  C  CD1   . PHE A 1 288 ? 157.557 128.474 117.335 1.00 27.58 ?  288 PHE A CD1   1 
ATOM   2308  C  CD2   . PHE A 1 288 ? 156.818 127.709 115.204 1.00 22.72 ?  288 PHE A CD2   1 
ATOM   2309  C  CE1   . PHE A 1 288 ? 157.093 127.311 117.916 1.00 26.22 ?  288 PHE A CE1   1 
ATOM   2310  C  CE2   . PHE A 1 288 ? 156.353 126.544 115.780 1.00 24.98 ?  288 PHE A CE2   1 
ATOM   2311  C  CZ    . PHE A 1 288 ? 156.490 126.345 117.138 1.00 29.33 ?  288 PHE A CZ    1 
ATOM   2312  N  N     . VAL A 1 289 ? 159.520 129.027 112.753 1.00 24.93 ?  289 VAL A N     1 
ATOM   2313  C  CA    . VAL A 1 289 ? 159.803 127.998 111.760 1.00 28.22 ?  289 VAL A CA    1 
ATOM   2314  C  C     . VAL A 1 289 ? 161.301 127.736 111.674 1.00 29.88 ?  289 VAL A C     1 
ATOM   2315  O  O     . VAL A 1 289 ? 161.734 126.592 111.503 1.00 33.12 ?  289 VAL A O     1 
ATOM   2316  C  CB    . VAL A 1 289 ? 159.213 128.395 110.395 1.00 31.83 ?  289 VAL A CB    1 
ATOM   2317  C  CG1   . VAL A 1 289 ? 159.263 127.221 109.433 1.00 25.97 ?  289 VAL A CG1   1 
ATOM   2318  C  CG2   . VAL A 1 289 ? 157.787 128.896 110.561 1.00 26.24 ?  289 VAL A CG2   1 
ATOM   2319  N  N     . GLU A 1 290 ? 162.117 128.789 111.786 1.00 33.29 ?  290 GLU A N     1 
ATOM   2320  C  CA    . GLU A 1 290 ? 163.565 128.602 111.794 1.00 32.38 ?  290 GLU A CA    1 
ATOM   2321  C  C     . GLU A 1 290 ? 164.013 127.819 113.021 1.00 35.00 ?  290 GLU A C     1 
ATOM   2322  O  O     . GLU A 1 290 ? 164.886 126.948 112.926 1.00 41.47 ?  290 GLU A O     1 
ATOM   2323  C  CB    . GLU A 1 290 ? 164.275 129.954 111.734 1.00 33.41 ?  290 GLU A CB    1 
ATOM   2324  C  CG    . GLU A 1 290 ? 164.350 130.566 110.346 1.00 38.34 ?  290 GLU A CG    1 
ATOM   2325  C  CD    . GLU A 1 290 ? 163.834 131.990 110.302 1.00 39.81 ?  290 GLU A CD    1 
ATOM   2326  O  OE1   . GLU A 1 290 ? 163.136 132.341 109.328 1.00 38.86 ?  290 GLU A OE1   1 
ATOM   2327  O  OE2   . GLU A 1 290 ? 164.124 132.759 111.242 1.00 40.07 -1 290 GLU A OE2   1 
ATOM   2328  N  N     . LEU A 1 291 ? 163.435 128.122 114.185 1.00 32.62 ?  291 LEU A N     1 
ATOM   2329  C  CA    . LEU A 1 291 ? 163.796 127.404 115.402 1.00 29.33 ?  291 LEU A CA    1 
ATOM   2330  C  C     . LEU A 1 291 ? 163.401 125.935 115.317 1.00 32.32 ?  291 LEU A C     1 
ATOM   2331  O  O     . LEU A 1 291 ? 164.167 125.057 115.731 1.00 39.75 ?  291 LEU A O     1 
ATOM   2332  C  CB    . LEU A 1 291 ? 163.144 128.067 116.616 1.00 31.03 ?  291 LEU A CB    1 
ATOM   2333  C  CG    . LEU A 1 291 ? 163.681 129.448 116.990 1.00 32.77 ?  291 LEU A CG    1 
ATOM   2334  C  CD1   . LEU A 1 291 ? 162.678 130.201 117.845 1.00 27.11 ?  291 LEU A CD1   1 
ATOM   2335  C  CD2   . LEU A 1 291 ? 165.017 129.328 117.700 1.00 32.96 ?  291 LEU A CD2   1 
ATOM   2336  N  N     . ALA A 1 292 ? 162.208 125.649 114.792 1.00 33.22 ?  292 ALA A N     1 
ATOM   2337  C  CA    . ALA A 1 292 ? 161.787 124.262 114.628 1.00 31.63 ?  292 ALA A CA    1 
ATOM   2338  C  C     . ALA A 1 292 ? 162.652 123.538 113.603 1.00 32.39 ?  292 ALA A C     1 
ATOM   2339  O  O     . ALA A 1 292 ? 162.984 122.361 113.782 1.00 37.80 ?  292 ALA A O     1 
ATOM   2340  C  CB    . ALA A 1 292 ? 160.314 124.204 114.229 1.00 30.62 ?  292 ALA A CB    1 
ATOM   2341  N  N     . ARG A 1 293 ? 163.020 124.227 112.521 1.00 34.05 ?  293 ARG A N     1 
ATOM   2342  C  CA    . ARG A 1 293 ? 163.829 123.613 111.473 1.00 33.45 ?  293 ARG A CA    1 
ATOM   2343  C  C     . ARG A 1 293 ? 165.202 123.209 111.994 1.00 39.26 ?  293 ARG A C     1 
ATOM   2344  O  O     . ARG A 1 293 ? 165.697 122.119 111.680 1.00 43.88 ?  293 ARG A O     1 
ATOM   2345  C  CB    . ARG A 1 293 ? 163.960 124.579 110.297 1.00 34.13 ?  293 ARG A CB    1 
ATOM   2346  C  CG    . ARG A 1 293 ? 164.841 124.091 109.164 1.00 34.36 ?  293 ARG A CG    1 
ATOM   2347  C  CD    . ARG A 1 293 ? 165.111 125.214 108.179 1.00 38.71 ?  293 ARG A CD    1 
ATOM   2348  N  NE    . ARG A 1 293 ? 163.902 125.977 107.896 1.00 40.23 ?  293 ARG A NE    1 
ATOM   2349  C  CZ    . ARG A 1 293 ? 163.829 127.301 107.922 1.00 39.33 ?  293 ARG A CZ    1 
ATOM   2350  N  NH1   . ARG A 1 293 ? 164.885 128.047 108.199 1.00 37.97 1  293 ARG A NH1   1 
ATOM   2351  N  NH2   . ARG A 1 293 ? 162.665 127.891 107.663 1.00 35.71 ?  293 ARG A NH2   1 
ATOM   2352  N  N     . GLU A 1 294 ? 165.832 124.070 112.788 1.00 41.45 ?  294 GLU A N     1 
ATOM   2353  C  CA    . GLU A 1 294 ? 167.144 123.781 113.350 1.00 39.06 ?  294 GLU A CA    1 
ATOM   2354  C  C     . GLU A 1 294 ? 167.071 122.977 114.640 1.00 40.16 ?  294 GLU A C     1 
ATOM   2355  O  O     . GLU A 1 294 ? 168.119 122.672 115.219 1.00 42.64 ?  294 GLU A O     1 
ATOM   2356  C  CB    . GLU A 1 294 ? 167.905 125.085 113.599 1.00 39.21 ?  294 GLU A CB    1 
ATOM   2357  C  CG    . GLU A 1 294 ? 168.445 125.739 112.338 1.00 41.33 ?  294 GLU A CG    1 
ATOM   2358  C  CD    . GLU A 1 294 ? 167.988 127.174 112.186 1.00 44.89 ?  294 GLU A CD    1 
ATOM   2359  O  OE1   . GLU A 1 294 ? 167.805 127.854 113.219 1.00 45.92 ?  294 GLU A OE1   1 
ATOM   2360  O  OE2   . GLU A 1 294 ? 167.808 127.625 111.036 1.00 46.51 -1 294 GLU A OE2   1 
ATOM   2361  N  N     . ASP A 1 295 ? 165.866 122.648 115.106 1.00 38.72 ?  295 ASP A N     1 
ATOM   2362  C  CA    . ASP A 1 295 ? 165.614 121.883 116.324 1.00 37.97 ?  295 ASP A CA    1 
ATOM   2363  C  C     . ASP A 1 295 ? 166.096 122.594 117.582 1.00 44.50 ?  295 ASP A C     1 
ATOM   2364  O  O     . ASP A 1 295 ? 166.126 121.984 118.657 1.00 44.19 ?  295 ASP A O     1 
ATOM   2365  C  CB    . ASP A 1 295 ? 166.233 120.480 116.251 1.00 40.78 ?  295 ASP A CB    1 
ATOM   2366  C  CG    . ASP A 1 295 ? 165.311 119.408 116.795 1.00 44.89 ?  295 ASP A CG    1 
ATOM   2367  O  OD1   . ASP A 1 295 ? 164.328 119.759 117.481 1.00 46.03 ?  295 ASP A OD1   1 
ATOM   2368  O  OD2   . ASP A 1 295 ? 165.571 118.214 116.539 1.00 42.65 -1 295 ASP A OD2   1 
ATOM   2369  N  N     . LYS A 1 296 ? 166.477 123.865 117.482 1.00 43.47 ?  296 LYS A N     1 
ATOM   2370  C  CA    . LYS A 1 296 ? 166.828 124.631 118.669 1.00 41.60 ?  296 LYS A CA    1 
ATOM   2371  C  C     . LYS A 1 296 ? 165.590 124.862 119.523 1.00 41.53 ?  296 LYS A C     1 
ATOM   2372  O  O     . LYS A 1 296 ? 164.505 125.138 119.008 1.00 45.89 ?  296 LYS A O     1 
ATOM   2373  C  CB    . LYS A 1 296 ? 167.451 125.972 118.283 1.00 42.27 ?  296 LYS A CB    1 
ATOM   2374  C  CG    . LYS A 1 296 ? 168.586 125.881 117.283 1.00 44.14 ?  296 LYS A CG    1 
ATOM   2375  C  CD    . LYS A 1 296 ? 168.660 127.140 116.435 1.00 42.91 ?  296 LYS A CD    1 
ATOM   2376  C  CE    . LYS A 1 296 ? 170.093 127.616 116.277 1.00 43.56 ?  296 LYS A CE    1 
ATOM   2377  N  NZ    . LYS A 1 296 ? 170.934 126.620 115.560 1.00 44.16 1  296 LYS A NZ    1 
ATOM   2378  N  N     . ALA A 1 297 ? 165.756 124.743 120.837 1.00 40.88 ?  297 ALA A N     1 
ATOM   2379  C  CA    . ALA A 1 297 ? 164.649 124.997 121.746 1.00 42.43 ?  297 ALA A CA    1 
ATOM   2380  C  C     . ALA A 1 297 ? 164.258 126.468 121.701 1.00 40.42 ?  297 ALA A C     1 
ATOM   2381  O  O     . ALA A 1 297 ? 165.112 127.357 121.724 1.00 41.09 ?  297 ALA A O     1 
ATOM   2382  C  CB    . ALA A 1 297 ? 165.026 124.594 123.168 1.00 37.53 ?  297 ALA A CB    1 
ATOM   2383  N  N     . ALA A 1 298 ? 162.955 126.721 121.636 1.00 35.05 ?  298 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 298 ? 162.435 128.070 121.510 1.00 34.96 ?  298 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 298 ? 162.005 128.595 122.875 1.00 35.60 ?  298 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 298 ? 161.982 127.874 123.875 1.00 39.04 ?  298 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 298 ? 161.273 128.104 120.515 1.00 33.74 ?  298 ALA A CB    1 
ATOM   2388  N  N     . TYR A 1 299 ? 161.648 129.875 122.911 1.00 33.59 ?  299 TYR A N     1 
ATOM   2389  C  CA    . TYR A 1 299 ? 161.180 130.519 124.128 1.00 27.91 ?  299 TYR A CA    1 
ATOM   2390  C  C     . TYR A 1 299 ? 159.854 131.206 123.847 1.00 29.08 ?  299 TYR A C     1 
ATOM   2391  O  O     . TYR A 1 299 ? 159.729 131.941 122.863 1.00 30.35 ?  299 TYR A O     1 
ATOM   2392  C  CB    . TYR A 1 299 ? 162.203 131.534 124.647 1.00 29.77 ?  299 TYR A CB    1 
ATOM   2393  C  CG    . TYR A 1 299 ? 163.407 130.903 125.302 1.00 31.98 ?  299 TYR A CG    1 
ATOM   2394  C  CD1   . TYR A 1 299 ? 163.357 130.468 126.620 1.00 34.99 ?  299 TYR A CD1   1 
ATOM   2395  C  CD2   . TYR A 1 299 ? 164.593 130.737 124.601 1.00 32.52 ?  299 TYR A CD2   1 
ATOM   2396  C  CE1   . TYR A 1 299 ? 164.457 129.888 127.221 1.00 35.03 ?  299 TYR A CE1   1 
ATOM   2397  C  CE2   . TYR A 1 299 ? 165.696 130.158 125.192 1.00 33.28 ?  299 TYR A CE2   1 
ATOM   2398  C  CZ    . TYR A 1 299 ? 165.623 129.735 126.502 1.00 35.74 ?  299 TYR A CZ    1 
ATOM   2399  O  OH    . TYR A 1 299 ? 166.721 129.158 127.097 1.00 39.40 ?  299 TYR A OH    1 
ATOM   2400  N  N     . VAL A 1 300 ? 158.871 130.960 124.705 1.00 32.74 ?  300 VAL A N     1 
ATOM   2401  C  CA    . VAL A 1 300 ? 157.606 131.685 124.678 1.00 27.48 ?  300 VAL A CA    1 
ATOM   2402  C  C     . VAL A 1 300 ? 157.676 132.770 125.742 1.00 28.99 ?  300 VAL A C     1 
ATOM   2403  O  O     . VAL A 1 300 ? 158.020 132.497 126.897 1.00 35.40 ?  300 VAL A O     1 
ATOM   2404  C  CB    . VAL A 1 300 ? 156.410 130.746 124.907 1.00 25.59 ?  300 VAL A CB    1 
ATOM   2405  C  CG1   . VAL A 1 300 ? 156.076 129.996 123.626 1.00 26.29 ?  300 VAL A CG1   1 
ATOM   2406  C  CG2   . VAL A 1 300 ? 156.692 129.775 126.041 1.00 28.34 ?  300 VAL A CG2   1 
ATOM   2407  N  N     . PHE A 1 301 ? 157.368 134.000 125.354 1.00 22.22 ?  301 PHE A N     1 
ATOM   2408  C  CA    . PHE A 1 301 ? 157.643 135.159 126.188 1.00 24.64 ?  301 PHE A CA    1 
ATOM   2409  C  C     . PHE A 1 301 ? 156.391 135.675 126.881 1.00 29.79 ?  301 PHE A C     1 
ATOM   2410  O  O     . PHE A 1 301 ? 155.271 135.528 126.386 1.00 32.59 ?  301 PHE A O     1 
ATOM   2411  C  CB    . PHE A 1 301 ? 158.274 136.277 125.358 1.00 23.17 ?  301 PHE A CB    1 
ATOM   2412  C  CG    . PHE A 1 301 ? 159.475 135.839 124.578 1.00 28.71 ?  301 PHE A CG    1 
ATOM   2413  C  CD1   . PHE A 1 301 ? 160.706 135.726 125.199 1.00 27.45 ?  301 PHE A CD1   1 
ATOM   2414  C  CD2   . PHE A 1 301 ? 159.376 135.526 123.234 1.00 27.89 ?  301 PHE A CD2   1 
ATOM   2415  C  CE1   . PHE A 1 301 ? 161.817 135.317 124.497 1.00 27.89 ?  301 PHE A CE1   1 
ATOM   2416  C  CE2   . PHE A 1 301 ? 160.487 135.117 122.525 1.00 26.73 ?  301 PHE A CE2   1 
ATOM   2417  C  CZ    . PHE A 1 301 ? 161.710 135.012 123.159 1.00 29.84 ?  301 PHE A CZ    1 
ATOM   2418  N  N     . TYR A 1 302 ? 156.601 136.278 128.049 1.00 27.90 ?  302 TYR A N     1 
ATOM   2419  C  CA    . TYR A 1 302 ? 155.551 136.989 128.761 1.00 24.69 ?  302 TYR A CA    1 
ATOM   2420  C  C     . TYR A 1 302 ? 155.412 138.377 128.153 1.00 28.70 ?  302 TYR A C     1 
ATOM   2421  O  O     . TYR A 1 302 ? 156.348 139.183 128.216 1.00 30.11 ?  302 TYR A O     1 
ATOM   2422  C  CB    . TYR A 1 302 ? 155.866 137.076 130.254 1.00 25.69 ?  302 TYR A CB    1 
ATOM   2423  C  CG    . TYR A 1 302 ? 155.724 135.766 130.994 1.00 28.28 ?  302 TYR A CG    1 
ATOM   2424  C  CD1   . TYR A 1 302 ? 156.645 134.744 130.822 1.00 27.90 ?  302 TYR A CD1   1 
ATOM   2425  C  CD2   . TYR A 1 302 ? 154.666 135.554 131.864 1.00 29.97 ?  302 TYR A CD2   1 
ATOM   2426  C  CE1   . TYR A 1 302 ? 156.516 133.549 131.499 1.00 26.48 ?  302 TYR A CE1   1 
ATOM   2427  C  CE2   . TYR A 1 302 ? 154.528 134.364 132.546 1.00 30.24 ?  302 TYR A CE2   1 
ATOM   2428  C  CZ    . TYR A 1 302 ? 155.458 133.366 132.365 1.00 33.79 ?  302 TYR A CZ    1 
ATOM   2429  O  OH    . TYR A 1 302 ? 155.321 132.176 133.040 1.00 34.01 ?  302 TYR A OH    1 
ATOM   2430  N  N     . PRO A 1 303 ? 154.267 138.681 127.540 1.00 24.50 ?  303 PRO A N     1 
ATOM   2431  C  CA    . PRO A 1 303 ? 154.141 139.951 126.806 1.00 21.46 ?  303 PRO A CA    1 
ATOM   2432  C  C     . PRO A 1 303 ? 154.303 141.188 127.668 1.00 28.11 ?  303 PRO A C     1 
ATOM   2433  O  O     . PRO A 1 303 ? 154.851 142.191 127.193 1.00 32.36 ?  303 PRO A O     1 
ATOM   2434  C  CB    . PRO A 1 303 ? 152.728 139.865 126.213 1.00 24.61 ?  303 PRO A CB    1 
ATOM   2435  C  CG    . PRO A 1 303 ? 152.415 138.413 126.192 1.00 26.14 ?  303 PRO A CG    1 
ATOM   2436  C  CD    . PRO A 1 303 ? 153.069 137.841 127.401 1.00 25.81 ?  303 PRO A CD    1 
ATOM   2437  N  N     . HIS A 1 304 ? 153.842 141.156 128.920 1.00 29.80 ?  304 HIS A N     1 
ATOM   2438  C  CA    . HIS A 1 304 ? 153.892 142.358 129.743 1.00 24.97 ?  304 HIS A CA    1 
ATOM   2439  C  C     . HIS A 1 304 ? 155.319 142.711 130.135 1.00 28.58 ?  304 HIS A C     1 
ATOM   2440  O  O     . HIS A 1 304 ? 155.653 143.894 130.233 1.00 36.19 ?  304 HIS A O     1 
ATOM   2441  C  CB    . HIS A 1 304 ? 153.026 142.191 130.989 1.00 28.66 ?  304 HIS A CB    1 
ATOM   2442  C  CG    . HIS A 1 304 ? 152.847 143.454 131.771 1.00 30.65 ?  304 HIS A CG    1 
ATOM   2443  N  ND1   . HIS A 1 304 ? 152.968 143.506 133.142 1.00 33.01 ?  304 HIS A ND1   1 
ATOM   2444  C  CD2   . HIS A 1 304 ? 152.561 144.716 131.370 1.00 29.10 ?  304 HIS A CD2   1 
ATOM   2445  C  CE1   . HIS A 1 304 ? 152.759 144.744 133.554 1.00 32.39 ?  304 HIS A CE1   1 
ATOM   2446  N  NE2   . HIS A 1 304 ? 152.510 145.498 132.499 1.00 30.65 ?  304 HIS A NE2   1 
ATOM   2447  N  N     . THR A 1 305 ? 156.169 141.708 130.368 1.00 29.10 ?  305 THR A N     1 
ATOM   2448  C  CA    . THR A 1 305 ? 157.572 141.989 130.657 1.00 32.57 ?  305 THR A CA    1 
ATOM   2449  C  C     . THR A 1 305 ? 158.260 142.633 129.460 1.00 27.80 ?  305 THR A C     1 
ATOM   2450  O  O     . THR A 1 305 ? 159.048 143.573 129.616 1.00 33.42 ?  305 THR A O     1 
ATOM   2451  C  CB    . THR A 1 305 ? 158.295 140.708 131.075 1.00 31.42 ?  305 THR A CB    1 
ATOM   2452  O  OG1   . THR A 1 305 ? 158.512 139.876 129.928 1.00 31.84 ?  305 THR A OG1   1 
ATOM   2453  C  CG2   . THR A 1 305 ? 157.471 139.946 132.097 1.00 29.19 ?  305 THR A CG2   1 
ATOM   2454  N  N     . ILE A 1 306 ? 157.964 142.145 128.253 1.00 32.77 ?  306 ILE A N     1 
ATOM   2455  C  CA    . ILE A 1 306 ? 158.512 142.757 127.047 1.00 32.57 ?  306 ILE A CA    1 
ATOM   2456  C  C     . ILE A 1 306 ? 158.010 144.188 126.903 1.00 31.32 ?  306 ILE A C     1 
ATOM   2457  O  O     . ILE A 1 306 ? 158.771 145.097 126.548 1.00 32.80 ?  306 ILE A O     1 
ATOM   2458  C  CB    . ILE A 1 306 ? 158.165 141.902 125.814 1.00 28.41 ?  306 ILE A CB    1 
ATOM   2459  C  CG1   . ILE A 1 306 ? 159.095 140.691 125.732 1.00 32.43 ?  306 ILE A CG1   1 
ATOM   2460  C  CG2   . ILE A 1 306 ? 158.232 142.730 124.542 1.00 31.73 ?  306 ILE A CG2   1 
ATOM   2461  C  CD1   . ILE A 1 306 ? 158.805 139.778 124.574 1.00 31.27 ?  306 ILE A CD1   1 
ATOM   2462  N  N     . TYR A 1 307 ? 156.722 144.413 127.172 1.00 31.91 ?  307 TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 307 ? 156.170 145.760 127.077 1.00 31.01 ?  307 TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 307 ? 156.821 146.697 128.087 1.00 33.45 ?  307 TYR A C     1 
ATOM   2465  O  O     . TYR A 1 307 ? 157.108 147.858 127.773 1.00 36.52 ?  307 TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 307 ? 154.654 145.724 127.277 1.00 28.97 ?  307 TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 307 ? 153.990 147.066 127.095 1.00 30.60 ?  307 TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 307 ? 153.724 147.561 125.826 1.00 30.65 ?  307 TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 307 ? 153.634 147.841 128.189 1.00 33.18 ?  307 TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 307 ? 153.123 148.785 125.652 1.00 33.00 ?  307 TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 307 ? 153.032 149.069 128.025 1.00 33.13 ?  307 TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 307 ? 152.779 149.534 126.753 1.00 34.63 ?  307 TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 307 ? 152.178 150.756 126.575 1.00 36.39 ?  307 TYR A OH    1 
ATOM   2474  N  N     . LYS A 1 308 ? 157.049 146.215 129.308 1.00 34.52 ?  308 LYS A N     1 
ATOM   2475  C  CA    . LYS A 1 308 ? 157.700 147.034 130.324 1.00 32.72 ?  308 LYS A CA    1 
ATOM   2476  C  C     . LYS A 1 308 ? 159.143 147.343 129.943 1.00 32.52 ?  308 LYS A C     1 
ATOM   2477  O  O     . LYS A 1 308 ? 159.625 148.458 130.172 1.00 38.35 ?  308 LYS A O     1 
ATOM   2478  C  CB    . LYS A 1 308 ? 157.642 146.331 131.679 1.00 33.87 ?  308 LYS A CB    1 
ATOM   2479  C  CG    . LYS A 1 308 ? 156.267 146.340 132.323 1.00 33.26 ?  308 LYS A CG    1 
ATOM   2480  C  CD    . LYS A 1 308 ? 156.315 145.786 133.737 1.00 36.34 ?  308 LYS A CD    1 
ATOM   2481  C  CE    . LYS A 1 308 ? 156.887 144.379 133.760 1.00 37.36 ?  308 LYS A CE    1 
ATOM   2482  N  NZ    . LYS A 1 308 ? 155.853 143.363 134.095 1.00 37.78 1  308 LYS A NZ    1 
ATOM   2483  N  N     . GLU A 1 309 ? 159.847 146.369 129.363 1.00 32.39 ?  309 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 309 ? 161.255 146.571 129.041 1.00 33.46 ?  309 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 309 ? 161.436 147.482 127.832 1.00 36.40 ?  309 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 309 ? 162.316 148.351 127.831 1.00 37.54 ?  309 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 309 ? 161.934 145.224 128.802 1.00 31.64 ?  309 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 309 ? 163.366 145.332 128.311 1.00 37.48 ?  309 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 309 ? 164.307 145.895 129.356 1.00 42.65 ?  309 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 309 ? 163.943 145.896 130.550 1.00 41.25 ?  309 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 309 ? 165.411 146.340 128.983 1.00 41.78 -1 309 GLU A OE2   1 
ATOM   2492  N  N     . TYR A 1 310 ? 160.614 147.306 126.796 1.00 37.05 ?  310 TYR A N     1 
ATOM   2493  C  CA    . TYR A 1 310 ? 160.824 147.985 125.526 1.00 36.10 ?  310 TYR A CA    1 
ATOM   2494  C  C     . TYR A 1 310 ? 159.784 149.051 125.211 1.00 33.12 ?  310 TYR A C     1 
ATOM   2495  O  O     . TYR A 1 310 ? 159.993 149.832 124.277 1.00 38.26 ?  310 TYR A O     1 
ATOM   2496  C  CB    . TYR A 1 310 ? 160.855 146.960 124.382 1.00 37.36 ?  310 TYR A CB    1 
ATOM   2497  C  CG    . TYR A 1 310 ? 161.933 145.911 124.538 1.00 33.85 ?  310 TYR A CG    1 
ATOM   2498  C  CD1   . TYR A 1 310 ? 163.224 146.145 124.088 1.00 34.94 ?  310 TYR A CD1   1 
ATOM   2499  C  CD2   . TYR A 1 310 ? 161.661 144.691 125.140 1.00 32.11 ?  310 TYR A CD2   1 
ATOM   2500  C  CE1   . TYR A 1 310 ? 164.215 145.194 124.231 1.00 36.55 ?  310 TYR A CE1   1 
ATOM   2501  C  CE2   . TYR A 1 310 ? 162.645 143.734 125.289 1.00 33.23 ?  310 TYR A CE2   1 
ATOM   2502  C  CZ    . TYR A 1 310 ? 163.919 143.990 124.831 1.00 37.01 ?  310 TYR A CZ    1 
ATOM   2503  O  OH    . TYR A 1 310 ? 164.901 143.039 124.977 1.00 41.12 ?  310 TYR A OH    1 
ATOM   2504  N  N     . GLY A 1 311 ? 158.683 149.115 125.955 1.00 27.93 ?  311 GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 311 ? 157.652 150.093 125.683 1.00 31.03 ?  311 GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 311 ? 156.736 149.752 124.531 1.00 36.06 ?  311 GLY A C     1 
ATOM   2507  O  O     . GLY A 1 311 ? 155.864 150.563 124.195 1.00 39.00 ?  311 GLY A O     1 
ATOM   2508  N  N     . GLN A 1 312 ? 156.907 148.586 123.913 1.00 35.59 ?  312 GLN A N     1 
ATOM   2509  C  CA    . GLN A 1 312 ? 156.066 148.139 122.814 1.00 32.40 ?  312 GLN A CA    1 
ATOM   2510  C  C     . GLN A 1 312 ? 155.628 146.706 123.074 1.00 34.00 ?  312 GLN A C     1 
ATOM   2511  O  O     . GLN A 1 312 ? 156.298 145.949 123.782 1.00 38.82 ?  312 GLN A O     1 
ATOM   2512  C  CB    . GLN A 1 312 ? 156.793 148.223 121.464 1.00 31.89 ?  312 GLN A CB    1 
ATOM   2513  C  CG    . GLN A 1 312 ? 157.949 149.208 121.427 1.00 34.46 ?  312 GLN A CG    1 
ATOM   2514  C  CD    . GLN A 1 312 ? 158.748 149.119 120.143 1.00 39.73 ?  312 GLN A CD    1 
ATOM   2515  O  OE1   . GLN A 1 312 ? 158.186 149.100 119.049 1.00 38.64 ?  312 GLN A OE1   1 
ATOM   2516  N  NE2   . GLN A 1 312 ? 160.069 149.061 120.270 1.00 38.75 ?  312 GLN A NE2   1 
ATOM   2517  N  N     . HIS A 1 313 ? 154.492 146.339 122.490 1.00 31.83 ?  313 HIS A N     1 
ATOM   2518  C  CA    . HIS A 1 313 ? 153.975 144.992 122.654 1.00 28.38 ?  313 HIS A CA    1 
ATOM   2519  C  C     . HIS A 1 313 ? 154.831 143.992 121.880 1.00 33.15 ?  313 HIS A C     1 
ATOM   2520  O  O     . HIS A 1 313 ? 155.521 144.336 120.917 1.00 35.26 ?  313 HIS A O     1 
ATOM   2521  C  CB    . HIS A 1 313 ? 152.521 144.915 122.189 1.00 28.95 ?  313 HIS A CB    1 
ATOM   2522  C  CG    . HIS A 1 313 ? 151.600 145.832 122.931 1.00 33.95 ?  313 HIS A CG    1 
ATOM   2523  N  ND1   . HIS A 1 313 ? 151.065 145.514 124.161 1.00 30.64 ?  313 HIS A ND1   1 
ATOM   2524  C  CD2   . HIS A 1 313 ? 151.115 147.056 122.615 1.00 32.84 ?  313 HIS A CD2   1 
ATOM   2525  C  CE1   . HIS A 1 313 ? 150.292 146.504 124.572 1.00 28.85 ?  313 HIS A CE1   1 
ATOM   2526  N  NE2   . HIS A 1 313 ? 150.306 147.451 123.652 1.00 30.06 ?  313 HIS A NE2   1 
ATOM   2527  N  N     . MET A 1 314 ? 154.779 142.734 122.324 1.00 34.61 ?  314 MET A N     1 
ATOM   2528  C  CA    . MET A 1 314 ? 155.585 141.691 121.699 1.00 27.28 ?  314 MET A CA    1 
ATOM   2529  C  C     . MET A 1 314 ? 155.198 141.485 120.240 1.00 31.93 ?  314 MET A C     1 
ATOM   2530  O  O     . MET A 1 314 ? 156.063 141.266 119.386 1.00 36.58 ?  314 MET A O     1 
ATOM   2531  C  CB    . MET A 1 314 ? 155.447 140.386 122.484 1.00 27.70 ?  314 MET A CB    1 
ATOM   2532  C  CG    . MET A 1 314 ? 156.330 139.258 121.979 1.00 28.99 ?  314 MET A CG    1 
ATOM   2533  S  SD    . MET A 1 314 ? 155.820 137.646 122.601 1.00 41.60 ?  314 MET A SD    1 
ATOM   2534  C  CE    . MET A 1 314 ? 154.039 137.800 122.513 1.00 30.84 ?  314 MET A CE    1 
ATOM   2535  N  N     . ASP A 1 315 ? 153.904 141.549 119.934 1.00 33.57 ?  315 ASP A N     1 
ATOM   2536  C  CA    . ASP A 1 315 ? 153.438 141.353 118.568 1.00 36.36 ?  315 ASP A CA    1 
ATOM   2537  C  C     . ASP A 1 315 ? 153.577 142.600 117.702 1.00 33.16 ?  315 ASP A C     1 
ATOM   2538  O  O     . ASP A 1 315 ? 153.294 142.531 116.501 1.00 35.57 ?  315 ASP A O     1 
ATOM   2539  C  CB    . ASP A 1 315 ? 151.981 140.880 118.572 1.00 27.80 ?  315 ASP A CB    1 
ATOM   2540  C  CG    . ASP A 1 315 ? 151.020 141.955 119.031 1.00 34.50 ?  315 ASP A CG    1 
ATOM   2541  O  OD1   . ASP A 1 315 ? 151.444 142.839 119.804 1.00 36.88 ?  315 ASP A OD1   1 
ATOM   2542  O  OD2   . ASP A 1 315 ? 149.842 141.917 118.618 1.00 31.81 -1 315 ASP A OD2   1 
ATOM   2543  N  N     . GLU A 1 316 ? 153.999 143.726 118.269 1.00 30.94 ?  316 GLU A N     1 
ATOM   2544  C  CA    . GLU A 1 316 ? 154.164 144.961 117.513 1.00 31.82 ?  316 GLU A CA    1 
ATOM   2545  C  C     . GLU A 1 316 ? 155.559 145.132 116.928 1.00 34.22 ?  316 GLU A C     1 
ATOM   2546  O  O     . GLU A 1 316 ? 155.775 146.066 116.149 1.00 36.40 ?  316 GLU A O     1 
ATOM   2547  C  CB    . GLU A 1 316 ? 153.837 146.167 118.398 1.00 34.66 ?  316 GLU A CB    1 
ATOM   2548  C  CG    . GLU A 1 316 ? 152.388 146.243 118.832 1.00 35.61 ?  316 GLU A CG    1 
ATOM   2549  C  CD    . GLU A 1 316 ? 151.568 147.148 117.940 1.00 39.42 ?  316 GLU A CD    1 
ATOM   2550  O  OE1   . GLU A 1 316 ? 151.764 147.106 116.707 1.00 36.52 ?  316 GLU A OE1   1 
ATOM   2551  O  OE2   . GLU A 1 316 ? 150.733 147.910 118.472 1.00 45.88 -1 316 GLU A OE2   1 
ATOM   2552  N  N     . MET A 1 317 ? 156.506 144.267 117.277 1.00 40.57 ?  317 MET A N     1 
ATOM   2553  C  CA    . MET A 1 317 ? 157.859 144.339 116.750 1.00 41.21 ?  317 MET A CA    1 
ATOM   2554  C  C     . MET A 1 317 ? 158.201 143.055 116.007 1.00 42.05 ?  317 MET A C     1 
ATOM   2555  O  O     . MET A 1 317 ? 157.571 142.012 116.200 1.00 38.59 ?  317 MET A O     1 
ATOM   2556  C  CB    . MET A 1 317 ? 158.888 144.589 117.859 1.00 40.57 ?  317 MET A CB    1 
ATOM   2557  C  CG    . MET A 1 317 ? 158.381 145.438 119.006 1.00 42.12 ?  317 MET A CG    1 
ATOM   2558  S  SD    . MET A 1 317 ? 159.598 145.575 120.327 1.00 51.18 ?  317 MET A SD    1 
ATOM   2559  C  CE    . MET A 1 317 ? 158.666 144.930 121.708 1.00 35.61 ?  317 MET A CE    1 
ATOM   2560  N  N     . ASP A 1 318 ? 159.222 143.143 115.158 1.00 43.69 ?  318 ASP A N     1 
ATOM   2561  C  CA    . ASP A 1 318 ? 159.648 142.016 114.335 1.00 41.03 ?  318 ASP A CA    1 
ATOM   2562  C  C     . ASP A 1 318 ? 160.374 141.008 115.214 1.00 40.87 ?  318 ASP A C     1 
ATOM   2563  O  O     . ASP A 1 318 ? 161.461 141.289 115.727 1.00 43.57 ?  318 ASP A O     1 
ATOM   2564  C  CB    . ASP A 1 318 ? 160.544 142.496 113.197 1.00 41.27 ?  318 ASP A CB    1 
ATOM   2565  C  CG    . ASP A 1 318 ? 161.134 141.350 112.400 1.00 47.77 ?  318 ASP A CG    1 
ATOM   2566  O  OD1   . ASP A 1 318 ? 160.399 140.381 112.118 1.00 46.74 ?  318 ASP A OD1   1 
ATOM   2567  O  OD2   . ASP A 1 318 ? 162.333 141.420 112.056 1.00 49.13 -1 318 ASP A OD2   1 
ATOM   2568  N  N     . MET A 1 319 ? 159.773 139.829 115.388 1.00 42.96 ?  319 MET A N     1 
ATOM   2569  C  CA    . MET A 1 319 ? 160.376 138.793 116.217 1.00 36.29 ?  319 MET A CA    1 
ATOM   2570  C  C     . MET A 1 319 ? 161.668 138.251 115.617 1.00 36.71 ?  319 MET A C     1 
ATOM   2571  O  O     . MET A 1 319 ? 162.517 137.753 116.361 1.00 41.37 ?  319 MET A O     1 
ATOM   2572  C  CB    . MET A 1 319 ? 159.369 137.660 116.440 1.00 33.84 ?  319 MET A CB    1 
ATOM   2573  C  CG    . MET A 1 319 ? 159.933 136.428 117.132 1.00 38.01 ?  319 MET A CG    1 
ATOM   2574  S  SD    . MET A 1 319 ? 159.885 136.512 118.935 1.00 45.80 ?  319 MET A SD    1 
ATOM   2575  C  CE    . MET A 1 319 ? 158.547 137.671 119.206 1.00 34.85 ?  319 MET A CE    1 
ATOM   2576  N  N     . ASN A 1 320 ? 161.854 138.365 114.301 1.00 38.02 ?  320 ASN A N     1 
ATOM   2577  C  CA    . ASN A 1 320 ? 163.079 137.862 113.688 1.00 41.12 ?  320 ASN A CA    1 
ATOM   2578  C  C     . ASN A 1 320 ? 164.306 138.587 114.226 1.00 41.90 ?  320 ASN A C     1 
ATOM   2579  O  O     . ASN A 1 320 ? 165.341 137.962 114.487 1.00 41.32 ?  320 ASN A O     1 
ATOM   2580  C  CB    . ASN A 1 320 ? 162.997 137.991 112.168 1.00 41.65 ?  320 ASN A CB    1 
ATOM   2581  C  CG    . ASN A 1 320 ? 162.326 136.798 111.521 1.00 43.37 ?  320 ASN A CG    1 
ATOM   2582  O  OD1   . ASN A 1 320 ? 161.103 136.666 111.553 1.00 38.61 ?  320 ASN A OD1   1 
ATOM   2583  N  ND2   . ASN A 1 320 ? 163.127 135.919 110.928 1.00 40.60 ?  320 ASN A ND2   1 
ATOM   2584  N  N     . GLU A 1 321 ? 164.211 139.903 114.402 1.00 42.91 ?  321 GLU A N     1 
ATOM   2585  C  CA    . GLU A 1 321 ? 165.309 140.686 114.951 1.00 44.57 ?  321 GLU A CA    1 
ATOM   2586  C  C     . GLU A 1 321 ? 165.201 140.898 116.456 1.00 42.96 ?  321 GLU A C     1 
ATOM   2587  O  O     . GLU A 1 321 ? 166.170 141.353 117.072 1.00 44.36 ?  321 GLU A O     1 
ATOM   2588  C  CB    . GLU A 1 321 ? 165.385 142.048 114.253 1.00 44.39 ?  321 GLU A CB    1 
ATOM   2589  C  CG    . GLU A 1 321 ? 164.209 142.961 114.552 1.00 47.17 ?  321 GLU A CG    1 
ATOM   2590  C  CD    . GLU A 1 321 ? 164.618 144.415 114.679 1.00 49.00 ?  321 GLU A CD    1 
ATOM   2591  O  OE1   . GLU A 1 321 ? 165.704 144.684 115.232 1.00 46.69 ?  321 GLU A OE1   1 
ATOM   2592  O  OE2   . GLU A 1 321 ? 163.851 145.290 114.224 1.00 47.46 -1 321 GLU A OE2   1 
ATOM   2593  N  N     . MET A 1 322 ? 164.057 140.578 117.060 1.00 41.35 ?  322 MET A N     1 
ATOM   2594  C  CA    . MET A 1 322 ? 163.832 140.824 118.478 1.00 35.79 ?  322 MET A CA    1 
ATOM   2595  C  C     . MET A 1 322 ? 163.965 139.578 119.343 1.00 33.07 ?  322 MET A C     1 
ATOM   2596  O  O     . MET A 1 322 ? 164.046 139.706 120.566 1.00 41.00 ?  322 MET A O     1 
ATOM   2597  C  CB    . MET A 1 322 ? 162.437 141.425 118.695 1.00 34.29 ?  322 MET A CB    1 
ATOM   2598  C  CG    . MET A 1 322 ? 162.387 142.944 118.714 1.00 39.93 ?  322 MET A CG    1 
ATOM   2599  S  SD    . MET A 1 322 ? 163.713 143.697 119.671 1.00 48.26 ?  322 MET A SD    1 
ATOM   2600  C  CE    . MET A 1 322 ? 164.607 144.550 118.375 1.00 39.75 ?  322 MET A CE    1 
ATOM   2601  N  N     . TYR A 1 323 ? 163.976 138.384 118.744 1.00 31.27 ?  323 TYR A N     1 
ATOM   2602  C  CA    . TYR A 1 323 ? 163.938 137.153 119.529 1.00 32.27 ?  323 TYR A CA    1 
ATOM   2603  C  C     . TYR A 1 323 ? 165.210 136.975 120.347 1.00 36.70 ?  323 TYR A C     1 
ATOM   2604  O  O     . TYR A 1 323 ? 165.155 136.621 121.530 1.00 38.05 ?  323 TYR A O     1 
ATOM   2605  C  CB    . TYR A 1 323 ? 163.718 135.956 118.604 1.00 30.02 ?  323 TYR A CB    1 
ATOM   2606  C  CG    . TYR A 1 323 ? 163.756 134.620 119.308 1.00 35.95 ?  323 TYR A CG    1 
ATOM   2607  C  CD1   . TYR A 1 323 ? 162.630 134.117 119.942 1.00 31.23 ?  323 TYR A CD1   1 
ATOM   2608  C  CD2   . TYR A 1 323 ? 164.918 133.862 119.337 1.00 33.51 ?  323 TYR A CD2   1 
ATOM   2609  C  CE1   . TYR A 1 323 ? 162.660 132.898 120.586 1.00 28.78 ?  323 TYR A CE1   1 
ATOM   2610  C  CE2   . TYR A 1 323 ? 164.958 132.644 119.978 1.00 26.53 ?  323 TYR A CE2   1 
ATOM   2611  C  CZ    . TYR A 1 323 ? 163.827 132.166 120.601 1.00 31.76 ?  323 TYR A CZ    1 
ATOM   2612  O  OH    . TYR A 1 323 ? 163.865 130.951 121.242 1.00 34.72 ?  323 TYR A OH    1 
ATOM   2613  N  N     . ASP A 1 324 ? 166.369 137.204 119.727 1.00 38.06 ?  324 ASP A N     1 
ATOM   2614  C  CA    . ASP A 1 324 ? 167.628 137.060 120.447 1.00 37.16 ?  324 ASP A CA    1 
ATOM   2615  C  C     . ASP A 1 324 ? 167.735 138.078 121.573 1.00 39.55 ?  324 ASP A C     1 
ATOM   2616  O  O     . ASP A 1 324 ? 168.224 137.761 122.664 1.00 45.08 ?  324 ASP A O     1 
ATOM   2617  C  CB    . ASP A 1 324 ? 168.804 137.198 119.482 1.00 40.36 ?  324 ASP A CB    1 
ATOM   2618  C  CG    . ASP A 1 324 ? 168.889 136.049 118.500 1.00 43.01 ?  324 ASP A CG    1 
ATOM   2619  O  OD1   . ASP A 1 324 ? 168.618 134.898 118.904 1.00 43.21 ?  324 ASP A OD1   1 
ATOM   2620  O  OD2   . ASP A 1 324 ? 169.228 136.294 117.324 1.00 43.38 -1 324 ASP A OD2   1 
ATOM   2621  N  N     . LYS A 1 325 ? 167.281 139.308 121.328 1.00 37.78 ?  325 LYS A N     1 
ATOM   2622  C  CA    . LYS A 1 325 ? 167.318 140.329 122.370 1.00 37.22 ?  325 LYS A CA    1 
ATOM   2623  C  C     . LYS A 1 325 ? 166.366 139.990 123.510 1.00 37.32 ?  325 LYS A C     1 
ATOM   2624  O  O     . LYS A 1 325 ? 166.679 140.240 124.678 1.00 44.63 ?  325 LYS A O     1 
ATOM   2625  C  CB    . LYS A 1 325 ? 166.992 141.697 121.773 1.00 40.71 ?  325 LYS A CB    1 
ATOM   2626  C  CG    . LYS A 1 325 ? 168.009 142.167 120.748 1.00 40.43 ?  325 LYS A CG    1 
ATOM   2627  C  CD    . LYS A 1 325 ? 167.604 143.490 120.125 1.00 40.26 ?  325 LYS A CD    1 
ATOM   2628  C  CE    . LYS A 1 325 ? 168.529 143.864 118.978 1.00 41.23 ?  325 LYS A CE    1 
ATOM   2629  N  NZ    . LYS A 1 325 ? 167.939 144.918 118.110 1.00 45.47 1  325 LYS A NZ    1 
ATOM   2630  N  N     . PHE A 1 326 ? 165.197 139.430 123.193 1.00 37.17 ?  326 PHE A N     1 
ATOM   2631  C  CA    . PHE A 1 326 ? 164.281 138.984 124.237 1.00 36.58 ?  326 PHE A CA    1 
ATOM   2632  C  C     . PHE A 1 326 ? 164.908 137.873 125.071 1.00 34.61 ?  326 PHE A C     1 
ATOM   2633  O  O     . PHE A 1 326 ? 164.826 137.884 126.304 1.00 41.38 ?  326 PHE A O     1 
ATOM   2634  C  CB    . PHE A 1 326 ? 162.967 138.501 123.621 1.00 34.54 ?  326 PHE A CB    1 
ATOM   2635  C  CG    . PHE A 1 326 ? 162.161 139.583 122.961 1.00 34.95 ?  326 PHE A CG    1 
ATOM   2636  C  CD1   . PHE A 1 326 ? 162.347 140.914 123.291 1.00 36.22 ?  326 PHE A CD1   1 
ATOM   2637  C  CD2   . PHE A 1 326 ? 161.209 139.263 122.008 1.00 34.82 ?  326 PHE A CD2   1 
ATOM   2638  C  CE1   . PHE A 1 326 ? 161.600 141.903 122.680 1.00 36.18 ?  326 PHE A CE1   1 
ATOM   2639  C  CE2   . PHE A 1 326 ? 160.460 140.248 121.397 1.00 36.20 ?  326 PHE A CE2   1 
ATOM   2640  C  CZ    . PHE A 1 326 ? 160.655 141.569 121.734 1.00 38.81 ?  326 PHE A CZ    1 
ATOM   2641  N  N     . VAL A 1 327 ? 165.538 136.903 124.408 1.00 38.25 ?  327 VAL A N     1 
ATOM   2642  C  CA    . VAL A 1 327 ? 166.131 135.774 125.118 1.00 39.48 ?  327 VAL A CA    1 
ATOM   2643  C  C     . VAL A 1 327 ? 167.284 136.238 126.001 1.00 42.72 ?  327 VAL A C     1 
ATOM   2644  O  O     . VAL A 1 327 ? 167.413 135.807 127.154 1.00 44.58 ?  327 VAL A O     1 
ATOM   2645  C  CB    . VAL A 1 327 ? 166.579 134.692 124.117 1.00 37.45 ?  327 VAL A CB    1 
ATOM   2646  C  CG1   . VAL A 1 327 ? 167.411 133.629 124.815 1.00 40.17 ?  327 VAL A CG1   1 
ATOM   2647  C  CG2   . VAL A 1 327 ? 165.370 134.064 123.445 1.00 32.45 ?  327 VAL A CG2   1 
ATOM   2648  N  N     . ASP A 1 328 ? 168.131 137.127 125.483 1.00 40.53 ?  328 ASP A N     1 
ATOM   2649  C  CA    . ASP A 1 328 ? 169.288 137.604 126.229 1.00 39.72 ?  328 ASP A CA    1 
ATOM   2650  C  C     . ASP A 1 328 ? 168.938 138.665 127.264 1.00 43.46 ?  328 ASP A C     1 
ATOM   2651  O  O     . ASP A 1 328 ? 169.812 139.049 128.048 1.00 47.01 ?  328 ASP A O     1 
ATOM   2652  C  CB    . ASP A 1 328 ? 170.339 138.159 125.266 1.00 41.20 ?  328 ASP A CB    1 
ATOM   2653  C  CG    . ASP A 1 328 ? 170.935 137.089 124.373 1.00 48.04 ?  328 ASP A CG    1 
ATOM   2654  O  OD1   . ASP A 1 328 ? 170.431 135.946 124.395 1.00 46.00 ?  328 ASP A OD1   1 
ATOM   2655  O  OD2   . ASP A 1 328 ? 171.907 137.389 123.650 1.00 47.87 -1 328 ASP A OD2   1 
ATOM   2656  N  N     . ASN A 1 329 ? 167.697 139.146 127.289 1.00 40.52 ?  329 ASN A N     1 
ATOM   2657  C  CA    . ASN A 1 329 ? 167.299 140.170 128.245 1.00 40.00 ?  329 ASN A CA    1 
ATOM   2658  C  C     . ASN A 1 329 ? 166.856 139.514 129.544 1.00 43.33 ?  329 ASN A C     1 
ATOM   2659  O  O     . ASN A 1 329 ? 165.871 138.764 129.539 1.00 43.25 ?  329 ASN A O     1 
ATOM   2660  C  CB    . ASN A 1 329 ? 166.174 141.022 127.683 1.00 36.36 ?  329 ASN A CB    1 
ATOM   2661  C  CG    . ASN A 1 329 ? 166.050 142.359 128.383 1.00 38.87 ?  329 ASN A CG    1 
ATOM   2662  O  OD1   . ASN A 1 329 ? 166.039 142.432 129.611 1.00 45.50 ?  329 ASN A OD1   1 
ATOM   2663  N  ND2   . ASN A 1 329 ? 165.961 143.427 127.602 1.00 36.20 ?  329 ASN A ND2   1 
ATOM   2664  N  N     . PRO A 1 330 ? 167.541 139.755 130.665 1.00 43.62 ?  330 PRO A N     1 
ATOM   2665  C  CA    . PRO A 1 330 ? 167.095 139.155 131.932 1.00 38.70 ?  330 PRO A CA    1 
ATOM   2666  C  C     . PRO A 1 330 ? 165.761 139.693 132.416 1.00 38.18 ?  330 PRO A C     1 
ATOM   2667  O  O     . PRO A 1 330 ? 165.044 138.981 133.130 1.00 41.07 ?  330 PRO A O     1 
ATOM   2668  C  CB    . PRO A 1 330 ? 168.232 139.503 132.902 1.00 40.51 ?  330 PRO A CB    1 
ATOM   2669  C  CG    . PRO A 1 330 ? 168.845 140.736 132.329 1.00 38.95 ?  330 PRO A CG    1 
ATOM   2670  C  CD    . PRO A 1 330 ? 168.742 140.590 130.838 1.00 40.23 ?  330 PRO A CD    1 
ATOM   2671  N  N     . ARG A 1 331 ? 165.405 140.925 132.052 1.00 37.03 ?  331 ARG A N     1 
ATOM   2672  C  CA    . ARG A 1 331 ? 164.150 141.520 132.495 1.00 38.27 ?  331 ARG A CA    1 
ATOM   2673  C  C     . ARG A 1 331 ? 162.952 141.050 131.684 1.00 39.55 ?  331 ARG A C     1 
ATOM   2674  O  O     . ARG A 1 331 ? 161.817 141.404 132.025 1.00 38.55 ?  331 ARG A O     1 
ATOM   2675  C  CB    . ARG A 1 331 ? 164.249 143.046 132.444 1.00 36.84 ?  331 ARG A CB    1 
ATOM   2676  C  CG    . ARG A 1 331 ? 165.152 143.631 133.517 1.00 38.30 ?  331 ARG A CG    1 
ATOM   2677  C  CD    . ARG A 1 331 ? 165.521 145.074 133.215 1.00 38.69 ?  331 ARG A CD    1 
ATOM   2678  N  NE    . ARG A 1 331 ? 166.131 145.222 131.898 1.00 41.16 ?  331 ARG A NE    1 
ATOM   2679  C  CZ    . ARG A 1 331 ? 167.361 144.835 131.591 1.00 40.35 ?  331 ARG A CZ    1 
ATOM   2680  N  NH1   . ARG A 1 331 ? 168.157 144.274 132.488 1.00 42.22 1  331 ARG A NH1   1 
ATOM   2681  N  NH2   . ARG A 1 331 ? 167.807 145.017 130.351 1.00 35.96 ?  331 ARG A NH2   1 
ATOM   2682  N  N     . VAL A 1 332 ? 163.170 140.274 130.629 1.00 35.93 ?  332 VAL A N     1 
ATOM   2683  C  CA    . VAL A 1 332 ? 162.096 139.662 129.859 1.00 34.17 ?  332 VAL A CA    1 
ATOM   2684  C  C     . VAL A 1 332 ? 161.931 138.232 130.353 1.00 37.50 ?  332 VAL A C     1 
ATOM   2685  O  O     . VAL A 1 332 ? 162.876 137.437 130.306 1.00 37.78 ?  332 VAL A O     1 
ATOM   2686  C  CB    . VAL A 1 332 ? 162.393 139.697 128.352 1.00 34.74 ?  332 VAL A CB    1 
ATOM   2687  C  CG1   . VAL A 1 332 ? 161.506 138.709 127.611 1.00 34.04 ?  332 VAL A CG1   1 
ATOM   2688  C  CG2   . VAL A 1 332 ? 162.206 141.102 127.806 1.00 35.22 ?  332 VAL A CG2   1 
ATOM   2689  N  N     . LYS A 1 333 ? 160.737 137.905 130.838 1.00 33.45 ?  333 LYS A N     1 
ATOM   2690  C  CA    . LYS A 1 333 ? 160.455 136.574 131.353 1.00 31.89 ?  333 LYS A CA    1 
ATOM   2691  C  C     . LYS A 1 333 ? 159.998 135.668 130.220 1.00 32.22 ?  333 LYS A C     1 
ATOM   2692  O  O     . LYS A 1 333 ? 159.192 136.066 129.375 1.00 36.70 ?  333 LYS A O     1 
ATOM   2693  C  CB    . LYS A 1 333 ? 159.392 136.635 132.450 1.00 29.77 ?  333 LYS A CB    1 
ATOM   2694  C  CG    . LYS A 1 333 ? 159.141 135.312 133.150 1.00 32.83 ?  333 LYS A CG    1 
ATOM   2695  C  CD    . LYS A 1 333 ? 158.296 135.503 134.398 1.00 33.72 ?  333 LYS A CD    1 
ATOM   2696  C  CE    . LYS A 1 333 ? 158.266 134.241 135.243 1.00 36.46 ?  333 LYS A CE    1 
ATOM   2697  N  NZ    . LYS A 1 333 ? 156.888 133.918 135.704 1.00 38.82 1  333 LYS A NZ    1 
ATOM   2698  N  N     . LYS A 1 334 ? 160.521 134.443 130.206 1.00 35.19 ?  334 LYS A N     1 
ATOM   2699  C  CA    . LYS A 1 334 ? 160.256 133.516 129.118 1.00 33.26 ?  334 LYS A CA    1 
ATOM   2700  C  C     . LYS A 1 334 ? 160.264 132.092 129.651 1.00 37.91 ?  334 LYS A C     1 
ATOM   2701  O  O     . LYS A 1 334 ? 160.817 131.807 130.717 1.00 40.87 ?  334 LYS A O     1 
ATOM   2702  C  CB    . LYS A 1 334 ? 161.287 133.664 127.994 1.00 31.87 ?  334 LYS A CB    1 
ATOM   2703  C  CG    . LYS A 1 334 ? 162.717 133.455 128.451 1.00 34.69 ?  334 LYS A CG    1 
ATOM   2704  C  CD    . LYS A 1 334 ? 163.695 134.188 127.557 1.00 33.81 ?  334 LYS A CD    1 
ATOM   2705  C  CE    . LYS A 1 334 ? 164.240 135.426 128.245 1.00 35.60 ?  334 LYS A CE    1 
ATOM   2706  N  NZ    . LYS A 1 334 ? 165.072 135.087 129.430 1.00 37.49 1  334 LYS A NZ    1 
ATOM   2707  N  N     . GLU A 1 335 ? 159.637 131.197 128.892 1.00 35.08 ?  335 GLU A N     1 
ATOM   2708  C  CA    . GLU A 1 335 ? 159.590 129.778 129.211 1.00 35.23 ?  335 GLU A CA    1 
ATOM   2709  C  C     . GLU A 1 335 ? 160.122 128.967 128.039 1.00 39.41 ?  335 GLU A C     1 
ATOM   2710  O  O     . GLU A 1 335 ? 159.836 129.270 126.876 1.00 44.34 ?  335 GLU A O     1 
ATOM   2711  C  CB    . GLU A 1 335 ? 158.168 129.328 129.560 1.00 34.11 ?  335 GLU A CB    1 
ATOM   2712  C  CG    . GLU A 1 335 ? 157.465 130.227 130.562 1.00 43.30 ?  335 GLU A CG    1 
ATOM   2713  C  CD    . GLU A 1 335 ? 157.171 129.523 131.872 1.00 43.64 ?  335 GLU A CD    1 
ATOM   2714  O  OE1   . GLU A 1 335 ? 158.098 128.903 132.435 1.00 40.96 ?  335 GLU A OE1   1 
ATOM   2715  O  OE2   . GLU A 1 335 ? 156.017 129.591 132.341 1.00 38.15 -1 335 GLU A OE2   1 
ATOM   2716  N  N     . LYS A 1 336 ? 160.900 127.936 128.361 1.00 38.66 ?  336 LYS A N     1 
ATOM   2717  C  CA    . LYS A 1 336 ? 161.487 127.056 127.361 1.00 34.38 ?  336 LYS A CA    1 
ATOM   2718  C  C     . LYS A 1 336 ? 160.424 126.135 126.773 1.00 38.68 ?  336 LYS A C     1 
ATOM   2719  O  O     . LYS A 1 336 ? 159.628 125.544 127.508 1.00 41.63 ?  336 LYS A O     1 
ATOM   2720  C  CB    . LYS A 1 336 ? 162.607 126.233 127.995 1.00 40.52 ?  336 LYS A CB    1 
ATOM   2721  C  CG    . LYS A 1 336 ? 163.815 125.983 127.113 1.00 42.05 ?  336 LYS A CG    1 
ATOM   2722  C  CD    . LYS A 1 336 ? 164.666 124.866 127.703 1.00 41.51 ?  336 LYS A CD    1 
ATOM   2723  C  CE    . LYS A 1 336 ? 165.516 124.184 126.649 1.00 40.22 ?  336 LYS A CE    1 
ATOM   2724  N  NZ    . LYS A 1 336 ? 166.066 122.886 127.127 1.00 41.73 1  336 LYS A NZ    1 
ATOM   2725  N  N     . ILE A 1 337 ? 160.413 126.014 125.443 1.00 36.69 ?  337 ILE A N     1 
ATOM   2726  C  CA    . ILE A 1 337 ? 159.522 125.101 124.740 1.00 33.68 ?  337 ILE A CA    1 
ATOM   2727  C  C     . ILE A 1 337 ? 160.300 124.429 123.618 1.00 32.64 ?  337 ILE A C     1 
ATOM   2728  O  O     . ILE A 1 337 ? 161.377 124.877 123.221 1.00 36.49 ?  337 ILE A O     1 
ATOM   2729  C  CB    . ILE A 1 337 ? 158.274 125.807 124.165 1.00 34.61 ?  337 ILE A CB    1 
ATOM   2730  C  CG1   . ILE A 1 337 ? 158.691 126.971 123.263 1.00 33.71 ?  337 ILE A CG1   1 
ATOM   2731  C  CG2   . ILE A 1 337 ? 157.351 126.277 125.280 1.00 35.33 ?  337 ILE A CG2   1 
ATOM   2732  C  CD1   . ILE A 1 337 ? 157.865 127.093 122.006 1.00 31.06 ?  337 ILE A CD1   1 
ATOM   2733  N  N     . ASN A 1 338 ? 159.736 123.337 123.105 1.00 33.74 ?  338 ASN A N     1 
ATOM   2734  C  CA    . ASN A 1 338 ? 160.291 122.681 121.933 1.00 35.16 ?  338 ASN A CA    1 
ATOM   2735  C  C     . ASN A 1 338 ? 159.451 123.061 120.725 1.00 32.98 ?  338 ASN A C     1 
ATOM   2736  O  O     . ASN A 1 338 ? 158.283 122.651 120.644 1.00 34.04 ?  338 ASN A O     1 
ATOM   2737  C  CB    . ASN A 1 338 ? 160.316 121.166 122.114 1.00 35.34 ?  338 ASN A CB    1 
ATOM   2738  C  CG    . ASN A 1 338 ? 161.079 120.462 121.010 1.00 36.98 ?  338 ASN A CG    1 
ATOM   2739  O  OD1   . ASN A 1 338 ? 160.668 119.409 120.527 1.00 37.66 ?  338 ASN A OD1   1 
ATOM   2740  N  ND2   . ASN A 1 338 ? 162.200 121.046 120.603 1.00 37.68 ?  338 ASN A ND2   1 
ATOM   2741  N  N     . PRO A 1 339 ? 159.978 123.845 119.781 1.00 35.25 ?  339 PRO A N     1 
ATOM   2742  C  CA    . PRO A 1 339 ? 159.158 124.260 118.631 1.00 31.07 ?  339 PRO A CA    1 
ATOM   2743  C  C     . PRO A 1 339 ? 158.656 123.103 117.786 1.00 32.75 ?  339 PRO A C     1 
ATOM   2744  O  O     . PRO A 1 339 ? 157.552 123.190 117.237 1.00 37.31 ?  339 PRO A O     1 
ATOM   2745  C  CB    . PRO A 1 339 ? 160.103 125.174 117.838 1.00 31.83 ?  339 PRO A CB    1 
ATOM   2746  C  CG    . PRO A 1 339 ? 161.470 124.798 118.284 1.00 34.70 ?  339 PRO A CG    1 
ATOM   2747  C  CD    . PRO A 1 339 ? 161.342 124.391 119.716 1.00 33.83 ?  339 PRO A CD    1 
ATOM   2748  N  N     . ARG A 1 340 ? 159.429 122.024 117.657 1.00 32.40 ?  340 ARG A N     1 
ATOM   2749  C  CA    . ARG A 1 340 ? 158.949 120.867 116.909 1.00 27.98 ?  340 ARG A CA    1 
ATOM   2750  C  C     . ARG A 1 340 ? 157.800 120.182 117.636 1.00 31.44 ?  340 ARG A C     1 
ATOM   2751  O  O     . ARG A 1 340 ? 156.836 119.733 117.004 1.00 37.96 ?  340 ARG A O     1 
ATOM   2752  C  CB    . ARG A 1 340 ? 160.095 119.889 116.657 1.00 30.71 ?  340 ARG A CB    1 
ATOM   2753  C  CG    . ARG A 1 340 ? 161.055 120.352 115.577 1.00 30.19 ?  340 ARG A CG    1 
ATOM   2754  C  CD    . ARG A 1 340 ? 161.908 119.214 115.053 1.00 27.86 ?  340 ARG A CD    1 
ATOM   2755  N  NE    . ARG A 1 340 ? 162.859 119.683 114.052 1.00 30.37 ?  340 ARG A NE    1 
ATOM   2756  C  CZ    . ARG A 1 340 ? 163.781 118.924 113.479 1.00 32.54 ?  340 ARG A CZ    1 
ATOM   2757  N  NH1   . ARG A 1 340 ? 163.909 117.643 113.784 1.00 32.83 1  340 ARG A NH1   1 
ATOM   2758  N  NH2   . ARG A 1 340 ? 164.597 119.463 112.577 1.00 32.68 ?  340 ARG A NH2   1 
ATOM   2759  N  N     . LYS A 1 341 ? 157.878 120.099 118.966 1.00 33.69 ?  341 LYS A N     1 
ATOM   2760  C  CA    . LYS A 1 341 ? 156.755 119.578 119.738 1.00 32.33 ?  341 LYS A CA    1 
ATOM   2761  C  C     . LYS A 1 341 ? 155.524 120.460 119.575 1.00 31.94 ?  341 LYS A C     1 
ATOM   2762  O  O     . LYS A 1 341 ? 154.400 119.957 119.486 1.00 35.86 ?  341 LYS A O     1 
ATOM   2763  C  CB    . LYS A 1 341 ? 157.137 119.457 121.212 1.00 35.30 ?  341 LYS A CB    1 
ATOM   2764  C  CG    . LYS A 1 341 ? 157.898 118.189 121.557 1.00 37.81 ?  341 LYS A CG    1 
ATOM   2765  C  CD    . LYS A 1 341 ? 157.205 116.955 121.004 1.00 36.37 ?  341 LYS A CD    1 
ATOM   2766  C  CE    . LYS A 1 341 ? 158.213 115.908 120.564 1.00 38.19 ?  341 LYS A CE    1 
ATOM   2767  N  NZ    . LYS A 1 341 ? 159.154 116.442 119.540 1.00 38.23 1  341 LYS A NZ    1 
ATOM   2768  N  N     . LEU A 1 342 ? 155.718 121.779 119.535 1.00 29.81 ?  342 LEU A N     1 
ATOM   2769  C  CA    . LEU A 1 342 ? 154.591 122.685 119.332 1.00 27.23 ?  342 LEU A CA    1 
ATOM   2770  C  C     . LEU A 1 342 ? 153.983 122.510 117.944 1.00 29.81 ?  342 LEU A C     1 
ATOM   2771  O  O     . LEU A 1 342 ? 152.758 122.554 117.788 1.00 36.01 ?  342 LEU A O     1 
ATOM   2772  C  CB    . LEU A 1 342 ? 155.038 124.130 119.554 1.00 28.01 ?  342 LEU A CB    1 
ATOM   2773  C  CG    . LEU A 1 342 ? 153.945 125.184 119.719 1.00 27.34 ?  342 LEU A CG    1 
ATOM   2774  C  CD1   . LEU A 1 342 ? 152.804 124.647 120.563 1.00 26.87 ?  342 LEU A CD1   1 
ATOM   2775  C  CD2   . LEU A 1 342 ? 154.523 126.442 120.344 1.00 28.36 ?  342 LEU A CD2   1 
ATOM   2776  N  N     . LEU A 1 343 ? 154.823 122.312 116.925 1.00 28.68 ?  343 LEU A N     1 
ATOM   2777  C  CA    . LEU A 1 343 ? 154.313 122.052 115.581 1.00 24.60 ?  343 LEU A CA    1 
ATOM   2778  C  C     . LEU A 1 343 ? 153.531 120.745 115.530 1.00 31.50 ?  343 LEU A C     1 
ATOM   2779  O  O     . LEU A 1 343 ? 152.479 120.664 114.885 1.00 36.23 ?  343 LEU A O     1 
ATOM   2780  C  CB    . LEU A 1 343 ? 155.467 122.023 114.581 1.00 28.60 ?  343 LEU A CB    1 
ATOM   2781  C  CG    . LEU A 1 343 ? 155.933 123.369 114.027 1.00 31.05 ?  343 LEU A CG    1 
ATOM   2782  C  CD1   . LEU A 1 343 ? 156.962 123.162 112.929 1.00 27.29 ?  343 LEU A CD1   1 
ATOM   2783  C  CD2   . LEU A 1 343 ? 154.753 124.175 113.512 1.00 30.62 ?  343 LEU A CD2   1 
ATOM   2784  N  N     . GLU A 1 344 ? 154.039 119.707 116.198 1.00 34.59 ?  344 GLU A N     1 
ATOM   2785  C  CA    . GLU A 1 344 ? 153.319 118.440 116.248 1.00 30.94 ?  344 GLU A CA    1 
ATOM   2786  C  C     . GLU A 1 344 ? 151.996 118.592 116.987 1.00 30.40 ?  344 GLU A C     1 
ATOM   2787  O  O     . GLU A 1 344 ? 150.994 117.976 116.612 1.00 39.33 ?  344 GLU A O     1 
ATOM   2788  C  CB    . GLU A 1 344 ? 154.186 117.365 116.904 1.00 31.41 ?  344 GLU A CB    1 
ATOM   2789  C  CG    . GLU A 1 344 ? 155.419 116.995 116.098 1.00 33.61 ?  344 GLU A CG    1 
ATOM   2790  C  CD    . GLU A 1 344 ? 156.460 116.271 116.927 1.00 40.44 ?  344 GLU A CD    1 
ATOM   2791  O  OE1   . GLU A 1 344 ? 156.116 115.790 118.027 1.00 41.47 ?  344 GLU A OE1   1 
ATOM   2792  O  OE2   . GLU A 1 344 ? 157.623 116.187 116.482 1.00 40.14 -1 344 GLU A OE2   1 
ATOM   2793  N  N     . LYS A 1 345 ? 151.975 119.406 118.043 1.00 29.13 ?  345 LYS A N     1 
ATOM   2794  C  CA    . LYS A 1 345 ? 150.726 119.681 118.748 1.00 29.09 ?  345 LYS A CA    1 
ATOM   2795  C  C     . LYS A 1 345 ? 149.735 120.411 117.850 1.00 29.83 ?  345 LYS A C     1 
ATOM   2796  O  O     . LYS A 1 345 ? 148.537 120.107 117.866 1.00 31.83 ?  345 LYS A O     1 
ATOM   2797  C  CB    . LYS A 1 345 ? 151.005 120.493 120.013 1.00 26.73 ?  345 LYS A CB    1 
ATOM   2798  C  CG    . LYS A 1 345 ? 149.768 120.786 120.842 1.00 29.26 ?  345 LYS A CG    1 
ATOM   2799  C  CD    . LYS A 1 345 ? 150.111 121.564 122.098 1.00 30.18 ?  345 LYS A CD    1 
ATOM   2800  C  CE    . LYS A 1 345 ? 148.861 121.886 122.900 1.00 32.03 ?  345 LYS A CE    1 
ATOM   2801  N  NZ    . LYS A 1 345 ? 149.164 122.696 124.109 1.00 31.82 1  345 LYS A NZ    1 
ATOM   2802  N  N     . LEU A 1 346 ? 150.215 121.377 117.064 1.00 32.88 ?  346 LEU A N     1 
ATOM   2803  C  CA    . LEU A 1 346 ? 149.345 122.062 116.112 1.00 25.13 ?  346 LEU A CA    1 
ATOM   2804  C  C     . LEU A 1 346 ? 148.768 121.086 115.098 1.00 26.69 ?  346 LEU A C     1 
ATOM   2805  O  O     . LEU A 1 346 ? 147.569 121.127 114.797 1.00 32.19 ?  346 LEU A O     1 
ATOM   2806  C  CB    . LEU A 1 346 ? 150.113 123.172 115.392 1.00 24.17 ?  346 LEU A CB    1 
ATOM   2807  C  CG    . LEU A 1 346 ? 150.654 124.352 116.198 1.00 26.88 ?  346 LEU A CG    1 
ATOM   2808  C  CD1   . LEU A 1 346 ? 151.710 125.091 115.396 1.00 27.67 ?  346 LEU A CD1   1 
ATOM   2809  C  CD2   . LEU A 1 346 ? 149.534 125.292 116.583 1.00 28.49 ?  346 LEU A CD2   1 
ATOM   2810  N  N     . ALA A 1 347 ? 149.608 120.199 114.560 1.00 25.65 ?  347 ALA A N     1 
ATOM   2811  C  CA    . ALA A 1 347 ? 149.134 119.224 113.584 1.00 26.16 ?  347 ALA A CA    1 
ATOM   2812  C  C     . ALA A 1 347 ? 148.126 118.262 114.202 1.00 29.62 ?  347 ALA A C     1 
ATOM   2813  O  O     . ALA A 1 347 ? 147.112 117.932 113.578 1.00 35.76 ?  347 ALA A O     1 
ATOM   2814  C  CB    . ALA A 1 347 ? 150.314 118.458 112.990 1.00 26.21 ?  347 ALA A CB    1 
ATOM   2815  N  N     . MET A 1 348 ? 148.386 117.805 115.429 1.00 31.30 ?  348 MET A N     1 
ATOM   2816  C  CA    . MET A 1 348 ? 147.455 116.905 116.100 1.00 34.50 ?  348 MET A CA    1 
ATOM   2817  C  C     . MET A 1 348 ? 146.119 117.588 116.359 1.00 31.34 ?  348 MET A C     1 
ATOM   2818  O  O     . MET A 1 348 ? 145.056 116.995 116.142 1.00 36.47 ?  348 MET A O     1 
ATOM   2819  C  CB    . MET A 1 348 ? 148.068 116.402 117.408 1.00 32.72 ?  348 MET A CB    1 
ATOM   2820  C  CG    . MET A 1 348 ? 147.073 115.786 118.375 1.00 37.45 ?  348 MET A CG    1 
ATOM   2821  S  SD    . MET A 1 348 ? 146.803 116.804 119.840 1.00 55.87 ?  348 MET A SD    1 
ATOM   2822  C  CE    . MET A 1 348 ? 148.448 116.826 120.546 1.00 38.89 ?  348 MET A CE    1 
ATOM   2823  N  N     . LEU A 1 349 ? 146.153 118.842 116.816 1.00 27.73 ?  349 LEU A N     1 
ATOM   2824  C  CA    . LEU A 1 349 ? 144.916 119.570 117.073 1.00 22.99 ?  349 LEU A CA    1 
ATOM   2825  C  C     . LEU A 1 349 ? 144.139 119.808 115.786 1.00 28.25 ?  349 LEU A C     1 
ATOM   2826  O  O     . LEU A 1 349 ? 142.905 119.729 115.775 1.00 30.06 ?  349 LEU A O     1 
ATOM   2827  C  CB    . LEU A 1 349 ? 145.225 120.893 117.768 1.00 26.16 ?  349 LEU A CB    1 
ATOM   2828  C  CG    . LEU A 1 349 ? 145.195 120.843 119.293 1.00 32.55 ?  349 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A 1 349 ? 146.043 121.957 119.863 1.00 30.67 ?  349 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A 1 349 ? 143.768 120.935 119.807 1.00 34.59 ?  349 LEU A CD2   1 
ATOM   2831  N  N     . ARG A 1 350 ? 144.840 120.115 114.692 1.00 29.88 ?  350 ARG A N     1 
ATOM   2832  C  CA    . ARG A 1 350 ? 144.163 120.282 113.412 1.00 24.31 ?  350 ARG A CA    1 
ATOM   2833  C  C     . ARG A 1 350 ? 143.570 118.970 112.917 1.00 30.19 ?  350 ARG A C     1 
ATOM   2834  O  O     . ARG A 1 350 ? 142.510 118.971 112.283 1.00 34.35 ?  350 ARG A O     1 
ATOM   2835  C  CB    . ARG A 1 350 ? 145.128 120.861 112.380 1.00 26.02 ?  350 ARG A CB    1 
ATOM   2836  C  CG    . ARG A 1 350 ? 145.419 122.340 112.576 1.00 24.05 ?  350 ARG A CG    1 
ATOM   2837  C  CD    . ARG A 1 350 ? 146.613 122.786 111.754 1.00 23.05 ?  350 ARG A CD    1 
ATOM   2838  N  NE    . ARG A 1 350 ? 146.327 122.736 110.327 1.00 34.27 ?  350 ARG A NE    1 
ATOM   2839  C  CZ    . ARG A 1 350 ? 145.608 123.638 109.671 1.00 31.39 ?  350 ARG A CZ    1 
ATOM   2840  N  NH1   . ARG A 1 350 ? 145.095 124.692 110.284 1.00 24.59 1  350 ARG A NH1   1 
ATOM   2841  N  NH2   . ARG A 1 350 ? 145.395 123.475 108.369 1.00 28.80 ?  350 ARG A NH2   1 
ATOM   2842  N  N     . SER A 1 351 ? 144.241 117.847 113.181 1.00 33.50 ?  351 SER A N     1 
ATOM   2843  C  CA    . SER A 1 351 ? 143.667 116.552 112.836 1.00 30.16 ?  351 SER A CA    1 
ATOM   2844  C  C     . SER A 1 351 ? 142.402 116.277 113.639 1.00 31.45 ?  351 SER A C     1 
ATOM   2845  O  O     . SER A 1 351 ? 141.409 115.780 113.097 1.00 38.80 ?  351 SER A O     1 
ATOM   2846  C  CB    . SER A 1 351 ? 144.697 115.446 113.060 1.00 30.96 ?  351 SER A CB    1 
ATOM   2847  O  OG    . SER A 1 351 ? 145.693 115.464 112.054 1.00 39.77 ?  351 SER A OG    1 
ATOM   2848  N  N     . GLU A 1 352 ? 142.419 116.596 114.936 1.00 29.70 ?  352 GLU A N     1 
ATOM   2849  C  CA    . GLU A 1 352 ? 141.260 116.314 115.780 1.00 30.98 ?  352 GLU A CA    1 
ATOM   2850  C  C     . GLU A 1 352 ? 140.080 117.221 115.443 1.00 34.19 ?  352 GLU A C     1 
ATOM   2851  O  O     . GLU A 1 352 ? 138.946 116.749 115.306 1.00 39.10 ?  352 GLU A O     1 
ATOM   2852  C  CB    . GLU A 1 352 ? 141.629 116.447 117.259 1.00 33.49 ?  352 GLU A CB    1 
ATOM   2853  C  CG    . GLU A 1 352 ? 142.826 115.621 117.693 1.00 33.65 ?  352 GLU A CG    1 
ATOM   2854  C  CD    . GLU A 1 352 ? 143.283 115.954 119.100 1.00 42.38 ?  352 GLU A CD    1 
ATOM   2855  O  OE1   . GLU A 1 352 ? 143.945 115.103 119.729 1.00 41.46 ?  352 GLU A OE1   1 
ATOM   2856  O  OE2   . GLU A 1 352 ? 142.978 117.067 119.578 1.00 41.70 -1 352 GLU A OE2   1 
ATOM   2857  N  N     . SER A 1 353 ? 140.321 118.528 115.309 1.00 34.69 ?  353 SER A N     1 
ATOM   2858  C  CA    . SER A 1 353 ? 139.231 119.488 115.207 1.00 34.74 ?  353 SER A CA    1 
ATOM   2859  C  C     . SER A 1 353 ? 139.381 120.511 114.089 1.00 30.47 ?  353 SER A C     1 
ATOM   2860  O  O     . SER A 1 353 ? 138.477 121.334 113.909 1.00 31.06 ?  353 SER A O     1 
ATOM   2861  C  CB    . SER A 1 353 ? 139.061 120.236 116.538 1.00 34.34 ?  353 SER A CB    1 
ATOM   2862  O  OG    . SER A 1 353 ? 140.211 121.006 116.842 1.00 32.37 ?  353 SER A OG    1 
ATOM   2863  N  N     . GLY A 1 354 ? 140.479 120.495 113.340 1.00 27.70 ?  354 GLY A N     1 
ATOM   2864  C  CA    . GLY A 1 354 ? 140.697 121.488 112.310 1.00 27.40 ?  354 GLY A CA    1 
ATOM   2865  C  C     . GLY A 1 354 ? 141.247 122.805 112.801 1.00 21.81 ?  354 GLY A C     1 
ATOM   2866  O  O     . GLY A 1 354 ? 141.467 123.709 111.985 1.00 25.58 ?  354 GLY A O     1 
ATOM   2867  N  N     . TYR A 1 355 ? 141.481 122.944 114.101 1.00 22.77 ?  355 TYR A N     1 
ATOM   2868  C  CA    . TYR A 1 355 ? 142.010 124.141 114.722 1.00 17.75 ?  355 TYR A CA    1 
ATOM   2869  C  C     . TYR A 1 355 ? 143.454 123.916 115.158 1.00 22.19 ?  355 TYR A C     1 
ATOM   2870  O  O     . TYR A 1 355 ? 143.850 122.781 115.438 1.00 28.86 ?  355 TYR A O     1 
ATOM   2871  C  CB    . TYR A 1 355 ? 141.167 124.544 115.937 1.00 23.82 ?  355 TYR A CB    1 
ATOM   2872  C  CG    . TYR A 1 355 ? 139.798 125.072 115.584 1.00 26.78 ?  355 TYR A CG    1 
ATOM   2873  C  CD1   . TYR A 1 355 ? 139.651 126.161 114.737 1.00 20.43 ?  355 TYR A CD1   1 
ATOM   2874  C  CD2   . TYR A 1 355 ? 138.651 124.481 116.096 1.00 25.91 ?  355 TYR A CD2   1 
ATOM   2875  C  CE1   . TYR A 1 355 ? 138.402 126.646 114.411 1.00 27.50 ?  355 TYR A CE1   1 
ATOM   2876  C  CE2   . TYR A 1 355 ? 137.397 124.960 115.776 1.00 26.03 ?  355 TYR A CE2   1 
ATOM   2877  C  CZ    . TYR A 1 355 ? 137.278 126.042 114.933 1.00 30.59 ?  355 TYR A CZ    1 
ATOM   2878  O  OH    . TYR A 1 355 ? 136.031 126.524 114.610 1.00 31.21 ?  355 TYR A OH    1 
ATOM   2879  N  N     . PRO A 1 356 ? 144.269 124.972 115.237 1.00 22.84 ?  356 PRO A N     1 
ATOM   2880  C  CA    . PRO A 1 356 ? 143.970 126.382 114.961 1.00 17.73 ?  356 PRO A CA    1 
ATOM   2881  C  C     . PRO A 1 356 ? 144.168 126.774 113.506 1.00 15.52 ?  356 PRO A C     1 
ATOM   2882  O  O     . PRO A 1 356 ? 144.759 126.033 112.728 1.00 19.50 ?  356 PRO A O     1 
ATOM   2883  C  CB    . PRO A 1 356 ? 144.970 127.107 115.863 1.00 18.27 ?  356 PRO A CB    1 
ATOM   2884  C  CG    . PRO A 1 356 ? 146.178 126.220 115.806 1.00 17.73 ?  356 PRO A CG    1 
ATOM   2885  C  CD    . PRO A 1 356 ? 145.644 124.807 115.740 1.00 13.52 ?  356 PRO A CD    1 
ATOM   2886  N  N     . TYR A 1 357 ? 143.676 127.945 113.110 1.00 18.54 ?  357 TYR A N     1 
ATOM   2887  C  CA    . TYR A 1 357 ? 144.119 128.541 111.861 1.00 11.30 ?  357 TYR A CA    1 
ATOM   2888  C  C     . TYR A 1 357 ? 145.586 128.933 111.982 1.00 16.15 ?  357 TYR A C     1 
ATOM   2889  O  O     . TYR A 1 357 ? 146.059 129.336 113.047 1.00 25.34 ?  357 TYR A O     1 
ATOM   2890  C  CB    . TYR A 1 357 ? 143.279 129.771 111.510 1.00 15.07 ?  357 TYR A CB    1 
ATOM   2891  C  CG    . TYR A 1 357 ? 141.788 129.621 111.721 1.00 18.99 ?  357 TYR A CG    1 
ATOM   2892  C  CD1   . TYR A 1 357 ? 141.147 128.415 111.485 1.00 14.29 ?  357 TYR A CD1   1 
ATOM   2893  C  CD2   . TYR A 1 357 ? 141.020 130.692 112.154 1.00 18.46 ?  357 TYR A CD2   1 
ATOM   2894  C  CE1   . TYR A 1 357 ? 139.790 128.276 111.670 1.00 14.64 ?  357 TYR A CE1   1 
ATOM   2895  C  CE2   . TYR A 1 357 ? 139.660 130.565 112.345 1.00 17.60 ?  357 TYR A CE2   1 
ATOM   2896  C  CZ    . TYR A 1 357 ? 139.050 129.353 112.102 1.00 21.97 ?  357 TYR A CZ    1 
ATOM   2897  O  OH    . TYR A 1 357 ? 137.695 129.215 112.288 1.00 26.52 ?  357 TYR A OH    1 
ATOM   2898  N  N     . ILE A 1 358 ? 146.313 128.803 110.879 1.00 14.85 ?  358 ILE A N     1 
ATOM   2899  C  CA    . ILE A 1 358 ? 147.740 129.092 110.841 1.00 13.71 ?  358 ILE A CA    1 
ATOM   2900  C  C     . ILE A 1 358 ? 147.952 130.362 110.032 1.00 16.73 ?  358 ILE A C     1 
ATOM   2901  O  O     . ILE A 1 358 ? 147.537 130.442 108.870 1.00 25.12 ?  358 ILE A O     1 
ATOM   2902  C  CB    . ILE A 1 358 ? 148.541 127.923 110.244 1.00 18.73 ?  358 ILE A CB    1 
ATOM   2903  C  CG1   . ILE A 1 358 ? 148.175 126.611 110.940 1.00 21.88 ?  358 ILE A CG1   1 
ATOM   2904  C  CG2   . ILE A 1 358 ? 150.032 128.193 110.356 1.00 17.24 ?  358 ILE A CG2   1 
ATOM   2905  C  CD1   . ILE A 1 358 ? 148.572 126.558 112.395 1.00 18.48 ?  358 ILE A CD1   1 
ATOM   2906  N  N     . MET A 1 359 ? 148.592 131.353 110.645 1.00 10.67 ?  359 MET A N     1 
ATOM   2907  C  CA    . MET A 1 359 ? 148.994 132.572 109.959 1.00 8.82  ?  359 MET A CA    1 
ATOM   2908  C  C     . MET A 1 359 ? 150.513 132.628 109.936 1.00 10.43 ?  359 MET A C     1 
ATOM   2909  O  O     . MET A 1 359 ? 151.151 132.679 110.993 1.00 21.36 ?  359 MET A O     1 
ATOM   2910  C  CB    . MET A 1 359 ? 148.423 133.815 110.641 1.00 11.87 ?  359 MET A CB    1 
ATOM   2911  C  CG    . MET A 1 359 ? 147.910 134.859 109.665 1.00 12.10 ?  359 MET A CG    1 
ATOM   2912  S  SD    . MET A 1 359 ? 147.991 136.558 110.256 1.00 33.65 ?  359 MET A SD    1 
ATOM   2913  C  CE    . MET A 1 359 ? 149.753 136.851 110.238 1.00 12.22 ?  359 MET A CE    1 
ATOM   2914  N  N     . PHE A 1 360 ? 151.086 132.612 108.738 1.00 10.78 ?  360 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 360 ? 152.527 132.761 108.566 1.00 11.58 ?  360 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 360 ? 152.818 134.253 108.474 1.00 15.89 ?  360 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 360 ? 152.655 134.865 107.417 1.00 25.75 ?  360 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 360 ? 153.001 131.998 107.335 1.00 9.13  ?  360 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 360 ? 152.805 130.512 107.442 1.00 17.71 ?  360 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 360 ? 153.394 129.798 108.470 1.00 16.06 ?  360 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 360 ? 152.022 129.833 106.525 1.00 13.68 ?  360 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 360 ? 153.212 128.434 108.578 1.00 11.57 ?  360 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 360 ? 151.838 128.471 106.627 1.00 17.28 ?  360 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 360 ? 152.434 127.769 107.655 1.00 15.05 ?  360 PHE A CZ    1 
ATOM   2925  N  N     . GLN A 1 361 ? 153.249 134.834 109.596 1.00 11.68 ?  361 GLN A N     1 
ATOM   2926  C  CA    . GLN A 1 361 ? 153.330 136.287 109.717 1.00 11.92 ?  361 GLN A CA    1 
ATOM   2927  C  C     . GLN A 1 361 ? 154.253 136.890 108.667 1.00 15.94 ?  361 GLN A C     1 
ATOM   2928  O  O     . GLN A 1 361 ? 153.913 137.892 108.024 1.00 20.44 ?  361 GLN A O     1 
ATOM   2929  C  CB    . GLN A 1 361 ? 153.805 136.661 111.121 1.00 23.22 ?  361 GLN A CB    1 
ATOM   2930  C  CG    . GLN A 1 361 ? 153.616 138.125 111.469 1.00 17.97 ?  361 GLN A CG    1 
ATOM   2931  C  CD    . GLN A 1 361 ? 153.213 138.334 112.911 1.00 20.29 ?  361 GLN A CD    1 
ATOM   2932  O  OE1   . GLN A 1 361 ? 153.611 137.576 113.793 1.00 24.15 ?  361 GLN A OE1   1 
ATOM   2933  N  NE2   . GLN A 1 361 ? 152.423 139.370 113.159 1.00 23.91 ?  361 GLN A NE2   1 
ATOM   2934  N  N     . ASP A 1 362 ? 155.433 136.298 108.480 1.00 18.11 ?  362 ASP A N     1 
ATOM   2935  C  CA    . ASP A 1 362 ? 156.387 136.868 107.537 1.00 17.14 ?  362 ASP A CA    1 
ATOM   2936  C  C     . ASP A 1 362 ? 155.950 136.662 106.094 1.00 18.27 ?  362 ASP A C     1 
ATOM   2937  O  O     . ASP A 1 362 ? 156.230 137.511 105.243 1.00 19.69 ?  362 ASP A O     1 
ATOM   2938  C  CB    . ASP A 1 362 ? 157.775 136.281 107.773 1.00 18.97 ?  362 ASP A CB    1 
ATOM   2939  C  CG    . ASP A 1 362 ? 158.281 136.542 109.175 1.00 30.49 ?  362 ASP A CG    1 
ATOM   2940  O  OD1   . ASP A 1 362 ? 157.526 136.292 110.139 1.00 27.74 ?  362 ASP A OD1   1 
ATOM   2941  O  OD2   . ASP A 1 362 ? 159.433 137.001 109.316 1.00 34.52 -1 362 ASP A OD2   1 
ATOM   2942  N  N     . ASN A 1 363 ? 155.251 135.564 105.802 1.00 18.08 ?  363 ASN A N     1 
ATOM   2943  C  CA    . ASN A 1 363 ? 154.691 135.386 104.467 1.00 10.98 ?  363 ASN A CA    1 
ATOM   2944  C  C     . ASN A 1 363 ? 153.676 136.477 104.151 1.00 13.44 ?  363 ASN A C     1 
ATOM   2945  O  O     . ASN A 1 363 ? 153.589 136.947 103.010 1.00 21.41 ?  363 ASN A O     1 
ATOM   2946  C  CB    . ASN A 1 363 ? 154.051 134.004 104.342 1.00 11.67 ?  363 ASN A CB    1 
ATOM   2947  C  CG    . ASN A 1 363 ? 155.069 132.913 104.089 1.00 18.13 ?  363 ASN A CG    1 
ATOM   2948  O  OD1   . ASN A 1 363 ? 156.234 133.188 103.808 1.00 19.36 ?  363 ASN A OD1   1 
ATOM   2949  N  ND2   . ASN A 1 363 ? 154.632 131.664 104.185 1.00 18.77 ?  363 ASN A ND2   1 
ATOM   2950  N  N     . VAL A 1 364 ? 152.893 136.888 105.149 1.00 9.09  ?  364 VAL A N     1 
ATOM   2951  C  CA    . VAL A 1 364 ? 151.940 137.974 104.950 1.00 10.59 ?  364 VAL A CA    1 
ATOM   2952  C  C     . VAL A 1 364 ? 152.667 139.304 104.797 1.00 17.38 ?  364 VAL A C     1 
ATOM   2953  O  O     . VAL A 1 364 ? 152.346 140.110 103.916 1.00 16.12 ?  364 VAL A O     1 
ATOM   2954  C  CB    . VAL A 1 364 ? 150.932 138.022 106.112 1.00 1.48  ?  364 VAL A CB    1 
ATOM   2955  C  CG1   . VAL A 1 364 ? 149.891 139.097 105.860 1.00 4.43  ?  364 VAL A CG1   1 
ATOM   2956  C  CG2   . VAL A 1 364 ? 150.275 136.671 106.307 1.00 8.10  ?  364 VAL A CG2   1 
ATOM   2957  N  N     . ASN A 1 365 ? 153.661 139.554 105.649 1.00 21.00 ?  365 ASN A N     1 
ATOM   2958  C  CA    . ASN A 1 365 ? 154.241 140.883 105.777 1.00 11.91 ?  365 ASN A CA    1 
ATOM   2959  C  C     . ASN A 1 365 ? 155.383 141.161 104.807 1.00 15.26 ?  365 ASN A C     1 
ATOM   2960  O  O     . ASN A 1 365 ? 155.772 142.324 104.663 1.00 21.76 ?  365 ASN A O     1 
ATOM   2961  C  CB    . ASN A 1 365 ? 154.726 141.102 107.213 1.00 13.85 ?  365 ASN A CB    1 
ATOM   2962  C  CG    . ASN A 1 365 ? 153.584 141.321 108.181 1.00 15.71 ?  365 ASN A CG    1 
ATOM   2963  O  OD1   . ASN A 1 365 ? 152.750 142.204 107.985 1.00 12.41 ?  365 ASN A OD1   1 
ATOM   2964  N  ND2   . ASN A 1 365 ? 153.535 140.511 109.231 1.00 18.99 ?  365 ASN A ND2   1 
ATOM   2965  N  N     . LYS A 1 366 ? 155.927 140.145 104.137 1.00 19.00 ?  366 LYS A N     1 
ATOM   2966  C  CA    . LYS A 1 366 ? 156.944 140.392 103.126 1.00 15.84 ?  366 LYS A CA    1 
ATOM   2967  C  C     . LYS A 1 366 ? 156.353 140.908 101.824 1.00 19.99 ?  366 LYS A C     1 
ATOM   2968  O  O     . LYS A 1 366 ? 157.095 141.442 100.992 1.00 29.30 ?  366 LYS A O     1 
ATOM   2969  C  CB    . LYS A 1 366 ? 157.749 139.116 102.865 1.00 13.23 ?  366 LYS A CB    1 
ATOM   2970  C  CG    . LYS A 1 366 ? 157.100 138.147 101.895 1.00 19.82 ?  366 LYS A CG    1 
ATOM   2971  C  CD    . LYS A 1 366 ? 157.565 136.723 102.156 1.00 23.35 ?  366 LYS A CD    1 
ATOM   2972  C  CE    . LYS A 1 366 ? 156.814 135.726 101.289 1.00 26.32 ?  366 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A 1 366 ? 155.375 136.080 101.142 1.00 25.54 1  366 LYS A NZ    1 
ATOM   2974  N  N     . VAL A 1 367 ? 155.044 140.764 101.635 1.00 25.26 ?  367 VAL A N     1 
ATOM   2975  C  CA    . VAL A 1 367 ? 154.331 141.331 100.500 1.00 15.02 ?  367 VAL A CA    1 
ATOM   2976  C  C     . VAL A 1 367 ? 153.263 142.319 100.929 1.00 14.05 ?  367 VAL A C     1 
ATOM   2977  O  O     . VAL A 1 367 ? 152.524 142.824 100.079 1.00 18.32 ?  367 VAL A O     1 
ATOM   2978  C  CB    . VAL A 1 367 ? 153.715 140.226 99.619  1.00 13.12 ?  367 VAL A CB    1 
ATOM   2979  C  CG1   . VAL A 1 367 ? 154.786 139.582 98.755  1.00 17.27 ?  367 VAL A CG1   1 
ATOM   2980  C  CG2   . VAL A 1 367 ? 153.037 139.185 100.486 1.00 4.98  ?  367 VAL A CG2   1 
ATOM   2981  N  N     . HIS A 1 368 ? 153.159 142.610 102.224 1.00 14.46 ?  368 HIS A N     1 
ATOM   2982  C  CA    . HIS A 1 368 ? 152.184 143.574 102.713 1.00 6.03  ?  368 HIS A CA    1 
ATOM   2983  C  C     . HIS A 1 368 ? 152.548 144.973 102.234 1.00 15.52 ?  368 HIS A C     1 
ATOM   2984  O  O     . HIS A 1 368 ? 153.685 145.424 102.399 1.00 25.03 ?  368 HIS A O     1 
ATOM   2985  C  CB    . HIS A 1 368 ? 152.127 143.531 104.238 1.00 12.53 ?  368 HIS A CB    1 
ATOM   2986  C  CG    . HIS A 1 368 ? 151.012 144.335 104.826 1.00 8.17  ?  368 HIS A CG    1 
ATOM   2987  N  ND1   . HIS A 1 368 ? 151.144 145.035 106.006 1.00 13.52 ?  368 HIS A ND1   1 
ATOM   2988  C  CD2   . HIS A 1 368 ? 149.745 144.550 104.401 1.00 10.74 ?  368 HIS A CD2   1 
ATOM   2989  C  CE1   . HIS A 1 368 ? 150.006 145.646 106.282 1.00 15.09 ?  368 HIS A CE1   1 
ATOM   2990  N  NE2   . HIS A 1 368 ? 149.141 145.368 105.323 1.00 7.25  ?  368 HIS A NE2   1 
ATOM   2991  N  N     . ALA A 1 369 ? 151.574 145.662 101.640 1.00 18.25 ?  369 ALA A N     1 
ATOM   2992  C  CA    . ALA A 1 369 ? 151.824 146.984 101.086 1.00 12.50 ?  369 ALA A CA    1 
ATOM   2993  C  C     . ALA A 1 369 ? 151.743 148.092 102.125 1.00 17.79 ?  369 ALA A C     1 
ATOM   2994  O  O     . ALA A 1 369 ? 152.235 149.195 101.870 1.00 25.01 ?  369 ALA A O     1 
ATOM   2995  C  CB    . ALA A 1 369 ? 150.834 147.273 99.957  1.00 8.96  ?  369 ALA A CB    1 
ATOM   2996  N  N     . ASN A 1 370 ? 151.153 147.828 103.286 1.00 17.23 ?  370 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 370 ? 150.910 148.849 104.297 1.00 12.34 ?  370 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 370 ? 151.603 148.505 105.608 1.00 12.14 ?  370 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 370 ? 151.027 148.637 106.689 1.00 21.21 ?  370 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 370 ? 149.413 149.047 104.515 1.00 12.21 ?  370 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 370 ? 148.689 149.430 103.244 1.00 10.47 ?  370 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 370 ? 148.991 150.451 102.628 1.00 26.58 ?  370 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 370 ? 147.729 148.611 102.839 1.00 12.40 ?  370 ASN A ND2   1 
ATOM   3004  N  N     . ASN A 1 371 ? 152.857 148.055 105.528 1.00 14.37 ?  371 ASN A N     1 
ATOM   3005  C  CA    . ASN A 1 371 ? 153.628 147.788 106.736 1.00 11.15 ?  371 ASN A CA    1 
ATOM   3006  C  C     . ASN A 1 371 ? 153.947 149.060 107.509 1.00 16.52 ?  371 ASN A C     1 
ATOM   3007  O  O     . ASN A 1 371 ? 154.177 148.991 108.720 1.00 19.08 ?  371 ASN A O     1 
ATOM   3008  C  CB    . ASN A 1 371 ? 154.922 147.054 106.387 1.00 8.50  ?  371 ASN A CB    1 
ATOM   3009  C  CG    . ASN A 1 371 ? 154.731 145.556 106.290 1.00 16.56 ?  371 ASN A CG    1 
ATOM   3010  O  OD1   . ASN A 1 371 ? 153.805 145.000 106.878 1.00 20.95 ?  371 ASN A OD1   1 
ATOM   3011  N  ND2   . ASN A 1 371 ? 155.608 144.894 105.547 1.00 18.37 ?  371 ASN A ND2   1 
ATOM   3012  N  N     . HIS A 1 372 ? 153.977 150.212 106.835 1.00 19.53 ?  372 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 372 ? 154.208 151.473 107.532 1.00 15.92 ?  372 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 372 ? 153.084 151.775 108.514 1.00 16.49 ?  372 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 372 ? 153.335 152.241 109.632 1.00 25.78 ?  372 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 372 ? 154.361 152.608 106.521 1.00 18.05 ?  372 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 372 ? 153.110 152.905 105.755 1.00 18.35 ?  372 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 372 ? 152.510 151.985 104.924 1.00 23.68 ?  372 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 372 ? 152.339 154.017 105.703 1.00 18.43 ?  372 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 372 ? 151.425 152.517 104.391 1.00 17.06 ?  372 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 372 ? 151.301 153.750 104.845 1.00 17.38 ?  372 HIS A NE2   1 
ATOM   3022  N  N     . ILE A 1 373 ? 151.836 151.528 108.110 1.00 16.32 ?  373 ILE A N     1 
ATOM   3023  C  CA    . ILE A 1 373 ? 150.712 151.692 109.028 1.00 18.68 ?  373 ILE A CA    1 
ATOM   3024  C  C     . ILE A 1 373 ? 150.829 150.703 110.177 1.00 15.16 ?  373 ILE A C     1 
ATOM   3025  O  O     . ILE A 1 373 ? 150.775 151.075 111.355 1.00 28.13 ?  373 ILE A O     1 
ATOM   3026  C  CB    . ILE A 1 373 ? 149.379 151.520 108.279 1.00 19.22 ?  373 ILE A CB    1 
ATOM   3027  C  CG1   . ILE A 1 373 ? 149.261 152.541 107.150 1.00 15.45 ?  373 ILE A CG1   1 
ATOM   3028  C  CG2   . ILE A 1 373 ? 148.206 151.634 109.240 1.00 19.60 ?  373 ILE A CG2   1 
ATOM   3029  C  CD1   . ILE A 1 373 ? 148.138 152.252 106.185 1.00 15.20 ?  373 ILE A CD1   1 
ATOM   3030  N  N     . SER A 1 374 ? 151.019 149.427 109.843 1.00 16.92 ?  374 SER A N     1 
ATOM   3031  C  CA    . SER A 1 374 ? 151.160 148.351 110.812 1.00 12.66 ?  374 SER A CA    1 
ATOM   3032  C  C     . SER A 1 374 ? 151.468 147.055 110.079 1.00 14.27 ?  374 SER A C     1 
ATOM   3033  O  O     . SER A 1 374 ? 151.115 146.904 108.906 1.00 21.20 ?  374 SER A O     1 
ATOM   3034  C  CB    . SER A 1 374 ? 149.889 148.195 111.647 1.00 19.05 ?  374 SER A CB    1 
ATOM   3035  O  OG    . SER A 1 374 ? 150.112 147.347 112.757 1.00 24.05 ?  374 SER A OG    1 
ATOM   3036  N  N     . LYS A 1 375 ? 152.124 146.118 110.749 1.00 22.39 ?  375 LYS A N     1 
ATOM   3037  C  CA    . LYS A 1 375 ? 152.252 144.782 110.196 1.00 19.34 ?  375 LYS A CA    1 
ATOM   3038  C  C     . LYS A 1 375 ? 151.003 143.972 110.512 1.00 15.28 ?  375 LYS A C     1 
ATOM   3039  O  O     . LYS A 1 375 ? 150.353 144.171 111.542 1.00 22.44 ?  375 LYS A O     1 
ATOM   3040  C  CB    . LYS A 1 375 ? 153.496 144.083 110.745 1.00 12.06 ?  375 LYS A CB    1 
ATOM   3041  C  CG    . LYS A 1 375 ? 154.789 144.563 110.110 1.00 16.85 ?  375 LYS A CG    1 
ATOM   3042  C  CD    . LYS A 1 375 ? 155.914 143.568 110.313 1.00 24.65 ?  375 LYS A CD    1 
ATOM   3043  C  CE    . LYS A 1 375 ? 157.146 143.972 109.523 1.00 24.19 ?  375 LYS A CE    1 
ATOM   3044  N  NZ    . LYS A 1 375 ? 158.206 142.930 109.570 1.00 29.43 1  375 LYS A NZ    1 
ATOM   3045  N  N     . VAL A 1 376 ? 150.656 143.065 109.604 1.00 15.10 ?  376 VAL A N     1 
ATOM   3046  C  CA    . VAL A 1 376 ? 149.486 142.216 109.795 1.00 15.74 ?  376 VAL A CA    1 
ATOM   3047  C  C     . VAL A 1 376 ? 149.791 141.246 110.933 1.00 13.96 ?  376 VAL A C     1 
ATOM   3048  O  O     . VAL A 1 376 ? 150.651 140.371 110.802 1.00 20.44 ?  376 VAL A O     1 
ATOM   3049  C  CB    . VAL A 1 376 ? 149.112 141.471 108.510 1.00 10.94 ?  376 VAL A CB    1 
ATOM   3050  C  CG1   . VAL A 1 376 ? 147.851 140.655 108.721 1.00 8.26  ?  376 VAL A CG1   1 
ATOM   3051  C  CG2   . VAL A 1 376 ? 148.933 142.454 107.365 1.00 3.91  ?  376 VAL A CG2   1 
ATOM   3052  N  N     . LYS A 1 377 ? 149.092 141.404 112.056 1.00 12.77 ?  377 LYS A N     1 
ATOM   3053  C  CA    . LYS A 1 377 ? 149.347 140.595 113.238 1.00 11.43 ?  377 LYS A CA    1 
ATOM   3054  C  C     . LYS A 1 377 ? 148.418 139.400 113.366 1.00 10.48 ?  377 LYS A C     1 
ATOM   3055  O  O     . LYS A 1 377 ? 148.759 138.452 114.079 1.00 24.90 ?  377 LYS A O     1 
ATOM   3056  C  CB    . LYS A 1 377 ? 149.226 141.446 114.506 1.00 15.92 ?  377 LYS A CB    1 
ATOM   3057  C  CG    . LYS A 1 377 ? 150.058 142.709 114.500 1.00 12.28 ?  377 LYS A CG    1 
ATOM   3058  C  CD    . LYS A 1 377 ? 149.379 143.781 115.325 1.00 21.26 ?  377 LYS A CD    1 
ATOM   3059  C  CE    . LYS A 1 377 ? 149.894 145.158 114.979 1.00 23.69 ?  377 LYS A CE    1 
ATOM   3060  N  NZ    . LYS A 1 377 ? 148.944 146.222 115.404 1.00 26.00 1  377 LYS A NZ    1 
ATOM   3061  N  N     . PHE A 1 378 ? 147.263 139.423 112.710 1.00 8.60  ?  378 PHE A N     1 
ATOM   3062  C  CA    . PHE A 1 378 ? 146.298 138.340 112.827 1.00 7.85  ?  378 PHE A CA    1 
ATOM   3063  C  C     . PHE A 1 378 ? 145.339 138.412 111.649 1.00 8.00  ?  378 PHE A C     1 
ATOM   3064  O  O     . PHE A 1 378 ? 145.368 139.353 110.852 1.00 15.64 ?  378 PHE A O     1 
ATOM   3065  C  CB    . PHE A 1 378 ? 145.554 138.393 114.167 1.00 6.52  ?  378 PHE A CB    1 
ATOM   3066  C  CG    . PHE A 1 378 ? 144.582 139.535 114.292 1.00 8.31  ?  378 PHE A CG    1 
ATOM   3067  C  CD1   . PHE A 1 378 ? 145.011 140.849 114.194 1.00 9.59  ?  378 PHE A CD1   1 
ATOM   3068  C  CD2   . PHE A 1 378 ? 143.242 139.292 114.533 1.00 5.15  ?  378 PHE A CD2   1 
ATOM   3069  C  CE1   . PHE A 1 378 ? 144.121 141.893 114.316 1.00 4.02  ?  378 PHE A CE1   1 
ATOM   3070  C  CE2   . PHE A 1 378 ? 142.348 140.333 114.656 1.00 9.56  ?  378 PHE A CE2   1 
ATOM   3071  C  CZ    . PHE A 1 378 ? 142.790 141.636 114.549 1.00 11.53 ?  378 PHE A CZ    1 
ATOM   3072  N  N     . SER A 1 379 ? 144.490 137.397 111.545 1.00 3.31  ?  379 SER A N     1 
ATOM   3073  C  CA    . SER A 1 379 ? 143.546 137.256 110.446 1.00 4.14  ?  379 SER A CA    1 
ATOM   3074  C  C     . SER A 1 379 ? 142.121 137.244 110.994 1.00 5.96  ?  379 SER A C     1 
ATOM   3075  O  O     . SER A 1 379 ? 141.885 137.482 112.180 1.00 12.37 ?  379 SER A O     1 
ATOM   3076  C  CB    . SER A 1 379 ? 143.853 135.994 109.637 1.00 5.03  ?  379 SER A CB    1 
ATOM   3077  O  OG    . SER A 1 379 ? 143.388 136.122 108.306 1.00 8.38  ?  379 SER A OG    1 
ATOM   3078  N  N     . ASN A 1 380 ? 141.166 136.967 110.113 1.00 11.92 ?  380 ASN A N     1 
ATOM   3079  C  CA    . ASN A 1 380 ? 139.756 136.996 110.456 1.00 9.17  ?  380 ASN A CA    1 
ATOM   3080  C  C     . ASN A 1 380 ? 139.276 135.601 110.850 1.00 9.46  ?  380 ASN A C     1 
ATOM   3081  O  O     . ASN A 1 380 ? 140.063 134.661 110.996 1.00 9.92  ?  380 ASN A O     1 
ATOM   3082  C  CB    . ASN A 1 380 ? 138.942 137.563 109.292 1.00 2.71  ?  380 ASN A CB    1 
ATOM   3083  C  CG    . ASN A 1 380 ? 138.891 136.628 108.105 1.00 3.90  ?  380 ASN A CG    1 
ATOM   3084  O  OD1   . ASN A 1 380 ? 139.920 136.149 107.632 1.00 12.64 ?  380 ASN A OD1   1 
ATOM   3085  N  ND2   . ASN A 1 380 ? 137.688 136.362 107.615 1.00 10.73 ?  380 ASN A ND2   1 
ATOM   3086  N  N     . LEU A 1 381 ? 137.961 135.467 111.031 1.00 17.84 ?  381 LEU A N     1 
ATOM   3087  C  CA    . LEU A 1 381 ? 137.365 134.180 111.367 1.00 6.52  ?  381 LEU A CA    1 
ATOM   3088  C  C     . LEU A 1 381 ? 137.524 133.160 110.248 1.00 6.70  ?  381 LEU A C     1 
ATOM   3089  O  O     . LEU A 1 381 ? 137.565 131.956 110.524 1.00 15.30 ?  381 LEU A O     1 
ATOM   3090  C  CB    . LEU A 1 381 ? 135.885 134.379 111.705 1.00 11.71 ?  381 LEU A CB    1 
ATOM   3091  C  CG    . LEU A 1 381 ? 134.987 133.165 111.946 1.00 20.37 ?  381 LEU A CG    1 
ATOM   3092  C  CD1   . LEU A 1 381 ? 135.414 132.401 113.187 1.00 14.47 ?  381 LEU A CD1   1 
ATOM   3093  C  CD2   . LEU A 1 381 ? 133.539 133.604 112.055 1.00 15.89 ?  381 LEU A CD2   1 
ATOM   3094  N  N     . CYS A 1 382 ? 137.624 133.607 108.999 1.00 8.83  ?  382 CYS A N     1 
ATOM   3095  C  CA    . CYS A 1 382 ? 137.831 132.720 107.864 1.00 6.39  ?  382 CYS A CA    1 
ATOM   3096  C  C     . CYS A 1 382 ? 139.282 132.678 107.406 1.00 10.63 ?  382 CYS A C     1 
ATOM   3097  O  O     . CYS A 1 382 ? 139.588 131.984 106.431 1.00 17.01 ?  382 CYS A O     1 
ATOM   3098  C  CB    . CYS A 1 382 ? 136.928 133.137 106.698 1.00 15.57 ?  382 CYS A CB    1 
ATOM   3099  S  SG    . CYS A 1 382 ? 135.170 133.226 107.113 1.00 35.34 ?  382 CYS A SG    1 
ATOM   3100  N  N     . SER A 1 383 ? 140.174 133.399 108.086 1.00 11.05 ?  383 SER A N     1 
ATOM   3101  C  CA    . SER A 1 383 ? 141.614 133.360 107.826 1.00 8.94  ?  383 SER A CA    1 
ATOM   3102  C  C     . SER A 1 383 ? 141.948 133.741 106.385 1.00 12.51 ?  383 SER A C     1 
ATOM   3103  O  O     . SER A 1 383 ? 142.748 133.082 105.720 1.00 22.80 ?  383 SER A O     1 
ATOM   3104  C  CB    . SER A 1 383 ? 142.200 131.989 108.170 1.00 12.13 ?  383 SER A CB    1 
ATOM   3105  O  OG    . SER A 1 383 ? 141.885 131.039 107.170 1.00 20.92 ?  383 SER A OG    1 
ATOM   3106  N  N     . GLU A 1 384 ? 141.329 134.813 105.891 1.00 8.02  ?  384 GLU A N     1 
ATOM   3107  C  CA    . GLU A 1 384 ? 141.693 135.360 104.591 1.00 11.46 ?  384 GLU A CA    1 
ATOM   3108  C  C     . GLU A 1 384 ? 141.858 136.873 104.590 1.00 13.32 ?  384 GLU A C     1 
ATOM   3109  O  O     . GLU A 1 384 ? 142.437 137.407 103.637 1.00 22.51 ?  384 GLU A O     1 
ATOM   3110  C  CB    . GLU A 1 384 ? 140.664 134.953 103.521 1.00 6.55  ?  384 GLU A CB    1 
ATOM   3111  C  CG    . GLU A 1 384 ? 139.698 136.037 103.070 1.00 7.25  ?  384 GLU A CG    1 
ATOM   3112  C  CD    . GLU A 1 384 ? 138.526 136.211 104.010 1.00 16.76 ?  384 GLU A CD    1 
ATOM   3113  O  OE1   . GLU A 1 384 ? 138.288 135.309 104.836 1.00 19.97 ?  384 GLU A OE1   1 
ATOM   3114  O  OE2   . GLU A 1 384 ? 137.831 137.242 103.909 1.00 21.02 -1 384 GLU A OE2   1 
ATOM   3115  N  N     . VAL A 1 385 ? 141.398 137.573 105.619 1.00 13.29 ?  385 VAL A N     1 
ATOM   3116  C  CA    . VAL A 1 385 ? 141.589 139.014 105.727 1.00 3.12  ?  385 VAL A CA    1 
ATOM   3117  C  C     . VAL A 1 385 ? 142.922 139.268 106.414 1.00 15.14 ?  385 VAL A C     1 
ATOM   3118  O  O     . VAL A 1 385 ? 143.132 138.848 107.556 1.00 19.40 ?  385 VAL A O     1 
ATOM   3119  C  CB    . VAL A 1 385 ? 140.438 139.674 106.497 1.00 3.77  ?  385 VAL A CB    1 
ATOM   3120  C  CG1   . VAL A 1 385 ? 140.642 141.168 106.547 1.00 10.14 ?  385 VAL A CG1   1 
ATOM   3121  C  CG2   . VAL A 1 385 ? 139.113 139.346 105.851 1.00 8.54  ?  385 VAL A CG2   1 
ATOM   3122  N  N     . LEU A 1 386 ? 143.826 139.955 105.719 1.00 16.86 ?  386 LEU A N     1 
ATOM   3123  C  CA    . LEU A 1 386 ? 145.164 140.243 106.226 1.00 3.54  ?  386 LEU A CA    1 
ATOM   3124  C  C     . LEU A 1 386 ? 145.452 141.721 105.990 1.00 7.34  ?  386 LEU A C     1 
ATOM   3125  O  O     . LEU A 1 386 ? 145.856 142.116 104.893 1.00 8.00  ?  386 LEU A O     1 
ATOM   3126  C  CB    . LEU A 1 386 ? 146.205 139.358 105.555 1.00 3.17  ?  386 LEU A CB    1 
ATOM   3127  C  CG    . LEU A 1 386 ? 146.016 137.869 105.835 1.00 7.86  ?  386 LEU A CG    1 
ATOM   3128  C  CD1   . LEU A 1 386 ? 146.946 137.058 104.979 1.00 9.37  ?  386 LEU A CD1   1 
ATOM   3129  C  CD2   . LEU A 1 386 ? 146.244 137.576 107.305 1.00 6.77  ?  386 LEU A CD2   1 
ATOM   3130  N  N     . GLN A 1 387 ? 145.244 142.535 107.022 1.00 14.69 ?  387 GLN A N     1 
ATOM   3131  C  CA    . GLN A 1 387 ? 145.354 143.979 106.901 1.00 4.40  ?  387 GLN A CA    1 
ATOM   3132  C  C     . GLN A 1 387 ? 146.099 144.545 108.098 1.00 6.85  ?  387 GLN A C     1 
ATOM   3133  O  O     . GLN A 1 387 ? 146.205 143.913 109.152 1.00 18.95 ?  387 GLN A O     1 
ATOM   3134  C  CB    . GLN A 1 387 ? 143.977 144.641 106.785 1.00 6.31  ?  387 GLN A CB    1 
ATOM   3135  C  CG    . GLN A 1 387 ? 143.134 144.108 105.650 1.00 8.48  ?  387 GLN A CG    1 
ATOM   3136  C  CD    . GLN A 1 387 ? 141.890 144.928 105.430 1.00 6.84  ?  387 GLN A CD    1 
ATOM   3137  O  OE1   . GLN A 1 387 ? 141.727 145.997 106.013 1.00 19.59 ?  387 GLN A OE1   1 
ATOM   3138  N  NE2   . GLN A 1 387 ? 141.009 144.437 104.574 1.00 8.43  ?  387 GLN A NE2   1 
ATOM   3139  N  N     . ALA A 1 388 ? 146.630 145.749 107.914 1.00 10.17 ?  388 ALA A N     1 
ATOM   3140  C  CA    . ALA A 1 388 ? 147.255 146.470 109.012 1.00 9.47  ?  388 ALA A CA    1 
ATOM   3141  C  C     . ALA A 1 388 ? 146.203 146.903 110.025 1.00 14.32 ?  388 ALA A C     1 
ATOM   3142  O  O     . ALA A 1 388 ? 145.125 147.380 109.661 1.00 25.46 ?  388 ALA A O     1 
ATOM   3143  C  CB    . ALA A 1 388 ? 148.008 147.690 108.484 1.00 12.02 ?  388 ALA A CB    1 
ATOM   3144  N  N     . SER A 1 389 ? 146.520 146.726 111.304 1.00 17.96 ?  389 SER A N     1 
ATOM   3145  C  CA    . SER A 1 389 ? 145.625 147.125 112.380 1.00 8.83  ?  389 SER A CA    1 
ATOM   3146  C  C     . SER A 1 389 ? 146.426 147.811 113.473 1.00 13.12 ?  389 SER A C     1 
ATOM   3147  O  O     . SER A 1 389 ? 147.551 147.407 113.777 1.00 24.46 ?  389 SER A O     1 
ATOM   3148  C  CB    . SER A 1 389 ? 144.872 145.923 112.959 1.00 16.70 ?  389 SER A CB    1 
ATOM   3149  O  OG    . SER A 1 389 ? 145.735 144.813 113.130 1.00 21.83 ?  389 SER A OG    1 
ATOM   3150  N  N     . GLN A 1 390 ? 145.838 148.848 114.062 1.00 17.64 ?  390 GLN A N     1 
ATOM   3151  C  CA    . GLN A 1 390 ? 146.430 149.560 115.185 1.00 14.92 ?  390 GLN A CA    1 
ATOM   3152  C  C     . GLN A 1 390 ? 145.535 149.382 116.400 1.00 13.36 ?  390 GLN A C     1 
ATOM   3153  O  O     . GLN A 1 390 ? 144.321 149.590 116.316 1.00 17.32 ?  390 GLN A O     1 
ATOM   3154  C  CB    . GLN A 1 390 ? 146.615 151.045 114.867 1.00 10.33 ?  390 GLN A CB    1 
ATOM   3155  C  CG    . GLN A 1 390 ? 147.739 151.329 113.886 1.00 15.85 ?  390 GLN A CG    1 
ATOM   3156  C  CD    . GLN A 1 390 ? 147.710 152.749 113.359 1.00 25.93 ?  390 GLN A CD    1 
ATOM   3157  O  OE1   . GLN A 1 390 ? 146.774 153.502 113.624 1.00 24.72 ?  390 GLN A OE1   1 
ATOM   3158  N  NE2   . GLN A 1 390 ? 148.737 153.120 112.604 1.00 21.61 ?  390 GLN A NE2   1 
ATOM   3159  N  N     . VAL A 1 391 ? 146.135 148.990 117.524 1.00 24.05 ?  391 VAL A N     1 
ATOM   3160  C  CA    . VAL A 1 391 ? 145.363 148.756 118.735 1.00 20.62 ?  391 VAL A CA    1 
ATOM   3161  C  C     . VAL A 1 391 ? 144.822 150.077 119.269 1.00 22.62 ?  391 VAL A C     1 
ATOM   3162  O  O     . VAL A 1 391 ? 145.405 151.150 119.063 1.00 24.03 ?  391 VAL A O     1 
ATOM   3163  C  CB    . VAL A 1 391 ? 146.214 148.026 119.792 1.00 19.09 ?  391 VAL A CB    1 
ATOM   3164  C  CG1   . VAL A 1 391 ? 147.133 148.998 120.517 1.00 20.19 ?  391 VAL A CG1   1 
ATOM   3165  C  CG2   . VAL A 1 391 ? 145.323 147.284 120.776 1.00 17.61 ?  391 VAL A CG2   1 
ATOM   3166  N  N     . SER A 1 392 ? 143.680 150.001 119.942 1.00 27.56 ?  392 SER A N     1 
ATOM   3167  C  CA    . SER A 1 392 ? 143.054 151.161 120.554 1.00 19.89 ?  392 SER A CA    1 
ATOM   3168  C  C     . SER A 1 392 ? 143.282 151.143 122.059 1.00 29.15 ?  392 SER A C     1 
ATOM   3169  O  O     . SER A 1 392 ? 143.342 150.082 122.685 1.00 29.80 ?  392 SER A O     1 
ATOM   3170  C  CB    . SER A 1 392 ? 141.554 151.195 120.256 1.00 20.67 ?  392 SER A CB    1 
ATOM   3171  O  OG    . SER A 1 392 ? 141.308 151.207 118.862 1.00 27.89 ?  392 SER A OG    1 
ATOM   3172  N  N     . SER A 1 393 ? 143.417 152.332 122.633 1.00 31.70 ?  393 SER A N     1 
ATOM   3173  C  CA    . SER A 1 393 ? 143.591 152.502 124.073 1.00 28.10 ?  393 SER A CA    1 
ATOM   3174  C  C     . SER A 1 393 ? 142.262 152.993 124.637 1.00 30.16 ?  393 SER A C     1 
ATOM   3175  O  O     . SER A 1 393 ? 142.001 154.196 124.700 1.00 34.98 ?  393 SER A O     1 
ATOM   3176  C  CB    . SER A 1 393 ? 144.726 153.472 124.382 1.00 30.37 ?  393 SER A CB    1 
ATOM   3177  O  OG    . SER A 1 393 ? 145.987 152.856 124.190 1.00 36.82 ?  393 SER A OG    1 
ATOM   3178  N  N     . TYR A 1 394 ? 141.416 152.049 125.038 1.00 29.20 ?  394 TYR A N     1 
ATOM   3179  C  CA    . TYR A 1 394 ? 140.140 152.378 125.660 1.00 28.90 ?  394 TYR A CA    1 
ATOM   3180  C  C     . TYR A 1 394 ? 140.382 152.642 127.140 1.00 28.85 ?  394 TYR A C     1 
ATOM   3181  O  O     . TYR A 1 394 ? 140.649 151.713 127.908 1.00 33.55 ?  394 TYR A O     1 
ATOM   3182  C  CB    . TYR A 1 394 ? 139.137 151.249 125.450 1.00 24.98 ?  394 TYR A CB    1 
ATOM   3183  C  CG    . TYR A 1 394 ? 138.686 151.100 124.015 1.00 28.24 ?  394 TYR A CG    1 
ATOM   3184  C  CD1   . TYR A 1 394 ? 137.808 152.011 123.444 1.00 29.50 ?  394 TYR A CD1   1 
ATOM   3185  C  CD2   . TYR A 1 394 ? 139.146 150.051 123.229 1.00 26.55 ?  394 TYR A CD2   1 
ATOM   3186  C  CE1   . TYR A 1 394 ? 137.394 151.878 122.135 1.00 28.34 ?  394 TYR A CE1   1 
ATOM   3187  C  CE2   . TYR A 1 394 ? 138.736 149.910 121.918 1.00 27.08 ?  394 TYR A CE2   1 
ATOM   3188  C  CZ    . TYR A 1 394 ? 137.861 150.827 121.376 1.00 36.10 ?  394 TYR A CZ    1 
ATOM   3189  O  OH    . TYR A 1 394 ? 137.453 150.690 120.069 1.00 38.36 ?  394 TYR A OH    1 
ATOM   3190  N  N     . THR A 1 395 ? 140.292 153.905 127.538 1.00 35.82 ?  395 THR A N     1 
ATOM   3191  C  CA    . THR A 1 395 ? 140.611 154.319 128.895 1.00 37.45 ?  395 THR A CA    1 
ATOM   3192  C  C     . THR A 1 395 ? 139.385 154.162 129.793 1.00 38.54 ?  395 THR A C     1 
ATOM   3193  O  O     . THR A 1 395 ? 138.385 153.544 129.419 1.00 38.57 ?  395 THR A O     1 
ATOM   3194  C  CB    . THR A 1 395 ? 141.133 155.753 128.893 1.00 36.92 ?  395 THR A CB    1 
ATOM   3195  O  OG1   . THR A 1 395 ? 140.149 156.619 128.314 1.00 38.62 ?  395 THR A OG1   1 
ATOM   3196  C  CG2   . THR A 1 395 ? 142.418 155.848 128.086 1.00 35.25 ?  395 THR A CG2   1 
ATOM   3197  N  N     . ASP A 1 396 ? 139.457 154.720 130.998 1.00 36.30 ?  396 ASP A N     1 
ATOM   3198  C  CA    . ASP A 1 396 ? 138.341 154.674 131.929 1.00 36.61 ?  396 ASP A CA    1 
ATOM   3199  C  C     . ASP A 1 396 ? 137.188 155.531 131.408 1.00 38.06 ?  396 ASP A C     1 
ATOM   3200  O  O     . ASP A 1 396 ? 137.264 156.153 130.345 1.00 42.28 ?  396 ASP A O     1 
ATOM   3201  C  CB    . ASP A 1 396 ? 138.781 155.150 133.312 1.00 38.06 ?  396 ASP A CB    1 
ATOM   3202  C  CG    . ASP A 1 396 ? 139.971 154.379 133.848 1.00 42.51 ?  396 ASP A CG    1 
ATOM   3203  O  OD1   . ASP A 1 396 ? 140.169 153.218 133.433 1.00 43.52 ?  396 ASP A OD1   1 
ATOM   3204  O  OD2   . ASP A 1 396 ? 140.706 154.935 134.689 1.00 44.02 -1 396 ASP A OD2   1 
ATOM   3205  N  N     . TYR A 1 397 ? 136.099 155.558 132.172 1.00 37.44 ?  397 TYR A N     1 
ATOM   3206  C  CA    . TYR A 1 397 ? 134.994 156.441 131.845 1.00 34.06 ?  397 TYR A CA    1 
ATOM   3207  C  C     . TYR A 1 397 ? 135.452 157.897 131.932 1.00 37.34 ?  397 TYR A C     1 
ATOM   3208  O  O     . TYR A 1 397 ? 136.542 158.200 132.416 1.00 39.74 ?  397 TYR A O     1 
ATOM   3209  C  CB    . TYR A 1 397 ? 133.808 156.183 132.773 1.00 33.65 ?  397 TYR A CB    1 
ATOM   3210  C  CG    . TYR A 1 397 ? 132.473 156.563 132.174 1.00 33.80 ?  397 TYR A CG    1 
ATOM   3211  C  CD1   . TYR A 1 397 ? 131.792 155.686 131.341 1.00 36.07 ?  397 TYR A CD1   1 
ATOM   3212  C  CD2   . TYR A 1 397 ? 131.892 157.796 132.442 1.00 34.56 ?  397 TYR A CD2   1 
ATOM   3213  C  CE1   . TYR A 1 397 ? 130.573 156.027 130.790 1.00 33.88 ?  397 TYR A CE1   1 
ATOM   3214  C  CE2   . TYR A 1 397 ? 130.675 158.146 131.896 1.00 31.84 ?  397 TYR A CE2   1 
ATOM   3215  C  CZ    . TYR A 1 397 ? 130.020 157.258 131.073 1.00 34.09 ?  397 TYR A CZ    1 
ATOM   3216  O  OH    . TYR A 1 397 ? 128.805 157.603 130.528 1.00 39.73 ?  397 TYR A OH    1 
ATOM   3217  N  N     . ASP A 1 398 ? 134.617 158.787 131.387 1.00 41.00 ?  398 ASP A N     1 
ATOM   3218  C  CA    . ASP A 1 398 ? 134.811 160.236 131.285 1.00 42.01 ?  398 ASP A CA    1 
ATOM   3219  C  C     . ASP A 1 398 ? 136.260 160.587 130.951 1.00 44.08 ?  398 ASP A C     1 
ATOM   3220  O  O     . ASP A 1 398 ? 136.790 161.612 131.394 1.00 41.83 ?  398 ASP A O     1 
ATOM   3221  C  CB    . ASP A 1 398 ? 134.289 160.965 132.546 1.00 41.67 ?  398 ASP A CB    1 
ATOM   3222  C  CG    . ASP A 1 398 ? 135.240 160.932 133.753 1.00 44.94 ?  398 ASP A CG    1 
ATOM   3223  O  OD1   . ASP A 1 398 ? 134.960 161.682 134.711 1.00 45.96 ?  398 ASP A OD1   1 
ATOM   3224  O  OD2   . ASP A 1 398 ? 136.248 160.210 133.778 1.00 42.18 -1 398 ASP A OD2   1 
ATOM   3225  N  N     . GLU A 1 399 ? 136.887 159.746 130.131 1.00 48.02 ?  399 GLU A N     1 
ATOM   3226  C  CA    . GLU A 1 399 ? 138.249 159.933 129.660 1.00 43.95 ?  399 GLU A CA    1 
ATOM   3227  C  C     . GLU A 1 399 ? 138.294 159.564 128.186 1.00 44.55 ?  399 GLU A C     1 
ATOM   3228  O  O     . GLU A 1 399 ? 137.708 158.558 127.773 1.00 42.49 ?  399 GLU A O     1 
ATOM   3229  C  CB    . GLU A 1 399 ? 139.239 159.075 130.458 1.00 39.19 ?  399 GLU A CB    1 
ATOM   3230  C  CG    . GLU A 1 399 ? 140.607 159.709 130.639 1.00 42.93 ?  399 GLU A CG    1 
ATOM   3231  C  CD    . GLU A 1 399 ? 141.668 158.700 131.037 1.00 48.39 ?  399 GLU A CD    1 
ATOM   3232  O  OE1   . GLU A 1 399 ? 141.342 157.754 131.783 1.00 47.56 ?  399 GLU A OE1   1 
ATOM   3233  O  OE2   . GLU A 1 399 ? 142.829 158.855 130.603 1.00 47.06 -1 399 GLU A OE2   1 
ATOM   3234  N  N     . GLU A 1 400 ? 138.985 160.379 127.396 1.00 44.73 ?  400 GLU A N     1 
ATOM   3235  C  CA    . GLU A 1 400 ? 138.986 160.190 125.952 1.00 40.43 ?  400 GLU A CA    1 
ATOM   3236  C  C     . GLU A 1 400 ? 139.766 158.938 125.572 1.00 43.83 ?  400 GLU A C     1 
ATOM   3237  O  O     . GLU A 1 400 ? 140.905 158.744 126.006 1.00 43.14 ?  400 GLU A O     1 
ATOM   3238  C  CB    . GLU A 1 400 ? 139.580 161.415 125.260 1.00 40.22 ?  400 GLU A CB    1 
ATOM   3239  C  CG    . GLU A 1 400 ? 138.817 161.860 124.022 1.00 45.83 ?  400 GLU A CG    1 
ATOM   3240  C  CD    . GLU A 1 400 ? 137.358 162.165 124.310 1.00 48.85 ?  400 GLU A CD    1 
ATOM   3241  O  OE1   . GLU A 1 400 ? 137.067 162.738 125.380 1.00 46.49 ?  400 GLU A OE1   1 
ATOM   3242  O  OE2   . GLU A 1 400 ? 136.502 161.831 123.464 1.00 47.21 -1 400 GLU A OE2   1 
ATOM   3243  N  N     . ASP A 1 401 ? 139.146 158.089 124.757 1.00 35.69 ?  401 ASP A N     1 
ATOM   3244  C  CA    . ASP A 1 401 ? 139.806 156.894 124.255 1.00 33.74 ?  401 ASP A CA    1 
ATOM   3245  C  C     . ASP A 1 401 ? 140.699 157.238 123.070 1.00 34.42 ?  401 ASP A C     1 
ATOM   3246  O  O     . ASP A 1 401 ? 140.441 158.188 122.325 1.00 38.08 ?  401 ASP A O     1 
ATOM   3247  C  CB    . ASP A 1 401 ? 138.778 155.844 123.836 1.00 32.53 ?  401 ASP A CB    1 
ATOM   3248  C  CG    . ASP A 1 401 ? 137.780 155.529 124.930 1.00 37.68 ?  401 ASP A CG    1 
ATOM   3249  O  OD1   . ASP A 1 401 ? 138.208 155.116 126.027 1.00 42.07 ?  401 ASP A OD1   1 
ATOM   3250  O  OD2   . ASP A 1 401 ? 136.566 155.693 124.691 1.00 38.40 -1 401 ASP A OD2   1 
ATOM   3251  N  N     . GLU A 1 402 ? 141.757 156.452 122.899 1.00 31.60 ?  402 GLU A N     1 
ATOM   3252  C  CA    . GLU A 1 402 ? 142.628 156.557 121.731 1.00 29.37 ?  402 GLU A CA    1 
ATOM   3253  C  C     . GLU A 1 402 ? 142.143 155.496 120.749 1.00 24.85 ?  402 GLU A C     1 
ATOM   3254  O  O     . GLU A 1 402 ? 142.382 154.302 120.937 1.00 30.34 ?  402 GLU A O     1 
ATOM   3255  C  CB    . GLU A 1 402 ? 144.094 156.375 122.116 1.00 31.18 ?  402 GLU A CB    1 
ATOM   3256  C  CG    . GLU A 1 402 ? 145.055 156.144 120.947 1.00 36.78 ?  402 GLU A CG    1 
ATOM   3257  C  CD    . GLU A 1 402 ? 145.268 154.678 120.613 1.00 40.42 ?  402 GLU A CD    1 
ATOM   3258  O  OE1   . GLU A 1 402 ? 145.865 153.956 121.437 1.00 35.31 ?  402 GLU A OE1   1 
ATOM   3259  O  OE2   . GLU A 1 402 ? 144.845 154.249 119.519 1.00 34.93 -1 402 GLU A OE2   1 
ATOM   3260  N  N     . ILE A 1 403 ? 141.429 155.934 119.718 1.00 27.50 ?  403 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 403 ? 140.818 155.013 118.769 1.00 26.57 ?  403 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 403 ? 141.843 154.630 117.711 1.00 28.07 ?  403 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 403 ? 142.436 155.496 117.058 1.00 28.44 ?  403 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 403 ? 139.566 155.638 118.133 1.00 24.55 ?  403 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 403 ? 138.531 155.973 119.209 1.00 24.49 ?  403 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 403 ? 138.970 154.702 117.096 1.00 20.31 ?  403 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 403 ? 138.224 154.826 120.145 1.00 26.84 ?  403 ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 404 ? 142.056 153.333 117.544 1.00 23.34 ?  404 GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 404 ? 142.968 152.795 116.559 1.00 9.27  ?  404 GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 404 ? 142.259 152.359 115.296 1.00 19.17 ?  404 GLY A C     1 
ATOM   3271  O  O     . GLY A 1 404 ? 141.241 152.936 114.894 1.00 31.31 ?  404 GLY A O     1 
ATOM   3272  N  N     . LEU A 1 405 ? 142.800 151.325 114.658 1.00 22.22 ?  405 LEU A N     1 
ATOM   3273  C  CA    . LEU A 1 405 ? 142.248 150.783 113.423 1.00 7.02  ?  405 LEU A CA    1 
ATOM   3274  C  C     . LEU A 1 405 ? 141.893 149.320 113.642 1.00 8.34  ?  405 LEU A C     1 
ATOM   3275  O  O     . LEU A 1 405 ? 142.764 148.510 113.972 1.00 18.34 ?  405 LEU A O     1 
ATOM   3276  C  CB    . LEU A 1 405 ? 143.241 150.926 112.268 1.00 17.23 ?  405 LEU A CB    1 
ATOM   3277  C  CG    . LEU A 1 405 ? 143.680 152.347 111.912 1.00 18.22 ?  405 LEU A CG    1 
ATOM   3278  C  CD1   . LEU A 1 405 ? 144.781 152.322 110.866 1.00 21.75 ?  405 LEU A CD1   1 
ATOM   3279  C  CD2   . LEU A 1 405 ? 142.499 153.172 111.432 1.00 15.48 ?  405 LEU A CD2   1 
ATOM   3280  N  N     . ASP A 1 406 ? 140.620 148.987 113.456 1.00 22.38 ?  406 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 406 ? 140.142 147.614 113.515 1.00 17.43 ?  406 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 406 ? 139.629 147.212 112.140 1.00 19.13 ?  406 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 406 ? 138.804 147.916 111.551 1.00 31.28 ?  406 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 406 ? 139.042 147.455 114.566 1.00 18.37 ?  406 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 406 ? 139.594 147.225 115.959 1.00 29.15 ?  406 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 406 ? 140.831 147.258 116.128 1.00 32.47 ?  406 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 406 ? 138.788 147.016 116.889 1.00 28.37 -1 406 ASP A OD2   1 
ATOM   3288  N  N     . ILE A 1 407 ? 140.105 146.080 111.646 1.00 21.24 ?  407 ILE A N     1 
ATOM   3289  C  CA    . ILE A 1 407 ? 139.889 145.697 110.258 1.00 15.66 ?  407 ILE A CA    1 
ATOM   3290  C  C     . ILE A 1 407 ? 138.447 145.260 110.048 1.00 14.81 ?  407 ILE A C     1 
ATOM   3291  O  O     . ILE A 1 407 ? 137.875 144.519 110.857 1.00 21.70 ?  407 ILE A O     1 
ATOM   3292  C  CB    . ILE A 1 407 ? 140.869 144.581 109.856 1.00 10.60 ?  407 ILE A CB    1 
ATOM   3293  C  CG1   . ILE A 1 407 ? 142.312 145.056 110.010 1.00 6.69  ?  407 ILE A CG1   1 
ATOM   3294  C  CG2   . ILE A 1 407 ? 140.600 144.129 108.444 1.00 16.52 ?  407 ILE A CG2   1 
ATOM   3295  C  CD1   . ILE A 1 407 ? 143.254 143.963 110.435 1.00 10.78 ?  407 ILE A CD1   1 
ATOM   3296  N  N     . SER A 1 408 ? 137.854 145.728 108.951 1.00 25.69 ?  408 SER A N     1 
ATOM   3297  C  CA    . SER A 1 408 ? 136.549 145.252 108.506 1.00 21.75 ?  408 SER A CA    1 
ATOM   3298  C  C     . SER A 1 408 ? 136.499 145.433 106.997 1.00 24.54 ?  408 SER A C     1 
ATOM   3299  O  O     . SER A 1 408 ? 136.216 146.535 106.517 1.00 30.62 ?  408 SER A O     1 
ATOM   3300  C  CB    . SER A 1 408 ? 135.418 146.014 109.188 1.00 26.05 ?  408 SER A CB    1 
ATOM   3301  O  OG    . SER A 1 408 ? 135.459 147.389 108.849 1.00 29.29 ?  408 SER A OG    1 
ATOM   3302  N  N     . CYS A 1 409 ? 136.769 144.367 106.252 1.00 20.52 ?  409 CYS A N     1 
ATOM   3303  C  CA    . CYS A 1 409 ? 136.806 144.453 104.801 1.00 26.32 ?  409 CYS A CA    1 
ATOM   3304  C  C     . CYS A 1 409 ? 135.478 144.006 104.202 1.00 30.59 ?  409 CYS A C     1 
ATOM   3305  O  O     . CYS A 1 409 ? 134.649 143.366 104.854 1.00 25.65 ?  409 CYS A O     1 
ATOM   3306  C  CB    . CYS A 1 409 ? 137.956 143.624 104.225 1.00 23.24 ?  409 CYS A CB    1 
ATOM   3307  S  SG    . CYS A 1 409 ? 137.553 141.927 103.791 1.00 41.88 ?  409 CYS A SG    1 
ATOM   3308  N  N     . ASN A 1 410 ? 135.294 144.356 102.936 1.00 30.01 ?  410 ASN A N     1 
ATOM   3309  C  CA    . ASN A 1 410 ? 134.029 144.206 102.233 1.00 18.67 ?  410 ASN A CA    1 
ATOM   3310  C  C     . ASN A 1 410 ? 134.153 143.061 101.238 1.00 21.72 ?  410 ASN A C     1 
ATOM   3311  O  O     . ASN A 1 410 ? 134.998 143.110 100.340 1.00 29.59 ?  410 ASN A O     1 
ATOM   3312  C  CB    . ASN A 1 410 ? 133.680 145.510 101.522 1.00 26.98 ?  410 ASN A CB    1 
ATOM   3313  C  CG    . ASN A 1 410 ? 132.239 145.585 101.117 1.00 32.40 ?  410 ASN A CG    1 
ATOM   3314  O  OD1   . ASN A 1 410 ? 131.437 144.711 101.437 1.00 35.72 ?  410 ASN A OD1   1 
ATOM   3315  N  ND2   . ASN A 1 410 ? 131.900 146.636 100.396 1.00 34.49 ?  410 ASN A ND2   1 
ATOM   3316  N  N     . LEU A 1 411 ? 133.304 142.047 101.385 1.00 21.50 ?  411 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 411 ? 133.440 140.815 100.622 1.00 11.76 ?  411 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 411 ? 132.607 140.841 99.345  1.00 16.12 ?  411 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 411 ? 131.531 141.443 99.288  1.00 26.82 ?  411 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 411 ? 133.031 139.609 101.469 1.00 19.14 ?  411 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 411 ? 134.125 138.738 102.089 1.00 20.45 ?  411 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 411 ? 135.214 139.592 102.698 1.00 19.01 ?  411 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 411 ? 133.531 137.800 103.127 1.00 18.70 ?  411 LEU A CD2   1 
ATOM   3324  N  N     . GLY A 1 412 ? 133.122 140.167 98.320  1.00 22.65 ?  412 GLY A N     1 
ATOM   3325  C  CA    . GLY A 1 412 ? 132.452 140.000 97.044  1.00 13.61 ?  412 GLY A CA    1 
ATOM   3326  C  C     . GLY A 1 412 ? 133.281 139.106 96.146  1.00 13.30 ?  412 GLY A C     1 
ATOM   3327  O  O     . GLY A 1 412 ? 134.507 139.248 96.110  1.00 23.34 ?  412 GLY A O     1 
ATOM   3328  N  N     . SER A 1 413 ? 132.653 138.185 95.417  1.00 14.80 ?  413 SER A N     1 
ATOM   3329  C  CA    . SER A 1 413 ? 133.382 137.138 94.711  1.00 10.91 ?  413 SER A CA    1 
ATOM   3330  C  C     . SER A 1 413 ? 133.081 137.168 93.221  1.00 17.65 ?  413 SER A C     1 
ATOM   3331  O  O     . SER A 1 413 ? 131.918 137.237 92.816  1.00 21.51 ?  413 SER A O     1 
ATOM   3332  C  CB    . SER A 1 413 ? 133.042 135.761 95.281  1.00 9.74  ?  413 SER A CB    1 
ATOM   3333  O  OG    . SER A 1 413 ? 133.486 135.651 96.620  1.00 32.49 ?  413 SER A OG    1 
ATOM   3334  N  N     . LEU A 1 414 ? 134.132 137.098 92.411  1.00 18.32 ?  414 LEU A N     1 
ATOM   3335  C  CA    . LEU A 1 414 ? 133.974 136.887 90.981  1.00 12.54 ?  414 LEU A CA    1 
ATOM   3336  C  C     . LEU A 1 414 ? 133.722 135.413 90.699  1.00 19.08 ?  414 LEU A C     1 
ATOM   3337  O  O     . LEU A 1 414 ? 134.339 134.537 91.309  1.00 24.42 ?  414 LEU A O     1 
ATOM   3338  C  CB    . LEU A 1 414 ? 135.220 137.351 90.229  1.00 17.56 ?  414 LEU A CB    1 
ATOM   3339  C  CG    . LEU A 1 414 ? 135.796 138.716 90.601  1.00 20.23 ?  414 LEU A CG    1 
ATOM   3340  C  CD1   . LEU A 1 414 ? 137.186 138.875 90.016  1.00 22.49 ?  414 LEU A CD1   1 
ATOM   3341  C  CD2   . LEU A 1 414 ? 134.881 139.827 90.124  1.00 20.11 ?  414 LEU A CD2   1 
ATOM   3342  N  N     . ASN A 1 415 ? 132.808 135.140 89.775  1.00 25.67 ?  415 ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 415 ? 132.584 133.781 89.289  1.00 24.25 ?  415 ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 415 ? 133.506 133.579 88.095  1.00 22.60 ?  415 ASN A C     1 
ATOM   3345  O  O     . ASN A 1 415 ? 133.243 134.084 87.002  1.00 27.33 ?  415 ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 415 ? 131.119 133.568 88.929  1.00 20.70 ?  415 ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 415 ? 130.754 132.102 88.797  1.00 25.69 ?  415 ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 415 ? 131.407 131.348 88.080  1.00 33.28 ?  415 ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 415 ? 129.704 131.691 89.498  1.00 29.90 ?  415 ASN A ND2   1 
ATOM   3350  N  N     . ILE A 1 416 ? 134.593 132.833 88.308  1.00 21.84 ?  416 ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 416 ? 135.653 132.737 87.307  1.00 24.00 ?  416 ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 416 ? 135.120 132.152 86.008  1.00 26.98 ?  416 ILE A C     1 
ATOM   3353  O  O     . ILE A 1 416 ? 135.468 132.613 84.914  1.00 29.35 ?  416 ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 416 ? 136.834 131.916 87.857  1.00 20.69 ?  416 ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 416 ? 137.465 132.629 89.051  1.00 18.38 ?  416 ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 416 ? 137.867 131.668 86.774  1.00 14.34 ?  416 ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 416 ? 138.474 131.794 89.794  1.00 19.31 ?  416 ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 417 ? 134.261 131.135 86.102  1.00 20.94 ?  417 LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 417 ? 133.693 130.539 84.898  1.00 22.96 ?  417 LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 417 ? 132.862 131.555 84.125  1.00 23.58 ?  417 LEU A C     1 
ATOM   3361  O  O     . LEU A 1 417 ? 133.073 131.764 82.924  1.00 34.84 ?  417 LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 417 ? 132.855 129.315 85.270  1.00 25.83 ?  417 LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 417 ? 132.143 128.576 84.136  1.00 28.56 ?  417 LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 417 ? 132.457 127.095 84.200  1.00 25.37 ?  417 LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 417 ? 130.644 128.803 84.205  1.00 28.76 ?  417 LEU A CD2   1 
ATOM   3366  N  N     . ASN A 1 418 ? 131.925 132.218 84.808  1.00 25.55 ?  418 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 418 ? 131.055 133.179 84.140  1.00 25.79 ?  418 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 418 ? 131.830 134.407 83.678  1.00 27.32 ?  418 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 418 ? 131.548 134.957 82.607  1.00 29.87 ?  418 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 418 ? 129.909 133.579 85.068  1.00 25.54 ?  418 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 418 ? 128.970 132.427 85.359  1.00 29.11 ?  418 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 418 ? 128.686 131.613 84.483  1.00 29.68 ?  418 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 418 ? 128.487 132.349 86.592  1.00 29.21 ?  418 ASN A ND2   1 
ATOM   3374  N  N     . VAL A 1 419 ? 132.804 134.855 84.473  1.00 31.03 ?  419 VAL A N     1 
ATOM   3375  C  CA    . VAL A 1 419 ? 133.606 136.013 84.087  1.00 28.81 ?  419 VAL A CA    1 
ATOM   3376  C  C     . VAL A 1 419 ? 134.423 135.708 82.839  1.00 29.87 ?  419 VAL A C     1 
ATOM   3377  O  O     . VAL A 1 419 ? 134.494 136.523 81.911  1.00 32.16 ?  419 VAL A O     1 
ATOM   3378  C  CB    . VAL A 1 419 ? 134.502 136.460 85.258  1.00 26.42 ?  419 VAL A CB    1 
ATOM   3379  C  CG1   . VAL A 1 419 ? 135.597 137.381 84.770  1.00 27.47 ?  419 VAL A CG1   1 
ATOM   3380  C  CG2   . VAL A 1 419 ? 133.675 137.166 86.309  1.00 28.81 ?  419 VAL A CG2   1 
ATOM   3381  N  N     . MET A 1 420 ? 135.047 134.529 82.786  1.00 32.84 ?  420 MET A N     1 
ATOM   3382  C  CA    . MET A 1 420 ? 135.939 134.242 81.670  1.00 33.42 ?  420 MET A CA    1 
ATOM   3383  C  C     . MET A 1 420 ? 135.180 133.837 80.413  1.00 30.71 ?  420 MET A C     1 
ATOM   3384  O  O     . MET A 1 420 ? 135.656 134.102 79.304  1.00 35.76 ?  420 MET A O     1 
ATOM   3385  C  CB    . MET A 1 420 ? 136.949 133.163 82.057  1.00 31.20 ?  420 MET A CB    1 
ATOM   3386  C  CG    . MET A 1 420 ? 138.196 133.738 82.716  1.00 26.08 ?  420 MET A CG    1 
ATOM   3387  S  SD    . MET A 1 420 ? 139.590 134.030 81.612  1.00 47.11 ?  420 MET A SD    1 
ATOM   3388  C  CE    . MET A 1 420 ? 139.688 132.488 80.721  1.00 33.81 ?  420 MET A CE    1 
ATOM   3389  N  N     . GLU A 1 421 ? 134.014 133.198 80.547  1.00 32.30 ?  421 GLU A N     1 
ATOM   3390  C  CA    . GLU A 1 421 ? 133.241 132.874 79.352  1.00 37.53 ?  421 GLU A CA    1 
ATOM   3391  C  C     . GLU A 1 421 ? 132.628 134.115 78.720  1.00 37.35 ?  421 GLU A C     1 
ATOM   3392  O  O     . GLU A 1 421 ? 132.337 134.105 77.520  1.00 40.20 ?  421 GLU A O     1 
ATOM   3393  C  CB    . GLU A 1 421 ? 132.140 131.859 79.670  1.00 34.43 ?  421 GLU A CB    1 
ATOM   3394  C  CG    . GLU A 1 421 ? 131.073 132.359 80.623  1.00 39.15 ?  421 GLU A CG    1 
ATOM   3395  C  CD    . GLU A 1 421 ? 129.921 131.385 80.764  1.00 43.34 ?  421 GLU A CD    1 
ATOM   3396  O  OE1   . GLU A 1 421 ? 129.784 130.496 79.897  1.00 44.06 ?  421 GLU A OE1   1 
ATOM   3397  O  OE2   . GLU A 1 421 ? 129.151 131.507 81.739  1.00 40.29 -1 421 GLU A OE2   1 
ATOM   3398  N  N     . HIS A 1 422 ? 132.432 135.178 79.496  1.00 35.77 ?  422 HIS A N     1 
ATOM   3399  C  CA    . HIS A 1 422 ? 131.968 136.457 78.979  1.00 35.28 ?  422 HIS A CA    1 
ATOM   3400  C  C     . HIS A 1 422 ? 133.112 137.364 78.551  1.00 39.14 ?  422 HIS A C     1 
ATOM   3401  O  O     . HIS A 1 422 ? 132.853 138.450 78.022  1.00 39.84 ?  422 HIS A O     1 
ATOM   3402  C  CB    . HIS A 1 422 ? 131.115 137.174 80.030  1.00 32.46 ?  422 HIS A CB    1 
ATOM   3403  C  CG    . HIS A 1 422 ? 129.740 136.606 80.184  1.00 36.58 ?  422 HIS A CG    1 
ATOM   3404  N  ND1   . HIS A 1 422 ? 129.435 135.638 81.115  1.00 36.83 ?  422 HIS A ND1   1 
ATOM   3405  C  CD2   . HIS A 1 422 ? 128.587 136.870 79.525  1.00 36.85 ?  422 HIS A CD2   1 
ATOM   3406  C  CE1   . HIS A 1 422 ? 128.154 135.329 81.025  1.00 38.65 ?  422 HIS A CE1   1 
ATOM   3407  N  NE2   . HIS A 1 422 ? 127.617 136.062 80.066  1.00 39.61 ?  422 HIS A NE2   1 
ATOM   3408  N  N     . LYS A 1 423 ? 134.359 136.942 78.765  1.00 40.10 ?  423 LYS A N     1 
ATOM   3409  C  CA    . LYS A 1 423 ? 135.543 137.723 78.406  1.00 39.49 ?  423 LYS A CA    1 
ATOM   3410  C  C     . LYS A 1 423 ? 135.478 139.125 79.006  1.00 42.48 ?  423 LYS A C     1 
ATOM   3411  O  O     . LYS A 1 423 ? 135.767 140.129 78.349  1.00 42.19 ?  423 LYS A O     1 
ATOM   3412  C  CB    . LYS A 1 423 ? 135.720 137.779 76.888  1.00 37.95 ?  423 LYS A CB    1 
ATOM   3413  C  CG    . LYS A 1 423 ? 135.967 136.425 76.246  1.00 38.37 ?  423 LYS A CG    1 
ATOM   3414  C  CD    . LYS A 1 423 ? 135.920 136.515 74.730  1.00 40.56 ?  423 LYS A CD    1 
ATOM   3415  C  CE    . LYS A 1 423 ? 135.912 135.136 74.096  1.00 40.10 ?  423 LYS A CE    1 
ATOM   3416  N  NZ    . LYS A 1 423 ? 136.952 134.251 74.688  1.00 43.35 1  423 LYS A NZ    1 
ATOM   3417  N  N     . SER A 1 424 ? 135.094 139.188 80.278  1.00 32.26 ?  424 SER A N     1 
ATOM   3418  C  CA    . SER A 1 424 ? 134.817 140.446 80.961  1.00 29.82 ?  424 SER A CA    1 
ATOM   3419  C  C     . SER A 1 424 ? 135.512 140.495 82.314  1.00 32.67 ?  424 SER A C     1 
ATOM   3420  O  O     . SER A 1 424 ? 134.906 140.814 83.336  1.00 32.96 ?  424 SER A O     1 
ATOM   3421  C  CB    . SER A 1 424 ? 133.313 140.643 81.128  1.00 34.00 ?  424 SER A CB    1 
ATOM   3422  O  OG    . SER A 1 424 ? 132.792 139.756 82.101  1.00 31.39 ?  424 SER A OG    1 
ATOM   3423  N  N     . ILE A 1 425 ? 136.805 140.168 82.343  1.00 31.72 ?  425 ILE A N     1 
ATOM   3424  C  CA    . ILE A 1 425 ? 137.561 140.289 83.587  1.00 23.87 ?  425 ILE A CA    1 
ATOM   3425  C  C     . ILE A 1 425 ? 137.628 141.747 84.027  1.00 29.13 ?  425 ILE A C     1 
ATOM   3426  O  O     . ILE A 1 425 ? 137.349 142.076 85.185  1.00 37.02 ?  425 ILE A O     1 
ATOM   3427  C  CB    . ILE A 1 425 ? 138.967 139.684 83.431  1.00 26.96 ?  425 ILE A CB    1 
ATOM   3428  C  CG1   . ILE A 1 425 ? 138.900 138.158 83.404  1.00 31.42 ?  425 ILE A CG1   1 
ATOM   3429  C  CG2   . ILE A 1 425 ? 139.877 140.145 84.560  1.00 27.22 ?  425 ILE A CG2   1 
ATOM   3430  C  CD1   . ILE A 1 425 ? 140.234 137.500 83.129  1.00 29.41 ?  425 ILE A CD1   1 
ATOM   3431  N  N     . GLU A 1 426 ? 137.976 142.644 83.101  1.00 25.95 ?  426 GLU A N     1 
ATOM   3432  C  CA    . GLU A 1 426 ? 138.149 144.051 83.450  1.00 26.36 ?  426 GLU A CA    1 
ATOM   3433  C  C     . GLU A 1 426 ? 136.846 144.671 83.936  1.00 27.33 ?  426 GLU A C     1 
ATOM   3434  O  O     . GLU A 1 426 ? 136.798 145.285 85.009  1.00 32.66 ?  426 GLU A O     1 
ATOM   3435  C  CB    . GLU A 1 426 ? 138.690 144.821 82.246  1.00 26.18 ?  426 GLU A CB    1 
ATOM   3436  C  CG    . GLU A 1 426 ? 138.499 146.324 82.336  1.00 28.32 ?  426 GLU A CG    1 
ATOM   3437  C  CD    . GLU A 1 426 ? 139.072 147.054 81.140  1.00 36.93 ?  426 GLU A CD    1 
ATOM   3438  O  OE1   . GLU A 1 426 ? 139.515 146.379 80.187  1.00 34.16 ?  426 GLU A OE1   1 
ATOM   3439  O  OE2   . GLU A 1 426 ? 139.078 148.303 81.151  1.00 37.58 -1 426 GLU A OE2   1 
ATOM   3440  N  N     . LYS A 1 427 ? 135.776 144.528 83.149  1.00 27.52 ?  427 LYS A N     1 
ATOM   3441  C  CA    . LYS A 1 427 ? 134.508 145.157 83.500  1.00 24.47 ?  427 LYS A CA    1 
ATOM   3442  C  C     . LYS A 1 427 ? 133.954 144.596 84.801  1.00 26.33 ?  427 LYS A C     1 
ATOM   3443  O  O     . LYS A 1 427 ? 133.486 145.351 85.662  1.00 31.77 ?  427 LYS A O     1 
ATOM   3444  C  CB    . LYS A 1 427 ? 133.505 144.979 82.360  1.00 31.26 ?  427 LYS A CB    1 
ATOM   3445  C  CG    . LYS A 1 427 ? 132.052 145.180 82.760  1.00 28.72 ?  427 LYS A CG    1 
ATOM   3446  C  CD    . LYS A 1 427 ? 131.131 144.267 81.967  1.00 32.81 ?  427 LYS A CD    1 
ATOM   3447  C  CE    . LYS A 1 427 ? 130.962 142.922 82.651  1.00 32.53 ?  427 LYS A CE    1 
ATOM   3448  N  NZ    . LYS A 1 427 ? 129.948 142.071 81.970  1.00 29.00 1  427 LYS A NZ    1 
ATOM   3449  N  N     . THR A 1 428 ? 134.009 143.273 84.970  1.00 26.39 ?  428 THR A N     1 
ATOM   3450  C  CA    . THR A 1 428 ? 133.500 142.668 86.194  1.00 21.30 ?  428 THR A CA    1 
ATOM   3451  C  C     . THR A 1 428 ? 134.311 143.106 87.405  1.00 23.90 ?  428 THR A C     1 
ATOM   3452  O  O     . THR A 1 428 ? 133.739 143.432 88.450  1.00 31.41 ?  428 THR A O     1 
ATOM   3453  C  CB    . THR A 1 428 ? 133.501 141.146 86.080  1.00 25.35 ?  428 THR A CB    1 
ATOM   3454  O  OG1   . THR A 1 428 ? 132.862 140.759 84.858  1.00 29.04 ?  428 THR A OG1   1 
ATOM   3455  C  CG2   . THR A 1 428 ? 132.756 140.529 87.250  1.00 24.41 ?  428 THR A CG2   1 
ATOM   3456  N  N     . VAL A 1 429 ? 135.640 143.128 87.285  1.00 24.51 ?  429 VAL A N     1 
ATOM   3457  C  CA    . VAL A 1 429 ? 136.474 143.528 88.413  1.00 24.24 ?  429 VAL A CA    1 
ATOM   3458  C  C     . VAL A 1 429 ? 136.203 144.977 88.790  1.00 23.22 ?  429 VAL A C     1 
ATOM   3459  O  O     . VAL A 1 429 ? 136.066 145.309 89.973  1.00 26.22 ?  429 VAL A O     1 
ATOM   3460  C  CB    . VAL A 1 429 ? 137.963 143.290 88.096  1.00 21.22 ?  429 VAL A CB    1 
ATOM   3461  C  CG1   . VAL A 1 429 ? 138.841 144.079 89.050  1.00 18.94 ?  429 VAL A CG1   1 
ATOM   3462  C  CG2   . VAL A 1 429 ? 138.293 141.813 88.184  1.00 23.02 ?  429 VAL A CG2   1 
ATOM   3463  N  N     . LYS A 1 430 ? 136.104 145.862 87.795  1.00 22.34 ?  430 LYS A N     1 
ATOM   3464  C  CA    . LYS A 1 430 ? 135.883 147.274 88.096  1.00 20.97 ?  430 LYS A CA    1 
ATOM   3465  C  C     . LYS A 1 430 ? 134.501 147.512 88.693  1.00 23.22 ?  430 LYS A C     1 
ATOM   3466  O  O     . LYS A 1 430 ? 134.358 148.289 89.646  1.00 30.05 ?  430 LYS A O     1 
ATOM   3467  C  CB    . LYS A 1 430 ? 136.090 148.116 86.838  1.00 19.83 ?  430 LYS A CB    1 
ATOM   3468  C  CG    . LYS A 1 430 ? 137.517 148.080 86.321  1.00 23.31 ?  430 LYS A CG    1 
ATOM   3469  C  CD    . LYS A 1 430 ? 137.828 149.273 85.443  1.00 27.87 ?  430 LYS A CD    1 
ATOM   3470  C  CE    . LYS A 1 430 ? 139.313 149.352 85.142  1.00 28.43 ?  430 LYS A CE    1 
ATOM   3471  N  NZ    . LYS A 1 430 ? 139.657 150.573 84.365  1.00 30.72 1  430 LYS A NZ    1 
ATOM   3472  N  N     . LEU A 1 431 ? 133.470 146.849 88.164  1.00 26.98 ?  431 LEU A N     1 
ATOM   3473  C  CA    . LEU A 1 431 ? 132.131 147.020 88.718  1.00 22.52 ?  431 LEU A CA    1 
ATOM   3474  C  C     . LEU A 1 431 ? 132.036 146.443 90.126  1.00 21.71 ?  431 LEU A C     1 
ATOM   3475  O  O     . LEU A 1 431 ? 131.381 147.026 90.998  1.00 28.12 ?  431 LEU A O     1 
ATOM   3476  C  CB    . LEU A 1 431 ? 131.096 146.380 87.796  1.00 27.33 ?  431 LEU A CB    1 
ATOM   3477  C  CG    . LEU A 1 431 ? 130.472 147.295 86.741  1.00 30.18 ?  431 LEU A CG    1 
ATOM   3478  C  CD1   . LEU A 1 431 ? 129.746 146.476 85.687  1.00 26.87 ?  431 LEU A CD1   1 
ATOM   3479  C  CD2   . LEU A 1 431 ? 129.528 148.291 87.391  1.00 28.35 ?  431 LEU A CD2   1 
ATOM   3480  N  N     . ALA A 1 432 ? 132.683 145.301 90.367  1.00 20.35 ?  432 ALA A N     1 
ATOM   3481  C  CA    . ALA A 1 432 ? 132.707 144.730 91.707  1.00 19.22 ?  432 ALA A CA    1 
ATOM   3482  C  C     . ALA A 1 432 ? 133.446 145.641 92.676  1.00 24.76 ?  432 ALA A C     1 
ATOM   3483  O  O     . ALA A 1 432 ? 133.035 145.794 93.829  1.00 26.67 ?  432 ALA A O     1 
ATOM   3484  C  CB    . ALA A 1 432 ? 133.350 143.346 91.673  1.00 26.31 ?  432 ALA A CB    1 
ATOM   3485  N  N     . THR A 1 433 ? 134.544 146.251 92.223  1.00 22.76 ?  433 THR A N     1 
ATOM   3486  C  CA    . THR A 1 433 ? 135.264 147.204 93.058  1.00 17.94 ?  433 THR A CA    1 
ATOM   3487  C  C     . THR A 1 433 ? 134.392 148.407 93.392  1.00 22.72 ?  433 THR A C     1 
ATOM   3488  O  O     . THR A 1 433 ? 134.392 148.882 94.532  1.00 27.81 ?  433 THR A O     1 
ATOM   3489  C  CB    . THR A 1 433 ? 136.546 147.651 92.354  1.00 20.26 ?  433 THR A CB    1 
ATOM   3490  O  OG1   . THR A 1 433 ? 137.305 146.501 91.964  1.00 25.56 ?  433 THR A OG1   1 
ATOM   3491  C  CG2   . THR A 1 433 ? 137.388 148.521 93.272  1.00 24.42 ?  433 THR A CG2   1 
ATOM   3492  N  N     . ASP A 1 434 ? 133.645 148.912 92.409  1.00 20.19 ?  434 ASP A N     1 
ATOM   3493  C  CA    . ASP A 1 434 ? 132.749 150.036 92.666  1.00 15.86 ?  434 ASP A CA    1 
ATOM   3494  C  C     . ASP A 1 434 ? 131.657 149.664 93.664  1.00 19.40 ?  434 ASP A C     1 
ATOM   3495  O  O     . ASP A 1 434 ? 131.337 150.445 94.567  1.00 25.70 ?  434 ASP A O     1 
ATOM   3496  C  CB    . ASP A 1 434 ? 132.135 150.525 91.355  1.00 23.42 ?  434 ASP A CB    1 
ATOM   3497  C  CG    . ASP A 1 434 ? 133.158 151.133 90.423  1.00 31.37 ?  434 ASP A CG    1 
ATOM   3498  O  OD1   . ASP A 1 434 ? 134.180 151.652 90.920  1.00 29.06 ?  434 ASP A OD1   1 
ATOM   3499  O  OD2   . ASP A 1 434 ? 132.944 151.092 89.195  1.00 30.81 -1 434 ASP A OD2   1 
ATOM   3500  N  N     . SER A 1 435 ? 131.072 148.473 93.515  1.00 20.41 ?  435 SER A N     1 
ATOM   3501  C  CA    . SER A 1 435 ? 130.038 148.034 94.450  1.00 17.04 ?  435 SER A CA    1 
ATOM   3502  C  C     . SER A 1 435 ? 130.599 147.853 95.856  1.00 25.13 ?  435 SER A C     1 
ATOM   3503  O  O     . SER A 1 435 ? 129.951 148.223 96.844  1.00 34.54 ?  435 SER A O     1 
ATOM   3504  C  CB    . SER A 1 435 ? 129.405 146.734 93.955  1.00 19.28 ?  435 SER A CB    1 
ATOM   3505  O  OG    . SER A 1 435 ? 130.295 145.645 94.102  1.00 23.37 ?  435 SER A OG    1 
ATOM   3506  N  N     . LEU A 1 436 ? 131.798 147.278 95.965  1.00 18.68 ?  436 LEU A N     1 
ATOM   3507  C  CA    . LEU A 1 436 ? 132.424 147.104 97.269  1.00 13.11 ?  436 LEU A CA    1 
ATOM   3508  C  C     . LEU A 1 436 ? 132.756 148.448 97.903  1.00 15.45 ?  436 LEU A C     1 
ATOM   3509  O  O     . LEU A 1 436 ? 132.599 148.625 99.115  1.00 27.01 ?  436 LEU A O     1 
ATOM   3510  C  CB    . LEU A 1 436 ? 133.676 146.240 97.137  1.00 20.26 ?  436 LEU A CB    1 
ATOM   3511  C  CG    . LEU A 1 436 ? 133.425 144.767 96.821  1.00 17.84 ?  436 LEU A CG    1 
ATOM   3512  C  CD1   . LEU A 1 436 ? 134.730 144.036 96.562  1.00 17.53 ?  436 LEU A CD1   1 
ATOM   3513  C  CD2   . LEU A 1 436 ? 132.654 144.114 97.947  1.00 18.63 ?  436 LEU A CD2   1 
ATOM   3514  N  N     . THR A 1 437 ? 133.216 149.407 97.095  1.00 19.99 ?  437 THR A N     1 
ATOM   3515  C  CA    . THR A 1 437 ? 133.459 150.753 97.600  1.00 20.52 ?  437 THR A CA    1 
ATOM   3516  C  C     . THR A 1 437 ? 132.172 151.388 98.105  1.00 23.63 ?  437 THR A C     1 
ATOM   3517  O  O     . THR A 1 437 ? 132.160 152.026 99.164  1.00 25.90 ?  437 THR A O     1 
ATOM   3518  C  CB    . THR A 1 437 ? 134.084 151.614 96.503  1.00 18.17 ?  437 THR A CB    1 
ATOM   3519  O  OG1   . THR A 1 437 ? 135.271 150.979 96.016  1.00 17.98 ?  437 THR A OG1   1 
ATOM   3520  C  CG2   . THR A 1 437 ? 134.434 152.989 97.040  1.00 22.56 ?  437 THR A CG2   1 
ATOM   3521  N  N     . HIS A 1 438 ? 131.074 151.221 97.364  1.00 22.47 ?  438 HIS A N     1 
ATOM   3522  C  CA    . HIS A 1 438 ? 129.799 151.777 97.801  1.00 23.06 ?  438 HIS A CA    1 
ATOM   3523  C  C     . HIS A 1 438 ? 129.347 151.160 99.118  1.00 22.61 ?  438 HIS A C     1 
ATOM   3524  O  O     . HIS A 1 438 ? 128.891 151.872 100.021 1.00 26.43 ?  438 HIS A O     1 
ATOM   3525  C  CB    . HIS A 1 438 ? 128.735 151.569 96.726  1.00 26.74 ?  438 HIS A CB    1 
ATOM   3526  C  CG    . HIS A 1 438 ? 127.346 151.879 97.190  1.00 27.35 ?  438 HIS A CG    1 
ATOM   3527  N  ND1   . HIS A 1 438 ? 126.846 153.162 97.237  1.00 25.41 ?  438 HIS A ND1   1 
ATOM   3528  C  CD2   . HIS A 1 438 ? 126.356 151.073 97.639  1.00 23.58 ?  438 HIS A CD2   1 
ATOM   3529  C  CE1   . HIS A 1 438 ? 125.606 153.132 97.691  1.00 30.51 ?  438 HIS A CE1   1 
ATOM   3530  N  NE2   . HIS A 1 438 ? 125.284 151.877 97.941  1.00 29.10 ?  438 HIS A NE2   1 
ATOM   3531  N  N     . VAL A 1 439 ? 129.467 149.838 99.248  1.00 24.67 ?  439 VAL A N     1 
ATOM   3532  C  CA    . VAL A 1 439 ? 129.035 149.186 100.482 1.00 20.20 ?  439 VAL A CA    1 
ATOM   3533  C  C     . VAL A 1 439 ? 129.930 149.586 101.649 1.00 27.85 ?  439 VAL A C     1 
ATOM   3534  O  O     . VAL A 1 439 ? 129.448 149.770 102.774 1.00 36.63 ?  439 VAL A O     1 
ATOM   3535  C  CB    . VAL A 1 439 ? 128.987 147.659 100.290 1.00 20.52 ?  439 VAL A CB    1 
ATOM   3536  C  CG1   . VAL A 1 439 ? 128.877 146.947 101.629 1.00 21.99 ?  439 VAL A CG1   1 
ATOM   3537  C  CG2   . VAL A 1 439 ? 127.832 147.280 99.395  1.00 30.53 ?  439 VAL A CG2   1 
ATOM   3538  N  N     . SER A 1 440 ? 131.235 149.741 101.410 1.00 21.50 ?  440 SER A N     1 
ATOM   3539  C  CA    . SER A 1 440 ? 132.131 150.204 102.464 1.00 20.63 ?  440 SER A CA    1 
ATOM   3540  C  C     . SER A 1 440 ? 131.799 151.631 102.885 1.00 24.45 ?  440 SER A C     1 
ATOM   3541  O  O     . SER A 1 440 ? 131.867 151.965 104.074 1.00 26.57 ?  440 SER A O     1 
ATOM   3542  C  CB    . SER A 1 440 ? 133.583 150.102 101.997 1.00 25.67 ?  440 SER A CB    1 
ATOM   3543  O  OG    . SER A 1 440 ? 134.477 150.553 102.999 1.00 24.86 ?  440 SER A OG    1 
ATOM   3544  N  N     . GLU A 1 441 ? 131.444 152.488 101.924 1.00 26.21 ?  441 GLU A N     1 
ATOM   3545  C  CA    . GLU A 1 441 ? 131.107 153.869 102.248 1.00 23.41 ?  441 GLU A CA    1 
ATOM   3546  C  C     . GLU A 1 441 ? 129.770 153.972 102.968 1.00 30.31 ?  441 GLU A C     1 
ATOM   3547  O  O     . GLU A 1 441 ? 129.580 154.876 103.789 1.00 38.74 ?  441 GLU A O     1 
ATOM   3548  C  CB    . GLU A 1 441 ? 131.086 154.718 100.977 1.00 25.90 ?  441 GLU A CB    1 
ATOM   3549  C  CG    . GLU A 1 441 ? 132.456 155.025 100.406 1.00 29.16 ?  441 GLU A CG    1 
ATOM   3550  C  CD    . GLU A 1 441 ? 132.412 155.299 98.917  1.00 36.38 ?  441 GLU A CD    1 
ATOM   3551  O  OE1   . GLU A 1 441 ? 131.397 154.952 98.276  1.00 34.67 ?  441 GLU A OE1   1 
ATOM   3552  O  OE2   . GLU A 1 441 ? 133.390 155.866 98.384  1.00 36.67 -1 441 GLU A OE2   1 
ATOM   3553  N  N     . THR A 1 442 ? 128.835 153.071 102.676 1.00 30.88 ?  442 THR A N     1 
ATOM   3554  C  CA    . THR A 1 442 ? 127.522 153.098 103.306 1.00 29.96 ?  442 THR A CA    1 
ATOM   3555  C  C     . THR A 1 442 ? 127.480 152.339 104.625 1.00 30.74 ?  442 THR A C     1 
ATOM   3556  O  O     . THR A 1 442 ? 126.415 152.266 105.246 1.00 38.69 ?  442 THR A O     1 
ATOM   3557  C  CB    . THR A 1 442 ? 126.462 152.528 102.358 1.00 29.97 ?  442 THR A CB    1 
ATOM   3558  O  OG1   . THR A 1 442 ? 126.871 151.233 101.902 1.00 33.39 ?  442 THR A OG1   1 
ATOM   3559  C  CG2   . THR A 1 442 ? 126.268 153.446 101.163 1.00 29.67 ?  442 THR A CG2   1 
ATOM   3560  N  N     . THR A 1 443 ? 128.602 151.778 105.066 1.00 29.39 ?  443 THR A N     1 
ATOM   3561  C  CA    . THR A 1 443 ? 128.665 151.082 106.343 1.00 32.14 ?  443 THR A CA    1 
ATOM   3562  C  C     . THR A 1 443 ? 129.022 152.071 107.444 1.00 37.04 ?  443 THR A C     1 
ATOM   3563  O  O     . THR A 1 443 ? 130.031 152.777 107.350 1.00 39.75 ?  443 THR A O     1 
ATOM   3564  C  CB    . THR A 1 443 ? 129.691 149.950 106.296 1.00 32.36 ?  443 THR A CB    1 
ATOM   3565  O  OG1   . THR A 1 443 ? 129.254 148.945 105.372 1.00 36.65 ?  443 THR A OG1   1 
ATOM   3566  C  CG2   . THR A 1 443 ? 129.857 149.325 107.671 1.00 26.65 ?  443 THR A CG2   1 
ATOM   3567  N  N     . ASP A 1 444 ? 128.190 152.120 108.483 1.00 43.45 ?  444 ASP A N     1 
ATOM   3568  C  CA    . ASP A 1 444 ? 128.398 153.026 109.613 1.00 42.13 ?  444 ASP A CA    1 
ATOM   3569  C  C     . ASP A 1 444 ? 128.025 152.270 110.884 1.00 41.49 ?  444 ASP A C     1 
ATOM   3570  O  O     . ASP A 1 444 ? 126.840 152.089 111.180 1.00 42.15 ?  444 ASP A O     1 
ATOM   3571  C  CB    . ASP A 1 444 ? 127.578 154.300 109.459 1.00 43.52 ?  444 ASP A CB    1 
ATOM   3572  C  CG    . ASP A 1 444 ? 128.394 155.551 109.707 1.00 47.76 ?  444 ASP A CG    1 
ATOM   3573  O  OD1   . ASP A 1 444 ? 129.632 155.441 109.824 1.00 46.38 ?  444 ASP A OD1   1 
ATOM   3574  O  OD2   . ASP A 1 444 ? 127.798 156.646 109.783 1.00 47.26 -1 444 ASP A OD2   1 
ATOM   3575  N  N     . ILE A 1 445 ? 129.035 151.838 111.632 1.00 34.72 ?  445 ILE A N     1 
ATOM   3576  C  CA    . ILE A 1 445 ? 128.841 151.078 112.859 1.00 37.80 ?  445 ILE A CA    1 
ATOM   3577  C  C     . ILE A 1 445 ? 129.094 152.006 114.037 1.00 38.51 ?  445 ILE A C     1 
ATOM   3578  O  O     . ILE A 1 445 ? 130.208 152.514 114.212 1.00 39.84 ?  445 ILE A O     1 
ATOM   3579  C  CB    . ILE A 1 445 ? 129.760 149.848 112.908 1.00 36.80 ?  445 ILE A CB    1 
ATOM   3580  C  CG1   . ILE A 1 445 ? 129.405 148.889 111.771 1.00 34.86 ?  445 ILE A CG1   1 
ATOM   3581  C  CG2   . ILE A 1 445 ? 129.644 149.150 114.250 1.00 37.90 ?  445 ILE A CG2   1 
ATOM   3582  C  CD1   . ILE A 1 445 ? 130.401 147.782 111.575 1.00 34.17 ?  445 ILE A CD1   1 
ATOM   3583  N  N     . ARG A 1 446 ? 128.062 152.227 114.846 1.00 40.85 ?  446 ARG A N     1 
ATOM   3584  C  CA    . ARG A 1 446 ? 128.098 153.213 115.916 1.00 46.28 ?  446 ARG A CA    1 
ATOM   3585  C  C     . ARG A 1 446 ? 128.527 152.630 117.257 1.00 44.95 ?  446 ARG A C     1 
ATOM   3586  O  O     . ARG A 1 446 ? 128.575 153.367 118.246 1.00 41.08 ?  446 ARG A O     1 
ATOM   3587  C  CB    . ARG A 1 446 ? 126.724 153.877 116.062 1.00 44.76 ?  446 ARG A CB    1 
ATOM   3588  C  CG    . ARG A 1 446 ? 125.863 153.812 114.808 1.00 43.05 ?  446 ARG A CG    1 
ATOM   3589  C  CD    . ARG A 1 446 ? 126.408 154.700 113.696 1.00 45.48 ?  446 ARG A CD    1 
ATOM   3590  N  NE    . ARG A 1 446 ? 126.048 156.101 113.878 1.00 47.02 ?  446 ARG A NE    1 
ATOM   3591  C  CZ    . ARG A 1 446 ? 124.847 156.604 113.623 1.00 47.76 ?  446 ARG A CZ    1 
ATOM   3592  N  NH1   . ARG A 1 446 ? 123.858 155.844 113.180 1.00 43.40 1  446 ARG A NH1   1 
ATOM   3593  N  NH2   . ARG A 1 446 ? 124.634 157.902 113.816 1.00 47.17 ?  446 ARG A NH2   1 
ATOM   3594  N  N     . ASN A 1 447 ? 128.839 151.336 117.316 1.00 34.40 ?  447 ASN A N     1 
ATOM   3595  C  CA    . ASN A 1 447 ? 129.273 150.700 118.550 1.00 29.03 ?  447 ASN A CA    1 
ATOM   3596  C  C     . ASN A 1 447 ? 130.670 150.107 118.455 1.00 32.18 ?  447 ASN A C     1 
ATOM   3597  O  O     . ASN A 1 447 ? 131.158 149.547 119.443 1.00 35.53 ?  447 ASN A O     1 
ATOM   3598  C  CB    . ASN A 1 447 ? 128.278 149.607 118.961 1.00 32.55 ?  447 ASN A CB    1 
ATOM   3599  C  CG    . ASN A 1 447 ? 127.164 150.136 119.836 1.00 29.77 ?  447 ASN A CG    1 
ATOM   3600  O  OD1   . ASN A 1 447 ? 127.361 151.068 120.614 1.00 28.36 ?  447 ASN A OD1   1 
ATOM   3601  N  ND2   . ASN A 1 447 ? 125.981 149.549 119.706 1.00 32.26 ?  447 ASN A ND2   1 
ATOM   3602  N  N     . ALA A 1 448 ? 131.323 150.210 117.298 1.00 34.16 ?  448 ALA A N     1 
ATOM   3603  C  CA    . ALA A 1 448 ? 132.702 149.766 117.105 1.00 29.31 ?  448 ALA A CA    1 
ATOM   3604  C  C     . ALA A 1 448 ? 133.496 150.963 116.597 1.00 29.15 ?  448 ALA A C     1 
ATOM   3605  O  O     . ALA A 1 448 ? 133.546 151.215 115.382 1.00 29.10 ?  448 ALA A O     1 
ATOM   3606  C  CB    . ALA A 1 448 ? 132.778 148.590 116.137 1.00 24.41 ?  448 ALA A CB    1 
ATOM   3607  N  N     . PRO A 1 449 ? 134.124 151.732 117.490 1.00 28.77 ?  449 PRO A N     1 
ATOM   3608  C  CA    . PRO A 1 449 ? 134.781 152.971 117.038 1.00 22.93 ?  449 PRO A CA    1 
ATOM   3609  C  C     . PRO A 1 449 ? 135.972 152.722 116.134 1.00 27.34 ?  449 PRO A C     1 
ATOM   3610  O  O     . PRO A 1 449 ? 136.130 153.416 115.122 1.00 22.25 ?  449 PRO A O     1 
ATOM   3611  C  CB    . PRO A 1 449 ? 135.200 153.650 118.353 1.00 19.14 ?  449 PRO A CB    1 
ATOM   3612  C  CG    . PRO A 1 449 ? 134.551 152.863 119.452 1.00 25.18 ?  449 PRO A CG    1 
ATOM   3613  C  CD    . PRO A 1 449 ? 134.310 151.496 118.928 1.00 23.69 ?  449 PRO A CD    1 
ATOM   3614  N  N     . ALA A 1 450 ? 136.817 151.744 116.467 1.00 25.81 ?  450 ALA A N     1 
ATOM   3615  C  CA    . ALA A 1 450 ? 137.987 151.473 115.641 1.00 16.45 ?  450 ALA A CA    1 
ATOM   3616  C  C     . ALA A 1 450 ? 137.599 150.843 114.309 1.00 22.90 ?  450 ALA A C     1 
ATOM   3617  O  O     . ALA A 1 450 ? 138.230 151.133 113.288 1.00 26.91 ?  450 ALA A O     1 
ATOM   3618  C  CB    . ALA A 1 450 ? 138.967 150.577 116.396 1.00 19.28 ?  450 ALA A CB    1 
ATOM   3619  N  N     . VAL A 1 451 ? 136.562 150.004 114.294 1.00 28.04 ?  451 VAL A N     1 
ATOM   3620  C  CA    . VAL A 1 451 ? 136.079 149.439 113.036 1.00 18.02 ?  451 VAL A CA    1 
ATOM   3621  C  C     . VAL A 1 451 ? 135.588 150.548 112.114 1.00 21.83 ?  451 VAL A C     1 
ATOM   3622  O  O     . VAL A 1 451 ? 135.915 150.583 110.923 1.00 30.56 ?  451 VAL A O     1 
ATOM   3623  C  CB    . VAL A 1 451 ? 134.976 148.398 113.300 1.00 21.98 ?  451 VAL A CB    1 
ATOM   3624  C  CG1   . VAL A 1 451 ? 134.188 148.118 112.032 1.00 23.76 ?  451 VAL A CG1   1 
ATOM   3625  C  CG2   . VAL A 1 451 ? 135.572 147.116 113.851 1.00 22.51 ?  451 VAL A CG2   1 
ATOM   3626  N  N     . ARG A 1 452 ? 134.799 151.478 112.658 1.00 20.50 ?  452 ARG A N     1 
ATOM   3627  C  CA    . ARG A 1 452 ? 134.293 152.588 111.857 1.00 22.77 ?  452 ARG A CA    1 
ATOM   3628  C  C     . ARG A 1 452 ? 135.425 153.485 111.372 1.00 23.83 ?  452 ARG A C     1 
ATOM   3629  O  O     . ARG A 1 452 ? 135.438 153.911 110.208 1.00 33.52 ?  452 ARG A O     1 
ATOM   3630  C  CB    . ARG A 1 452 ? 133.280 153.391 112.673 1.00 21.08 ?  452 ARG A CB    1 
ATOM   3631  C  CG    . ARG A 1 452 ? 132.873 154.711 112.052 1.00 26.53 ?  452 ARG A CG    1 
ATOM   3632  C  CD    . ARG A 1 452 ? 131.804 155.392 112.885 1.00 27.26 ?  452 ARG A CD    1 
ATOM   3633  N  NE    . ARG A 1 452 ? 132.136 155.374 114.305 1.00 38.94 ?  452 ARG A NE    1 
ATOM   3634  C  CZ    . ARG A 1 452 ? 131.368 155.876 115.262 1.00 41.10 ?  452 ARG A CZ    1 
ATOM   3635  N  NH1   . ARG A 1 452 ? 130.204 156.444 114.988 1.00 34.44 1  452 ARG A NH1   1 
ATOM   3636  N  NH2   . ARG A 1 452 ? 131.778 155.807 116.525 1.00 29.62 ?  452 ARG A NH2   1 
ATOM   3637  N  N     . ARG A 1 453 ? 136.388 153.780 112.248 1.00 21.78 ?  453 ARG A N     1 
ATOM   3638  C  CA    . ARG A 1 453 ? 137.504 154.636 111.859 1.00 20.91 ?  453 ARG A CA    1 
ATOM   3639  C  C     . ARG A 1 453 ? 138.339 153.988 110.763 1.00 25.75 ?  453 ARG A C     1 
ATOM   3640  O  O     . ARG A 1 453 ? 138.734 154.654 109.799 1.00 29.91 ?  453 ARG A O     1 
ATOM   3641  C  CB    . ARG A 1 453 ? 138.369 154.958 113.079 1.00 20.33 ?  453 ARG A CB    1 
ATOM   3642  C  CG    . ARG A 1 453 ? 139.759 155.466 112.737 1.00 23.78 ?  453 ARG A CG    1 
ATOM   3643  C  CD    . ARG A 1 453 ? 140.366 156.259 113.881 1.00 21.86 ?  453 ARG A CD    1 
ATOM   3644  N  NE    . ARG A 1 453 ? 141.655 155.714 114.291 1.00 21.77 ?  453 ARG A NE    1 
ATOM   3645  C  CZ    . ARG A 1 453 ? 142.813 156.026 113.726 1.00 23.79 ?  453 ARG A CZ    1 
ATOM   3646  N  NH1   . ARG A 1 453 ? 142.883 156.878 112.718 1.00 24.12 1  453 ARG A NH1   1 
ATOM   3647  N  NH2   . ARG A 1 453 ? 143.929 155.466 114.183 1.00 25.71 ?  453 ARG A NH2   1 
ATOM   3648  N  N     . ALA A 1 454 ? 138.605 152.685 110.883 1.00 23.64 ?  454 ALA A N     1 
ATOM   3649  C  CA    . ALA A 1 454 ? 139.386 151.995 109.865 1.00 18.39 ?  454 ALA A CA    1 
ATOM   3650  C  C     . ALA A 1 454 ? 138.608 151.837 108.566 1.00 18.15 ?  454 ALA A C     1 
ATOM   3651  O  O     . ALA A 1 454 ? 139.207 151.844 107.488 1.00 23.75 ?  454 ALA A O     1 
ATOM   3652  C  CB    . ALA A 1 454 ? 139.841 150.634 110.382 1.00 20.65 ?  454 ALA A CB    1 
ATOM   3653  N  N     . ASN A 1 455 ? 137.285 151.692 108.640 1.00 20.68 ?  455 ASN A N     1 
ATOM   3654  C  CA    . ASN A 1 455 ? 136.489 151.657 107.419 1.00 21.99 ?  455 ASN A CA    1 
ATOM   3655  C  C     . ASN A 1 455 ? 136.533 153.000 106.701 1.00 25.45 ?  455 ASN A C     1 
ATOM   3656  O  O     . ASN A 1 455 ? 136.634 153.051 105.471 1.00 30.27 ?  455 ASN A O     1 
ATOM   3657  C  CB    . ASN A 1 455 ? 135.049 151.261 107.738 1.00 19.31 ?  455 ASN A CB    1 
ATOM   3658  C  CG    . ASN A 1 455 ? 134.186 151.155 106.498 1.00 27.04 ?  455 ASN A CG    1 
ATOM   3659  O  OD1   . ASN A 1 455 ? 134.491 150.395 105.580 1.00 31.25 ?  455 ASN A OD1   1 
ATOM   3660  N  ND2   . ASN A 1 455 ? 133.101 151.919 106.464 1.00 26.78 ?  455 ASN A ND2   1 
ATOM   3661  N  N     . LYS A 1 456 ? 136.456 154.099 107.457 1.00 24.12 ?  456 LYS A N     1 
ATOM   3662  C  CA    . LYS A 1 456 ? 136.529 155.420 106.841 1.00 25.23 ?  456 LYS A CA    1 
ATOM   3663  C  C     . LYS A 1 456 ? 137.916 155.701 106.276 1.00 23.97 ?  456 LYS A C     1 
ATOM   3664  O  O     . LYS A 1 456 ? 138.045 156.301 105.202 1.00 29.54 ?  456 LYS A O     1 
ATOM   3665  C  CB    . LYS A 1 456 ? 136.139 156.494 107.857 1.00 27.55 ?  456 LYS A CB    1 
ATOM   3666  C  CG    . LYS A 1 456 ? 134.727 157.033 107.685 1.00 30.26 ?  456 LYS A CG    1 
ATOM   3667  C  CD    . LYS A 1 456 ? 134.028 157.239 109.025 1.00 33.55 ?  456 LYS A CD    1 
ATOM   3668  C  CE    . LYS A 1 456 ? 135.015 157.587 110.133 1.00 33.77 ?  456 LYS A CE    1 
ATOM   3669  N  NZ    . LYS A 1 456 ? 134.356 157.688 111.463 1.00 31.84 1  456 LYS A NZ    1 
ATOM   3670  N  N     . ALA A 1 457 ? 138.966 155.277 106.982 1.00 19.17 ?  457 ALA A N     1 
ATOM   3671  C  CA    . ALA A 1 457 ? 140.327 155.636 106.598 1.00 17.96 ?  457 ALA A CA    1 
ATOM   3672  C  C     . ALA A 1 457 ? 140.886 154.696 105.534 1.00 24.71 ?  457 ALA A C     1 
ATOM   3673  O  O     . ALA A 1 457 ? 141.264 155.129 104.441 1.00 29.05 ?  457 ALA A O     1 
ATOM   3674  C  CB    . ALA A 1 457 ? 141.229 155.637 107.835 1.00 15.33 ?  457 ALA A CB    1 
ATOM   3675  N  N     . MET A 1 458 ? 140.950 153.402 105.847 1.00 23.82 ?  458 MET A N     1 
ATOM   3676  C  CA    . MET A 1 458 ? 141.580 152.429 104.964 1.00 19.43 ?  458 MET A CA    1 
ATOM   3677  C  C     . MET A 1 458 ? 140.777 152.185 103.693 1.00 23.77 ?  458 MET A C     1 
ATOM   3678  O  O     . MET A 1 458 ? 141.370 151.955 102.633 1.00 30.03 ?  458 MET A O     1 
ATOM   3679  C  CB    . MET A 1 458 ? 141.788 151.114 105.714 1.00 22.61 ?  458 MET A CB    1 
ATOM   3680  C  CG    . MET A 1 458 ? 142.629 151.249 106.971 1.00 14.51 ?  458 MET A CG    1 
ATOM   3681  S  SD    . MET A 1 458 ? 144.351 151.637 106.611 1.00 33.37 ?  458 MET A SD    1 
ATOM   3682  C  CE    . MET A 1 458 ? 145.109 150.030 106.835 1.00 22.54 ?  458 MET A CE    1 
ATOM   3683  N  N     . LYS A 1 459 ? 139.446 152.221 103.779 1.00 18.14 ?  459 LYS A N     1 
ATOM   3684  C  CA    . LYS A 1 459 ? 138.574 151.937 102.637 1.00 21.43 ?  459 LYS A CA    1 
ATOM   3685  C  C     . LYS A 1 459 ? 138.906 150.580 102.022 1.00 21.56 ?  459 LYS A C     1 
ATOM   3686  O  O     . LYS A 1 459 ? 138.906 150.407 100.802 1.00 27.81 ?  459 LYS A O     1 
ATOM   3687  C  CB    . LYS A 1 459 ? 138.655 153.043 101.583 1.00 22.37 ?  459 LYS A CB    1 
ATOM   3688  C  CG    . LYS A 1 459 ? 138.323 154.430 102.098 1.00 24.94 ?  459 LYS A CG    1 
ATOM   3689  C  CD    . LYS A 1 459 ? 139.404 155.425 101.718 1.00 25.12 ?  459 LYS A CD    1 
ATOM   3690  C  CE    . LYS A 1 459 ? 138.851 156.836 101.649 1.00 27.52 ?  459 LYS A CE    1 
ATOM   3691  N  NZ    . LYS A 1 459 ? 137.629 156.994 102.485 1.00 30.30 1  459 LYS A NZ    1 
ATOM   3692  N  N     . SER A 1 460 ? 139.195 149.609 102.881 1.00 20.55 ?  460 SER A N     1 
ATOM   3693  C  CA    . SER A 1 460 ? 139.632 148.300 102.423 1.00 11.16 ?  460 SER A CA    1 
ATOM   3694  C  C     . SER A 1 460 ? 138.440 147.445 102.018 1.00 15.54 ?  460 SER A C     1 
ATOM   3695  O  O     . SER A 1 460 ? 137.427 147.390 102.719 1.00 26.00 ?  460 SER A O     1 
ATOM   3696  C  CB    . SER A 1 460 ? 140.436 147.596 103.514 1.00 13.25 ?  460 SER A CB    1 
ATOM   3697  O  OG    . SER A 1 460 ? 139.631 146.672 104.220 1.00 13.78 ?  460 SER A OG    1 
ATOM   3698  N  N     . ILE A 1 461 ? 138.571 146.779 100.873 1.00 17.07 ?  461 ILE A N     1 
ATOM   3699  C  CA    . ILE A 1 461 ? 137.554 145.876 100.359 1.00 11.44 ?  461 ILE A CA    1 
ATOM   3700  C  C     . ILE A 1 461 ? 138.215 144.540 100.055 1.00 18.03 ?  461 ILE A C     1 
ATOM   3701  O  O     . ILE A 1 461 ? 139.427 144.451 99.855  1.00 18.23 ?  461 ILE A O     1 
ATOM   3702  C  CB    . ILE A 1 461 ? 136.861 146.433 99.098  1.00 13.11 ?  461 ILE A CB    1 
ATOM   3703  C  CG1   . ILE A 1 461 ? 137.891 146.672 97.993  1.00 8.92  ?  461 ILE A CG1   1 
ATOM   3704  C  CG2   . ILE A 1 461 ? 136.114 147.718 99.423  1.00 13.75 ?  461 ILE A CG2   1 
ATOM   3705  C  CD1   . ILE A 1 461 ? 137.286 146.986 96.650  1.00 8.18  ?  461 ILE A CD1   1 
ATOM   3706  N  N     . GLY A 1 462 ? 137.405 143.488 100.051 1.00 17.97 ?  462 GLY A N     1 
ATOM   3707  C  CA    . GLY A 1 462 ? 137.893 142.193 99.631  1.00 8.19  ?  462 GLY A CA    1 
ATOM   3708  C  C     . GLY A 1 462 ? 137.157 141.659 98.422  1.00 5.51  ?  462 GLY A C     1 
ATOM   3709  O  O     . GLY A 1 462 ? 135.997 141.254 98.525  1.00 19.62 ?  462 GLY A O     1 
ATOM   3710  N  N     . LEU A 1 463 ? 137.824 141.633 97.274  1.00 11.37 ?  463 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 463 ? 137.254 141.087 96.049  1.00 9.14  ?  463 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 463 ? 137.811 139.684 95.854  1.00 11.19 ?  463 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 463 ? 138.997 139.515 95.558  1.00 20.03 ?  463 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 463 ? 137.567 141.980 94.852  1.00 18.61 ?  463 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 463 ? 137.016 141.510 93.503  1.00 18.85 ?  463 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 463 ? 135.539 141.178 93.615  1.00 9.23  ?  463 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 463 ? 137.253 142.561 92.433  1.00 15.50 ?  463 LEU A CD2   1 
ATOM   3718  N  N     . GLY A 1 464 ? 136.954 138.678 96.024  1.00 12.27 ?  464 GLY A N     1 
ATOM   3719  C  CA    . GLY A 1 464 ? 137.353 137.296 95.898  1.00 8.91  ?  464 GLY A CA    1 
ATOM   3720  C  C     . GLY A 1 464 ? 136.965 136.691 94.558  1.00 14.99 ?  464 GLY A C     1 
ATOM   3721  O  O     . GLY A 1 464 ? 136.416 137.341 93.671  1.00 21.90 ?  464 GLY A O     1 
ATOM   3722  N  N     . ALA A 1 465 ? 137.274 135.407 94.427  1.00 14.56 ?  465 ALA A N     1 
ATOM   3723  C  CA    . ALA A 1 465 ? 136.930 134.642 93.241  1.00 10.65 ?  465 ALA A CA    1 
ATOM   3724  C  C     . ALA A 1 465 ? 136.420 133.274 93.665  1.00 13.06 ?  465 ALA A C     1 
ATOM   3725  O  O     . ALA A 1 465 ? 136.763 132.772 94.738  1.00 22.50 ?  465 ALA A O     1 
ATOM   3726  C  CB    . ALA A 1 465 ? 138.127 134.493 92.296  1.00 16.40 ?  465 ALA A CB    1 
ATOM   3727  N  N     . MET A 1 466 ? 135.589 132.682 92.814  1.00 13.84 ?  466 MET A N     1 
ATOM   3728  C  CA    . MET A 1 466 ? 135.057 131.353 93.060  1.00 20.15 ?  466 MET A CA    1 
ATOM   3729  C  C     . MET A 1 466 ? 134.883 130.646 91.725  1.00 20.70 ?  466 MET A C     1 
ATOM   3730  O  O     . MET A 1 466 ? 135.095 131.230 90.659  1.00 27.41 ?  466 MET A O     1 
ATOM   3731  C  CB    . MET A 1 466 ? 133.733 131.410 93.828  1.00 25.63 ?  466 MET A CB    1 
ATOM   3732  C  CG    . MET A 1 466 ? 132.617 132.083 93.061  1.00 21.84 ?  466 MET A CG    1 
ATOM   3733  S  SD    . MET A 1 466 ? 131.144 132.358 94.053  1.00 34.17 ?  466 MET A SD    1 
ATOM   3734  C  CE    . MET A 1 466 ? 130.237 133.435 92.957  1.00 25.31 ?  466 MET A CE    1 
ATOM   3735  N  N     . ASN A 1 467 ? 134.493 129.373 91.800  1.00 13.45 ?  467 ASN A N     1 
ATOM   3736  C  CA    . ASN A 1 467 ? 134.305 128.520 90.626  1.00 16.31 ?  467 ASN A CA    1 
ATOM   3737  C  C     . ASN A 1 467 ? 135.606 128.313 89.860  1.00 18.38 ?  467 ASN A C     1 
ATOM   3738  O  O     . ASN A 1 467 ? 135.596 128.127 88.642  1.00 23.98 ?  467 ASN A O     1 
ATOM   3739  C  CB    . ASN A 1 467 ? 133.223 129.072 89.693  1.00 20.54 ?  467 ASN A CB    1 
ATOM   3740  C  CG    . ASN A 1 467 ? 132.373 127.982 89.078  1.00 23.54 ?  467 ASN A CG    1 
ATOM   3741  O  OD1   . ASN A 1 467 ? 132.499 126.810 89.429  1.00 31.27 ?  467 ASN A OD1   1 
ATOM   3742  N  ND2   . ASN A 1 467 ? 131.499 128.362 88.156  1.00 23.37 ?  467 ASN A ND2   1 
ATOM   3743  N  N     . LEU A 1 468 ? 136.739 128.350 90.562  1.00 18.69 ?  468 LEU A N     1 
ATOM   3744  C  CA    . LEU A 1 468 ? 138.012 128.057 89.913  1.00 13.32 ?  468 LEU A CA    1 
ATOM   3745  C  C     . LEU A 1 468 ? 138.077 126.598 89.485  1.00 20.58 ?  468 LEU A C     1 
ATOM   3746  O  O     . LEU A 1 468 ? 138.375 126.291 88.324  1.00 21.33 ?  468 LEU A O     1 
ATOM   3747  C  CB    . LEU A 1 468 ? 139.173 128.393 90.847  1.00 22.42 ?  468 LEU A CB    1 
ATOM   3748  C  CG    . LEU A 1 468 ? 140.557 127.949 90.372  1.00 19.10 ?  468 LEU A CG    1 
ATOM   3749  C  CD1   . LEU A 1 468 ? 141.004 128.760 89.167  1.00 16.67 ?  468 LEU A CD1   1 
ATOM   3750  C  CD2   . LEU A 1 468 ? 141.572 128.046 91.495  1.00 14.68 ?  468 LEU A CD2   1 
ATOM   3751  N  N     . HIS A 1 469 ? 137.780 125.683 90.409  1.00 25.22 ?  469 HIS A N     1 
ATOM   3752  C  CA    . HIS A 1 469 ? 137.798 124.266 90.071  1.00 16.21 ?  469 HIS A CA    1 
ATOM   3753  C  C     . HIS A 1 469 ? 136.691 123.923 89.087  1.00 25.21 ?  469 HIS A C     1 
ATOM   3754  O  O     . HIS A 1 469 ? 136.888 123.098 88.191  1.00 33.67 ?  469 HIS A O     1 
ATOM   3755  C  CB    . HIS A 1 469 ? 137.675 123.411 91.329  1.00 17.64 ?  469 HIS A CB    1 
ATOM   3756  C  CG    . HIS A 1 469 ? 137.988 121.965 91.102  1.00 22.56 ?  469 HIS A CG    1 
ATOM   3757  N  ND1   . HIS A 1 469 ? 137.759 120.994 92.050  1.00 27.87 ?  469 HIS A ND1   1 
ATOM   3758  C  CD2   . HIS A 1 469 ? 138.516 121.327 90.030  1.00 23.49 ?  469 HIS A CD2   1 
ATOM   3759  C  CE1   . HIS A 1 469 ? 138.130 119.819 91.573  1.00 23.94 ?  469 HIS A CE1   1 
ATOM   3760  N  NE2   . HIS A 1 469 ? 138.593 119.995 90.349  1.00 28.10 ?  469 HIS A NE2   1 
ATOM   3761  N  N     . GLY A 1 470 ? 135.518 124.539 89.239  1.00 24.88 ?  470 GLY A N     1 
ATOM   3762  C  CA    . GLY A 1 470 ? 134.462 124.327 88.266  1.00 20.72 ?  470 GLY A CA    1 
ATOM   3763  C  C     . GLY A 1 470 ? 134.877 124.751 86.872  1.00 18.09 ?  470 GLY A C     1 
ATOM   3764  O  O     . GLY A 1 470 ? 134.697 124.009 85.904  1.00 35.24 ?  470 GLY A O     1 
ATOM   3765  N  N     . TYR A 1 471 ? 135.466 125.943 86.756  1.00 17.42 ?  471 TYR A N     1 
ATOM   3766  C  CA    . TYR A 1 471 ? 135.909 126.422 85.452  1.00 21.95 ?  471 TYR A CA    1 
ATOM   3767  C  C     . TYR A 1 471 ? 136.980 125.509 84.868  1.00 25.73 ?  471 TYR A C     1 
ATOM   3768  O  O     . TYR A 1 471 ? 136.963 125.198 83.673  1.00 28.80 ?  471 TYR A O     1 
ATOM   3769  C  CB    . TYR A 1 471 ? 136.437 127.852 85.556  1.00 22.09 ?  471 TYR A CB    1 
ATOM   3770  C  CG    . TYR A 1 471 ? 137.062 128.330 84.268  1.00 19.48 ?  471 TYR A CG    1 
ATOM   3771  C  CD1   . TYR A 1 471 ? 136.271 128.782 83.221  1.00 23.38 ?  471 TYR A CD1   1 
ATOM   3772  C  CD2   . TYR A 1 471 ? 138.438 128.297 84.081  1.00 18.44 ?  471 TYR A CD2   1 
ATOM   3773  C  CE1   . TYR A 1 471 ? 136.830 129.207 82.036  1.00 25.73 ?  471 TYR A CE1   1 
ATOM   3774  C  CE2   . TYR A 1 471 ? 139.006 128.716 82.895  1.00 22.96 ?  471 TYR A CE2   1 
ATOM   3775  C  CZ    . TYR A 1 471 ? 138.196 129.172 81.878  1.00 25.21 ?  471 TYR A CZ    1 
ATOM   3776  O  OH    . TYR A 1 471 ? 138.753 129.591 80.695  1.00 31.66 ?  471 TYR A OH    1 
ATOM   3777  N  N     . LEU A 1 472 ? 137.937 125.086 85.698  1.00 27.82 ?  472 LEU A N     1 
ATOM   3778  C  CA    . LEU A 1 472 ? 139.018 124.235 85.208  1.00 24.74 ?  472 LEU A CA    1 
ATOM   3779  C  C     . LEU A 1 472 ? 138.501 122.867 84.776  1.00 27.35 ?  472 LEU A C     1 
ATOM   3780  O  O     . LEU A 1 472 ? 138.952 122.320 83.764  1.00 32.46 ?  472 LEU A O     1 
ATOM   3781  C  CB    . LEU A 1 472 ? 140.100 124.092 86.279  1.00 25.71 ?  472 LEU A CB    1 
ATOM   3782  C  CG    . LEU A 1 472 ? 140.890 125.355 86.624  1.00 24.59 ?  472 LEU A CG    1 
ATOM   3783  C  CD1   . LEU A 1 472 ? 141.682 125.160 87.906  1.00 23.05 ?  472 LEU A CD1   1 
ATOM   3784  C  CD2   . LEU A 1 472 ? 141.807 125.743 85.476  1.00 23.35 ?  472 LEU A CD2   1 
ATOM   3785  N  N     . ALA A 1 473 ? 137.562 122.296 85.533  1.00 26.73 ?  473 ALA A N     1 
ATOM   3786  C  CA    . ALA A 1 473 ? 137.039 120.977 85.203  1.00 24.56 ?  473 ALA A CA    1 
ATOM   3787  C  C     . ALA A 1 473 ? 136.164 121.019 83.956  1.00 35.21 ?  473 ALA A C     1 
ATOM   3788  O  O     . ALA A 1 473 ? 136.226 120.110 83.120  1.00 42.98 ?  473 ALA A O     1 
ATOM   3789  C  CB    . ALA A 1 473 ? 136.263 120.412 86.391  1.00 27.08 ?  473 ALA A CB    1 
ATOM   3790  N  N     . GLN A 1 474 ? 135.344 122.063 83.808  1.00 29.14 ?  474 GLN A N     1 
ATOM   3791  C  CA    . GLN A 1 474 ? 134.534 122.198 82.602  1.00 29.13 ?  474 GLN A CA    1 
ATOM   3792  C  C     . GLN A 1 474 ? 135.357 122.567 81.376  1.00 32.16 ?  474 GLN A C     1 
ATOM   3793  O  O     . GLN A 1 474 ? 134.817 122.560 80.265  1.00 36.34 ?  474 GLN A O     1 
ATOM   3794  C  CB    . GLN A 1 474 ? 133.428 123.232 82.810  1.00 28.84 ?  474 GLN A CB    1 
ATOM   3795  C  CG    . GLN A 1 474 ? 132.560 122.986 84.028  1.00 30.82 ?  474 GLN A CG    1 
ATOM   3796  C  CD    . GLN A 1 474 ? 131.170 123.561 83.874  1.00 32.74 ?  474 GLN A CD    1 
ATOM   3797  O  OE1   . GLN A 1 474 ? 130.573 123.491 82.800  1.00 37.49 ?  474 GLN A OE1   1 
ATOM   3798  N  NE2   . GLN A 1 474 ? 130.646 124.140 84.948  1.00 31.46 ?  474 GLN A NE2   1 
ATOM   3799  N  N     . ASN A 1 475 ? 136.640 122.891 81.544  1.00 33.08 ?  475 ASN A N     1 
ATOM   3800  C  CA    . ASN A 1 475 ? 137.529 123.184 80.430  1.00 35.90 ?  475 ASN A CA    1 
ATOM   3801  C  C     . ASN A 1 475 ? 138.591 122.107 80.243  1.00 35.04 ?  475 ASN A C     1 
ATOM   3802  O  O     . ASN A 1 475 ? 139.584 122.333 79.543  1.00 33.44 ?  475 ASN A O     1 
ATOM   3803  C  CB    . ASN A 1 475 ? 138.183 124.553 80.623  1.00 32.28 ?  475 ASN A CB    1 
ATOM   3804  C  CG    . ASN A 1 475 ? 137.226 125.694 80.355  1.00 31.54 ?  475 ASN A CG    1 
ATOM   3805  O  OD1   . ASN A 1 475 ? 137.111 126.171 79.226  1.00 33.91 ?  475 ASN A OD1   1 
ATOM   3806  N  ND2   . ASN A 1 475 ? 136.521 126.128 81.391  1.00 29.10 ?  475 ASN A ND2   1 
ATOM   3807  N  N     . GLY A 1 476 ? 138.397 120.941 80.850  1.00 29.82 ?  476 GLY A N     1 
ATOM   3808  C  CA    . GLY A 1 476 ? 139.339 119.842 80.697  1.00 29.15 ?  476 GLY A CA    1 
ATOM   3809  C  C     . GLY A 1 476 ? 140.711 120.117 81.271  1.00 35.07 ?  476 GLY A C     1 
ATOM   3810  O  O     . GLY A 1 476 ? 141.722 119.786 80.640  1.00 37.01 ?  476 GLY A O     1 
ATOM   3811  N  N     . ILE A 1 477 ? 140.772 120.720 82.455  1.00 31.50 ?  477 ILE A N     1 
ATOM   3812  C  CA    . ILE A 1 477 ? 142.031 121.036 83.116  1.00 26.83 ?  477 ILE A CA    1 
ATOM   3813  C  C     . ILE A 1 477 ? 141.982 120.499 84.539  1.00 31.18 ?  477 ILE A C     1 
ATOM   3814  O  O     . ILE A 1 477 ? 141.061 120.821 85.297  1.00 34.93 ?  477 ILE A O     1 
ATOM   3815  C  CB    . ILE A 1 477 ? 142.311 122.550 83.121  1.00 27.36 ?  477 ILE A CB    1 
ATOM   3816  C  CG1   . ILE A 1 477 ? 142.452 123.069 81.691  1.00 30.88 ?  477 ILE A CG1   1 
ATOM   3817  C  CG2   . ILE A 1 477 ? 143.565 122.854 83.917  1.00 28.51 ?  477 ILE A CG2   1 
ATOM   3818  C  CD1   . ILE A 1 477 ? 142.321 124.562 81.576  1.00 30.35 ?  477 ILE A CD1   1 
ATOM   3819  N  N     . ALA A 1 478 ? 142.969 119.684 84.897  1.00 31.04 ?  478 ALA A N     1 
ATOM   3820  C  CA    . ALA A 1 478 ? 143.065 119.177 86.257  1.00 27.78 ?  478 ALA A CA    1 
ATOM   3821  C  C     . ALA A 1 478 ? 143.504 120.288 87.203  1.00 30.47 ?  478 ALA A C     1 
ATOM   3822  O  O     . ALA A 1 478 ? 144.354 121.113 86.862  1.00 31.20 ?  478 ALA A O     1 
ATOM   3823  C  CB    . ALA A 1 478 ? 144.046 118.008 86.324  1.00 28.28 ?  478 ALA A CB    1 
ATOM   3824  N  N     . TYR A 1 479 ? 142.915 120.301 88.402  1.00 29.75 ?  479 TYR A N     1 
ATOM   3825  C  CA    . TYR A 1 479 ? 143.227 121.345 89.373  1.00 22.93 ?  479 TYR A CA    1 
ATOM   3826  C  C     . TYR A 1 479 ? 144.696 121.327 89.771  1.00 27.34 ?  479 TYR A C     1 
ATOM   3827  O  O     . TYR A 1 479 ? 145.276 122.382 90.051  1.00 33.22 ?  479 TYR A O     1 
ATOM   3828  C  CB    . TYR A 1 479 ? 142.335 121.186 90.605  1.00 21.32 ?  479 TYR A CB    1 
ATOM   3829  C  CG    . TYR A 1 479 ? 142.448 122.298 91.624  1.00 28.50 ?  479 TYR A CG    1 
ATOM   3830  C  CD1   . TYR A 1 479 ? 143.380 122.234 92.652  1.00 26.50 ?  479 TYR A CD1   1 
ATOM   3831  C  CD2   . TYR A 1 479 ? 141.611 123.403 91.568  1.00 22.04 ?  479 TYR A CD2   1 
ATOM   3832  C  CE1   . TYR A 1 479 ? 143.482 123.243 93.587  1.00 22.41 ?  479 TYR A CE1   1 
ATOM   3833  C  CE2   . TYR A 1 479 ? 141.705 124.417 92.500  1.00 22.90 ?  479 TYR A CE2   1 
ATOM   3834  C  CZ    . TYR A 1 479 ? 142.642 124.332 93.506  1.00 29.54 ?  479 TYR A CZ    1 
ATOM   3835  O  OH    . TYR A 1 479 ? 142.737 125.341 94.437  1.00 31.36 ?  479 TYR A OH    1 
ATOM   3836  N  N     . GLU A 1 480 ? 145.315 120.151 89.800  1.00 30.91 ?  480 GLU A N     1 
ATOM   3837  C  CA    . GLU A 1 480 ? 146.716 120.022 90.174  1.00 29.89 ?  480 GLU A CA    1 
ATOM   3838  C  C     . GLU A 1 480 ? 147.665 120.166 88.994  1.00 32.47 ?  480 GLU A C     1 
ATOM   3839  O  O     . GLU A 1 480 ? 148.884 120.120 89.190  1.00 37.66 ?  480 GLU A O     1 
ATOM   3840  C  CB    . GLU A 1 480 ? 146.956 118.673 90.853  1.00 29.48 ?  480 GLU A CB    1 
ATOM   3841  C  CG    . GLU A 1 480 ? 146.089 118.415 92.067  1.00 30.62 ?  480 GLU A CG    1 
ATOM   3842  C  CD    . GLU A 1 480 ? 145.866 116.937 92.304  1.00 37.66 ?  480 GLU A CD    1 
ATOM   3843  O  OE1   . GLU A 1 480 ? 145.002 116.348 91.622  1.00 38.85 ?  480 GLU A OE1   1 
ATOM   3844  O  OE2   . GLU A 1 480 ? 146.560 116.362 93.168  1.00 38.05 -1 480 GLU A OE2   1 
ATOM   3845  N  N     . SER A 1 481 ? 147.145 120.335 87.783  1.00 30.10 ?  481 SER A N     1 
ATOM   3846  C  CA    . SER A 1 481 ? 148.000 120.418 86.613  1.00 27.49 ?  481 SER A CA    1 
ATOM   3847  C  C     . SER A 1 481 ? 148.736 121.758 86.574  1.00 31.91 ?  481 SER A C     1 
ATOM   3848  O  O     . SER A 1 481 ? 148.245 122.761 87.099  1.00 32.24 ?  481 SER A O     1 
ATOM   3849  C  CB    . SER A 1 481 ? 147.179 120.242 85.340  1.00 29.10 ?  481 SER A CB    1 
ATOM   3850  O  OG    . SER A 1 481 ? 146.638 121.477 84.909  1.00 33.68 ?  481 SER A OG    1 
ATOM   3851  N  N     . PRO A 1 482 ? 149.925 121.795 85.967  1.00 37.78 ?  482 PRO A N     1 
ATOM   3852  C  CA    . PRO A 1 482 ? 150.604 123.088 85.778  1.00 30.91 ?  482 PRO A CA    1 
ATOM   3853  C  C     . PRO A 1 482 ? 149.808 124.060 84.928  1.00 29.86 ?  482 PRO A C     1 
ATOM   3854  O  O     . PRO A 1 482 ? 149.968 125.277 85.082  1.00 34.98 ?  482 PRO A O     1 
ATOM   3855  C  CB    . PRO A 1 482 ? 151.925 122.694 85.103  1.00 30.41 ?  482 PRO A CB    1 
ATOM   3856  C  CG    . PRO A 1 482 ? 152.120 121.257 85.448  1.00 32.89 ?  482 PRO A CG    1 
ATOM   3857  C  CD    . PRO A 1 482 ? 150.748 120.666 85.509  1.00 31.72 ?  482 PRO A CD    1 
ATOM   3858  N  N     . GLU A 1 483 ? 148.958 123.559 84.029  1.00 36.10 ?  483 GLU A N     1 
ATOM   3859  C  CA    . GLU A 1 483 ? 148.105 124.440 83.238  1.00 32.70 ?  483 GLU A CA    1 
ATOM   3860  C  C     . GLU A 1 483 ? 147.100 125.171 84.118  1.00 31.18 ?  483 GLU A C     1 
ATOM   3861  O  O     . GLU A 1 483 ? 146.799 126.347 83.882  1.00 35.55 ?  483 GLU A O     1 
ATOM   3862  C  CB    . GLU A 1 483 ? 147.384 123.639 82.154  1.00 33.67 ?  483 GLU A CB    1 
ATOM   3863  C  CG    . GLU A 1 483 ? 148.275 123.215 81.001  1.00 36.84 ?  483 GLU A CG    1 
ATOM   3864  C  CD    . GLU A 1 483 ? 148.972 121.893 81.254  1.00 39.71 ?  483 GLU A CD    1 
ATOM   3865  O  OE1   . GLU A 1 483 ? 148.971 121.429 82.413  1.00 37.12 ?  483 GLU A OE1   1 
ATOM   3866  O  OE2   . GLU A 1 483 ? 149.523 121.319 80.294  1.00 41.10 -1 483 GLU A OE2   1 
ATOM   3867  N  N     . ALA A 1 484 ? 146.561 124.488 85.131  1.00 26.19 ?  484 ALA A N     1 
ATOM   3868  C  CA    . ALA A 1 484 ? 145.645 125.144 86.057  1.00 25.77 ?  484 ALA A CA    1 
ATOM   3869  C  C     . ALA A 1 484 ? 146.338 126.267 86.816  1.00 25.99 ?  484 ALA A C     1 
ATOM   3870  O  O     . ALA A 1 484 ? 145.767 127.348 87.000  1.00 25.65 ?  484 ALA A O     1 
ATOM   3871  C  CB    . ALA A 1 484 ? 145.061 124.123 87.030  1.00 20.79 ?  484 ALA A CB    1 
ATOM   3872  N  N     . ARG A 1 485 ? 147.571 126.030 87.268  1.00 27.55 ?  485 ARG A N     1 
ATOM   3873  C  CA    . ARG A 1 485 ? 148.315 127.078 87.954  1.00 21.77 ?  485 ARG A CA    1 
ATOM   3874  C  C     . ARG A 1 485 ? 148.667 128.221 87.012  1.00 22.14 ?  485 ARG A C     1 
ATOM   3875  O  O     . ARG A 1 485 ? 148.661 129.383 87.426  1.00 30.74 ?  485 ARG A O     1 
ATOM   3876  C  CB    . ARG A 1 485 ? 149.578 126.501 88.589  1.00 24.49 ?  485 ARG A CB    1 
ATOM   3877  C  CG    . ARG A 1 485 ? 149.309 125.642 89.809  1.00 25.08 ?  485 ARG A CG    1 
ATOM   3878  C  CD    . ARG A 1 485 ? 150.596 125.289 90.526  1.00 26.67 ?  485 ARG A CD    1 
ATOM   3879  N  NE    . ARG A 1 485 ? 151.499 124.515 89.684  1.00 27.79 ?  485 ARG A NE    1 
ATOM   3880  C  CZ    . ARG A 1 485 ? 151.431 123.201 89.525  1.00 29.59 ?  485 ARG A CZ    1 
ATOM   3881  N  NH1   . ARG A 1 485 ? 150.503 122.479 90.130  1.00 27.74 1  485 ARG A NH1   1 
ATOM   3882  N  NH2   . ARG A 1 485 ? 152.317 122.597 88.739  1.00 25.12 ?  485 ARG A NH2   1 
ATOM   3883  N  N     . ASP A 1 486 ? 148.976 127.914 85.752  1.00 29.60 ?  486 ASP A N     1 
ATOM   3884  C  CA    . ASP A 1 486 ? 149.215 128.960 84.763  1.00 28.93 ?  486 ASP A CA    1 
ATOM   3885  C  C     . ASP A 1 486 ? 147.973 129.823 84.569  1.00 29.97 ?  486 ASP A C     1 
ATOM   3886  O  O     . ASP A 1 486 ? 148.056 131.060 84.526  1.00 35.68 ?  486 ASP A O     1 
ATOM   3887  C  CB    . ASP A 1 486 ? 149.647 128.324 83.443  1.00 33.99 ?  486 ASP A CB    1 
ATOM   3888  C  CG    . ASP A 1 486 ? 150.097 129.343 82.424  1.00 39.53 ?  486 ASP A CG    1 
ATOM   3889  O  OD1   . ASP A 1 486 ? 151.027 130.121 82.725  1.00 38.33 ?  486 ASP A OD1   1 
ATOM   3890  O  OD2   . ASP A 1 486 ? 149.521 129.359 81.317  1.00 40.45 -1 486 ASP A OD2   1 
ATOM   3891  N  N     . PHE A 1 487 ? 146.808 129.183 84.455  1.00 27.52 ?  487 PHE A N     1 
ATOM   3892  C  CA    . PHE A 1 487 ? 145.569 129.937 84.322  1.00 24.06 ?  487 PHE A CA    1 
ATOM   3893  C  C     . PHE A 1 487 ? 145.301 130.783 85.555  1.00 23.48 ?  487 PHE A C     1 
ATOM   3894  O  O     . PHE A 1 487 ? 144.875 131.934 85.440  1.00 28.50 ?  487 PHE A O     1 
ATOM   3895  C  CB    . PHE A 1 487 ? 144.382 129.010 84.074  1.00 23.47 ?  487 PHE A CB    1 
ATOM   3896  C  CG    . PHE A 1 487 ? 143.061 129.673 84.328  1.00 24.82 ?  487 PHE A CG    1 
ATOM   3897  C  CD1   . PHE A 1 487 ? 142.530 130.553 83.402  1.00 22.38 ?  487 PHE A CD1   1 
ATOM   3898  C  CD2   . PHE A 1 487 ? 142.369 129.450 85.508  1.00 24.88 ?  487 PHE A CD2   1 
ATOM   3899  C  CE1   . PHE A 1 487 ? 141.328 131.183 83.637  1.00 24.63 ?  487 PHE A CE1   1 
ATOM   3900  C  CE2   . PHE A 1 487 ? 141.167 130.079 85.746  1.00 25.98 ?  487 PHE A CE2   1 
ATOM   3901  C  CZ    . PHE A 1 487 ? 140.646 130.947 84.809  1.00 24.61 ?  487 PHE A CZ    1 
ATOM   3902  N  N     . ALA A 1 488 ? 145.503 130.216 86.746  1.00 20.43 ?  488 ALA A N     1 
ATOM   3903  C  CA    . ALA A 1 488 ? 145.275 130.980 87.965  1.00 16.31 ?  488 ALA A CA    1 
ATOM   3904  C  C     . ALA A 1 488 ? 146.206 132.180 88.033  1.00 23.39 ?  488 ALA A C     1 
ATOM   3905  O  O     . ALA A 1 488 ? 145.777 133.291 88.366  1.00 28.14 ?  488 ALA A O     1 
ATOM   3906  C  CB    . ALA A 1 488 ? 145.457 130.085 89.190  1.00 22.74 ?  488 ALA A CB    1 
ATOM   3907  N  N     . ASN A 1 489 ? 147.479 131.979 87.687  1.00 25.91 ?  489 ASN A N     1 
ATOM   3908  C  CA    . ASN A 1 489 ? 148.436 133.076 87.657  1.00 21.39 ?  489 ASN A CA    1 
ATOM   3909  C  C     . ASN A 1 489 ? 147.958 134.191 86.740  1.00 20.60 ?  489 ASN A C     1 
ATOM   3910  O  O     . ASN A 1 489 ? 147.862 135.351 87.154  1.00 23.98 ?  489 ASN A O     1 
ATOM   3911  C  CB    . ASN A 1 489 ? 149.801 132.556 87.203  1.00 17.63 ?  489 ASN A CB    1 
ATOM   3912  C  CG    . ASN A 1 489 ? 150.897 133.584 87.348  1.00 25.69 ?  489 ASN A CG    1 
ATOM   3913  O  OD1   . ASN A 1 489 ? 150.993 134.268 88.365  1.00 31.29 ?  489 ASN A OD1   1 
ATOM   3914  N  ND2   . ASN A 1 489 ? 151.740 133.694 86.329  1.00 28.39 ?  489 ASN A ND2   1 
ATOM   3915  N  N     . THR A 1 490 ? 147.620 133.850 85.495  1.00 22.74 ?  490 THR A N     1 
ATOM   3916  C  CA    . THR A 1 490 ? 147.216 134.880 84.543  1.00 21.31 ?  490 THR A CA    1 
ATOM   3917  C  C     . THR A 1 490 ? 145.921 135.560 84.975  1.00 22.67 ?  490 THR A C     1 
ATOM   3918  O  O     . THR A 1 490 ? 145.829 136.794 84.985  1.00 24.89 ?  490 THR A O     1 
ATOM   3919  C  CB    . THR A 1 490 ? 147.067 134.284 83.145  1.00 28.93 ?  490 THR A CB    1 
ATOM   3920  O  OG1   . THR A 1 490 ? 148.254 133.556 82.807  1.00 33.78 ?  490 THR A OG1   1 
ATOM   3921  C  CG2   . THR A 1 490 ? 146.844 135.388 82.125  1.00 22.59 ?  490 THR A CG2   1 
ATOM   3922  N  N     . PHE A 1 491 ? 144.913 134.769 85.346  1.00 19.82 ?  491 PHE A N     1 
ATOM   3923  C  CA    . PHE A 1 491 ? 143.604 135.319 85.683  1.00 17.95 ?  491 PHE A CA    1 
ATOM   3924  C  C     . PHE A 1 491 ? 143.692 136.244 86.885  1.00 22.82 ?  491 PHE A C     1 
ATOM   3925  O  O     . PHE A 1 491 ? 143.142 137.350 86.872  1.00 22.93 ?  491 PHE A O     1 
ATOM   3926  C  CB    . PHE A 1 491 ? 142.616 134.180 85.946  1.00 22.92 ?  491 PHE A CB    1 
ATOM   3927  C  CG    . PHE A 1 491 ? 141.277 134.641 86.455  1.00 19.23 ?  491 PHE A CG    1 
ATOM   3928  C  CD1   . PHE A 1 491 ? 140.275 134.998 85.573  1.00 17.23 ?  491 PHE A CD1   1 
ATOM   3929  C  CD2   . PHE A 1 491 ? 141.019 134.709 87.816  1.00 17.98 ?  491 PHE A CD2   1 
ATOM   3930  C  CE1   . PHE A 1 491 ? 139.046 135.424 86.032  1.00 15.75 ?  491 PHE A CE1   1 
ATOM   3931  C  CE2   . PHE A 1 491 ? 139.793 135.134 88.281  1.00 17.31 ?  491 PHE A CE2   1 
ATOM   3932  C  CZ    . PHE A 1 491 ? 138.804 135.492 87.387  1.00 19.56 ?  491 PHE A CZ    1 
ATOM   3933  N  N     . PHE A 1 492 ? 144.394 135.819 87.935  1.00 23.17 ?  492 PHE A N     1 
ATOM   3934  C  CA    . PHE A 1 492 ? 144.475 136.650 89.123  1.00 12.41 ?  492 PHE A CA    1 
ATOM   3935  C  C     . PHE A 1 492 ? 145.446 137.809 88.960  1.00 14.90 ?  492 PHE A C     1 
ATOM   3936  O  O     . PHE A 1 492 ? 145.275 138.829 89.630  1.00 20.08 ?  492 PHE A O     1 
ATOM   3937  C  CB    . PHE A 1 492 ? 144.838 135.789 90.331  1.00 19.66 ?  492 PHE A CB    1 
ATOM   3938  C  CG    . PHE A 1 492 ? 143.690 134.962 90.833  1.00 16.33 ?  492 PHE A CG    1 
ATOM   3939  C  CD1   . PHE A 1 492 ? 142.699 135.537 91.608  1.00 11.74 ?  492 PHE A CD1   1 
ATOM   3940  C  CD2   . PHE A 1 492 ? 143.582 133.623 90.504  1.00 16.15 ?  492 PHE A CD2   1 
ATOM   3941  C  CE1   . PHE A 1 492 ? 141.635 134.787 92.063  1.00 12.40 ?  492 PHE A CE1   1 
ATOM   3942  C  CE2   . PHE A 1 492 ? 142.518 132.866 90.956  1.00 14.11 ?  492 PHE A CE2   1 
ATOM   3943  C  CZ    . PHE A 1 492 ? 141.544 133.450 91.737  1.00 16.69 ?  492 PHE A CZ    1 
ATOM   3944  N  N     . MET A 1 493 ? 146.422 137.714 88.052  1.00 19.05 ?  493 MET A N     1 
ATOM   3945  C  CA    . MET A 1 493 ? 147.210 138.898 87.738  1.00 16.78 ?  493 MET A CA    1 
ATOM   3946  C  C     . MET A 1 493 ? 146.353 139.935 87.028  1.00 16.20 ?  493 MET A C     1 
ATOM   3947  O  O     . MET A 1 493 ? 146.463 141.131 87.313  1.00 22.30 ?  493 MET A O     1 
ATOM   3948  C  CB    . MET A 1 493 ? 148.448 138.503 86.919  1.00 17.19 ?  493 MET A CB    1 
ATOM   3949  C  CG    . MET A 1 493 ? 149.155 139.577 86.054  1.00 17.53 ?  493 MET A CG    1 
ATOM   3950  S  SD    . MET A 1 493 ? 148.285 140.503 84.767  1.00 32.83 ?  493 MET A SD    1 
ATOM   3951  C  CE    . MET A 1 493 ? 148.252 139.282 83.464  1.00 21.93 ?  493 MET A CE    1 
ATOM   3952  N  N     . MET A 1 494 ? 145.488 139.503 86.102  1.00 20.52 ?  494 MET A N     1 
ATOM   3953  C  CA    . MET A 1 494 ? 144.562 140.451 85.483  1.00 19.50 ?  494 MET A CA    1 
ATOM   3954  C  C     . MET A 1 494 ? 143.585 141.022 86.503  1.00 21.79 ?  494 MET A C     1 
ATOM   3955  O  O     . MET A 1 494 ? 143.249 142.212 86.451  1.00 24.82 ?  494 MET A O     1 
ATOM   3956  C  CB    . MET A 1 494 ? 143.796 139.800 84.328  1.00 17.94 ?  494 MET A CB    1 
ATOM   3957  C  CG    . MET A 1 494 ? 144.639 138.991 83.367  1.00 22.98 ?  494 MET A CG    1 
ATOM   3958  S  SD    . MET A 1 494 ? 143.830 138.689 81.785  1.00 39.60 ?  494 MET A SD    1 
ATOM   3959  C  CE    . MET A 1 494 ? 142.665 140.047 81.726  1.00 24.17 ?  494 MET A CE    1 
ATOM   3960  N  N     . VAL A 1 495 ? 143.108 140.189 87.430  1.00 19.25 ?  495 VAL A N     1 
ATOM   3961  C  CA    . VAL A 1 495 ? 142.204 140.674 88.469  1.00 14.86 ?  495 VAL A CA    1 
ATOM   3962  C  C     . VAL A 1 495 ? 142.894 141.734 89.316  1.00 21.00 ?  495 VAL A C     1 
ATOM   3963  O  O     . VAL A 1 495 ? 142.321 142.790 89.604  1.00 32.06 ?  495 VAL A O     1 
ATOM   3964  C  CB    . VAL A 1 495 ? 141.695 139.505 89.332  1.00 19.73 ?  495 VAL A CB    1 
ATOM   3965  C  CG1   . VAL A 1 495 ? 140.999 140.029 90.578  1.00 13.65 ?  495 VAL A CG1   1 
ATOM   3966  C  CG2   . VAL A 1 495 ? 140.750 138.629 88.534  1.00 14.21 ?  495 VAL A CG2   1 
ATOM   3967  N  N     . ASN A 1 496 ? 144.141 141.474 89.718  1.00 18.39 ?  496 ASN A N     1 
ATOM   3968  C  CA    . ASN A 1 496 ? 144.898 142.455 90.487  1.00 11.72 ?  496 ASN A CA    1 
ATOM   3969  C  C     . ASN A 1 496 ? 145.137 143.725 89.682  1.00 16.27 ?  496 ASN A C     1 
ATOM   3970  O  O     . ASN A 1 496 ? 145.025 144.834 90.214  1.00 26.76 ?  496 ASN A O     1 
ATOM   3971  C  CB    . ASN A 1 496 ? 146.226 141.848 90.939  1.00 17.45 ?  496 ASN A CB    1 
ATOM   3972  C  CG    . ASN A 1 496 ? 146.846 142.600 92.097  1.00 18.49 ?  496 ASN A CG    1 
ATOM   3973  O  OD1   . ASN A 1 496 ? 146.144 143.198 92.909  1.00 24.08 ?  496 ASN A OD1   1 
ATOM   3974  N  ND2   . ASN A 1 496 ? 148.168 142.573 92.177  1.00 18.71 ?  496 ASN A ND2   1 
ATOM   3975  N  N     . PHE A 1 497 ? 145.463 143.582 88.396  1.00 18.94 ?  497 PHE A N     1 
ATOM   3976  C  CA    . PHE A 1 497 ? 145.712 144.742 87.549  1.00 14.12 ?  497 PHE A CA    1 
ATOM   3977  C  C     . PHE A 1 497 ? 144.480 145.631 87.467  1.00 19.38 ?  497 PHE A C     1 
ATOM   3978  O  O     . PHE A 1 497 ? 144.561 146.847 87.670  1.00 24.23 ?  497 PHE A O     1 
ATOM   3979  C  CB    . PHE A 1 497 ? 146.141 144.280 86.154  1.00 17.00 ?  497 PHE A CB    1 
ATOM   3980  C  CG    . PHE A 1 497 ? 146.420 145.403 85.194  1.00 20.91 ?  497 PHE A CG    1 
ATOM   3981  C  CD1   . PHE A 1 497 ? 145.409 145.926 84.404  1.00 20.09 ?  497 PHE A CD1   1 
ATOM   3982  C  CD2   . PHE A 1 497 ? 147.696 145.924 85.068  1.00 25.45 ?  497 PHE A CD2   1 
ATOM   3983  C  CE1   . PHE A 1 497 ? 145.664 146.955 83.521  1.00 22.74 ?  497 PHE A CE1   1 
ATOM   3984  C  CE2   . PHE A 1 497 ? 147.955 146.953 84.185  1.00 23.32 ?  497 PHE A CE2   1 
ATOM   3985  C  CZ    . PHE A 1 497 ? 146.938 147.468 83.410  1.00 22.22 ?  497 PHE A CZ    1 
ATOM   3986  N  N     . TYR A 1 498 ? 143.322 145.035 87.187  1.00 25.25 ?  498 TYR A N     1 
ATOM   3987  C  CA    . TYR A 1 498 ? 142.116 145.838 87.028  1.00 18.22 ?  498 TYR A CA    1 
ATOM   3988  C  C     . TYR A 1 498 ? 141.592 146.341 88.367  1.00 23.26 ?  498 TYR A C     1 
ATOM   3989  O  O     . TYR A 1 498 ? 140.993 147.417 88.423  1.00 29.58 ?  498 TYR A O     1 
ATOM   3990  C  CB    . TYR A 1 498 ? 141.053 145.041 86.276  1.00 19.42 ?  498 TYR A CB    1 
ATOM   3991  C  CG    . TYR A 1 498 ? 141.433 144.806 84.834  1.00 22.71 ?  498 TYR A CG    1 
ATOM   3992  C  CD1   . TYR A 1 498 ? 141.737 145.873 83.998  1.00 23.96 ?  498 TYR A CD1   1 
ATOM   3993  C  CD2   . TYR A 1 498 ? 141.512 143.523 84.313  1.00 23.81 ?  498 TYR A CD2   1 
ATOM   3994  C  CE1   . TYR A 1 498 ? 142.096 145.668 82.681  1.00 19.02 ?  498 TYR A CE1   1 
ATOM   3995  C  CE2   . TYR A 1 498 ? 141.870 143.308 82.998  1.00 26.18 ?  498 TYR A CE2   1 
ATOM   3996  C  CZ    . TYR A 1 498 ? 142.160 144.384 82.186  1.00 27.69 ?  498 TYR A CZ    1 
ATOM   3997  O  OH    . TYR A 1 498 ? 142.516 144.174 80.874  1.00 33.10 ?  498 TYR A OH    1 
ATOM   3998  N  N     . SER A 1 499 ? 141.840 145.609 89.455  1.00 21.40 ?  499 SER A N     1 
ATOM   3999  C  CA    . SER A 1 499 ? 141.476 146.106 90.777  1.00 7.93  ?  499 SER A CA    1 
ATOM   4000  C  C     . SER A 1 499 ? 142.310 147.325 91.149  1.00 13.95 ?  499 SER A C     1 
ATOM   4001  O  O     . SER A 1 499 ? 141.781 148.321 91.656  1.00 20.78 ?  499 SER A O     1 
ATOM   4002  C  CB    . SER A 1 499 ? 141.641 144.996 91.814  1.00 10.95 ?  499 SER A CB    1 
ATOM   4003  O  OG    . SER A 1 499 ? 140.883 145.265 92.978  1.00 23.91 ?  499 SER A OG    1 
ATOM   4004  N  N     . ILE A 1 500 ? 143.619 147.270 90.890  1.00 13.96 ?  500 ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 500 ? 144.481 148.419 91.145  1.00 17.91 ?  500 ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 500 ? 144.091 149.585 90.248  1.00 18.43 ?  500 ILE A C     1 
ATOM   4007  O  O     . ILE A 1 500 ? 144.069 150.741 90.685  1.00 27.23 ?  500 ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 500 ? 145.960 148.032 90.958  1.00 20.89 ?  500 ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 500 ? 146.400 147.053 92.042  1.00 17.96 ?  500 ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 500 ? 146.843 149.262 90.993  1.00 14.38 ?  500 ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 500 ? 147.656 146.295 91.696  1.00 17.65 ?  500 ILE A CD1   1 
ATOM   4012  N  N     . GLN A 1 501 ? 143.779 149.303 88.982  1.00 21.74 ?  501 GLN A N     1 
ATOM   4013  C  CA    . GLN A 1 501 ? 143.373 150.361 88.066  1.00 21.17 ?  501 GLN A CA    1 
ATOM   4014  C  C     . GLN A 1 501 ? 142.084 151.026 88.526  1.00 23.95 ?  501 GLN A C     1 
ATOM   4015  O  O     . GLN A 1 501 ? 141.971 152.255 88.499  1.00 33.02 ?  501 GLN A O     1 
ATOM   4016  C  CB    . GLN A 1 501 ? 143.217 149.798 86.654  1.00 26.40 ?  501 GLN A CB    1 
ATOM   4017  C  CG    . GLN A 1 501 ? 143.549 150.787 85.552  1.00 26.12 ?  501 GLN A CG    1 
ATOM   4018  C  CD    . GLN A 1 501 ? 143.362 150.200 84.170  1.00 29.50 ?  501 GLN A CD    1 
ATOM   4019  O  OE1   . GLN A 1 501 ? 142.309 149.644 83.857  1.00 30.35 ?  501 GLN A OE1   1 
ATOM   4020  N  NE2   . GLN A 1 501 ? 144.386 150.317 83.334  1.00 31.13 ?  501 GLN A NE2   1 
ATOM   4021  N  N     . ARG A 1 502 ? 141.103 150.233 88.963  1.00 22.64 ?  502 ARG A N     1 
ATOM   4022  C  CA    . ARG A 1 502 ? 139.852 150.802 89.452  1.00 21.00 ?  502 ARG A CA    1 
ATOM   4023  C  C     . ARG A 1 502 ? 140.066 151.587 90.740  1.00 21.54 ?  502 ARG A C     1 
ATOM   4024  O  O     . ARG A 1 502 ? 139.456 152.643 90.933  1.00 25.89 ?  502 ARG A O     1 
ATOM   4025  C  CB    . ARG A 1 502 ? 138.818 149.698 89.662  1.00 19.91 ?  502 ARG A CB    1 
ATOM   4026  C  CG    . ARG A 1 502 ? 137.412 150.218 89.891  1.00 22.74 ?  502 ARG A CG    1 
ATOM   4027  C  CD    . ARG A 1 502 ? 136.991 151.168 88.785  1.00 23.43 ?  502 ARG A CD    1 
ATOM   4028  N  NE    . ARG A 1 502 ? 135.920 152.059 89.212  1.00 26.60 ?  502 ARG A NE    1 
ATOM   4029  C  CZ    . ARG A 1 502 ? 135.783 153.314 88.808  1.00 25.59 ?  502 ARG A CZ    1 
ATOM   4030  N  NH1   . ARG A 1 502 ? 136.629 153.860 87.950  1.00 29.04 1  502 ARG A NH1   1 
ATOM   4031  N  NH2   . ARG A 1 502 ? 134.772 154.039 89.275  1.00 26.36 ?  502 ARG A NH2   1 
ATOM   4032  N  N     . SER A 1 503 ? 140.920 151.087 91.637  1.00 19.21 ?  503 SER A N     1 
ATOM   4033  C  CA    . SER A 1 503 ? 141.211 151.821 92.865  1.00 20.41 ?  503 SER A CA    1 
ATOM   4034  C  C     . SER A 1 503 ? 141.864 153.162 92.559  1.00 23.19 ?  503 SER A C     1 
ATOM   4035  O  O     . SER A 1 503 ? 141.502 154.188 93.147  1.00 26.02 ?  503 SER A O     1 
ATOM   4036  C  CB    . SER A 1 503 ? 142.108 150.979 93.773  1.00 19.03 ?  503 SER A CB    1 
ATOM   4037  O  OG    . SER A 1 503 ? 142.067 151.443 95.110  1.00 23.30 ?  503 SER A OG    1 
ATOM   4038  N  N     . ALA A 1 504 ? 142.814 153.178 91.623  1.00 24.12 ?  504 ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 504 ? 143.465 154.426 91.243  1.00 21.09 ?  504 ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 504 ? 142.494 155.366 90.539  1.00 28.52 ?  504 ALA A C     1 
ATOM   4041  O  O     . ALA A 1 504 ? 142.552 156.585 90.733  1.00 37.22 ?  504 ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 504 ? 144.674 154.136 90.356  1.00 24.49 ?  504 ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 505 ? 141.591 154.820 89.723  1.00 26.33 ?  505 GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 505 ? 140.592 155.649 89.059  1.00 26.93 ?  505 GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 505 ? 139.633 156.272 90.065  1.00 29.67 ?  505 GLU A C     1 
ATOM   4046  O  O     . GLU A 1 505 ? 139.265 157.443 89.934  1.00 35.60 ?  505 GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 505 ? 139.826 154.822 88.027  1.00 26.49 ?  505 GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 505 ? 140.601 154.543 86.750  1.00 27.33 ?  505 GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 505 ? 140.132 153.284 86.047  1.00 33.62 ?  505 GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 505 ? 139.185 152.641 86.546  1.00 34.56 ?  505 GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 505 ? 140.711 152.937 84.997  1.00 35.30 -1 505 GLU A OE2   1 
ATOM   4052  N  N     . ILE A 1 506 ? 139.218 155.506 91.074  1.00 26.44 ?  506 ILE A N     1 
ATOM   4053  C  CA    . ILE A 1 506 ? 138.353 156.049 92.116  1.00 24.78 ?  506 ILE A CA    1 
ATOM   4054  C  C     . ILE A 1 506 ? 139.091 157.111 92.921  1.00 28.62 ?  506 ILE A C     1 
ATOM   4055  O  O     . ILE A 1 506 ? 138.518 158.146 93.280  1.00 34.21 ?  506 ILE A O     1 
ATOM   4056  C  CB    . ILE A 1 506 ? 137.821 154.916 93.014  1.00 23.01 ?  506 ILE A CB    1 
ATOM   4057  C  CG1   . ILE A 1 506 ? 136.900 153.992 92.218  1.00 26.55 ?  506 ILE A CG1   1 
ATOM   4058  C  CG2   . ILE A 1 506 ? 137.081 155.483 94.214  1.00 23.61 ?  506 ILE A CG2   1 
ATOM   4059  C  CD1   . ILE A 1 506 ? 136.614 152.677 92.905  1.00 21.55 ?  506 ILE A CD1   1 
ATOM   4060  N  N     . ALA A 1 507 ? 140.373 156.877 93.214  1.00 30.57 ?  507 ALA A N     1 
ATOM   4061  C  CA    . ALA A 1 507 ? 141.165 157.881 93.918  1.00 28.17 ?  507 ALA A CA    1 
ATOM   4062  C  C     . ALA A 1 507 ? 141.276 159.166 93.107  1.00 30.16 ?  507 ALA A C     1 
ATOM   4063  O  O     . ALA A 1 507 ? 141.185 160.268 93.660  1.00 33.75 ?  507 ALA A O     1 
ATOM   4064  C  CB    . ALA A 1 507 ? 142.553 157.326 94.235  1.00 24.00 ?  507 ALA A CB    1 
ATOM   4065  N  N     . LYS A 1 508 ? 141.481 159.044 91.795  1.00 34.66 ?  508 LYS A N     1 
ATOM   4066  C  CA    . LYS A 1 508 ? 141.559 160.221 90.935  1.00 32.34 ?  508 LYS A CA    1 
ATOM   4067  C  C     . LYS A 1 508 ? 140.221 160.948 90.862  1.00 37.17 ?  508 LYS A C     1 
ATOM   4068  O  O     . LYS A 1 508 ? 140.176 162.183 90.908  1.00 43.61 ?  508 LYS A O     1 
ATOM   4069  C  CB    . LYS A 1 508 ? 142.028 159.810 89.539  1.00 34.75 ?  508 LYS A CB    1 
ATOM   4070  C  CG    . LYS A 1 508 ? 141.899 160.896 88.488  1.00 36.97 ?  508 LYS A CG    1 
ATOM   4071  C  CD    . LYS A 1 508 ? 142.104 160.332 87.093  1.00 38.51 ?  508 LYS A CD    1 
ATOM   4072  C  CE    . LYS A 1 508 ? 142.017 161.421 86.038  1.00 37.16 ?  508 LYS A CE    1 
ATOM   4073  N  NZ    . LYS A 1 508 ? 142.895 161.135 84.870  1.00 40.86 1  508 LYS A NZ    1 
ATOM   4074  N  N     . GLU A 1 509 ? 139.121 160.200 90.744  1.00 35.71 ?  509 GLU A N     1 
ATOM   4075  C  CA    . GLU A 1 509 ? 137.803 160.818 90.636  1.00 34.30 ?  509 GLU A CA    1 
ATOM   4076  C  C     . GLU A 1 509 ? 137.428 161.547 91.920  1.00 37.22 ?  509 GLU A C     1 
ATOM   4077  O  O     . GLU A 1 509 ? 137.013 162.712 91.886  1.00 41.97 ?  509 GLU A O     1 
ATOM   4078  C  CB    . GLU A 1 509 ? 136.755 159.758 90.296  1.00 33.13 ?  509 GLU A CB    1 
ATOM   4079  C  CG    . GLU A 1 509 ? 136.822 159.253 88.865  1.00 40.38 ?  509 GLU A CG    1 
ATOM   4080  C  CD    . GLU A 1 509 ? 136.315 157.830 88.726  1.00 43.69 ?  509 GLU A CD    1 
ATOM   4081  O  OE1   . GLU A 1 509 ? 135.734 157.305 89.700  1.00 42.01 ?  509 GLU A OE1   1 
ATOM   4082  O  OE2   . GLU A 1 509 ? 136.499 157.235 87.643  1.00 40.06 -1 509 GLU A OE2   1 
ATOM   4083  N  N     . LYS A 1 510 ? 137.568 160.878 93.062  1.00 33.73 ?  510 LYS A N     1 
ATOM   4084  C  CA    . LYS A 1 510 ? 137.230 161.481 94.344  1.00 30.44 ?  510 LYS A CA    1 
ATOM   4085  C  C     . LYS A 1 510 ? 138.327 162.388 94.882  1.00 32.19 ?  510 LYS A C     1 
ATOM   4086  O  O     . LYS A 1 510 ? 138.076 163.137 95.832  1.00 38.71 ?  510 LYS A O     1 
ATOM   4087  C  CB    . LYS A 1 510 ? 136.914 160.388 95.368  1.00 29.73 ?  510 LYS A CB    1 
ATOM   4088  C  CG    . LYS A 1 510 ? 135.838 159.416 94.916  1.00 29.83 ?  510 LYS A CG    1 
ATOM   4089  C  CD    . LYS A 1 510 ? 135.482 158.432 96.014  1.00 30.57 ?  510 LYS A CD    1 
ATOM   4090  C  CE    . LYS A 1 510 ? 134.016 158.036 95.946  1.00 35.93 ?  510 LYS A CE    1 
ATOM   4091  N  NZ    . LYS A 1 510 ? 133.828 156.566 96.082  1.00 35.29 1  510 LYS A NZ    1 
ATOM   4092  N  N     . GLY A 1 511 ? 139.526 162.340 94.307  1.00 31.46 ?  511 GLY A N     1 
ATOM   4093  C  CA    . GLY A 1 511 ? 140.609 163.181 94.769  1.00 28.76 ?  511 GLY A CA    1 
ATOM   4094  C  C     . GLY A 1 511 ? 141.223 162.771 96.085  1.00 36.85 ?  511 GLY A C     1 
ATOM   4095  O  O     . GLY A 1 511 ? 141.991 163.547 96.662  1.00 40.96 ?  511 GLY A O     1 
ATOM   4096  N  N     . GLU A 1 512 ? 140.911 161.576 96.582  1.00 29.37 ?  512 GLU A N     1 
ATOM   4097  C  CA    . GLU A 1 512 ? 141.411 161.121 97.870  1.00 27.23 ?  512 GLU A CA    1 
ATOM   4098  C  C     . GLU A 1 512 ? 141.853 159.669 97.769  1.00 29.79 ?  512 GLU A C     1 
ATOM   4099  O  O     . GLU A 1 512 ? 141.258 158.869 97.044  1.00 29.31 ?  512 GLU A O     1 
ATOM   4100  C  CB    . GLU A 1 512 ? 140.348 161.266 98.968  1.00 29.38 ?  512 GLU A CB    1 
ATOM   4101  C  CG    . GLU A 1 512 ? 139.037 160.567 98.657  1.00 31.17 ?  512 GLU A CG    1 
ATOM   4102  C  CD    . GLU A 1 512 ? 138.243 160.235 99.903  1.00 33.54 ?  512 GLU A CD    1 
ATOM   4103  O  OE1   . GLU A 1 512 ? 138.866 160.017 100.963 1.00 31.95 ?  512 GLU A OE1   1 
ATOM   4104  O  OE2   . GLU A 1 512 ? 136.998 160.190 99.824  1.00 30.20 -1 512 GLU A OE2   1 
ATOM   4105  N  N     . THR A 1 513 ? 142.908 159.343 98.506  1.00 31.54 ?  513 THR A N     1 
ATOM   4106  C  CA    . THR A 1 513 ? 143.403 157.986 98.659  1.00 24.41 ?  513 THR A CA    1 
ATOM   4107  C  C     . THR A 1 513 ? 143.043 157.485 100.056 1.00 26.94 ?  513 THR A C     1 
ATOM   4108  O  O     . THR A 1 513 ? 142.364 158.172 100.827 1.00 31.85 ?  513 THR A O     1 
ATOM   4109  C  CB    . THR A 1 513 ? 144.910 157.942 98.407  1.00 26.12 ?  513 THR A CB    1 
ATOM   4110  O  OG1   . THR A 1 513 ? 145.596 158.539 99.513  1.00 35.94 ?  513 THR A OG1   1 
ATOM   4111  C  CG2   . THR A 1 513 ? 145.256 158.702 97.139  1.00 25.68 ?  513 THR A CG2   1 
ATOM   4112  N  N     . PHE A 1 514 ? 143.497 156.282 100.388 1.00 23.23 ?  514 PHE A N     1 
ATOM   4113  C  CA    . PHE A 1 514 ? 143.308 155.792 101.742 1.00 23.53 ?  514 PHE A CA    1 
ATOM   4114  C  C     . PHE A 1 514 ? 144.336 156.424 102.670 1.00 19.94 ?  514 PHE A C     1 
ATOM   4115  O  O     . PHE A 1 514 ? 145.404 156.867 102.237 1.00 28.21 ?  514 PHE A O     1 
ATOM   4116  C  CB    . PHE A 1 514 ? 143.388 154.264 101.800 1.00 16.82 ?  514 PHE A CB    1 
ATOM   4117  C  CG    . PHE A 1 514 ? 144.735 153.696 101.445 1.00 18.74 ?  514 PHE A CG    1 
ATOM   4118  C  CD1   . PHE A 1 514 ? 145.056 153.408 100.131 1.00 18.81 ?  514 PHE A CD1   1 
ATOM   4119  C  CD2   . PHE A 1 514 ? 145.665 153.415 102.432 1.00 19.05 ?  514 PHE A CD2   1 
ATOM   4120  C  CE1   . PHE A 1 514 ? 146.285 152.871 99.807  1.00 12.80 ?  514 PHE A CE1   1 
ATOM   4121  C  CE2   . PHE A 1 514 ? 146.894 152.880 102.112 1.00 16.19 ?  514 PHE A CE2   1 
ATOM   4122  C  CZ    . PHE A 1 514 ? 147.205 152.608 100.797 1.00 15.17 ?  514 PHE A CZ    1 
ATOM   4123  N  N     . ASP A 1 515 ? 143.993 156.486 103.954 1.00 22.86 ?  515 ASP A N     1 
ATOM   4124  C  CA    . ASP A 1 515 ? 144.856 157.147 104.922 1.00 26.17 ?  515 ASP A CA    1 
ATOM   4125  C  C     . ASP A 1 515 ? 146.215 156.461 104.988 1.00 27.64 ?  515 ASP A C     1 
ATOM   4126  O  O     . ASP A 1 515 ? 146.311 155.231 104.979 1.00 32.62 ?  515 ASP A O     1 
ATOM   4127  C  CB    . ASP A 1 515 ? 144.199 157.157 106.302 1.00 27.91 ?  515 ASP A CB    1 
ATOM   4128  C  CG    . ASP A 1 515 ? 143.094 158.188 106.410 1.00 30.13 ?  515 ASP A CG    1 
ATOM   4129  O  OD1   . ASP A 1 515 ? 142.572 158.616 105.359 1.00 30.97 ?  515 ASP A OD1   1 
ATOM   4130  O  OD2   . ASP A 1 515 ? 142.747 158.574 107.546 1.00 31.63 -1 515 ASP A OD2   1 
ATOM   4131  N  N     . GLN A 1 516 ? 147.268 157.278 105.049 1.00 29.29 ?  516 GLN A N     1 
ATOM   4132  C  CA    . GLN A 1 516 ? 148.652 156.806 105.064 1.00 27.02 ?  516 GLN A CA    1 
ATOM   4133  C  C     . GLN A 1 516 ? 148.996 156.011 103.809 1.00 24.74 ?  516 GLN A C     1 
ATOM   4134  O  O     . GLN A 1 516 ? 149.758 155.045 103.864 1.00 31.63 ?  516 GLN A O     1 
ATOM   4135  C  CB    . GLN A 1 516 ? 148.947 155.977 106.317 1.00 23.58 ?  516 GLN A CB    1 
ATOM   4136  C  CG    . GLN A 1 516 ? 148.706 156.707 107.626 1.00 27.32 ?  516 GLN A CG    1 
ATOM   4137  C  CD    . GLN A 1 516 ? 148.836 155.796 108.829 1.00 28.96 ?  516 GLN A CD    1 
ATOM   4138  O  OE1   . GLN A 1 516 ? 149.941 155.418 109.219 1.00 24.45 ?  516 GLN A OE1   1 
ATOM   4139  N  NE2   . GLN A 1 516 ? 147.705 155.435 109.424 1.00 30.70 ?  516 GLN A NE2   1 
ATOM   4140  N  N     . TYR A 1 517 ? 148.433 156.403 102.663 1.00 21.14 ?  517 TYR A N     1 
ATOM   4141  C  CA    . TYR A 1 517 ? 148.801 155.754 101.409 1.00 19.39 ?  517 TYR A CA    1 
ATOM   4142  C  C     . TYR A 1 517 ? 150.219 156.113 100.987 1.00 29.46 ?  517 TYR A C     1 
ATOM   4143  O  O     . TYR A 1 517 ? 150.905 155.292 100.369 1.00 36.04 ?  517 TYR A O     1 
ATOM   4144  C  CB    . TYR A 1 517 ? 147.813 156.128 100.303 1.00 18.68 ?  517 TYR A CB    1 
ATOM   4145  C  CG    . TYR A 1 517 ? 148.423 156.108 98.918  1.00 27.03 ?  517 TYR A CG    1 
ATOM   4146  C  CD1   . TYR A 1 517 ? 148.576 154.916 98.223  1.00 23.94 ?  517 TYR A CD1   1 
ATOM   4147  C  CD2   . TYR A 1 517 ? 148.849 157.282 98.307  1.00 29.69 ?  517 TYR A CD2   1 
ATOM   4148  C  CE1   . TYR A 1 517 ? 149.137 154.892 96.962  1.00 27.36 ?  517 TYR A CE1   1 
ATOM   4149  C  CE2   . TYR A 1 517 ? 149.413 157.266 97.049  1.00 25.86 ?  517 TYR A CE2   1 
ATOM   4150  C  CZ    . TYR A 1 517 ? 149.554 156.069 96.382  1.00 29.69 ?  517 TYR A CZ    1 
ATOM   4151  O  OH    . TYR A 1 517 ? 150.111 156.051 95.125  1.00 34.33 ?  517 TYR A OH    1 
ATOM   4152  N  N     . GLU A 1 518 ? 150.670 157.328 101.309 1.00 31.48 ?  518 GLU A N     1 
ATOM   4153  C  CA    . GLU A 1 518 ? 151.967 157.799 100.837 1.00 33.30 ?  518 GLU A CA    1 
ATOM   4154  C  C     . GLU A 1 518 ? 153.105 156.910 101.319 1.00 37.36 ?  518 GLU A C     1 
ATOM   4155  O  O     . GLU A 1 518 ? 154.128 156.788 100.637 1.00 39.66 ?  518 GLU A O     1 
ATOM   4156  C  CB    . GLU A 1 518 ? 152.205 159.248 101.279 1.00 32.58 ?  518 GLU A CB    1 
ATOM   4157  C  CG    . GLU A 1 518 ? 151.104 160.253 100.915 1.00 34.94 ?  518 GLU A CG    1 
ATOM   4158  C  CD    . GLU A 1 518 ? 149.806 160.040 101.675 1.00 42.69 ?  518 GLU A CD    1 
ATOM   4159  O  OE1   . GLU A 1 518 ? 148.734 160.381 101.132 1.00 41.60 ?  518 GLU A OE1   1 
ATOM   4160  O  OE2   . GLU A 1 518 ? 149.858 159.531 102.815 1.00 40.31 -1 518 GLU A OE2   1 
ATOM   4161  N  N     . GLY A 1 519 ? 152.952 156.286 102.485 1.00 26.93 ?  519 GLY A N     1 
ATOM   4162  C  CA    . GLY A 1 519 ? 153.958 155.361 102.965 1.00 23.56 ?  519 GLY A CA    1 
ATOM   4163  C  C     . GLY A 1 519 ? 153.847 153.953 102.425 1.00 23.79 ?  519 GLY A C     1 
ATOM   4164  O  O     . GLY A 1 519 ? 154.735 153.135 102.683 1.00 28.85 ?  519 GLY A O     1 
ATOM   4165  N  N     . SER A 1 520 ? 152.787 153.654 101.679 1.00 22.77 ?  520 SER A N     1 
ATOM   4166  C  CA    . SER A 1 520 ? 152.573 152.306 101.182 1.00 24.37 ?  520 SER A CA    1 
ATOM   4167  C  C     . SER A 1 520 ? 153.494 152.003 100.005 1.00 22.49 ?  520 SER A C     1 
ATOM   4168  O  O     . SER A 1 520 ? 154.056 152.898 99.368  1.00 31.54 ?  520 SER A O     1 
ATOM   4169  C  CB    . SER A 1 520 ? 151.114 152.113 100.766 1.00 19.01 ?  520 SER A CB    1 
ATOM   4170  O  OG    . SER A 1 520 ? 150.771 152.972 99.694  1.00 21.50 ?  520 SER A OG    1 
ATOM   4171  N  N     . THR A 1 521 ? 153.649 150.707 99.723  1.00 20.34 ?  521 THR A N     1 
ATOM   4172  C  CA    . THR A 1 521 ? 154.459 150.282 98.590  1.00 21.16 ?  521 THR A CA    1 
ATOM   4173  C  C     . THR A 1 521 ? 153.815 150.637 97.256  1.00 23.54 ?  521 THR A C     1 
ATOM   4174  O  O     . THR A 1 521 ? 154.510 150.662 96.235  1.00 24.52 ?  521 THR A O     1 
ATOM   4175  C  CB    . THR A 1 521 ? 154.720 148.777 98.659  1.00 22.76 ?  521 THR A CB    1 
ATOM   4176  O  OG1   . THR A 1 521 ? 153.505 148.066 98.396  1.00 23.73 ?  521 THR A OG1   1 
ATOM   4177  C  CG2   . THR A 1 521 ? 155.236 148.392 100.036 1.00 19.65 ?  521 THR A CG2   1 
ATOM   4178  N  N     . TYR A 1 522 ? 152.504 150.895 97.239  1.00 26.55 ?  522 TYR A N     1 
ATOM   4179  C  CA    . TYR A 1 522 ? 151.873 151.423 96.034  1.00 18.97 ?  522 TYR A CA    1 
ATOM   4180  C  C     . TYR A 1 522 ? 152.435 152.795 95.689  1.00 23.87 ?  522 TYR A C     1 
ATOM   4181  O  O     . TYR A 1 522 ? 152.750 153.081 94.527  1.00 25.62 ?  522 TYR A O     1 
ATOM   4182  C  CB    . TYR A 1 522 ? 150.358 151.506 96.222  1.00 17.28 ?  522 TYR A CB    1 
ATOM   4183  C  CG    . TYR A 1 522 ? 149.674 150.184 96.484  1.00 17.83 ?  522 TYR A CG    1 
ATOM   4184  C  CD1   . TYR A 1 522 ? 149.624 149.199 95.508  1.00 19.28 ?  522 TYR A CD1   1 
ATOM   4185  C  CD2   . TYR A 1 522 ? 149.060 149.931 97.702  1.00 21.38 ?  522 TYR A CD2   1 
ATOM   4186  C  CE1   . TYR A 1 522 ? 148.994 147.995 95.743  1.00 18.02 ?  522 TYR A CE1   1 
ATOM   4187  C  CE2   . TYR A 1 522 ? 148.424 148.730 97.945  1.00 18.03 ?  522 TYR A CE2   1 
ATOM   4188  C  CZ    . TYR A 1 522 ? 148.397 147.765 96.964  1.00 19.92 ?  522 TYR A CZ    1 
ATOM   4189  O  OH    . TYR A 1 522 ? 147.768 146.567 97.203  1.00 25.93 ?  522 TYR A OH    1 
ATOM   4190  N  N     . ALA A 1 523 ? 152.572 153.661 96.696  1.00 25.50 ?  523 ALA A N     1 
ATOM   4191  C  CA    . ALA A 1 523 ? 153.079 155.009 96.459  1.00 26.43 ?  523 ALA A CA    1 
ATOM   4192  C  C     . ALA A 1 523 ? 154.540 154.986 96.034  1.00 31.21 ?  523 ALA A C     1 
ATOM   4193  O  O     . ALA A 1 523 ? 154.945 155.740 95.141  1.00 32.89 ?  523 ALA A O     1 
ATOM   4194  C  CB    . ALA A 1 523 ? 152.895 155.863 97.712  1.00 25.19 ?  523 ALA A CB    1 
ATOM   4195  N  N     . THR A 1 524 ? 155.348 154.132 96.661  1.00 24.86 ?  524 THR A N     1 
ATOM   4196  C  CA    . THR A 1 524 ? 156.761 154.035 96.325  1.00 24.67 ?  524 THR A CA    1 
ATOM   4197  C  C     . THR A 1 524 ? 157.018 153.215 95.069  1.00 30.74 ?  524 THR A C     1 
ATOM   4198  O  O     . THR A 1 524 ? 158.152 153.209 94.577  1.00 36.80 ?  524 THR A O     1 
ATOM   4199  C  CB    . THR A 1 524 ? 157.541 153.430 97.495  1.00 28.88 ?  524 THR A CB    1 
ATOM   4200  O  OG1   . THR A 1 524 ? 157.291 152.021 97.564  1.00 30.78 ?  524 THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1 524 ? 157.122 154.076 98.805  1.00 26.81 ?  524 THR A CG2   1 
ATOM   4202  N  N     . GLY A 1 525 ? 156.007 152.527 94.543  1.00 26.63 ?  525 GLY A N     1 
ATOM   4203  C  CA    . GLY A 1 525 ? 156.166 151.718 93.355  1.00 24.39 ?  525 GLY A CA    1 
ATOM   4204  C  C     . GLY A 1 525 ? 156.785 150.358 93.582  1.00 29.59 ?  525 GLY A C     1 
ATOM   4205  O  O     . GLY A 1 525 ? 156.976 149.615 92.611  1.00 32.79 ?  525 GLY A O     1 
ATOM   4206  N  N     . GLU A 1 526 ? 157.108 150.007 94.829  1.00 29.06 ?  526 GLU A N     1 
ATOM   4207  C  CA    . GLU A 1 526 ? 157.699 148.702 95.106  1.00 29.80 ?  526 GLU A CA    1 
ATOM   4208  C  C     . GLU A 1 526 ? 156.720 147.577 94.799  1.00 31.92 ?  526 GLU A C     1 
ATOM   4209  O  O     . GLU A 1 526 ? 157.117 146.517 94.297  1.00 37.13 ?  526 GLU A O     1 
ATOM   4210  C  CB    . GLU A 1 526 ? 158.158 148.640 96.563  1.00 30.68 ?  526 GLU A CB    1 
ATOM   4211  C  CG    . GLU A 1 526 ? 158.446 147.240 97.075  1.00 31.72 ?  526 GLU A CG    1 
ATOM   4212  C  CD    . GLU A 1 526 ? 158.474 147.169 98.590  1.00 36.24 ?  526 GLU A CD    1 
ATOM   4213  O  OE1   . GLU A 1 526 ? 158.578 148.233 99.233  1.00 35.08 ?  526 GLU A OE1   1 
ATOM   4214  O  OE2   . GLU A 1 526 ? 158.389 146.049 99.136  1.00 34.53 -1 526 GLU A OE2   1 
ATOM   4215  N  N     . TYR A 1 527 ? 155.432 147.796 95.083  1.00 31.75 ?  527 TYR A N     1 
ATOM   4216  C  CA    . TYR A 1 527 ? 154.419 146.768 94.858  1.00 22.45 ?  527 TYR A CA    1 
ATOM   4217  C  C     . TYR A 1 527 ? 154.430 146.275 93.417  1.00 24.31 ?  527 TYR A C     1 
ATOM   4218  O  O     . TYR A 1 527 ? 154.205 145.088 93.157  1.00 30.71 ?  527 TYR A O     1 
ATOM   4219  C  CB    . TYR A 1 527 ? 153.037 147.316 95.223  1.00 18.46 ?  527 TYR A CB    1 
ATOM   4220  C  CG    . TYR A 1 527 ? 151.920 146.305 95.104  1.00 25.45 ?  527 TYR A CG    1 
ATOM   4221  C  CD1   . TYR A 1 527 ? 151.252 146.112 93.900  1.00 23.33 ?  527 TYR A CD1   1 
ATOM   4222  C  CD2   . TYR A 1 527 ? 151.529 145.546 96.197  1.00 24.14 ?  527 TYR A CD2   1 
ATOM   4223  C  CE1   . TYR A 1 527 ? 150.235 145.189 93.791  1.00 20.19 ?  527 TYR A CE1   1 
ATOM   4224  C  CE2   . TYR A 1 527 ? 150.512 144.623 96.096  1.00 22.64 ?  527 TYR A CE2   1 
ATOM   4225  C  CZ    . TYR A 1 527 ? 149.867 144.449 94.891  1.00 23.29 ?  527 TYR A CZ    1 
ATOM   4226  O  OH    . TYR A 1 527 ? 148.851 143.528 94.788  1.00 29.93 ?  527 TYR A OH    1 
ATOM   4227  N  N     . PHE A 1 528 ? 154.693 147.170 92.471  1.00 26.54 ?  528 PHE A N     1 
ATOM   4228  C  CA    . PHE A 1 528 ? 154.661 146.843 91.054  1.00 27.56 ?  528 PHE A CA    1 
ATOM   4229  C  C     . PHE A 1 528 ? 155.966 146.246 90.546  1.00 31.65 ?  528 PHE A C     1 
ATOM   4230  O  O     . PHE A 1 528 ? 156.055 145.931 89.355  1.00 37.05 ?  528 PHE A O     1 
ATOM   4231  C  CB    . PHE A 1 528 ? 154.317 148.091 90.236  1.00 28.67 ?  528 PHE A CB    1 
ATOM   4232  C  CG    . PHE A 1 528 ? 153.035 148.752 90.651  1.00 31.81 ?  528 PHE A CG    1 
ATOM   4233  C  CD1   . PHE A 1 528 ? 151.833 148.375 90.077  1.00 27.01 ?  528 PHE A CD1   1 
ATOM   4234  C  CD2   . PHE A 1 528 ? 153.029 149.745 91.615  1.00 29.35 ?  528 PHE A CD2   1 
ATOM   4235  C  CE1   . PHE A 1 528 ? 150.650 148.977 90.456  1.00 27.38 ?  528 PHE A CE1   1 
ATOM   4236  C  CE2   . PHE A 1 528 ? 151.849 150.350 91.998  1.00 29.22 ?  528 PHE A CE2   1 
ATOM   4237  C  CZ    . PHE A 1 528 ? 150.659 149.964 91.418  1.00 28.09 ?  528 PHE A CZ    1 
ATOM   4238  N  N     . ASP A 1 529 ? 156.969 146.082 91.414  1.00 30.61 ?  529 ASP A N     1 
ATOM   4239  C  CA    . ASP A 1 529 ? 158.273 145.589 90.978  1.00 29.55 ?  529 ASP A CA    1 
ATOM   4240  C  C     . ASP A 1 529 ? 158.145 144.276 90.213  1.00 33.50 ?  529 ASP A C     1 
ATOM   4241  O  O     . ASP A 1 529 ? 158.473 144.197 89.023  1.00 35.83 ?  529 ASP A O     1 
ATOM   4242  C  CB    . ASP A 1 529 ? 159.192 145.422 92.190  1.00 32.37 ?  529 ASP A CB    1 
ATOM   4243  C  CG    . ASP A 1 529 ? 159.808 146.731 92.639  1.00 39.19 ?  529 ASP A CG    1 
ATOM   4244  O  OD1   . ASP A 1 529 ? 159.600 147.754 91.952  1.00 36.61 ?  529 ASP A OD1   1 
ATOM   4245  O  OD2   . ASP A 1 529 ? 160.499 146.738 93.680  1.00 39.06 -1 529 ASP A OD2   1 
ATOM   4246  N  N     . LYS A 1 530 ? 157.621 143.241 90.876  1.00 34.90 ?  530 LYS A N     1 
ATOM   4247  C  CA    . LYS A 1 530 ? 157.457 141.947 90.224  1.00 32.53 ?  530 LYS A CA    1 
ATOM   4248  C  C     . LYS A 1 530 ? 156.537 142.026 89.016  1.00 32.70 ?  530 LYS A C     1 
ATOM   4249  O  O     . LYS A 1 530 ? 156.577 141.138 88.159  1.00 34.96 ?  530 LYS A O     1 
ATOM   4250  C  CB    . LYS A 1 530 ? 156.916 140.921 91.220  1.00 31.49 ?  530 LYS A CB    1 
ATOM   4251  C  CG    . LYS A 1 530 ? 155.413 140.729 91.145  1.00 29.76 ?  530 LYS A CG    1 
ATOM   4252  C  CD    . LYS A 1 530 ? 154.894 139.923 92.313  1.00 31.93 ?  530 LYS A CD    1 
ATOM   4253  C  CE    . LYS A 1 530 ? 153.427 139.602 92.131  1.00 27.82 ?  530 LYS A CE    1 
ATOM   4254  N  NZ    . LYS A 1 530 ? 152.639 139.956 93.341  1.00 33.29 1  530 LYS A NZ    1 
ATOM   4255  N  N     . TYR A 1 531 ? 155.712 143.067 88.927  1.00 30.64 ?  531 TYR A N     1 
ATOM   4256  C  CA    . TYR A 1 531 ? 154.824 143.234 87.789  1.00 28.11 ?  531 TYR A CA    1 
ATOM   4257  C  C     . TYR A 1 531 ? 155.474 143.978 86.633  1.00 26.93 ?  531 TYR A C     1 
ATOM   4258  O  O     . TYR A 1 531 ? 155.032 143.818 85.490  1.00 32.56 ?  531 TYR A O     1 
ATOM   4259  C  CB    . TYR A 1 531 ? 153.553 143.965 88.223  1.00 27.82 ?  531 TYR A CB    1 
ATOM   4260  C  CG    . TYR A 1 531 ? 152.607 143.102 89.023  1.00 28.79 ?  531 TYR A CG    1 
ATOM   4261  C  CD1   . TYR A 1 531 ? 152.148 141.893 88.519  1.00 23.74 ?  531 TYR A CD1   1 
ATOM   4262  C  CD2   . TYR A 1 531 ? 152.173 143.495 90.282  1.00 25.66 ?  531 TYR A CD2   1 
ATOM   4263  C  CE1   . TYR A 1 531 ? 151.283 141.100 89.243  1.00 29.88 ?  531 TYR A CE1   1 
ATOM   4264  C  CE2   . TYR A 1 531 ? 151.307 142.708 91.013  1.00 25.40 ?  531 TYR A CE2   1 
ATOM   4265  C  CZ    . TYR A 1 531 ? 150.866 141.512 90.489  1.00 28.75 ?  531 TYR A CZ    1 
ATOM   4266  O  OH    . TYR A 1 531 ? 150.003 140.724 91.214  1.00 26.64 ?  531 TYR A OH    1 
ATOM   4267  N  N     . VAL A 1 532 ? 156.508 144.784 86.897  1.00 36.73 ?  532 VAL A N     1 
ATOM   4268  C  CA    . VAL A 1 532 ? 157.193 145.492 85.821  1.00 35.08 ?  532 VAL A CA    1 
ATOM   4269  C  C     . VAL A 1 532 ? 158.409 144.733 85.315  1.00 36.69 ?  532 VAL A C     1 
ATOM   4270  O  O     . VAL A 1 532 ? 159.084 145.205 84.391  1.00 41.15 ?  532 VAL A O     1 
ATOM   4271  C  CB    . VAL A 1 532 ? 157.607 146.914 86.258  1.00 35.29 ?  532 VAL A CB    1 
ATOM   4272  C  CG1   . VAL A 1 532 ? 156.389 147.710 86.697  1.00 34.97 ?  532 VAL A CG1   1 
ATOM   4273  C  CG2   . VAL A 1 532 ? 158.642 146.856 87.366  1.00 33.74 ?  532 VAL A CG2   1 
ATOM   4274  N  N     . SER A 1 533 ? 158.707 143.569 85.887  1.00 37.31 ?  533 SER A N     1 
ATOM   4275  C  CA    . SER A 1 533 ? 159.837 142.755 85.468  1.00 39.93 ?  533 SER A CA    1 
ATOM   4276  C  C     . SER A 1 533 ? 159.452 141.354 85.022  1.00 40.94 ?  533 SER A C     1 
ATOM   4277  O  O     . SER A 1 533 ? 160.120 140.799 84.146  1.00 43.31 ?  533 SER A O     1 
ATOM   4278  C  CB    . SER A 1 533 ? 160.866 142.646 86.604  1.00 41.14 ?  533 SER A CB    1 
ATOM   4279  O  OG    . SER A 1 533 ? 160.388 141.812 87.644  1.00 44.41 ?  533 SER A OG    1 
ATOM   4280  N  N     . THR A 1 534 ? 158.402 140.771 85.592  1.00 40.28 ?  534 THR A N     1 
ATOM   4281  C  CA    . THR A 1 534 ? 157.967 139.422 85.257  1.00 38.86 ?  534 THR A CA    1 
ATOM   4282  C  C     . THR A 1 534 ? 156.691 139.491 84.431  1.00 38.19 ?  534 THR A C     1 
ATOM   4283  O  O     . THR A 1 534 ? 155.728 140.159 84.822  1.00 43.56 ?  534 THR A O     1 
ATOM   4284  C  CB    . THR A 1 534 ? 157.730 138.591 86.521  1.00 39.36 ?  534 THR A CB    1 
ATOM   4285  O  OG1   . THR A 1 534 ? 158.972 138.397 87.209  1.00 42.76 ?  534 THR A OG1   1 
ATOM   4286  C  CG2   . THR A 1 534 ? 157.134 137.236 86.168  1.00 38.66 ?  534 THR A CG2   1 
ATOM   4287  N  N     . ASP A 1 535 ? 156.690 138.806 83.292  1.00 40.64 ?  535 ASP A N     1 
ATOM   4288  C  CA    . ASP A 1 535 ? 155.512 138.717 82.443  1.00 39.74 ?  535 ASP A CA    1 
ATOM   4289  C  C     . ASP A 1 535 ? 154.644 137.553 82.906  1.00 41.84 ?  535 ASP A C     1 
ATOM   4290  O  O     . ASP A 1 535 ? 155.127 136.425 83.037  1.00 42.89 ?  535 ASP A O     1 
ATOM   4291  C  CB    . ASP A 1 535 ? 155.914 138.535 80.979  1.00 38.68 ?  535 ASP A CB    1 
ATOM   4292  C  CG    . ASP A 1 535 ? 154.796 138.882 80.020  1.00 44.50 ?  535 ASP A CG    1 
ATOM   4293  O  OD1   . ASP A 1 535 ? 154.432 140.073 79.932  1.00 45.74 ?  535 ASP A OD1   1 
ATOM   4294  O  OD2   . ASP A 1 535 ? 154.282 137.962 79.351  1.00 45.92 -1 535 ASP A OD2   1 
ATOM   4295  N  N     . PHE A 1 536 ? 153.365 137.834 83.155  1.00 34.20 ?  536 PHE A N     1 
ATOM   4296  C  CA    . PHE A 1 536 ? 152.438 136.838 83.676  1.00 26.98 ?  536 PHE A CA    1 
ATOM   4297  C  C     . PHE A 1 536 ? 151.472 136.335 82.610  1.00 31.33 ?  536 PHE A C     1 
ATOM   4298  O  O     . PHE A 1 536 ? 150.398 135.823 82.941  1.00 37.66 ?  536 PHE A O     1 
ATOM   4299  C  CB    . PHE A 1 536 ? 151.674 137.407 84.871  1.00 29.06 ?  536 PHE A CB    1 
ATOM   4300  C  CG    . PHE A 1 536 ? 152.532 137.636 86.083  1.00 27.91 ?  536 PHE A CG    1 
ATOM   4301  C  CD1   . PHE A 1 536 ? 152.772 136.612 86.981  1.00 27.98 ?  536 PHE A CD1   1 
ATOM   4302  C  CD2   . PHE A 1 536 ? 153.104 138.873 86.319  1.00 27.54 ?  536 PHE A CD2   1 
ATOM   4303  C  CE1   . PHE A 1 536 ? 153.564 136.818 88.094  1.00 28.05 ?  536 PHE A CE1   1 
ATOM   4304  C  CE2   . PHE A 1 536 ? 153.898 139.084 87.431  1.00 32.24 ?  536 PHE A CE2   1 
ATOM   4305  C  CZ    . PHE A 1 536 ? 154.126 138.056 88.320  1.00 28.77 ?  536 PHE A CZ    1 
ATOM   4306  N  N     . SER A 1 537 ? 151.833 136.476 81.338  1.00 37.02 ?  537 SER A N     1 
ATOM   4307  C  CA    . SER A 1 537 ? 151.050 135.891 80.265  1.00 33.64 ?  537 SER A CA    1 
ATOM   4308  C  C     . SER A 1 537 ? 151.114 134.367 80.350  1.00 38.82 ?  537 SER A C     1 
ATOM   4309  O  O     . SER A 1 537 ? 152.096 133.807 80.845  1.00 39.19 ?  537 SER A O     1 
ATOM   4310  C  CB    . SER A 1 537 ? 151.569 136.370 78.911  1.00 37.25 ?  537 SER A CB    1 
ATOM   4311  O  OG    . SER A 1 537 ? 151.173 135.510 77.858  1.00 44.12 ?  537 SER A OG    1 
ATOM   4312  N  N     . PRO A 1 538 ? 150.069 133.673 79.896  1.00 37.27 ?  538 PRO A N     1 
ATOM   4313  C  CA    . PRO A 1 538 ? 150.064 132.208 79.994  1.00 34.32 ?  538 PRO A CA    1 
ATOM   4314  C  C     . PRO A 1 538 ? 151.233 131.584 79.246  1.00 39.19 ?  538 PRO A C     1 
ATOM   4315  O  O     . PRO A 1 538 ? 151.585 132.002 78.141  1.00 39.38 ?  538 PRO A O     1 
ATOM   4316  C  CB    . PRO A 1 538 ? 148.723 131.817 79.366  1.00 37.31 ?  538 PRO A CB    1 
ATOM   4317  C  CG    . PRO A 1 538 ? 147.872 133.027 79.510  1.00 34.46 ?  538 PRO A CG    1 
ATOM   4318  C  CD    . PRO A 1 538 ? 148.801 134.188 79.353  1.00 33.65 ?  538 PRO A CD    1 
ATOM   4319  N  N     . LYS A 1 539 ? 151.831 130.568 79.866  1.00 44.39 ?  539 LYS A N     1 
ATOM   4320  C  CA    . LYS A 1 539 ? 152.924 129.823 79.260  1.00 44.62 ?  539 LYS A CA    1 
ATOM   4321  C  C     . LYS A 1 539 ? 152.447 128.613 78.470  1.00 44.99 ?  539 LYS A C     1 
ATOM   4322  O  O     . LYS A 1 539 ? 153.259 127.974 77.793  1.00 47.43 ?  539 LYS A O     1 
ATOM   4323  C  CB    . LYS A 1 539 ? 153.914 129.368 80.337  1.00 43.77 ?  539 LYS A CB    1 
ATOM   4324  C  CG    . LYS A 1 539 ? 154.336 130.468 81.295  1.00 42.84 ?  539 LYS A CG    1 
ATOM   4325  C  CD    . LYS A 1 539 ? 155.510 131.261 80.744  1.00 45.68 ?  539 LYS A CD    1 
ATOM   4326  C  CE    . LYS A 1 539 ? 155.755 132.519 81.560  1.00 45.50 ?  539 LYS A CE    1 
ATOM   4327  N  NZ    . LYS A 1 539 ? 155.115 133.713 80.943  1.00 44.13 1  539 LYS A NZ    1 
ATOM   4328  N  N     . TYR A 1 540 ? 151.159 128.290 78.538  1.00 42.49 ?  540 TYR A N     1 
ATOM   4329  C  CA    . TYR A 1 540 ? 150.584 127.160 77.826  1.00 41.58 ?  540 TYR A CA    1 
ATOM   4330  C  C     . TYR A 1 540 ? 149.605 127.665 76.775  1.00 42.99 ?  540 TYR A C     1 
ATOM   4331  O  O     . TYR A 1 540 ? 148.881 128.639 77.005  1.00 44.81 ?  540 TYR A O     1 
ATOM   4332  C  CB    . TYR A 1 540 ? 149.879 126.202 78.790  1.00 42.66 ?  540 TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1 540 ? 150.818 125.508 79.747  1.00 44.40 ?  540 TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1 540 ? 151.150 126.082 80.966  1.00 42.75 ?  540 TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1 540 ? 151.381 124.279 79.427  1.00 45.61 ?  540 TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1 540 ? 152.011 125.451 81.843  1.00 45.50 ?  540 TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1 540 ? 152.242 123.641 80.297  1.00 40.60 ?  540 TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1 540 ? 152.554 124.231 81.503  1.00 45.33 ?  540 TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1 540 ? 153.413 123.597 82.369  1.00 46.48 ?  540 TYR A OH    1 
ATOM   4340  N  N     . GLU A 1 541 ? 149.594 126.998 75.618  1.00 47.04 ?  541 GLU A N     1 
ATOM   4341  C  CA    . GLU A 1 541 ? 148.729 127.426 74.523  1.00 47.04 ?  541 GLU A CA    1 
ATOM   4342  C  C     . GLU A 1 541 ? 147.257 127.291 74.892  1.00 47.07 ?  541 GLU A C     1 
ATOM   4343  O  O     . GLU A 1 541 ? 146.429 128.111 74.479  1.00 44.24 ?  541 GLU A O     1 
ATOM   4344  C  CB    . GLU A 1 541 ? 149.041 126.619 73.263  1.00 45.13 ?  541 GLU A CB    1 
ATOM   4345  C  CG    . GLU A 1 541 ? 148.671 127.321 71.968  1.00 46.40 ?  541 GLU A CG    1 
ATOM   4346  C  CD    . GLU A 1 541 ? 148.610 126.370 70.790  1.00 52.19 ?  541 GLU A CD    1 
ATOM   4347  O  OE1   . GLU A 1 541 ? 148.541 125.144 71.017  1.00 52.67 ?  541 GLU A OE1   1 
ATOM   4348  O  OE2   . GLU A 1 541 ? 148.633 126.847 69.635  1.00 50.07 -1 541 GLU A OE2   1 
ATOM   4349  N  N     . LYS A 1 542 ? 146.910 126.255 75.659  1.00 42.45 ?  542 LYS A N     1 
ATOM   4350  C  CA    . LYS A 1 542 ? 145.519 126.057 76.051  1.00 41.73 ?  542 LYS A CA    1 
ATOM   4351  C  C     . LYS A 1 542 ? 145.013 127.214 76.904  1.00 43.05 ?  542 LYS A C     1 
ATOM   4352  O  O     . LYS A 1 542 ? 143.900 127.711 76.696  1.00 41.93 ?  542 LYS A O     1 
ATOM   4353  C  CB    . LYS A 1 542 ? 145.374 124.732 76.800  1.00 40.93 ?  542 LYS A CB    1 
ATOM   4354  C  CG    . LYS A 1 542 ? 143.945 124.356 77.141  1.00 43.00 ?  542 LYS A CG    1 
ATOM   4355  C  CD    . LYS A 1 542 ? 143.893 123.026 77.871  1.00 39.38 ?  542 LYS A CD    1 
ATOM   4356  C  CE    . LYS A 1 542 ? 142.463 122.560 78.070  1.00 41.15 ?  542 LYS A CE    1 
ATOM   4357  N  NZ    . LYS A 1 542 ? 142.405 121.192 78.653  1.00 42.60 1  542 LYS A NZ    1 
ATOM   4358  N  N     . ILE A 1 543 ? 145.826 127.671 77.857  1.00 38.22 ?  543 ILE A N     1 
ATOM   4359  C  CA    . ILE A 1 543 ? 145.413 128.780 78.711  1.00 36.34 ?  543 ILE A CA    1 
ATOM   4360  C  C     . ILE A 1 543 ? 145.325 130.070 77.901  1.00 38.94 ?  543 ILE A C     1 
ATOM   4361  O  O     . ILE A 1 543 ? 144.421 130.891 78.109  1.00 41.41 ?  543 ILE A O     1 
ATOM   4362  C  CB    . ILE A 1 543 ? 146.372 128.920 79.906  1.00 35.88 ?  543 ILE A CB    1 
ATOM   4363  C  CG1   . ILE A 1 543 ? 146.385 127.646 80.755  1.00 39.31 ?  543 ILE A CG1   1 
ATOM   4364  C  CG2   . ILE A 1 543 ? 145.965 130.093 80.773  1.00 37.77 ?  543 ILE A CG2   1 
ATOM   4365  C  CD1   . ILE A 1 543 ? 145.047 126.944 80.865  1.00 37.09 ?  543 ILE A CD1   1 
ATOM   4366  N  N     . ALA A 1 544 ? 146.256 130.268 76.965  1.00 37.81 ?  544 ALA A N     1 
ATOM   4367  C  CA    . ALA A 1 544 ? 146.203 131.445 76.106  1.00 40.47 ?  544 ALA A CA    1 
ATOM   4368  C  C     . ALA A 1 544 ? 144.937 131.454 75.258  1.00 42.32 ?  544 ALA A C     1 
ATOM   4369  O  O     . ALA A 1 544 ? 144.315 132.505 75.068  1.00 42.94 ?  544 ALA A O     1 
ATOM   4370  C  CB    . ALA A 1 544 ? 147.446 131.502 75.218  1.00 40.60 ?  544 ALA A CB    1 
ATOM   4371  N  N     . ASN A 1 545 ? 144.542 130.290 74.737  1.00 43.74 ?  545 ASN A N     1 
ATOM   4372  C  CA    . ASN A 1 545 ? 143.283 130.198 74.006  1.00 44.64 ?  545 ASN A CA    1 
ATOM   4373  C  C     . ASN A 1 545 ? 142.090 130.426 74.924  1.00 44.81 ?  545 ASN A C     1 
ATOM   4374  O  O     . ASN A 1 545 ? 141.063 130.958 74.485  1.00 47.71 ?  545 ASN A O     1 
ATOM   4375  C  CB    . ASN A 1 545 ? 143.171 128.840 73.314  1.00 44.57 ?  545 ASN A CB    1 
ATOM   4376  C  CG    . ASN A 1 545 ? 144.290 128.598 72.324  1.00 47.93 ?  545 ASN A CG    1 
ATOM   4377  O  OD1   . ASN A 1 545 ? 144.894 129.539 71.811  1.00 47.94 ?  545 ASN A OD1   1 
ATOM   4378  N  ND2   . ASN A 1 545 ? 144.575 127.330 72.051  1.00 47.29 ?  545 ASN A ND2   1 
ATOM   4379  N  N     . LEU A 1 546 ? 142.200 130.021 76.191  1.00 40.52 ?  546 LEU A N     1 
ATOM   4380  C  CA    . LEU A 1 546 ? 141.157 130.343 77.160  1.00 38.34 ?  546 LEU A CA    1 
ATOM   4381  C  C     . LEU A 1 546 ? 141.019 131.849 77.333  1.00 38.77 ?  546 LEU A C     1 
ATOM   4382  O  O     . LEU A 1 546 ? 139.903 132.372 77.437  1.00 40.95 ?  546 LEU A O     1 
ATOM   4383  C  CB    . LEU A 1 546 ? 141.460 129.678 78.502  1.00 35.29 ?  546 LEU A CB    1 
ATOM   4384  C  CG    . LEU A 1 546 ? 141.211 128.175 78.599  1.00 38.57 ?  546 LEU A CG    1 
ATOM   4385  C  CD1   . LEU A 1 546 ? 141.442 127.705 80.022  1.00 36.37 ?  546 LEU A CD1   1 
ATOM   4386  C  CD2   . LEU A 1 546 ? 139.804 127.836 78.141  1.00 34.75 ?  546 LEU A CD2   1 
ATOM   4387  N  N     . PHE A 1 547 ? 142.141 132.564 77.363  1.00 37.80 ?  547 PHE A N     1 
ATOM   4388  C  CA    . PHE A 1 547 ? 142.139 134.013 77.514  1.00 36.82 ?  547 PHE A CA    1 
ATOM   4389  C  C     . PHE A 1 547 ? 141.949 134.748 76.193  1.00 37.34 ?  547 PHE A C     1 
ATOM   4390  O  O     . PHE A 1 547 ? 142.102 135.973 76.155  1.00 38.01 ?  547 PHE A O     1 
ATOM   4391  C  CB    . PHE A 1 547 ? 143.435 134.478 78.179  1.00 35.38 ?  547 PHE A CB    1 
ATOM   4392  C  CG    . PHE A 1 547 ? 143.455 134.283 79.663  1.00 35.44 ?  547 PHE A CG    1 
ATOM   4393  C  CD1   . PHE A 1 547 ? 142.858 135.205 80.504  1.00 34.89 ?  547 PHE A CD1   1 
ATOM   4394  C  CD2   . PHE A 1 547 ? 144.071 133.177 80.220  1.00 32.16 ?  547 PHE A CD2   1 
ATOM   4395  C  CE1   . PHE A 1 547 ? 142.875 135.028 81.873  1.00 31.83 ?  547 PHE A CE1   1 
ATOM   4396  C  CE2   . PHE A 1 547 ? 144.090 132.995 81.586  1.00 34.52 ?  547 PHE A CE2   1 
ATOM   4397  C  CZ    . PHE A 1 547 ? 143.490 133.920 82.413  1.00 33.71 ?  547 PHE A CZ    1 
ATOM   4398  N  N     . GLU A 1 548 ? 141.626 134.036 75.115  1.00 43.65 ?  548 GLU A N     1 
ATOM   4399  C  CA    . GLU A 1 548 ? 141.426 134.682 73.825  1.00 46.68 ?  548 GLU A CA    1 
ATOM   4400  C  C     . GLU A 1 548 ? 140.241 135.639 73.881  1.00 47.86 ?  548 GLU A C     1 
ATOM   4401  O  O     . GLU A 1 548 ? 139.225 135.362 74.524  1.00 47.21 ?  548 GLU A O     1 
ATOM   4402  C  CB    . GLU A 1 548 ? 141.206 133.635 72.734  1.00 45.30 ?  548 GLU A CB    1 
ATOM   4403  C  CG    . GLU A 1 548 ? 142.010 133.884 71.471  1.00 46.87 ?  548 GLU A CG    1 
ATOM   4404  C  CD    . GLU A 1 548 ? 143.504 133.804 71.708  1.00 49.11 ?  548 GLU A CD    1 
ATOM   4405  O  OE1   . GLU A 1 548 ? 144.048 132.679 71.712  1.00 48.26 ?  548 GLU A OE1   1 
ATOM   4406  O  OE2   . GLU A 1 548 ? 144.136 134.865 71.894  1.00 47.53 -1 548 GLU A OE2   1 
ATOM   4407  N  N     . GLY A 1 549 ? 140.378 136.772 73.196  1.00 44.32 ?  549 GLY A N     1 
ATOM   4408  C  CA    . GLY A 1 549 ? 139.370 137.809 73.214  1.00 40.96 ?  549 GLY A CA    1 
ATOM   4409  C  C     . GLY A 1 549 ? 139.494 138.798 74.350  1.00 43.69 ?  549 GLY A C     1 
ATOM   4410  O  O     . GLY A 1 549 ? 138.679 139.725 74.433  1.00 44.76 ?  549 GLY A O     1 
ATOM   4411  N  N     . MET A 1 550 ? 140.482 138.632 75.226  1.00 43.09 ?  550 MET A N     1 
ATOM   4412  C  CA    . MET A 1 550 ? 140.689 139.509 76.370  1.00 40.92 ?  550 MET A CA    1 
ATOM   4413  C  C     . MET A 1 550 ? 142.129 139.995 76.364  1.00 41.67 ?  550 MET A C     1 
ATOM   4414  O  O     . MET A 1 550 ? 143.052 139.200 76.155  1.00 42.25 ?  550 MET A O     1 
ATOM   4415  C  CB    . MET A 1 550 ? 140.389 138.784 77.683  1.00 38.56 ?  550 MET A CB    1 
ATOM   4416  C  CG    . MET A 1 550 ? 139.118 139.232 78.370  1.00 42.56 ?  550 MET A CG    1 
ATOM   4417  S  SD    . MET A 1 550 ? 138.857 138.328 79.902  1.00 55.69 ?  550 MET A SD    1 
ATOM   4418  C  CE    . MET A 1 550 ? 138.857 136.642 79.300  1.00 41.52 ?  550 MET A CE    1 
ATOM   4419  N  N     . HIS A 1 551 ? 142.323 141.289 76.597  1.00 38.98 ?  551 HIS A N     1 
ATOM   4420  C  CA    . HIS A 1 551 ? 143.669 141.842 76.645  1.00 38.16 ?  551 HIS A CA    1 
ATOM   4421  C  C     . HIS A 1 551 ? 144.339 141.451 77.957  1.00 38.90 ?  551 HIS A C     1 
ATOM   4422  O  O     . HIS A 1 551 ? 143.824 141.749 79.040  1.00 40.01 ?  551 HIS A O     1 
ATOM   4423  C  CB    . HIS A 1 551 ? 143.629 143.360 76.494  1.00 39.46 ?  551 HIS A CB    1 
ATOM   4424  C  CG    . HIS A 1 551 ? 144.951 144.022 76.728  1.00 41.61 ?  551 HIS A CG    1 
ATOM   4425  N  ND1   . HIS A 1 551 ? 146.064 143.752 75.960  1.00 42.78 ?  551 HIS A ND1   1 
ATOM   4426  C  CD2   . HIS A 1 551 ? 145.340 144.941 77.643  1.00 42.39 ?  551 HIS A CD2   1 
ATOM   4427  C  CE1   . HIS A 1 551 ? 147.081 144.476 76.392  1.00 40.85 ?  551 HIS A CE1   1 
ATOM   4428  N  NE2   . HIS A 1 551 ? 146.668 145.206 77.413  1.00 41.74 ?  551 HIS A NE2   1 
ATOM   4429  N  N     . ILE A 1 552 ? 145.481 140.783 77.859  1.00 35.62 ?  552 ILE A N     1 
ATOM   4430  C  CA    . ILE A 1 552 ? 146.246 140.359 79.026  1.00 31.64 ?  552 ILE A CA    1 
ATOM   4431  C  C     . ILE A 1 552 ? 147.278 141.442 79.329  1.00 33.24 ?  552 ILE A C     1 
ATOM   4432  O  O     . ILE A 1 552 ? 148.121 141.732 78.465  1.00 36.10 ?  552 ILE A O     1 
ATOM   4433  C  CB    . ILE A 1 552 ? 146.925 139.005 78.789  1.00 33.70 ?  552 ILE A CB    1 
ATOM   4434  C  CG1   . ILE A 1 552 ? 145.870 137.918 78.576  1.00 32.99 ?  552 ILE A CG1   1 
ATOM   4435  C  CG2   . ILE A 1 552 ? 147.835 138.652 79.951  1.00 34.38 ?  552 ILE A CG2   1 
ATOM   4436  C  CD1   . ILE A 1 552 ? 146.442 136.598 78.125  1.00 34.55 ?  552 ILE A CD1   1 
ATOM   4437  N  N     . PRO A 1 553 ? 147.241 142.063 80.507  1.00 38.28 ?  553 PRO A N     1 
ATOM   4438  C  CA    . PRO A 1 553 ? 148.195 143.139 80.806  1.00 32.24 ?  553 PRO A CA    1 
ATOM   4439  C  C     . PRO A 1 553 ? 149.633 142.640 80.761  1.00 35.19 ?  553 PRO A C     1 
ATOM   4440  O  O     . PRO A 1 553 ? 149.972 141.611 81.349  1.00 36.48 ?  553 PRO A O     1 
ATOM   4441  C  CB    . PRO A 1 553 ? 147.794 143.584 82.217  1.00 31.02 ?  553 PRO A CB    1 
ATOM   4442  C  CG    . PRO A 1 553 ? 146.369 143.152 82.359  1.00 30.52 ?  553 PRO A CG    1 
ATOM   4443  C  CD    . PRO A 1 553 ? 146.261 141.875 81.587  1.00 32.28 ?  553 PRO A CD    1 
ATOM   4444  N  N     . THR A 1 554 ? 150.477 143.383 80.056  1.00 39.01 ?  554 THR A N     1 
ATOM   4445  C  CA    . THR A 1 554 ? 151.882 143.059 79.905  1.00 38.97 ?  554 THR A CA    1 
ATOM   4446  C  C     . THR A 1 554 ? 152.705 143.859 80.911  1.00 37.81 ?  554 THR A C     1 
ATOM   4447  O  O     . THR A 1 554 ? 152.168 144.531 81.796  1.00 39.91 ?  554 THR A O     1 
ATOM   4448  C  CB    . THR A 1 554 ? 152.332 143.325 78.468  1.00 37.93 ?  554 THR A CB    1 
ATOM   4449  O  OG1   . THR A 1 554 ? 152.306 144.734 78.211  1.00 40.49 ?  554 THR A OG1   1 
ATOM   4450  C  CG2   . THR A 1 554 ? 151.412 142.621 77.483  1.00 35.01 ?  554 THR A CG2   1 
ATOM   4451  N  N     . THR A 1 555 ? 154.032 143.787 80.779  1.00 38.74 ?  555 THR A N     1 
ATOM   4452  C  CA    . THR A 1 555 ? 154.898 144.573 81.650  1.00 36.20 ?  555 THR A CA    1 
ATOM   4453  C  C     . THR A 1 555 ? 154.781 146.063 81.362  1.00 38.34 ?  555 THR A C     1 
ATOM   4454  O  O     . THR A 1 555 ? 154.881 146.879 82.282  1.00 40.28 ?  555 THR A O     1 
ATOM   4455  C  CB    . THR A 1 555 ? 156.350 144.117 81.505  1.00 38.61 ?  555 THR A CB    1 
ATOM   4456  O  OG1   . THR A 1 555 ? 156.681 143.997 80.115  1.00 41.79 ?  555 THR A OG1   1 
ATOM   4457  C  CG2   . THR A 1 555 ? 156.556 142.774 82.190  1.00 37.28 ?  555 THR A CG2   1 
ATOM   4458  N  N     . GLU A 1 556 ? 154.576 146.439 80.096  1.00 39.91 ?  556 GLU A N     1 
ATOM   4459  C  CA    . GLU A 1 556 ? 154.367 147.845 79.767  1.00 39.82 ?  556 GLU A CA    1 
ATOM   4460  C  C     . GLU A 1 556 ? 153.057 148.360 80.354  1.00 38.55 ?  556 GLU A C     1 
ATOM   4461  O  O     . GLU A 1 556 ? 152.995 149.486 80.862  1.00 40.13 ?  556 GLU A O     1 
ATOM   4462  C  CB    . GLU A 1 556 ? 154.391 148.039 78.252  1.00 40.74 ?  556 GLU A CB    1 
ATOM   4463  C  CG    . GLU A 1 556 ? 154.464 149.491 77.814  1.00 43.25 ?  556 GLU A CG    1 
ATOM   4464  C  CD    . GLU A 1 556 ? 155.672 150.210 78.381  1.00 44.78 ?  556 GLU A CD    1 
ATOM   4465  O  OE1   . GLU A 1 556 ? 156.764 149.603 78.422  1.00 41.96 ?  556 GLU A OE1   1 
ATOM   4466  O  OE2   . GLU A 1 556 ? 155.531 151.383 78.787  1.00 44.90 -1 556 GLU A OE2   1 
ATOM   4467  N  N     . ASP A 1 557 ? 151.999 147.549 80.288  1.00 40.02 ?  557 ASP A N     1 
ATOM   4468  C  CA    . ASP A 1 557 ? 150.735 147.929 80.905  1.00 36.22 ?  557 ASP A CA    1 
ATOM   4469  C  C     . ASP A 1 557 ? 150.888 148.081 82.412  1.00 36.15 ?  557 ASP A C     1 
ATOM   4470  O  O     . ASP A 1 557 ? 150.315 148.995 83.015  1.00 37.41 ?  557 ASP A O     1 
ATOM   4471  C  CB    . ASP A 1 557 ? 149.656 146.899 80.574  1.00 35.10 ?  557 ASP A CB    1 
ATOM   4472  C  CG    . ASP A 1 557 ? 149.105 147.064 79.173  1.00 40.32 ?  557 ASP A CG    1 
ATOM   4473  O  OD1   . ASP A 1 557 ? 149.029 148.215 78.695  1.00 43.55 ?  557 ASP A OD1   1 
ATOM   4474  O  OD2   . ASP A 1 557 ? 148.749 146.043 78.550  1.00 42.22 -1 557 ASP A OD2   1 
ATOM   4475  N  N     . TRP A 1 558 ? 151.663 147.193 83.038  1.00 29.19 ?  558 TRP A N     1 
ATOM   4476  C  CA    . TRP A 1 558 ? 151.905 147.310 84.470  1.00 27.33 ?  558 TRP A CA    1 
ATOM   4477  C  C     . TRP A 1 558 ? 152.737 148.541 84.804  1.00 29.30 ?  558 TRP A C     1 
ATOM   4478  O  O     . TRP A 1 558 ? 152.518 149.165 85.846  1.00 33.21 ?  558 TRP A O     1 
ATOM   4479  C  CB    . TRP A 1 558 ? 152.583 146.046 84.991  1.00 29.55 ?  558 TRP A CB    1 
ATOM   4480  C  CG    . TRP A 1 558 ? 151.617 144.989 85.421  1.00 27.37 ?  558 TRP A CG    1 
ATOM   4481  C  CD1   . TRP A 1 558 ? 151.328 143.829 84.769  1.00 27.28 ?  558 TRP A CD1   1 
ATOM   4482  C  CD2   . TRP A 1 558 ? 150.810 144.997 86.604  1.00 28.16 ?  558 TRP A CD2   1 
ATOM   4483  N  NE1   . TRP A 1 558 ? 150.394 143.110 85.473  1.00 30.85 ?  558 TRP A NE1   1 
ATOM   4484  C  CE2   . TRP A 1 558 ? 150.061 143.805 86.606  1.00 28.47 ?  558 TRP A CE2   1 
ATOM   4485  C  CE3   . TRP A 1 558 ? 150.654 145.892 87.666  1.00 30.88 ?  558 TRP A CE3   1 
ATOM   4486  C  CZ2   . TRP A 1 558 ? 149.168 143.487 87.624  1.00 26.24 ?  558 TRP A CZ2   1 
ATOM   4487  C  CZ3   . TRP A 1 558 ? 149.766 145.575 88.677  1.00 26.03 ?  558 TRP A CZ3   1 
ATOM   4488  C  CH2   . TRP A 1 558 ? 149.035 144.383 88.648  1.00 22.82 ?  558 TRP A CH2   1 
ATOM   4489  N  N     . LYS A 1 559 ? 153.689 148.908 83.944  1.00 36.33 ?  559 LYS A N     1 
ATOM   4490  C  CA    . LYS A 1 559 ? 154.439 150.143 84.153  1.00 32.59 ?  559 LYS A CA    1 
ATOM   4491  C  C     . LYS A 1 559 ? 153.527 151.360 84.052  1.00 31.12 ?  559 LYS A C     1 
ATOM   4492  O  O     . LYS A 1 559 ? 153.640 152.303 84.846  1.00 34.31 ?  559 LYS A O     1 
ATOM   4493  C  CB    . LYS A 1 559 ? 155.576 150.246 83.136  1.00 36.36 ?  559 LYS A CB    1 
ATOM   4494  C  CG    . LYS A 1 559 ? 156.833 149.489 83.522  1.00 38.00 ?  559 LYS A CG    1 
ATOM   4495  C  CD    . LYS A 1 559 ? 157.562 148.982 82.290  1.00 39.16 ?  559 LYS A CD    1 
ATOM   4496  C  CE    . LYS A 1 559 ? 158.672 148.015 82.661  1.00 37.84 ?  559 LYS A CE    1 
ATOM   4497  N  NZ    . LYS A 1 559 ? 159.835 148.131 81.741  1.00 39.17 1  559 LYS A NZ    1 
ATOM   4498  N  N     . LYS A 1 560 ? 152.619 151.355 83.075  1.00 33.31 ?  560 LYS A N     1 
ATOM   4499  C  CA    . LYS A 1 560 ? 151.656 152.444 82.951  1.00 32.75 ?  560 LYS A CA    1 
ATOM   4500  C  C     . LYS A 1 560 ? 150.750 152.517 84.173  1.00 36.91 ?  560 LYS A C     1 
ATOM   4501  O  O     . LYS A 1 560 ? 150.443 153.609 84.663  1.00 36.57 ?  560 LYS A O     1 
ATOM   4502  C  CB    . LYS A 1 560 ? 150.828 152.273 81.679  1.00 32.44 ?  560 LYS A CB    1 
ATOM   4503  C  CG    . LYS A 1 560 ? 151.618 152.448 80.395  1.00 37.98 ?  560 LYS A CG    1 
ATOM   4504  C  CD    . LYS A 1 560 ? 150.759 152.146 79.179  1.00 38.81 ?  560 LYS A CD    1 
ATOM   4505  C  CE    . LYS A 1 560 ? 151.601 152.026 77.921  1.00 35.97 ?  560 LYS A CE    1 
ATOM   4506  N  NZ    . LYS A 1 560 ? 150.857 151.356 76.821  1.00 38.72 1  560 LYS A NZ    1 
ATOM   4507  N  N     . LEU A 1 561 ? 150.311 151.362 84.679  1.00 35.84 ?  561 LEU A N     1 
ATOM   4508  C  CA    . LEU A 1 561 ? 149.492 151.344 85.887  1.00 28.48 ?  561 LEU A CA    1 
ATOM   4509  C  C     . LEU A 1 561 ? 150.273 151.846 87.095  1.00 28.17 ?  561 LEU A C     1 
ATOM   4510  O  O     . LEU A 1 561 ? 149.720 152.543 87.951  1.00 30.26 ?  561 LEU A O     1 
ATOM   4511  C  CB    . LEU A 1 561 ? 148.958 149.935 86.142  1.00 28.29 ?  561 LEU A CB    1 
ATOM   4512  C  CG    . LEU A 1 561 ? 148.055 149.803 87.371  1.00 29.77 ?  561 LEU A CG    1 
ATOM   4513  C  CD1   . LEU A 1 561 ? 146.878 150.755 87.261  1.00 26.57 ?  561 LEU A CD1   1 
ATOM   4514  C  CD2   . LEU A 1 561 ? 147.577 148.376 87.551  1.00 24.71 ?  561 LEU A CD2   1 
ATOM   4515  N  N     . LYS A 1 562 ? 151.555 151.489 87.188  1.00 29.68 ?  562 LYS A N     1 
ATOM   4516  C  CA    . LYS A 1 562 ? 152.392 151.984 88.276  1.00 30.82 ?  562 LYS A CA    1 
ATOM   4517  C  C     . LYS A 1 562 ? 152.526 153.500 88.220  1.00 35.47 ?  562 LYS A C     1 
ATOM   4518  O  O     . LYS A 1 562 ? 152.430 154.179 89.248  1.00 35.60 ?  562 LYS A O     1 
ATOM   4519  C  CB    . LYS A 1 562 ? 153.766 151.317 88.215  1.00 28.95 ?  562 LYS A CB    1 
ATOM   4520  C  CG    . LYS A 1 562 ? 154.788 151.875 89.185  1.00 29.87 ?  562 LYS A CG    1 
ATOM   4521  C  CD    . LYS A 1 562 ? 156.167 151.310 88.892  1.00 30.17 ?  562 LYS A CD    1 
ATOM   4522  C  CE    . LYS A 1 562 ? 157.206 151.835 89.864  1.00 32.22 ?  562 LYS A CE    1 
ATOM   4523  N  NZ    . LYS A 1 562 ? 158.413 150.966 89.895  1.00 34.97 1  562 LYS A NZ    1 
ATOM   4524  N  N     . ALA A 1 563 ? 152.738 154.048 87.020  1.00 34.18 ?  563 ALA A N     1 
ATOM   4525  C  CA    . ALA A 1 563 ? 152.804 155.500 86.874  1.00 31.91 ?  563 ALA A CA    1 
ATOM   4526  C  C     . ALA A 1 563 ? 151.469 156.150 87.222  1.00 31.32 ?  563 ALA A C     1 
ATOM   4527  O  O     . ALA A 1 563 ? 151.432 157.212 87.855  1.00 37.17 ?  563 ALA A O     1 
ATOM   4528  C  CB    . ALA A 1 563 ? 153.227 155.864 85.450  1.00 33.30 ?  563 ALA A CB    1 
ATOM   4529  N  N     . PHE A 1 564 ? 150.363 155.526 86.813  1.00 33.10 ?  564 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 564 ? 149.041 156.056 87.129  1.00 30.55 ?  564 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 564 ? 148.796 156.071 88.632  1.00 31.17 ?  564 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 564 ? 148.233 157.031 89.169  1.00 35.80 ?  564 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 564 ? 147.973 155.228 86.414  1.00 30.41 ?  564 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 564 ? 146.620 155.875 86.377  1.00 30.40 ?  564 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 564 ? 146.298 156.783 85.385  1.00 32.82 ?  564 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 564 ? 145.664 155.562 87.327  1.00 33.53 ?  564 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 564 ? 145.051 157.375 85.347  1.00 38.30 ?  564 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 564 ? 144.416 156.151 87.295  1.00 34.07 ?  564 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 564 ? 144.108 157.058 86.304  1.00 36.68 ?  564 PHE A CZ    1 
ATOM   4540  N  N     . VAL A 1 565 ? 149.208 155.010 89.327  1.00 32.53 ?  565 VAL A N     1 
ATOM   4541  C  CA    . VAL A 1 565 ? 149.058 154.956 90.778  1.00 27.22 ?  565 VAL A CA    1 
ATOM   4542  C  C     . VAL A 1 565 ? 149.950 155.994 91.445  1.00 31.96 ?  565 VAL A C     1 
ATOM   4543  O  O     . VAL A 1 565 ? 149.554 156.635 92.426  1.00 36.49 ?  565 VAL A O     1 
ATOM   4544  C  CB    . VAL A 1 565 ? 149.355 153.534 91.288  1.00 26.89 ?  565 VAL A CB    1 
ATOM   4545  C  CG1   . VAL A 1 565 ? 149.554 153.526 92.795  1.00 28.44 ?  565 VAL A CG1   1 
ATOM   4546  C  CG2   . VAL A 1 565 ? 148.232 152.596 90.897  1.00 30.95 ?  565 VAL A CG2   1 
ATOM   4547  N  N     . ALA A 1 566 ? 151.162 156.186 90.923  1.00 35.27 ?  566 ALA A N     1 
ATOM   4548  C  CA    . ALA A 1 566 ? 152.048 157.207 91.472  1.00 33.21 ?  566 ALA A CA    1 
ATOM   4549  C  C     . ALA A 1 566 ? 151.446 158.598 91.320  1.00 36.36 ?  566 ALA A C     1 
ATOM   4550  O  O     . ALA A 1 566 ? 151.540 159.429 92.232  1.00 36.75 ?  566 ALA A O     1 
ATOM   4551  C  CB    . ALA A 1 566 ? 153.415 157.135 90.794  1.00 32.08 ?  566 ALA A CB    1 
ATOM   4552  N  N     . GLU A 1 567 ? 150.823 158.872 90.173  1.00 36.78 ?  567 GLU A N     1 
ATOM   4553  C  CA    . GLU A 1 567 ? 150.259 160.198 89.937  1.00 35.42 ?  567 GLU A CA    1 
ATOM   4554  C  C     . GLU A 1 567 ? 148.975 160.420 90.732  1.00 38.61 ?  567 GLU A C     1 
ATOM   4555  O  O     . GLU A 1 567 ? 148.766 161.505 91.286  1.00 41.33 ?  567 GLU A O     1 
ATOM   4556  C  CB    . GLU A 1 567 ? 150.005 160.403 88.445  1.00 37.27 ?  567 GLU A CB    1 
ATOM   4557  C  CG    . GLU A 1 567 ? 151.104 161.174 87.729  1.00 42.63 ?  567 GLU A CG    1 
ATOM   4558  C  CD    . GLU A 1 567 ? 152.428 160.436 87.717  1.00 45.29 ?  567 GLU A CD    1 
ATOM   4559  O  OE1   . GLU A 1 567 ? 153.304 160.768 88.544  1.00 42.73 ?  567 GLU A OE1   1 
ATOM   4560  O  OE2   . GLU A 1 567 ? 152.599 159.530 86.874  1.00 42.47 -1 567 GLU A OE2   1 
ATOM   4561  N  N     . HIS A 1 568 ? 148.106 159.409 90.805  1.00 39.00 ?  568 HIS A N     1 
ATOM   4562  C  CA    . HIS A 1 568 ? 146.764 159.589 91.341  1.00 36.41 ?  568 HIS A CA    1 
ATOM   4563  C  C     . HIS A 1 568 ? 146.523 158.901 92.677  1.00 35.41 ?  568 HIS A C     1 
ATOM   4564  O  O     . HIS A 1 568 ? 145.534 159.219 93.344  1.00 41.18 ?  568 HIS A O     1 
ATOM   4565  C  CB    . HIS A 1 568 ? 145.723 159.089 90.329  1.00 33.87 ?  568 HIS A CB    1 
ATOM   4566  C  CG    . HIS A 1 568 ? 145.624 159.932 89.098  1.00 38.50 ?  568 HIS A CG    1 
ATOM   4567  N  ND1   . HIS A 1 568 ? 145.358 161.284 89.142  1.00 36.84 ?  568 HIS A ND1   1 
ATOM   4568  C  CD2   . HIS A 1 568 ? 145.760 159.618 87.788  1.00 37.26 ?  568 HIS A CD2   1 
ATOM   4569  C  CE1   . HIS A 1 568 ? 145.332 161.765 87.912  1.00 40.24 ?  568 HIS A CE1   1 
ATOM   4570  N  NE2   . HIS A 1 568 ? 145.572 160.776 87.072  1.00 40.01 ?  568 HIS A NE2   1 
ATOM   4571  N  N     . GLY A 1 569 ? 147.385 157.980 93.089  1.00 28.17 ?  569 GLY A N     1 
ATOM   4572  C  CA    . GLY A 1 569 ? 147.160 157.263 94.323  1.00 28.04 ?  569 GLY A CA    1 
ATOM   4573  C  C     . GLY A 1 569 ? 146.228 156.079 94.144  1.00 28.41 ?  569 GLY A C     1 
ATOM   4574  O  O     . GLY A 1 569 ? 145.837 155.708 93.036  1.00 34.15 ?  569 GLY A O     1 
ATOM   4575  N  N     . MET A 1 570 ? 145.874 155.475 95.275  1.00 25.27 ?  570 MET A N     1 
ATOM   4576  C  CA    . MET A 1 570 ? 144.985 154.321 95.303  1.00 25.78 ?  570 MET A CA    1 
ATOM   4577  C  C     . MET A 1 570 ? 143.941 154.532 96.387  1.00 24.58 ?  570 MET A C     1 
ATOM   4578  O  O     . MET A 1 570 ? 144.282 154.879 97.521  1.00 27.32 ?  570 MET A O     1 
ATOM   4579  C  CB    . MET A 1 570 ? 145.770 153.028 95.548  1.00 24.02 ?  570 MET A CB    1 
ATOM   4580  C  CG    . MET A 1 570 ? 146.313 152.392 94.277  1.00 20.26 ?  570 MET A CG    1 
ATOM   4581  S  SD    . MET A 1 570 ? 146.567 150.615 94.408  1.00 39.13 ?  570 MET A SD    1 
ATOM   4582  C  CE    . MET A 1 570 ? 145.388 150.194 95.682  1.00 25.71 ?  570 MET A CE    1 
ATOM   4583  N  N     . TYR A 1 571 ? 142.671 154.323 96.036  1.00 21.91 ?  571 TYR A N     1 
ATOM   4584  C  CA    . TYR A 1 571 ? 141.585 154.598 96.969  1.00 14.14 ?  571 TYR A CA    1 
ATOM   4585  C  C     . TYR A 1 571 ? 141.476 153.550 98.069  1.00 20.21 ?  571 TYR A C     1 
ATOM   4586  O  O     . TYR A 1 571 ? 141.147 153.892 99.210  1.00 24.53 ?  571 TYR A O     1 
ATOM   4587  C  CB    . TYR A 1 571 ? 140.258 154.695 96.217  1.00 22.96 ?  571 TYR A CB    1 
ATOM   4588  C  CG    . TYR A 1 571 ? 139.116 155.207 97.064  1.00 24.15 ?  571 TYR A CG    1 
ATOM   4589  C  CD1   . TYR A 1 571 ? 138.984 156.561 97.335  1.00 23.12 ?  571 TYR A CD1   1 
ATOM   4590  C  CD2   . TYR A 1 571 ? 138.176 154.337 97.597  1.00 18.53 ?  571 TYR A CD2   1 
ATOM   4591  C  CE1   . TYR A 1 571 ? 137.945 157.034 98.110  1.00 22.43 ?  571 TYR A CE1   1 
ATOM   4592  C  CE2   . TYR A 1 571 ? 137.135 154.801 98.374  1.00 19.81 ?  571 TYR A CE2   1 
ATOM   4593  C  CZ    . TYR A 1 571 ? 137.022 156.150 98.625  1.00 25.46 ?  571 TYR A CZ    1 
ATOM   4594  O  OH    . TYR A 1 571 ? 135.987 156.619 99.398  1.00 28.14 ?  571 TYR A OH    1 
ATOM   4595  N  N     . HIS A 1 572 ? 141.744 152.286 97.758  1.00 22.73 ?  572 HIS A N     1 
ATOM   4596  C  CA    . HIS A 1 572 ? 141.582 151.197 98.710  1.00 13.70 ?  572 HIS A CA    1 
ATOM   4597  C  C     . HIS A 1 572 ? 142.941 150.753 99.230  1.00 10.41 ?  572 HIS A C     1 
ATOM   4598  O  O     . HIS A 1 572 ? 143.865 150.519 98.446  1.00 22.35 ?  572 HIS A O     1 
ATOM   4599  C  CB    . HIS A 1 572 ? 140.858 150.011 98.071  1.00 14.68 ?  572 HIS A CB    1 
ATOM   4600  C  CG    . HIS A 1 572 ? 139.607 150.386 97.340  1.00 15.57 ?  572 HIS A CG    1 
ATOM   4601  N  ND1   . HIS A 1 572 ? 139.594 150.693 95.997  1.00 16.85 ?  572 HIS A ND1   1 
ATOM   4602  C  CD2   . HIS A 1 572 ? 138.326 150.500 97.764  1.00 9.72  ?  572 HIS A CD2   1 
ATOM   4603  C  CE1   . HIS A 1 572 ? 138.361 150.982 95.625  1.00 16.23 ?  572 HIS A CE1   1 
ATOM   4604  N  NE2   . HIS A 1 572 ? 137.572 150.873 96.678  1.00 23.78 ?  572 HIS A NE2   1 
ATOM   4605  N  N     . SER A 1 573 ? 143.059 150.646 100.554 1.00 5.57  ?  573 SER A N     1 
ATOM   4606  C  CA    . SER A 1 573 ? 144.265 150.072 101.139 1.00 7.60  ?  573 SER A CA    1 
ATOM   4607  C  C     . SER A 1 573 ? 144.403 148.603 100.770 1.00 11.79 ?  573 SER A C     1 
ATOM   4608  O  O     . SER A 1 573 ? 145.513 148.119 100.519 1.00 19.77 ?  573 SER A O     1 
ATOM   4609  C  CB    . SER A 1 573 ? 144.244 150.247 102.655 1.00 15.52 ?  573 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 573 ? 143.063 149.699 103.207 1.00 22.99 ?  573 SER A OG    1 
ATOM   4611  N  N     . TYR A 1 574 ? 143.287 147.878 100.739 1.00 12.39 ?  574 TYR A N     1 
ATOM   4612  C  CA    . TYR A 1 574 ? 143.261 146.478 100.346 1.00 1.15  ?  574 TYR A CA    1 
ATOM   4613  C  C     . TYR A 1 574 ? 142.087 146.262 99.407  1.00 8.90  ?  574 TYR A C     1 
ATOM   4614  O  O     . TYR A 1 574 ? 141.028 146.872 99.581  1.00 16.56 ?  574 TYR A O     1 
ATOM   4615  C  CB    . TYR A 1 574 ? 143.158 145.560 101.569 1.00 11.68 ?  574 TYR A CB    1 
ATOM   4616  C  CG    . TYR A 1 574 ? 144.229 145.828 102.601 1.00 8.23  ?  574 TYR A CG    1 
ATOM   4617  C  CD1   . TYR A 1 574 ? 144.042 146.789 103.584 1.00 10.27 ?  574 TYR A CD1   1 
ATOM   4618  C  CD2   . TYR A 1 574 ? 145.427 145.131 102.586 1.00 8.46  ?  574 TYR A CD2   1 
ATOM   4619  C  CE1   . TYR A 1 574 ? 145.016 147.049 104.520 1.00 6.62  ?  574 TYR A CE1   1 
ATOM   4620  C  CE2   . TYR A 1 574 ? 146.407 145.382 103.522 1.00 11.12 ?  574 TYR A CE2   1 
ATOM   4621  C  CZ    . TYR A 1 574 ? 146.194 146.343 104.488 1.00 5.82  ?  574 TYR A CZ    1 
ATOM   4622  O  OH    . TYR A 1 574 ? 147.164 146.598 105.426 1.00 18.04 ?  574 TYR A OH    1 
ATOM   4623  N  N     . ARG A 1 575 ? 142.277 145.401 98.414  1.00 11.09 ?  575 ARG A N     1 
ATOM   4624  C  CA    . ARG A 1 575 ? 141.284 145.206 97.366  1.00 4.65  ?  575 ARG A CA    1 
ATOM   4625  C  C     . ARG A 1 575 ? 140.810 143.770 97.230  1.00 9.69  ?  575 ARG A C     1 
ATOM   4626  O  O     . ARG A 1 575 ? 139.616 143.540 97.027  1.00 19.78 ?  575 ARG A O     1 
ATOM   4627  C  CB    . ARG A 1 575 ? 141.847 145.670 96.018  1.00 17.10 ?  575 ARG A CB    1 
ATOM   4628  C  CG    . ARG A 1 575 ? 142.198 147.142 95.952  1.00 11.51 ?  575 ARG A CG    1 
ATOM   4629  C  CD    . ARG A 1 575 ? 143.273 147.385 94.909  1.00 11.59 ?  575 ARG A CD    1 
ATOM   4630  N  NE    . ARG A 1 575 ? 144.557 146.832 95.320  1.00 16.30 ?  575 ARG A NE    1 
ATOM   4631  C  CZ    . ARG A 1 575 ? 145.074 145.703 94.852  1.00 14.92 ?  575 ARG A CZ    1 
ATOM   4632  N  NH1   . ARG A 1 575 ? 144.445 144.982 93.940  1.00 12.79 1  575 ARG A NH1   1 
ATOM   4633  N  NH2   . ARG A 1 575 ? 146.252 145.291 95.309  1.00 14.91 ?  575 ARG A NH2   1 
ATOM   4634  N  N     . LEU A 1 576 ? 141.709 142.795 97.334  1.00 19.64 ?  576 LEU A N     1 
ATOM   4635  C  CA    . LEU A 1 576 ? 141.405 141.413 96.995  1.00 12.26 ?  576 LEU A CA    1 
ATOM   4636  C  C     . LEU A 1 576 ? 141.597 140.520 98.210  1.00 3.41  ?  576 LEU A C     1 
ATOM   4637  O  O     . LEU A 1 576 ? 142.652 140.556 98.851  1.00 19.60 ?  576 LEU A O     1 
ATOM   4638  C  CB    . LEU A 1 576 ? 142.296 140.926 95.848  1.00 4.91  ?  576 LEU A CB    1 
ATOM   4639  C  CG    . LEU A 1 576 ? 142.385 141.819 94.610  1.00 8.38  ?  576 LEU A CG    1 
ATOM   4640  C  CD1   . LEU A 1 576 ? 143.448 141.296 93.662  1.00 11.87 ?  576 LEU A CD1   1 
ATOM   4641  C  CD2   . LEU A 1 576 ? 141.043 141.914 93.910  1.00 10.83 ?  576 LEU A CD2   1 
ATOM   4642  N  N     . CYS A 1 577 ? 140.577 139.725 98.522  1.00 1.85  ?  577 CYS A N     1 
ATOM   4643  C  CA    . CYS A 1 577 ? 140.696 138.646 99.492  1.00 6.52  ?  577 CYS A CA    1 
ATOM   4644  C  C     . CYS A 1 577 ? 139.710 137.561 99.089  1.00 16.04 ?  577 CYS A C     1 
ATOM   4645  O  O     . CYS A 1 577 ? 138.567 137.863 98.738  1.00 21.38 ?  577 CYS A O     1 
ATOM   4646  C  CB    . CYS A 1 577 ? 140.434 139.129 100.926 1.00 5.82  ?  577 CYS A CB    1 
ATOM   4647  S  SG    . CYS A 1 577 ? 138.701 139.258 101.429 1.00 27.63 ?  577 CYS A SG    1 
ATOM   4648  N  N     . ILE A 1 578 ? 140.157 136.311 99.118  1.00 8.13  ?  578 ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 578 ? 139.363 135.185 98.641  1.00 11.51 ?  578 ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 578 ? 138.732 134.520 99.858  1.00 8.57  ?  578 ILE A C     1 
ATOM   4651  O  O     . ILE A 1 578 ? 139.391 133.786 100.597 1.00 10.89 ?  578 ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 578 ? 140.205 134.205 97.822  1.00 12.84 ?  578 ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 578 ? 140.908 134.946 96.683  1.00 0.32  ?  578 ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 578 ? 139.333 133.097 97.265  1.00 8.42  ?  578 ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 578 ? 141.486 134.038 95.633  1.00 9.81  ?  578 ILE A CD1   1 
ATOM   4656  N  N     . ALA A 1 579 ? 137.446 134.779 100.060 1.00 16.56 ?  579 ALA A N     1 
ATOM   4657  C  CA    . ALA A 1 579 ? 136.634 134.240 101.139 1.00 8.89  ?  579 ALA A CA    1 
ATOM   4658  C  C     . ALA A 1 579 ? 136.143 132.840 100.789 1.00 16.81 ?  579 ALA A C     1 
ATOM   4659  O  O     . ALA A 1 579 ? 136.142 132.445 99.620  1.00 21.14 ?  579 ALA A O     1 
ATOM   4660  C  CB    . ALA A 1 579 ? 135.451 135.166 101.409 1.00 13.01 ?  579 ALA A CB    1 
ATOM   4661  N  N     . PRO A 1 580 ? 135.740 132.049 101.790 1.00 24.08 ?  580 PRO A N     1 
ATOM   4662  C  CA    . PRO A 1 580 ? 135.252 130.690 101.495 1.00 20.95 ?  580 PRO A CA    1 
ATOM   4663  C  C     . PRO A 1 580 ? 134.028 130.645 100.591 1.00 25.56 ?  580 PRO A C     1 
ATOM   4664  O  O     . PRO A 1 580 ? 133.880 129.678 99.831  1.00 31.34 ?  580 PRO A O     1 
ATOM   4665  C  CB    . PRO A 1 580 ? 134.947 130.114 102.887 1.00 17.28 ?  580 PRO A CB    1 
ATOM   4666  C  CG    . PRO A 1 580 ? 134.939 131.285 103.815 1.00 20.67 ?  580 PRO A CG    1 
ATOM   4667  C  CD    . PRO A 1 580 ? 135.890 132.270 103.237 1.00 20.22 ?  580 PRO A CD    1 
ATOM   4668  N  N     . THR A 1 581 ? 133.149 131.645 100.651 1.00 21.90 ?  581 THR A N     1 
ATOM   4669  C  CA    . THR A 1 581 ? 131.932 131.703 99.834  1.00 27.67 ?  581 THR A CA    1 
ATOM   4670  C  C     . THR A 1 581 ? 131.073 130.451 100.043 1.00 31.22 ?  581 THR A C     1 
ATOM   4671  O  O     . THR A 1 581 ? 130.876 129.631 99.147  1.00 32.14 ?  581 THR A O     1 
ATOM   4672  C  CB    . THR A 1 581 ? 132.257 131.894 98.348  1.00 27.73 ?  581 THR A CB    1 
ATOM   4673  O  OG1   . THR A 1 581 ? 132.646 130.641 97.772  1.00 23.00 ?  581 THR A OG1   1 
ATOM   4674  C  CG2   . THR A 1 581 ? 133.370 132.907 98.162  1.00 28.64 ?  581 THR A CG2   1 
ATOM   4675  N  N     . GLY A 1 582 ? 130.565 130.332 101.267 1.00 28.49 ?  582 GLY A N     1 
ATOM   4676  C  CA    . GLY A 1 582 ? 129.844 129.145 101.682 1.00 31.03 ?  582 GLY A CA    1 
ATOM   4677  C  C     . GLY A 1 582 ? 128.577 128.835 100.910 1.00 34.80 ?  582 GLY A C     1 
ATOM   4678  O  O     . GLY A 1 582 ? 128.523 127.839 100.181 1.00 33.60 ?  582 GLY A O     1 
ATOM   4679  N  N     . SER A 1 583 ? 127.550 129.672 101.052 1.00 34.42 ?  583 SER A N     1 
ATOM   4680  C  CA    . SER A 1 583 ? 126.244 129.381 100.472 1.00 38.66 ?  583 SER A CA    1 
ATOM   4681  C  C     . SER A 1 583 ? 125.974 130.115 99.168  1.00 35.70 ?  583 SER A C     1 
ATOM   4682  O  O     . SER A 1 583 ? 125.131 129.664 98.386  1.00 34.27 ?  583 SER A O     1 
ATOM   4683  C  CB    . SER A 1 583 ? 125.131 129.717 101.472 1.00 40.58 ?  583 SER A CB    1 
ATOM   4684  O  OG    . SER A 1 583 ? 125.071 128.753 102.509 1.00 41.67 ?  583 SER A OG    1 
ATOM   4685  N  N     . ILE A 1 584 ? 126.656 131.234 98.910  1.00 32.67 ?  584 ILE A N     1 
ATOM   4686  C  CA    . ILE A 1 584 ? 126.457 131.939 97.650  1.00 26.88 ?  584 ILE A CA    1 
ATOM   4687  C  C     . ILE A 1 584 ? 126.975 131.133 96.467  1.00 29.09 ?  584 ILE A C     1 
ATOM   4688  O  O     . ILE A 1 584 ? 126.548 131.366 95.331  1.00 36.37 ?  584 ILE A O     1 
ATOM   4689  C  CB    . ILE A 1 584 ? 127.120 133.329 97.687  1.00 33.33 ?  584 ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1 584 ? 128.608 133.208 98.025  1.00 34.20 ?  584 ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1 584 ? 126.398 134.239 98.669  1.00 34.09 ?  584 ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1 584 ? 129.248 134.509 98.460  1.00 28.91 ?  584 ILE A CD1   1 
ATOM   4693  N  N     . SER A 1 585 ? 127.890 130.191 96.702  1.00 30.54 ?  585 SER A N     1 
ATOM   4694  C  CA    . SER A 1 585 ? 128.366 129.338 95.618  1.00 27.64 ?  585 SER A CA    1 
ATOM   4695  C  C     . SER A 1 585 ? 127.263 128.425 95.101  1.00 26.77 ?  585 SER A C     1 
ATOM   4696  O  O     . SER A 1 585 ? 127.273 128.048 93.925  1.00 27.43 ?  585 SER A O     1 
ATOM   4697  C  CB    . SER A 1 585 ? 129.566 128.516 96.083  1.00 24.39 ?  585 SER A CB    1 
ATOM   4698  O  OG    . SER A 1 585 ? 129.233 127.719 97.206  1.00 31.13 ?  585 SER A OG    1 
ATOM   4699  N  N     . TYR A 1 586 ? 126.314 128.052 95.963  1.00 34.80 ?  586 TYR A N     1 
ATOM   4700  C  CA    . TYR A 1 586 ? 125.167 127.271 95.513  1.00 33.30 ?  586 TYR A CA    1 
ATOM   4701  C  C     . TYR A 1 586 ? 124.292 128.086 94.571  1.00 31.89 ?  586 TYR A C     1 
ATOM   4702  O  O     . TYR A 1 586 ? 123.952 127.630 93.474  1.00 35.40 ?  586 TYR A O     1 
ATOM   4703  C  CB    . TYR A 1 586 ? 124.350 126.799 96.715  1.00 32.22 ?  586 TYR A CB    1 
ATOM   4704  C  CG    . TYR A 1 586 ? 124.986 125.688 97.515  1.00 30.72 ?  586 TYR A CG    1 
ATOM   4705  C  CD1   . TYR A 1 586 ? 125.332 125.880 98.846  1.00 33.44 ?  586 TYR A CD1   1 
ATOM   4706  C  CD2   . TYR A 1 586 ? 125.230 124.445 96.948  1.00 34.07 ?  586 TYR A CD2   1 
ATOM   4707  C  CE1   . TYR A 1 586 ? 125.911 124.870 99.586  1.00 35.12 ?  586 TYR A CE1   1 
ATOM   4708  C  CE2   . TYR A 1 586 ? 125.808 123.428 97.683  1.00 34.78 ?  586 TYR A CE2   1 
ATOM   4709  C  CZ    . TYR A 1 586 ? 126.145 123.646 99.001  1.00 36.82 ?  586 TYR A CZ    1 
ATOM   4710  O  OH    . TYR A 1 586 ? 126.722 122.638 99.738  1.00 38.57 ?  586 TYR A OH    1 
ATOM   4711  N  N     . VAL A 1 587 ? 123.930 129.304 94.982  1.00 29.42 ?  587 VAL A N     1 
ATOM   4712  C  CA    . VAL A 1 587 ? 123.036 130.143 94.189  1.00 27.19 ?  587 VAL A CA    1 
ATOM   4713  C  C     . VAL A 1 587 ? 123.661 130.467 92.840  1.00 29.12 ?  587 VAL A C     1 
ATOM   4714  O  O     . VAL A 1 587 ? 122.970 130.526 91.815  1.00 34.89 ?  587 VAL A O     1 
ATOM   4715  C  CB    . VAL A 1 587 ? 122.678 131.420 94.969  1.00 31.21 ?  587 VAL A CB    1 
ATOM   4716  C  CG1   . VAL A 1 587 ? 121.700 132.270 94.181  1.00 31.59 ?  587 VAL A CG1   1 
ATOM   4717  C  CG2   . VAL A 1 587 ? 122.107 131.065 96.332  1.00 33.64 ?  587 VAL A CG2   1 
ATOM   4718  N  N     . GLN A 1 588 ? 124.973 130.676 92.815  1.00 31.49 ?  588 GLN A N     1 
ATOM   4719  C  CA    . GLN A 1 588 ? 125.680 130.972 91.578  1.00 26.60 ?  588 GLN A CA    1 
ATOM   4720  C  C     . GLN A 1 588 ? 126.016 129.723 90.779  1.00 28.18 ?  588 GLN A C     1 
ATOM   4721  O  O     . GLN A 1 588 ? 126.597 129.846 89.694  1.00 29.80 ?  588 GLN A O     1 
ATOM   4722  C  CB    . GLN A 1 588 ? 126.961 131.750 91.882  1.00 24.80 ?  588 GLN A CB    1 
ATOM   4723  C  CG    . GLN A 1 588 ? 126.719 133.158 92.387  1.00 23.53 ?  588 GLN A CG    1 
ATOM   4724  C  CD    . GLN A 1 588 ? 126.817 134.189 91.284  1.00 26.75 ?  588 GLN A CD    1 
ATOM   4725  O  OE1   . GLN A 1 588 ? 127.656 134.081 90.392  1.00 24.74 ?  588 GLN A OE1   1 
ATOM   4726  N  NE2   . GLN A 1 588 ? 125.960 135.200 91.342  1.00 32.10 ?  588 GLN A NE2   1 
ATOM   4727  N  N     . SER A 1 589 ? 125.658 128.542 91.280  1.00 29.68 ?  589 SER A N     1 
ATOM   4728  C  CA    . SER A 1 589 ? 126.014 127.266 90.664  1.00 26.27 ?  589 SER A CA    1 
ATOM   4729  C  C     . SER A 1 589 ? 127.515 127.216 90.385  1.00 28.13 ?  589 SER A C     1 
ATOM   4730  O  O     . SER A 1 589 ? 127.971 127.100 89.246  1.00 30.35 ?  589 SER A O     1 
ATOM   4731  C  CB    . SER A 1 589 ? 125.196 127.019 89.393  1.00 28.07 ?  589 SER A CB    1 
ATOM   4732  O  OG    . SER A 1 589 ? 125.719 127.742 88.294  1.00 34.21 ?  589 SER A OG    1 
ATOM   4733  N  N     . SER A 1 590 ? 128.282 127.317 91.467  1.00 27.77 ?  590 SER A N     1 
ATOM   4734  C  CA    . SER A 1 590 ? 129.727 127.425 91.387  1.00 22.98 ?  590 SER A CA    1 
ATOM   4735  C  C     . SER A 1 590 ? 130.357 126.606 92.502  1.00 24.82 ?  590 SER A C     1 
ATOM   4736  O  O     . SER A 1 590 ? 129.734 126.337 93.532  1.00 29.39 ?  590 SER A O     1 
ATOM   4737  C  CB    . SER A 1 590 ? 130.181 128.887 91.487  1.00 22.09 ?  590 SER A CB    1 
ATOM   4738  O  OG    . SER A 1 590 ? 130.478 129.237 92.825  1.00 29.32 ?  590 SER A OG    1 
ATOM   4739  N  N     . THR A 1 591 ? 131.603 126.201 92.280  1.00 23.96 ?  591 THR A N     1 
ATOM   4740  C  CA    . THR A 1 591 ? 132.382 125.574 93.333  1.00 24.18 ?  591 THR A CA    1 
ATOM   4741  C  C     . THR A 1 591 ? 132.854 126.631 94.325  1.00 23.05 ?  591 THR A C     1 
ATOM   4742  O  O     . THR A 1 591 ? 133.089 127.788 93.966  1.00 17.67 ?  591 THR A O     1 
ATOM   4743  C  CB    . THR A 1 591 ? 133.576 124.817 92.750  1.00 26.23 ?  591 THR A CB    1 
ATOM   4744  O  OG1   . THR A 1 591 ? 134.554 125.748 92.275  1.00 30.00 ?  591 THR A OG1   1 
ATOM   4745  C  CG2   . THR A 1 591 ? 133.126 123.937 91.597  1.00 25.88 ?  591 THR A CG2   1 
ATOM   4746  N  N     . ALA A 1 592 ? 132.984 126.223 95.584  1.00 22.30 ?  592 ALA A N     1 
ATOM   4747  C  CA    . ALA A 1 592 ? 133.245 127.179 96.651  1.00 22.38 ?  592 ALA A CA    1 
ATOM   4748  C  C     . ALA A 1 592 ? 134.672 127.703 96.576  1.00 22.73 ?  592 ALA A C     1 
ATOM   4749  O  O     . ALA A 1 592 ? 135.632 126.926 96.590  1.00 27.19 ?  592 ALA A O     1 
ATOM   4750  C  CB    . ALA A 1 592 ? 132.991 126.534 98.012  1.00 24.34 ?  592 ALA A CB    1 
ATOM   4751  N  N     . SER A 1 593 ? 134.803 129.022 96.501  1.00 24.21 ?  593 SER A N     1 
ATOM   4752  C  CA    . SER A 1 593 ? 136.083 129.732 96.559  1.00 16.30 ?  593 SER A CA    1 
ATOM   4753  C  C     . SER A 1 593 ? 137.006 129.210 95.457  1.00 15.94 ?  593 SER A C     1 
ATOM   4754  O  O     . SER A 1 593 ? 136.548 128.722 94.419  1.00 23.75 ?  593 SER A O     1 
ATOM   4755  C  CB    . SER A 1 593 ? 136.644 129.613 97.966  1.00 25.18 ?  593 SER A CB    1 
ATOM   4756  O  OG    . SER A 1 593 ? 137.722 130.506 98.167  1.00 24.78 ?  593 SER A OG    1 
ATOM   4757  N  N     . VAL A 1 594 ? 138.317 129.318 95.669  1.00 21.63 ?  594 VAL A N     1 
ATOM   4758  C  CA    . VAL A 1 594 ? 139.302 128.711 94.785  1.00 19.48 ?  594 VAL A CA    1 
ATOM   4759  C  C     . VAL A 1 594 ? 139.694 127.319 95.261  1.00 18.95 ?  594 VAL A C     1 
ATOM   4760  O  O     . VAL A 1 594 ? 140.631 126.721 94.724  1.00 18.36 ?  594 VAL A O     1 
ATOM   4761  C  CB    . VAL A 1 594 ? 140.541 129.608 94.638  1.00 21.54 ?  594 VAL A CB    1 
ATOM   4762  C  CG1   . VAL A 1 594 ? 140.176 130.897 93.919  1.00 9.11  ?  594 VAL A CG1   1 
ATOM   4763  C  CG2   . VAL A 1 594 ? 141.146 129.901 95.999  1.00 17.90 ?  594 VAL A CG2   1 
ATOM   4764  N  N     . MET A 1 595 ? 138.999 126.791 96.264  1.00 25.45 ?  595 MET A N     1 
ATOM   4765  C  CA    . MET A 1 595 ? 139.281 125.460 96.764  1.00 18.76 ?  595 MET A CA    1 
ATOM   4766  C  C     . MET A 1 595 ? 138.840 124.407 95.751  1.00 24.58 ?  595 MET A C     1 
ATOM   4767  O  O     . MET A 1 595 ? 137.900 124.625 94.982  1.00 32.18 ?  595 MET A O     1 
ATOM   4768  C  CB    . MET A 1 595 ? 138.556 125.224 98.087  1.00 22.37 ?  595 MET A CB    1 
ATOM   4769  C  CG    . MET A 1 595 ? 139.196 125.763 99.385  1.00 25.47 ?  595 MET A CG    1 
ATOM   4770  S  SD    . MET A 1 595 ? 140.979 125.626 99.689  1.00 31.61 ?  595 MET A SD    1 
ATOM   4771  C  CE    . MET A 1 595 ? 141.680 126.887 98.631  1.00 18.71 ?  595 MET A CE    1 
ATOM   4772  N  N     . PRO A 1 596 ? 139.509 123.258 95.723  1.00 27.55 ?  596 PRO A N     1 
ATOM   4773  C  CA    . PRO A 1 596 ? 138.982 122.120 94.966  1.00 22.18 ?  596 PRO A CA    1 
ATOM   4774  C  C     . PRO A 1 596 ? 137.744 121.548 95.641  1.00 27.22 ?  596 PRO A C     1 
ATOM   4775  O  O     . PRO A 1 596 ? 137.527 121.703 96.844  1.00 31.05 ?  596 PRO A O     1 
ATOM   4776  C  CB    . PRO A 1 596 ? 140.138 121.116 94.976  1.00 23.92 ?  596 PRO A CB    1 
ATOM   4777  C  CG    . PRO A 1 596 ? 140.947 121.482 96.173  1.00 28.34 ?  596 PRO A CG    1 
ATOM   4778  C  CD    . PRO A 1 596 ? 140.818 122.966 96.333  1.00 28.46 ?  596 PRO A CD    1 
ATOM   4779  N  N     . ILE A 1 597 ? 136.917 120.880 94.835  1.00 29.21 ?  597 ILE A N     1 
ATOM   4780  C  CA    . ILE A 1 597 ? 135.659 120.347 95.341  1.00 31.33 ?  597 ILE A CA    1 
ATOM   4781  C  C     . ILE A 1 597 ? 135.929 119.209 96.319  1.00 34.65 ?  597 ILE A C     1 
ATOM   4782  O  O     . ILE A 1 597 ? 136.850 118.401 96.140  1.00 36.12 ?  597 ILE A O     1 
ATOM   4783  C  CB    . ILE A 1 597 ? 134.757 119.883 94.182  1.00 32.00 ?  597 ILE A CB    1 
ATOM   4784  C  CG1   . ILE A 1 597 ? 135.390 118.706 93.436  1.00 31.16 ?  597 ILE A CG1   1 
ATOM   4785  C  CG2   . ILE A 1 597 ? 134.494 121.030 93.228  1.00 31.63 ?  597 ILE A CG2   1 
ATOM   4786  C  CD1   . ILE A 1 597 ? 134.393 117.833 92.716  1.00 31.93 ?  597 ILE A CD1   1 
ATOM   4787  N  N     . MET A 1 598 ? 135.121 119.154 97.378  1.00 39.86 ?  598 MET A N     1 
ATOM   4788  C  CA    . MET A 1 598 ? 135.251 118.078 98.352  1.00 38.55 ?  598 MET A CA    1 
ATOM   4789  C  C     . MET A 1 598 ? 134.617 116.789 97.844  1.00 38.59 ?  598 MET A C     1 
ATOM   4790  O  O     . MET A 1 598 ? 135.193 115.708 97.994  1.00 44.29 ?  598 MET A O     1 
ATOM   4791  C  CB    . MET A 1 598 ? 134.621 118.495 99.679  1.00 37.06 ?  598 MET A CB    1 
ATOM   4792  C  CG    . MET A 1 598 ? 135.543 119.294 100.578 1.00 35.00 ?  598 MET A CG    1 
ATOM   4793  S  SD    . MET A 1 598 ? 134.695 119.980 102.012 1.00 53.18 ?  598 MET A SD    1 
ATOM   4794  C  CE    . MET A 1 598 ? 133.593 121.148 101.222 1.00 39.51 ?  598 MET A CE    1 
ATOM   4795  N  N     . GLU A 1 599 ? 133.430 116.889 97.250  1.00 38.15 ?  599 GLU A N     1 
ATOM   4796  C  CA    . GLU A 1 599 ? 132.722 115.751 96.688  1.00 37.01 ?  599 GLU A CA    1 
ATOM   4797  C  C     . GLU A 1 599 ? 132.209 116.117 95.305  1.00 36.30 ?  599 GLU A C     1 
ATOM   4798  O  O     . GLU A 1 599 ? 131.894 117.277 95.033  1.00 40.49 ?  599 GLU A O     1 
ATOM   4799  C  CB    . GLU A 1 599 ? 131.546 115.318 97.578  1.00 38.85 ?  599 GLU A CB    1 
ATOM   4800  C  CG    . GLU A 1 599 ? 131.846 115.320 99.068  1.00 39.53 ?  599 GLU A CG    1 
ATOM   4801  C  CD    . GLU A 1 599 ? 130.607 115.543 99.913  1.00 43.17 ?  599 GLU A CD    1 
ATOM   4802  O  OE1   . GLU A 1 599 ? 130.173 116.706 100.041 1.00 40.97 ?  599 GLU A OE1   1 
ATOM   4803  O  OE2   . GLU A 1 599 ? 130.068 114.553 100.451 1.00 45.94 -1 599 GLU A OE2   1 
ATOM   4804  N  N     . ARG A 1 600 ? 132.135 115.119 94.424  1.00 38.66 ?  600 ARG A N     1 
ATOM   4805  C  CA    . ARG A 1 600 ? 131.557 115.356 93.105  1.00 35.38 ?  600 ARG A CA    1 
ATOM   4806  C  C     . ARG A 1 600 ? 130.055 115.587 93.206  1.00 34.16 ?  600 ARG A C     1 
ATOM   4807  O  O     . ARG A 1 600 ? 129.517 116.526 92.610  1.00 37.87 ?  600 ARG A O     1 
ATOM   4808  C  CB    . ARG A 1 600 ? 131.863 114.184 92.177  1.00 34.71 ?  600 ARG A CB    1 
ATOM   4809  C  CG    . ARG A 1 600 ? 133.260 114.215 91.603  1.00 35.12 ?  600 ARG A CG    1 
ATOM   4810  C  CD    . ARG A 1 600 ? 133.455 113.113 90.588  1.00 34.48 ?  600 ARG A CD    1 
ATOM   4811  N  NE    . ARG A 1 600 ? 134.801 113.110 90.030  1.00 34.15 ?  600 ARG A NE    1 
ATOM   4812  C  CZ    . ARG A 1 600 ? 135.841 112.514 90.595  1.00 37.48 ?  600 ARG A CZ    1 
ATOM   4813  N  NH1   . ARG A 1 600 ? 135.728 111.870 91.744  1.00 36.61 1  600 ARG A NH1   1 
ATOM   4814  N  NH2   . ARG A 1 600 ? 137.025 112.566 89.990  1.00 37.83 ?  600 ARG A NH2   1 
ATOM   4815  N  N     . ILE A 1 601 ? 129.365 114.733 93.955  1.00 39.12 ?  601 ILE A N     1 
ATOM   4816  C  CA    . ILE A 1 601 ? 127.957 114.910 94.280  1.00 41.28 ?  601 ILE A CA    1 
ATOM   4817  C  C     . ILE A 1 601 ? 127.841 114.889 95.796  1.00 40.35 ?  601 ILE A C     1 
ATOM   4818  O  O     . ILE A 1 601 ? 128.285 113.933 96.444  1.00 41.59 ?  601 ILE A O     1 
ATOM   4819  C  CB    . ILE A 1 601 ? 127.076 113.822 93.648  1.00 40.71 ?  601 ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1 601 ? 127.334 113.732 92.143  1.00 41.03 ?  601 ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1 601 ? 125.608 114.105 93.918  1.00 37.03 ?  601 ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1 601 ? 126.705 112.524 91.491  1.00 39.55 ?  601 ILE A CD1   1 
ATOM   4823  N  N     . GLU A 1 602 ? 127.254 115.938 96.361  1.00 45.16 ?  602 GLU A N     1 
ATOM   4824  C  CA    . GLU A 1 602 ? 127.105 116.056 97.802  1.00 47.44 ?  602 GLU A CA    1 
ATOM   4825  C  C     . GLU A 1 602 ? 125.680 115.719 98.219  1.00 48.63 ?  602 GLU A C     1 
ATOM   4826  O  O     . GLU A 1 602 ? 124.711 116.158 97.593  1.00 48.67 ?  602 GLU A O     1 
ATOM   4827  C  CB    . GLU A 1 602 ? 127.481 117.460 98.283  1.00 45.19 ?  602 GLU A CB    1 
ATOM   4828  C  CG    . GLU A 1 602 ? 126.777 118.588 97.560  1.00 47.09 ?  602 GLU A CG    1 
ATOM   4829  C  CD    . GLU A 1 602 ? 127.023 119.935 98.209  1.00 50.58 ?  602 GLU A CD    1 
ATOM   4830  O  OE1   . GLU A 1 602 ? 128.123 120.494 98.022  1.00 50.27 ?  602 GLU A OE1   1 
ATOM   4831  O  OE2   . GLU A 1 602 ? 126.115 120.434 98.906  1.00 51.85 -1 602 GLU A OE2   1 
ATOM   4832  N  N     . GLU A 1 603 ? 125.567 114.922 99.276  1.00 56.87 ?  603 GLU A N     1 
ATOM   4833  C  CA    . GLU A 1 603 ? 124.288 114.507 99.834  1.00 57.73 ?  603 GLU A CA    1 
ATOM   4834  C  C     . GLU A 1 603 ? 123.980 115.345 101.066 1.00 57.59 ?  603 GLU A C     1 
ATOM   4835  O  O     . GLU A 1 603 ? 124.791 115.414 101.994 1.00 57.50 ?  603 GLU A O     1 
ATOM   4836  C  CB    . GLU A 1 603 ? 124.318 113.022 100.198 1.00 57.17 ?  603 GLU A CB    1 
ATOM   4837  C  CG    . GLU A 1 603 ? 123.024 112.493 100.783 1.00 58.95 ?  603 GLU A CG    1 
ATOM   4838  C  CD    . GLU A 1 603 ? 123.254 111.378 101.782 1.00 60.15 ?  603 GLU A CD    1 
ATOM   4839  O  OE1   . GLU A 1 603 ? 123.543 111.683 102.958 1.00 60.48 ?  603 GLU A OE1   1 
ATOM   4840  O  OE2   . GLU A 1 603 ? 123.146 110.198 101.393 1.00 59.56 -1 603 GLU A OE2   1 
ATOM   4841  N  N     . ARG A 1 604 ? 122.810 115.979 101.073 1.00 58.62 ?  604 ARG A N     1 
ATOM   4842  C  CA    . ARG A 1 604 ? 122.398 116.821 102.185 1.00 59.06 ?  604 ARG A CA    1 
ATOM   4843  C  C     . ARG A 1 604 ? 121.032 116.379 102.686 1.00 59.92 ?  604 ARG A C     1 
ATOM   4844  O  O     . ARG A 1 604 ? 120.247 115.776 101.951 1.00 59.33 ?  604 ARG A O     1 
ATOM   4845  C  CB    . ARG A 1 604 ? 122.360 118.302 101.790 1.00 58.99 ?  604 ARG A CB    1 
ATOM   4846  C  CG    . ARG A 1 604 ? 123.683 118.833 101.268 1.00 58.38 ?  604 ARG A CG    1 
ATOM   4847  C  CD    . ARG A 1 604 ? 124.515 119.434 102.388 1.00 58.50 ?  604 ARG A CD    1 
ATOM   4848  N  NE    . ARG A 1 604 ? 125.548 118.515 102.851 1.00 58.72 ?  604 ARG A NE    1 
ATOM   4849  C  CZ    . ARG A 1 604 ? 126.780 118.467 102.365 1.00 59.29 ?  604 ARG A CZ    1 
ATOM   4850  N  NH1   . ARG A 1 604 ? 127.173 119.274 101.394 1.00 57.85 1  604 ARG A NH1   1 
ATOM   4851  N  NH2   . ARG A 1 604 ? 127.641 117.583 102.865 1.00 57.26 ?  604 ARG A NH2   1 
ATOM   4852  N  N     . THR A 1 605 ? 120.763 116.671 103.956 1.00 65.73 ?  605 THR A N     1 
ATOM   4853  C  CA    . THR A 1 605 ? 119.495 116.334 104.594 1.00 66.61 ?  605 THR A CA    1 
ATOM   4854  C  C     . THR A 1 605 ? 118.829 117.625 105.049 1.00 66.54 ?  605 THR A C     1 
ATOM   4855  O  O     . THR A 1 605 ? 119.319 118.291 105.967 1.00 65.70 ?  605 THR A O     1 
ATOM   4856  C  CB    . THR A 1 605 ? 119.707 115.385 105.774 1.00 66.19 ?  605 THR A CB    1 
ATOM   4857  O  OG1   . THR A 1 605 ? 120.428 114.227 105.336 1.00 66.36 ?  605 THR A OG1   1 
ATOM   4858  C  CG2   . THR A 1 605 ? 118.369 114.954 106.355 1.00 66.87 ?  605 THR A CG2   1 
ATOM   4859  N  N     . TYR A 1 606 ? 117.718 117.978 104.410 1.00 66.48 ?  606 TYR A N     1 
ATOM   4860  C  CA    . TYR A 1 606 ? 116.924 119.135 104.796 1.00 68.28 ?  606 TYR A CA    1 
ATOM   4861  C  C     . TYR A 1 606 ? 115.576 118.655 105.312 1.00 70.28 ?  606 TYR A C     1 
ATOM   4862  O  O     . TYR A 1 606 ? 114.866 117.920 104.616 1.00 69.13 ?  606 TYR A O     1 
ATOM   4863  C  CB    . TYR A 1 606 ? 116.740 120.102 103.623 1.00 66.57 ?  606 TYR A CB    1 
ATOM   4864  C  CG    . TYR A 1 606 ? 118.028 120.738 103.154 1.00 68.29 ?  606 TYR A CG    1 
ATOM   4865  C  CD1   . TYR A 1 606 ? 118.734 121.610 103.974 1.00 66.92 ?  606 TYR A CD1   1 
ATOM   4866  C  CD2   . TYR A 1 606 ? 118.537 120.472 101.893 1.00 67.97 ?  606 TYR A CD2   1 
ATOM   4867  C  CE1   . TYR A 1 606 ? 119.912 122.195 103.547 1.00 66.54 ?  606 TYR A CE1   1 
ATOM   4868  C  CE2   . TYR A 1 606 ? 119.713 121.051 101.458 1.00 65.78 ?  606 TYR A CE2   1 
ATOM   4869  C  CZ    . TYR A 1 606 ? 120.397 121.911 102.288 1.00 67.46 ?  606 TYR A CZ    1 
ATOM   4870  O  OH    . TYR A 1 606 ? 121.568 122.489 101.856 1.00 66.96 ?  606 TYR A OH    1 
ATOM   4871  N  N     . GLY A 1 607 ? 115.227 119.076 106.525 1.00 75.36 ?  607 GLY A N     1 
ATOM   4872  C  CA    . GLY A 1 607 ? 114.048 118.521 107.169 1.00 74.97 ?  607 GLY A CA    1 
ATOM   4873  C  C     . GLY A 1 607 ? 114.215 117.026 107.337 1.00 75.53 ?  607 GLY A C     1 
ATOM   4874  O  O     . GLY A 1 607 ? 115.210 116.546 107.891 1.00 75.04 ?  607 GLY A O     1 
ATOM   4875  N  N     . ASN A 1 608 ? 113.232 116.271 106.850 1.00 78.59 ?  608 ASN A N     1 
ATOM   4876  C  CA    . ASN A 1 608 ? 113.307 114.817 106.814 1.00 80.29 ?  608 ASN A CA    1 
ATOM   4877  C  C     . ASN A 1 608 ? 113.522 114.294 105.398 1.00 79.21 ?  608 ASN A C     1 
ATOM   4878  O  O     . ASN A 1 608 ? 113.230 113.127 105.119 1.00 78.37 ?  608 ASN A O     1 
ATOM   4879  C  CB    . ASN A 1 608 ? 112.048 114.202 107.426 1.00 79.45 ?  608 ASN A CB    1 
ATOM   4880  C  CG    . ASN A 1 608 ? 112.038 114.287 108.940 1.00 79.47 ?  608 ASN A CG    1 
ATOM   4881  O  OD1   . ASN A 1 608 ? 113.052 114.602 109.563 1.00 79.06 ?  608 ASN A OD1   1 
ATOM   4882  N  ND2   . ASN A 1 608 ? 110.888 114.004 109.541 1.00 78.01 ?  608 ASN A ND2   1 
ATOM   4883  N  N     . SER A 1 609 ? 114.028 115.137 104.501 1.00 73.08 ?  609 SER A N     1 
ATOM   4884  C  CA    . SER A 1 609 ? 114.200 114.788 103.101 1.00 72.48 ?  609 SER A CA    1 
ATOM   4885  C  C     . SER A 1 609 ? 115.673 114.837 102.718 1.00 73.03 ?  609 SER A C     1 
ATOM   4886  O  O     . SER A 1 609 ? 116.458 115.604 103.285 1.00 72.83 ?  609 SER A O     1 
ATOM   4887  C  CB    . SER A 1 609 ? 113.398 115.729 102.196 1.00 71.53 ?  609 SER A CB    1 
ATOM   4888  O  OG    . SER A 1 609 ? 113.841 117.069 102.333 1.00 70.80 ?  609 SER A OG    1 
ATOM   4889  N  N     . LYS A 1 610 ? 116.040 113.997 101.755 1.00 65.08 ?  610 LYS A N     1 
ATOM   4890  C  CA    . LYS A 1 610 ? 117.402 113.927 101.248 1.00 62.96 ?  610 LYS A CA    1 
ATOM   4891  C  C     . LYS A 1 610 ? 117.480 114.622 99.895  1.00 63.45 ?  610 LYS A C     1 
ATOM   4892  O  O     . LYS A 1 610 ? 116.538 114.563 99.099  1.00 64.05 ?  610 LYS A O     1 
ATOM   4893  C  CB    . LYS A 1 610 ? 117.861 112.473 101.118 1.00 62.17 ?  610 LYS A CB    1 
ATOM   4894  C  CG    . LYS A 1 610 ? 119.368 112.292 101.129 1.00 63.41 ?  610 LYS A CG    1 
ATOM   4895  C  CD    . LYS A 1 610 ? 119.772 111.133 102.028 1.00 64.78 ?  610 LYS A CD    1 
ATOM   4896  C  CE    . LYS A 1 610 ? 119.833 111.553 103.489 1.00 64.27 ?  610 LYS A CE    1 
ATOM   4897  N  NZ    . LYS A 1 610 ? 121.070 112.316 103.809 1.00 62.54 1  610 LYS A NZ    1 
ATOM   4898  N  N     . THR A 1 611 ? 118.607 115.281 99.640  1.00 61.72 ?  611 THR A N     1 
ATOM   4899  C  CA    . THR A 1 611 ? 118.811 116.007 98.398  1.00 58.73 ?  611 THR A CA    1 
ATOM   4900  C  C     . THR A 1 611 ? 120.239 115.792 97.921  1.00 57.57 ?  611 THR A C     1 
ATOM   4901  O  O     . THR A 1 611 ? 121.150 115.516 98.707  1.00 56.69 ?  611 THR A O     1 
ATOM   4902  C  CB    . THR A 1 611 ? 118.522 117.504 98.563  1.00 58.99 ?  611 THR A CB    1 
ATOM   4903  O  OG1   . THR A 1 611 ? 118.663 118.160 97.298  1.00 61.87 ?  611 THR A OG1   1 
ATOM   4904  C  CG2   . THR A 1 611 ? 119.483 118.118 99.558  1.00 59.35 ?  611 THR A CG2   1 
ATOM   4905  N  N     . TYR A 1 612 ? 120.421 115.932 96.610  1.00 53.41 ?  612 TYR A N     1 
ATOM   4906  C  CA    . TYR A 1 612 ? 121.667 115.584 95.940  1.00 51.64 ?  612 TYR A CA    1 
ATOM   4907  C  C     . TYR A 1 612 ? 122.091 116.753 95.068  1.00 54.03 ?  612 TYR A C     1 
ATOM   4908  O  O     . TYR A 1 612 ? 121.342 117.166 94.177  1.00 56.09 ?  612 TYR A O     1 
ATOM   4909  C  CB    . TYR A 1 612 ? 121.477 114.320 95.098  1.00 53.90 ?  612 TYR A CB    1 
ATOM   4910  C  CG    . TYR A 1 612 ? 121.320 113.066 95.924  1.00 55.12 ?  612 TYR A CG    1 
ATOM   4911  C  CD1   . TYR A 1 612 ? 122.251 112.727 96.894  1.00 54.59 ?  612 TYR A CD1   1 
ATOM   4912  C  CD2   . TYR A 1 612 ? 120.208 112.251 95.772  1.00 54.58 ?  612 TYR A CD2   1 
ATOM   4913  C  CE1   . TYR A 1 612 ? 122.100 111.586 97.656  1.00 55.95 ?  612 TYR A CE1   1 
ATOM   4914  C  CE2   . TYR A 1 612 ? 120.043 111.112 96.537  1.00 55.96 ?  612 TYR A CE2   1 
ATOM   4915  C  CZ    . TYR A 1 612 ? 120.994 110.784 97.477  1.00 57.43 ?  612 TYR A CZ    1 
ATOM   4916  O  OH    . TYR A 1 612 ? 120.841 109.651 98.244  1.00 58.99 ?  612 TYR A OH    1 
ATOM   4917  N  N     . TYR A 1 613 ? 123.282 117.289 95.321  1.00 46.07 ?  613 TYR A N     1 
ATOM   4918  C  CA    . TYR A 1 613 ? 123.828 118.386 94.522  1.00 40.41 ?  613 TYR A CA    1 
ATOM   4919  C  C     . TYR A 1 613 ? 125.092 117.936 93.809  1.00 39.86 ?  613 TYR A C     1 
ATOM   4920  O  O     . TYR A 1 613 ? 126.149 117.794 94.446  1.00 39.39 ?  613 TYR A O     1 
ATOM   4921  C  CB    . TYR A 1 613 ? 124.117 119.609 95.389  1.00 40.96 ?  613 TYR A CB    1 
ATOM   4922  C  CG    . TYR A 1 613 ? 124.678 120.778 94.610  1.00 37.21 ?  613 TYR A CG    1 
ATOM   4923  C  CD1   . TYR A 1 613 ? 124.009 121.285 93.504  1.00 37.85 ?  613 TYR A CD1   1 
ATOM   4924  C  CD2   . TYR A 1 613 ? 125.880 121.370 94.975  1.00 37.53 ?  613 TYR A CD2   1 
ATOM   4925  C  CE1   . TYR A 1 613 ? 124.516 122.352 92.789  1.00 41.31 ?  613 TYR A CE1   1 
ATOM   4926  C  CE2   . TYR A 1 613 ? 126.394 122.437 94.265  1.00 39.98 ?  613 TYR A CE2   1 
ATOM   4927  C  CZ    . TYR A 1 613 ? 125.709 122.923 93.173  1.00 44.91 ?  613 TYR A CZ    1 
ATOM   4928  O  OH    . TYR A 1 613 ? 126.216 123.986 92.462  1.00 41.53 ?  613 TYR A OH    1 
ATOM   4929  N  N     . PRO A 1 614 ? 125.032 117.661 92.510  1.00 41.29 ?  614 PRO A N     1 
ATOM   4930  C  CA    . PRO A 1 614 ? 126.268 117.471 91.749  1.00 38.89 ?  614 PRO A CA    1 
ATOM   4931  C  C     . PRO A 1 614 ? 126.997 118.793 91.585  1.00 39.14 ?  614 PRO A C     1 
ATOM   4932  O  O     . PRO A 1 614 ? 126.393 119.868 91.593  1.00 37.77 ?  614 PRO A O     1 
ATOM   4933  C  CB    . PRO A 1 614 ? 125.783 116.930 90.398  1.00 35.09 ?  614 PRO A CB    1 
ATOM   4934  C  CG    . PRO A 1 614 ? 124.343 116.553 90.605  1.00 39.46 ?  614 PRO A CG    1 
ATOM   4935  C  CD    . PRO A 1 614 ? 123.835 117.450 91.682  1.00 39.99 ?  614 PRO A CD    1 
ATOM   4936  N  N     . MET A 1 615 ? 128.315 118.707 91.443  1.00 37.84 ?  615 MET A N     1 
ATOM   4937  C  CA    . MET A 1 615 ? 129.097 119.904 91.194  1.00 35.62 ?  615 MET A CA    1 
ATOM   4938  C  C     . MET A 1 615 ? 128.715 120.504 89.841  1.00 38.19 ?  615 MET A C     1 
ATOM   4939  O  O     . MET A 1 615 ? 128.342 119.779 88.915  1.00 40.78 ?  615 MET A O     1 
ATOM   4940  C  CB    . MET A 1 615 ? 130.590 119.591 91.253  1.00 36.41 ?  615 MET A CB    1 
ATOM   4941  C  CG    . MET A 1 615 ? 131.130 119.585 92.673  1.00 37.79 ?  615 MET A CG    1 
ATOM   4942  S  SD    . MET A 1 615 ? 130.178 120.702 93.725  1.00 44.79 ?  615 MET A SD    1 
ATOM   4943  C  CE    . MET A 1 615 ? 130.565 120.081 95.356  1.00 37.65 ?  615 MET A CE    1 
ATOM   4944  N  N     . PRO A 1 616 ? 128.766 121.829 89.714  1.00 38.31 ?  616 PRO A N     1 
ATOM   4945  C  CA    . PRO A 1 616 ? 128.255 122.477 88.499  1.00 35.48 ?  616 PRO A CA    1 
ATOM   4946  C  C     . PRO A 1 616 ? 128.994 122.010 87.254  1.00 36.21 ?  616 PRO A C     1 
ATOM   4947  O  O     . PRO A 1 616 ? 130.224 121.956 87.223  1.00 38.12 ?  616 PRO A O     1 
ATOM   4948  C  CB    . PRO A 1 616 ? 128.492 123.967 88.769  1.00 36.48 ?  616 PRO A CB    1 
ATOM   4949  C  CG    . PRO A 1 616 ? 128.610 124.069 90.256  1.00 35.50 ?  616 PRO A CG    1 
ATOM   4950  C  CD    . PRO A 1 616 ? 129.255 122.806 90.700  1.00 35.95 ?  616 PRO A CD    1 
ATOM   4951  N  N     . GLY A 1 617 ? 128.227 121.677 86.219  1.00 37.13 ?  617 GLY A N     1 
ATOM   4952  C  CA    . GLY A 1 617 ? 128.804 121.195 84.983  1.00 36.09 ?  617 GLY A CA    1 
ATOM   4953  C  C     . GLY A 1 617 ? 129.336 119.783 85.031  1.00 40.13 ?  617 GLY A C     1 
ATOM   4954  O  O     . GLY A 1 617 ? 130.021 119.365 84.092  1.00 42.08 ?  617 GLY A O     1 
ATOM   4955  N  N     . LEU A 1 618 ? 129.047 119.033 86.091  1.00 41.11 ?  618 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 618 ? 129.544 117.668 86.199  1.00 37.11 ?  618 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 618 ? 128.820 116.761 85.212  1.00 39.55 ?  618 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 618 ? 127.590 116.781 85.116  1.00 44.58 ?  618 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 618 ? 129.368 117.145 87.623  1.00 37.34 ?  618 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 618 ? 129.877 115.729 87.896  1.00 38.46 ?  618 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 618 ? 131.357 115.617 87.580  1.00 38.88 ?  618 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 618 ? 129.605 115.332 89.338  1.00 39.00 ?  618 LEU A CD2   1 
ATOM   4963  N  N     . ALA A 1 619 ? 129.592 115.966 84.478  1.00 45.15 ?  619 ALA A N     1 
ATOM   4964  C  CA    . ALA A 1 619 ? 129.049 115.017 83.521  1.00 45.77 ?  619 ALA A CA    1 
ATOM   4965  C  C     . ALA A 1 619 ? 130.010 113.840 83.424  1.00 49.12 ?  619 ALA A C     1 
ATOM   4966  O  O     . ALA A 1 619 ? 130.977 113.740 84.183  1.00 51.63 ?  619 ALA A O     1 
ATOM   4967  C  CB    . ALA A 1 619 ? 128.821 115.675 82.157  1.00 44.64 ?  619 ALA A CB    1 
ATOM   4968  N  N     . SER A 1 620 ? 129.735 112.941 82.479  1.00 50.10 ?  620 SER A N     1 
ATOM   4969  C  CA    . SER A 1 620 ? 130.616 111.796 82.282  1.00 49.28 ?  620 SER A CA    1 
ATOM   4970  C  C     . SER A 1 620 ? 131.951 112.222 81.687  1.00 49.15 ?  620 SER A C     1 
ATOM   4971  O  O     . SER A 1 620 ? 132.994 111.638 82.006  1.00 51.61 ?  620 SER A O     1 
ATOM   4972  C  CB    . SER A 1 620 ? 129.933 110.759 81.391  1.00 52.72 ?  620 SER A CB    1 
ATOM   4973  O  OG    . SER A 1 620 ? 128.660 110.406 81.904  1.00 54.05 ?  620 SER A OG    1 
ATOM   4974  N  N     . ASN A 1 621 ? 131.942 113.237 80.820  1.00 47.90 ?  621 ASN A N     1 
ATOM   4975  C  CA    . ASN A 1 621 ? 133.174 113.659 80.162  1.00 50.30 ?  621 ASN A CA    1 
ATOM   4976  C  C     . ASN A 1 621 ? 134.129 114.337 81.139  1.00 50.21 ?  621 ASN A C     1 
ATOM   4977  O  O     . ASN A 1 621 ? 135.347 114.138 81.060  1.00 50.40 ?  621 ASN A O     1 
ATOM   4978  C  CB    . ASN A 1 621 ? 132.851 114.588 78.993  1.00 49.26 ?  621 ASN A CB    1 
ATOM   4979  C  CG    . ASN A 1 621 ? 131.630 115.445 79.250  1.00 51.92 ?  621 ASN A CG    1 
ATOM   4980  O  OD1   . ASN A 1 621 ? 131.587 116.209 80.214  1.00 50.98 ?  621 ASN A OD1   1 
ATOM   4981  N  ND2   . ASN A 1 621 ? 130.628 115.321 78.389  1.00 51.57 ?  621 ASN A ND2   1 
ATOM   4982  N  N     . ASN A 1 622 ? 133.600 115.139 82.063  1.00 40.26 ?  622 ASN A N     1 
ATOM   4983  C  CA    . ASN A 1 622 ? 134.422 115.869 83.019  1.00 39.73 ?  622 ASN A CA    1 
ATOM   4984  C  C     . ASN A 1 622 ? 134.352 115.275 84.422  1.00 43.21 ?  622 ASN A C     1 
ATOM   4985  O  O     . ASN A 1 622 ? 134.690 115.955 85.396  1.00 47.91 ?  622 ASN A O     1 
ATOM   4986  C  CB    . ASN A 1 622 ? 134.030 117.349 83.040  1.00 40.12 ?  622 ASN A CB    1 
ATOM   4987  C  CG    . ASN A 1 622 ? 132.552 117.563 83.309  1.00 41.94 ?  622 ASN A CG    1 
ATOM   4988  O  OD1   . ASN A 1 622 ? 131.848 116.659 83.756  1.00 47.40 ?  622 ASN A OD1   1 
ATOM   4989  N  ND2   . ASN A 1 622 ? 132.074 118.769 83.033  1.00 38.35 ?  622 ASN A ND2   1 
ATOM   4990  N  N     . TRP A 1 623 ? 133.913 114.021 84.546  1.00 40.70 ?  623 TRP A N     1 
ATOM   4991  C  CA    . TRP A 1 623 ? 133.889 113.371 85.852  1.00 40.55 ?  623 TRP A CA    1 
ATOM   4992  C  C     . TRP A 1 623 ? 135.299 113.211 86.408  1.00 41.55 ?  623 TRP A C     1 
ATOM   4993  O  O     . TRP A 1 623 ? 135.527 113.398 87.609  1.00 40.00 ?  623 TRP A O     1 
ATOM   4994  C  CB    . TRP A 1 623 ? 133.191 112.014 85.749  1.00 41.25 ?  623 TRP A CB    1 
ATOM   4995  C  CG    . TRP A 1 623 ? 133.213 111.211 87.016  1.00 40.04 ?  623 TRP A CG    1 
ATOM   4996  C  CD1   . TRP A 1 623 ? 134.209 110.383 87.447  1.00 37.86 ?  623 TRP A CD1   1 
ATOM   4997  C  CD2   . TRP A 1 623 ? 132.187 111.155 88.014  1.00 39.38 ?  623 TRP A CD2   1 
ATOM   4998  N  NE1   . TRP A 1 623 ? 133.868 109.819 88.651  1.00 37.74 ?  623 TRP A NE1   1 
ATOM   4999  C  CE2   . TRP A 1 623 ? 132.631 110.275 89.020  1.00 37.65 ?  623 TRP A CE2   1 
ATOM   5000  C  CE3   . TRP A 1 623 ? 130.937 111.765 88.154  1.00 38.03 ?  623 TRP A CE3   1 
ATOM   5001  C  CZ2   . TRP A 1 623 ? 131.870 109.992 90.153  1.00 38.90 ?  623 TRP A CZ2   1 
ATOM   5002  C  CZ3   . TRP A 1 623 ? 130.184 111.482 89.278  1.00 39.91 ?  623 TRP A CZ3   1 
ATOM   5003  C  CH2   . TRP A 1 623 ? 130.652 110.604 90.262  1.00 39.28 ?  623 TRP A CH2   1 
ATOM   5004  N  N     . PHE A 1 624 ? 136.259 112.863 85.549  1.00 43.25 ?  624 PHE A N     1 
ATOM   5005  C  CA    . PHE A 1 624 ? 137.635 112.692 85.997  1.00 43.02 ?  624 PHE A CA    1 
ATOM   5006  C  C     . PHE A 1 624 ? 138.291 114.022 86.342  1.00 41.73 ?  624 PHE A C     1 
ATOM   5007  O  O     . PHE A 1 624 ? 139.091 114.086 87.281  1.00 45.72 ?  624 PHE A O     1 
ATOM   5008  C  CB    . PHE A 1 624 ? 138.435 111.933 84.931  1.00 41.79 ?  624 PHE A CB    1 
ATOM   5009  C  CG    . PHE A 1 624 ? 139.894 112.306 84.863  1.00 45.02 ?  624 PHE A CG    1 
ATOM   5010  C  CD1   . PHE A 1 624 ? 140.326 113.370 84.083  1.00 42.97 ?  624 PHE A CD1   1 
ATOM   5011  C  CD2   . PHE A 1 624 ? 140.834 111.588 85.583  1.00 44.13 ?  624 PHE A CD2   1 
ATOM   5012  C  CE1   . PHE A 1 624 ? 141.664 113.707 84.024  1.00 43.88 ?  624 PHE A CE1   1 
ATOM   5013  C  CE2   . PHE A 1 624 ? 142.174 111.922 85.528  1.00 43.74 ?  624 PHE A CE2   1 
ATOM   5014  C  CZ    . PHE A 1 624 ? 142.588 112.982 84.748  1.00 44.28 ?  624 PHE A CZ    1 
ATOM   5015  N  N     . PHE A 1 625 ? 137.971 115.087 85.602  1.00 35.51 ?  625 PHE A N     1 
ATOM   5016  C  CA    . PHE A 1 625 ? 138.547 116.393 85.897  1.00 34.02 ?  625 PHE A CA    1 
ATOM   5017  C  C     . PHE A 1 625 ? 137.970 117.007 87.165  1.00 33.14 ?  625 PHE A C     1 
ATOM   5018  O  O     . PHE A 1 625 ? 138.603 117.888 87.754  1.00 35.40 ?  625 PHE A O     1 
ATOM   5019  C  CB    . PHE A 1 625 ? 138.342 117.343 84.717  1.00 32.94 ?  625 PHE A CB    1 
ATOM   5020  C  CG    . PHE A 1 625 ? 139.189 117.013 83.523  1.00 34.92 ?  625 PHE A CG    1 
ATOM   5021  C  CD1   . PHE A 1 625 ? 140.550 117.268 83.533  1.00 33.87 ?  625 PHE A CD1   1 
ATOM   5022  C  CD2   . PHE A 1 625 ? 138.626 116.447 82.393  1.00 34.90 ?  625 PHE A CD2   1 
ATOM   5023  C  CE1   . PHE A 1 625 ? 141.334 116.965 82.436  1.00 35.98 ?  625 PHE A CE1   1 
ATOM   5024  C  CE2   . PHE A 1 625 ? 139.404 116.143 81.293  1.00 36.21 ?  625 PHE A CE2   1 
ATOM   5025  C  CZ    . PHE A 1 625 ? 140.759 116.401 81.315  1.00 38.49 ?  625 PHE A CZ    1 
ATOM   5026  N  N     . TYR A 1 626 ? 136.791 116.562 87.599  1.00 29.63 ?  626 TYR A N     1 
ATOM   5027  C  CA    . TYR A 1 626 ? 136.233 117.026 88.862  1.00 32.34 ?  626 TYR A CA    1 
ATOM   5028  C  C     . TYR A 1 626 ? 136.769 116.187 90.013  1.00 31.25 ?  626 TYR A C     1 
ATOM   5029  O  O     . TYR A 1 626 ? 135.997 115.645 90.808  1.00 34.79 ?  626 TYR A O     1 
ATOM   5030  C  CB    . TYR A 1 626 ? 134.705 116.978 88.834  1.00 32.25 ?  626 TYR A CB    1 
ATOM   5031  C  CG    . TYR A 1 626 ? 134.071 118.299 88.473  1.00 31.54 ?  626 TYR A CG    1 
ATOM   5032  C  CD1   . TYR A 1 626 ? 134.100 119.367 89.359  1.00 34.40 ?  626 TYR A CD1   1 
ATOM   5033  C  CD2   . TYR A 1 626 ? 133.442 118.478 87.250  1.00 30.33 ?  626 TYR A CD2   1 
ATOM   5034  C  CE1   . TYR A 1 626 ? 133.526 120.576 89.035  1.00 34.43 ?  626 TYR A CE1   1 
ATOM   5035  C  CE2   . TYR A 1 626 ? 132.862 119.684 86.918  1.00 32.29 ?  626 TYR A CE2   1 
ATOM   5036  C  CZ    . TYR A 1 626 ? 132.908 120.729 87.814  1.00 33.86 ?  626 TYR A CZ    1 
ATOM   5037  O  OH    . TYR A 1 626 ? 132.335 121.935 87.491  1.00 36.02 ?  626 TYR A OH    1 
ATOM   5038  N  N     . LYS A 1 627 ? 138.092 116.082 90.106  1.00 31.15 ?  627 LYS A N     1 
ATOM   5039  C  CA    . LYS A 1 627 ? 138.715 115.288 91.155  1.00 30.24 ?  627 LYS A CA    1 
ATOM   5040  C  C     . LYS A 1 627 ? 138.376 115.855 92.526  1.00 34.65 ?  627 LYS A C     1 
ATOM   5041  O  O     . LYS A 1 627 ? 138.342 117.072 92.722  1.00 40.73 ?  627 LYS A O     1 
ATOM   5042  C  CB    . LYS A 1 627 ? 140.228 115.256 90.950  1.00 35.22 ?  627 LYS A CB    1 
ATOM   5043  C  CG    . LYS A 1 627 ? 140.976 114.309 91.865  1.00 34.08 ?  627 LYS A CG    1 
ATOM   5044  C  CD    . LYS A 1 627 ? 142.425 114.186 91.431  1.00 31.12 ?  627 LYS A CD    1 
ATOM   5045  C  CE    . LYS A 1 627 ? 143.235 113.373 92.422  1.00 36.23 ?  627 LYS A CE    1 
ATOM   5046  N  NZ    . LYS A 1 627 ? 144.689 113.421 92.111  1.00 36.73 1  627 LYS A NZ    1 
ATOM   5047  N  N     . GLU A 1 628 ? 138.105 114.965 93.475  1.00 38.83 ?  628 GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 628 ? 137.791 115.404 94.825  1.00 36.13 ?  628 GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 628 ? 139.040 115.930 95.521  1.00 38.43 ?  628 GLU A C     1 
ATOM   5050  O  O     . GLU A 1 628 ? 140.164 115.506 95.237  1.00 40.81 ?  628 GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 628 ? 137.171 114.262 95.629  1.00 37.33 ?  628 GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 628 ? 135.728 113.968 95.252  1.00 39.57 ?  628 GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 628 ? 135.195 112.716 95.913  1.00 43.19 ?  628 GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 628 ? 135.867 112.188 96.824  1.00 45.12 ?  628 GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 628 ? 134.100 112.259 95.523  1.00 39.83 -1 628 GLU A OE2   1 
ATOM   5056  N  N     . ALA A 1 629 ? 138.830 116.876 96.440  1.00 39.43 ?  629 ALA A N     1 
ATOM   5057  C  CA    . ALA A 1 629 ? 139.951 117.542 97.096  1.00 33.25 ?  629 ALA A CA    1 
ATOM   5058  C  C     . ALA A 1 629 ? 140.773 116.569 97.930  1.00 35.69 ?  629 ALA A C     1 
ATOM   5059  O  O     . ALA A 1 629 ? 142.003 116.679 97.991  1.00 42.03 ?  629 ALA A O     1 
ATOM   5060  C  CB    . ALA A 1 629 ? 139.439 118.691 97.963  1.00 30.29 ?  629 ALA A CB    1 
ATOM   5061  N  N     . TYR A 1 630 ? 140.112 115.617 98.591  1.00 40.56 ?  630 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 630 ? 140.831 114.678 99.446  1.00 36.66 ?  630 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 630 ? 141.744 113.765 98.640  1.00 41.15 ?  630 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 630 ? 142.823 113.395 99.118  1.00 44.81 ?  630 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 630 ? 139.841 113.856 100.267 1.00 35.20 ?  630 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 630 ? 138.920 114.696 101.120 1.00 36.69 ?  630 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 630 ? 139.352 115.220 102.331 1.00 34.53 ?  630 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 630 ? 137.622 114.968 100.714 1.00 37.62 ?  630 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 630 ? 138.515 115.988 103.114 1.00 37.48 ?  630 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 630 ? 136.779 115.736 101.490 1.00 38.03 ?  630 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 630 ? 137.230 116.244 102.688 1.00 44.44 ?  630 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 630 ? 136.392 117.009 103.465 1.00 44.97 ?  630 TYR A OH    1 
ATOM   5073  N  N     . ASP A 1 631 ? 141.340 113.393 97.427  1.00 38.93 ?  631 ASP A N     1 
ATOM   5074  C  CA    . ASP A 1 631 ? 142.172 112.562 96.568  1.00 38.97 ?  631 ASP A CA    1 
ATOM   5075  C  C     . ASP A 1 631 ? 143.356 113.316 95.981  1.00 41.98 ?  631 ASP A C     1 
ATOM   5076  O  O     . ASP A 1 631 ? 144.263 112.681 95.432  1.00 43.81 ?  631 ASP A O     1 
ATOM   5077  C  CB    . ASP A 1 631 ? 141.331 111.975 95.432  1.00 39.94 ?  631 ASP A CB    1 
ATOM   5078  C  CG    . ASP A 1 631 ? 140.136 111.192 95.936  1.00 45.71 ?  631 ASP A CG    1 
ATOM   5079  O  OD1   . ASP A 1 631 ? 140.243 110.567 97.012  1.00 46.44 ?  631 ASP A OD1   1 
ATOM   5080  O  OD2   . ASP A 1 631 ? 139.088 111.202 95.257  1.00 43.66 -1 631 ASP A OD2   1 
ATOM   5081  N  N     . MET A 1 632 ? 143.375 114.641 96.087  1.00 35.51 ?  632 MET A N     1 
ATOM   5082  C  CA    . MET A 1 632 ? 144.417 115.443 95.470  1.00 32.76 ?  632 MET A CA    1 
ATOM   5083  C  C     . MET A 1 632 ? 145.667 115.487 96.343  1.00 37.18 ?  632 MET A C     1 
ATOM   5084  O  O     . MET A 1 632 ? 145.622 115.281 97.559  1.00 35.27 ?  632 MET A O     1 
ATOM   5085  C  CB    . MET A 1 632 ? 143.922 116.865 95.217  1.00 31.39 ?  632 MET A CB    1 
ATOM   5086  C  CG    . MET A 1 632 ? 142.912 116.981 94.097  1.00 35.86 ?  632 MET A CG    1 
ATOM   5087  S  SD    . MET A 1 632 ? 142.458 118.690 93.768  1.00 39.76 ?  632 MET A SD    1 
ATOM   5088  C  CE    . MET A 1 632 ? 141.186 118.454 92.537  1.00 33.94 ?  632 MET A CE    1 
ATOM   5089  N  N     . ASP A 1 633 ? 146.796 115.763 95.697  1.00 33.46 ?  633 ASP A N     1 
ATOM   5090  C  CA    . ASP A 1 633 ? 148.046 116.003 96.404  1.00 31.47 ?  633 ASP A CA    1 
ATOM   5091  C  C     . ASP A 1 633 ? 148.005 117.400 97.010  1.00 31.69 ?  633 ASP A C     1 
ATOM   5092  O  O     . ASP A 1 633 ? 147.863 118.391 96.286  1.00 35.01 ?  633 ASP A O     1 
ATOM   5093  C  CB    . ASP A 1 633 ? 149.233 115.856 95.455  1.00 29.78 ?  633 ASP A CB    1 
ATOM   5094  C  CG    . ASP A 1 633 ? 150.566 115.874 96.177  1.00 36.13 ?  633 ASP A CG    1 
ATOM   5095  O  OD1   . ASP A 1 633 ? 150.574 115.878 97.425  1.00 38.03 ?  633 ASP A OD1   1 
ATOM   5096  O  OD2   . ASP A 1 633 ? 151.610 115.888 95.492  1.00 37.92 -1 633 ASP A OD2   1 
ATOM   5097  N  N     . MET A 1 634 ? 148.125 117.481 98.337  1.00 27.77 ?  634 MET A N     1 
ATOM   5098  C  CA    . MET A 1 634 ? 148.038 118.771 99.007  1.00 25.57 ?  634 MET A CA    1 
ATOM   5099  C  C     . MET A 1 634 ? 149.195 119.694 98.653  1.00 27.47 ?  634 MET A C     1 
ATOM   5100  O  O     . MET A 1 634 ? 149.052 120.914 98.776  1.00 26.26 ?  634 MET A O     1 
ATOM   5101  C  CB    . MET A 1 634 ? 147.969 118.577 100.521 1.00 27.41 ?  634 MET A CB    1 
ATOM   5102  C  CG    . MET A 1 634 ? 146.561 118.357 101.042 1.00 28.92 ?  634 MET A CG    1 
ATOM   5103  S  SD    . MET A 1 634 ? 145.446 119.697 100.580 1.00 43.53 ?  634 MET A SD    1 
ATOM   5104  C  CE    . MET A 1 634 ? 144.303 118.832 99.508  1.00 28.34 ?  634 MET A CE    1 
ATOM   5105  N  N     . PHE A 1 635 ? 150.330 119.149 98.213  1.00 26.68 ?  635 PHE A N     1 
ATOM   5106  C  CA    . PHE A 1 635 ? 151.432 120.001 97.779  1.00 23.26 ?  635 PHE A CA    1 
ATOM   5107  C  C     . PHE A 1 635 ? 151.064 120.778 96.521  1.00 21.66 ?  635 PHE A C     1 
ATOM   5108  O  O     . PHE A 1 635 ? 151.395 121.962 96.397  1.00 25.79 ?  635 PHE A O     1 
ATOM   5109  C  CB    . PHE A 1 635 ? 152.688 119.162 97.550  1.00 23.22 ?  635 PHE A CB    1 
ATOM   5110  C  CG    . PHE A 1 635 ? 153.509 118.951 98.790  1.00 24.30 ?  635 PHE A CG    1 
ATOM   5111  C  CD1   . PHE A 1 635 ? 152.907 118.605 99.987  1.00 23.65 ?  635 PHE A CD1   1 
ATOM   5112  C  CD2   . PHE A 1 635 ? 154.884 119.099 98.758  1.00 27.13 ?  635 PHE A CD2   1 
ATOM   5113  C  CE1   . PHE A 1 635 ? 153.659 118.411 101.128 1.00 22.91 ?  635 PHE A CE1   1 
ATOM   5114  C  CE2   . PHE A 1 635 ? 155.643 118.907 99.896  1.00 29.75 ?  635 PHE A CE2   1 
ATOM   5115  C  CZ    . PHE A 1 635 ? 155.028 118.562 101.082 1.00 26.44 ?  635 PHE A CZ    1 
ATOM   5116  N  N     . LYS A 1 636 ? 150.364 120.139 95.584  1.00 23.36 ?  636 LYS A N     1 
ATOM   5117  C  CA    . LYS A 1 636 ? 149.956 120.839 94.371  1.00 26.62 ?  636 LYS A CA    1 
ATOM   5118  C  C     . LYS A 1 636 ? 148.831 121.831 94.646  1.00 27.24 ?  636 LYS A C     1 
ATOM   5119  O  O     . LYS A 1 636 ? 148.769 122.891 94.009  1.00 32.63 ?  636 LYS A O     1 
ATOM   5120  C  CB    . LYS A 1 636 ? 149.549 119.826 93.303  1.00 28.33 ?  636 LYS A CB    1 
ATOM   5121  C  CG    . LYS A 1 636 ? 150.720 118.998 92.795  1.00 28.04 ?  636 LYS A CG    1 
ATOM   5122  C  CD    . LYS A 1 636 ? 150.292 117.990 91.748  1.00 33.47 ?  636 LYS A CD    1 
ATOM   5123  C  CE    . LYS A 1 636 ? 151.405 117.003 91.440  1.00 32.60 ?  636 LYS A CE    1 
ATOM   5124  N  NZ    . LYS A 1 636 ? 150.920 115.867 90.610  1.00 33.68 1  636 LYS A NZ    1 
ATOM   5125  N  N     . VAL A 1 637 ? 147.948 121.519 95.595  1.00 23.94 ?  637 VAL A N     1 
ATOM   5126  C  CA    . VAL A 1 637 ? 146.952 122.496 96.028  1.00 16.29 ?  637 VAL A CA    1 
ATOM   5127  C  C     . VAL A 1 637 ? 147.637 123.701 96.659  1.00 23.84 ?  637 VAL A C     1 
ATOM   5128  O  O     . VAL A 1 637 ? 147.244 124.851 96.426  1.00 27.23 ?  637 VAL A O     1 
ATOM   5129  C  CB    . VAL A 1 637 ? 145.945 121.843 96.992  1.00 20.35 ?  637 VAL A CB    1 
ATOM   5130  C  CG1   . VAL A 1 637 ? 144.826 122.814 97.331  1.00 21.92 ?  637 VAL A CG1   1 
ATOM   5131  C  CG2   . VAL A 1 637 ? 145.381 120.571 96.384  1.00 25.87 ?  637 VAL A CG2   1 
ATOM   5132  N  N     . VAL A 1 638 ? 148.674 123.458 97.465  1.00 25.45 ?  638 VAL A N     1 
ATOM   5133  C  CA    . VAL A 1 638 ? 149.458 124.551 98.036  1.00 21.79 ?  638 VAL A CA    1 
ATOM   5134  C  C     . VAL A 1 638 ? 150.109 125.370 96.930  1.00 17.02 ?  638 VAL A C     1 
ATOM   5135  O  O     . VAL A 1 638 ? 150.161 126.602 96.999  1.00 25.22 ?  638 VAL A O     1 
ATOM   5136  C  CB    . VAL A 1 638 ? 150.507 124.002 99.022  1.00 20.12 ?  638 VAL A CB    1 
ATOM   5137  C  CG1   . VAL A 1 638 ? 151.594 125.031 99.276  1.00 15.90 ?  638 VAL A CG1   1 
ATOM   5138  C  CG2   . VAL A 1 638 ? 149.854 123.591 100.327 1.00 18.74 ?  638 VAL A CG2   1 
ATOM   5139  N  N     . ASP A 1 639 ? 150.627 124.698 95.901  1.00 20.16 ?  639 ASP A N     1 
ATOM   5140  C  CA    . ASP A 1 639 ? 151.251 125.408 94.788  1.00 17.42 ?  639 ASP A CA    1 
ATOM   5141  C  C     . ASP A 1 639 ? 150.251 126.309 94.075  1.00 23.65 ?  639 ASP A C     1 
ATOM   5142  O  O     . ASP A 1 639 ? 150.559 127.464 93.759  1.00 34.49 ?  639 ASP A O     1 
ATOM   5143  C  CB    . ASP A 1 639 ? 151.862 124.407 93.808  1.00 22.23 ?  639 ASP A CB    1 
ATOM   5144  C  CG    . ASP A 1 639 ? 153.177 123.840 94.297  1.00 30.93 ?  639 ASP A CG    1 
ATOM   5145  O  OD1   . ASP A 1 639 ? 153.956 124.592 94.918  1.00 31.40 ?  639 ASP A OD1   1 
ATOM   5146  O  OD2   . ASP A 1 639 ? 153.433 122.641 94.061  1.00 30.53 -1 639 ASP A OD2   1 
ATOM   5147  N  N     . MET A 1 640 ? 149.044 125.799 93.821  1.00 23.94 ?  640 MET A N     1 
ATOM   5148  C  CA    . MET A 1 640 ? 148.016 126.619 93.186  1.00 17.59 ?  640 MET A CA    1 
ATOM   5149  C  C     . MET A 1 640 ? 147.615 127.795 94.070  1.00 19.97 ?  640 MET A C     1 
ATOM   5150  O  O     . MET A 1 640 ? 147.445 128.922 93.585  1.00 30.73 ?  640 MET A O     1 
ATOM   5151  C  CB    . MET A 1 640 ? 146.794 125.767 92.847  1.00 23.08 ?  640 MET A CB    1 
ATOM   5152  C  CG    . MET A 1 640 ? 145.491 126.552 92.825  1.00 26.44 ?  640 MET A CG    1 
ATOM   5153  S  SD    . MET A 1 640 ? 145.017 127.091 91.174  1.00 31.92 ?  640 MET A SD    1 
ATOM   5154  C  CE    . MET A 1 640 ? 144.879 125.523 90.332  1.00 23.12 ?  640 MET A CE    1 
ATOM   5155  N  N     . ILE A 1 641 ? 147.454 127.552 95.372  1.00 15.77 ?  641 ILE A N     1 
ATOM   5156  C  CA    . ILE A 1 641 ? 147.039 128.628 96.263  1.00 18.94 ?  641 ILE A CA    1 
ATOM   5157  C  C     . ILE A 1 641 ? 148.130 129.684 96.374  1.00 19.32 ?  641 ILE A C     1 
ATOM   5158  O  O     . ILE A 1 641 ? 147.831 130.875 96.463  1.00 24.40 ?  641 ILE A O     1 
ATOM   5159  C  CB    . ILE A 1 641 ? 146.632 128.062 97.636  1.00 20.90 ?  641 ILE A CB    1 
ATOM   5160  C  CG1   . ILE A 1 641 ? 145.403 127.166 97.485  1.00 17.33 ?  641 ILE A CG1   1 
ATOM   5161  C  CG2   . ILE A 1 641 ? 146.311 129.184 98.610  1.00 16.43 ?  641 ILE A CG2   1 
ATOM   5162  C  CD1   . ILE A 1 641 ? 144.374 127.705 96.515  1.00 20.72 ?  641 ILE A CD1   1 
ATOM   5163  N  N     . ALA A 1 642 ? 149.401 129.280 96.346  1.00 15.52 ?  642 ALA A N     1 
ATOM   5164  C  CA    . ALA A 1 642 ? 150.492 130.253 96.347  1.00 16.76 ?  642 ALA A CA    1 
ATOM   5165  C  C     . ALA A 1 642 ? 150.539 131.032 95.039  1.00 19.56 ?  642 ALA A C     1 
ATOM   5166  O  O     . ALA A 1 642 ? 150.810 132.241 95.035  1.00 30.33 ?  642 ALA A O     1 
ATOM   5167  C  CB    . ALA A 1 642 ? 151.823 129.546 96.598  1.00 17.60 ?  642 ALA A CB    1 
ATOM   5168  N  N     . THR A 1 643 ? 150.278 130.353 93.920  1.00 16.40 ?  643 THR A N     1 
ATOM   5169  C  CA    . THR A 1 643 ? 150.213 131.033 92.634  1.00 16.82 ?  643 THR A CA    1 
ATOM   5170  C  C     . THR A 1 643 ? 149.133 132.107 92.640  1.00 20.72 ?  643 THR A C     1 
ATOM   5171  O  O     . THR A 1 643 ? 149.345 133.217 92.139  1.00 23.15 ?  643 THR A O     1 
ATOM   5172  C  CB    . THR A 1 643 ? 149.956 130.014 91.524  1.00 18.01 ?  643 THR A CB    1 
ATOM   5173  O  OG1   . THR A 1 643 ? 151.098 129.160 91.385  1.00 22.20 ?  643 THR A OG1   1 
ATOM   5174  C  CG2   . THR A 1 643 ? 149.691 130.710 90.210  1.00 14.96 ?  643 THR A CG2   1 
ATOM   5175  N  N     . ILE A 1 644 ? 147.970 131.796 93.211  1.00 17.72 ?  644 ILE A N     1 
ATOM   5176  C  CA    . ILE A 1 644 ? 146.922 132.806 93.335  1.00 11.61 ?  644 ILE A CA    1 
ATOM   5177  C  C     . ILE A 1 644 ? 147.331 133.889 94.329  1.00 15.14 ?  644 ILE A C     1 
ATOM   5178  O  O     . ILE A 1 644 ? 147.111 135.083 94.092  1.00 19.99 ?  644 ILE A O     1 
ATOM   5179  C  CB    . ILE A 1 644 ? 145.588 132.148 93.731  1.00 15.27 ?  644 ILE A CB    1 
ATOM   5180  C  CG1   . ILE A 1 644 ? 145.173 131.110 92.690  1.00 18.05 ?  644 ILE A CG1   1 
ATOM   5181  C  CG2   . ILE A 1 644 ? 144.509 133.200 93.891  1.00 9.24  ?  644 ILE A CG2   1 
ATOM   5182  C  CD1   . ILE A 1 644 ? 144.075 130.186 93.163  1.00 21.85 ?  644 ILE A CD1   1 
ATOM   5183  N  N     . GLN A 1 645 ? 147.941 133.492 95.449  1.00 13.04 ?  645 GLN A N     1 
ATOM   5184  C  CA    . GLN A 1 645 ? 148.268 134.421 96.524  1.00 14.10 ?  645 GLN A CA    1 
ATOM   5185  C  C     . GLN A 1 645 ? 149.291 135.456 96.090  1.00 15.57 ?  645 GLN A C     1 
ATOM   5186  O  O     . GLN A 1 645 ? 149.312 136.569 96.630  1.00 19.84 ?  645 GLN A O     1 
ATOM   5187  C  CB    . GLN A 1 645 ? 148.785 133.645 97.735  1.00 12.50 ?  645 GLN A CB    1 
ATOM   5188  C  CG    . GLN A 1 645 ? 149.033 134.491 98.968  1.00 8.73  ?  645 GLN A CG    1 
ATOM   5189  C  CD    . GLN A 1 645 ? 147.748 134.968 99.607  1.00 11.82 ?  645 GLN A CD    1 
ATOM   5190  O  OE1   . GLN A 1 645 ? 147.154 134.269 100.426 1.00 17.05 ?  645 GLN A OE1   1 
ATOM   5191  N  NE2   . GLN A 1 645 ? 147.310 136.164 99.236  1.00 6.56  ?  645 GLN A NE2   1 
ATOM   5192  N  N     . GLN A 1 646 ? 150.142 135.118 95.125  1.00 20.80 ?  646 GLN A N     1 
ATOM   5193  C  CA    . GLN A 1 646 ? 151.101 136.106 94.650  1.00 14.50 ?  646 GLN A CA    1 
ATOM   5194  C  C     . GLN A 1 646 ? 150.427 137.294 93.972  1.00 13.51 ?  646 GLN A C     1 
ATOM   5195  O  O     . GLN A 1 646 ? 151.082 138.321 93.770  1.00 17.75 ?  646 GLN A O     1 
ATOM   5196  C  CB    . GLN A 1 646 ? 152.106 135.453 93.700  1.00 17.94 ?  646 GLN A CB    1 
ATOM   5197  C  CG    . GLN A 1 646 ? 151.644 135.348 92.266  1.00 21.82 ?  646 GLN A CG    1 
ATOM   5198  C  CD    . GLN A 1 646 ? 152.569 134.495 91.424  1.00 26.95 ?  646 GLN A CD    1 
ATOM   5199  O  OE1   . GLN A 1 646 ? 153.727 134.846 91.207  1.00 25.36 ?  646 GLN A OE1   1 
ATOM   5200  N  NE2   . GLN A 1 646 ? 152.063 133.365 90.947  1.00 22.86 ?  646 GLN A NE2   1 
ATOM   5201  N  N     . HIS A 1 647 ? 149.140 137.191 93.635  1.00 21.28 ?  647 HIS A N     1 
ATOM   5202  C  CA    . HIS A 1 647 ? 148.393 138.293 93.040  1.00 14.87 ?  647 HIS A CA    1 
ATOM   5203  C  C     . HIS A 1 647 ? 147.291 138.819 93.949  1.00 11.61 ?  647 HIS A C     1 
ATOM   5204  O  O     . HIS A 1 647 ? 146.519 139.687 93.529  1.00 19.13 ?  647 HIS A O     1 
ATOM   5205  C  CB    . HIS A 1 647 ? 147.797 137.865 91.697  1.00 10.26 ?  647 HIS A CB    1 
ATOM   5206  C  CG    . HIS A 1 647 ? 148.807 137.320 90.740  1.00 15.52 ?  647 HIS A CG    1 
ATOM   5207  N  ND1   . HIS A 1 647 ? 149.840 138.082 90.238  1.00 16.09 ?  647 HIS A ND1   1 
ATOM   5208  C  CD2   . HIS A 1 647 ? 148.949 136.089 90.199  1.00 13.32 ?  647 HIS A CD2   1 
ATOM   5209  C  CE1   . HIS A 1 647 ? 150.573 137.344 89.426  1.00 18.02 ?  647 HIS A CE1   1 
ATOM   5210  N  NE2   . HIS A 1 647 ? 150.054 136.130 89.384  1.00 19.55 ?  647 HIS A NE2   1 
ATOM   5211  N  N     . ILE A 1 648 ? 147.193 138.320 95.177  1.00 11.14 ?  648 ILE A N     1 
ATOM   5212  C  CA    . ILE A 1 648 ? 146.182 138.751 96.137  1.00 13.31 ?  648 ILE A CA    1 
ATOM   5213  C  C     . ILE A 1 648 ? 146.891 139.479 97.270  1.00 13.02 ?  648 ILE A C     1 
ATOM   5214  O  O     . ILE A 1 648 ? 147.811 138.930 97.887  1.00 23.58 ?  648 ILE A O     1 
ATOM   5215  C  CB    . ILE A 1 648 ? 145.365 137.560 96.666  1.00 11.46 ?  648 ILE A CB    1 
ATOM   5216  C  CG1   . ILE A 1 648 ? 144.754 136.766 95.509  1.00 7.66  ?  648 ILE A CG1   1 
ATOM   5217  C  CG2   . ILE A 1 648 ? 144.278 138.035 97.611  1.00 9.21  ?  648 ILE A CG2   1 
ATOM   5218  C  CD1   . ILE A 1 648 ? 143.663 137.500 94.763  1.00 9.58  ?  648 ILE A CD1   1 
ATOM   5219  N  N     . ASP A 1 649 ? 146.472 140.719 97.534  1.00 6.66  ?  649 ASP A N     1 
ATOM   5220  C  CA    . ASP A 1 649 ? 147.130 141.509 98.572  1.00 11.95 ?  649 ASP A CA    1 
ATOM   5221  C  C     . ASP A 1 649 ? 146.808 140.977 99.962  1.00 9.56  ?  649 ASP A C     1 
ATOM   5222  O  O     . ASP A 1 649 ? 147.673 140.969 100.844 1.00 28.87 ?  649 ASP A O     1 
ATOM   5223  C  CB    . ASP A 1 649 ? 146.732 142.979 98.448  1.00 21.67 ?  649 ASP A CB    1 
ATOM   5224  C  CG    . ASP A 1 649 ? 145.262 143.160 98.148  1.00 18.65 ?  649 ASP A CG    1 
ATOM   5225  O  OD1   . ASP A 1 649 ? 144.681 142.284 97.479  1.00 24.11 ?  649 ASP A OD1   1 
ATOM   5226  O  OD2   . ASP A 1 649 ? 144.687 144.180 98.578  1.00 15.97 -1 649 ASP A OD2   1 
ATOM   5227  N  N     . GLN A 1 650 ? 145.575 140.538 100.179 1.00 10.05 ?  650 GLN A N     1 
ATOM   5228  C  CA    . GLN A 1 650 ? 145.193 139.892 101.425 1.00 6.55  ?  650 GLN A CA    1 
ATOM   5229  C  C     . GLN A 1 650 ? 145.381 138.382 101.271 1.00 5.55  ?  650 GLN A C     1 
ATOM   5230  O  O     . GLN A 1 650 ? 146.028 137.919 100.329 1.00 16.73 ?  650 GLN A O     1 
ATOM   5231  C  CB    . GLN A 1 650 ? 143.762 140.286 101.803 1.00 3.48  ?  650 GLN A CB    1 
ATOM   5232  C  CG    . GLN A 1 650 ? 143.563 141.777 101.995 1.00 4.86  ?  650 GLN A CG    1 
ATOM   5233  C  CD    . GLN A 1 650 ? 142.132 142.130 102.330 1.00 10.24 ?  650 GLN A CD    1 
ATOM   5234  O  OE1   . GLN A 1 650 ? 141.662 141.869 103.436 1.00 21.25 ?  650 GLN A OE1   1 
ATOM   5235  N  NE2   . GLN A 1 650 ? 141.430 142.725 101.376 1.00 5.10  ?  650 GLN A NE2   1 
ATOM   5236  N  N     . GLY A 1 651 ? 144.836 137.598 102.198 1.00 6.66  ?  651 GLY A N     1 
ATOM   5237  C  CA    . GLY A 1 651 ? 145.004 136.163 102.170 1.00 8.64  ?  651 GLY A CA    1 
ATOM   5238  C  C     . GLY A 1 651 ? 143.895 135.445 101.425 1.00 6.35  ?  651 GLY A C     1 
ATOM   5239  O  O     . GLY A 1 651 ? 142.944 136.038 100.918 1.00 9.60  ?  651 GLY A O     1 
ATOM   5240  N  N     . ILE A 1 652 ? 144.040 134.126 101.366 1.00 18.34 ?  652 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 652 ? 143.072 133.232 100.747 1.00 8.90  ?  652 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 652 ? 142.649 132.213 101.791 1.00 7.64  ?  652 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 652 ? 143.500 131.632 102.475 1.00 19.66 ?  652 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 652 ? 143.659 132.525 99.511  1.00 6.86  ?  652 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 652 ? 144.161 133.547 98.492  1.00 0.00  ?  652 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 652 ? 142.634 131.597 98.887  1.00 10.78 ?  652 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 652 ? 145.064 132.948 97.448  1.00 4.02  ?  652 ILE A CD1   1 
ATOM   5248  N  N     . SER A 1 653 ? 141.344 132.002 101.924 1.00 15.16 ?  653 SER A N     1 
ATOM   5249  C  CA    . SER A 1 653 ? 140.841 130.963 102.817 1.00 12.99 ?  653 SER A CA    1 
ATOM   5250  C  C     . SER A 1 653 ? 141.261 129.615 102.250 1.00 13.55 ?  653 SER A C     1 
ATOM   5251  O  O     . SER A 1 653 ? 140.675 129.118 101.286 1.00 26.18 ?  653 SER A O     1 
ATOM   5252  C  CB    . SER A 1 653 ? 139.329 131.062 102.966 1.00 12.53 ?  653 SER A CB    1 
ATOM   5253  O  OG    . SER A 1 653 ? 138.981 131.634 104.212 1.00 15.77 ?  653 SER A OG    1 
ATOM   5254  N  N     . PHE A 1 654 ? 142.283 129.020 102.851 1.00 18.67 ?  654 PHE A N     1 
ATOM   5255  C  CA    . PHE A 1 654 ? 142.932 127.819 102.331 1.00 9.68  ?  654 PHE A CA    1 
ATOM   5256  C  C     . PHE A 1 654 ? 142.676 126.681 103.312 1.00 15.65 ?  654 PHE A C     1 
ATOM   5257  O  O     . PHE A 1 654 ? 143.326 126.589 104.357 1.00 24.30 ?  654 PHE A O     1 
ATOM   5258  C  CB    . PHE A 1 654 ? 144.423 128.067 102.128 1.00 9.20  ?  654 PHE A CB    1 
ATOM   5259  C  CG    . PHE A 1 654 ? 145.162 126.911 101.515 1.00 16.73 ?  654 PHE A CG    1 
ATOM   5260  C  CD1   . PHE A 1 654 ? 144.490 125.916 100.825 1.00 22.93 ?  654 PHE A CD1   1 
ATOM   5261  C  CD2   . PHE A 1 654 ? 146.537 126.823 101.629 1.00 18.70 ?  654 PHE A CD2   1 
ATOM   5262  C  CE1   . PHE A 1 654 ? 145.173 124.857 100.267 1.00 14.90 ?  654 PHE A CE1   1 
ATOM   5263  C  CE2   . PHE A 1 654 ? 147.225 125.769 101.071 1.00 20.49 ?  654 PHE A CE2   1 
ATOM   5264  C  CZ    . PHE A 1 654 ? 146.542 124.784 100.390 1.00 15.99 ?  654 PHE A CZ    1 
ATOM   5265  N  N     . THR A 1 655 ? 141.736 125.811 102.964 1.00 20.69 ?  655 THR A N     1 
ATOM   5266  C  CA    . THR A 1 655 ? 141.426 124.638 103.766 1.00 16.46 ?  655 THR A CA    1 
ATOM   5267  C  C     . THR A 1 655 ? 142.244 123.452 103.272 1.00 23.11 ?  655 THR A C     1 
ATOM   5268  O  O     . THR A 1 655 ? 142.280 123.173 102.070 1.00 28.79 ?  655 THR A O     1 
ATOM   5269  C  CB    . THR A 1 655 ? 139.932 124.317 103.696 1.00 23.48 ?  655 THR A CB    1 
ATOM   5270  O  OG1   . THR A 1 655 ? 139.195 125.294 104.443 1.00 23.66 ?  655 THR A OG1   1 
ATOM   5271  C  CG2   . THR A 1 655 ? 139.648 122.934 104.259 1.00 24.36 ?  655 THR A CG2   1 
ATOM   5272  N  N     . LEU A 1 656 ? 142.915 122.772 104.198 1.00 31.95 ?  656 LEU A N     1 
ATOM   5273  C  CA    . LEU A 1 656 ? 143.595 121.528 103.872 1.00 28.61 ?  656 LEU A CA    1 
ATOM   5274  C  C     . LEU A 1 656 ? 142.589 120.387 103.845 1.00 27.54 ?  656 LEU A C     1 
ATOM   5275  O  O     . LEU A 1 656 ? 141.680 120.325 104.674 1.00 31.16 ?  656 LEU A O     1 
ATOM   5276  C  CB    . LEU A 1 656 ? 144.693 121.229 104.891 1.00 29.59 ?  656 LEU A CB    1 
ATOM   5277  C  CG    . LEU A 1 656 ? 145.835 122.240 104.975 1.00 30.46 ?  656 LEU A CG    1 
ATOM   5278  C  CD1   . LEU A 1 656 ? 146.961 121.705 105.845 1.00 26.80 ?  656 LEU A CD1   1 
ATOM   5279  C  CD2   . LEU A 1 656 ? 146.339 122.602 103.587 1.00 27.73 ?  656 LEU A CD2   1 
ATOM   5280  N  N     . PHE A 1 657 ? 142.747 119.490 102.878 1.00 26.53 ?  657 PHE A N     1 
ATOM   5281  C  CA    . PHE A 1 657 ? 141.863 118.340 102.723 1.00 28.20 ?  657 PHE A CA    1 
ATOM   5282  C  C     . PHE A 1 657 ? 142.699 117.080 102.893 1.00 36.33 ?  657 PHE A C     1 
ATOM   5283  O  O     . PHE A 1 657 ? 143.483 116.725 102.006 1.00 37.74 ?  657 PHE A O     1 
ATOM   5284  C  CB    . PHE A 1 657 ? 141.162 118.368 101.368 1.00 29.41 ?  657 PHE A CB    1 
ATOM   5285  C  CG    . PHE A 1 657 ? 140.422 119.645 101.102 1.00 32.69 ?  657 PHE A CG    1 
ATOM   5286  C  CD1   . PHE A 1 657 ? 139.135 119.825 101.573 1.00 30.22 ?  657 PHE A CD1   1 
ATOM   5287  C  CD2   . PHE A 1 657 ? 141.016 120.668 100.381 1.00 33.87 ?  657 PHE A CD2   1 
ATOM   5288  C  CE1   . PHE A 1 657 ? 138.455 121.001 101.331 1.00 32.64 ?  657 PHE A CE1   1 
ATOM   5289  C  CE2   . PHE A 1 657 ? 140.337 121.842 100.132 1.00 29.81 ?  657 PHE A CE2   1 
ATOM   5290  C  CZ    . PHE A 1 657 ? 139.056 122.010 100.609 1.00 32.98 ?  657 PHE A CZ    1 
ATOM   5291  N  N     . LEU A 1 658 ? 142.530 116.408 104.025 1.00 40.31 ?  658 LEU A N     1 
ATOM   5292  C  CA    . LEU A 1 658 ? 143.370 115.285 104.402 1.00 42.67 ?  658 LEU A CA    1 
ATOM   5293  C  C     . LEU A 1 658 ? 142.561 113.997 104.433 1.00 45.45 ?  658 LEU A C     1 
ATOM   5294  O  O     . LEU A 1 658 ? 141.349 114.007 104.664 1.00 46.68 ?  658 LEU A O     1 
ATOM   5295  C  CB    . LEU A 1 658 ? 144.009 115.521 105.772 1.00 40.37 ?  658 LEU A CB    1 
ATOM   5296  C  CG    . LEU A 1 658 ? 144.374 116.969 106.099 1.00 39.41 ?  658 LEU A CG    1 
ATOM   5297  C  CD1   . LEU A 1 658 ? 144.595 117.128 107.590 1.00 41.38 ?  658 LEU A CD1   1 
ATOM   5298  C  CD2   . LEU A 1 658 ? 145.600 117.412 105.318 1.00 42.05 ?  658 LEU A CD2   1 
ATOM   5299  N  N     . LYS A 1 659 ? 143.245 112.891 104.172 1.00 51.27 ?  659 LYS A N     1 
ATOM   5300  C  CA    . LYS A 1 659 ? 142.685 111.567 104.380 1.00 51.78 ?  659 LYS A CA    1 
ATOM   5301  C  C     . LYS A 1 659 ? 142.946 111.119 105.813 1.00 52.89 ?  659 LYS A C     1 
ATOM   5302  O  O     . LYS A 1 659 ? 143.864 111.599 106.483 1.00 54.58 ?  659 LYS A O     1 
ATOM   5303  C  CB    . LYS A 1 659 ? 143.285 110.564 103.394 1.00 54.80 ?  659 LYS A CB    1 
ATOM   5304  C  CG    . LYS A 1 659 ? 143.131 110.958 101.935 1.00 53.58 ?  659 LYS A CG    1 
ATOM   5305  C  CD    . LYS A 1 659 ? 143.548 109.826 101.010 1.00 53.18 ?  659 LYS A CD    1 
ATOM   5306  C  CE    . LYS A 1 659 ? 143.371 110.210 99.550  1.00 53.02 ?  659 LYS A CE    1 
ATOM   5307  N  NZ    . LYS A 1 659 ? 143.422 109.025 98.651  1.00 52.86 1  659 LYS A NZ    1 
ATOM   5308  N  N     . ASP A 1 660 ? 142.114 110.188 106.286 1.00 57.82 ?  660 ASP A N     1 
ATOM   5309  C  CA    . ASP A 1 660 ? 142.304 109.647 107.625 1.00 57.29 ?  660 ASP A CA    1 
ATOM   5310  C  C     . ASP A 1 660 ? 143.593 108.844 107.746 1.00 55.49 ?  660 ASP A C     1 
ATOM   5311  O  O     . ASP A 1 660 ? 144.067 108.622 108.865 1.00 56.14 ?  660 ASP A O     1 
ATOM   5312  C  CB    . ASP A 1 660 ? 141.107 108.780 108.018 1.00 58.51 ?  660 ASP A CB    1 
ATOM   5313  C  CG    . ASP A 1 660 ? 140.555 107.985 106.852 1.00 61.52 ?  660 ASP A CG    1 
ATOM   5314  O  OD1   . ASP A 1 660 ? 141.352 107.351 106.129 1.00 59.08 ?  660 ASP A OD1   1 
ATOM   5315  O  OD2   . ASP A 1 660 ? 139.321 107.996 106.656 1.00 61.60 -1 660 ASP A OD2   1 
ATOM   5316  N  N     . THR A 1 661 ? 144.169 108.410 106.622 1.00 53.18 ?  661 THR A N     1 
ATOM   5317  C  CA    . THR A 1 661 ? 145.382 107.602 106.678 1.00 55.32 ?  661 THR A CA    1 
ATOM   5318  C  C     . THR A 1 661 ? 146.601 108.443 107.037 1.00 54.64 ?  661 THR A C     1 
ATOM   5319  O  O     . THR A 1 661 ? 147.462 107.997 107.805 1.00 55.17 ?  661 THR A O     1 
ATOM   5320  C  CB    . THR A 1 661 ? 145.602 106.890 105.343 1.00 56.55 ?  661 THR A CB    1 
ATOM   5321  O  OG1   . THR A 1 661 ? 146.265 107.776 104.432 1.00 56.41 ?  661 THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1 661 ? 144.273 106.457 104.746 1.00 54.38 ?  661 THR A CG2   1 
ATOM   5323  N  N     . MET A 1 662 ? 146.698 109.655 106.495 1.00 52.78 ?  662 MET A N     1 
ATOM   5324  C  CA    . MET A 1 662 ? 147.874 110.476 106.740 1.00 52.47 ?  662 MET A CA    1 
ATOM   5325  C  C     . MET A 1 662 ? 147.921 110.938 108.193 1.00 51.28 ?  662 MET A C     1 
ATOM   5326  O  O     . MET A 1 662 ? 146.893 111.151 108.841 1.00 49.11 ?  662 MET A O     1 
ATOM   5327  C  CB    . MET A 1 662 ? 147.909 111.675 105.789 1.00 50.11 ?  662 MET A CB    1 
ATOM   5328  C  CG    . MET A 1 662 ? 147.392 112.982 106.362 1.00 51.94 ?  662 MET A CG    1 
ATOM   5329  S  SD    . MET A 1 662 ? 147.406 114.288 105.121 1.00 62.99 ?  662 MET A SD    1 
ATOM   5330  C  CE    . MET A 1 662 ? 146.480 113.511 103.803 1.00 48.13 ?  662 MET A CE    1 
ATOM   5331  N  N     . THR A 1 663 ? 149.139 111.066 108.704 1.00 45.64 ?  663 THR A N     1 
ATOM   5332  C  CA    . THR A 1 663 ? 149.397 111.330 110.108 1.00 44.52 ?  663 THR A CA    1 
ATOM   5333  C  C     . THR A 1 663 ? 149.682 112.815 110.324 1.00 44.92 ?  663 THR A C     1 
ATOM   5334  O  O     . THR A 1 663 ? 149.571 113.633 109.406 1.00 46.43 ?  663 THR A O     1 
ATOM   5335  C  CB    . THR A 1 663 ? 150.556 110.455 110.585 1.00 43.39 ?  663 THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 663 ? 151.796 111.127 110.332 1.00 42.25 ?  663 THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 663 ? 150.549 109.128 109.841 1.00 44.97 ?  663 THR A CG2   1 
ATOM   5338  N  N     . THR A 1 664 ? 150.054 113.173 111.556 1.00 39.16 ?  664 THR A N     1 
ATOM   5339  C  CA    . THR A 1 664 ? 150.393 114.559 111.851 1.00 38.73 ?  664 THR A CA    1 
ATOM   5340  C  C     . THR A 1 664 ? 151.688 114.992 111.181 1.00 37.04 ?  664 THR A C     1 
ATOM   5341  O  O     . THR A 1 664 ? 151.883 116.191 110.961 1.00 40.13 ?  664 THR A O     1 
ATOM   5342  C  CB    . THR A 1 664 ? 150.498 114.779 113.361 1.00 39.50 ?  664 THR A CB    1 
ATOM   5343  O  OG1   . THR A 1 664 ? 151.707 114.187 113.853 1.00 39.06 ?  664 THR A OG1   1 
ATOM   5344  C  CG2   . THR A 1 664 ? 149.303 114.172 114.076 1.00 36.70 ?  664 THR A CG2   1 
ATOM   5345  N  N     . ARG A 1 665 ? 152.577 114.051 110.855 1.00 37.74 ?  665 ARG A N     1 
ATOM   5346  C  CA    . ARG A 1 665 ? 153.775 114.405 110.101 1.00 34.74 ?  665 ARG A CA    1 
ATOM   5347  C  C     . ARG A 1 665 ? 153.413 114.930 108.719 1.00 39.12 ?  665 ARG A C     1 
ATOM   5348  O  O     . ARG A 1 665 ? 154.006 115.903 108.244 1.00 44.89 ?  665 ARG A O     1 
ATOM   5349  C  CB    . ARG A 1 665 ? 154.707 113.201 109.986 1.00 37.03 ?  665 ARG A CB    1 
ATOM   5350  C  CG    . ARG A 1 665 ? 155.751 113.331 108.890 1.00 35.80 ?  665 ARG A CG    1 
ATOM   5351  C  CD    . ARG A 1 665 ? 157.119 112.880 109.365 1.00 37.90 ?  665 ARG A CD    1 
ATOM   5352  N  NE    . ARG A 1 665 ? 158.102 112.899 108.289 1.00 40.76 ?  665 ARG A NE    1 
ATOM   5353  C  CZ    . ARG A 1 665 ? 158.371 111.867 107.500 1.00 42.19 ?  665 ARG A CZ    1 
ATOM   5354  N  NH1   . ARG A 1 665 ? 157.743 110.711 107.638 1.00 41.36 1  665 ARG A NH1   1 
ATOM   5355  N  NH2   . ARG A 1 665 ? 159.291 112.000 106.549 1.00 41.42 ?  665 ARG A NH2   1 
ATOM   5356  N  N     . ASP A 1 666 ? 152.436 114.304 108.061 1.00 37.63 ?  666 ASP A N     1 
ATOM   5357  C  CA    . ASP A 1 666 ? 151.997 114.784 106.756 1.00 36.14 ?  666 ASP A CA    1 
ATOM   5358  C  C     . ASP A 1 666 ? 151.353 116.162 106.859 1.00 39.97 ?  666 ASP A C     1 
ATOM   5359  O  O     . ASP A 1 666 ? 151.582 117.025 106.005 1.00 44.17 ?  666 ASP A O     1 
ATOM   5360  C  CB    . ASP A 1 666 ? 151.032 113.780 106.128 1.00 42.08 ?  666 ASP A CB    1 
ATOM   5361  C  CG    . ASP A 1 666 ? 151.681 112.436 105.870 1.00 46.23 ?  666 ASP A CG    1 
ATOM   5362  O  OD1   . ASP A 1 666 ? 152.755 112.407 105.236 1.00 44.32 ?  666 ASP A OD1   1 
ATOM   5363  O  OD2   . ASP A 1 666 ? 151.118 111.408 106.304 1.00 46.85 -1 666 ASP A OD2   1 
ATOM   5364  N  N     . LEU A 1 667 ? 150.546 116.385 107.898 1.00 33.15 ?  667 LEU A N     1 
ATOM   5365  C  CA    . LEU A 1 667 ? 149.947 117.700 108.102 1.00 30.35 ?  667 LEU A CA    1 
ATOM   5366  C  C     . LEU A 1 667 ? 151.016 118.759 108.330 1.00 30.18 ?  667 LEU A C     1 
ATOM   5367  O  O     . LEU A 1 667 ? 150.949 119.857 107.765 1.00 33.76 ?  667 LEU A O     1 
ATOM   5368  C  CB    . LEU A 1 667 ? 148.981 117.652 109.287 1.00 33.25 ?  667 LEU A CB    1 
ATOM   5369  C  CG    . LEU A 1 667 ? 147.699 118.482 109.216 1.00 35.96 ?  667 LEU A CG    1 
ATOM   5370  C  CD1   . LEU A 1 667 ? 146.750 118.058 110.320 1.00 35.10 ?  667 LEU A CD1   1 
ATOM   5371  C  CD2   . LEU A 1 667 ? 147.988 119.970 109.305 1.00 33.24 ?  667 LEU A CD2   1 
ATOM   5372  N  N     . ASN A 1 668 ? 152.016 118.445 109.158 1.00 30.42 ?  668 ASN A N     1 
ATOM   5373  C  CA    . ASN A 1 668 ? 153.104 119.382 109.399 1.00 27.03 ?  668 ASN A CA    1 
ATOM   5374  C  C     . ASN A 1 668 ? 153.902 119.637 108.129 1.00 27.13 ?  668 ASN A C     1 
ATOM   5375  O  O     . ASN A 1 668 ? 154.350 120.761 107.888 1.00 33.76 ?  668 ASN A O     1 
ATOM   5376  C  CB    . ASN A 1 668 ? 154.014 118.858 110.508 1.00 28.88 ?  668 ASN A CB    1 
ATOM   5377  C  CG    . ASN A 1 668 ? 153.541 119.255 111.889 1.00 31.15 ?  668 ASN A CG    1 
ATOM   5378  O  OD1   . ASN A 1 668 ? 153.717 118.511 112.852 1.00 39.82 ?  668 ASN A OD1   1 
ATOM   5379  N  ND2   . ASN A 1 668 ? 152.935 120.430 111.992 1.00 28.99 ?  668 ASN A ND2   1 
ATOM   5380  N  N     . ARG A 1 669 ? 154.100 118.603 107.309 1.00 29.15 ?  669 ARG A N     1 
ATOM   5381  C  CA    . ARG A 1 669 ? 154.802 118.784 106.043 1.00 30.94 ?  669 ARG A CA    1 
ATOM   5382  C  C     . ARG A 1 669 ? 154.027 119.699 105.108 1.00 28.85 ?  669 ARG A C     1 
ATOM   5383  O  O     . ARG A 1 669 ? 154.618 120.547 104.432 1.00 28.98 ?  669 ARG A O     1 
ATOM   5384  C  CB    . ARG A 1 669 ? 155.054 117.431 105.381 1.00 31.95 ?  669 ARG A CB    1 
ATOM   5385  C  CG    . ARG A 1 669 ? 156.500 116.983 105.422 1.00 29.86 ?  669 ARG A CG    1 
ATOM   5386  C  CD    . ARG A 1 669 ? 156.697 115.683 104.658 1.00 35.06 ?  669 ARG A CD    1 
ATOM   5387  N  NE    . ARG A 1 669 ? 156.886 115.905 103.229 1.00 33.74 ?  669 ARG A NE    1 
ATOM   5388  C  CZ    . ARG A 1 669 ? 157.983 116.411 102.682 1.00 34.89 ?  669 ARG A CZ    1 
ATOM   5389  N  NH1   . ARG A 1 669 ? 159.026 116.759 103.417 1.00 33.74 1  669 ARG A NH1   1 
ATOM   5390  N  NH2   . ARG A 1 669 ? 158.035 116.571 101.363 1.00 37.58 ?  669 ARG A NH2   1 
ATOM   5391  N  N     . ILE A 1 670 ? 152.703 119.538 105.049 1.00 25.18 ?  670 ILE A N     1 
ATOM   5392  C  CA    . ILE A 1 670 ? 151.888 120.433 104.230 1.00 25.57 ?  670 ILE A CA    1 
ATOM   5393  C  C     . ILE A 1 670 ? 151.982 121.862 104.749 1.00 27.89 ?  670 ILE A C     1 
ATOM   5394  O  O     . ILE A 1 670 ? 152.105 122.813 103.969 1.00 32.77 ?  670 ILE A O     1 
ATOM   5395  C  CB    . ILE A 1 670 ? 150.429 119.945 104.178 1.00 28.03 ?  670 ILE A CB    1 
ATOM   5396  C  CG1   . ILE A 1 670 ? 150.350 118.544 103.572 1.00 30.18 ?  670 ILE A CG1   1 
ATOM   5397  C  CG2   . ILE A 1 670 ? 149.577 120.907 103.370 1.00 25.40 ?  670 ILE A CG2   1 
ATOM   5398  C  CD1   . ILE A 1 670 ? 149.096 117.790 103.952 1.00 26.89 ?  670 ILE A CD1   1 
ATOM   5399  N  N     . ASP A 1 671 ? 151.928 122.037 106.072 1.00 24.47 ?  671 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 671 ? 152.038 123.376 106.647 1.00 21.06 ?  671 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 671 ? 153.393 124.006 106.341 1.00 25.88 ?  671 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 671 ? 153.475 125.193 106.006 1.00 27.34 ?  671 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 671 ? 151.805 123.320 108.156 1.00 22.89 ?  671 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 671 ? 150.422 122.816 108.515 1.00 34.47 ?  671 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 671 ? 149.520 122.888 107.654 1.00 34.26 ?  671 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 671 ? 150.237 122.347 109.658 1.00 35.03 -1 671 ASP A OD2   1 
ATOM   5407  N  N     . LEU A 1 672 ? 154.468 123.225 106.450 1.00 23.57 ?  672 LEU A N     1 
ATOM   5408  C  CA    . LEU A 1 672 ? 155.802 123.755 106.196 1.00 19.62 ?  672 LEU A CA    1 
ATOM   5409  C  C     . LEU A 1 672 ? 156.027 124.037 104.718 1.00 18.97 ?  672 LEU A C     1 
ATOM   5410  O  O     . LEU A 1 672 ? 156.751 124.976 104.374 1.00 24.16 ?  672 LEU A O     1 
ATOM   5411  C  CB    . LEU A 1 672 ? 156.860 122.785 106.720 1.00 27.26 ?  672 LEU A CB    1 
ATOM   5412  C  CG    . LEU A 1 672 ? 156.891 122.594 108.237 1.00 23.67 ?  672 LEU A CG    1 
ATOM   5413  C  CD1   . LEU A 1 672 ? 157.711 121.370 108.602 1.00 21.82 ?  672 LEU A CD1   1 
ATOM   5414  C  CD2   . LEU A 1 672 ? 157.429 123.836 108.923 1.00 20.76 ?  672 LEU A CD2   1 
ATOM   5415  N  N     . TYR A 1 673 ? 155.428 123.239 103.831 1.00 21.31 ?  673 TYR A N     1 
ATOM   5416  C  CA    . TYR A 1 673 ? 155.515 123.530 102.405 1.00 18.01 ?  673 TYR A CA    1 
ATOM   5417  C  C     . TYR A 1 673 ? 154.699 124.765 102.050 1.00 21.32 ?  673 TYR A C     1 
ATOM   5418  O  O     . TYR A 1 673 ? 155.085 125.539 101.167 1.00 23.54 ?  673 TYR A O     1 
ATOM   5419  C  CB    . TYR A 1 673 ? 155.048 122.321 101.595 1.00 16.74 ?  673 TYR A CB    1 
ATOM   5420  C  CG    . TYR A 1 673 ? 155.198 122.496 100.103 1.00 22.24 ?  673 TYR A CG    1 
ATOM   5421  C  CD1   . TYR A 1 673 ? 156.452 122.612 99.523  1.00 23.24 ?  673 TYR A CD1   1 
ATOM   5422  C  CD2   . TYR A 1 673 ? 154.086 122.545 99.275  1.00 20.22 ?  673 TYR A CD2   1 
ATOM   5423  C  CE1   . TYR A 1 673 ? 156.596 122.771 98.161  1.00 18.97 ?  673 TYR A CE1   1 
ATOM   5424  C  CE2   . TYR A 1 673 ? 154.219 122.705 97.911  1.00 22.76 ?  673 TYR A CE2   1 
ATOM   5425  C  CZ    . TYR A 1 673 ? 155.476 122.816 97.360  1.00 21.41 ?  673 TYR A CZ    1 
ATOM   5426  O  OH    . TYR A 1 673 ? 155.616 122.976 96.002  1.00 26.15 ?  673 TYR A OH    1 
ATOM   5427  N  N     . ALA A 1 674 ? 153.563 124.960 102.724 1.00 21.02 ?  674 ALA A N     1 
ATOM   5428  C  CA    . ALA A 1 674 ? 152.798 126.188 102.553 1.00 16.37 ?  674 ALA A CA    1 
ATOM   5429  C  C     . ALA A 1 674 ? 153.604 127.398 103.005 1.00 16.90 ?  674 ALA A C     1 
ATOM   5430  O  O     . ALA A 1 674 ? 153.627 128.431 102.327 1.00 25.79 ?  674 ALA A O     1 
ATOM   5431  C  CB    . ALA A 1 674 ? 151.484 126.091 103.325 1.00 18.01 ?  674 ALA A CB    1 
ATOM   5432  N  N     . HIS A 1 675 ? 154.279 127.282 104.149 1.00 15.15 ?  675 HIS A N     1 
ATOM   5433  C  CA    . HIS A 1 675 ? 155.150 128.357 104.609 1.00 15.76 ?  675 HIS A CA    1 
ATOM   5434  C  C     . HIS A 1 675 ? 156.284 128.608 103.620 1.00 20.74 ?  675 HIS A C     1 
ATOM   5435  O  O     . HIS A 1 675 ? 156.643 129.759 103.353 1.00 27.09 ?  675 HIS A O     1 
ATOM   5436  C  CB    . HIS A 1 675 ? 155.705 128.023 105.994 1.00 12.33 ?  675 HIS A CB    1 
ATOM   5437  C  CG    . HIS A 1 675 ? 156.698 129.018 106.501 1.00 21.52 ?  675 HIS A CG    1 
ATOM   5438  N  ND1   . HIS A 1 675 ? 158.059 128.806 106.443 1.00 24.93 ?  675 HIS A ND1   1 
ATOM   5439  C  CD2   . HIS A 1 675 ? 156.531 130.234 107.072 1.00 19.57 ?  675 HIS A CD2   1 
ATOM   5440  C  CE1   . HIS A 1 675 ? 158.686 129.847 106.957 1.00 25.63 ?  675 HIS A CE1   1 
ATOM   5441  N  NE2   . HIS A 1 675 ? 157.783 130.728 107.347 1.00 22.92 ?  675 HIS A NE2   1 
ATOM   5442  N  N     . HIS A 1 676 ? 156.859 127.538 103.071 1.00 19.67 ?  676 HIS A N     1 
ATOM   5443  C  CA    . HIS A 1 676 ? 157.944 127.676 102.106 1.00 20.42 ?  676 HIS A CA    1 
ATOM   5444  C  C     . HIS A 1 676 ? 157.461 128.306 100.805 1.00 24.31 ?  676 HIS A C     1 
ATOM   5445  O  O     . HIS A 1 676 ? 158.171 129.117 100.200 1.00 25.05 ?  676 HIS A O     1 
ATOM   5446  C  CB    . HIS A 1 676 ? 158.576 126.311 101.838 1.00 23.92 ?  676 HIS A CB    1 
ATOM   5447  C  CG    . HIS A 1 676 ? 159.512 126.294 100.671 1.00 25.00 ?  676 HIS A CG    1 
ATOM   5448  N  ND1   . HIS A 1 676 ? 160.735 126.929 100.688 1.00 20.88 ?  676 HIS A ND1   1 
ATOM   5449  C  CD2   . HIS A 1 676 ? 159.404 125.719 99.450  1.00 19.79 ?  676 HIS A CD2   1 
ATOM   5450  C  CE1   . HIS A 1 676 ? 161.339 126.745 99.528  1.00 25.77 ?  676 HIS A CE1   1 
ATOM   5451  N  NE2   . HIS A 1 676 ? 160.553 126.014 98.759  1.00 28.82 ?  676 HIS A NE2   1 
ATOM   5452  N  N     . ARG A 1 677 ? 156.258 127.949 100.361 1.00 21.42 ?  677 ARG A N     1 
ATOM   5453  C  CA    . ARG A 1 677 ? 155.738 128.422 99.084  1.00 20.36 ?  677 ARG A CA    1 
ATOM   5454  C  C     . ARG A 1 677 ? 155.115 129.807 99.170  1.00 24.10 ?  677 ARG A C     1 
ATOM   5455  O  O     . ARG A 1 677 ? 154.648 130.321 98.148  1.00 25.29 ?  677 ARG A O     1 
ATOM   5456  C  CB    . ARG A 1 677 ? 154.711 127.429 98.536  1.00 18.85 ?  677 ARG A CB    1 
ATOM   5457  C  CG    . ARG A 1 677 ? 155.322 126.278 97.758  1.00 20.21 ?  677 ARG A CG    1 
ATOM   5458  C  CD    . ARG A 1 677 ? 155.941 126.757 96.457  1.00 20.22 ?  677 ARG A CD    1 
ATOM   5459  N  NE    . ARG A 1 677 ? 154.971 126.787 95.369  1.00 25.02 ?  677 ARG A NE    1 
ATOM   5460  C  CZ    . ARG A 1 677 ? 154.550 127.893 94.772  1.00 27.26 ?  677 ARG A CZ    1 
ATOM   5461  N  NH1   . ARG A 1 677 ? 154.995 129.086 95.133  1.00 21.21 1  677 ARG A NH1   1 
ATOM   5462  N  NH2   . ARG A 1 677 ? 153.660 127.801 93.788  1.00 22.30 ?  677 ARG A NH2   1 
ATOM   5463  N  N     . GLY A 1 678 ? 155.097 130.422 100.349 1.00 20.70 ?  678 GLY A N     1 
ATOM   5464  C  CA    . GLY A 1 678 ? 154.542 131.750 100.497 1.00 16.08 ?  678 GLY A CA    1 
ATOM   5465  C  C     . GLY A 1 678 ? 153.076 131.802 100.848 1.00 16.22 ?  678 GLY A C     1 
ATOM   5466  O  O     . GLY A 1 678 ? 152.457 132.861 100.695 1.00 23.71 ?  678 GLY A O     1 
ATOM   5467  N  N     . ILE A 1 679 ? 152.494 130.693 101.304 1.00 15.50 ?  679 ILE A N     1 
ATOM   5468  C  CA    . ILE A 1 679 ? 151.103 130.703 101.737 1.00 11.34 ?  679 ILE A CA    1 
ATOM   5469  C  C     . ILE A 1 679 ? 150.977 131.581 102.972 1.00 15.26 ?  679 ILE A C     1 
ATOM   5470  O  O     . ILE A 1 679 ? 151.755 131.457 103.926 1.00 23.09 ?  679 ILE A O     1 
ATOM   5471  C  CB    . ILE A 1 679 ? 150.612 129.275 102.015 1.00 15.65 ?  679 ILE A CB    1 
ATOM   5472  C  CG1   . ILE A 1 679 ? 150.564 128.462 100.722 1.00 15.46 ?  679 ILE A CG1   1 
ATOM   5473  C  CG2   . ILE A 1 679 ? 149.252 129.295 102.689 1.00 15.73 ?  679 ILE A CG2   1 
ATOM   5474  C  CD1   . ILE A 1 679 ? 149.739 129.095 99.651  1.00 13.41 ?  679 ILE A CD1   1 
ATOM   5475  N  N     . LYS A 1 680 ? 150.000 132.483 102.955 1.00 13.20 ?  680 LYS A N     1 
ATOM   5476  C  CA    . LYS A 1 680 ? 149.823 133.424 104.052 1.00 8.26  ?  680 LYS A CA    1 
ATOM   5477  C  C     . LYS A 1 680 ? 149.028 132.820 105.205 1.00 8.16  ?  680 LYS A C     1 
ATOM   5478  O  O     . LYS A 1 680 ? 149.412 132.965 106.369 1.00 16.91 ?  680 LYS A O     1 
ATOM   5479  C  CB    . LYS A 1 680 ? 149.138 134.694 103.542 1.00 8.86  ?  680 LYS A CB    1 
ATOM   5480  C  CG    . LYS A 1 680 ? 150.000 135.545 102.628 1.00 0.00  ?  680 LYS A CG    1 
ATOM   5481  C  CD    . LYS A 1 680 ? 149.258 136.793 102.190 1.00 6.45  ?  680 LYS A CD    1 
ATOM   5482  C  CE    . LYS A 1 680 ? 149.945 137.469 101.023 1.00 13.22 ?  680 LYS A CE    1 
ATOM   5483  N  NZ    . LYS A 1 680 ? 149.265 138.734 100.637 1.00 10.77 1  680 LYS A NZ    1 
ATOM   5484  N  N     . THR A 1 681 ? 147.924 132.143 104.902 1.00 15.71 ?  681 THR A N     1 
ATOM   5485  C  CA    . THR A 1 681 ? 147.061 131.565 105.918 1.00 8.89  ?  681 THR A CA    1 
ATOM   5486  C  C     . THR A 1 681 ? 146.649 130.156 105.517 1.00 15.33 ?  681 THR A C     1 
ATOM   5487  O  O     . THR A 1 681 ? 146.521 129.843 104.332 1.00 22.36 ?  681 THR A O     1 
ATOM   5488  C  CB    . THR A 1 681 ? 145.797 132.409 106.146 1.00 16.05 ?  681 THR A CB    1 
ATOM   5489  O  OG1   . THR A 1 681 ? 145.180 132.701 104.886 1.00 30.21 ?  681 THR A OG1   1 
ATOM   5490  C  CG2   . THR A 1 681 ? 146.130 133.708 106.848 1.00 3.10  ?  681 THR A CG2   1 
ATOM   5491  N  N     . ILE A 1 682 ? 146.439 129.312 106.523 1.00 15.27 ?  682 ILE A N     1 
ATOM   5492  C  CA    . ILE A 1 682 ? 145.843 127.994 106.347 1.00 9.32  ?  682 ILE A CA    1 
ATOM   5493  C  C     . ILE A 1 682 ? 144.569 127.949 107.178 1.00 13.63 ?  682 ILE A C     1 
ATOM   5494  O  O     . ILE A 1 682 ? 144.606 128.193 108.389 1.00 21.07 ?  682 ILE A O     1 
ATOM   5495  C  CB    . ILE A 1 682 ? 146.807 126.868 106.755 1.00 12.93 ?  682 ILE A CB    1 
ATOM   5496  C  CG1   . ILE A 1 682 ? 148.239 127.208 106.342 1.00 17.99 ?  682 ILE A CG1   1 
ATOM   5497  C  CG2   . ILE A 1 682 ? 146.387 125.572 106.110 1.00 20.80 ?  682 ILE A CG2   1 
ATOM   5498  C  CD1   . ILE A 1 682 ? 149.219 126.080 106.568 1.00 19.45 ?  682 ILE A CD1   1 
ATOM   5499  N  N     . TYR A 1 683 ? 143.445 127.651 106.526 1.00 18.77 ?  683 TYR A N     1 
ATOM   5500  C  CA    . TYR A 1 683 ? 142.149 127.791 107.189 1.00 12.07 ?  683 TYR A CA    1 
ATOM   5501  C  C     . TYR A 1 683 ? 141.797 126.561 108.024 1.00 19.43 ?  683 TYR A C     1 
ATOM   5502  O  O     . TYR A 1 683 ? 141.706 126.636 109.251 1.00 32.31 ?  683 TYR A O     1 
ATOM   5503  C  CB    . TYR A 1 683 ? 141.063 128.070 106.143 1.00 18.00 ?  683 TYR A CB    1 
ATOM   5504  C  CG    . TYR A 1 683 ? 139.707 128.408 106.721 1.00 16.18 ?  683 TYR A CG    1 
ATOM   5505  C  CD1   . TYR A 1 683 ? 139.583 128.902 108.013 1.00 12.18 ?  683 TYR A CD1   1 
ATOM   5506  C  CD2   . TYR A 1 683 ? 138.552 128.243 105.971 1.00 9.75  ?  683 TYR A CD2   1 
ATOM   5507  C  CE1   . TYR A 1 683 ? 138.350 129.214 108.542 1.00 15.88 ?  683 TYR A CE1   1 
ATOM   5508  C  CE2   . TYR A 1 683 ? 137.313 128.554 106.493 1.00 18.37 ?  683 TYR A CE2   1 
ATOM   5509  C  CZ    . TYR A 1 683 ? 137.219 129.040 107.778 1.00 19.26 ?  683 TYR A CZ    1 
ATOM   5510  O  OH    . TYR A 1 683 ? 135.987 129.350 108.304 1.00 26.27 ?  683 TYR A OH    1 
ATOM   5511  N  N     . TYR A 1 684 ? 141.615 125.416 107.377 1.00 29.27 ?  684 TYR A N     1 
ATOM   5512  C  CA    . TYR A 1 684 ? 141.060 124.258 108.057 1.00 25.72 ?  684 TYR A CA    1 
ATOM   5513  C  C     . TYR A 1 684 ? 141.780 122.999 107.609 1.00 32.85 ?  684 TYR A C     1 
ATOM   5514  O  O     . TYR A 1 684 ? 142.361 122.947 106.522 1.00 36.53 ?  684 TYR A O     1 
ATOM   5515  C  CB    . TYR A 1 684 ? 139.556 124.118 107.786 1.00 23.92 ?  684 TYR A CB    1 
ATOM   5516  C  CG    . TYR A 1 684 ? 138.678 124.672 108.883 1.00 22.24 ?  684 TYR A CG    1 
ATOM   5517  C  CD1   . TYR A 1 684 ? 138.805 124.230 110.193 1.00 26.54 ?  684 TYR A CD1   1 
ATOM   5518  C  CD2   . TYR A 1 684 ? 137.720 125.638 108.608 1.00 29.36 ?  684 TYR A CD2   1 
ATOM   5519  C  CE1   . TYR A 1 684 ? 138.002 124.734 111.198 1.00 30.37 ?  684 TYR A CE1   1 
ATOM   5520  C  CE2   . TYR A 1 684 ? 136.913 126.151 109.606 1.00 26.07 ?  684 TYR A CE2   1 
ATOM   5521  C  CZ    . TYR A 1 684 ? 137.058 125.695 110.898 1.00 29.63 ?  684 TYR A CZ    1 
ATOM   5522  O  OH    . TYR A 1 684 ? 136.257 126.202 111.894 1.00 32.26 ?  684 TYR A OH    1 
ATOM   5523  N  N     . ALA A 1 685 ? 141.737 121.984 108.466 1.00 31.03 ?  685 ALA A N     1 
ATOM   5524  C  CA    . ALA A 1 685 ? 142.246 120.652 108.164 1.00 32.41 ?  685 ALA A CA    1 
ATOM   5525  C  C     . ALA A 1 685 ? 141.053 119.704 108.229 1.00 36.55 ?  685 ALA A C     1 
ATOM   5526  O  O     . ALA A 1 685 ? 140.775 119.105 109.270 1.00 43.59 ?  685 ALA A O     1 
ATOM   5527  C  CB    . ALA A 1 685 ? 143.352 120.246 109.131 1.00 32.11 ?  685 ALA A CB    1 
ATOM   5528  N  N     . ARG A 1 686 ? 140.342 119.579 107.111 1.00 32.51 ?  686 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 686 ? 139.177 118.712 107.029 1.00 33.05 ?  686 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 686 ? 139.630 117.298 106.691 1.00 38.70 ?  686 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 686 ? 140.204 117.064 105.622 1.00 40.64 ?  686 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 686 ? 138.204 119.232 105.974 1.00 38.13 ?  686 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 686 ? 137.527 120.539 106.341 1.00 38.73 ?  686 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 686 ? 136.301 120.784 105.480 1.00 39.90 ?  686 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 686 ? 135.364 119.668 105.528 1.00 42.70 ?  686 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 686 ? 134.047 119.800 105.594 1.00 42.66 ?  686 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 686 ? 133.472 120.992 105.617 1.00 41.77 1  686 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 686 ? 133.286 118.710 105.636 1.00 42.47 ?  686 ARG A NH2   1 
ATOM   5539  N  N     . THR A 1 687 ? 139.377 116.361 107.599 1.00 48.40 ?  687 THR A N     1 
ATOM   5540  C  CA    . THR A 1 687 ? 139.746 114.967 107.409 1.00 46.64 ?  687 THR A CA    1 
ATOM   5541  C  C     . THR A 1 687 ? 138.547 114.184 106.893 1.00 47.93 ?  687 THR A C     1 
ATOM   5542  O  O     . THR A 1 687 ? 137.445 114.282 107.440 1.00 50.75 ?  687 THR A O     1 
ATOM   5543  C  CB    . THR A 1 687 ? 140.255 114.352 108.716 1.00 46.66 ?  687 THR A CB    1 
ATOM   5544  O  OG1   . THR A 1 687 ? 141.568 114.852 109.004 1.00 48.39 ?  687 THR A OG1   1 
ATOM   5545  C  CG2   . THR A 1 687 ? 140.311 112.835 108.613 1.00 47.30 ?  687 THR A CG2   1 
ATOM   5546  N  N     . LYS A 1 688 ? 138.769 113.411 105.836 1.00 48.04 ?  688 LYS A N     1 
ATOM   5547  C  CA    . LYS A 1 688 ? 137.706 112.616 105.234 1.00 48.98 ?  688 LYS A CA    1 
ATOM   5548  C  C     . LYS A 1 688 ? 137.476 111.331 106.021 1.00 53.36 ?  688 LYS A C     1 
ATOM   5549  O  O     . LYS A 1 688 ? 138.401 110.785 106.622 1.00 55.18 ?  688 LYS A O     1 
ATOM   5550  C  CB    . LYS A 1 688 ? 138.039 112.288 103.777 1.00 49.54 ?  688 LYS A CB    1 
ATOM   5551  C  CG    . LYS A 1 688 ? 136.908 111.613 103.021 1.00 48.07 ?  688 LYS A CG    1 
ATOM   5552  C  CD    . LYS A 1 688 ? 137.279 111.375 101.569 1.00 47.51 ?  688 LYS A CD    1 
ATOM   5553  C  CE    . LYS A 1 688 ? 136.124 110.752 100.803 1.00 51.68 ?  688 LYS A CE    1 
ATOM   5554  N  NZ    . LYS A 1 688 ? 136.462 110.536 99.369  1.00 52.23 ?  688 LYS A NZ    1 
ATOM   5555  N  N     . VAL B 1 6   ? 154.077 121.303 165.953 1.00 57.44 ?  6   VAL B N     1 
ATOM   5556  C  CA    . VAL B 1 6   ? 153.000 122.263 166.158 1.00 58.35 ?  6   VAL B CA    1 
ATOM   5557  C  C     . VAL B 1 6   ? 153.467 123.410 167.048 1.00 60.21 ?  6   VAL B C     1 
ATOM   5558  O  O     . VAL B 1 6   ? 154.250 123.203 167.975 1.00 58.78 ?  6   VAL B O     1 
ATOM   5559  C  CB    . VAL B 1 6   ? 151.754 121.580 166.755 1.00 58.16 ?  6   VAL B CB    1 
ATOM   5560  C  CG1   . VAL B 1 6   ? 151.079 120.708 165.709 1.00 58.66 ?  6   VAL B CG1   1 
ATOM   5561  C  CG2   . VAL B 1 6   ? 152.132 120.757 167.974 1.00 58.25 ?  6   VAL B CG2   1 
ATOM   5562  N  N     . PRO B 1 7   ? 152.996 124.619 166.756 1.00 57.76 ?  7   PRO B N     1 
ATOM   5563  C  CA    . PRO B 1 7   ? 153.398 125.783 167.553 1.00 53.33 ?  7   PRO B CA    1 
ATOM   5564  C  C     . PRO B 1 7   ? 152.867 125.705 168.977 1.00 52.92 ?  7   PRO B C     1 
ATOM   5565  O  O     . PRO B 1 7   ? 151.861 125.054 169.266 1.00 55.02 ?  7   PRO B O     1 
ATOM   5566  C  CB    . PRO B 1 7   ? 152.782 126.966 166.798 1.00 52.57 ?  7   PRO B CB    1 
ATOM   5567  C  CG    . PRO B 1 7   ? 152.464 126.451 165.435 1.00 52.52 ?  7   PRO B CG    1 
ATOM   5568  C  CD    . PRO B 1 7   ? 152.178 124.994 165.592 1.00 54.44 ?  7   PRO B CD    1 
ATOM   5569  N  N     . LYS B 1 8   ? 153.578 126.390 169.876 1.00 50.58 ?  8   LYS B N     1 
ATOM   5570  C  CA    . LYS B 1 8   ? 153.199 126.383 171.287 1.00 49.37 ?  8   LYS B CA    1 
ATOM   5571  C  C     . LYS B 1 8   ? 151.828 127.014 171.498 1.00 52.20 ?  8   LYS B C     1 
ATOM   5572  O  O     . LYS B 1 8   ? 151.008 126.493 172.264 1.00 54.02 ?  8   LYS B O     1 
ATOM   5573  C  CB    . LYS B 1 8   ? 154.258 127.108 172.115 1.00 51.24 ?  8   LYS B CB    1 
ATOM   5574  C  CG    . LYS B 1 8   ? 153.790 127.514 173.502 1.00 52.38 ?  8   LYS B CG    1 
ATOM   5575  C  CD    . LYS B 1 8   ? 154.955 127.636 174.468 1.00 51.18 ?  8   LYS B CD    1 
ATOM   5576  C  CE    . LYS B 1 8   ? 154.468 127.836 175.893 1.00 51.50 ?  8   LYS B CE    1 
ATOM   5577  N  NZ    . LYS B 1 8   ? 154.462 129.273 176.282 1.00 52.01 1  8   LYS B NZ    1 
ATOM   5578  N  N     . TRP B 1 9   ? 151.560 128.139 170.829 1.00 53.51 ?  9   TRP B N     1 
ATOM   5579  C  CA    . TRP B 1 9   ? 150.255 128.774 170.968 1.00 51.21 ?  9   TRP B CA    1 
ATOM   5580  C  C     . TRP B 1 9   ? 149.147 127.895 170.407 1.00 49.73 ?  9   TRP B C     1 
ATOM   5581  O  O     . TRP B 1 9   ? 148.026 127.911 170.924 1.00 51.44 ?  9   TRP B O     1 
ATOM   5582  C  CB    . TRP B 1 9   ? 150.243 130.143 170.286 1.00 51.68 ?  9   TRP B CB    1 
ATOM   5583  C  CG    . TRP B 1 9   ? 150.639 130.124 168.843 1.00 49.36 ?  9   TRP B CG    1 
ATOM   5584  C  CD1   . TRP B 1 9   ? 149.813 129.959 167.771 1.00 48.25 ?  9   TRP B CD1   1 
ATOM   5585  C  CD2   . TRP B 1 9   ? 151.957 130.302 168.311 1.00 49.96 ?  9   TRP B CD2   1 
ATOM   5586  N  NE1   . TRP B 1 9   ? 150.534 130.013 166.604 1.00 47.82 ?  9   TRP B NE1   1 
ATOM   5587  C  CE2   . TRP B 1 9   ? 151.853 130.224 166.908 1.00 49.58 ?  9   TRP B CE2   1 
ATOM   5588  C  CE3   . TRP B 1 9   ? 153.214 130.514 168.883 1.00 47.79 ?  9   TRP B CE3   1 
ATOM   5589  C  CZ2   . TRP B 1 9   ? 152.958 130.349 166.070 1.00 48.99 ?  9   TRP B CZ2   1 
ATOM   5590  C  CZ3   . TRP B 1 9   ? 154.309 130.638 168.050 1.00 49.28 ?  9   TRP B CZ3   1 
ATOM   5591  C  CH2   . TRP B 1 9   ? 154.174 130.553 166.659 1.00 50.26 ?  9   TRP B CH2   1 
ATOM   5592  N  N     . ILE B 1 10  ? 149.441 127.117 169.364 1.00 52.27 ?  10  ILE B N     1 
ATOM   5593  C  CA    . ILE B 1 10  ? 148.452 126.190 168.827 1.00 52.32 ?  10  ILE B CA    1 
ATOM   5594  C  C     . ILE B 1 10  ? 148.102 125.127 169.861 1.00 53.45 ?  10  ILE B C     1 
ATOM   5595  O  O     . ILE B 1 10  ? 146.927 124.791 170.054 1.00 55.24 ?  10  ILE B O     1 
ATOM   5596  C  CB    . ILE B 1 10  ? 148.969 125.566 167.519 1.00 52.71 ?  10  ILE B CB    1 
ATOM   5597  C  CG1   . ILE B 1 10  ? 148.925 126.596 166.386 1.00 52.31 ?  10  ILE B CG1   1 
ATOM   5598  C  CG2   . ILE B 1 10  ? 148.169 124.322 167.161 1.00 53.05 ?  10  ILE B CG2   1 
ATOM   5599  C  CD1   . ILE B 1 10  ? 147.646 126.588 165.588 1.00 53.46 ?  10  ILE B CD1   1 
ATOM   5600  N  N     . GLN B 1 11  ? 149.112 124.585 170.546 1.00 53.92 ?  11  GLN B N     1 
ATOM   5601  C  CA    . GLN B 1 11  ? 148.853 123.611 171.603 1.00 55.14 ?  11  GLN B CA    1 
ATOM   5602  C  C     . GLN B 1 11  ? 148.062 124.233 172.746 1.00 54.84 ?  11  GLN B C     1 
ATOM   5603  O  O     . GLN B 1 11  ? 147.138 123.611 173.284 1.00 57.06 ?  11  GLN B O     1 
ATOM   5604  C  CB    . GLN B 1 11  ? 150.170 123.034 172.122 1.00 56.03 ?  11  GLN B CB    1 
ATOM   5605  C  CG    . GLN B 1 11  ? 151.049 122.420 171.048 1.00 56.59 ?  11  GLN B CG    1 
ATOM   5606  C  CD    . GLN B 1 11  ? 152.511 122.390 171.445 1.00 58.95 ?  11  GLN B CD    1 
ATOM   5607  O  OE1   . GLN B 1 11  ? 153.399 122.439 170.594 1.00 58.89 ?  11  GLN B OE1   1 
ATOM   5608  N  NE2   . GLN B 1 11  ? 152.769 122.313 172.745 1.00 55.94 ?  11  GLN B NE2   1 
ATOM   5609  N  N     . LEU B 1 12  ? 148.409 125.463 173.133 1.00 51.73 ?  12  LEU B N     1 
ATOM   5610  C  CA    . LEU B 1 12  ? 147.682 126.122 174.213 1.00 50.64 ?  12  LEU B CA    1 
ATOM   5611  C  C     . LEU B 1 12  ? 146.228 126.374 173.829 1.00 51.29 ?  12  LEU B C     1 
ATOM   5612  O  O     . LEU B 1 12  ? 145.327 126.244 174.666 1.00 53.55 ?  12  LEU B O     1 
ATOM   5613  C  CB    . LEU B 1 12  ? 148.378 127.428 174.592 1.00 52.10 ?  12  LEU B CB    1 
ATOM   5614  C  CG    . LEU B 1 12  ? 149.576 127.278 175.529 1.00 52.39 ?  12  LEU B CG    1 
ATOM   5615  C  CD1   . LEU B 1 12  ? 150.427 128.538 175.527 1.00 52.91 ?  12  LEU B CD1   1 
ATOM   5616  C  CD2   . LEU B 1 12  ? 149.114 126.940 176.936 1.00 51.76 ?  12  LEU B CD2   1 
ATOM   5617  N  N     . ASN B 1 13  ? 145.982 126.739 172.569 1.00 51.33 ?  13  ASN B N     1 
ATOM   5618  C  CA    . ASN B 1 13  ? 144.613 126.951 172.110 1.00 49.42 ?  13  ASN B CA    1 
ATOM   5619  C  C     . ASN B 1 13  ? 143.843 125.638 172.038 1.00 52.08 ?  13  ASN B C     1 
ATOM   5620  O  O     . ASN B 1 13  ? 142.645 125.598 172.341 1.00 56.58 ?  13  ASN B O     1 
ATOM   5621  C  CB    . ASN B 1 13  ? 144.621 127.649 170.750 1.00 51.33 ?  13  ASN B CB    1 
ATOM   5622  C  CG    . ASN B 1 13  ? 143.232 127.824 170.178 1.00 50.05 ?  13  ASN B CG    1 
ATOM   5623  O  OD1   . ASN B 1 13  ? 142.848 127.142 169.230 1.00 50.41 ?  13  ASN B OD1   1 
ATOM   5624  N  ND2   . ASN B 1 13  ? 142.466 128.743 170.755 1.00 51.28 ?  13  ASN B ND2   1 
ATOM   5625  N  N     . ASN B 1 14  ? 144.505 124.554 171.631 1.00 53.76 ?  14  ASN B N     1 
ATOM   5626  C  CA    . ASN B 1 14  ? 143.851 123.251 171.622 1.00 52.32 ?  14  ASN B CA    1 
ATOM   5627  C  C     . ASN B 1 14  ? 143.619 122.717 173.027 1.00 53.34 ?  14  ASN B C     1 
ATOM   5628  O  O     . ASN B 1 14  ? 142.775 121.835 173.212 1.00 56.59 ?  14  ASN B O     1 
ATOM   5629  C  CB    . ASN B 1 14  ? 144.675 122.250 170.812 1.00 52.91 ?  14  ASN B CB    1 
ATOM   5630  C  CG    . ASN B 1 14  ? 144.693 122.575 169.335 1.00 55.92 ?  14  ASN B CG    1 
ATOM   5631  O  OD1   . ASN B 1 14  ? 143.980 123.467 168.877 1.00 58.01 ?  14  ASN B OD1   1 
ATOM   5632  N  ND2   . ASN B 1 14  ? 145.508 121.850 168.578 1.00 54.69 ?  14  ASN B ND2   1 
ATOM   5633  N  N     . GLU B 1 15  ? 144.351 123.232 174.016 1.00 56.23 ?  15  GLU B N     1 
ATOM   5634  C  CA    . GLU B 1 15  ? 144.144 122.831 175.403 1.00 56.56 ?  15  GLU B CA    1 
ATOM   5635  C  C     . GLU B 1 15  ? 142.803 123.288 175.963 1.00 57.08 ?  15  GLU B C     1 
ATOM   5636  O  O     . GLU B 1 15  ? 142.432 122.848 177.057 1.00 60.06 ?  15  GLU B O     1 
ATOM   5637  C  CB    . GLU B 1 15  ? 145.277 123.369 176.278 1.00 55.53 ?  15  GLU B CB    1 
ATOM   5638  C  CG    . GLU B 1 15  ? 146.386 122.363 176.542 1.00 57.49 ?  15  GLU B CG    1 
ATOM   5639  C  CD    . GLU B 1 15  ? 147.703 123.022 176.898 1.00 61.35 ?  15  GLU B CD    1 
ATOM   5640  O  OE1   . GLU B 1 15  ? 147.809 123.576 178.013 1.00 60.81 ?  15  GLU B OE1   1 
ATOM   5641  O  OE2   . GLU B 1 15  ? 148.634 122.985 176.066 1.00 60.08 -1 15  GLU B OE2   1 
ATOM   5642  N  N     . ILE B 1 16  ? 142.080 124.161 175.258 1.00 56.73 ?  16  ILE B N     1 
ATOM   5643  C  CA    . ILE B 1 16  ? 140.768 124.600 175.732 1.00 56.54 ?  16  ILE B CA    1 
ATOM   5644  C  C     . ILE B 1 16  ? 139.808 123.419 175.805 1.00 56.57 ?  16  ILE B C     1 
ATOM   5645  O  O     . ILE B 1 16  ? 139.095 123.234 176.798 1.00 54.26 ?  16  ILE B O     1 
ATOM   5646  C  CB    . ILE B 1 16  ? 140.211 125.710 174.824 1.00 55.92 ?  16  ILE B CB    1 
ATOM   5647  C  CG1   . ILE B 1 16  ? 141.125 126.932 174.827 1.00 55.42 ?  16  ILE B CG1   1 
ATOM   5648  C  CG2   . ILE B 1 16  ? 138.806 126.100 175.259 1.00 56.40 ?  16  ILE B CG2   1 
ATOM   5649  C  CD1   . ILE B 1 16  ? 140.861 127.868 173.674 1.00 54.74 ?  16  ILE B CD1   1 
ATOM   5650  N  N     . MET B 1 17  ? 139.780 122.601 174.753 1.00 56.33 ?  17  MET B N     1 
ATOM   5651  C  CA    . MET B 1 17  ? 138.828 121.501 174.679 1.00 56.69 ?  17  MET B CA    1 
ATOM   5652  C  C     . MET B 1 17  ? 139.186 120.343 175.597 1.00 57.42 ?  17  MET B C     1 
ATOM   5653  O  O     . MET B 1 17  ? 138.312 119.528 175.910 1.00 56.86 ?  17  MET B O     1 
ATOM   5654  C  CB    . MET B 1 17  ? 138.714 121.002 173.239 1.00 57.47 ?  17  MET B CB    1 
ATOM   5655  C  CG    . MET B 1 17  ? 138.435 122.105 172.243 1.00 57.59 ?  17  MET B CG    1 
ATOM   5656  S  SD    . MET B 1 17  ? 136.874 122.947 172.563 1.00 63.33 ?  17  MET B SD    1 
ATOM   5657  C  CE    . MET B 1 17  ? 135.785 122.095 171.426 1.00 55.92 ?  17  MET B CE    1 
ATOM   5658  N  N     . ILE B 1 18  ? 140.440 120.245 176.032 1.00 59.62 ?  18  ILE B N     1 
ATOM   5659  C  CA    . ILE B 1 18  ? 140.813 119.244 177.021 1.00 58.94 ?  18  ILE B CA    1 
ATOM   5660  C  C     . ILE B 1 18  ? 140.204 119.674 178.347 1.00 60.09 ?  18  ILE B C     1 
ATOM   5661  O  O     . ILE B 1 18  ? 140.690 120.608 178.996 1.00 59.84 ?  18  ILE B O     1 
ATOM   5662  C  CB    . ILE B 1 18  ? 142.339 119.076 177.121 1.00 60.01 ?  18  ILE B CB    1 
ATOM   5663  C  CG1   . ILE B 1 18  ? 142.881 118.419 175.849 1.00 60.22 ?  18  ILE B CG1   1 
ATOM   5664  C  CG2   . ILE B 1 18  ? 142.708 118.240 178.336 1.00 59.20 ?  18  ILE B CG2   1 
ATOM   5665  C  CD1   . ILE B 1 18  ? 144.045 119.156 175.228 1.00 60.47 ?  18  ILE B CD1   1 
ATOM   5666  N  N     . GLN B 1 19  ? 139.125 119.008 178.747 1.00 62.58 ?  19  GLN B N     1 
ATOM   5667  C  CA    . GLN B 1 19  ? 138.373 119.438 179.914 1.00 62.09 ?  19  GLN B CA    1 
ATOM   5668  C  C     . GLN B 1 19  ? 139.122 119.104 181.197 1.00 64.61 ?  19  GLN B C     1 
ATOM   5669  O  O     . GLN B 1 19  ? 139.734 118.040 181.323 1.00 66.56 ?  19  GLN B O     1 
ATOM   5670  C  CB    . GLN B 1 19  ? 136.993 118.781 179.926 1.00 64.69 ?  19  GLN B CB    1 
ATOM   5671  C  CG    . GLN B 1 19  ? 136.452 118.460 178.543 1.00 64.60 ?  19  GLN B CG    1 
ATOM   5672  C  CD    . GLN B 1 19  ? 134.965 118.728 178.420 1.00 64.39 ?  19  GLN B CD    1 
ATOM   5673  O  OE1   . GLN B 1 19  ? 134.212 118.572 179.382 1.00 64.88 ?  19  GLN B OE1   1 
ATOM   5674  N  NE2   . GLN B 1 19  ? 134.533 119.135 177.233 1.00 64.21 ?  19  GLN B NE2   1 
ATOM   5675  N  N     . LYS B 1 20  ? 139.073 120.030 182.151 1.00 67.86 ?  20  LYS B N     1 
ATOM   5676  C  CA    . LYS B 1 20  ? 139.633 119.834 183.482 1.00 69.26 ?  20  LYS B CA    1 
ATOM   5677  C  C     . LYS B 1 20  ? 138.496 119.948 184.486 1.00 69.23 ?  20  LYS B C     1 
ATOM   5678  O  O     . LYS B 1 20  ? 137.823 120.983 184.548 1.00 68.81 ?  20  LYS B O     1 
ATOM   5679  C  CB    . LYS B 1 20  ? 140.732 120.856 183.776 1.00 67.79 ?  20  LYS B CB    1 
ATOM   5680  C  CG    . LYS B 1 20  ? 140.965 121.118 185.255 1.00 68.45 ?  20  LYS B CG    1 
ATOM   5681  C  CD    . LYS B 1 20  ? 142.355 121.683 185.500 1.00 69.24 ?  20  LYS B CD    1 
ATOM   5682  C  CE    . LYS B 1 20  ? 142.312 123.191 185.678 1.00 69.19 ?  20  LYS B CE    1 
ATOM   5683  N  NZ    . LYS B 1 20  ? 143.670 123.798 185.607 1.00 68.51 1  20  LYS B NZ    1 
ATOM   5684  N  N     . ASP B 1 21  ? 138.285 118.884 185.263 1.00 71.38 ?  21  ASP B N     1 
ATOM   5685  C  CA    . ASP B 1 21  ? 137.173 118.803 186.214 1.00 71.25 ?  21  ASP B CA    1 
ATOM   5686  C  C     . ASP B 1 21  ? 135.831 119.009 185.514 1.00 72.08 ?  21  ASP B C     1 
ATOM   5687  O  O     . ASP B 1 21  ? 134.916 119.633 186.055 1.00 71.47 ?  21  ASP B O     1 
ATOM   5688  C  CB    . ASP B 1 21  ? 137.351 119.800 187.361 1.00 71.76 ?  21  ASP B CB    1 
ATOM   5689  C  CG    . ASP B 1 21  ? 138.767 119.819 187.903 1.00 73.48 ?  21  ASP B CG    1 
ATOM   5690  O  OD1   . ASP B 1 21  ? 139.366 118.732 188.044 1.00 72.23 ?  21  ASP B OD1   1 
ATOM   5691  O  OD2   . ASP B 1 21  ? 139.282 120.921 188.187 1.00 72.92 -1 21  ASP B OD2   1 
ATOM   5692  N  N     . GLY B 1 22  ? 135.714 118.481 184.297 1.00 68.63 ?  22  GLY B N     1 
ATOM   5693  C  CA    . GLY B 1 22  ? 134.476 118.554 183.549 1.00 66.05 ?  22  GLY B CA    1 
ATOM   5694  C  C     . GLY B 1 22  ? 134.164 119.897 182.932 1.00 67.44 ?  22  GLY B C     1 
ATOM   5695  O  O     . GLY B 1 22  ? 133.049 120.084 182.432 1.00 67.11 ?  22  GLY B O     1 
ATOM   5696  N  N     . LYS B 1 23  ? 135.105 120.837 182.945 1.00 66.70 ?  23  LYS B N     1 
ATOM   5697  C  CA    . LYS B 1 23  ? 134.886 122.176 182.421 1.00 63.82 ?  23  LYS B CA    1 
ATOM   5698  C  C     . LYS B 1 23  ? 135.944 122.512 181.379 1.00 63.01 ?  23  LYS B C     1 
ATOM   5699  O  O     . LYS B 1 23  ? 137.093 122.070 181.471 1.00 64.84 ?  23  LYS B O     1 
ATOM   5700  C  CB    . LYS B 1 23  ? 134.917 123.225 183.540 1.00 63.78 ?  23  LYS B CB    1 
ATOM   5701  C  CG    . LYS B 1 23  ? 134.213 122.796 184.814 1.00 65.44 ?  23  LYS B CG    1 
ATOM   5702  C  CD    . LYS B 1 23  ? 132.714 122.684 184.600 1.00 65.22 ?  23  LYS B CD    1 
ATOM   5703  C  CE    . LYS B 1 23  ? 132.063 124.054 184.578 1.00 64.91 ?  23  LYS B CE    1 
ATOM   5704  N  NZ    . LYS B 1 23  ? 132.742 124.996 185.508 1.00 63.67 1  23  LYS B NZ    1 
ATOM   5705  N  N     . PHE B 1 24  ? 135.542 123.299 180.384 1.00 59.23 ?  24  PHE B N     1 
ATOM   5706  C  CA    . PHE B 1 24  ? 136.473 123.743 179.356 1.00 57.17 ?  24  PHE B CA    1 
ATOM   5707  C  C     . PHE B 1 24  ? 137.516 124.679 179.953 1.00 56.29 ?  24  PHE B C     1 
ATOM   5708  O  O     . PHE B 1 24  ? 137.227 125.461 180.862 1.00 56.56 ?  24  PHE B O     1 
ATOM   5709  C  CB    . PHE B 1 24  ? 135.725 124.449 178.226 1.00 55.54 ?  24  PHE B CB    1 
ATOM   5710  C  CG    . PHE B 1 24  ? 135.025 123.515 177.281 1.00 55.27 ?  24  PHE B CG    1 
ATOM   5711  C  CD1   . PHE B 1 24  ? 135.733 122.832 176.308 1.00 57.16 ?  24  PHE B CD1   1 
ATOM   5712  C  CD2   . PHE B 1 24  ? 133.655 123.330 177.359 1.00 55.44 ?  24  PHE B CD2   1 
ATOM   5713  C  CE1   . PHE B 1 24  ? 135.090 121.975 175.435 1.00 56.09 ?  24  PHE B CE1   1 
ATOM   5714  C  CE2   . PHE B 1 24  ? 133.007 122.475 176.488 1.00 56.44 ?  24  PHE B CE2   1 
ATOM   5715  C  CZ    . PHE B 1 24  ? 133.726 121.798 175.526 1.00 55.50 ?  24  PHE B CZ    1 
ATOM   5716  N  N     . GLN B 1 25  ? 138.741 124.595 179.432 1.00 57.29 ?  25  GLN B N     1 
ATOM   5717  C  CA    . GLN B 1 25  ? 139.841 125.444 179.894 1.00 57.15 ?  25  GLN B CA    1 
ATOM   5718  C  C     . GLN B 1 25  ? 139.891 126.691 179.017 1.00 57.88 ?  25  GLN B C     1 
ATOM   5719  O  O     . GLN B 1 25  ? 140.746 126.848 178.142 1.00 59.45 ?  25  GLN B O     1 
ATOM   5720  C  CB    . GLN B 1 25  ? 141.158 124.677 179.870 1.00 57.43 ?  25  GLN B CB    1 
ATOM   5721  C  CG    . GLN B 1 25  ? 141.147 123.403 180.695 1.00 57.27 ?  25  GLN B CG    1 
ATOM   5722  C  CD    . GLN B 1 25  ? 142.477 122.679 180.659 1.00 58.27 ?  25  GLN B CD    1 
ATOM   5723  O  OE1   . GLN B 1 25  ? 143.311 122.847 181.549 1.00 58.75 ?  25  GLN B OE1   1 
ATOM   5724  N  NE2   . GLN B 1 25  ? 142.684 121.869 179.628 1.00 58.57 ?  25  GLN B NE2   1 
ATOM   5725  N  N     . PHE B 1 26  ? 138.943 127.597 179.265 1.00 51.55 ?  26  PHE B N     1 
ATOM   5726  C  CA    . PHE B 1 26  ? 138.869 128.827 178.483 1.00 52.93 ?  26  PHE B CA    1 
ATOM   5727  C  C     . PHE B 1 26  ? 140.081 129.718 178.733 1.00 53.51 ?  26  PHE B C     1 
ATOM   5728  O  O     . PHE B 1 26  ? 140.582 130.366 177.806 1.00 52.89 ?  26  PHE B O     1 
ATOM   5729  C  CB    . PHE B 1 26  ? 137.576 129.574 178.805 1.00 50.12 ?  26  PHE B CB    1 
ATOM   5730  C  CG    . PHE B 1 26  ? 136.333 128.834 178.405 1.00 51.96 ?  26  PHE B CG    1 
ATOM   5731  C  CD1   . PHE B 1 26  ? 136.144 128.429 177.095 1.00 51.08 ?  26  PHE B CD1   1 
ATOM   5732  C  CD2   . PHE B 1 26  ? 135.353 128.543 179.339 1.00 50.64 ?  26  PHE B CD2   1 
ATOM   5733  C  CE1   . PHE B 1 26  ? 135.002 127.747 176.723 1.00 49.46 ?  26  PHE B CE1   1 
ATOM   5734  C  CE2   . PHE B 1 26  ? 134.209 127.861 178.973 1.00 49.81 ?  26  PHE B CE2   1 
ATOM   5735  C  CZ    . PHE B 1 26  ? 134.032 127.465 177.663 1.00 49.40 ?  26  PHE B CZ    1 
ATOM   5736  N  N     . ASP B 1 27  ? 140.565 129.760 179.978 1.00 57.05 ?  27  ASP B N     1 
ATOM   5737  C  CA    . ASP B 1 27  ? 141.700 130.617 180.308 1.00 54.92 ?  27  ASP B CA    1 
ATOM   5738  C  C     . ASP B 1 27  ? 142.941 130.249 179.507 1.00 55.84 ?  27  ASP B C     1 
ATOM   5739  O  O     . ASP B 1 27  ? 143.775 131.118 179.222 1.00 55.38 ?  27  ASP B O     1 
ATOM   5740  C  CB    . ASP B 1 27  ? 141.994 130.541 181.807 1.00 55.14 ?  27  ASP B CB    1 
ATOM   5741  C  CG    . ASP B 1 27  ? 141.747 129.159 182.379 1.00 59.58 ?  27  ASP B CG    1 
ATOM   5742  O  OD1   . ASP B 1 27  ? 142.139 128.167 181.732 1.00 58.90 ?  27  ASP B OD1   1 
ATOM   5743  O  OD2   . ASP B 1 27  ? 141.158 129.066 183.477 1.00 60.21 -1 27  ASP B OD2   1 
ATOM   5744  N  N     . LYS B 1 28  ? 143.074 128.975 179.125 1.00 55.09 ?  28  LYS B N     1 
ATOM   5745  C  CA    . LYS B 1 28  ? 144.197 128.562 178.287 1.00 55.69 ?  28  LYS B CA    1 
ATOM   5746  C  C     . LYS B 1 28  ? 144.270 129.403 177.021 1.00 55.91 ?  28  LYS B C     1 
ATOM   5747  O  O     . LYS B 1 28  ? 145.366 129.733 176.549 1.00 58.39 ?  28  LYS B O     1 
ATOM   5748  C  CB    . LYS B 1 28  ? 144.075 127.080 177.938 1.00 56.35 ?  28  LYS B CB    1 
ATOM   5749  C  CG    . LYS B 1 28  ? 144.486 126.134 179.054 1.00 56.47 ?  28  LYS B CG    1 
ATOM   5750  C  CD    . LYS B 1 28  ? 145.987 126.162 179.278 1.00 56.20 ?  28  LYS B CD    1 
ATOM   5751  C  CE    . LYS B 1 28  ? 146.381 125.313 180.475 1.00 56.98 ?  28  LYS B CE    1 
ATOM   5752  N  NZ    . LYS B 1 28  ? 147.184 126.083 181.464 1.00 55.47 1  28  LYS B NZ    1 
ATOM   5753  N  N     . ASP B 1 29  ? 143.109 129.781 176.475 1.00 54.35 ?  29  ASP B N     1 
ATOM   5754  C  CA    . ASP B 1 29  ? 143.072 130.640 175.297 1.00 52.22 ?  29  ASP B CA    1 
ATOM   5755  C  C     . ASP B 1 29  ? 143.921 131.884 175.504 1.00 52.26 ?  29  ASP B C     1 
ATOM   5756  O  O     . ASP B 1 29  ? 144.748 132.233 174.653 1.00 52.34 ?  29  ASP B O     1 
ATOM   5757  C  CB    . ASP B 1 29  ? 141.628 131.029 174.979 1.00 52.42 ?  29  ASP B CB    1 
ATOM   5758  C  CG    . ASP B 1 29  ? 141.426 131.380 173.519 1.00 54.90 ?  29  ASP B CG    1 
ATOM   5759  O  OD1   . ASP B 1 29  ? 142.175 130.854 172.670 1.00 55.08 ?  29  ASP B OD1   1 
ATOM   5760  O  OD2   . ASP B 1 29  ? 140.517 132.182 173.222 1.00 52.90 -1 29  ASP B OD2   1 
ATOM   5761  N  N     . LYS B 1 30  ? 143.756 132.543 176.655 1.00 52.18 ?  30  LYS B N     1 
ATOM   5762  C  CA    . LYS B 1 30  ? 144.552 133.728 176.952 1.00 53.26 ?  30  LYS B CA    1 
ATOM   5763  C  C     . LYS B 1 30  ? 146.037 133.409 176.873 1.00 51.63 ?  30  LYS B C     1 
ATOM   5764  O  O     . LYS B 1 30  ? 146.806 134.124 176.215 1.00 55.03 ?  30  LYS B O     1 
ATOM   5765  C  CB    . LYS B 1 30  ? 144.188 134.270 178.335 1.00 52.12 ?  30  LYS B CB    1 
ATOM   5766  C  CG    . LYS B 1 30  ? 144.937 135.533 178.723 1.00 51.47 ?  30  LYS B CG    1 
ATOM   5767  C  CD    . LYS B 1 30  ? 144.484 136.051 180.076 1.00 53.30 ?  30  LYS B CD    1 
ATOM   5768  C  CE    . LYS B 1 30  ? 145.249 137.304 180.470 1.00 55.90 ?  30  LYS B CE    1 
ATOM   5769  N  NZ    . LYS B 1 30  ? 144.815 137.825 181.795 1.00 55.29 1  30  LYS B NZ    1 
ATOM   5770  N  N     . GLU B 1 31  ? 146.448 132.303 177.501 1.00 53.21 ?  31  GLU B N     1 
ATOM   5771  C  CA    . GLU B 1 31  ? 147.845 131.893 177.434 1.00 52.85 ?  31  GLU B CA    1 
ATOM   5772  C  C     . GLU B 1 31  ? 148.306 131.799 175.988 1.00 52.18 ?  31  GLU B C     1 
ATOM   5773  O  O     . GLU B 1 31  ? 149.382 132.300 175.636 1.00 54.46 ?  31  GLU B O     1 
ATOM   5774  C  CB    . GLU B 1 31  ? 148.034 130.555 178.148 1.00 52.70 ?  31  GLU B CB    1 
ATOM   5775  C  CG    . GLU B 1 31  ? 147.715 130.595 179.634 1.00 54.76 ?  31  GLU B CG    1 
ATOM   5776  C  CD    . GLU B 1 31  ? 147.652 129.212 180.252 1.00 57.88 ?  31  GLU B CD    1 
ATOM   5777  O  OE1   . GLU B 1 31  ? 148.441 128.339 179.838 1.00 59.45 ?  31  GLU B OE1   1 
ATOM   5778  O  OE2   . GLU B 1 31  ? 146.812 128.999 181.151 1.00 56.50 -1 31  GLU B OE2   1 
ATOM   5779  N  N     . ALA B 1 32  ? 147.467 131.217 175.127 1.00 43.56 ?  32  ALA B N     1 
ATOM   5780  C  CA    . ALA B 1 32  ? 147.816 131.082 173.719 1.00 44.58 ?  32  ALA B CA    1 
ATOM   5781  C  C     . ALA B 1 32  ? 148.195 132.428 173.122 1.00 48.74 ?  32  ALA B C     1 
ATOM   5782  O  O     . ALA B 1 32  ? 149.252 132.563 172.491 1.00 50.09 ?  32  ALA B O     1 
ATOM   5783  C  CB    . ALA B 1 32  ? 146.655 130.453 172.948 1.00 44.78 ?  32  ALA B CB    1 
ATOM   5784  N  N     . VAL B 1 33  ? 147.371 133.455 173.366 1.00 49.04 ?  33  VAL B N     1 
ATOM   5785  C  CA    . VAL B 1 33  ? 147.667 134.773 172.811 1.00 47.36 ?  33  VAL B CA    1 
ATOM   5786  C  C     . VAL B 1 33  ? 149.048 135.223 173.258 1.00 47.53 ?  33  VAL B C     1 
ATOM   5787  O  O     . VAL B 1 33  ? 149.872 135.657 172.443 1.00 49.67 ?  33  VAL B O     1 
ATOM   5788  C  CB    . VAL B 1 33  ? 146.588 135.798 173.205 1.00 45.21 ?  33  VAL B CB    1 
ATOM   5789  C  CG1   . VAL B 1 33  ? 146.296 136.727 172.040 1.00 45.04 ?  33  VAL B CG1   1 
ATOM   5790  C  CG2   . VAL B 1 33  ? 145.325 135.103 173.646 1.00 47.96 ?  33  VAL B CG2   1 
ATOM   5791  N  N     . HIS B 1 34  ? 149.339 135.069 174.554 1.00 44.02 ?  34  HIS B N     1 
ATOM   5792  C  CA    . HIS B 1 34  ? 150.660 135.423 175.052 1.00 45.18 ?  34  HIS B CA    1 
ATOM   5793  C  C     . HIS B 1 34  ? 151.736 134.701 174.257 1.00 45.96 ?  34  HIS B C     1 
ATOM   5794  O  O     . HIS B 1 34  ? 152.650 135.333 173.711 1.00 49.13 ?  34  HIS B O     1 
ATOM   5795  C  CB    . HIS B 1 34  ? 150.769 135.096 176.540 1.00 50.39 ?  34  HIS B CB    1 
ATOM   5796  C  CG    . HIS B 1 34  ? 151.752 135.953 177.274 1.00 49.36 ?  34  HIS B CG    1 
ATOM   5797  N  ND1   . HIS B 1 34  ? 153.002 135.504 177.643 1.00 48.47 ?  34  HIS B ND1   1 
ATOM   5798  C  CD2   . HIS B 1 34  ? 151.671 137.234 177.704 1.00 49.42 ?  34  HIS B CD2   1 
ATOM   5799  C  CE1   . HIS B 1 34  ? 153.647 136.471 178.270 1.00 50.02 ?  34  HIS B CE1   1 
ATOM   5800  N  NE2   . HIS B 1 34  ? 152.862 137.532 178.320 1.00 51.44 ?  34  HIS B NE2   1 
ATOM   5801  N  N     . SER B 1 35  ? 151.600 133.380 174.120 1.00 46.26 ?  35  SER B N     1 
ATOM   5802  C  CA    . SER B 1 35  ? 152.545 132.630 173.305 1.00 47.37 ?  35  SER B CA    1 
ATOM   5803  C  C     . SER B 1 35  ? 152.591 133.195 171.896 1.00 46.78 ?  35  SER B C     1 
ATOM   5804  O  O     . SER B 1 35  ? 153.668 133.523 171.380 1.00 50.48 ?  35  SER B O     1 
ATOM   5805  C  CB    . SER B 1 35  ? 152.166 131.148 173.288 1.00 48.20 ?  35  SER B CB    1 
ATOM   5806  O  OG    . SER B 1 35  ? 152.872 130.454 172.276 1.00 48.65 ?  35  SER B OG    1 
ATOM   5807  N  N     . TYR B 1 36  ? 151.415 133.400 171.293 1.00 47.40 ?  36  TYR B N     1 
ATOM   5808  C  CA    . TYR B 1 36  ? 151.353 133.885 169.921 1.00 45.60 ?  36  TYR B CA    1 
ATOM   5809  C  C     . TYR B 1 36  ? 152.075 135.213 169.772 1.00 46.42 ?  36  TYR B C     1 
ATOM   5810  O  O     . TYR B 1 36  ? 152.544 135.545 168.678 1.00 47.08 ?  36  TYR B O     1 
ATOM   5811  C  CB    . TYR B 1 36  ? 149.896 134.018 169.477 1.00 44.83 ?  36  TYR B CB    1 
ATOM   5812  C  CG    . TYR B 1 36  ? 149.721 134.396 168.025 1.00 45.26 ?  36  TYR B CG    1 
ATOM   5813  C  CD1   . TYR B 1 36  ? 150.228 133.592 167.012 1.00 44.63 ?  36  TYR B CD1   1 
ATOM   5814  C  CD2   . TYR B 1 36  ? 149.047 135.554 167.665 1.00 42.99 ?  36  TYR B CD2   1 
ATOM   5815  C  CE1   . TYR B 1 36  ? 150.068 133.931 165.684 1.00 43.22 ?  36  TYR B CE1   1 
ATOM   5816  C  CE2   . TYR B 1 36  ? 148.883 135.902 166.340 1.00 44.18 ?  36  TYR B CE2   1 
ATOM   5817  C  CZ    . TYR B 1 36  ? 149.395 135.087 165.354 1.00 44.46 ?  36  TYR B CZ    1 
ATOM   5818  O  OH    . TYR B 1 36  ? 149.234 135.431 164.031 1.00 43.59 ?  36  TYR B OH    1 
ATOM   5819  N  N     . PHE B 1 37  ? 152.191 135.975 170.858 1.00 49.89 ?  37  PHE B N     1 
ATOM   5820  C  CA    . PHE B 1 37  ? 152.924 137.229 170.795 1.00 49.17 ?  37  PHE B CA    1 
ATOM   5821  C  C     . PHE B 1 37  ? 154.375 137.071 171.226 1.00 51.17 ?  37  PHE B C     1 
ATOM   5822  O  O     . PHE B 1 37  ? 155.256 137.724 170.660 1.00 55.25 ?  37  PHE B O     1 
ATOM   5823  C  CB    . PHE B 1 37  ? 152.226 138.289 171.647 1.00 49.72 ?  37  PHE B CB    1 
ATOM   5824  C  CG    . PHE B 1 37  ? 151.099 138.977 170.937 1.00 50.79 ?  37  PHE B CG    1 
ATOM   5825  C  CD1   . PHE B 1 37  ? 151.347 140.050 170.099 1.00 51.43 ?  37  PHE B CD1   1 
ATOM   5826  C  CD2   . PHE B 1 37  ? 149.796 138.542 171.093 1.00 50.28 ?  37  PHE B CD2   1 
ATOM   5827  C  CE1   . PHE B 1 37  ? 150.314 140.682 169.438 1.00 50.45 ?  37  PHE B CE1   1 
ATOM   5828  C  CE2   . PHE B 1 37  ? 148.760 139.170 170.434 1.00 48.78 ?  37  PHE B CE2   1 
ATOM   5829  C  CZ    . PHE B 1 37  ? 149.020 140.239 169.604 1.00 48.83 ?  37  PHE B CZ    1 
ATOM   5830  N  N     . VAL B 1 38  ? 154.656 136.206 172.206 1.00 52.14 ?  38  VAL B N     1 
ATOM   5831  C  CA    . VAL B 1 38  ? 156.030 136.101 172.696 1.00 51.44 ?  38  VAL B CA    1 
ATOM   5832  C  C     . VAL B 1 38  ? 156.875 135.153 171.864 1.00 53.54 ?  38  VAL B C     1 
ATOM   5833  O  O     . VAL B 1 38  ? 158.086 135.055 172.096 1.00 56.53 ?  38  VAL B O     1 
ATOM   5834  C  CB    . VAL B 1 38  ? 156.089 135.655 174.169 1.00 50.73 ?  38  VAL B CB    1 
ATOM   5835  C  CG1   . VAL B 1 38  ? 155.268 136.592 175.044 1.00 50.91 ?  38  VAL B CG1   1 
ATOM   5836  C  CG2   . VAL B 1 38  ? 155.626 134.216 174.316 1.00 49.68 ?  38  VAL B CG2   1 
ATOM   5837  N  N     . ASP B 1 39  ? 156.278 134.457 170.902 1.00 50.18 ?  39  ASP B N     1 
ATOM   5838  C  CA    . ASP B 1 39  ? 157.008 133.532 170.052 1.00 51.31 ?  39  ASP B CA    1 
ATOM   5839  C  C     . ASP B 1 39  ? 156.891 133.828 168.566 1.00 53.35 ?  39  ASP B C     1 
ATOM   5840  O  O     . ASP B 1 39  ? 157.804 133.481 167.815 1.00 56.10 ?  39  ASP B O     1 
ATOM   5841  C  CB    . ASP B 1 39  ? 156.539 132.089 170.306 1.00 52.76 ?  39  ASP B CB    1 
ATOM   5842  C  CG    . ASP B 1 39  ? 156.549 131.724 171.777 1.00 54.28 ?  39  ASP B CG    1 
ATOM   5843  O  OD1   . ASP B 1 39  ? 157.461 132.179 172.497 1.00 54.59 ?  39  ASP B OD1   1 
ATOM   5844  O  OD2   . ASP B 1 39  ? 155.645 130.980 172.212 1.00 53.25 -1 39  ASP B OD2   1 
ATOM   5845  N  N     . TYR B 1 40  ? 155.801 134.453 168.115 1.00 53.18 ?  40  TYR B N     1 
ATOM   5846  C  CA    . TYR B 1 40  ? 155.616 134.722 166.693 1.00 53.04 ?  40  TYR B CA    1 
ATOM   5847  C  C     . TYR B 1 40  ? 155.526 136.209 166.377 1.00 55.10 ?  40  TYR B C     1 
ATOM   5848  O  O     . TYR B 1 40  ? 156.296 136.697 165.544 1.00 55.56 ?  40  TYR B O     1 
ATOM   5849  C  CB    . TYR B 1 40  ? 154.366 133.996 166.180 1.00 52.98 ?  40  TYR B CB    1 
ATOM   5850  C  CG    . TYR B 1 40  ? 154.297 133.904 164.673 1.00 52.53 ?  40  TYR B CG    1 
ATOM   5851  C  CD1   . TYR B 1 40  ? 155.039 132.955 163.983 1.00 53.26 ?  40  TYR B CD1   1 
ATOM   5852  C  CD2   . TYR B 1 40  ? 153.493 134.767 163.940 1.00 51.96 ?  40  TYR B CD2   1 
ATOM   5853  C  CE1   . TYR B 1 40  ? 154.980 132.866 162.606 1.00 55.40 ?  40  TYR B CE1   1 
ATOM   5854  C  CE2   . TYR B 1 40  ? 153.429 134.687 162.562 1.00 52.85 ?  40  TYR B CE2   1 
ATOM   5855  C  CZ    . TYR B 1 40  ? 154.175 133.734 161.901 1.00 56.50 ?  40  TYR B CZ    1 
ATOM   5856  O  OH    . TYR B 1 40  ? 154.114 133.648 160.528 1.00 57.66 ?  40  TYR B OH    1 
ATOM   5857  N  N     . ILE B 1 41  ? 154.615 136.947 167.013 1.00 55.05 ?  41  ILE B N     1 
ATOM   5858  C  CA    . ILE B 1 41  ? 154.331 138.311 166.569 1.00 53.28 ?  41  ILE B CA    1 
ATOM   5859  C  C     . ILE B 1 41  ? 155.498 139.238 166.882 1.00 52.04 ?  41  ILE B C     1 
ATOM   5860  O  O     . ILE B 1 41  ? 155.929 140.023 166.028 1.00 54.19 ?  41  ILE B O     1 
ATOM   5861  C  CB    . ILE B 1 41  ? 153.020 138.820 167.193 1.00 50.85 ?  41  ILE B CB    1 
ATOM   5862  C  CG1   . ILE B 1 41  ? 151.847 137.939 166.761 1.00 48.55 ?  41  ILE B CG1   1 
ATOM   5863  C  CG2   . ILE B 1 41  ? 152.767 140.265 166.793 1.00 49.09 ?  41  ILE B CG2   1 
ATOM   5864  C  CD1   . ILE B 1 41  ? 151.763 137.726 165.269 1.00 49.11 ?  41  ILE B CD1   1 
ATOM   5865  N  N     . ASN B 1 42  ? 156.031 139.165 168.103 1.00 50.52 ?  42  ASN B N     1 
ATOM   5866  C  CA    . ASN B 1 42  ? 157.131 140.051 168.470 1.00 51.96 ?  42  ASN B CA    1 
ATOM   5867  C  C     . ASN B 1 42  ? 158.400 139.725 167.694 1.00 54.31 ?  42  ASN B C     1 
ATOM   5868  O  O     . ASN B 1 42  ? 159.197 140.624 167.407 1.00 54.08 ?  42  ASN B O     1 
ATOM   5869  C  CB    . ASN B 1 42  ? 157.391 139.979 169.973 1.00 53.11 ?  42  ASN B CB    1 
ATOM   5870  C  CG    . ASN B 1 42  ? 156.247 140.547 170.790 1.00 53.45 ?  42  ASN B CG    1 
ATOM   5871  O  OD1   . ASN B 1 42  ? 155.333 141.167 170.249 1.00 56.58 ?  42  ASN B OD1   1 
ATOM   5872  N  ND2   . ASN B 1 42  ? 156.294 140.336 172.100 1.00 53.35 ?  42  ASN B ND2   1 
ATOM   5873  N  N     . GLN B 1 43  ? 158.609 138.453 167.351 1.00 58.65 ?  43  GLN B N     1 
ATOM   5874  C  CA    . GLN B 1 43  ? 159.773 138.083 166.555 1.00 57.83 ?  43  GLN B CA    1 
ATOM   5875  C  C     . GLN B 1 43  ? 159.592 138.449 165.086 1.00 56.26 ?  43  GLN B C     1 
ATOM   5876  O  O     . GLN B 1 43  ? 160.554 138.848 164.422 1.00 58.13 ?  43  GLN B O     1 
ATOM   5877  C  CB    . GLN B 1 43  ? 160.057 136.589 166.703 1.00 58.46 ?  43  GLN B CB    1 
ATOM   5878  C  CG    . GLN B 1 43  ? 161.023 136.253 167.827 1.00 58.98 ?  43  GLN B CG    1 
ATOM   5879  C  CD    . GLN B 1 43  ? 160.339 136.152 169.175 1.00 60.06 ?  43  GLN B CD    1 
ATOM   5880  O  OE1   . GLN B 1 43  ? 159.840 135.093 169.552 1.00 59.73 ?  43  GLN B OE1   1 
ATOM   5881  N  NE2   . GLN B 1 43  ? 160.313 137.257 169.911 1.00 59.72 ?  43  GLN B NE2   1 
ATOM   5882  N  N     . ASN B 1 44  ? 158.374 138.322 164.565 1.00 56.45 ?  44  ASN B N     1 
ATOM   5883  C  CA    . ASN B 1 44  ? 158.100 138.614 163.165 1.00 56.94 ?  44  ASN B CA    1 
ATOM   5884  C  C     . ASN B 1 44  ? 157.780 140.081 162.912 1.00 55.64 ?  44  ASN B C     1 
ATOM   5885  O  O     . ASN B 1 44  ? 157.634 140.476 161.751 1.00 56.35 ?  44  ASN B O     1 
ATOM   5886  C  CB    . ASN B 1 44  ? 156.944 137.745 162.659 1.00 55.57 ?  44  ASN B CB    1 
ATOM   5887  C  CG    . ASN B 1 44  ? 157.419 136.439 162.056 1.00 56.91 ?  44  ASN B CG    1 
ATOM   5888  O  OD1   . ASN B 1 44  ? 158.320 135.790 162.587 1.00 58.79 ?  44  ASN B OD1   1 
ATOM   5889  N  ND2   . ASN B 1 44  ? 156.813 136.045 160.943 1.00 58.76 ?  44  ASN B ND2   1 
ATOM   5890  N  N     . THR B 1 45  ? 157.663 140.893 163.957 1.00 55.50 ?  45  THR B N     1 
ATOM   5891  C  CA    . THR B 1 45  ? 157.425 142.314 163.771 1.00 56.66 ?  45  THR B CA    1 
ATOM   5892  C  C     . THR B 1 45  ? 158.719 143.023 163.391 1.00 57.37 ?  45  THR B C     1 
ATOM   5893  O  O     . THR B 1 45  ? 159.821 142.574 163.720 1.00 60.83 ?  45  THR B O     1 
ATOM   5894  C  CB    . THR B 1 45  ? 156.822 142.938 165.036 1.00 56.50 ?  45  THR B CB    1 
ATOM   5895  O  OG1   . THR B 1 45  ? 156.405 144.279 164.758 1.00 56.05 ?  45  THR B OG1   1 
ATOM   5896  C  CG2   . THR B 1 45  ? 157.827 142.951 166.180 1.00 55.69 ?  45  THR B CG2   1 
ATOM   5897  N  N     . VAL B 1 46  ? 158.577 144.124 162.661 1.00 56.32 ?  46  VAL B N     1 
ATOM   5898  C  CA    . VAL B 1 46  ? 159.708 144.942 162.241 1.00 57.35 ?  46  VAL B CA    1 
ATOM   5899  C  C     . VAL B 1 46  ? 159.720 146.199 163.099 1.00 57.06 ?  46  VAL B C     1 
ATOM   5900  O  O     . VAL B 1 46  ? 158.791 147.013 163.038 1.00 58.31 ?  46  VAL B O     1 
ATOM   5901  C  CB    . VAL B 1 46  ? 159.627 145.290 160.747 1.00 56.58 ?  46  VAL B CB    1 
ATOM   5902  C  CG1   . VAL B 1 46  ? 160.591 146.414 160.412 1.00 55.16 ?  46  VAL B CG1   1 
ATOM   5903  C  CG2   . VAL B 1 46  ? 159.925 144.066 159.903 1.00 55.55 ?  46  VAL B CG2   1 
ATOM   5904  N  N     . PHE B 1 47  ? 160.767 146.356 163.901 1.00 58.54 ?  47  PHE B N     1 
ATOM   5905  C  CA    . PHE B 1 47  ? 160.894 147.495 164.794 1.00 60.28 ?  47  PHE B CA    1 
ATOM   5906  C  C     . PHE B 1 47  ? 161.894 148.500 164.238 1.00 60.60 ?  47  PHE B C     1 
ATOM   5907  O  O     . PHE B 1 47  ? 162.916 148.134 163.654 1.00 61.43 ?  47  PHE B O     1 
ATOM   5908  C  CB    . PHE B 1 47  ? 161.328 147.051 166.192 1.00 60.54 ?  47  PHE B CB    1 
ATOM   5909  C  CG    . PHE B 1 47  ? 161.025 148.056 167.267 1.00 60.62 ?  47  PHE B CG    1 
ATOM   5910  C  CD1   . PHE B 1 47  ? 159.726 148.484 167.486 1.00 59.97 ?  47  PHE B CD1   1 
ATOM   5911  C  CD2   . PHE B 1 47  ? 162.039 148.575 168.056 1.00 60.05 ?  47  PHE B CD2   1 
ATOM   5912  C  CE1   . PHE B 1 47  ? 159.444 149.409 168.474 1.00 60.86 ?  47  PHE B CE1   1 
ATOM   5913  C  CE2   . PHE B 1 47  ? 161.763 149.499 169.045 1.00 60.57 ?  47  PHE B CE2   1 
ATOM   5914  C  CZ    . PHE B 1 47  ? 160.464 149.918 169.253 1.00 61.43 ?  47  PHE B CZ    1 
ATOM   5915  N  N     . PHE B 1 48  ? 161.582 149.777 164.426 1.00 56.81 ?  48  PHE B N     1 
ATOM   5916  C  CA    . PHE B 1 48  ? 162.437 150.874 164.004 1.00 56.47 ?  48  PHE B CA    1 
ATOM   5917  C  C     . PHE B 1 48  ? 162.917 151.637 165.231 1.00 59.30 ?  48  PHE B C     1 
ATOM   5918  O  O     . PHE B 1 48  ? 162.416 151.443 166.342 1.00 59.94 ?  48  PHE B O     1 
ATOM   5919  C  CB    . PHE B 1 48  ? 161.704 151.821 163.044 1.00 56.72 ?  48  PHE B CB    1 
ATOM   5920  C  CG    . PHE B 1 48  ? 161.221 151.158 161.783 1.00 57.71 ?  48  PHE B CG    1 
ATOM   5921  C  CD1   . PHE B 1 48  ? 160.080 150.372 161.786 1.00 56.37 ?  48  PHE B CD1   1 
ATOM   5922  C  CD2   . PHE B 1 48  ? 161.907 151.326 160.593 1.00 57.45 ?  48  PHE B CD2   1 
ATOM   5923  C  CE1   . PHE B 1 48  ? 159.635 149.767 160.627 1.00 56.89 ?  48  PHE B CE1   1 
ATOM   5924  C  CE2   . PHE B 1 48  ? 161.467 150.722 159.432 1.00 56.57 ?  48  PHE B CE2   1 
ATOM   5925  C  CZ    . PHE B 1 48  ? 160.330 149.942 159.449 1.00 56.22 ?  48  PHE B CZ    1 
ATOM   5926  N  N     . HIS B 1 49  ? 163.907 152.507 165.019 1.00 62.05 ?  49  HIS B N     1 
ATOM   5927  C  CA    . HIS B 1 49  ? 164.451 153.282 166.130 1.00 62.83 ?  49  HIS B CA    1 
ATOM   5928  C  C     . HIS B 1 49  ? 163.389 154.190 166.738 1.00 63.07 ?  49  HIS B C     1 
ATOM   5929  O  O     . HIS B 1 49  ? 163.287 154.302 167.965 1.00 64.37 ?  49  HIS B O     1 
ATOM   5930  C  CB    . HIS B 1 49  ? 165.656 154.098 165.664 1.00 64.35 ?  49  HIS B CB    1 
ATOM   5931  C  CG    . HIS B 1 49  ? 166.340 154.843 166.767 1.00 65.21 ?  49  HIS B CG    1 
ATOM   5932  N  ND1   . HIS B 1 49  ? 166.774 154.228 167.921 1.00 63.91 ?  49  HIS B ND1   1 
ATOM   5933  C  CD2   . HIS B 1 49  ? 166.661 156.152 166.895 1.00 63.74 ?  49  HIS B CD2   1 
ATOM   5934  C  CE1   . HIS B 1 49  ? 167.336 155.126 168.711 1.00 63.98 ?  49  HIS B CE1   1 
ATOM   5935  N  NE2   . HIS B 1 49  ? 167.280 156.301 168.112 1.00 63.41 ?  49  HIS B NE2   1 
ATOM   5936  N  N     . ASN B 1 50  ? 162.590 154.842 165.897 1.00 61.05 ?  50  ASN B N     1 
ATOM   5937  C  CA    . ASN B 1 50  ? 161.458 155.629 166.360 1.00 62.50 ?  50  ASN B CA    1 
ATOM   5938  C  C     . ASN B 1 50  ? 160.381 155.603 165.283 1.00 60.99 ?  50  ASN B C     1 
ATOM   5939  O  O     . ASN B 1 50  ? 160.525 154.947 164.248 1.00 58.84 ?  50  ASN B O     1 
ATOM   5940  C  CB    . ASN B 1 50  ? 161.875 157.061 166.716 1.00 61.56 ?  50  ASN B CB    1 
ATOM   5941  C  CG    . ASN B 1 50  ? 162.647 157.738 165.605 1.00 62.99 ?  50  ASN B CG    1 
ATOM   5942  O  OD1   . ASN B 1 50  ? 162.906 157.143 164.562 1.00 62.27 ?  50  ASN B OD1   1 
ATOM   5943  N  ND2   . ASN B 1 50  ? 163.017 158.995 165.822 1.00 63.03 ?  50  ASN B ND2   1 
ATOM   5944  N  N     . LEU B 1 51  ? 159.289 156.326 165.539 1.00 55.35 ?  51  LEU B N     1 
ATOM   5945  C  CA    . LEU B 1 51  ? 158.168 156.331 164.605 1.00 54.03 ?  51  LEU B CA    1 
ATOM   5946  C  C     . LEU B 1 51  ? 158.529 157.011 163.290 1.00 56.24 ?  51  LEU B C     1 
ATOM   5947  O  O     . LEU B 1 51  ? 157.940 156.695 162.249 1.00 56.85 ?  51  LEU B O     1 
ATOM   5948  C  CB    . LEU B 1 51  ? 156.961 157.014 165.247 1.00 55.44 ?  51  LEU B CB    1 
ATOM   5949  C  CG    . LEU B 1 51  ? 155.643 156.975 164.473 1.00 53.80 ?  51  LEU B CG    1 
ATOM   5950  C  CD1   . LEU B 1 51  ? 155.166 155.542 164.296 1.00 51.80 ?  51  LEU B CD1   1 
ATOM   5951  C  CD2   . LEU B 1 51  ? 154.593 157.812 165.178 1.00 53.40 ?  51  LEU B CD2   1 
ATOM   5952  N  N     . LYS B 1 52  ? 159.482 157.945 163.316 1.00 56.71 ?  52  LYS B N     1 
ATOM   5953  C  CA    . LYS B 1 52  ? 159.858 158.655 162.096 1.00 55.26 ?  52  LYS B CA    1 
ATOM   5954  C  C     . LYS B 1 52  ? 160.427 157.699 161.055 1.00 56.32 ?  52  LYS B C     1 
ATOM   5955  O  O     . LYS B 1 52  ? 160.047 157.746 159.879 1.00 57.80 ?  52  LYS B O     1 
ATOM   5956  C  CB    . LYS B 1 52  ? 160.867 159.758 162.420 1.00 56.33 ?  52  LYS B CB    1 
ATOM   5957  C  CG    . LYS B 1 52  ? 160.427 161.148 161.989 1.00 57.26 ?  52  LYS B CG    1 
ATOM   5958  C  CD    . LYS B 1 52  ? 160.390 161.278 160.477 1.00 58.35 ?  52  LYS B CD    1 
ATOM   5959  C  CE    . LYS B 1 52  ? 159.653 162.538 160.053 1.00 58.29 ?  52  LYS B CE    1 
ATOM   5960  N  NZ    . LYS B 1 52  ? 159.473 162.607 158.576 1.00 58.58 1  52  LYS B NZ    1 
ATOM   5961  N  N     . GLU B 1 53  ? 161.341 156.819 161.473 1.00 59.10 ?  53  GLU B N     1 
ATOM   5962  C  CA    . GLU B 1 53  ? 161.924 155.862 160.538 1.00 59.32 ?  53  GLU B CA    1 
ATOM   5963  C  C     . GLU B 1 53  ? 160.870 154.898 160.011 1.00 57.39 ?  53  GLU B C     1 
ATOM   5964  O  O     . GLU B 1 53  ? 160.879 154.547 158.827 1.00 59.82 ?  53  GLU B O     1 
ATOM   5965  C  CB    . GLU B 1 53  ? 163.067 155.098 161.204 1.00 59.95 ?  53  GLU B CB    1 
ATOM   5966  C  CG    . GLU B 1 53  ? 164.075 155.983 161.910 1.00 60.72 ?  53  GLU B CG    1 
ATOM   5967  C  CD    . GLU B 1 53  ? 165.502 155.518 161.706 1.00 62.00 ?  53  GLU B CD    1 
ATOM   5968  O  OE1   . GLU B 1 53  ? 165.826 154.388 162.129 1.00 62.82 ?  53  GLU B OE1   1 
ATOM   5969  O  OE2   . GLU B 1 53  ? 166.299 156.280 161.120 1.00 61.66 -1 53  GLU B OE2   1 
ATOM   5970  N  N     . LYS B 1 54  ? 159.954 154.458 160.876 1.00 54.54 ?  54  LYS B N     1 
ATOM   5971  C  CA    . LYS B 1 54  ? 158.890 153.561 160.439 1.00 54.20 ?  54  LYS B CA    1 
ATOM   5972  C  C     . LYS B 1 54  ? 158.014 154.222 159.384 1.00 52.54 ?  54  LYS B C     1 
ATOM   5973  O  O     . LYS B 1 54  ? 157.725 153.628 158.337 1.00 52.90 ?  54  LYS B O     1 
ATOM   5974  C  CB    . LYS B 1 54  ? 158.048 153.128 161.638 1.00 53.29 ?  54  LYS B CB    1 
ATOM   5975  C  CG    . LYS B 1 54  ? 156.795 152.361 161.262 1.00 54.25 ?  54  LYS B CG    1 
ATOM   5976  C  CD    . LYS B 1 54  ? 156.301 151.522 162.421 1.00 53.22 ?  54  LYS B CD    1 
ATOM   5977  C  CE    . LYS B 1 54  ? 155.077 150.717 162.036 1.00 53.86 ?  54  LYS B CE    1 
ATOM   5978  N  NZ    . LYS B 1 54  ? 154.919 149.514 162.898 1.00 54.25 1  54  LYS B NZ    1 
ATOM   5979  N  N     . LEU B 1 55  ? 157.585 155.458 159.644 1.00 52.77 ?  55  LEU B N     1 
ATOM   5980  C  CA    . LEU B 1 55  ? 156.731 156.158 158.690 1.00 53.11 ?  55  LEU B CA    1 
ATOM   5981  C  C     . LEU B 1 55  ? 157.463 156.420 157.382 1.00 56.57 ?  55  LEU B C     1 
ATOM   5982  O  O     . LEU B 1 55  ? 156.883 156.263 156.302 1.00 60.90 ?  55  LEU B O     1 
ATOM   5983  C  CB    . LEU B 1 55  ? 156.227 157.466 159.297 1.00 55.67 ?  55  LEU B CB    1 
ATOM   5984  C  CG    . LEU B 1 55  ? 155.006 157.357 160.212 1.00 55.50 ?  55  LEU B CG    1 
ATOM   5985  C  CD1   . LEU B 1 55  ? 154.285 158.689 160.265 1.00 56.44 ?  55  LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B 1 55  ? 154.066 156.255 159.746 1.00 54.78 ?  55  LEU B CD2   1 
ATOM   5987  N  N     . ASP B 1 56  ? 158.737 156.815 157.453 1.00 56.68 ?  56  ASP B N     1 
ATOM   5988  C  CA    . ASP B 1 56  ? 159.501 157.047 156.232 1.00 56.24 ?  56  ASP B CA    1 
ATOM   5989  C  C     . ASP B 1 56  ? 159.654 155.763 155.426 1.00 57.03 ?  56  ASP B C     1 
ATOM   5990  O  O     . ASP B 1 56  ? 159.479 155.766 154.203 1.00 57.75 ?  56  ASP B O     1 
ATOM   5991  C  CB    . ASP B 1 56  ? 160.868 157.637 156.573 1.00 59.58 ?  56  ASP B CB    1 
ATOM   5992  C  CG    . ASP B 1 56  ? 160.768 159.004 157.219 1.00 60.61 ?  56  ASP B CG    1 
ATOM   5993  O  OD1   . ASP B 1 56  ? 159.650 159.559 157.271 1.00 61.48 ?  56  ASP B OD1   1 
ATOM   5994  O  OD2   . ASP B 1 56  ? 161.806 159.525 157.677 1.00 59.36 -1 56  ASP B OD2   1 
ATOM   5995  N  N     . TYR B 1 57  ? 159.972 154.652 156.095 1.00 55.74 ?  57  TYR B N     1 
ATOM   5996  C  CA    . TYR B 1 57  ? 160.123 153.384 155.393 1.00 56.06 ?  57  TYR B CA    1 
ATOM   5997  C  C     . TYR B 1 57  ? 158.812 152.957 154.747 1.00 56.30 ?  57  TYR B C     1 
ATOM   5998  O  O     . TYR B 1 57  ? 158.803 152.460 153.616 1.00 60.11 ?  57  TYR B O     1 
ATOM   5999  C  CB    . TYR B 1 57  ? 160.626 152.307 156.357 1.00 55.53 ?  57  TYR B CB    1 
ATOM   6000  C  CG    . TYR B 1 57  ? 160.632 150.907 155.783 1.00 56.81 ?  57  TYR B CG    1 
ATOM   6001  C  CD1   . TYR B 1 57  ? 161.718 150.441 155.057 1.00 57.13 ?  57  TYR B CD1   1 
ATOM   6002  C  CD2   . TYR B 1 57  ? 159.556 150.048 155.976 1.00 59.01 ?  57  TYR B CD2   1 
ATOM   6003  C  CE1   . TYR B 1 57  ? 161.731 149.163 154.531 1.00 57.09 ?  57  TYR B CE1   1 
ATOM   6004  C  CE2   . TYR B 1 57  ? 159.560 148.770 155.454 1.00 59.36 ?  57  TYR B CE2   1 
ATOM   6005  C  CZ    . TYR B 1 57  ? 160.651 148.331 154.734 1.00 59.35 ?  57  TYR B CZ    1 
ATOM   6006  O  OH    . TYR B 1 57  ? 160.658 147.058 154.213 1.00 59.74 ?  57  TYR B OH    1 
ATOM   6007  N  N     . LEU B 1 58  ? 157.693 153.144 155.448 1.00 53.38 ?  58  LEU B N     1 
ATOM   6008  C  CA    . LEU B 1 58  ? 156.406 152.758 154.883 1.00 52.61 ?  58  LEU B CA    1 
ATOM   6009  C  C     . LEU B 1 58  ? 155.975 153.696 153.761 1.00 51.55 ?  58  LEU B C     1 
ATOM   6010  O  O     . LEU B 1 58  ? 155.205 153.293 152.883 1.00 53.00 ?  58  LEU B O     1 
ATOM   6011  C  CB    . LEU B 1 58  ? 155.347 152.708 155.984 1.00 52.55 ?  58  LEU B CB    1 
ATOM   6012  C  CG    . LEU B 1 58  ? 155.566 151.609 157.027 1.00 52.17 ?  58  LEU B CG    1 
ATOM   6013  C  CD1   . LEU B 1 58  ? 154.749 151.871 158.280 1.00 52.11 ?  58  LEU B CD1   1 
ATOM   6014  C  CD2   . LEU B 1 58  ? 155.238 150.244 156.447 1.00 53.03 ?  58  LEU B CD2   1 
ATOM   6015  N  N     . VAL B 1 59  ? 156.455 154.939 153.767 1.00 55.47 ?  59  VAL B N     1 
ATOM   6016  C  CA    . VAL B 1 59  ? 156.057 155.886 152.732 1.00 56.82 ?  59  VAL B CA    1 
ATOM   6017  C  C     . VAL B 1 59  ? 156.874 155.680 151.461 1.00 57.98 ?  59  VAL B C     1 
ATOM   6018  O  O     . VAL B 1 59  ? 156.317 155.579 150.361 1.00 56.51 ?  59  VAL B O     1 
ATOM   6019  C  CB    . VAL B 1 59  ? 156.173 157.329 153.256 1.00 56.13 ?  59  VAL B CB    1 
ATOM   6020  C  CG1   . VAL B 1 59  ? 156.343 158.308 152.104 1.00 55.82 ?  59  VAL B CG1   1 
ATOM   6021  C  CG2   . VAL B 1 59  ? 154.953 157.687 154.089 1.00 55.43 ?  59  VAL B CG2   1 
ATOM   6022  N  N     . GLU B 1 60  ? 158.204 155.612 151.585 1.00 59.74 ?  60  GLU B N     1 
ATOM   6023  C  CA    . GLU B 1 60  ? 159.038 155.481 150.392 1.00 59.69 ?  60  GLU B CA    1 
ATOM   6024  C  C     . GLU B 1 60  ? 158.900 154.110 149.741 1.00 59.71 ?  60  GLU B C     1 
ATOM   6025  O  O     . GLU B 1 60  ? 159.053 153.992 148.520 1.00 61.21 ?  60  GLU B O     1 
ATOM   6026  C  CB    . GLU B 1 60  ? 160.506 155.764 150.718 1.00 59.21 ?  60  GLU B CB    1 
ATOM   6027  C  CG    . GLU B 1 60  ? 160.739 156.929 151.661 1.00 60.66 ?  60  GLU B CG    1 
ATOM   6028  C  CD    . GLU B 1 60  ? 161.882 156.675 152.624 1.00 62.93 ?  60  GLU B CD    1 
ATOM   6029  O  OE1   . GLU B 1 60  ? 162.338 157.638 153.276 1.00 59.92 ?  60  GLU B OE1   1 
ATOM   6030  O  OE2   . GLU B 1 60  ? 162.325 155.512 152.731 1.00 61.95 -1 60  GLU B OE2   1 
ATOM   6031  N  N     . ASN B 1 61  ? 158.621 153.068 150.523 1.00 55.81 ?  61  ASN B N     1 
ATOM   6032  C  CA    . ASN B 1 61  ? 158.467 151.723 149.988 1.00 56.10 ?  61  ASN B CA    1 
ATOM   6033  C  C     . ASN B 1 61  ? 157.061 151.456 149.463 1.00 56.29 ?  61  ASN B C     1 
ATOM   6034  O  O     . ASN B 1 61  ? 156.692 150.291 149.272 1.00 58.43 ?  61  ASN B O     1 
ATOM   6035  C  CB    . ASN B 1 61  ? 158.843 150.685 151.046 1.00 56.83 ?  61  ASN B CB    1 
ATOM   6036  C  CG    . ASN B 1 61  ? 160.335 150.634 151.305 1.00 58.89 ?  61  ASN B CG    1 
ATOM   6037  O  OD1   . ASN B 1 61  ? 161.044 149.798 150.747 1.00 58.92 ?  61  ASN B OD1   1 
ATOM   6038  N  ND2   . ASN B 1 61  ? 160.819 151.536 152.150 1.00 58.89 ?  61  ASN B ND2   1 
ATOM   6039  N  N     . GLN B 1 62  ? 156.277 152.511 149.229 1.00 55.77 ?  62  GLN B N     1 
ATOM   6040  C  CA    . GLN B 1 62  ? 154.944 152.407 148.632 1.00 57.06 ?  62  GLN B CA    1 
ATOM   6041  C  C     . GLN B 1 62  ? 154.020 151.513 149.455 1.00 55.48 ?  62  GLN B C     1 
ATOM   6042  O  O     . GLN B 1 62  ? 153.194 150.775 148.914 1.00 56.00 ?  62  GLN B O     1 
ATOM   6043  C  CB    . GLN B 1 62  ? 155.025 151.919 147.182 1.00 54.59 ?  62  GLN B CB    1 
ATOM   6044  C  CG    . GLN B 1 62  ? 156.046 152.661 146.335 1.00 55.59 ?  62  GLN B CG    1 
ATOM   6045  C  CD    . GLN B 1 62  ? 155.944 154.167 146.478 1.00 58.59 ?  62  GLN B CD    1 
ATOM   6046  O  OE1   . GLN B 1 62  ? 154.982 154.782 146.020 1.00 58.31 ?  62  GLN B OE1   1 
ATOM   6047  N  NE2   . GLN B 1 62  ? 156.941 154.769 147.115 1.00 57.60 ?  62  GLN B NE2   1 
ATOM   6048  N  N     . TYR B 1 63  ? 154.158 151.576 150.779 1.00 52.92 ?  63  TYR B N     1 
ATOM   6049  C  CA    . TYR B 1 63  ? 153.206 150.929 151.672 1.00 52.23 ?  63  TYR B CA    1 
ATOM   6050  C  C     . TYR B 1 63  ? 152.082 151.872 152.074 1.00 52.08 ?  63  TYR B C     1 
ATOM   6051  O  O     . TYR B 1 63  ? 150.926 151.450 152.181 1.00 51.06 ?  63  TYR B O     1 
ATOM   6052  C  CB    . TYR B 1 63  ? 153.912 150.412 152.928 1.00 51.41 ?  63  TYR B CB    1 
ATOM   6053  C  CG    . TYR B 1 63  ? 154.781 149.199 152.702 1.00 53.74 ?  63  TYR B CG    1 
ATOM   6054  C  CD1   . TYR B 1 63  ? 154.231 147.994 152.288 1.00 51.61 ?  63  TYR B CD1   1 
ATOM   6055  C  CD2   . TYR B 1 63  ? 156.151 149.257 152.912 1.00 53.83 ?  63  TYR B CD2   1 
ATOM   6056  C  CE1   . TYR B 1 63  ? 155.023 146.883 152.085 1.00 54.06 ?  63  TYR B CE1   1 
ATOM   6057  C  CE2   . TYR B 1 63  ? 156.951 148.153 152.712 1.00 52.91 ?  63  TYR B CE2   1 
ATOM   6058  C  CZ    . TYR B 1 63  ? 156.384 146.969 152.297 1.00 55.02 ?  63  TYR B CZ    1 
ATOM   6059  O  OH    . TYR B 1 63  ? 157.182 145.867 152.096 1.00 55.71 ?  63  TYR B OH    1 
ATOM   6060  N  N     . TYR B 1 64  ? 152.404 153.143 152.295 1.00 49.23 ?  64  TYR B N     1 
ATOM   6061  C  CA    . TYR B 1 64  ? 151.448 154.142 152.739 1.00 46.99 ?  64  TYR B CA    1 
ATOM   6062  C  C     . TYR B 1 64  ? 151.324 155.251 151.705 1.00 48.94 ?  64  TYR B C     1 
ATOM   6063  O  O     . TYR B 1 64  ? 152.291 155.595 151.019 1.00 50.62 ?  64  TYR B O     1 
ATOM   6064  C  CB    . TYR B 1 64  ? 151.866 154.757 154.077 1.00 47.69 ?  64  TYR B CB    1 
ATOM   6065  C  CG    . TYR B 1 64  ? 151.587 153.895 155.281 1.00 47.26 ?  64  TYR B CG    1 
ATOM   6066  C  CD1   . TYR B 1 64  ? 150.920 152.683 155.156 1.00 47.65 ?  64  TYR B CD1   1 
ATOM   6067  C  CD2   . TYR B 1 64  ? 151.994 154.293 156.544 1.00 47.78 ?  64  TYR B CD2   1 
ATOM   6068  C  CE1   . TYR B 1 64  ? 150.666 151.895 156.259 1.00 45.62 ?  64  TYR B CE1   1 
ATOM   6069  C  CE2   . TYR B 1 64  ? 151.746 153.514 157.648 1.00 48.04 ?  64  TYR B CE2   1 
ATOM   6070  C  CZ    . TYR B 1 64  ? 151.084 152.317 157.503 1.00 47.45 ?  64  TYR B CZ    1 
ATOM   6071  O  OH    . TYR B 1 64  ? 150.840 151.545 158.612 1.00 49.14 ?  64  TYR B OH    1 
ATOM   6072  N  N     . GLU B 1 65  ? 150.122 155.805 151.597 1.00 51.99 ?  65  GLU B N     1 
ATOM   6073  C  CA    . GLU B 1 65  ? 149.939 157.038 150.846 1.00 51.96 ?  65  GLU B CA    1 
ATOM   6074  C  C     . GLU B 1 65  ? 150.489 158.205 151.655 1.00 54.39 ?  65  GLU B C     1 
ATOM   6075  O  O     . GLU B 1 65  ? 150.186 158.347 152.843 1.00 55.86 ?  65  GLU B O     1 
ATOM   6076  C  CB    . GLU B 1 65  ? 148.462 157.255 150.525 1.00 50.39 ?  65  GLU B CB    1 
ATOM   6077  C  CG    . GLU B 1 65  ? 147.815 156.102 149.777 1.00 51.97 ?  65  GLU B CG    1 
ATOM   6078  C  CD    . GLU B 1 65  ? 146.329 156.307 149.560 1.00 55.50 ?  65  GLU B CD    1 
ATOM   6079  O  OE1   . GLU B 1 65  ? 145.680 156.930 150.426 1.00 54.42 ?  65  GLU B OE1   1 
ATOM   6080  O  OE2   . GLU B 1 65  ? 145.810 155.847 148.520 1.00 54.21 -1 65  GLU B OE2   1 
ATOM   6081  N  N     . GLU B 1 66  ? 151.311 159.037 151.018 1.00 52.84 ?  66  GLU B N     1 
ATOM   6082  C  CA    . GLU B 1 66  ? 151.931 160.147 151.729 1.00 54.72 ?  66  GLU B CA    1 
ATOM   6083  C  C     . GLU B 1 66  ? 151.003 161.345 151.877 1.00 54.99 ?  66  GLU B C     1 
ATOM   6084  O  O     . GLU B 1 66  ? 151.276 162.222 152.704 1.00 54.13 ?  66  GLU B O     1 
ATOM   6085  C  CB    . GLU B 1 66  ? 153.218 160.572 151.018 1.00 55.88 ?  66  GLU B CB    1 
ATOM   6086  C  CG    . GLU B 1 66  ? 153.003 161.490 149.828 1.00 55.41 ?  66  GLU B CG    1 
ATOM   6087  C  CD    . GLU B 1 66  ? 154.278 162.184 149.394 1.00 56.78 ?  66  GLU B CD    1 
ATOM   6088  O  OE1   . GLU B 1 66  ? 155.349 161.543 149.444 1.00 55.65 ?  66  GLU B OE1   1 
ATOM   6089  O  OE2   . GLU B 1 66  ? 154.209 163.368 149.005 1.00 56.59 -1 66  GLU B OE2   1 
ATOM   6090  N  N     . GLU B 1 67  ? 149.911 161.394 151.113 1.00 53.83 ?  67  GLU B N     1 
ATOM   6091  C  CA    . GLU B 1 67  ? 149.036 162.563 151.141 1.00 53.55 ?  67  GLU B CA    1 
ATOM   6092  C  C     . GLU B 1 67  ? 148.318 162.689 152.480 1.00 55.20 ?  67  GLU B C     1 
ATOM   6093  O  O     . GLU B 1 67  ? 148.274 163.774 153.068 1.00 55.05 ?  67  GLU B O     1 
ATOM   6094  C  CB    . GLU B 1 67  ? 148.025 162.507 149.991 1.00 54.00 ?  67  GLU B CB    1 
ATOM   6095  C  CG    . GLU B 1 67  ? 148.612 162.275 148.596 1.00 55.13 ?  67  GLU B CG    1 
ATOM   6096  C  CD    . GLU B 1 67  ? 149.097 160.855 148.369 1.00 58.09 ?  67  GLU B CD    1 
ATOM   6097  O  OE1   . GLU B 1 67  ? 150.277 160.680 147.999 1.00 57.11 ?  67  GLU B OE1   1 
ATOM   6098  O  OE2   . GLU B 1 67  ? 148.297 159.915 148.557 1.00 56.98 -1 67  GLU B OE2   1 
ATOM   6099  N  N     . PHE B 1 68  ? 147.747 161.589 152.977 1.00 50.07 ?  68  PHE B N     1 
ATOM   6100  C  CA    . PHE B 1 68  ? 146.996 161.666 154.227 1.00 46.19 ?  68  PHE B CA    1 
ATOM   6101  C  C     . PHE B 1 68  ? 147.916 161.887 155.421 1.00 46.50 ?  68  PHE B C     1 
ATOM   6102  O  O     . PHE B 1 68  ? 147.513 162.527 156.399 1.00 50.04 ?  68  PHE B O     1 
ATOM   6103  C  CB    . PHE B 1 68  ? 146.141 160.409 154.412 1.00 47.47 ?  68  PHE B CB    1 
ATOM   6104  C  CG    . PHE B 1 68  ? 146.814 159.311 155.189 1.00 47.17 ?  68  PHE B CG    1 
ATOM   6105  C  CD1   . PHE B 1 68  ? 147.660 158.418 154.560 1.00 45.17 ?  68  PHE B CD1   1 
ATOM   6106  C  CD2   . PHE B 1 68  ? 146.573 159.157 156.544 1.00 43.14 ?  68  PHE B CD2   1 
ATOM   6107  C  CE1   . PHE B 1 68  ? 148.273 157.405 155.270 1.00 44.22 ?  68  PHE B CE1   1 
ATOM   6108  C  CE2   . PHE B 1 68  ? 147.181 158.146 157.259 1.00 42.72 ?  68  PHE B CE2   1 
ATOM   6109  C  CZ    . PHE B 1 68  ? 148.029 157.267 156.620 1.00 44.93 ?  68  PHE B CZ    1 
ATOM   6110  N  N     . LEU B 1 69  ? 149.145 161.372 155.365 1.00 49.73 ?  69  LEU B N     1 
ATOM   6111  C  CA    . LEU B 1 69  ? 150.114 161.628 156.422 1.00 47.63 ?  69  LEU B CA    1 
ATOM   6112  C  C     . LEU B 1 69  ? 150.709 163.026 156.343 1.00 48.62 ?  69  LEU B C     1 
ATOM   6113  O  O     . LEU B 1 69  ? 151.190 163.537 157.360 1.00 52.37 ?  69  LEU B O     1 
ATOM   6114  C  CB    . LEU B 1 69  ? 151.238 160.591 156.374 1.00 47.53 ?  69  LEU B CB    1 
ATOM   6115  C  CG    . LEU B 1 69  ? 150.929 159.219 156.974 1.00 47.12 ?  69  LEU B CG    1 
ATOM   6116  C  CD1   . LEU B 1 69  ? 152.044 158.232 156.662 1.00 48.48 ?  69  LEU B CD1   1 
ATOM   6117  C  CD2   . LEU B 1 69  ? 150.704 159.324 158.473 1.00 47.04 ?  69  LEU B CD2   1 
ATOM   6118  N  N     . SER B 1 70  ? 150.689 163.654 155.165 1.00 48.36 ?  70  SER B N     1 
ATOM   6119  C  CA    . SER B 1 70  ? 151.255 164.990 155.024 1.00 47.28 ?  70  SER B CA    1 
ATOM   6120  C  C     . SER B 1 70  ? 150.371 166.067 155.638 1.00 49.11 ?  70  SER B C     1 
ATOM   6121  O  O     . SER B 1 70  ? 150.841 167.190 155.847 1.00 51.02 ?  70  SER B O     1 
ATOM   6122  C  CB    . SER B 1 70  ? 151.503 165.303 153.548 1.00 49.35 ?  70  SER B CB    1 
ATOM   6123  O  OG    . SER B 1 70  ? 150.299 165.660 152.893 1.00 49.06 ?  70  SER B OG    1 
ATOM   6124  N  N     . LEU B 1 71  ? 149.107 165.757 155.930 1.00 46.46 ?  71  LEU B N     1 
ATOM   6125  C  CA    . LEU B 1 71  ? 148.215 166.726 156.551 1.00 45.72 ?  71  LEU B CA    1 
ATOM   6126  C  C     . LEU B 1 71  ? 148.516 166.948 158.026 1.00 45.67 ?  71  LEU B C     1 
ATOM   6127  O  O     . LEU B 1 71  ? 147.969 167.885 158.617 1.00 46.85 ?  71  LEU B O     1 
ATOM   6128  C  CB    . LEU B 1 71  ? 146.758 166.283 156.391 1.00 44.59 ?  71  LEU B CB    1 
ATOM   6129  C  CG    . LEU B 1 71  ? 146.268 166.048 154.963 1.00 47.01 ?  71  LEU B CG    1 
ATOM   6130  C  CD1   . LEU B 1 71  ? 145.325 164.859 154.915 1.00 49.18 ?  71  LEU B CD1   1 
ATOM   6131  C  CD2   . LEU B 1 71  ? 145.591 167.294 154.420 1.00 45.72 ?  71  LEU B CD2   1 
ATOM   6132  N  N     . TYR B 1 72  ? 149.362 166.118 158.628 1.00 43.56 ?  72  TYR B N     1 
ATOM   6133  C  CA    . TYR B 1 72  ? 149.742 166.246 160.026 1.00 44.85 ?  72  TYR B CA    1 
ATOM   6134  C  C     . TYR B 1 72  ? 151.242 166.473 160.130 1.00 46.70 ?  72  TYR B C     1 
ATOM   6135  O  O     . TYR B 1 72  ? 152.022 165.878 159.380 1.00 48.51 ?  72  TYR B O     1 
ATOM   6136  C  CB    . TYR B 1 72  ? 149.377 164.996 160.837 1.00 45.55 ?  72  TYR B CB    1 
ATOM   6137  C  CG    . TYR B 1 72  ? 147.979 164.466 160.625 1.00 42.98 ?  72  TYR B CG    1 
ATOM   6138  C  CD1   . TYR B 1 72  ? 147.683 163.642 159.547 1.00 42.35 ?  72  TYR B CD1   1 
ATOM   6139  C  CD2   . TYR B 1 72  ? 146.963 164.765 161.519 1.00 42.77 ?  72  TYR B CD2   1 
ATOM   6140  C  CE1   . TYR B 1 72  ? 146.410 163.149 159.357 1.00 40.87 ?  72  TYR B CE1   1 
ATOM   6141  C  CE2   . TYR B 1 72  ? 145.687 164.275 161.339 1.00 42.72 ?  72  TYR B CE2   1 
ATOM   6142  C  CZ    . TYR B 1 72  ? 145.417 163.468 160.254 1.00 42.62 ?  72  TYR B CZ    1 
ATOM   6143  O  OH    . TYR B 1 72  ? 144.148 162.977 160.066 1.00 45.08 ?  72  TYR B OH    1 
ATOM   6144  N  N     . SER B 1 73  ? 151.640 167.335 161.060 1.00 52.19 ?  73  SER B N     1 
ATOM   6145  C  CA    . SER B 1 73  ? 153.038 167.385 161.459 1.00 52.49 ?  73  SER B CA    1 
ATOM   6146  C  C     . SER B 1 73  ? 153.404 166.090 162.171 1.00 51.86 ?  73  SER B C     1 
ATOM   6147  O  O     . SER B 1 73  ? 152.548 165.411 162.744 1.00 54.01 ?  73  SER B O     1 
ATOM   6148  C  CB    . SER B 1 73  ? 153.296 168.586 162.368 1.00 51.38 ?  73  SER B CB    1 
ATOM   6149  O  OG    . SER B 1 73  ? 152.841 168.333 163.686 1.00 50.60 ?  73  SER B OG    1 
ATOM   6150  N  N     . PHE B 1 74  ? 154.691 165.735 162.119 1.00 54.68 ?  74  PHE B N     1 
ATOM   6151  C  CA    . PHE B 1 74  ? 155.106 164.465 162.707 1.00 53.82 ?  74  PHE B CA    1 
ATOM   6152  C  C     . PHE B 1 74  ? 154.847 164.424 164.207 1.00 54.02 ?  74  PHE B C     1 
ATOM   6153  O  O     . PHE B 1 74  ? 154.649 163.342 164.768 1.00 55.52 ?  74  PHE B O     1 
ATOM   6154  C  CB    . PHE B 1 74  ? 156.582 164.188 162.429 1.00 54.59 ?  74  PHE B CB    1 
ATOM   6155  C  CG    . PHE B 1 74  ? 157.099 162.971 163.139 1.00 55.45 ?  74  PHE B CG    1 
ATOM   6156  C  CD1   . PHE B 1 74  ? 156.684 161.706 162.757 1.00 53.33 ?  74  PHE B CD1   1 
ATOM   6157  C  CD2   . PHE B 1 74  ? 157.975 163.090 164.203 1.00 55.41 ?  74  PHE B CD2   1 
ATOM   6158  C  CE1   . PHE B 1 74  ? 157.142 160.582 163.414 1.00 55.48 ?  74  PHE B CE1   1 
ATOM   6159  C  CE2   . PHE B 1 74  ? 158.439 161.968 164.865 1.00 55.10 ?  74  PHE B CE2   1 
ATOM   6160  C  CZ    . PHE B 1 74  ? 158.022 160.714 164.470 1.00 55.55 ?  74  PHE B CZ    1 
ATOM   6161  N  N     . GLU B 1 75  ? 154.846 165.580 164.872 1.00 54.99 ?  75  GLU B N     1 
ATOM   6162  C  CA    . GLU B 1 75  ? 154.509 165.603 166.293 1.00 56.01 ?  75  GLU B CA    1 
ATOM   6163  C  C     . GLU B 1 75  ? 153.078 165.135 166.521 1.00 56.55 ?  75  GLU B C     1 
ATOM   6164  O  O     . GLU B 1 75  ? 152.804 164.384 167.463 1.00 57.06 ?  75  GLU B O     1 
ATOM   6165  C  CB    . GLU B 1 75  ? 154.716 167.008 166.860 1.00 56.12 ?  75  GLU B CB    1 
ATOM   6166  C  CG    . GLU B 1 75  ? 156.103 167.257 167.435 1.00 56.08 ?  75  GLU B CG    1 
ATOM   6167  C  CD    . GLU B 1 75  ? 157.209 166.674 166.578 1.00 59.46 ?  75  GLU B CD    1 
ATOM   6168  O  OE1   . GLU B 1 75  ? 157.464 167.216 165.482 1.00 59.31 ?  75  GLU B OE1   1 
ATOM   6169  O  OE2   . GLU B 1 75  ? 157.826 165.672 167.000 1.00 59.07 -1 75  GLU B OE2   1 
ATOM   6170  N  N     . ASP B 1 76  ? 152.153 165.561 165.659 1.00 52.52 ?  76  ASP B N     1 
ATOM   6171  C  CA    . ASP B 1 76  ? 150.762 165.138 165.787 1.00 51.01 ?  76  ASP B CA    1 
ATOM   6172  C  C     . ASP B 1 76  ? 150.607 163.643 165.532 1.00 49.96 ?  76  ASP B C     1 
ATOM   6173  O  O     . ASP B 1 76  ? 149.852 162.963 166.238 1.00 53.31 ?  76  ASP B O     1 
ATOM   6174  C  CB    . ASP B 1 76  ? 149.889 165.945 164.829 1.00 52.34 ?  76  ASP B CB    1 
ATOM   6175  C  CG    . ASP B 1 76  ? 149.738 167.389 165.262 1.00 54.36 ?  76  ASP B CG    1 
ATOM   6176  O  OD1   . ASP B 1 76  ? 150.164 167.719 166.389 1.00 53.96 ?  76  ASP B OD1   1 
ATOM   6177  O  OD2   . ASP B 1 76  ? 149.193 168.193 164.478 1.00 53.46 -1 76  ASP B OD2   1 
ATOM   6178  N  N     . ILE B 1 77  ? 151.308 163.113 164.528 1.00 47.36 ?  77  ILE B N     1 
ATOM   6179  C  CA    . ILE B 1 77  ? 151.251 161.679 164.256 1.00 47.58 ?  77  ILE B CA    1 
ATOM   6180  C  C     . ILE B 1 77  ? 151.832 160.893 165.422 1.00 48.60 ?  77  ILE B C     1 
ATOM   6181  O  O     . ILE B 1 77  ? 151.307 159.840 165.809 1.00 50.21 ?  77  ILE B O     1 
ATOM   6182  C  CB    . ILE B 1 77  ? 151.978 161.354 162.939 1.00 49.12 ?  77  ILE B CB    1 
ATOM   6183  C  CG1   . ILE B 1 77  ? 151.364 162.141 161.783 1.00 48.20 ?  77  ILE B CG1   1 
ATOM   6184  C  CG2   . ILE B 1 77  ? 151.917 159.865 162.657 1.00 46.74 ?  77  ILE B CG2   1 
ATOM   6185  C  CD1   . ILE B 1 77  ? 152.190 162.109 160.519 1.00 45.94 ?  77  ILE B CD1   1 
ATOM   6186  N  N     . LYS B 1 78  ? 152.936 161.382 165.991 1.00 50.55 ?  78  LYS B N     1 
ATOM   6187  C  CA    . LYS B 1 78  ? 153.519 160.743 167.164 1.00 50.70 ?  78  LYS B CA    1 
ATOM   6188  C  C     . LYS B 1 78  ? 152.544 160.755 168.332 1.00 49.63 ?  78  LYS B C     1 
ATOM   6189  O  O     . LYS B 1 78  ? 152.424 159.763 169.056 1.00 50.68 ?  78  LYS B O     1 
ATOM   6190  C  CB    . LYS B 1 78  ? 154.822 161.445 167.549 1.00 53.57 ?  78  LYS B CB    1 
ATOM   6191  C  CG    . LYS B 1 78  ? 155.791 160.584 168.336 1.00 52.73 ?  78  LYS B CG    1 
ATOM   6192  C  CD    . LYS B 1 78  ? 156.691 161.443 169.209 1.00 53.81 ?  78  LYS B CD    1 
ATOM   6193  C  CE    . LYS B 1 78  ? 157.930 160.687 169.649 1.00 54.50 ?  78  LYS B CE    1 
ATOM   6194  N  NZ    . LYS B 1 78  ? 159.167 161.245 169.037 1.00 52.68 1  78  LYS B NZ    1 
ATOM   6195  N  N     . GLU B 1 79  ? 151.840 161.871 168.528 1.00 51.71 ?  79  GLU B N     1 
ATOM   6196  C  CA    . GLU B 1 79  ? 150.855 161.950 169.602 1.00 51.17 ?  79  GLU B CA    1 
ATOM   6197  C  C     . GLU B 1 79  ? 149.709 160.971 169.372 1.00 49.54 ?  79  GLU B C     1 
ATOM   6198  O  O     . GLU B 1 79  ? 149.225 160.339 170.316 1.00 51.83 ?  79  GLU B O     1 
ATOM   6199  C  CB    . GLU B 1 79  ? 150.336 163.382 169.720 1.00 49.44 ?  79  GLU B CB    1 
ATOM   6200  C  CG    . GLU B 1 79  ? 150.971 164.171 170.854 1.00 52.62 ?  79  GLU B CG    1 
ATOM   6201  C  CD    . GLU B 1 79  ? 150.118 165.337 171.309 1.00 56.12 ?  79  GLU B CD    1 
ATOM   6202  O  OE1   . GLU B 1 79  ? 150.470 165.972 172.325 1.00 54.05 ?  79  GLU B OE1   1 
ATOM   6203  O  OE2   . GLU B 1 79  ? 149.104 165.629 170.643 1.00 56.75 -1 79  GLU B OE2   1 
ATOM   6204  N  N     . VAL B 1 80  ? 149.268 160.828 168.122 1.00 43.97 ?  80  VAL B N     1 
ATOM   6205  C  CA    . VAL B 1 80  ? 148.203 159.879 167.806 1.00 41.94 ?  80  VAL B CA    1 
ATOM   6206  C  C     . VAL B 1 80  ? 148.655 158.447 168.079 1.00 46.28 ?  80  VAL B C     1 
ATOM   6207  O  O     . VAL B 1 80  ? 147.919 157.647 168.672 1.00 48.04 ?  80  VAL B O     1 
ATOM   6208  C  CB    . VAL B 1 80  ? 147.750 160.067 166.346 1.00 43.34 ?  80  VAL B CB    1 
ATOM   6209  C  CG1   . VAL B 1 80  ? 146.913 158.888 165.884 1.00 44.32 ?  80  VAL B CG1   1 
ATOM   6210  C  CG2   . VAL B 1 80  ? 146.973 161.364 166.199 1.00 44.52 ?  80  VAL B CG2   1 
ATOM   6211  N  N     . PHE B 1 81  ? 149.873 158.100 167.656 1.00 46.65 ?  81  PHE B N     1 
ATOM   6212  C  CA    . PHE B 1 81  ? 150.386 156.755 167.900 1.00 43.06 ?  81  PHE B CA    1 
ATOM   6213  C  C     . PHE B 1 81  ? 150.573 156.495 169.392 1.00 45.86 ?  81  PHE B C     1 
ATOM   6214  O  O     . PHE B 1 81  ? 150.315 155.386 169.876 1.00 48.13 ?  81  PHE B O     1 
ATOM   6215  C  CB    . PHE B 1 81  ? 151.701 156.551 167.147 1.00 40.92 ?  81  PHE B CB    1 
ATOM   6216  C  CG    . PHE B 1 81  ? 151.525 156.015 165.755 1.00 40.82 ?  81  PHE B CG    1 
ATOM   6217  C  CD1   . PHE B 1 81  ? 151.207 156.863 164.708 1.00 41.95 ?  81  PHE B CD1   1 
ATOM   6218  C  CD2   . PHE B 1 81  ? 151.678 154.665 165.492 1.00 42.08 ?  81  PHE B CD2   1 
ATOM   6219  C  CE1   . PHE B 1 81  ? 151.046 156.374 163.425 1.00 43.36 ?  81  PHE B CE1   1 
ATOM   6220  C  CE2   . PHE B 1 81  ? 151.518 154.171 164.212 1.00 42.11 ?  81  PHE B CE2   1 
ATOM   6221  C  CZ    . PHE B 1 81  ? 151.201 155.027 163.178 1.00 41.06 ?  81  PHE B CZ    1 
ATOM   6222  N  N     . LYS B 1 82  ? 151.031 157.505 170.134 1.00 47.33 ?  82  LYS B N     1 
ATOM   6223  C  CA    . LYS B 1 82  ? 151.169 157.363 171.579 1.00 46.06 ?  82  LYS B CA    1 
ATOM   6224  C  C     . LYS B 1 82  ? 149.813 157.178 172.244 1.00 44.98 ?  82  LYS B C     1 
ATOM   6225  O  O     . LYS B 1 82  ? 149.684 156.406 173.198 1.00 46.57 ?  82  LYS B O     1 
ATOM   6226  C  CB    . LYS B 1 82  ? 151.892 158.578 172.161 1.00 46.55 ?  82  LYS B CB    1 
ATOM   6227  C  CG    . LYS B 1 82  ? 153.386 158.600 171.891 1.00 47.41 ?  82  LYS B CG    1 
ATOM   6228  C  CD    . LYS B 1 82  ? 154.171 158.157 173.113 1.00 47.76 ?  82  LYS B CD    1 
ATOM   6229  C  CE    . LYS B 1 82  ? 153.839 159.018 174.321 1.00 49.18 ?  82  LYS B CE    1 
ATOM   6230  N  NZ    . LYS B 1 82  ? 154.506 160.347 174.255 1.00 48.24 1  82  LYS B NZ    1 
ATOM   6231  N  N     . THR B 1 83  ? 148.789 157.880 171.756 1.00 42.72 ?  83  THR B N     1 
ATOM   6232  C  CA    . THR B 1 83  ? 147.440 157.672 172.270 1.00 41.20 ?  83  THR B CA    1 
ATOM   6233  C  C     . THR B 1 83  ? 146.966 156.252 171.992 1.00 42.79 ?  83  THR B C     1 
ATOM   6234  O  O     . THR B 1 83  ? 146.312 155.628 172.835 1.00 45.00 ?  83  THR B O     1 
ATOM   6235  C  CB    . THR B 1 83  ? 146.481 158.691 171.655 1.00 41.20 ?  83  THR B CB    1 
ATOM   6236  O  OG1   . THR B 1 83  ? 146.935 160.016 171.955 1.00 46.81 ?  83  THR B OG1   1 
ATOM   6237  C  CG2   . THR B 1 83  ? 145.078 158.511 172.211 1.00 44.21 ?  83  THR B CG2   1 
ATOM   6238  N  N     . ALA B 1 84  ? 147.285 155.727 170.807 1.00 41.52 ?  84  ALA B N     1 
ATOM   6239  C  CA    . ALA B 1 84  ? 146.908 154.354 170.482 1.00 38.00 ?  84  ALA B CA    1 
ATOM   6240  C  C     . ALA B 1 84  ? 147.603 153.351 171.394 1.00 38.28 ?  84  ALA B C     1 
ATOM   6241  O  O     . ALA B 1 84  ? 146.979 152.393 171.863 1.00 43.99 ?  84  ALA B O     1 
ATOM   6242  C  CB    . ALA B 1 84  ? 147.225 154.054 169.019 1.00 39.60 ?  84  ALA B CB    1 
ATOM   6243  N  N     . TYR B 1 85  ? 148.894 153.553 171.652 1.00 45.05 ?  85  TYR B N     1 
ATOM   6244  C  CA    . TYR B 1 85  ? 149.654 152.614 172.471 1.00 43.36 ?  85  TYR B CA    1 
ATOM   6245  C  C     . TYR B 1 85  ? 149.460 152.818 173.969 1.00 44.29 ?  85  TYR B C     1 
ATOM   6246  O  O     . TYR B 1 85  ? 149.846 151.940 174.746 1.00 46.49 ?  85  TYR B O     1 
ATOM   6247  C  CB    . TYR B 1 85  ? 151.142 152.707 172.129 1.00 40.26 ?  85  TYR B CB    1 
ATOM   6248  C  CG    . TYR B 1 85  ? 151.531 151.922 170.898 1.00 41.59 ?  85  TYR B CG    1 
ATOM   6249  C  CD1   . TYR B 1 85  ? 151.891 150.586 170.993 1.00 43.79 ?  85  TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B 1 85  ? 151.531 152.513 169.642 1.00 43.92 ?  85  TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B 1 85  ? 152.247 149.861 169.875 1.00 44.17 ?  85  TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B 1 85  ? 151.884 151.795 168.518 1.00 43.73 ?  85  TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B 1 85  ? 152.241 150.470 168.640 1.00 43.21 ?  85  TYR B CZ    1 
ATOM   6254  O  OH    . TYR B 1 85  ? 152.594 149.749 167.525 1.00 45.29 ?  85  TYR B OH    1 
ATOM   6255  N  N     . ALA B 1 86  ? 148.877 153.941 174.392 1.00 43.66 ?  86  ALA B N     1 
ATOM   6256  C  CA    . ALA B 1 86  ? 148.677 154.175 175.818 1.00 42.01 ?  86  ALA B CA    1 
ATOM   6257  C  C     . ALA B 1 86  ? 147.607 153.263 176.398 1.00 45.48 ?  86  ALA B C     1 
ATOM   6258  O  O     . ALA B 1 86  ? 147.615 152.993 177.604 1.00 47.31 ?  86  ALA B O     1 
ATOM   6259  C  CB    . ALA B 1 86  ? 148.313 155.639 176.062 1.00 42.20 ?  86  ALA B CB    1 
ATOM   6260  N  N     . LYS B 1 87  ? 146.679 152.787 175.567 1.00 44.46 ?  87  LYS B N     1 
ATOM   6261  C  CA    . LYS B 1 87  ? 145.632 151.900 176.056 1.00 45.39 ?  87  LYS B CA    1 
ATOM   6262  C  C     . LYS B 1 87  ? 146.169 150.534 176.461 1.00 44.55 ?  87  LYS B C     1 
ATOM   6263  O  O     . LYS B 1 87  ? 145.503 149.828 177.226 1.00 46.37 ?  87  LYS B O     1 
ATOM   6264  C  CB    . LYS B 1 87  ? 144.543 151.736 174.995 1.00 43.93 ?  87  LYS B CB    1 
ATOM   6265  C  CG    . LYS B 1 87  ? 143.149 151.536 175.563 1.00 43.92 ?  87  LYS B CG    1 
ATOM   6266  C  CD    . LYS B 1 87  ? 142.543 150.226 175.092 1.00 44.50 ?  87  LYS B CD    1 
ATOM   6267  C  CE    . LYS B 1 87  ? 141.355 149.829 175.954 1.00 42.38 ?  87  LYS B CE    1 
ATOM   6268  N  NZ    . LYS B 1 87  ? 140.638 148.645 175.406 1.00 40.62 1  87  LYS B NZ    1 
ATOM   6269  N  N     . LYS B 1 88  ? 147.355 150.158 175.979 1.00 44.68 ?  88  LYS B N     1 
ATOM   6270  C  CA    . LYS B 1 88  ? 147.932 148.838 176.227 1.00 44.57 ?  88  LYS B CA    1 
ATOM   6271  C  C     . LYS B 1 88  ? 146.944 147.737 175.849 1.00 42.41 ?  88  LYS B C     1 
ATOM   6272  O  O     . LYS B 1 88  ? 146.678 146.811 176.619 1.00 43.90 ?  88  LYS B O     1 
ATOM   6273  C  CB    . LYS B 1 88  ? 148.386 148.693 177.681 1.00 45.79 ?  88  LYS B CB    1 
ATOM   6274  C  CG    . LYS B 1 88  ? 149.789 149.208 177.960 1.00 46.36 ?  88  LYS B CG    1 
ATOM   6275  C  CD    . LYS B 1 88  ? 149.794 150.694 178.269 1.00 45.95 ?  88  LYS B CD    1 
ATOM   6276  C  CE    . LYS B 1 88  ? 151.117 151.333 177.879 1.00 46.97 ?  88  LYS B CE    1 
ATOM   6277  N  NZ    . LYS B 1 88  ? 151.019 152.816 177.784 1.00 47.47 1  88  LYS B NZ    1 
ATOM   6278  N  N     . PHE B 1 89  ? 146.385 147.856 174.647 1.00 42.94 ?  89  PHE B N     1 
ATOM   6279  C  CA    . PHE B 1 89  ? 145.370 146.911 174.199 1.00 39.07 ?  89  PHE B CA    1 
ATOM   6280  C  C     . PHE B 1 89  ? 145.949 145.507 174.107 1.00 43.73 ?  89  PHE B C     1 
ATOM   6281  O  O     . PHE B 1 89  ? 147.030 145.299 173.548 1.00 46.25 ?  89  PHE B O     1 
ATOM   6282  C  CB    . PHE B 1 89  ? 144.804 147.337 172.844 1.00 37.31 ?  89  PHE B CB    1 
ATOM   6283  C  CG    . PHE B 1 89  ? 143.849 146.340 172.251 1.00 38.71 ?  89  PHE B CG    1 
ATOM   6284  C  CD1   . PHE B 1 89  ? 142.512 146.353 172.599 1.00 37.31 ?  89  PHE B CD1   1 
ATOM   6285  C  CD2   . PHE B 1 89  ? 144.292 145.384 171.350 1.00 38.40 ?  89  PHE B CD2   1 
ATOM   6286  C  CE1   . PHE B 1 89  ? 141.633 145.435 172.061 1.00 37.73 ?  89  PHE B CE1   1 
ATOM   6287  C  CE2   . PHE B 1 89  ? 143.417 144.463 170.811 1.00 34.60 ?  89  PHE B CE2   1 
ATOM   6288  C  CZ    . PHE B 1 89  ? 142.086 144.490 171.165 1.00 36.67 ?  89  PHE B CZ    1 
ATOM   6289  N  N     . ARG B 1 90  ? 145.217 144.541 174.652 1.00 42.62 ?  90  ARG B N     1 
ATOM   6290  C  CA    . ARG B 1 90  ? 145.594 143.137 174.607 1.00 40.51 ?  90  ARG B CA    1 
ATOM   6291  C  C     . ARG B 1 90  ? 144.466 142.345 173.967 1.00 41.89 ?  90  ARG B C     1 
ATOM   6292  O  O     . ARG B 1 90  ? 143.295 142.535 174.312 1.00 42.84 ?  90  ARG B O     1 
ATOM   6293  C  CB    . ARG B 1 90  ? 145.891 142.600 176.009 1.00 45.34 ?  90  ARG B CB    1 
ATOM   6294  C  CG    . ARG B 1 90  ? 147.033 143.307 176.716 1.00 42.68 ?  90  ARG B CG    1 
ATOM   6295  C  CD    . ARG B 1 90  ? 148.365 143.001 176.054 1.00 45.15 ?  90  ARG B CD    1 
ATOM   6296  N  NE    . ARG B 1 90  ? 149.430 143.864 176.550 1.00 45.79 ?  90  ARG B NE    1 
ATOM   6297  C  CZ    . ARG B 1 90  ? 149.925 144.897 175.884 1.00 44.67 ?  90  ARG B CZ    1 
ATOM   6298  N  NH1   . ARG B 1 90  ? 149.481 145.223 174.682 1.00 46.68 1  90  ARG B NH1   1 
ATOM   6299  N  NH2   . ARG B 1 90  ? 150.893 145.622 176.439 1.00 44.05 ?  90  ARG B NH2   1 
ATOM   6300  N  N     . PHE B 1 91  ? 144.816 141.471 173.037 1.00 39.25 ?  91  PHE B N     1 
ATOM   6301  C  CA    . PHE B 1 91  ? 143.829 140.589 172.435 1.00 38.08 ?  91  PHE B CA    1 
ATOM   6302  C  C     . PHE B 1 91  ? 143.428 139.528 173.450 1.00 43.46 ?  91  PHE B C     1 
ATOM   6303  O  O     . PHE B 1 91  ? 144.293 138.774 173.916 1.00 45.50 ?  91  PHE B O     1 
ATOM   6304  C  CB    . PHE B 1 91  ? 144.390 139.944 171.174 1.00 38.01 ?  91  PHE B CB    1 
ATOM   6305  C  CG    . PHE B 1 91  ? 144.447 140.869 169.992 1.00 39.78 ?  91  PHE B CG    1 
ATOM   6306  C  CD1   . PHE B 1 91  ? 143.304 141.161 169.267 1.00 40.90 ?  91  PHE B CD1   1 
ATOM   6307  C  CD2   . PHE B 1 91  ? 145.643 141.449 169.607 1.00 39.02 ?  91  PHE B CD2   1 
ATOM   6308  C  CE1   . PHE B 1 91  ? 143.355 142.010 168.180 1.00 39.44 ?  91  PHE B CE1   1 
ATOM   6309  C  CE2   . PHE B 1 91  ? 145.699 142.298 168.521 1.00 39.13 ?  91  PHE B CE2   1 
ATOM   6310  C  CZ    . PHE B 1 91  ? 144.553 142.580 167.808 1.00 39.68 ?  91  PHE B CZ    1 
ATOM   6311  N  N     . PRO B 1 92  ? 142.149 139.426 173.822 1.00 42.41 ?  92  PRO B N     1 
ATOM   6312  C  CA    . PRO B 1 92  ? 141.765 138.458 174.859 1.00 42.17 ?  92  PRO B CA    1 
ATOM   6313  C  C     . PRO B 1 92  ? 141.733 137.021 174.375 1.00 42.72 ?  92  PRO B C     1 
ATOM   6314  O  O     . PRO B 1 92  ? 141.725 136.107 175.210 1.00 43.37 ?  92  PRO B O     1 
ATOM   6315  C  CB    . PRO B 1 92  ? 140.368 138.931 175.274 1.00 41.94 ?  92  PRO B CB    1 
ATOM   6316  C  CG    . PRO B 1 92  ? 139.820 139.554 174.039 1.00 41.93 ?  92  PRO B CG    1 
ATOM   6317  C  CD    . PRO B 1 92  ? 140.989 140.177 173.310 1.00 40.90 ?  92  PRO B CD    1 
ATOM   6318  N  N     . SER B 1 93  ? 141.717 136.793 173.065 1.00 42.05 ?  93  SER B N     1 
ATOM   6319  C  CA    . SER B 1 93  ? 141.680 135.455 172.502 1.00 39.78 ?  93  SER B CA    1 
ATOM   6320  C  C     . SER B 1 93  ? 142.757 135.328 171.436 1.00 40.03 ?  93  SER B C     1 
ATOM   6321  O  O     . SER B 1 93  ? 143.144 136.312 170.802 1.00 44.07 ?  93  SER B O     1 
ATOM   6322  C  CB    . SER B 1 93  ? 140.304 135.135 171.902 1.00 42.98 ?  93  SER B CB    1 
ATOM   6323  O  OG    . SER B 1 93  ? 140.201 135.617 170.574 1.00 44.75 ?  93  SER B OG    1 
ATOM   6324  N  N     . PHE B 1 94  ? 143.245 134.099 171.254 1.00 40.58 ?  94  PHE B N     1 
ATOM   6325  C  CA    . PHE B 1 94  ? 144.273 133.858 170.249 1.00 41.09 ?  94  PHE B CA    1 
ATOM   6326  C  C     . PHE B 1 94  ? 143.755 134.151 168.848 1.00 41.10 ?  94  PHE B C     1 
ATOM   6327  O  O     . PHE B 1 94  ? 144.479 134.705 168.013 1.00 43.52 ?  94  PHE B O     1 
ATOM   6328  C  CB    . PHE B 1 94  ? 144.775 132.416 170.342 1.00 42.58 ?  94  PHE B CB    1 
ATOM   6329  C  CG    . PHE B 1 94  ? 145.365 131.899 169.061 1.00 39.39 ?  94  PHE B CG    1 
ATOM   6330  C  CD1   . PHE B 1 94  ? 146.582 132.372 168.603 1.00 41.36 ?  94  PHE B CD1   1 
ATOM   6331  C  CD2   . PHE B 1 94  ? 144.700 130.944 168.310 1.00 41.92 ?  94  PHE B CD2   1 
ATOM   6332  C  CE1   . PHE B 1 94  ? 147.124 131.904 167.423 1.00 41.54 ?  94  PHE B CE1   1 
ATOM   6333  C  CE2   . PHE B 1 94  ? 145.237 130.471 167.130 1.00 44.46 ?  94  PHE B CE2   1 
ATOM   6334  C  CZ    . PHE B 1 94  ? 146.452 130.952 166.686 1.00 41.24 ?  94  PHE B CZ    1 
ATOM   6335  N  N     . MET B 1 95  ? 142.502 133.783 168.572 1.00 38.90 ?  95  MET B N     1 
ATOM   6336  C  CA    . MET B 1 95  ? 141.969 133.932 167.224 1.00 36.29 ?  95  MET B CA    1 
ATOM   6337  C  C     . MET B 1 95  ? 141.823 135.394 166.823 1.00 38.72 ?  95  MET B C     1 
ATOM   6338  O  O     . MET B 1 95  ? 141.970 135.718 165.644 1.00 44.00 ?  95  MET B O     1 
ATOM   6339  C  CB    . MET B 1 95  ? 140.630 133.205 167.103 1.00 39.90 ?  95  MET B CB    1 
ATOM   6340  C  CG    . MET B 1 95  ? 140.008 133.255 165.713 1.00 42.25 ?  95  MET B CG    1 
ATOM   6341  S  SD    . MET B 1 95  ? 140.646 132.054 164.522 1.00 51.03 ?  95  MET B SD    1 
ATOM   6342  C  CE    . MET B 1 95  ? 141.512 130.894 165.578 1.00 43.73 ?  95  MET B CE    1 
ATOM   6343  N  N     . SER B 1 96  ? 141.548 136.287 167.775 1.00 33.31 ?  96  SER B N     1 
ATOM   6344  C  CA    . SER B 1 96  ? 141.461 137.708 167.445 1.00 30.40 ?  96  SER B CA    1 
ATOM   6345  C  C     . SER B 1 96  ? 142.782 138.220 166.880 1.00 32.32 ?  96  SER B C     1 
ATOM   6346  O  O     . SER B 1 96  ? 142.827 138.804 165.787 1.00 34.21 ?  96  SER B O     1 
ATOM   6347  C  CB    . SER B 1 96  ? 141.065 138.503 168.688 1.00 33.47 ?  96  SER B CB    1 
ATOM   6348  O  OG    . SER B 1 96  ? 139.902 137.962 169.289 1.00 38.67 ?  96  SER B OG    1 
ATOM   6349  N  N     . ALA B 1 97  ? 143.873 137.986 167.611 1.00 37.86 ?  97  ALA B N     1 
ATOM   6350  C  CA    . ALA B 1 97  ? 145.187 138.418 167.154 1.00 34.01 ?  97  ALA B CA    1 
ATOM   6351  C  C     . ALA B 1 97  ? 145.592 137.693 165.880 1.00 35.07 ?  97  ALA B C     1 
ATOM   6352  O  O     . ALA B 1 97  ? 146.179 138.297 164.975 1.00 42.03 ?  97  ALA B O     1 
ATOM   6353  C  CB    . ALA B 1 97  ? 146.222 138.190 168.254 1.00 36.35 ?  97  ALA B CB    1 
ATOM   6354  N  N     . PHE B 1 98  ? 145.299 136.394 165.796 1.00 33.42 ?  98  PHE B N     1 
ATOM   6355  C  CA    . PHE B 1 98  ? 145.652 135.634 164.602 1.00 32.89 ?  98  PHE B CA    1 
ATOM   6356  C  C     . PHE B 1 98  ? 144.950 136.195 163.374 1.00 35.95 ?  98  PHE B C     1 
ATOM   6357  O  O     . PHE B 1 98  ? 145.571 136.394 162.324 1.00 43.40 ?  98  PHE B O     1 
ATOM   6358  C  CB    . PHE B 1 98  ? 145.301 134.159 164.801 1.00 37.17 ?  98  PHE B CB    1 
ATOM   6359  C  CG    . PHE B 1 98  ? 145.515 133.316 163.578 1.00 39.18 ?  98  PHE B CG    1 
ATOM   6360  C  CD1   . PHE B 1 98  ? 146.773 132.825 163.273 1.00 39.78 ?  98  PHE B CD1   1 
ATOM   6361  C  CD2   . PHE B 1 98  ? 144.460 133.013 162.734 1.00 41.11 ?  98  PHE B CD2   1 
ATOM   6362  C  CE1   . PHE B 1 98  ? 146.975 132.050 162.151 1.00 37.68 ?  98  PHE B CE1   1 
ATOM   6363  C  CE2   . PHE B 1 98  ? 144.658 132.238 161.607 1.00 43.04 ?  98  PHE B CE2   1 
ATOM   6364  C  CZ    . PHE B 1 98  ? 145.917 131.756 161.316 1.00 40.72 ?  98  PHE B CZ    1 
ATOM   6365  N  N     . LYS B 1 99  ? 143.651 136.474 163.493 1.00 39.14 ?  99  LYS B N     1 
ATOM   6366  C  CA    . LYS B 1 99  ? 142.892 137.006 162.371 1.00 37.77 ?  99  LYS B CA    1 
ATOM   6367  C  C     . LYS B 1 99  ? 143.385 138.389 161.980 1.00 35.59 ?  99  LYS B C     1 
ATOM   6368  O  O     . LYS B 1 99  ? 143.501 138.692 160.787 1.00 41.58 ?  99  LYS B O     1 
ATOM   6369  C  CB    . LYS B 1 99  ? 141.403 137.041 162.713 1.00 36.70 ?  99  LYS B CB    1 
ATOM   6370  C  CG    . LYS B 1 99  ? 140.699 135.708 162.535 1.00 39.01 ?  99  LYS B CG    1 
ATOM   6371  C  CD    . LYS B 1 99  ? 141.048 135.071 161.202 1.00 42.01 ?  99  LYS B CD    1 
ATOM   6372  C  CE    . LYS B 1 99  ? 139.893 134.245 160.667 1.00 40.21 ?  99  LYS B CE    1 
ATOM   6373  N  NZ    . LYS B 1 99  ? 139.747 134.396 159.193 1.00 42.41 1  99  LYS B NZ    1 
ATOM   6374  N  N     . PHE B 1 100 ? 143.690 139.243 162.962 1.00 32.10 ?  100 PHE B N     1 
ATOM   6375  C  CA    . PHE B 1 100 ? 144.210 140.561 162.616 1.00 35.03 ?  100 PHE B CA    1 
ATOM   6376  C  C     . PHE B 1 100 ? 145.547 140.458 161.893 1.00 35.92 ?  100 PHE B C     1 
ATOM   6377  O  O     . PHE B 1 100 ? 145.745 141.073 160.839 1.00 41.09 ?  100 PHE B O     1 
ATOM   6378  C  CB    . PHE B 1 100 ? 144.364 141.442 163.849 1.00 33.33 ?  100 PHE B CB    1 
ATOM   6379  C  CG    . PHE B 1 100 ? 145.073 142.728 163.553 1.00 35.46 ?  100 PHE B CG    1 
ATOM   6380  C  CD1   . PHE B 1 100 ? 144.455 143.710 162.798 1.00 34.60 ?  100 PHE B CD1   1 
ATOM   6381  C  CD2   . PHE B 1 100 ? 146.376 142.929 163.968 1.00 34.53 ?  100 PHE B CD2   1 
ATOM   6382  C  CE1   . PHE B 1 100 ? 145.108 144.885 162.498 1.00 34.60 ?  100 PHE B CE1   1 
ATOM   6383  C  CE2   . PHE B 1 100 ? 147.035 144.100 163.666 1.00 35.28 ?  100 PHE B CE2   1 
ATOM   6384  C  CZ    . PHE B 1 100 ? 146.400 145.081 162.931 1.00 34.72 ?  100 PHE B CZ    1 
ATOM   6385  N  N     . TYR B 1 101 ? 146.480 139.682 162.443 1.00 36.51 ?  101 TYR B N     1 
ATOM   6386  C  CA    . TYR B 1 101 ? 147.827 139.635 161.893 1.00 35.32 ?  101 TYR B CA    1 
ATOM   6387  C  C     . TYR B 1 101 ? 147.935 138.761 160.653 1.00 37.20 ?  101 TYR B C     1 
ATOM   6388  O  O     . TYR B 1 101 ? 148.983 138.773 160.000 1.00 45.47 ?  101 TYR B O     1 
ATOM   6389  C  CB    . TYR B 1 101 ? 148.812 139.164 162.965 1.00 38.28 ?  101 TYR B CB    1 
ATOM   6390  C  CG    . TYR B 1 101 ? 149.093 140.224 164.007 1.00 37.54 ?  101 TYR B CG    1 
ATOM   6391  C  CD1   . TYR B 1 101 ? 149.846 141.347 163.695 1.00 36.80 ?  101 TYR B CD1   1 
ATOM   6392  C  CD2   . TYR B 1 101 ? 148.590 140.112 165.295 1.00 36.97 ?  101 TYR B CD2   1 
ATOM   6393  C  CE1   . TYR B 1 101 ? 150.097 142.324 164.638 1.00 36.63 ?  101 TYR B CE1   1 
ATOM   6394  C  CE2   . TYR B 1 101 ? 148.836 141.083 166.245 1.00 38.05 ?  101 TYR B CE2   1 
ATOM   6395  C  CZ    . TYR B 1 101 ? 149.590 142.187 165.911 1.00 39.59 ?  101 TYR B CZ    1 
ATOM   6396  O  OH    . TYR B 1 101 ? 149.837 143.156 166.854 1.00 42.17 ?  101 TYR B OH    1 
ATOM   6397  N  N     . ASN B 1 102 ? 146.888 138.013 160.310 1.00 40.40 ?  102 ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 102 ? 146.875 137.254 159.069 1.00 41.86 ?  102 ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 102 ? 146.062 137.915 157.966 1.00 43.32 ?  102 ASN B C     1 
ATOM   6400  O  O     . ASN B 1 102 ? 146.377 137.730 156.787 1.00 47.54 ?  102 ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 102 ? 146.327 135.846 159.318 1.00 40.01 ?  102 ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 102 ? 147.348 134.929 159.959 1.00 43.14 ?  102 ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 102 ? 147.938 135.260 160.987 1.00 45.88 ?  102 ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 102 ? 147.564 133.768 159.353 1.00 43.81 ?  102 ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 103 ? 145.027 138.684 158.314 1.00 38.59 ?  103 ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 103 ? 144.147 139.280 157.320 1.00 40.61 ?  103 ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 103 ? 144.248 140.794 157.222 1.00 40.98 ?  103 ASP B C     1 
ATOM   6408  O  O     . ASP B 1 103 ? 143.966 141.343 156.156 1.00 46.47 ?  103 ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 103 ? 142.684 138.915 157.611 1.00 42.23 ?  103 ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 103 ? 142.490 137.436 157.883 1.00 45.37 ?  103 ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 103 ? 143.382 136.635 157.532 1.00 44.78 ?  103 ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 103 ? 141.437 137.073 158.449 1.00 47.06 -1 103 ASP B OD2   1 
ATOM   6413  N  N     . TYR B 1 104 ? 144.636 141.486 158.294 1.00 31.95 ?  104 TYR B N     1 
ATOM   6414  C  CA    . TYR B 1 104 ? 144.563 142.942 158.315 1.00 35.66 ?  104 TYR B CA    1 
ATOM   6415  C  C     . TYR B 1 104 ? 145.869 143.647 158.644 1.00 38.78 ?  104 TYR B C     1 
ATOM   6416  O  O     . TYR B 1 104 ? 146.033 144.803 158.235 1.00 43.88 ?  104 TYR B O     1 
ATOM   6417  C  CB    . TYR B 1 104 ? 143.485 143.410 159.305 1.00 37.44 ?  104 TYR B CB    1 
ATOM   6418  C  CG    . TYR B 1 104 ? 142.139 142.772 159.057 1.00 36.15 ?  104 TYR B CG    1 
ATOM   6419  C  CD1   . TYR B 1 104 ? 141.235 143.339 158.167 1.00 34.65 ?  104 TYR B CD1   1 
ATOM   6420  C  CD2   . TYR B 1 104 ? 141.768 141.605 159.712 1.00 33.99 ?  104 TYR B CD2   1 
ATOM   6421  C  CE1   . TYR B 1 104 ? 140.006 142.756 157.930 1.00 36.14 ?  104 TYR B CE1   1 
ATOM   6422  C  CE2   . TYR B 1 104 ? 140.540 141.017 159.483 1.00 37.33 ?  104 TYR B CE2   1 
ATOM   6423  C  CZ    . TYR B 1 104 ? 139.664 141.596 158.590 1.00 38.90 ?  104 TYR B CZ    1 
ATOM   6424  O  OH    . TYR B 1 104 ? 138.438 141.014 158.362 1.00 38.34 ?  104 TYR B OH    1 
ATOM   6425  N  N     . ALA B 1 105 ? 146.793 143.018 159.364 1.00 40.73 ?  105 ALA B N     1 
ATOM   6426  C  CA    . ALA B 1 105 ? 148.070 143.658 159.644 1.00 40.00 ?  105 ALA B CA    1 
ATOM   6427  C  C     . ALA B 1 105 ? 148.899 143.766 158.371 1.00 43.61 ?  105 ALA B C     1 
ATOM   6428  O  O     . ALA B 1 105 ? 148.960 142.830 157.568 1.00 40.70 ?  105 ALA B O     1 
ATOM   6429  C  CB    . ALA B 1 105 ? 148.840 142.882 160.707 1.00 37.04 ?  105 ALA B CB    1 
ATOM   6430  N  N     . LEU B 1 106 ? 149.536 144.918 158.187 1.00 46.91 ?  106 LEU B N     1 
ATOM   6431  C  CA    . LEU B 1 106 ? 150.351 145.139 157.001 1.00 44.23 ?  106 LEU B CA    1 
ATOM   6432  C  C     . LEU B 1 106 ? 151.646 144.343 157.097 1.00 47.83 ?  106 LEU B C     1 
ATOM   6433  O  O     . LEU B 1 106 ? 152.352 144.400 158.108 1.00 46.99 ?  106 LEU B O     1 
ATOM   6434  C  CB    . LEU B 1 106 ? 150.653 146.626 156.831 1.00 46.87 ?  106 LEU B CB    1 
ATOM   6435  C  CG    . LEU B 1 106 ? 151.570 147.007 155.669 1.00 45.27 ?  106 LEU B CG    1 
ATOM   6436  C  CD1   . LEU B 1 106 ? 150.860 146.809 154.340 1.00 45.59 ?  106 LEU B CD1   1 
ATOM   6437  C  CD2   . LEU B 1 106 ? 152.049 148.442 155.815 1.00 46.37 ?  106 LEU B CD2   1 
ATOM   6438  N  N     . LYS B 1 107 ? 151.954 143.600 156.040 1.00 53.13 ?  107 LYS B N     1 
ATOM   6439  C  CA    . LYS B 1 107 ? 153.171 142.813 155.945 1.00 52.70 ?  107 LYS B CA    1 
ATOM   6440  C  C     . LYS B 1 107 ? 154.045 143.360 154.826 1.00 55.30 ?  107 LYS B C     1 
ATOM   6441  O  O     . LYS B 1 107 ? 153.643 144.241 154.061 1.00 56.79 ?  107 LYS B O     1 
ATOM   6442  C  CB    . LYS B 1 107 ? 152.857 141.331 155.702 1.00 52.84 ?  107 LYS B CB    1 
ATOM   6443  C  CG    . LYS B 1 107 ? 152.187 140.633 156.874 1.00 51.33 ?  107 LYS B CG    1 
ATOM   6444  C  CD    . LYS B 1 107 ? 151.831 139.198 156.521 1.00 54.71 ?  107 LYS B CD    1 
ATOM   6445  C  CE    . LYS B 1 107 ? 151.195 138.481 157.698 1.00 55.56 ?  107 LYS B CE    1 
ATOM   6446  N  NZ    . LYS B 1 107 ? 150.607 137.170 157.301 1.00 52.71 1  107 LYS B NZ    1 
ATOM   6447  N  N     . THR B 1 108 ? 155.259 142.822 154.735 1.00 59.23 ?  108 THR B N     1 
ATOM   6448  C  CA    . THR B 1 108 ? 156.194 143.241 153.703 1.00 59.39 ?  108 THR B CA    1 
ATOM   6449  C  C     . THR B 1 108 ? 155.736 142.728 152.339 1.00 61.88 ?  108 THR B C     1 
ATOM   6450  O  O     . THR B 1 108 ? 154.725 142.032 152.207 1.00 61.58 ?  108 THR B O     1 
ATOM   6451  C  CB    . THR B 1 108 ? 157.600 142.746 154.031 1.00 60.99 ?  108 THR B CB    1 
ATOM   6452  O  OG1   . THR B 1 108 ? 157.536 141.397 154.507 1.00 65.24 ?  108 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 1 108 ? 158.235 143.622 155.100 1.00 58.11 ?  108 THR B CG2   1 
ATOM   6454  N  N     . ASN B 1 109 ? 156.495 143.089 151.301 1.00 63.97 ?  109 ASN B N     1 
ATOM   6455  C  CA    . ASN B 1 109 ? 156.158 142.653 149.949 1.00 61.95 ?  109 ASN B CA    1 
ATOM   6456  C  C     . ASN B 1 109 ? 156.203 141.135 149.830 1.00 64.82 ?  109 ASN B C     1 
ATOM   6457  O  O     . ASN B 1 109 ? 155.339 140.529 149.186 1.00 64.81 ?  109 ASN B O     1 
ATOM   6458  C  CB    . ASN B 1 109 ? 157.105 143.299 148.937 1.00 63.18 ?  109 ASN B CB    1 
ATOM   6459  C  CG    . ASN B 1 109 ? 157.045 144.811 148.967 1.00 63.25 ?  109 ASN B CG    1 
ATOM   6460  O  OD1   . ASN B 1 109 ? 156.170 145.396 149.604 1.00 61.63 ?  109 ASN B OD1   1 
ATOM   6461  N  ND2   . ASN B 1 109 ? 157.977 145.455 148.275 1.00 64.76 ?  109 ASN B ND2   1 
ATOM   6462  N  N     . ASP B 1 110 ? 157.203 140.504 150.443 1.00 66.37 ?  110 ASP B N     1 
ATOM   6463  C  CA    . ASP B 1 110 ? 157.312 139.051 150.445 1.00 66.12 ?  110 ASP B CA    1 
ATOM   6464  C  C     . ASP B 1 110 ? 156.499 138.398 151.555 1.00 66.70 ?  110 ASP B C     1 
ATOM   6465  O  O     . ASP B 1 110 ? 156.498 137.166 151.653 1.00 67.58 ?  110 ASP B O     1 
ATOM   6466  C  CB    . ASP B 1 110 ? 158.782 138.638 150.562 1.00 66.14 ?  110 ASP B CB    1 
ATOM   6467  C  CG    . ASP B 1 110 ? 159.481 139.294 151.734 1.00 67.51 ?  110 ASP B CG    1 
ATOM   6468  O  OD1   . ASP B 1 110 ? 158.898 140.219 152.336 1.00 67.34 ?  110 ASP B OD1   1 
ATOM   6469  O  OD2   . ASP B 1 110 ? 160.619 138.890 152.048 1.00 67.65 -1 110 ASP B OD2   1 
ATOM   6470  N  N     . LYS B 1 111 ? 155.814 139.193 152.382 1.00 62.24 ?  111 LYS B N     1 
ATOM   6471  C  CA    . LYS B 1 111 ? 154.960 138.686 153.459 1.00 63.06 ?  111 LYS B CA    1 
ATOM   6472  C  C     . LYS B 1 111 ? 155.736 137.785 154.417 1.00 64.05 ?  111 LYS B C     1 
ATOM   6473  O  O     . LYS B 1 111 ? 155.236 136.754 154.871 1.00 65.21 ?  111 LYS B O     1 
ATOM   6474  C  CB    . LYS B 1 111 ? 153.734 137.957 152.901 1.00 63.14 ?  111 LYS B CB    1 
ATOM   6475  C  CG    . LYS B 1 111 ? 153.096 138.633 151.696 1.00 63.13 ?  111 LYS B CG    1 
ATOM   6476  C  CD    . LYS B 1 111 ? 152.077 139.677 152.121 1.00 64.53 ?  111 LYS B CD    1 
ATOM   6477  C  CE    . LYS B 1 111 ? 151.916 140.755 151.063 1.00 64.19 ?  111 LYS B CE    1 
ATOM   6478  N  NZ    . LYS B 1 111 ? 152.023 140.200 149.686 1.00 63.59 1  111 LYS B NZ    1 
ATOM   6479  N  N     . LYS B 1 112 ? 156.971 138.177 154.729 1.00 64.60 ?  112 LYS B N     1 
ATOM   6480  C  CA    . LYS B 1 112 ? 157.787 137.441 155.685 1.00 64.95 ?  112 LYS B CA    1 
ATOM   6481  C  C     . LYS B 1 112 ? 157.835 138.094 157.058 1.00 64.12 ?  112 LYS B C     1 
ATOM   6482  O  O     . LYS B 1 112 ? 158.218 137.430 158.028 1.00 64.02 ?  112 LYS B O     1 
ATOM   6483  C  CB    . LYS B 1 112 ? 159.220 137.287 155.159 1.00 64.38 ?  112 LYS B CB    1 
ATOM   6484  C  CG    . LYS B 1 112 ? 160.086 138.520 155.354 1.00 65.17 ?  112 LYS B CG    1 
ATOM   6485  C  CD    . LYS B 1 112 ? 161.543 138.234 155.030 1.00 66.05 ?  112 LYS B CD    1 
ATOM   6486  C  CE    . LYS B 1 112 ? 162.389 139.491 155.152 1.00 64.52 ?  112 LYS B CE    1 
ATOM   6487  N  NZ    . LYS B 1 112 ? 161.651 140.702 154.698 1.00 64.63 1  112 LYS B NZ    1 
ATOM   6488  N  N     . LYS B 1 113 ? 157.457 139.365 157.166 1.00 59.57 ?  113 LYS B N     1 
ATOM   6489  C  CA    . LYS B 1 113 ? 157.530 140.093 158.423 1.00 59.62 ?  113 LYS B CA    1 
ATOM   6490  C  C     . LYS B 1 113 ? 156.282 140.947 158.579 1.00 57.88 ?  113 LYS B C     1 
ATOM   6491  O  O     . LYS B 1 113 ? 155.555 141.205 157.617 1.00 60.09 ?  113 LYS B O     1 
ATOM   6492  C  CB    . LYS B 1 113 ? 158.788 140.969 158.494 1.00 60.10 ?  113 LYS B CB    1 
ATOM   6493  C  CG    . LYS B 1 113 ? 160.085 140.191 158.662 1.00 58.77 ?  113 LYS B CG    1 
ATOM   6494  C  CD    . LYS B 1 113 ? 160.133 139.477 160.001 1.00 60.69 ?  113 LYS B CD    1 
ATOM   6495  C  CE    . LYS B 1 113 ? 161.436 138.719 160.177 1.00 61.41 ?  113 LYS B CE    1 
ATOM   6496  N  NZ    . LYS B 1 113 ? 161.412 137.850 161.385 1.00 60.18 1  113 LYS B NZ    1 
ATOM   6497  N  N     . ILE B 1 114 ? 156.041 141.385 159.812 1.00 52.57 ?  114 ILE B N     1 
ATOM   6498  C  CA    . ILE B 1 114 ? 154.871 142.183 160.157 1.00 52.15 ?  114 ILE B CA    1 
ATOM   6499  C  C     . ILE B 1 114 ? 155.320 143.625 160.343 1.00 53.20 ?  114 ILE B C     1 
ATOM   6500  O  O     . ILE B 1 114 ? 156.161 143.916 161.204 1.00 54.37 ?  114 ILE B O     1 
ATOM   6501  C  CB    . ILE B 1 114 ? 154.179 141.654 161.423 1.00 53.28 ?  114 ILE B CB    1 
ATOM   6502  C  CG1   . ILE B 1 114 ? 153.459 140.338 161.125 1.00 49.72 ?  114 ILE B CG1   1 
ATOM   6503  C  CG2   . ILE B 1 114 ? 153.206 142.684 161.969 1.00 51.69 ?  114 ILE B CG2   1 
ATOM   6504  C  CD1   . ILE B 1 114 ? 153.066 139.571 162.363 1.00 50.40 ?  114 ILE B CD1   1 
ATOM   6505  N  N     . LEU B 1 115 ? 154.762 144.526 159.538 1.00 49.76 ?  115 LEU B N     1 
ATOM   6506  C  CA    . LEU B 1 115 ? 155.091 145.941 159.642 1.00 48.02 ?  115 LEU B CA    1 
ATOM   6507  C  C     . LEU B 1 115 ? 154.113 146.714 160.511 1.00 49.77 ?  115 LEU B C     1 
ATOM   6508  O  O     . LEU B 1 115 ? 154.489 147.741 161.087 1.00 50.66 ?  115 LEU B O     1 
ATOM   6509  C  CB    . LEU B 1 115 ? 155.140 146.578 158.250 1.00 48.78 ?  115 LEU B CB    1 
ATOM   6510  C  CG    . LEU B 1 115 ? 156.364 146.254 157.394 1.00 48.87 ?  115 LEU B CG    1 
ATOM   6511  C  CD1   . LEU B 1 115 ? 156.092 146.590 155.939 1.00 48.97 ?  115 LEU B CD1   1 
ATOM   6512  C  CD2   . LEU B 1 115 ? 157.583 147.005 157.904 1.00 49.55 ?  115 LEU B CD2   1 
ATOM   6513  N  N     . GLU B 1 116 ? 152.871 146.250 160.625 1.00 49.06 ?  116 GLU B N     1 
ATOM   6514  C  CA    . GLU B 1 116 ? 151.827 146.968 161.342 1.00 45.44 ?  116 GLU B CA    1 
ATOM   6515  C  C     . GLU B 1 116 ? 151.360 146.161 162.543 1.00 45.77 ?  116 GLU B C     1 
ATOM   6516  O  O     . GLU B 1 116 ? 150.984 144.993 162.404 1.00 48.91 ?  116 GLU B O     1 
ATOM   6517  C  CB    . GLU B 1 116 ? 150.634 147.261 160.428 1.00 44.67 ?  116 GLU B CB    1 
ATOM   6518  C  CG    . GLU B 1 116 ? 150.559 148.690 159.939 1.00 44.82 ?  116 GLU B CG    1 
ATOM   6519  C  CD    . GLU B 1 116 ? 149.319 148.950 159.110 1.00 45.82 ?  116 GLU B CD    1 
ATOM   6520  O  OE1   . GLU B 1 116 ? 148.549 147.996 158.875 1.00 44.53 ?  116 GLU B OE1   1 
ATOM   6521  O  OE2   . GLU B 1 116 ? 149.112 150.108 158.691 1.00 47.68 -1 116 GLU B OE2   1 
ATOM   6522  N  N     . ARG B 1 117 ? 151.377 146.791 163.713 1.00 40.37 ?  117 ARG B N     1 
ATOM   6523  C  CA    . ARG B 1 117 ? 150.703 146.245 164.878 1.00 41.84 ?  117 ARG B CA    1 
ATOM   6524  C  C     . ARG B 1 117 ? 149.234 146.659 164.848 1.00 42.11 ?  117 ARG B C     1 
ATOM   6525  O  O     . ARG B 1 117 ? 148.782 147.371 163.947 1.00 44.85 ?  117 ARG B O     1 
ATOM   6526  C  CB    . ARG B 1 117 ? 151.390 146.714 166.159 1.00 43.52 ?  117 ARG B CB    1 
ATOM   6527  C  CG    . ARG B 1 117 ? 152.777 146.133 166.371 1.00 43.24 ?  117 ARG B CG    1 
ATOM   6528  C  CD    . ARG B 1 117 ? 152.770 144.620 166.233 1.00 45.76 ?  117 ARG B CD    1 
ATOM   6529  N  NE    . ARG B 1 117 ? 153.683 143.978 167.171 1.00 45.69 ?  117 ARG B NE    1 
ATOM   6530  C  CZ    . ARG B 1 117 ? 153.431 143.796 168.460 1.00 45.62 ?  117 ARG B CZ    1 
ATOM   6531  N  NH1   . ARG B 1 117 ? 152.294 144.195 169.006 1.00 44.83 1  117 ARG B NH1   1 
ATOM   6532  N  NH2   . ARG B 1 117 ? 154.343 143.197 169.221 1.00 48.06 ?  117 ARG B NH2   1 
ATOM   6533  N  N     . TYR B 1 118 ? 148.466 146.201 165.838 1.00 39.73 ?  118 TYR B N     1 
ATOM   6534  C  CA    . TYR B 1 118 ? 147.077 146.638 165.937 1.00 36.21 ?  118 TYR B CA    1 
ATOM   6535  C  C     . TYR B 1 118 ? 146.998 148.135 166.194 1.00 37.83 ?  118 TYR B C     1 
ATOM   6536  O  O     . TYR B 1 118 ? 146.182 148.839 165.585 1.00 41.14 ?  118 TYR B O     1 
ATOM   6537  C  CB    . TYR B 1 118 ? 146.354 145.860 167.033 1.00 34.13 ?  118 TYR B CB    1 
ATOM   6538  C  CG    . TYR B 1 118 ? 144.853 146.035 167.011 1.00 35.58 ?  118 TYR B CG    1 
ATOM   6539  C  CD1   . TYR B 1 118 ? 144.125 145.802 165.852 1.00 34.33 ?  118 TYR B CD1   1 
ATOM   6540  C  CD2   . TYR B 1 118 ? 144.165 146.437 168.145 1.00 35.30 ?  118 TYR B CD2   1 
ATOM   6541  C  CE1   . TYR B 1 118 ? 142.755 145.961 165.827 1.00 34.36 ?  118 TYR B CE1   1 
ATOM   6542  C  CE2   . TYR B 1 118 ? 142.796 146.596 168.132 1.00 30.65 ?  118 TYR B CE2   1 
ATOM   6543  C  CZ    . TYR B 1 118 ? 142.096 146.358 166.969 1.00 36.75 ?  118 TYR B CZ    1 
ATOM   6544  O  OH    . TYR B 1 118 ? 140.729 146.520 166.950 1.00 40.55 ?  118 TYR B OH    1 
ATOM   6545  N  N     . GLU B 1 119 ? 147.854 148.642 167.082 1.00 39.86 ?  119 GLU B N     1 
ATOM   6546  C  CA    . GLU B 1 119 ? 147.876 150.071 167.358 1.00 39.18 ?  119 GLU B CA    1 
ATOM   6547  C  C     . GLU B 1 119 ? 148.330 150.864 166.139 1.00 38.98 ?  119 GLU B C     1 
ATOM   6548  O  O     . GLU B 1 119 ? 147.806 151.949 165.876 1.00 43.90 ?  119 GLU B O     1 
ATOM   6549  C  CB    . GLU B 1 119 ? 148.776 150.359 168.558 1.00 36.58 ?  119 GLU B CB    1 
ATOM   6550  C  CG    . GLU B 1 119 ? 148.154 150.003 169.896 1.00 36.87 ?  119 GLU B CG    1 
ATOM   6551  C  CD    . GLU B 1 119 ? 148.607 148.654 170.410 1.00 44.14 ?  119 GLU B CD    1 
ATOM   6552  O  OE1   . GLU B 1 119 ? 148.924 147.774 169.580 1.00 43.47 ?  119 GLU B OE1   1 
ATOM   6553  O  OE2   . GLU B 1 119 ? 148.646 148.470 171.645 1.00 45.63 -1 119 GLU B OE2   1 
ATOM   6554  N  N     . ASP B 1 120 ? 149.297 150.342 165.381 1.00 40.51 ?  120 ASP B N     1 
ATOM   6555  C  CA    . ASP B 1 120 ? 149.748 151.035 164.177 1.00 37.36 ?  120 ASP B CA    1 
ATOM   6556  C  C     . ASP B 1 120 ? 148.632 151.125 163.144 1.00 35.98 ?  120 ASP B C     1 
ATOM   6557  O  O     . ASP B 1 120 ? 148.400 152.185 162.549 1.00 39.04 ?  120 ASP B O     1 
ATOM   6558  C  CB    . ASP B 1 120 ? 150.965 150.322 163.584 1.00 41.42 ?  120 ASP B CB    1 
ATOM   6559  C  CG    . ASP B 1 120 ? 152.099 150.183 164.575 1.00 45.25 ?  120 ASP B CG    1 
ATOM   6560  O  OD1   . ASP B 1 120 ? 152.224 151.052 165.461 1.00 45.23 ?  120 ASP B OD1   1 
ATOM   6561  O  OD2   . ASP B 1 120 ? 152.866 149.205 164.467 1.00 48.28 -1 120 ASP B OD2   1 
ATOM   6562  N  N     . ARG B 1 121 ? 147.930 150.013 162.917 1.00 33.62 ?  121 ARG B N     1 
ATOM   6563  C  CA    . ARG B 1 121 ? 146.821 150.011 161.970 1.00 33.76 ?  121 ARG B CA    1 
ATOM   6564  C  C     . ARG B 1 121 ? 145.719 150.963 162.414 1.00 36.24 ?  121 ARG B C     1 
ATOM   6565  O  O     . ARG B 1 121 ? 145.178 151.723 161.602 1.00 37.10 ?  121 ARG B O     1 
ATOM   6566  C  CB    . ARG B 1 121 ? 146.281 148.590 161.810 1.00 32.18 ?  121 ARG B CB    1 
ATOM   6567  C  CG    . ARG B 1 121 ? 145.020 148.475 160.974 1.00 30.15 ?  121 ARG B CG    1 
ATOM   6568  C  CD    . ARG B 1 121 ? 145.341 148.376 159.496 1.00 30.70 ?  121 ARG B CD    1 
ATOM   6569  N  NE    . ARG B 1 121 ? 144.939 149.577 158.778 1.00 37.96 ?  121 ARG B NE    1 
ATOM   6570  C  CZ    . ARG B 1 121 ? 145.634 150.133 157.796 1.00 34.88 ?  121 ARG B CZ    1 
ATOM   6571  N  NH1   . ARG B 1 121 ? 146.778 149.616 157.380 1.00 37.95 1  121 ARG B NH1   1 
ATOM   6572  N  NH2   . ARG B 1 121 ? 145.171 151.236 157.218 1.00 31.85 ?  121 ARG B NH2   1 
ATOM   6573  N  N     . ILE B 1 122 ? 145.386 150.945 163.707 1.00 33.71 ?  122 ILE B N     1 
ATOM   6574  C  CA    . ILE B 1 122 ? 144.339 151.823 164.215 1.00 26.54 ?  122 ILE B CA    1 
ATOM   6575  C  C     . ILE B 1 122 ? 144.752 153.284 164.087 1.00 30.87 ?  122 ILE B C     1 
ATOM   6576  O  O     . ILE B 1 122 ? 143.940 154.138 163.721 1.00 37.19 ?  122 ILE B O     1 
ATOM   6577  C  CB    . ILE B 1 122 ? 143.990 151.446 165.665 1.00 33.72 ?  122 ILE B CB    1 
ATOM   6578  C  CG1   . ILE B 1 122 ? 143.068 150.227 165.673 1.00 29.67 ?  122 ILE B CG1   1 
ATOM   6579  C  CG2   . ILE B 1 122 ? 143.342 152.616 166.394 1.00 31.03 ?  122 ILE B CG2   1 
ATOM   6580  C  CD1   . ILE B 1 122 ? 142.523 149.891 167.027 1.00 29.81 ?  122 ILE B CD1   1 
ATOM   6581  N  N     . SER B 1 123 ? 146.018 153.595 164.377 1.00 35.20 ?  123 SER B N     1 
ATOM   6582  C  CA    . SER B 1 123 ? 146.498 154.966 164.242 1.00 30.91 ?  123 SER B CA    1 
ATOM   6583  C  C     . SER B 1 123 ? 146.440 155.432 162.795 1.00 30.80 ?  123 SER B C     1 
ATOM   6584  O  O     . SER B 1 123 ? 146.043 156.567 162.518 1.00 39.32 ?  123 SER B O     1 
ATOM   6585  C  CB    . SER B 1 123 ? 147.925 155.081 164.774 1.00 32.46 ?  123 SER B CB    1 
ATOM   6586  O  OG    . SER B 1 123 ? 148.045 154.490 166.051 1.00 36.41 ?  123 SER B OG    1 
ATOM   6587  N  N     . ILE B 1 124 ? 146.842 154.571 161.857 1.00 30.84 ?  124 ILE B N     1 
ATOM   6588  C  CA    . ILE B 1 124 ? 146.810 154.953 160.448 1.00 31.07 ?  124 ILE B CA    1 
ATOM   6589  C  C     . ILE B 1 124 ? 145.375 155.182 159.991 1.00 34.58 ?  124 ILE B C     1 
ATOM   6590  O  O     . ILE B 1 124 ? 145.078 156.162 159.291 1.00 36.70 ?  124 ILE B O     1 
ATOM   6591  C  CB    . ILE B 1 124 ? 147.524 153.891 159.592 1.00 37.99 ?  124 ILE B CB    1 
ATOM   6592  C  CG1   . ILE B 1 124 ? 149.034 153.963 159.827 1.00 37.08 ?  124 ILE B CG1   1 
ATOM   6593  C  CG2   . ILE B 1 124 ? 147.201 154.077 158.119 1.00 34.09 ?  124 ILE B CG2   1 
ATOM   6594  C  CD1   . ILE B 1 124 ? 149.595 155.368 159.765 1.00 34.28 ?  124 ILE B CD1   1 
ATOM   6595  N  N     . VAL B 1 125 ? 144.459 154.297 160.390 1.00 33.80 ?  125 VAL B N     1 
ATOM   6596  C  CA    . VAL B 1 125 ? 143.059 154.456 160.007 1.00 27.57 ?  125 VAL B CA    1 
ATOM   6597  C  C     . VAL B 1 125 ? 142.480 155.730 160.613 1.00 24.37 ?  125 VAL B C     1 
ATOM   6598  O  O     . VAL B 1 125 ? 141.725 156.458 159.957 1.00 35.89 ?  125 VAL B O     1 
ATOM   6599  C  CB    . VAL B 1 125 ? 142.249 153.209 160.412 1.00 31.00 ?  125 VAL B CB    1 
ATOM   6600  C  CG1   . VAL B 1 125 ? 140.771 153.435 160.180 1.00 31.11 ?  125 VAL B CG1   1 
ATOM   6601  C  CG2   . VAL B 1 125 ? 142.719 152.000 159.623 1.00 28.16 ?  125 VAL B CG2   1 
ATOM   6602  N  N     . ALA B 1 126 ? 142.830 156.027 161.867 1.00 23.02 ?  126 ALA B N     1 
ATOM   6603  C  CA    . ALA B 1 126 ? 142.336 157.237 162.516 1.00 25.33 ?  126 ALA B CA    1 
ATOM   6604  C  C     . ALA B 1 126 ? 142.879 158.493 161.848 1.00 30.57 ?  126 ALA B C     1 
ATOM   6605  O  O     . ALA B 1 126 ? 142.147 159.475 161.674 1.00 35.12 ?  126 ALA B O     1 
ATOM   6606  C  CB    . ALA B 1 126 ? 142.710 157.220 163.995 1.00 31.54 ?  126 ALA B CB    1 
ATOM   6607  N  N     . LEU B 1 127 ? 144.162 158.487 161.484 1.00 33.87 ?  127 LEU B N     1 
ATOM   6608  C  CA    . LEU B 1 127 ? 144.745 159.638 160.806 1.00 29.95 ?  127 LEU B CA    1 
ATOM   6609  C  C     . LEU B 1 127 ? 144.118 159.840 159.436 1.00 30.74 ?  127 LEU B C     1 
ATOM   6610  O  O     . LEU B 1 127 ? 143.916 160.980 159.001 1.00 36.71 ?  127 LEU B O     1 
ATOM   6611  C  CB    . LEU B 1 127 ? 146.259 159.466 160.689 1.00 33.31 ?  127 LEU B CB    1 
ATOM   6612  C  CG    . LEU B 1 127 ? 147.058 159.606 161.986 1.00 32.21 ?  127 LEU B CG    1 
ATOM   6613  C  CD1   . LEU B 1 127 ? 148.434 158.989 161.829 1.00 36.25 ?  127 LEU B CD1   1 
ATOM   6614  C  CD2   . LEU B 1 127 ? 147.164 161.062 162.402 1.00 33.87 ?  127 LEU B CD2   1 
ATOM   6615  N  N     . PHE B 1 128 ? 143.811 158.746 158.734 1.00 29.85 ?  128 PHE B N     1 
ATOM   6616  C  CA    . PHE B 1 128 ? 143.091 158.870 157.470 1.00 29.40 ?  128 PHE B CA    1 
ATOM   6617  C  C     . PHE B 1 128 ? 141.690 159.430 157.689 1.00 28.36 ?  128 PHE B C     1 
ATOM   6618  O  O     . PHE B 1 128 ? 141.220 160.270 156.913 1.00 33.31 ?  128 PHE B O     1 
ATOM   6619  C  CB    . PHE B 1 128 ? 143.023 157.513 156.768 1.00 28.61 ?  128 PHE B CB    1 
ATOM   6620  C  CG    . PHE B 1 128 ? 141.971 157.442 155.700 1.00 33.12 ?  128 PHE B CG    1 
ATOM   6621  C  CD1   . PHE B 1 128 ? 142.187 158.018 154.461 1.00 31.02 ?  128 PHE B CD1   1 
ATOM   6622  C  CD2   . PHE B 1 128 ? 140.763 156.808 155.938 1.00 32.42 ?  128 PHE B CD2   1 
ATOM   6623  C  CE1   . PHE B 1 128 ? 141.223 157.960 153.477 1.00 31.53 ?  128 PHE B CE1   1 
ATOM   6624  C  CE2   . PHE B 1 128 ? 139.794 156.751 154.960 1.00 31.93 ?  128 PHE B CE2   1 
ATOM   6625  C  CZ    . PHE B 1 128 ? 140.025 157.328 153.726 1.00 31.58 ?  128 PHE B CZ    1 
ATOM   6626  N  N     . PHE B 1 129 ? 141.007 158.968 158.738 1.00 29.04 ?  129 PHE B N     1 
ATOM   6627  C  CA    . PHE B 1 129 ? 139.649 159.430 159.014 1.00 26.13 ?  129 PHE B CA    1 
ATOM   6628  C  C     . PHE B 1 129 ? 139.617 160.917 159.341 1.00 28.48 ?  129 PHE B C     1 
ATOM   6629  O  O     . PHE B 1 129 ? 138.740 161.647 158.865 1.00 32.18 ?  129 PHE B O     1 
ATOM   6630  C  CB    . PHE B 1 129 ? 139.050 158.633 160.172 1.00 28.98 ?  129 PHE B CB    1 
ATOM   6631  C  CG    . PHE B 1 129 ? 138.533 157.281 159.785 1.00 26.86 ?  129 PHE B CG    1 
ATOM   6632  C  CD1   . PHE B 1 129 ? 138.355 156.943 158.456 1.00 25.66 ?  129 PHE B CD1   1 
ATOM   6633  C  CD2   . PHE B 1 129 ? 138.210 156.352 160.757 1.00 25.26 ?  129 PHE B CD2   1 
ATOM   6634  C  CE1   . PHE B 1 129 ? 137.874 155.699 158.106 1.00 26.72 ?  129 PHE B CE1   1 
ATOM   6635  C  CE2   . PHE B 1 129 ? 137.726 155.108 160.413 1.00 28.32 ?  129 PHE B CE2   1 
ATOM   6636  C  CZ    . PHE B 1 129 ? 137.558 154.780 159.085 1.00 30.23 ?  129 PHE B CZ    1 
ATOM   6637  N  N     . ALA B 1 130 ? 140.562 161.383 160.159 1.00 33.69 ?  130 ALA B N     1 
ATOM   6638  C  CA    . ALA B 1 130 ? 140.488 162.745 160.678 1.00 35.78 ?  130 ALA B CA    1 
ATOM   6639  C  C     . ALA B 1 130 ? 140.745 163.788 159.598 1.00 40.17 ?  130 ALA B C     1 
ATOM   6640  O  O     . ALA B 1 130 ? 140.223 164.905 159.688 1.00 46.69 ?  130 ALA B O     1 
ATOM   6641  C  CB    . ALA B 1 130 ? 141.474 162.919 161.827 1.00 33.05 ?  130 ALA B CB    1 
ATOM   6642  N  N     . ASN B 1 131 ? 141.543 163.449 158.584 1.00 41.05 ?  131 ASN B N     1 
ATOM   6643  C  CA    . ASN B 1 131 ? 141.835 164.346 157.465 1.00 41.85 ?  131 ASN B CA    1 
ATOM   6644  C  C     . ASN B 1 131 ? 142.471 165.652 157.944 1.00 41.78 ?  131 ASN B C     1 
ATOM   6645  O  O     . ASN B 1 131 ? 142.048 166.750 157.578 1.00 44.86 ?  131 ASN B O     1 
ATOM   6646  C  CB    . ASN B 1 131 ? 140.574 164.620 156.638 1.00 38.10 ?  131 ASN B CB    1 
ATOM   6647  C  CG    . ASN B 1 131 ? 140.884 164.919 155.185 1.00 45.08 ?  131 ASN B CG    1 
ATOM   6648  O  OD1   . ASN B 1 131 ? 141.875 164.439 154.638 1.00 45.24 ?  131 ASN B OD1   1 
ATOM   6649  N  ND2   . ASN B 1 131 ? 140.031 165.716 154.551 1.00 43.88 ?  131 ASN B ND2   1 
ATOM   6650  N  N     . GLY B 1 132 ? 143.502 165.523 158.778 1.00 42.24 ?  132 GLY B N     1 
ATOM   6651  C  CA    . GLY B 1 132 ? 144.274 166.661 159.230 1.00 43.72 ?  132 GLY B CA    1 
ATOM   6652  C  C     . GLY B 1 132 ? 143.940 167.184 160.610 1.00 46.62 ?  132 GLY B C     1 
ATOM   6653  O  O     . GLY B 1 132 ? 144.573 168.149 161.053 1.00 49.36 ?  132 GLY B O     1 
ATOM   6654  N  N     . ASP B 1 133 ? 142.976 166.584 161.305 1.00 42.99 ?  133 ASP B N     1 
ATOM   6655  C  CA    . ASP B 1 133 ? 142.570 167.031 162.635 1.00 43.79 ?  133 ASP B CA    1 
ATOM   6656  C  C     . ASP B 1 133 ? 143.188 166.102 163.675 1.00 46.29 ?  133 ASP B C     1 
ATOM   6657  O  O     . ASP B 1 133 ? 142.804 164.934 163.778 1.00 48.43 ?  133 ASP B O     1 
ATOM   6658  C  CB    . ASP B 1 133 ? 141.048 167.059 162.752 1.00 45.24 ?  133 ASP B CB    1 
ATOM   6659  C  CG    . ASP B 1 133 ? 140.565 167.929 163.898 1.00 48.48 ?  133 ASP B CG    1 
ATOM   6660  O  OD1   . ASP B 1 133 ? 141.367 168.220 164.810 1.00 49.94 ?  133 ASP B OD1   1 
ATOM   6661  O  OD2   . ASP B 1 133 ? 139.379 168.319 163.887 1.00 49.76 -1 133 ASP B OD2   1 
ATOM   6662  N  N     . THR B 1 134 ? 144.144 166.625 164.444 1.00 46.10 ?  134 THR B N     1 
ATOM   6663  C  CA    . THR B 1 134 ? 144.829 165.798 165.434 1.00 45.62 ?  134 THR B CA    1 
ATOM   6664  C  C     . THR B 1 134 ? 143.883 165.347 166.540 1.00 45.11 ?  134 THR B C     1 
ATOM   6665  O  O     . THR B 1 134 ? 143.921 164.186 166.961 1.00 45.77 ?  134 THR B O     1 
ATOM   6666  C  CB    . THR B 1 134 ? 146.014 166.560 166.023 1.00 47.78 ?  134 THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 134 ? 146.799 167.109 164.959 1.00 49.81 ?  134 THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 134 ? 146.878 165.632 166.862 1.00 46.42 ?  134 THR B CG2   1 
ATOM   6669  N  N     . GLU B 1 135 ? 143.030 166.251 167.029 1.00 43.87 ?  135 GLU B N     1 
ATOM   6670  C  CA    . GLU B 1 135 ? 142.082 165.879 168.074 1.00 42.72 ?  135 GLU B CA    1 
ATOM   6671  C  C     . GLU B 1 135 ? 141.073 164.857 167.567 1.00 44.61 ?  135 GLU B C     1 
ATOM   6672  O  O     . GLU B 1 135 ? 140.729 163.908 168.280 1.00 45.08 ?  135 GLU B O     1 
ATOM   6673  C  CB    . GLU B 1 135 ? 141.373 167.123 168.607 1.00 45.96 ?  135 GLU B CB    1 
ATOM   6674  C  CG    . GLU B 1 135 ? 142.293 168.077 169.348 1.00 46.64 ?  135 GLU B CG    1 
ATOM   6675  C  CD    . GLU B 1 135 ? 143.156 167.369 170.374 1.00 50.56 ?  135 GLU B CD    1 
ATOM   6676  O  OE1   . GLU B 1 135 ? 142.594 166.737 171.292 1.00 49.79 ?  135 GLU B OE1   1 
ATOM   6677  O  OE2   . GLU B 1 135 ? 144.398 167.442 170.260 1.00 49.37 -1 135 GLU B OE2   1 
ATOM   6678  N  N     . LYS B 1 136 ? 140.591 165.032 166.335 1.00 40.26 ?  136 LYS B N     1 
ATOM   6679  C  CA    . LYS B 1 136 ? 139.691 164.045 165.748 1.00 37.63 ?  136 LYS B CA    1 
ATOM   6680  C  C     . LYS B 1 136 ? 140.400 162.711 165.549 1.00 37.69 ?  136 LYS B C     1 
ATOM   6681  O  O     . LYS B 1 136 ? 139.798 161.645 165.727 1.00 41.90 ?  136 LYS B O     1 
ATOM   6682  C  CB    . LYS B 1 136 ? 139.135 164.566 164.425 1.00 42.81 ?  136 LYS B CB    1 
ATOM   6683  C  CG    . LYS B 1 136 ? 137.886 163.853 163.943 1.00 41.41 ?  136 LYS B CG    1 
ATOM   6684  C  CD    . LYS B 1 136 ? 136.629 164.515 164.477 1.00 41.96 ?  136 LYS B CD    1 
ATOM   6685  C  CE    . LYS B 1 136 ? 135.411 164.117 163.664 1.00 42.73 ?  136 LYS B CE    1 
ATOM   6686  N  NZ    . LYS B 1 136 ? 134.240 164.987 163.958 1.00 43.51 1  136 LYS B NZ    1 
ATOM   6687  N  N     . ALA B 1 137 ? 141.681 162.750 165.177 1.00 36.90 ?  137 ALA B N     1 
ATOM   6688  C  CA    . ALA B 1 137 ? 142.448 161.517 165.038 1.00 33.48 ?  137 ALA B CA    1 
ATOM   6689  C  C     . ALA B 1 137 ? 142.582 160.799 166.373 1.00 36.36 ?  137 ALA B C     1 
ATOM   6690  O  O     . ALA B 1 137 ? 142.471 159.571 166.440 1.00 39.45 ?  137 ALA B O     1 
ATOM   6691  C  CB    . ALA B 1 137 ? 143.824 161.816 164.444 1.00 33.49 ?  137 ALA B CB    1 
ATOM   6692  N  N     . LYS B 1 138 ? 142.811 161.552 167.451 1.00 38.61 ?  138 LYS B N     1 
ATOM   6693  C  CA    . LYS B 1 138 ? 142.869 160.944 168.778 1.00 36.74 ?  138 LYS B CA    1 
ATOM   6694  C  C     . LYS B 1 138 ? 141.516 160.381 169.189 1.00 37.49 ?  138 LYS B C     1 
ATOM   6695  O  O     . LYS B 1 138 ? 141.445 159.332 169.837 1.00 39.01 ?  138 LYS B O     1 
ATOM   6696  C  CB    . LYS B 1 138 ? 143.361 161.960 169.806 1.00 41.46 ?  138 LYS B CB    1 
ATOM   6697  C  CG    . LYS B 1 138 ? 144.763 162.473 169.551 1.00 41.35 ?  138 LYS B CG    1 
ATOM   6698  C  CD    . LYS B 1 138 ? 145.494 162.716 170.856 1.00 38.39 ?  138 LYS B CD    1 
ATOM   6699  C  CE    . LYS B 1 138 ? 146.533 163.808 170.704 1.00 41.44 ?  138 LYS B CE    1 
ATOM   6700  N  NZ    . LYS B 1 138 ? 145.941 165.063 170.163 1.00 43.43 1  138 LYS B NZ    1 
ATOM   6701  N  N     . GLU B 1 139 ? 140.430 161.073 168.837 1.00 37.44 ?  139 GLU B N     1 
ATOM   6702  C  CA    . GLU B 1 139 ? 139.097 160.552 169.129 1.00 37.33 ?  139 GLU B CA    1 
ATOM   6703  C  C     . GLU B 1 139 ? 138.850 159.236 168.403 1.00 36.11 ?  139 GLU B C     1 
ATOM   6704  O  O     . GLU B 1 139 ? 138.322 158.284 168.987 1.00 41.74 ?  139 GLU B O     1 
ATOM   6705  C  CB    . GLU B 1 139 ? 138.034 161.582 168.750 1.00 34.82 ?  139 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 1 139 ? 138.004 162.805 169.651 1.00 38.00 ?  139 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 1 139 ? 136.961 163.816 169.224 1.00 45.17 ?  139 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 1 139 ? 135.925 163.402 168.662 1.00 43.55 ?  139 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 1 139 ? 137.176 165.025 169.448 1.00 44.22 -1 139 GLU B OE2   1 
ATOM   6710  N  N     . TYR B 1 140 ? 139.238 159.160 167.128 1.00 29.54 ?  140 TYR B N     1 
ATOM   6711  C  CA    . TYR B 1 140 ? 139.099 157.912 166.381 1.00 28.47 ?  140 TYR B CA    1 
ATOM   6712  C  C     . TYR B 1 140 ? 139.978 156.817 166.972 1.00 31.07 ?  140 TYR B C     1 
ATOM   6713  O  O     . TYR B 1 140 ? 139.578 155.646 167.022 1.00 35.49 ?  140 TYR B O     1 
ATOM   6714  C  CB    . TYR B 1 140 ? 139.449 158.135 164.911 1.00 29.36 ?  140 TYR B CB    1 
ATOM   6715  C  CG    . TYR B 1 140 ? 138.388 158.852 164.115 1.00 30.90 ?  140 TYR B CG    1 
ATOM   6716  C  CD1   . TYR B 1 140 ? 137.081 158.385 164.079 1.00 31.12 ?  140 TYR B CD1   1 
ATOM   6717  C  CD2   . TYR B 1 140 ? 138.696 159.994 163.392 1.00 32.00 ?  140 TYR B CD2   1 
ATOM   6718  C  CE1   . TYR B 1 140 ? 136.114 159.039 163.345 1.00 34.65 ?  140 TYR B CE1   1 
ATOM   6719  C  CE2   . TYR B 1 140 ? 137.737 160.654 162.661 1.00 30.75 ?  140 TYR B CE2   1 
ATOM   6720  C  CZ    . TYR B 1 140 ? 136.449 160.174 162.639 1.00 28.98 ?  140 TYR B CZ    1 
ATOM   6721  O  OH    . TYR B 1 140 ? 135.498 160.839 161.905 1.00 37.84 ?  140 TYR B OH    1 
ATOM   6722  N  N     . VAL B 1 141 ? 141.187 157.176 167.407 1.00 32.75 ?  141 VAL B N     1 
ATOM   6723  C  CA    . VAL B 1 141 ? 142.084 156.207 168.030 1.00 32.90 ?  141 VAL B CA    1 
ATOM   6724  C  C     . VAL B 1 141 ? 141.460 155.644 169.298 1.00 32.97 ?  141 VAL B C     1 
ATOM   6725  O  O     . VAL B 1 141 ? 141.488 154.434 169.541 1.00 38.73 ?  141 VAL B O     1 
ATOM   6726  C  CB    . VAL B 1 141 ? 143.454 156.849 168.311 1.00 35.19 ?  141 VAL B CB    1 
ATOM   6727  C  CG1   . VAL B 1 141 ? 144.113 156.187 169.495 1.00 33.55 ?  141 VAL B CG1   1 
ATOM   6728  C  CG2   . VAL B 1 141 ? 144.345 156.725 167.098 1.00 33.99 ?  141 VAL B CG2   1 
ATOM   6729  N  N     . ASN B 1 142 ? 140.893 156.516 170.132 1.00 32.61 ?  142 ASN B N     1 
ATOM   6730  C  CA    . ASN B 1 142 ? 140.247 156.050 171.352 1.00 30.80 ?  142 ASN B CA    1 
ATOM   6731  C  C     . ASN B 1 142 ? 139.007 155.226 171.045 1.00 31.55 ?  142 ASN B C     1 
ATOM   6732  O  O     . ASN B 1 142 ? 138.685 154.291 171.786 1.00 35.97 ?  142 ASN B O     1 
ATOM   6733  C  CB    . ASN B 1 142 ? 139.893 157.238 172.245 1.00 28.16 ?  142 ASN B CB    1 
ATOM   6734  C  CG    . ASN B 1 142 ? 141.110 157.849 172.907 1.00 32.27 ?  142 ASN B CG    1 
ATOM   6735  O  OD1   . ASN B 1 142 ? 141.879 157.158 173.573 1.00 32.50 ?  142 ASN B OD1   1 
ATOM   6736  N  ND2   . ASN B 1 142 ? 141.293 159.150 172.722 1.00 34.28 ?  142 ASN B ND2   1 
ATOM   6737  N  N     . LEU B 1 143 ? 138.302 155.555 169.962 1.00 31.52 ?  143 LEU B N     1 
ATOM   6738  C  CA    . LEU B 1 143 ? 137.105 154.809 169.594 1.00 25.88 ?  143 LEU B CA    1 
ATOM   6739  C  C     . LEU B 1 143 ? 137.448 153.406 169.105 1.00 30.44 ?  143 LEU B C     1 
ATOM   6740  O  O     . LEU B 1 143 ? 136.725 152.447 169.398 1.00 32.84 ?  143 LEU B O     1 
ATOM   6741  C  CB    . LEU B 1 143 ? 136.332 155.578 168.527 1.00 25.23 ?  143 LEU B CB    1 
ATOM   6742  C  CG    . LEU B 1 143 ? 134.837 155.298 168.408 1.00 28.76 ?  143 LEU B CG    1 
ATOM   6743  C  CD1   . LEU B 1 143 ? 134.093 155.990 169.533 1.00 31.58 ?  143 LEU B CD1   1 
ATOM   6744  C  CD2   . LEU B 1 143 ? 134.334 155.776 167.063 1.00 28.42 ?  143 LEU B CD2   1 
ATOM   6745  N  N     . MET B 1 144 ? 138.538 153.268 168.353 1.00 28.96 ?  144 MET B N     1 
ATOM   6746  C  CA    . MET B 1 144 ? 138.900 151.974 167.785 1.00 21.69 ?  144 MET B CA    1 
ATOM   6747  C  C     . MET B 1 144 ? 139.741 151.116 168.721 1.00 26.49 ?  144 MET B C     1 
ATOM   6748  O  O     . MET B 1 144 ? 139.611 149.887 168.701 1.00 30.49 ?  144 MET B O     1 
ATOM   6749  C  CB    . MET B 1 144 ? 139.644 152.168 166.462 1.00 24.86 ?  144 MET B CB    1 
ATOM   6750  C  CG    . MET B 1 144 ? 138.782 152.741 165.352 1.00 25.95 ?  144 MET B CG    1 
ATOM   6751  S  SD    . MET B 1 144 ? 139.618 152.749 163.759 1.00 37.66 ?  144 MET B SD    1 
ATOM   6752  C  CE    . MET B 1 144 ? 140.290 154.407 163.751 1.00 27.90 ?  144 MET B CE    1 
ATOM   6753  N  N     . ILE B 1 145 ? 140.609 151.726 169.530 1.00 29.57 ?  145 ILE B N     1 
ATOM   6754  C  CA    . ILE B 1 145 ? 141.403 150.959 170.484 1.00 30.47 ?  145 ILE B CA    1 
ATOM   6755  C  C     . ILE B 1 145 ? 140.533 150.458 171.634 1.00 31.16 ?  145 ILE B C     1 
ATOM   6756  O  O     . ILE B 1 145 ? 140.779 149.374 172.174 1.00 35.22 ?  145 ILE B O     1 
ATOM   6757  C  CB    . ILE B 1 145 ? 142.605 151.789 170.977 1.00 29.75 ?  145 ILE B CB    1 
ATOM   6758  C  CG1   . ILE B 1 145 ? 143.793 150.878 171.290 1.00 28.07 ?  145 ILE B CG1   1 
ATOM   6759  C  CG2   . ILE B 1 145 ? 142.246 152.647 172.184 1.00 31.72 ?  145 ILE B CG2   1 
ATOM   6760  C  CD1   . ILE B 1 145 ? 144.463 150.302 170.065 1.00 28.63 ?  145 ILE B CD1   1 
ATOM   6761  N  N     . ASN B 1 146 ? 139.508 151.222 172.022 1.00 28.14 ?  146 ASN B N     1 
ATOM   6762  C  CA    . ASN B 1 146 ? 138.486 150.702 172.921 1.00 28.75 ?  146 ASN B CA    1 
ATOM   6763  C  C     . ASN B 1 146 ? 137.584 149.696 172.227 1.00 30.68 ?  146 ASN B C     1 
ATOM   6764  O  O     . ASN B 1 146 ? 136.766 149.056 172.897 1.00 37.17 ?  146 ASN B O     1 
ATOM   6765  C  CB    . ASN B 1 146 ? 137.640 151.841 173.489 1.00 28.50 ?  146 ASN B CB    1 
ATOM   6766  C  CG    . ASN B 1 146 ? 138.424 152.743 174.417 1.00 31.95 ?  146 ASN B CG    1 
ATOM   6767  O  OD1   . ASN B 1 146 ? 139.474 152.363 174.932 1.00 33.23 ?  146 ASN B OD1   1 
ATOM   6768  N  ND2   . ASN B 1 146 ? 137.915 153.950 174.636 1.00 31.99 ?  146 ASN B ND2   1 
ATOM   6769  N  N     . GLN B 1 147 ? 137.711 149.562 170.907 1.00 27.45 ?  147 GLN B N     1 
ATOM   6770  C  CA    . GLN B 1 147 ? 136.915 148.638 170.105 1.00 23.39 ?  147 GLN B CA    1 
ATOM   6771  C  C     . GLN B 1 147 ? 135.426 148.941 170.211 1.00 23.64 ?  147 GLN B C     1 
ATOM   6772  O  O     . GLN B 1 147 ? 134.594 148.037 170.144 1.00 30.53 ?  147 GLN B O     1 
ATOM   6773  C  CB    . GLN B 1 147 ? 137.203 147.184 170.487 1.00 26.93 ?  147 GLN B CB    1 
ATOM   6774  C  CG    . GLN B 1 147 ? 138.628 146.752 170.197 1.00 20.38 ?  147 GLN B CG    1 
ATOM   6775  C  CD    . GLN B 1 147 ? 138.751 145.261 169.983 1.00 27.43 ?  147 GLN B CD    1 
ATOM   6776  O  OE1   . GLN B 1 147 ? 139.464 144.808 169.088 1.00 28.19 ?  147 GLN B OE1   1 
ATOM   6777  N  NE2   . GLN B 1 147 ? 138.059 144.487 170.807 1.00 34.56 ?  147 GLN B NE2   1 
ATOM   6778  N  N     . GLU B 1 148 ? 135.083 150.216 170.393 1.00 26.03 ?  148 GLU B N     1 
ATOM   6779  C  CA    . GLU B 1 148 ? 133.687 150.630 170.330 1.00 23.10 ?  148 GLU B CA    1 
ATOM   6780  C  C     . GLU B 1 148 ? 133.170 150.643 168.899 1.00 26.63 ?  148 GLU B C     1 
ATOM   6781  O  O     . GLU B 1 148 ? 132.008 150.301 168.658 1.00 32.90 ?  148 GLU B O     1 
ATOM   6782  C  CB    . GLU B 1 148 ? 133.520 152.015 170.955 1.00 21.39 ?  148 GLU B CB    1 
ATOM   6783  C  CG    . GLU B 1 148 ? 133.891 152.082 172.423 1.00 26.46 ?  148 GLU B CG    1 
ATOM   6784  C  CD    . GLU B 1 148 ? 133.948 153.504 172.938 1.00 32.26 ?  148 GLU B CD    1 
ATOM   6785  O  OE1   . GLU B 1 148 ? 134.986 154.169 172.741 1.00 33.54 ?  148 GLU B OE1   1 
ATOM   6786  O  OE2   . GLU B 1 148 ? 132.953 153.959 173.539 1.00 37.57 -1 148 GLU B OE2   1 
ATOM   6787  N  N     . TYR B 1 149 ? 134.015 151.026 167.948 1.00 23.60 ?  149 TYR B N     1 
ATOM   6788  C  CA    . TYR B 1 149 ? 133.655 151.082 166.542 1.00 19.15 ?  149 TYR B CA    1 
ATOM   6789  C  C     . TYR B 1 149 ? 134.702 150.350 165.721 1.00 22.53 ?  149 TYR B C     1 
ATOM   6790  O  O     . TYR B 1 149 ? 135.897 150.409 166.022 1.00 28.88 ?  149 TYR B O     1 
ATOM   6791  C  CB    . TYR B 1 149 ? 133.527 152.525 166.054 1.00 21.16 ?  149 TYR B CB    1 
ATOM   6792  C  CG    . TYR B 1 149 ? 133.391 152.655 164.556 1.00 21.61 ?  149 TYR B CG    1 
ATOM   6793  C  CD1   . TYR B 1 149 ? 132.275 152.163 163.893 1.00 13.92 ?  149 TYR B CD1   1 
ATOM   6794  C  CD2   . TYR B 1 149 ? 134.379 153.274 163.804 1.00 19.53 ?  149 TYR B CD2   1 
ATOM   6795  C  CE1   . TYR B 1 149 ? 132.149 152.282 162.524 1.00 17.41 ?  149 TYR B CE1   1 
ATOM   6796  C  CE2   . TYR B 1 149 ? 134.263 153.399 162.437 1.00 20.91 ?  149 TYR B CE2   1 
ATOM   6797  C  CZ    . TYR B 1 149 ? 133.146 152.902 161.801 1.00 20.04 ?  149 TYR B CZ    1 
ATOM   6798  O  OH    . TYR B 1 149 ? 133.029 153.025 160.437 1.00 18.44 ?  149 TYR B OH    1 
ATOM   6799  N  N     . GLN B 1 150 ? 134.243 149.659 164.689 1.00 17.68 ?  150 GLN B N     1 
ATOM   6800  C  CA    . GLN B 1 150 ? 135.115 148.907 163.795 1.00 10.71 ?  150 GLN B CA    1 
ATOM   6801  C  C     . GLN B 1 150 ? 134.801 149.285 162.358 1.00 20.38 ?  150 GLN B C     1 
ATOM   6802  O  O     . GLN B 1 150 ? 133.683 149.012 161.879 1.00 23.27 ?  150 GLN B O     1 
ATOM   6803  C  CB    . GLN B 1 150 ? 134.929 147.407 164.012 1.00 17.41 ?  150 GLN B CB    1 
ATOM   6804  C  CG    . GLN B 1 150 ? 135.760 146.542 163.098 1.00 18.97 ?  150 GLN B CG    1 
ATOM   6805  C  CD    . GLN B 1 150 ? 137.239 146.847 163.187 1.00 17.16 ?  150 GLN B CD    1 
ATOM   6806  O  OE1   . GLN B 1 150 ? 137.860 146.677 164.235 1.00 30.40 ?  150 GLN B OE1   1 
ATOM   6807  N  NE2   . GLN B 1 150 ? 137.816 147.296 162.081 1.00 15.84 ?  150 GLN B NE2   1 
ATOM   6808  N  N     . PRO B 1 151 ? 135.720 149.931 161.644 1.00 26.31 ?  151 PRO B N     1 
ATOM   6809  C  CA    . PRO B 1 151 ? 135.519 150.135 160.208 1.00 16.21 ?  151 PRO B CA    1 
ATOM   6810  C  C     . PRO B 1 151 ? 135.472 148.801 159.483 1.00 16.18 ?  151 PRO B C     1 
ATOM   6811  O  O     . PRO B 1 151 ? 136.051 147.807 159.928 1.00 21.62 ?  151 PRO B O     1 
ATOM   6812  C  CB    . PRO B 1 151 ? 136.740 150.962 159.788 1.00 18.71 ?  151 PRO B CB    1 
ATOM   6813  C  CG    . PRO B 1 151 ? 137.236 151.584 161.053 1.00 18.97 ?  151 PRO B CG    1 
ATOM   6814  C  CD    . PRO B 1 151 ? 136.933 150.603 162.138 1.00 21.62 ?  151 PRO B CD    1 
ATOM   6815  N  N     . SER B 1 152 ? 134.756 148.781 158.363 1.00 21.04 ?  152 SER B N     1 
ATOM   6816  C  CA    . SER B 1 152 ? 134.601 147.557 157.594 1.00 14.61 ?  152 SER B CA    1 
ATOM   6817  C  C     . SER B 1 152 ? 135.959 147.020 157.152 1.00 22.02 ?  152 SER B C     1 
ATOM   6818  O  O     . SER B 1 152 ? 136.977 147.715 157.187 1.00 25.96 ?  152 SER B O     1 
ATOM   6819  C  CB    . SER B 1 152 ? 133.719 147.798 156.373 1.00 20.91 ?  152 SER B CB    1 
ATOM   6820  O  OG    . SER B 1 152 ? 134.359 148.652 155.441 1.00 24.93 ?  152 SER B OG    1 
ATOM   6821  N  N     . THR B 1 153 ? 135.962 145.753 156.740 1.00 28.20 ?  153 THR B N     1 
ATOM   6822  C  CA    . THR B 1 153 ? 137.187 145.119 156.258 1.00 20.89 ?  153 THR B CA    1 
ATOM   6823  C  C     . THR B 1 153 ? 137.876 145.909 155.148 1.00 27.54 ?  153 THR B C     1 
ATOM   6824  O  O     . THR B 1 153 ? 139.098 146.104 155.238 1.00 27.63 ?  153 THR B O     1 
ATOM   6825  C  CB    . THR B 1 153 ? 136.875 143.682 155.814 1.00 25.86 ?  153 THR B CB    1 
ATOM   6826  O  OG1   . THR B 1 153 ? 136.654 142.862 156.967 1.00 29.62 ?  153 THR B OG1   1 
ATOM   6827  C  CG2   . THR B 1 153 ? 138.020 143.106 154.996 1.00 25.78 ?  153 THR B CG2   1 
ATOM   6828  N  N     . PRO B 1 154 ? 137.184 146.402 154.110 1.00 25.81 ?  154 PRO B N     1 
ATOM   6829  C  CA    . PRO B 1 154 ? 137.888 147.251 153.131 1.00 19.80 ?  154 PRO B CA    1 
ATOM   6830  C  C     . PRO B 1 154 ? 138.497 148.496 153.751 1.00 20.96 ?  154 PRO B C     1 
ATOM   6831  O  O     . PRO B 1 154 ? 139.668 148.806 153.496 1.00 26.68 ?  154 PRO B O     1 
ATOM   6832  C  CB    . PRO B 1 154 ? 136.790 147.592 152.115 1.00 21.37 ?  154 PRO B CB    1 
ATOM   6833  C  CG    . PRO B 1 154 ? 135.799 146.508 152.249 1.00 24.97 ?  154 PRO B CG    1 
ATOM   6834  C  CD    . PRO B 1 154 ? 135.792 146.148 153.696 1.00 19.97 ?  154 PRO B CD    1 
ATOM   6835  N  N     . THR B 1 155 ? 137.736 149.212 154.580 1.00 22.65 ?  155 THR B N     1 
ATOM   6836  C  CA    . THR B 1 155 ? 138.242 150.443 155.176 1.00 20.13 ?  155 THR B CA    1 
ATOM   6837  C  C     . THR B 1 155 ? 139.358 150.159 156.173 1.00 24.21 ?  155 THR B C     1 
ATOM   6838  O  O     . THR B 1 155 ? 140.417 150.795 156.132 1.00 29.73 ?  155 THR B O     1 
ATOM   6839  C  CB    . THR B 1 155 ? 137.104 151.210 155.848 1.00 22.59 ?  155 THR B CB    1 
ATOM   6840  O  OG1   . THR B 1 155 ? 136.029 151.387 154.919 1.00 23.45 ?  155 THR B OG1   1 
ATOM   6841  C  CG2   . THR B 1 155 ? 137.587 152.570 156.316 1.00 17.64 ?  155 THR B CG2   1 
ATOM   6842  N  N     . PHE B 1 156 ? 139.141 149.203 157.079 1.00 23.30 ?  156 PHE B N     1 
ATOM   6843  C  CA    . PHE B 1 156 ? 140.153 148.902 158.086 1.00 20.13 ?  156 PHE B CA    1 
ATOM   6844  C  C     . PHE B 1 156 ? 141.436 148.384 157.448 1.00 29.69 ?  156 PHE B C     1 
ATOM   6845  O  O     . PHE B 1 156 ? 142.539 148.748 157.869 1.00 29.95 ?  156 PHE B O     1 
ATOM   6846  C  CB    . PHE B 1 156 ? 139.610 147.888 159.093 1.00 23.60 ?  156 PHE B CB    1 
ATOM   6847  C  CG    . PHE B 1 156 ? 140.397 147.822 160.370 1.00 28.03 ?  156 PHE B CG    1 
ATOM   6848  C  CD1   . PHE B 1 156 ? 140.552 148.948 161.162 1.00 24.88 ?  156 PHE B CD1   1 
ATOM   6849  C  CD2   . PHE B 1 156 ? 140.982 146.636 160.779 1.00 23.77 ?  156 PHE B CD2   1 
ATOM   6850  C  CE1   . PHE B 1 156 ? 141.276 148.891 162.336 1.00 26.16 ?  156 PHE B CE1   1 
ATOM   6851  C  CE2   . PHE B 1 156 ? 141.707 146.574 161.952 1.00 22.91 ?  156 PHE B CE2   1 
ATOM   6852  C  CZ    . PHE B 1 156 ? 141.853 147.702 162.731 1.00 29.01 ?  156 PHE B CZ    1 
ATOM   6853  N  N     . LEU B 1 157 ? 141.310 147.533 156.430 1.00 30.11 ?  157 LEU B N     1 
ATOM   6854  C  CA    . LEU B 1 157 ? 142.481 146.925 155.811 1.00 26.59 ?  157 LEU B CA    1 
ATOM   6855  C  C     . LEU B 1 157 ? 143.215 147.893 154.892 1.00 31.97 ?  157 LEU B C     1 
ATOM   6856  O  O     . LEU B 1 157 ? 144.448 147.865 154.821 1.00 40.37 ?  157 LEU B O     1 
ATOM   6857  C  CB    . LEU B 1 157 ? 142.060 145.671 155.039 1.00 30.79 ?  157 LEU B CB    1 
ATOM   6858  C  CG    . LEU B 1 157 ? 143.095 145.001 154.136 1.00 29.61 ?  157 LEU B CG    1 
ATOM   6859  C  CD1   . LEU B 1 157 ? 144.238 144.435 154.957 1.00 32.68 ?  157 LEU B CD1   1 
ATOM   6860  C  CD2   . LEU B 1 157 ? 142.445 143.915 153.297 1.00 30.30 ?  157 LEU B CD2   1 
ATOM   6861  N  N     . ASN B 1 158 ? 142.489 148.764 154.189 1.00 30.57 ?  158 ASN B N     1 
ATOM   6862  C  CA    . ASN B 1 158 ? 143.067 149.521 153.090 1.00 29.15 ?  158 ASN B CA    1 
ATOM   6863  C  C     . ASN B 1 158 ? 143.260 151.005 153.371 1.00 32.44 ?  158 ASN B C     1 
ATOM   6864  O  O     . ASN B 1 158 ? 143.834 151.698 152.525 1.00 39.63 ?  158 ASN B O     1 
ATOM   6865  C  CB    . ASN B 1 158 ? 142.194 149.363 151.836 1.00 29.82 ?  158 ASN B CB    1 
ATOM   6866  C  CG    . ASN B 1 158 ? 142.106 147.927 151.367 1.00 35.71 ?  158 ASN B CG    1 
ATOM   6867  O  OD1   . ASN B 1 158 ? 143.019 147.133 151.588 1.00 40.03 ?  158 ASN B OD1   1 
ATOM   6868  N  ND2   . ASN B 1 158 ? 141.001 147.585 150.717 1.00 35.98 ?  158 ASN B ND2   1 
ATOM   6869  N  N     . ALA B 1 159 ? 142.804 151.516 154.513 1.00 31.90 ?  159 ALA B N     1 
ATOM   6870  C  CA    . ALA B 1 159 ? 142.924 152.946 154.775 1.00 33.22 ?  159 ALA B CA    1 
ATOM   6871  C  C     . ALA B 1 159 ? 144.389 153.355 154.863 1.00 38.83 ?  159 ALA B C     1 
ATOM   6872  O  O     . ALA B 1 159 ? 145.174 152.751 155.599 1.00 42.87 ?  159 ALA B O     1 
ATOM   6873  C  CB    . ALA B 1 159 ? 142.198 153.319 156.066 1.00 32.12 ?  159 ALA B CB    1 
ATOM   6874  N  N     . GLY B 1 160 ? 144.755 154.385 154.106 1.00 45.42 ?  160 GLY B N     1 
ATOM   6875  C  CA    . GLY B 1 160 ? 146.101 154.913 154.153 1.00 40.42 ?  160 GLY B CA    1 
ATOM   6876  C  C     . GLY B 1 160 ? 147.157 154.072 153.475 1.00 40.71 ?  160 GLY B C     1 
ATOM   6877  O  O     . GLY B 1 160 ? 148.348 154.341 153.661 1.00 45.57 ?  160 GLY B O     1 
ATOM   6878  N  N     . ARG B 1 161 ? 146.768 153.065 152.699 1.00 43.00 ?  161 ARG B N     1 
ATOM   6879  C  CA    . ARG B 1 161 ? 147.712 152.187 152.023 1.00 44.08 ?  161 ARG B CA    1 
ATOM   6880  C  C     . ARG B 1 161 ? 147.848 152.587 150.560 1.00 46.63 ?  161 ARG B C     1 
ATOM   6881  O  O     . ARG B 1 161 ? 146.864 152.949 149.909 1.00 46.53 ?  161 ARG B O     1 
ATOM   6882  C  CB    . ARG B 1 161 ? 147.271 150.726 152.123 1.00 38.66 ?  161 ARG B CB    1 
ATOM   6883  C  CG    . ARG B 1 161 ? 147.422 150.125 153.509 1.00 39.48 ?  161 ARG B CG    1 
ATOM   6884  C  CD    . ARG B 1 161 ? 147.404 148.607 153.458 1.00 40.50 ?  161 ARG B CD    1 
ATOM   6885  N  NE    . ARG B 1 161 ? 147.313 148.018 154.789 1.00 44.00 ?  161 ARG B NE    1 
ATOM   6886  C  CZ    . ARG B 1 161 ? 147.208 146.718 155.029 1.00 44.80 ?  161 ARG B CZ    1 
ATOM   6887  N  NH1   . ARG B 1 161 ? 147.186 145.834 154.046 1.00 44.14 1  161 ARG B NH1   1 
ATOM   6888  N  NH2   . ARG B 1 161 ? 147.122 146.296 156.286 1.00 43.06 ?  161 ARG B NH2   1 
ATOM   6889  N  N     . LYS B 1 162 ? 149.081 152.531 150.049 1.00 53.05 ?  162 LYS B N     1 
ATOM   6890  C  CA    . LYS B 1 162 ? 149.310 152.847 148.643 1.00 52.29 ?  162 LYS B CA    1 
ATOM   6891  C  C     . LYS B 1 162 ? 148.795 151.735 147.736 1.00 52.62 ?  162 LYS B C     1 
ATOM   6892  O  O     . LYS B 1 162 ? 148.144 152.007 146.720 1.00 52.82 ?  162 LYS B O     1 
ATOM   6893  C  CB    . LYS B 1 162 ? 150.798 153.099 148.398 1.00 52.13 ?  162 LYS B CB    1 
ATOM   6894  C  CG    . LYS B 1 162 ? 151.182 153.189 146.931 1.00 52.46 ?  162 LYS B CG    1 
ATOM   6895  C  CD    . LYS B 1 162 ? 151.081 154.617 146.416 1.00 54.30 ?  162 LYS B CD    1 
ATOM   6896  C  CE    . LYS B 1 162 ? 151.921 155.569 147.252 1.00 54.39 ?  162 LYS B CE    1 
ATOM   6897  N  NZ    . LYS B 1 162 ? 151.323 156.932 147.303 1.00 54.64 1  162 LYS B NZ    1 
ATOM   6898  N  N     . ARG B 1 163 ? 149.064 150.479 148.091 1.00 53.33 ?  163 ARG B N     1 
ATOM   6899  C  CA    . ARG B 1 163 ? 148.613 149.323 147.325 1.00 55.14 ?  163 ARG B CA    1 
ATOM   6900  C  C     . ARG B 1 163 ? 147.176 148.930 147.651 1.00 57.86 ?  163 ARG B C     1 
ATOM   6901  O  O     . ARG B 1 163 ? 146.770 147.791 147.387 1.00 56.49 ?  163 ARG B O     1 
ATOM   6902  C  CB    . ARG B 1 163 ? 149.555 148.138 147.561 1.00 56.25 ?  163 ARG B CB    1 
ATOM   6903  C  CG    . ARG B 1 163 ? 149.646 147.162 146.396 1.00 58.12 ?  163 ARG B CG    1 
ATOM   6904  C  CD    . ARG B 1 163 ? 149.943 145.748 146.873 1.00 56.45 ?  163 ARG B CD    1 
ATOM   6905  N  NE    . ARG B 1 163 ? 149.218 145.405 148.091 1.00 59.28 ?  163 ARG B NE    1 
ATOM   6906  C  CZ    . ARG B 1 163 ? 147.950 145.022 148.129 1.00 58.45 ?  163 ARG B CZ    1 
ATOM   6907  N  NH1   . ARG B 1 163 ? 147.225 144.919 147.026 1.00 56.93 1  163 ARG B NH1   1 
ATOM   6908  N  NH2   . ARG B 1 163 ? 147.393 144.732 149.302 1.00 56.83 ?  163 ARG B NH2   1 
ATOM   6909  N  N     . ARG B 1 164 ? 146.404 149.849 148.220 1.00 55.68 ?  164 ARG B N     1 
ATOM   6910  C  CA    . ARG B 1 164 ? 145.047 149.560 148.646 1.00 50.63 ?  164 ARG B CA    1 
ATOM   6911  C  C     . ARG B 1 164 ? 144.113 149.407 147.449 1.00 50.63 ?  164 ARG B C     1 
ATOM   6912  O  O     . ARG B 1 164 ? 144.424 149.798 146.320 1.00 50.44 ?  164 ARG B O     1 
ATOM   6913  C  CB    . ARG B 1 164 ? 144.528 150.673 149.553 1.00 48.84 ?  164 ARG B CB    1 
ATOM   6914  C  CG    . ARG B 1 164 ? 144.057 151.909 148.802 1.00 45.63 ?  164 ARG B CG    1 
ATOM   6915  C  CD    . ARG B 1 164 ? 143.060 152.711 149.620 1.00 48.21 ?  164 ARG B CD    1 
ATOM   6916  N  NE    . ARG B 1 164 ? 142.512 153.834 148.870 1.00 50.38 ?  164 ARG B NE    1 
ATOM   6917  C  CZ    . ARG B 1 164 ? 142.209 155.011 149.401 1.00 53.94 ?  164 ARG B CZ    1 
ATOM   6918  N  NH1   . ARG B 1 164 ? 142.397 155.258 150.686 1.00 51.60 1  164 ARG B NH1   1 
ATOM   6919  N  NH2   . ARG B 1 164 ? 141.707 155.964 148.621 1.00 53.54 ?  164 ARG B NH2   1 
ATOM   6920  N  N     . GLY B 1 165 ? 142.955 148.819 147.715 1.00 49.03 ?  165 GLY B N     1 
ATOM   6921  C  CA    . GLY B 1 165 ? 141.843 148.808 146.786 1.00 45.13 ?  165 GLY B CA    1 
ATOM   6922  C  C     . GLY B 1 165 ? 140.886 149.944 147.067 1.00 48.10 ?  165 GLY B C     1 
ATOM   6923  O  O     . GLY B 1 165 ? 141.291 151.087 147.303 1.00 48.97 ?  165 GLY B O     1 
ATOM   6924  N  N     . GLU B 1 166 ? 139.596 149.631 147.041 1.00 43.00 ?  166 GLU B N     1 
ATOM   6925  C  CA    . GLU B 1 166 ? 138.575 150.598 147.412 1.00 39.82 ?  166 GLU B CA    1 
ATOM   6926  C  C     . GLU B 1 166 ? 138.066 150.318 148.820 1.00 37.59 ?  166 GLU B C     1 
ATOM   6927  O  O     . GLU B 1 166 ? 138.021 149.170 149.270 1.00 33.46 ?  166 GLU B O     1 
ATOM   6928  C  CB    . GLU B 1 166 ? 137.412 150.575 146.420 1.00 36.97 ?  166 GLU B CB    1 
ATOM   6929  C  CG    . GLU B 1 166 ? 137.632 151.452 145.201 1.00 41.28 ?  166 GLU B CG    1 
ATOM   6930  C  CD    . GLU B 1 166 ? 137.739 152.923 145.550 1.00 42.78 ?  166 GLU B CD    1 
ATOM   6931  O  OE1   . GLU B 1 166 ? 137.074 153.358 146.513 1.00 47.42 ?  166 GLU B OE1   1 
ATOM   6932  O  OE2   . GLU B 1 166 ? 138.491 153.643 144.861 1.00 39.22 -1 166 GLU B OE2   1 
ATOM   6933  N  N     . LEU B 1 167 ? 137.685 151.388 149.517 1.00 30.71 ?  167 LEU B N     1 
ATOM   6934  C  CA    . LEU B 1 167 ? 137.168 151.268 150.872 1.00 23.73 ?  167 LEU B CA    1 
ATOM   6935  C  C     . LEU B 1 167 ? 135.698 150.878 150.916 1.00 29.03 ?  167 LEU B C     1 
ATOM   6936  O  O     . LEU B 1 167 ? 135.195 150.549 151.996 1.00 30.76 ?  167 LEU B O     1 
ATOM   6937  C  CB    . LEU B 1 167 ? 137.366 152.581 151.632 1.00 30.06 ?  167 LEU B CB    1 
ATOM   6938  C  CG    . LEU B 1 167 ? 138.789 153.129 151.743 1.00 26.48 ?  167 LEU B CG    1 
ATOM   6939  C  CD1   . LEU B 1 167 ? 138.862 154.136 152.867 1.00 27.89 ?  167 LEU B CD1   1 
ATOM   6940  C  CD2   . LEU B 1 167 ? 139.789 152.013 151.970 1.00 26.02 ?  167 LEU B CD2   1 
ATOM   6941  N  N     . VAL B 1 168 ? 135.003 150.909 149.784 1.00 29.42 ?  168 VAL B N     1 
ATOM   6942  C  CA    . VAL B 1 168 ? 133.593 150.540 149.745 1.00 22.91 ?  168 VAL B CA    1 
ATOM   6943  C  C     . VAL B 1 168 ? 133.480 149.030 149.602 1.00 26.85 ?  168 VAL B C     1 
ATOM   6944  O  O     . VAL B 1 168 ? 134.142 148.421 148.752 1.00 28.67 ?  168 VAL B O     1 
ATOM   6945  C  CB    . VAL B 1 168 ? 132.872 151.263 148.598 1.00 27.41 ?  168 VAL B CB    1 
ATOM   6946  C  CG1   . VAL B 1 168 ? 131.376 151.021 148.684 1.00 28.93 ?  168 VAL B CG1   1 
ATOM   6947  C  CG2   . VAL B 1 168 ? 133.178 152.748 148.637 1.00 27.27 ?  168 VAL B CG2   1 
ATOM   6948  N  N     . SER B 1 169 ? 132.640 148.420 150.439 1.00 35.86 ?  169 SER B N     1 
ATOM   6949  C  CA    . SER B 1 169 ? 132.515 146.968 150.448 1.00 37.59 ?  169 SER B CA    1 
ATOM   6950  C  C     . SER B 1 169 ? 131.600 146.473 149.333 1.00 36.82 ?  169 SER B C     1 
ATOM   6951  O  O     . SER B 1 169 ? 131.962 145.561 148.583 1.00 34.09 ?  169 SER B O     1 
ATOM   6952  C  CB    . SER B 1 169 ? 131.999 146.498 151.810 1.00 31.71 ?  169 SER B CB    1 
ATOM   6953  O  OG    . SER B 1 169 ? 131.946 145.083 151.877 1.00 34.78 ?  169 SER B OG    1 
ATOM   6954  N  N     . CYS B 1 170 ? 130.412 147.058 149.211 1.00 31.77 ?  170 CYS B N     1 
ATOM   6955  C  CA    . CYS B 1 170 ? 129.375 146.546 148.328 1.00 26.64 ?  170 CYS B CA    1 
ATOM   6956  C  C     . CYS B 1 170 ? 128.972 147.596 147.302 1.00 25.35 ?  170 CYS B C     1 
ATOM   6957  O  O     . CYS B 1 170 ? 128.947 148.795 147.599 1.00 24.91 ?  170 CYS B O     1 
ATOM   6958  C  CB    . CYS B 1 170 ? 128.148 146.108 149.131 1.00 34.42 ?  170 CYS B CB    1 
ATOM   6959  S  SG    . CYS B 1 170 ? 127.557 147.345 150.306 1.00 53.61 ?  170 CYS B SG    1 
ATOM   6960  N  N     . PHE B 1 171 ? 128.658 147.131 146.095 1.00 22.77 ?  171 PHE B N     1 
ATOM   6961  C  CA    . PHE B 1 171 ? 128.157 147.973 145.021 1.00 13.83 ?  171 PHE B CA    1 
ATOM   6962  C  C     . PHE B 1 171 ? 126.912 147.335 144.427 1.00 12.90 ?  171 PHE B C     1 
ATOM   6963  O  O     . PHE B 1 171 ? 126.846 146.112 144.272 1.00 24.47 ?  171 PHE B O     1 
ATOM   6964  C  CB    . PHE B 1 171 ? 129.204 148.176 143.925 1.00 16.07 ?  171 PHE B CB    1 
ATOM   6965  C  CG    . PHE B 1 171 ? 130.528 148.652 144.435 1.00 19.04 ?  171 PHE B CG    1 
ATOM   6966  C  CD1   . PHE B 1 171 ? 130.731 149.988 144.725 1.00 15.01 ?  171 PHE B CD1   1 
ATOM   6967  C  CD2   . PHE B 1 171 ? 131.573 147.764 144.617 1.00 18.02 ?  171 PHE B CD2   1 
ATOM   6968  C  CE1   . PHE B 1 171 ? 131.947 150.427 145.194 1.00 13.11 ?  171 PHE B CE1   1 
ATOM   6969  C  CE2   . PHE B 1 171 ? 132.792 148.201 145.083 1.00 15.58 ?  171 PHE B CE2   1 
ATOM   6970  C  CZ    . PHE B 1 171 ? 132.980 149.534 145.372 1.00 15.68 ?  171 PHE B CZ    1 
ATOM   6971  N  N     . LEU B 1 172 ? 125.927 148.165 144.098 1.00 13.06 ?  172 LEU B N     1 
ATOM   6972  C  CA    . LEU B 1 172 ? 124.664 147.707 143.534 1.00 10.19 ?  172 LEU B CA    1 
ATOM   6973  C  C     . LEU B 1 172 ? 124.450 148.402 142.199 1.00 11.41 ?  172 LEU B C     1 
ATOM   6974  O  O     . LEU B 1 172 ? 124.434 149.635 142.137 1.00 17.26 ?  172 LEU B O     1 
ATOM   6975  C  CB    . LEU B 1 172 ? 123.502 147.998 144.484 1.00 13.81 ?  172 LEU B CB    1 
ATOM   6976  C  CG    . LEU B 1 172 ? 123.426 147.230 145.804 1.00 8.92  ?  172 LEU B CG    1 
ATOM   6977  C  CD1   . LEU B 1 172 ? 124.309 147.873 146.862 1.00 10.47 ?  172 LEU B CD1   1 
ATOM   6978  C  CD2   . LEU B 1 172 ? 121.992 147.179 146.273 1.00 10.66 ?  172 LEU B CD2   1 
ATOM   6979  N  N     . LEU B 1 173 ? 124.278 147.616 141.142 1.00 17.95 ?  173 LEU B N     1 
ATOM   6980  C  CA    . LEU B 1 173 ? 124.134 148.136 139.790 1.00 9.04  ?  173 LEU B CA    1 
ATOM   6981  C  C     . LEU B 1 173 ? 122.740 147.853 139.251 1.00 14.71 ?  173 LEU B C     1 
ATOM   6982  O  O     . LEU B 1 173 ? 122.197 146.762 139.445 1.00 20.11 ?  173 LEU B O     1 
ATOM   6983  C  CB    . LEU B 1 173 ? 125.173 147.528 138.847 1.00 13.46 ?  173 LEU B CB    1 
ATOM   6984  C  CG    . LEU B 1 173 ? 126.642 147.560 139.267 1.00 18.36 ?  173 LEU B CG    1 
ATOM   6985  C  CD1   . LEU B 1 173 ? 127.495 146.925 138.185 1.00 21.69 ?  173 LEU B CD1   1 
ATOM   6986  C  CD2   . LEU B 1 173 ? 127.092 148.983 139.548 1.00 20.29 ?  173 LEU B CD2   1 
ATOM   6987  N  N     . GLU B 1 174 ? 122.168 148.845 138.578 1.00 23.41 ?  174 GLU B N     1 
ATOM   6988  C  CA    . GLU B 1 174 ? 120.930 148.669 137.834 1.00 20.21 ?  174 GLU B CA    1 
ATOM   6989  C  C     . GLU B 1 174 ? 121.267 148.436 136.367 1.00 18.27 ?  174 GLU B C     1 
ATOM   6990  O  O     . GLU B 1 174 ? 121.986 149.232 135.757 1.00 27.43 ?  174 GLU B O     1 
ATOM   6991  C  CB    . GLU B 1 174 ? 120.027 149.892 137.985 1.00 23.89 ?  174 GLU B CB    1 
ATOM   6992  C  CG    . GLU B 1 174 ? 119.322 149.989 139.325 1.00 18.30 ?  174 GLU B CG    1 
ATOM   6993  C  CD    . GLU B 1 174 ? 117.816 149.911 139.195 1.00 21.69 ?  174 GLU B CD    1 
ATOM   6994  O  OE1   . GLU B 1 174 ? 117.331 149.157 138.327 1.00 28.18 ?  174 GLU B OE1   1 
ATOM   6995  O  OE2   . GLU B 1 174 ? 117.116 150.605 139.960 1.00 24.53 -1 174 GLU B OE2   1 
ATOM   6996  N  N     . VAL B 1 175 ? 120.748 147.348 135.806 1.00 16.95 ?  175 VAL B N     1 
ATOM   6997  C  CA    . VAL B 1 175 ? 121.027 146.959 134.428 1.00 18.41 ?  175 VAL B CA    1 
ATOM   6998  C  C     . VAL B 1 175 ? 119.785 147.234 133.594 1.00 17.16 ?  175 VAL B C     1 
ATOM   6999  O  O     . VAL B 1 175 ? 118.731 146.626 133.815 1.00 13.81 ?  175 VAL B O     1 
ATOM   7000  C  CB    . VAL B 1 175 ? 121.440 145.483 134.330 1.00 19.90 ?  175 VAL B CB    1 
ATOM   7001  C  CG1   . VAL B 1 175 ? 122.124 145.207 132.999 1.00 14.27 ?  175 VAL B CG1   1 
ATOM   7002  C  CG2   . VAL B 1 175 ? 122.345 145.109 135.490 1.00 14.16 ?  175 VAL B CG2   1 
ATOM   7003  N  N     . ASN B 1 176 ? 119.909 148.148 132.636 1.00 18.38 ?  176 ASN B N     1 
ATOM   7004  C  CA    . ASN B 1 176 ? 118.811 148.443 131.732 1.00 19.52 ?  176 ASN B CA    1 
ATOM   7005  C  C     . ASN B 1 176 ? 118.709 147.370 130.652 1.00 20.93 ?  176 ASN B C     1 
ATOM   7006  O  O     . ASN B 1 176 ? 119.654 146.623 130.385 1.00 19.66 ?  176 ASN B O     1 
ATOM   7007  C  CB    . ASN B 1 176 ? 118.988 149.820 131.094 1.00 18.09 ?  176 ASN B CB    1 
ATOM   7008  C  CG    . ASN B 1 176 ? 117.678 150.559 130.935 1.00 19.52 ?  176 ASN B CG    1 
ATOM   7009  O  OD1   . ASN B 1 176 ? 116.604 149.964 131.005 1.00 27.15 ?  176 ASN B OD1   1 
ATOM   7010  N  ND2   . ASN B 1 176 ? 117.759 151.865 130.718 1.00 21.83 ?  176 ASN B ND2   1 
ATOM   7011  N  N     . ASP B 1 177 ? 117.537 147.308 130.020 1.00 25.27 ?  177 ASP B N     1 
ATOM   7012  C  CA    . ASP B 1 177 ? 117.225 146.262 129.047 1.00 22.19 ?  177 ASP B CA    1 
ATOM   7013  C  C     . ASP B 1 177 ? 117.774 146.666 127.680 1.00 23.70 ?  177 ASP B C     1 
ATOM   7014  O  O     . ASP B 1 177 ? 117.059 147.141 126.794 1.00 26.99 ?  177 ASP B O     1 
ATOM   7015  C  CB    . ASP B 1 177 ? 115.724 146.013 129.001 1.00 18.71 ?  177 ASP B CB    1 
ATOM   7016  C  CG    . ASP B 1 177 ? 115.342 144.930 128.020 1.00 26.22 ?  177 ASP B CG    1 
ATOM   7017  O  OD1   . ASP B 1 177 ? 116.095 143.942 127.900 1.00 30.83 ?  177 ASP B OD1   1 
ATOM   7018  O  OD2   . ASP B 1 177 ? 114.287 145.068 127.368 1.00 29.50 -1 177 ASP B OD2   1 
ATOM   7019  N  N     . SER B 1 178 ? 119.080 146.468 127.513 1.00 19.01 ?  178 SER B N     1 
ATOM   7020  C  CA    . SER B 1 178 ? 119.737 146.729 126.241 1.00 18.37 ?  178 SER B CA    1 
ATOM   7021  C  C     . SER B 1 178 ? 121.090 146.034 126.233 1.00 16.76 ?  178 SER B C     1 
ATOM   7022  O  O     . SER B 1 178 ? 121.675 145.778 127.288 1.00 23.35 ?  178 SER B O     1 
ATOM   7023  C  CB    . SER B 1 178 ? 119.905 148.231 125.986 1.00 14.28 ?  178 SER B CB    1 
ATOM   7024  O  OG    . SER B 1 178 ? 121.146 148.699 126.477 1.00 19.63 ?  178 SER B OG    1 
ATOM   7025  N  N     . LEU B 1 179 ? 121.574 145.724 125.028 1.00 23.99 ?  179 LEU B N     1 
ATOM   7026  C  CA    . LEU B 1 179 ? 122.890 145.104 124.897 1.00 19.15 ?  179 LEU B CA    1 
ATOM   7027  C  C     . LEU B 1 179 ? 123.991 146.046 125.361 1.00 14.42 ?  179 LEU B C     1 
ATOM   7028  O  O     . LEU B 1 179 ? 124.959 145.615 125.998 1.00 18.64 ?  179 LEU B O     1 
ATOM   7029  C  CB    . LEU B 1 179 ? 123.131 144.674 123.450 1.00 20.55 ?  179 LEU B CB    1 
ATOM   7030  C  CG    . LEU B 1 179 ? 124.432 143.911 123.201 1.00 17.53 ?  179 LEU B CG    1 
ATOM   7031  C  CD1   . LEU B 1 179 ? 124.423 142.581 123.942 1.00 14.12 ?  179 LEU B CD1   1 
ATOM   7032  C  CD2   . LEU B 1 179 ? 124.661 143.704 121.715 1.00 15.45 ?  179 LEU B CD2   1 
ATOM   7033  N  N     . ASN B 1 180 ? 123.869 147.336 125.039 1.00 18.45 ?  180 ASN B N     1 
ATOM   7034  C  CA    . ASN B 1 180 ? 124.844 148.312 125.512 1.00 19.17 ?  180 ASN B CA    1 
ATOM   7035  C  C     . ASN B 1 180 ? 124.871 148.360 127.033 1.00 19.71 ?  180 ASN B C     1 
ATOM   7036  O  O     . ASN B 1 180 ? 125.946 148.369 127.645 1.00 23.44 ?  180 ASN B O     1 
ATOM   7037  C  CB    . ASN B 1 180 ? 124.522 149.694 124.943 1.00 18.93 ?  180 ASN B CB    1 
ATOM   7038  C  CG    . ASN B 1 180 ? 124.976 149.855 123.509 1.00 24.64 ?  180 ASN B CG    1 
ATOM   7039  O  OD1   . ASN B 1 180 ? 125.859 149.138 123.041 1.00 31.55 ?  180 ASN B OD1   1 
ATOM   7040  N  ND2   . ASN B 1 180 ? 124.369 150.798 122.801 1.00 25.83 ?  180 ASN B ND2   1 
ATOM   7041  N  N     . ASP B 1 181 ? 123.694 148.370 127.658 1.00 19.83 ?  181 ASP B N     1 
ATOM   7042  C  CA    . ASP B 1 181 ? 123.623 148.408 129.113 1.00 15.41 ?  181 ASP B CA    1 
ATOM   7043  C  C     . ASP B 1 181 ? 124.135 147.112 129.729 1.00 14.51 ?  181 ASP B C     1 
ATOM   7044  O  O     . ASP B 1 181 ? 124.782 147.138 130.779 1.00 25.19 ?  181 ASP B O     1 
ATOM   7045  C  CB    . ASP B 1 181 ? 122.190 148.693 129.557 1.00 21.97 ?  181 ASP B CB    1 
ATOM   7046  C  CG    . ASP B 1 181 ? 121.751 150.105 129.226 1.00 24.91 ?  181 ASP B CG    1 
ATOM   7047  O  OD1   . ASP B 1 181 ? 122.269 151.050 129.855 1.00 24.60 ?  181 ASP B OD1   1 
ATOM   7048  O  OD2   . ASP B 1 181 ? 120.888 150.271 128.339 1.00 29.14 -1 181 ASP B OD2   1 
ATOM   7049  N  N     . ILE B 1 182 ? 123.861 145.973 129.093 1.00 15.82 ?  182 ILE B N     1 
ATOM   7050  C  CA    . ILE B 1 182 ? 124.357 144.697 129.606 1.00 17.64 ?  182 ILE B CA    1 
ATOM   7051  C  C     . ILE B 1 182 ? 125.880 144.653 129.549 1.00 17.43 ?  182 ILE B C     1 
ATOM   7052  O  O     . ILE B 1 182 ? 126.545 144.236 130.506 1.00 21.16 ?  182 ILE B O     1 
ATOM   7053  C  CB    . ILE B 1 182 ? 123.728 143.528 128.825 1.00 18.63 ?  182 ILE B CB    1 
ATOM   7054  C  CG1   . ILE B 1 182 ? 122.304 143.267 129.317 1.00 15.17 ?  182 ILE B CG1   1 
ATOM   7055  C  CG2   . ILE B 1 182 ? 124.571 142.270 128.957 1.00 20.80 ?  182 ILE B CG2   1 
ATOM   7056  C  CD1   . ILE B 1 182 ? 121.503 142.378 128.403 1.00 16.89 ?  182 ILE B CD1   1 
ATOM   7057  N  N     . SER B 1 183 ? 126.456 145.081 128.423 1.00 17.86 ?  183 SER B N     1 
ATOM   7058  C  CA    . SER B 1 183 ? 127.909 145.102 128.296 1.00 18.73 ?  183 SER B CA    1 
ATOM   7059  C  C     . SER B 1 183 ? 128.536 146.080 129.281 1.00 21.57 ?  183 SER B C     1 
ATOM   7060  O  O     . SER B 1 183 ? 129.579 145.785 129.879 1.00 28.03 ?  183 SER B O     1 
ATOM   7061  C  CB    . SER B 1 183 ? 128.302 145.450 126.863 1.00 15.98 ?  183 SER B CB    1 
ATOM   7062  O  OG    . SER B 1 183 ? 127.769 146.704 126.480 1.00 30.83 ?  183 SER B OG    1 
ATOM   7063  N  N     . ARG B 1 184 ? 127.913 147.246 129.470 1.00 18.88 ?  184 ARG B N     1 
ATOM   7064  C  CA    . ARG B 1 184 ? 128.421 148.196 130.452 1.00 16.57 ?  184 ARG B CA    1 
ATOM   7065  C  C     . ARG B 1 184 ? 128.332 147.630 131.863 1.00 25.25 ?  184 ARG B C     1 
ATOM   7066  O  O     . ARG B 1 184 ? 129.221 147.861 132.685 1.00 29.17 ?  184 ARG B O     1 
ATOM   7067  C  CB    . ARG B 1 184 ? 127.660 149.516 130.356 1.00 15.37 ?  184 ARG B CB    1 
ATOM   7068  C  CG    . ARG B 1 184 ? 128.301 150.639 131.149 1.00 24.71 ?  184 ARG B CG    1 
ATOM   7069  C  CD    . ARG B 1 184 ? 129.748 150.845 130.741 1.00 24.41 ?  184 ARG B CD    1 
ATOM   7070  N  NE    . ARG B 1 184 ? 129.860 151.666 129.543 1.00 31.42 ?  184 ARG B NE    1 
ATOM   7071  C  CZ    . ARG B 1 184 ? 131.005 152.109 129.042 1.00 33.23 ?  184 ARG B CZ    1 
ATOM   7072  N  NH1   . ARG B 1 184 ? 132.164 151.809 129.602 1.00 27.36 1  184 ARG B NH1   1 
ATOM   7073  N  NH2   . ARG B 1 184 ? 130.984 152.871 127.953 1.00 28.64 ?  184 ARG B NH2   1 
ATOM   7074  N  N     . ALA B 1 185 ? 127.260 146.894 132.165 1.00 22.10 ?  185 ALA B N     1 
ATOM   7075  C  CA    . ALA B 1 185 ? 127.135 146.270 133.476 1.00 11.35 ?  185 ALA B CA    1 
ATOM   7076  C  C     . ALA B 1 185 ? 128.221 145.227 133.693 1.00 15.81 ?  185 ALA B C     1 
ATOM   7077  O  O     . ALA B 1 185 ? 128.788 145.133 134.785 1.00 20.15 ?  185 ALA B O     1 
ATOM   7078  C  CB    . ALA B 1 185 ? 125.751 145.642 133.631 1.00 15.68 ?  185 ALA B CB    1 
ATOM   7079  N  N     . ILE B 1 186 ? 128.521 144.434 132.663 1.00 24.17 ?  186 ILE B N     1 
ATOM   7080  C  CA    . ILE B 1 186 ? 129.609 143.462 132.768 1.00 21.97 ?  186 ILE B CA    1 
ATOM   7081  C  C     . ILE B 1 186 ? 130.936 144.172 133.011 1.00 20.56 ?  186 ILE B C     1 
ATOM   7082  O  O     . ILE B 1 186 ? 131.734 143.764 133.869 1.00 26.55 ?  186 ILE B O     1 
ATOM   7083  C  CB    . ILE B 1 186 ? 129.663 142.582 131.505 1.00 26.98 ?  186 ILE B CB    1 
ATOM   7084  C  CG1   . ILE B 1 186 ? 128.409 141.716 131.397 1.00 20.24 ?  186 ILE B CG1   1 
ATOM   7085  C  CG2   . ILE B 1 186 ? 130.908 141.712 131.508 1.00 22.94 ?  186 ILE B CG2   1 
ATOM   7086  C  CD1   . ILE B 1 186 ? 128.120 141.251 129.990 1.00 23.18 ?  186 ILE B CD1   1 
ATOM   7087  N  N     . ASP B 1 187 ? 131.187 145.249 132.263 1.00 22.65 ?  187 ASP B N     1 
ATOM   7088  C  CA    . ASP B 1 187 ? 132.426 146.003 132.429 1.00 21.24 ?  187 ASP B CA    1 
ATOM   7089  C  C     . ASP B 1 187 ? 132.537 146.580 133.836 1.00 23.70 ?  187 ASP B C     1 
ATOM   7090  O  O     . ASP B 1 187 ? 133.587 146.480 134.479 1.00 29.52 ?  187 ASP B O     1 
ATOM   7091  C  CB    . ASP B 1 187 ? 132.500 147.116 131.384 1.00 21.82 ?  187 ASP B CB    1 
ATOM   7092  C  CG    . ASP B 1 187 ? 133.525 148.177 131.730 1.00 30.86 ?  187 ASP B CG    1 
ATOM   7093  O  OD1   . ASP B 1 187 ? 134.697 147.820 131.975 1.00 30.90 ?  187 ASP B OD1   1 
ATOM   7094  O  OD2   . ASP B 1 187 ? 133.160 149.371 131.759 1.00 35.86 -1 187 ASP B OD2   1 
ATOM   7095  N  N     . ILE B 1 188 ? 131.455 147.184 134.332 1.00 21.60 ?  188 ILE B N     1 
ATOM   7096  C  CA    . ILE B 1 188 ? 131.476 147.801 135.654 1.00 19.74 ?  188 ILE B CA    1 
ATOM   7097  C  C     . ILE B 1 188 ? 131.617 146.741 136.738 1.00 21.48 ?  188 ILE B C     1 
ATOM   7098  O  O     . ILE B 1 188 ? 132.284 146.961 137.754 1.00 28.68 ?  188 ILE B O     1 
ATOM   7099  C  CB    . ILE B 1 188 ? 130.219 148.667 135.857 1.00 21.13 ?  188 ILE B CB    1 
ATOM   7100  C  CG1   . ILE B 1 188 ? 130.214 149.840 134.879 1.00 22.43 ?  188 ILE B CG1   1 
ATOM   7101  C  CG2   . ILE B 1 188 ? 130.152 149.197 137.273 1.00 23.49 ?  188 ILE B CG2   1 
ATOM   7102  C  CD1   . ILE B 1 188 ? 128.906 150.594 134.838 1.00 18.85 ?  188 ILE B CD1   1 
ATOM   7103  N  N     . SER B 1 189 ? 130.996 145.575 136.543 1.00 17.21 ?  189 SER B N     1 
ATOM   7104  C  CA    . SER B 1 189 ? 131.154 144.486 137.498 1.00 10.40 ?  189 SER B CA    1 
ATOM   7105  C  C     . SER B 1 189 ? 132.602 144.025 137.566 1.00 22.08 ?  189 SER B C     1 
ATOM   7106  O  O     . SER B 1 189 ? 133.141 143.814 138.658 1.00 23.66 ?  189 SER B O     1 
ATOM   7107  C  CB    . SER B 1 189 ? 130.236 143.324 137.122 1.00 18.67 ?  189 SER B CB    1 
ATOM   7108  O  OG    . SER B 1 189 ? 128.891 143.750 137.028 1.00 25.30 ?  189 SER B OG    1 
ATOM   7109  N  N     . MET B 1 190 ? 133.253 143.871 136.408 1.00 27.49 ?  190 MET B N     1 
ATOM   7110  C  CA    . MET B 1 190 ? 134.666 143.503 136.415 1.00 19.93 ?  190 MET B CA    1 
ATOM   7111  C  C     . MET B 1 190 ? 135.517 144.586 137.067 1.00 19.96 ?  190 MET B C     1 
ATOM   7112  O  O     . MET B 1 190 ? 136.450 144.283 137.817 1.00 24.18 ?  190 MET B O     1 
ATOM   7113  C  CB    . MET B 1 190 ? 135.157 143.222 134.995 1.00 20.87 ?  190 MET B CB    1 
ATOM   7114  C  CG    . MET B 1 190 ? 134.525 142.010 134.345 1.00 22.70 ?  190 MET B CG    1 
ATOM   7115  S  SD    . MET B 1 190 ? 135.329 141.567 132.795 1.00 37.29 ?  190 MET B SD    1 
ATOM   7116  C  CE    . MET B 1 190 ? 134.447 142.613 131.641 1.00 24.55 ?  190 MET B CE    1 
ATOM   7117  N  N     . GLN B 1 191 ? 135.209 145.856 136.794 1.00 19.21 ?  191 GLN B N     1 
ATOM   7118  C  CA    . GLN B 1 191 ? 135.984 146.947 137.375 1.00 23.96 ?  191 GLN B CA    1 
ATOM   7119  C  C     . GLN B 1 191 ? 135.849 146.984 138.892 1.00 23.51 ?  191 GLN B C     1 
ATOM   7120  O  O     . GLN B 1 191 ? 136.835 147.201 139.605 1.00 29.80 ?  191 GLN B O     1 
ATOM   7121  C  CB    . GLN B 1 191 ? 135.551 148.284 136.773 1.00 21.47 ?  191 GLN B CB    1 
ATOM   7122  C  CG    . GLN B 1 191 ? 135.853 148.441 135.293 1.00 20.65 ?  191 GLN B CG    1 
ATOM   7123  C  CD    . GLN B 1 191 ? 137.337 148.428 134.991 1.00 26.80 ?  191 GLN B CD    1 
ATOM   7124  O  OE1   . GLN B 1 191 ? 138.163 148.729 135.852 1.00 30.50 ?  191 GLN B OE1   1 
ATOM   7125  N  NE2   . GLN B 1 191 ? 137.682 148.080 133.758 1.00 25.97 ?  191 GLN B NE2   1 
ATOM   7126  N  N     . LEU B 1 192 ? 134.636 146.779 139.404 1.00 23.86 ?  192 LEU B N     1 
ATOM   7127  C  CA    . LEU B 1 192 ? 134.415 146.843 140.843 1.00 18.39 ?  192 LEU B CA    1 
ATOM   7128  C  C     . LEU B 1 192 ? 134.911 145.597 141.561 1.00 22.39 ?  192 LEU B C     1 
ATOM   7129  O  O     . LEU B 1 192 ? 135.333 145.687 142.719 1.00 33.29 ?  192 LEU B O     1 
ATOM   7130  C  CB    . LEU B 1 192 ? 132.933 147.074 141.137 1.00 19.17 ?  192 LEU B CB    1 
ATOM   7131  C  CG    . LEU B 1 192 ? 132.373 148.430 140.704 1.00 20.72 ?  192 LEU B CG    1 
ATOM   7132  C  CD1   . LEU B 1 192 ? 130.857 148.422 140.750 1.00 20.16 ?  192 LEU B CD1   1 
ATOM   7133  C  CD2   . LEU B 1 192 ? 132.936 149.547 141.565 1.00 21.42 ?  192 LEU B CD2   1 
ATOM   7134  N  N     . SER B 1 193 ? 134.866 144.430 140.911 1.00 19.80 ?  193 SER B N     1 
ATOM   7135  C  CA    . SER B 1 193 ? 135.493 143.248 141.490 1.00 22.09 ?  193 SER B CA    1 
ATOM   7136  C  C     . SER B 1 193 ? 137.008 143.371 141.484 1.00 27.73 ?  193 SER B C     1 
ATOM   7137  O  O     . SER B 1 193 ? 137.677 142.845 142.380 1.00 36.62 ?  193 SER B O     1 
ATOM   7138  C  CB    . SER B 1 193 ? 135.056 141.997 140.735 1.00 24.90 ?  193 SER B CB    1 
ATOM   7139  O  OG    . SER B 1 193 ? 133.666 141.793 140.877 1.00 35.01 ?  193 SER B OG    1 
ATOM   7140  N  N     . LYS B 1 194 ? 137.560 144.051 140.479 1.00 29.29 ?  194 LYS B N     1 
ATOM   7141  C  CA    . LYS B 1 194 ? 138.977 144.389 140.495 1.00 29.16 ?  194 LYS B CA    1 
ATOM   7142  C  C     . LYS B 1 194 ? 139.308 145.273 141.689 1.00 35.14 ?  194 LYS B C     1 
ATOM   7143  O  O     . LYS B 1 194 ? 140.351 145.102 142.331 1.00 39.81 ?  194 LYS B O     1 
ATOM   7144  C  CB    . LYS B 1 194 ? 139.352 145.073 139.181 1.00 26.06 ?  194 LYS B CB    1 
ATOM   7145  C  CG    . LYS B 1 194 ? 140.680 145.797 139.189 1.00 33.46 ?  194 LYS B CG    1 
ATOM   7146  C  CD    . LYS B 1 194 ? 140.814 146.671 137.954 1.00 33.37 ?  194 LYS B CD    1 
ATOM   7147  C  CE    . LYS B 1 194 ? 142.218 147.230 137.818 1.00 34.95 ?  194 LYS B CE    1 
ATOM   7148  N  NZ    . LYS B 1 194 ? 142.344 148.124 136.633 1.00 35.12 1  194 LYS B NZ    1 
ATOM   7149  N  N     . LEU B 1 195 ? 138.423 146.220 142.008 1.00 30.45 ?  195 LEU B N     1 
ATOM   7150  C  CA    . LEU B 1 195 ? 138.584 147.057 143.188 1.00 29.84 ?  195 LEU B CA    1 
ATOM   7151  C  C     . LEU B 1 195 ? 138.335 146.301 144.486 1.00 31.64 ?  195 LEU B C     1 
ATOM   7152  O  O     . LEU B 1 195 ? 138.602 146.848 145.562 1.00 35.04 ?  195 LEU B O     1 
ATOM   7153  C  CB    . LEU B 1 195 ? 137.648 148.263 143.100 1.00 31.01 ?  195 LEU B CB    1 
ATOM   7154  C  CG    . LEU B 1 195 ? 137.943 149.233 141.953 1.00 32.60 ?  195 LEU B CG    1 
ATOM   7155  C  CD1   . LEU B 1 195 ? 136.874 150.308 141.859 1.00 32.68 ?  195 LEU B CD1   1 
ATOM   7156  C  CD2   . LEU B 1 195 ? 139.323 149.853 142.118 1.00 30.72 ?  195 LEU B CD2   1 
ATOM   7157  N  N     . GLY B 1 196 ? 137.826 145.071 144.417 1.00 31.68 ?  196 GLY B N     1 
ATOM   7158  C  CA    . GLY B 1 196 ? 137.645 144.235 145.582 1.00 32.64 ?  196 GLY B CA    1 
ATOM   7159  C  C     . GLY B 1 196 ? 136.241 144.208 146.150 1.00 33.71 ?  196 GLY B C     1 
ATOM   7160  O  O     . GLY B 1 196 ? 135.990 143.445 147.091 1.00 35.13 ?  196 GLY B O     1 
ATOM   7161  N  N     . GLY B 1 197 ? 135.324 145.008 145.615 1.00 30.62 ?  197 GLY B N     1 
ATOM   7162  C  CA    . GLY B 1 197 ? 133.994 145.083 146.181 1.00 26.25 ?  197 GLY B CA    1 
ATOM   7163  C  C     . GLY B 1 197 ? 133.042 144.057 145.597 1.00 22.65 ?  197 GLY B C     1 
ATOM   7164  O  O     . GLY B 1 197 ? 133.142 143.660 144.438 1.00 27.65 ?  197 GLY B O     1 
ATOM   7165  N  N     . GLY B 1 198 ? 132.097 143.624 146.429 1.00 19.98 ?  198 GLY B N     1 
ATOM   7166  C  CA    . GLY B 1 198 ? 131.044 142.735 145.971 1.00 16.72 ?  198 GLY B CA    1 
ATOM   7167  C  C     . GLY B 1 198 ? 130.006 143.514 145.185 1.00 17.83 ?  198 GLY B C     1 
ATOM   7168  O  O     . GLY B 1 198 ? 129.541 144.571 145.623 1.00 21.91 ?  198 GLY B O     1 
ATOM   7169  N  N     . VAL B 1 199 ? 129.640 142.992 144.019 1.00 20.11 ?  199 VAL B N     1 
ATOM   7170  C  CA    . VAL B 1 199 ? 128.776 143.690 143.074 1.00 12.78 ?  199 VAL B CA    1 
ATOM   7171  C  C     . VAL B 1 199 ? 127.438 142.971 143.009 1.00 7.15  ?  199 VAL B C     1 
ATOM   7172  O  O     . VAL B 1 199 ? 127.390 141.750 142.830 1.00 15.02 ?  199 VAL B O     1 
ATOM   7173  C  CB    . VAL B 1 199 ? 129.419 143.772 141.680 1.00 13.70 ?  199 VAL B CB    1 
ATOM   7174  C  CG1   . VAL B 1 199 ? 128.573 144.623 140.754 1.00 16.53 ?  199 VAL B CG1   1 
ATOM   7175  C  CG2   . VAL B 1 199 ? 130.831 144.314 141.780 1.00 11.69 ?  199 VAL B CG2   1 
ATOM   7176  N  N     . SER B 1 200 ? 126.355 143.729 143.151 1.00 13.20 ?  200 SER B N     1 
ATOM   7177  C  CA    . SER B 1 200 ? 125.001 143.222 142.998 1.00 3.98  ?  200 SER B CA    1 
ATOM   7178  C  C     . SER B 1 200 ? 124.346 143.907 141.808 1.00 13.16 ?  200 SER B C     1 
ATOM   7179  O  O     . SER B 1 200 ? 124.462 145.124 141.641 1.00 23.38 ?  200 SER B O     1 
ATOM   7180  C  CB    . SER B 1 200 ? 124.174 143.458 144.264 1.00 10.36 ?  200 SER B CB    1 
ATOM   7181  O  OG    . SER B 1 200 ? 123.014 142.649 144.272 1.00 15.93 ?  200 SER B OG    1 
ATOM   7182  N  N     . LEU B 1 201 ? 123.667 143.123 140.977 1.00 15.98 ?  201 LEU B N     1 
ATOM   7183  C  CA    . LEU B 1 201 ? 123.045 143.624 139.760 1.00 8.21  ?  201 LEU B CA    1 
ATOM   7184  C  C     . LEU B 1 201 ? 121.568 143.267 139.751 1.00 7.83  ?  201 LEU B C     1 
ATOM   7185  O  O     . LEU B 1 201 ? 121.203 142.109 139.976 1.00 14.96 ?  201 LEU B O     1 
ATOM   7186  C  CB    . LEU B 1 201 ? 123.733 143.057 138.518 1.00 14.50 ?  201 LEU B CB    1 
ATOM   7187  C  CG    . LEU B 1 201 ? 125.234 143.325 138.413 1.00 19.27 ?  201 LEU B CG    1 
ATOM   7188  C  CD1   . LEU B 1 201 ? 126.025 142.061 138.711 1.00 16.44 ?  201 LEU B CD1   1 
ATOM   7189  C  CD2   . LEU B 1 201 ? 125.583 143.876 137.042 1.00 17.08 ?  201 LEU B CD2   1 
ATOM   7190  N  N     . ASN B 1 202 ? 120.728 144.261 139.478 1.00 13.30 ?  202 ASN B N     1 
ATOM   7191  C  CA    . ASN B 1 202 ? 119.292 144.060 139.339 1.00 4.34  ?  202 ASN B CA    1 
ATOM   7192  C  C     . ASN B 1 202 ? 119.001 143.681 137.893 1.00 19.44 ?  202 ASN B C     1 
ATOM   7193  O  O     . ASN B 1 202 ? 119.180 144.494 136.981 1.00 25.78 ?  202 ASN B O     1 
ATOM   7194  C  CB    . ASN B 1 202 ? 118.529 145.318 139.743 1.00 8.57  ?  202 ASN B CB    1 
ATOM   7195  C  CG    . ASN B 1 202 ? 117.061 145.052 140.002 1.00 9.79  ?  202 ASN B CG    1 
ATOM   7196  O  OD1   . ASN B 1 202 ? 116.665 143.924 140.290 1.00 17.92 ?  202 ASN B OD1   1 
ATOM   7197  N  ND2   . ASN B 1 202 ? 116.244 146.092 139.899 1.00 12.16 ?  202 ASN B ND2   1 
ATOM   7198  N  N     . LEU B 1 203 ? 118.553 142.445 137.681 1.00 12.94 ?  203 LEU B N     1 
ATOM   7199  C  CA    . LEU B 1 203 ? 118.250 141.942 136.351 1.00 9.62  ?  203 LEU B CA    1 
ATOM   7200  C  C     . LEU B 1 203 ? 116.761 141.974 136.038 1.00 12.21 ?  203 LEU B C     1 
ATOM   7201  O  O     . LEU B 1 203 ? 116.336 141.384 135.040 1.00 17.15 ?  203 LEU B O     1 
ATOM   7202  C  CB    . LEU B 1 203 ? 118.789 140.519 136.194 1.00 15.46 ?  203 LEU B CB    1 
ATOM   7203  C  CG    . LEU B 1 203 ? 120.276 140.319 136.498 1.00 15.40 ?  203 LEU B CG    1 
ATOM   7204  C  CD1   . LEU B 1 203 ? 120.724 138.934 136.073 1.00 14.42 ?  203 LEU B CD1   1 
ATOM   7205  C  CD2   . LEU B 1 203 ? 121.119 141.386 135.821 1.00 15.77 ?  203 LEU B CD2   1 
ATOM   7206  N  N     . SER B 1 204 ? 115.961 142.654 136.862 1.00 15.54 ?  204 SER B N     1 
ATOM   7207  C  CA    . SER B 1 204 ? 114.516 142.656 136.681 1.00 10.71 ?  204 SER B CA    1 
ATOM   7208  C  C     . SER B 1 204 ? 114.068 143.483 135.484 1.00 20.34 ?  204 SER B C     1 
ATOM   7209  O  O     . SER B 1 204 ? 112.980 143.236 134.953 1.00 23.52 ?  204 SER B O     1 
ATOM   7210  C  CB    . SER B 1 204 ? 113.831 143.177 137.945 1.00 8.35  ?  204 SER B CB    1 
ATOM   7211  O  OG    . SER B 1 204 ? 114.215 142.418 139.077 1.00 20.64 ?  204 SER B OG    1 
ATOM   7212  N  N     . LYS B 1 205 ? 114.871 144.454 135.052 1.00 22.11 ?  205 LYS B N     1 
ATOM   7213  C  CA    . LYS B 1 205 ? 114.521 145.240 133.877 1.00 16.32 ?  205 LYS B CA    1 
ATOM   7214  C  C     . LYS B 1 205 ? 114.814 144.509 132.576 1.00 15.37 ?  205 LYS B C     1 
ATOM   7215  O  O     . LYS B 1 205 ? 114.177 144.807 131.560 1.00 26.69 ?  205 LYS B O     1 
ATOM   7216  C  CB    . LYS B 1 205 ? 115.262 146.577 133.895 1.00 18.23 ?  205 LYS B CB    1 
ATOM   7217  C  CG    . LYS B 1 205 ? 114.755 147.536 134.954 1.00 15.88 ?  205 LYS B CG    1 
ATOM   7218  C  CD    . LYS B 1 205 ? 115.472 148.868 134.884 1.00 21.18 ?  205 LYS B CD    1 
ATOM   7219  C  CE    . LYS B 1 205 ? 114.769 149.909 135.734 1.00 24.74 ?  205 LYS B CE    1 
ATOM   7220  N  NZ    . LYS B 1 205 ? 114.714 149.512 137.167 1.00 17.90 1  205 LYS B NZ    1 
ATOM   7221  N  N     . LEU B 1 206 ? 115.754 143.568 132.584 1.00 19.58 ?  206 LEU B N     1 
ATOM   7222  C  CA    . LEU B 1 206 ? 116.052 142.791 131.390 1.00 19.72 ?  206 LEU B CA    1 
ATOM   7223  C  C     . LEU B 1 206 ? 114.841 141.965 130.982 1.00 20.06 ?  206 LEU B C     1 
ATOM   7224  O  O     . LEU B 1 206 ? 114.204 141.319 131.821 1.00 24.64 ?  206 LEU B O     1 
ATOM   7225  C  CB    . LEU B 1 206 ? 117.250 141.879 131.639 1.00 19.51 ?  206 LEU B CB    1 
ATOM   7226  C  CG    . LEU B 1 206 ? 118.526 142.561 132.125 1.00 18.70 ?  206 LEU B CG    1 
ATOM   7227  C  CD1   . LEU B 1 206 ? 119.575 141.523 132.465 1.00 19.93 ?  206 LEU B CD1   1 
ATOM   7228  C  CD2   . LEU B 1 206 ? 119.042 143.521 131.073 1.00 22.12 ?  206 LEU B CD2   1 
ATOM   7229  N  N     . ARG B 1 207 ? 114.522 141.986 129.692 1.00 26.04 ?  207 ARG B N     1 
ATOM   7230  C  CA    . ARG B 1 207 ? 113.369 141.242 129.211 1.00 23.84 ?  207 ARG B CA    1 
ATOM   7231  C  C     . ARG B 1 207 ? 113.632 139.742 129.274 1.00 25.07 ?  207 ARG B C     1 
ATOM   7232  O  O     . ARG B 1 207 ? 114.770 139.279 129.160 1.00 30.59 ?  207 ARG B O     1 
ATOM   7233  C  CB    . ARG B 1 207 ? 113.009 141.666 127.787 1.00 22.30 ?  207 ARG B CB    1 
ATOM   7234  C  CG    . ARG B 1 207 ? 114.112 141.521 126.762 1.00 26.52 ?  207 ARG B CG    1 
ATOM   7235  C  CD    . ARG B 1 207 ? 113.706 142.189 125.459 1.00 24.61 ?  207 ARG B CD    1 
ATOM   7236  N  NE    . ARG B 1 207 ? 113.964 143.623 125.473 1.00 25.92 ?  207 ARG B NE    1 
ATOM   7237  C  CZ    . ARG B 1 207 ? 114.135 144.364 124.387 1.00 23.22 ?  207 ARG B CZ    1 
ATOM   7238  N  NH1   . ARG B 1 207 ? 114.064 143.840 123.174 1.00 26.34 1  207 ARG B NH1   1 
ATOM   7239  N  NH2   . ARG B 1 207 ? 114.384 145.663 124.521 1.00 20.80 ?  207 ARG B NH2   1 
ATOM   7240  N  N     . ALA B 1 208 ? 112.557 138.984 129.462 1.00 29.42 ?  208 ALA B N     1 
ATOM   7241  C  CA    . ALA B 1 208 ? 112.663 137.557 129.713 1.00 21.81 ?  208 ALA B CA    1 
ATOM   7242  C  C     . ALA B 1 208 ? 113.035 136.802 128.440 1.00 28.96 ?  208 ALA B C     1 
ATOM   7243  O  O     . ALA B 1 208 ? 113.165 137.370 127.353 1.00 34.82 ?  208 ALA B O     1 
ATOM   7244  C  CB    . ALA B 1 208 ? 111.353 137.021 130.285 1.00 23.95 ?  208 ALA B CB    1 
ATOM   7245  N  N     . LYS B 1 209 ? 113.217 135.493 128.596 1.00 28.19 ?  209 LYS B N     1 
ATOM   7246  C  CA    . LYS B 1 209 ? 113.514 134.634 127.461 1.00 24.45 ?  209 LYS B CA    1 
ATOM   7247  C  C     . LYS B 1 209 ? 112.313 134.557 126.527 1.00 31.93 ?  209 LYS B C     1 
ATOM   7248  O  O     . LYS B 1 209 ? 111.163 134.494 126.970 1.00 34.54 ?  209 LYS B O     1 
ATOM   7249  C  CB    . LYS B 1 209 ? 113.900 133.235 127.942 1.00 27.07 ?  209 LYS B CB    1 
ATOM   7250  C  CG    . LYS B 1 209 ? 114.576 132.380 126.884 1.00 32.28 ?  209 LYS B CG    1 
ATOM   7251  C  CD    . LYS B 1 209 ? 115.328 131.219 127.512 1.00 29.21 ?  209 LYS B CD    1 
ATOM   7252  C  CE    . LYS B 1 209 ? 114.376 130.152 128.025 1.00 32.67 ?  209 LYS B CE    1 
ATOM   7253  N  NZ    . LYS B 1 209 ? 113.176 130.010 127.155 1.00 33.89 1  209 LYS B NZ    1 
ATOM   7254  N  N     . GLY B 1 210 ? 112.587 134.561 125.226 1.00 35.25 ?  210 GLY B N     1 
ATOM   7255  C  CA    . GLY B 1 210 ? 111.524 134.516 124.245 1.00 34.69 ?  210 GLY B CA    1 
ATOM   7256  C  C     . GLY B 1 210 ? 110.881 135.849 123.944 1.00 35.24 ?  210 GLY B C     1 
ATOM   7257  O  O     . GLY B 1 210 ? 109.721 135.886 123.519 1.00 38.95 ?  210 GLY B O     1 
ATOM   7258  N  N     . GLU B 1 211 ? 111.595 136.948 124.154 1.00 33.78 ?  211 GLU B N     1 
ATOM   7259  C  CA    . GLU B 1 211 ? 111.104 138.273 123.815 1.00 33.10 ?  211 GLU B CA    1 
ATOM   7260  C  C     . GLU B 1 211 ? 111.732 138.749 122.508 1.00 37.21 ?  211 GLU B C     1 
ATOM   7261  O  O     . GLU B 1 211 ? 112.666 138.145 121.977 1.00 40.01 ?  211 GLU B O     1 
ATOM   7262  C  CB    . GLU B 1 211 ? 111.386 139.264 124.947 1.00 31.64 ?  211 GLU B CB    1 
ATOM   7263  C  CG    . GLU B 1 211 ? 110.641 138.947 126.230 1.00 33.93 ?  211 GLU B CG    1 
ATOM   7264  C  CD    . GLU B 1 211 ? 109.767 140.092 126.697 1.00 36.00 ?  211 GLU B CD    1 
ATOM   7265  O  OE1   . GLU B 1 211 ? 108.833 140.467 125.959 1.00 39.65 ?  211 GLU B OE1   1 
ATOM   7266  O  OE2   . GLU B 1 211 ? 110.002 140.609 127.808 1.00 32.33 -1 211 GLU B OE2   1 
ATOM   7267  N  N     . ALA B 1 212 ? 111.202 139.854 121.993 1.00 38.34 ?  212 ALA B N     1 
ATOM   7268  C  CA    . ALA B 1 212 ? 111.573 140.347 120.675 1.00 35.63 ?  212 ALA B CA    1 
ATOM   7269  C  C     . ALA B 1 212 ? 112.659 141.412 120.779 1.00 41.57 ?  212 ALA B C     1 
ATOM   7270  O  O     . ALA B 1 212 ? 112.561 142.331 121.598 1.00 44.34 ?  212 ALA B O     1 
ATOM   7271  C  CB    . ALA B 1 212 ? 110.351 140.913 119.952 1.00 38.46 ?  212 ALA B CB    1 
ATOM   7272  N  N     . ILE B 1 213 ? 113.690 141.277 119.950 1.00 40.74 ?  213 ILE B N     1 
ATOM   7273  C  CA    . ILE B 1 213 ? 114.720 142.296 119.788 1.00 43.49 ?  213 ILE B CA    1 
ATOM   7274  C  C     . ILE B 1 213 ? 114.482 142.948 118.431 1.00 41.50 ?  213 ILE B C     1 
ATOM   7275  O  O     . ILE B 1 213 ? 114.973 142.468 117.407 1.00 44.98 ?  213 ILE B O     1 
ATOM   7276  C  CB    . ILE B 1 213 ? 116.129 141.706 119.892 1.00 41.22 ?  213 ILE B CB    1 
ATOM   7277  C  CG1   . ILE B 1 213 ? 116.267 140.871 121.162 1.00 41.47 ?  213 ILE B CG1   1 
ATOM   7278  C  CG2   . ILE B 1 213 ? 117.172 142.812 119.862 1.00 38.15 ?  213 ILE B CG2   1 
ATOM   7279  C  CD1   . ILE B 1 213 ? 117.343 139.818 121.081 1.00 41.34 ?  213 ILE B CD1   1 
ATOM   7280  N  N     . LYS B 1 214 ? 113.737 144.051 118.426 1.00 46.02 ?  214 LYS B N     1 
ATOM   7281  C  CA    . LYS B 1 214 ? 113.370 144.770 117.205 1.00 46.63 ?  214 LYS B CA    1 
ATOM   7282  C  C     . LYS B 1 214 ? 112.596 143.871 116.239 1.00 52.94 ?  214 LYS B C     1 
ATOM   7283  O  O     . LYS B 1 214 ? 113.057 143.534 115.145 1.00 55.44 ?  214 LYS B O     1 
ATOM   7284  C  CB    . LYS B 1 214 ? 114.600 145.377 116.526 1.00 48.06 ?  214 LYS B CB    1 
ATOM   7285  C  CG    . LYS B 1 214 ? 114.775 146.863 116.792 1.00 49.74 ?  214 LYS B CG    1 
ATOM   7286  C  CD    . LYS B 1 214 ? 116.235 147.278 116.742 1.00 49.95 ?  214 LYS B CD    1 
ATOM   7287  C  CE    . LYS B 1 214 ? 116.998 146.523 115.664 1.00 48.13 ?  214 LYS B CE    1 
ATOM   7288  N  NZ    . LYS B 1 214 ? 118.460 146.484 115.940 1.00 51.60 1  214 LYS B NZ    1 
ATOM   7289  N  N     . ASP B 1 215 ? 111.411 143.456 116.694 1.00 54.72 ?  215 ASP B N     1 
ATOM   7290  C  CA    . ASP B 1 215 ? 110.368 142.872 115.854 1.00 56.27 ?  215 ASP B CA    1 
ATOM   7291  C  C     . ASP B 1 215 ? 110.650 141.436 115.419 1.00 55.86 ?  215 ASP B C     1 
ATOM   7292  O  O     . ASP B 1 215 ? 109.812 140.822 114.752 1.00 57.90 ?  215 ASP B O     1 
ATOM   7293  C  CB    . ASP B 1 215 ? 110.125 143.748 114.620 1.00 56.75 ?  215 ASP B CB    1 
ATOM   7294  C  CG    . ASP B 1 215 ? 109.221 144.929 114.913 1.00 58.77 ?  215 ASP B CG    1 
ATOM   7295  O  OD1   . ASP B 1 215 ? 108.013 144.712 115.141 1.00 57.83 ?  215 ASP B OD1   1 
ATOM   7296  O  OD2   . ASP B 1 215 ? 109.720 146.074 114.919 1.00 57.94 -1 215 ASP B OD2   1 
ATOM   7297  N  N     . VAL B 1 216 ? 111.806 140.884 115.781 1.00 49.80 ?  216 VAL B N     1 
ATOM   7298  C  CA    . VAL B 1 216 ? 112.053 139.457 115.577 1.00 49.24 ?  216 VAL B CA    1 
ATOM   7299  C  C     . VAL B 1 216 ? 111.819 138.780 116.926 1.00 51.37 ?  216 VAL B C     1 
ATOM   7300  O  O     . VAL B 1 216 ? 112.477 139.095 117.919 1.00 54.49 ?  216 VAL B O     1 
ATOM   7301  C  CB    . VAL B 1 216 ? 113.453 139.178 115.018 1.00 49.43 ?  216 VAL B CB    1 
ATOM   7302  C  CG1   . VAL B 1 216 ? 114.365 140.371 115.218 1.00 48.26 ?  216 VAL B CG1   1 
ATOM   7303  C  CG2   . VAL B 1 216 ? 114.054 137.904 115.614 1.00 49.08 ?  216 VAL B CG2   1 
ATOM   7304  N  N     . GLU B 1 217 ? 110.852 137.867 116.969 1.00 49.49 ?  217 GLU B N     1 
ATOM   7305  C  CA    . GLU B 1 217 ? 110.357 137.347 118.233 1.00 48.12 ?  217 GLU B CA    1 
ATOM   7306  C  C     . GLU B 1 217 ? 111.150 136.116 118.668 1.00 47.97 ?  217 GLU B C     1 
ATOM   7307  O  O     . GLU B 1 217 ? 111.876 135.494 117.887 1.00 49.55 ?  217 GLU B O     1 
ATOM   7308  C  CB    . GLU B 1 217 ? 108.872 137.008 118.120 1.00 49.89 ?  217 GLU B CB    1 
ATOM   7309  C  CG    . GLU B 1 217 ? 108.040 138.104 117.475 1.00 50.43 ?  217 GLU B CG    1 
ATOM   7310  C  CD    . GLU B 1 217 ? 107.644 139.189 118.455 1.00 53.17 ?  217 GLU B CD    1 
ATOM   7311  O  OE1   . GLU B 1 217 ? 107.669 138.926 119.676 1.00 52.28 ?  217 GLU B OE1   1 
ATOM   7312  O  OE2   . GLU B 1 217 ? 107.309 140.305 118.006 1.00 49.00 -1 217 GLU B OE2   1 
ATOM   7313  N  N     . ASN B 1 218 ? 110.988 135.767 119.944 1.00 43.64 ?  218 ASN B N     1 
ATOM   7314  C  CA    . ASN B 1 218 ? 111.652 134.617 120.559 1.00 41.92 ?  218 ASN B CA    1 
ATOM   7315  C  C     . ASN B 1 218 ? 113.159 134.675 120.336 1.00 45.22 ?  218 ASN B C     1 
ATOM   7316  O  O     . ASN B 1 218 ? 113.808 133.689 119.980 1.00 46.74 ?  218 ASN B O     1 
ATOM   7317  C  CB    . ASN B 1 218 ? 111.066 133.305 120.041 1.00 43.14 ?  218 ASN B CB    1 
ATOM   7318  C  CG    . ASN B 1 218 ? 110.036 132.719 120.983 1.00 46.85 ?  218 ASN B CG    1 
ATOM   7319  O  OD1   . ASN B 1 218 ? 109.018 133.346 121.277 1.00 45.77 ?  218 ASN B OD1   1 
ATOM   7320  N  ND2   . ASN B 1 218 ? 110.297 131.511 121.468 1.00 48.32 ?  218 ASN B ND2   1 
ATOM   7321  N  N     . ALA B 1 219 ? 113.720 135.859 120.560 1.00 37.53 ?  219 ALA B N     1 
ATOM   7322  C  CA    . ALA B 1 219 ? 115.120 136.137 120.271 1.00 35.07 ?  219 ALA B CA    1 
ATOM   7323  C  C     . ALA B 1 219 ? 115.983 136.289 121.513 1.00 37.31 ?  219 ALA B C     1 
ATOM   7324  O  O     . ALA B 1 219 ? 117.167 135.951 121.476 1.00 35.41 ?  219 ALA B O     1 
ATOM   7325  C  CB    . ALA B 1 219 ? 115.231 137.409 119.425 1.00 36.43 ?  219 ALA B CB    1 
ATOM   7326  N  N     . THR B 1 220 ? 115.424 136.789 122.609 1.00 34.97 ?  220 THR B N     1 
ATOM   7327  C  CA    . THR B 1 220 ? 116.211 137.056 123.803 1.00 31.02 ?  220 THR B CA    1 
ATOM   7328  C  C     . THR B 1 220 ? 116.578 135.764 124.521 1.00 34.50 ?  220 THR B C     1 
ATOM   7329  O  O     . THR B 1 220 ? 115.816 134.794 124.535 1.00 35.03 ?  220 THR B O     1 
ATOM   7330  C  CB    . THR B 1 220 ? 115.448 137.971 124.760 1.00 32.28 ?  220 THR B CB    1 
ATOM   7331  O  OG1   . THR B 1 220 ? 114.285 137.292 125.250 1.00 38.26 ?  220 THR B OG1   1 
ATOM   7332  C  CG2   . THR B 1 220 ? 115.018 139.229 124.045 1.00 32.74 ?  220 THR B CG2   1 
ATOM   7333  N  N     . LYS B 1 221 ? 117.768 135.765 125.119 1.00 32.78 ?  221 LYS B N     1 
ATOM   7334  C  CA    . LYS B 1 221 ? 118.207 134.670 125.970 1.00 29.71 ?  221 LYS B CA    1 
ATOM   7335  C  C     . LYS B 1 221 ? 117.685 134.787 127.394 1.00 31.82 ?  221 LYS B C     1 
ATOM   7336  O  O     . LYS B 1 221 ? 117.886 133.863 128.189 1.00 34.84 ?  221 LYS B O     1 
ATOM   7337  C  CB    . LYS B 1 221 ? 119.737 134.601 125.997 1.00 29.40 ?  221 LYS B CB    1 
ATOM   7338  C  CG    . LYS B 1 221 ? 120.350 134.101 124.708 1.00 30.09 ?  221 LYS B CG    1 
ATOM   7339  C  CD    . LYS B 1 221 ? 121.475 133.121 124.985 1.00 32.86 ?  221 LYS B CD    1 
ATOM   7340  C  CE    . LYS B 1 221 ? 121.950 132.464 123.705 1.00 35.04 ?  221 LYS B CE    1 
ATOM   7341  N  NZ    . LYS B 1 221 ? 120.957 132.622 122.607 1.00 32.52 1  221 LYS B NZ    1 
ATOM   7342  N  N     . GLY B 1 222 ? 117.025 135.889 127.730 1.00 31.02 ?  222 GLY B N     1 
ATOM   7343  C  CA    . GLY B 1 222 ? 116.524 136.085 129.067 1.00 27.64 ?  222 GLY B CA    1 
ATOM   7344  C  C     . GLY B 1 222 ? 117.611 136.516 130.032 1.00 28.06 ?  222 GLY B C     1 
ATOM   7345  O  O     . GLY B 1 222 ? 118.733 136.867 129.653 1.00 31.31 ?  222 GLY B O     1 
ATOM   7346  N  N     . VAL B 1 223 ? 117.257 136.486 131.317 1.00 27.28 ?  223 VAL B N     1 
ATOM   7347  C  CA    . VAL B 1 223 ? 118.208 136.876 132.350 1.00 25.17 ?  223 VAL B CA    1 
ATOM   7348  C  C     . VAL B 1 223 ? 119.257 135.802 132.586 1.00 20.16 ?  223 VAL B C     1 
ATOM   7349  O  O     . VAL B 1 223 ? 120.279 136.078 133.217 1.00 26.46 ?  223 VAL B O     1 
ATOM   7350  C  CB    . VAL B 1 223 ? 117.479 137.218 133.663 1.00 21.99 ?  223 VAL B CB    1 
ATOM   7351  C  CG1   . VAL B 1 223 ? 116.280 138.109 133.389 1.00 22.24 ?  223 VAL B CG1   1 
ATOM   7352  C  CG2   . VAL B 1 223 ? 117.060 135.950 134.393 1.00 22.98 ?  223 VAL B CG2   1 
ATOM   7353  N  N     . VAL B 1 224 ? 119.036 134.579 132.101 1.00 24.17 ?  224 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 224 ? 120.008 133.510 132.316 1.00 22.49 ?  224 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 224 ? 121.274 133.730 131.490 1.00 26.27 ?  224 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 224 ? 122.382 133.450 131.962 1.00 30.84 ?  224 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 224 ? 119.363 132.146 132.020 1.00 27.68 ?  224 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 224 ? 120.402 131.037 132.066 1.00 27.23 ?  224 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 224 ? 118.252 131.871 133.016 1.00 26.03 ?  224 VAL B CG2   1 
ATOM   7360  N  N     . GLY B 1 225 ? 121.147 134.227 130.258 1.00 22.82 ?  225 GLY B N     1 
ATOM   7361  C  CA    . GLY B 1 225 ? 122.334 134.536 129.476 1.00 18.39 ?  225 GLY B CA    1 
ATOM   7362  C  C     . GLY B 1 225 ? 123.162 135.648 130.093 1.00 21.88 ?  225 GLY B C     1 
ATOM   7363  O  O     . GLY B 1 225 ? 124.392 135.556 130.167 1.00 34.08 ?  225 GLY B O     1 
ATOM   7364  N  N     . VAL B 1 226 ? 122.497 136.710 130.552 1.00 19.13 ?  226 VAL B N     1 
ATOM   7365  C  CA    . VAL B 1 226 ? 123.194 137.778 131.258 1.00 19.93 ?  226 VAL B CA    1 
ATOM   7366  C  C     . VAL B 1 226 ? 123.803 137.251 132.545 1.00 19.06 ?  226 VAL B C     1 
ATOM   7367  O  O     . VAL B 1 226 ? 124.881 137.688 132.959 1.00 23.03 ?  226 VAL B O     1 
ATOM   7368  C  CB    . VAL B 1 226 ? 122.238 138.955 131.527 1.00 17.08 ?  226 VAL B CB    1 
ATOM   7369  C  CG1   . VAL B 1 226 ? 123.020 140.193 131.940 1.00 22.26 ?  226 VAL B CG1   1 
ATOM   7370  C  CG2   . VAL B 1 226 ? 121.392 139.233 130.303 1.00 16.72 ?  226 VAL B CG2   1 
ATOM   7371  N  N     . MET B 1 227 ? 123.124 136.308 133.201 1.00 22.71 ?  227 MET B N     1 
ATOM   7372  C  CA    . MET B 1 227 ? 123.668 135.686 134.401 1.00 21.23 ?  227 MET B CA    1 
ATOM   7373  C  C     . MET B 1 227 ? 124.955 134.936 134.098 1.00 21.57 ?  227 MET B C     1 
ATOM   7374  O  O     . MET B 1 227 ? 125.918 135.011 134.864 1.00 27.55 ?  227 MET B O     1 
ATOM   7375  C  CB    . MET B 1 227 ? 122.634 134.739 135.005 1.00 20.01 ?  227 MET B CB    1 
ATOM   7376  C  CG    . MET B 1 227 ? 121.688 135.390 135.982 1.00 16.03 ?  227 MET B CG    1 
ATOM   7377  S  SD    . MET B 1 227 ? 120.632 134.161 136.757 1.00 40.04 ?  227 MET B SD    1 
ATOM   7378  C  CE    . MET B 1 227 ? 121.375 134.107 138.376 1.00 24.27 ?  227 MET B CE    1 
ATOM   7379  N  N     . LYS B 1 228 ? 124.983 134.194 132.991 1.00 22.19 ?  228 LYS B N     1 
ATOM   7380  C  CA    . LYS B 1 228 ? 126.200 133.485 132.603 1.00 22.43 ?  228 LYS B CA    1 
ATOM   7381  C  C     . LYS B 1 228 ? 127.322 134.462 132.273 1.00 22.93 ?  228 LYS B C     1 
ATOM   7382  O  O     . LYS B 1 228 ? 128.482 134.244 132.653 1.00 23.93 ?  228 LYS B O     1 
ATOM   7383  C  CB    . LYS B 1 228 ? 125.917 132.573 131.411 1.00 24.69 ?  228 LYS B CB    1 
ATOM   7384  C  CG    . LYS B 1 228 ? 125.605 131.140 131.788 1.00 29.35 ?  228 LYS B CG    1 
ATOM   7385  C  CD    . LYS B 1 228 ? 124.202 130.763 131.351 1.00 29.88 ?  228 LYS B CD    1 
ATOM   7386  C  CE    . LYS B 1 228 ? 124.039 130.912 129.848 1.00 33.12 ?  228 LYS B CE    1 
ATOM   7387  N  NZ    . LYS B 1 228 ? 122.824 130.214 129.346 1.00 34.24 1  228 LYS B NZ    1 
ATOM   7388  N  N     . LEU B 1 229 ? 126.992 135.547 131.567 1.00 22.47 ?  229 LEU B N     1 
ATOM   7389  C  CA    . LEU B 1 229 ? 127.995 136.562 131.259 1.00 20.86 ?  229 LEU B CA    1 
ATOM   7390  C  C     . LEU B 1 229 ? 128.568 137.168 132.533 1.00 19.28 ?  229 LEU B C     1 
ATOM   7391  O  O     . LEU B 1 229 ? 129.787 137.327 132.667 1.00 25.07 ?  229 LEU B O     1 
ATOM   7392  C  CB    . LEU B 1 229 ? 127.386 137.656 130.384 1.00 23.23 ?  229 LEU B CB    1 
ATOM   7393  C  CG    . LEU B 1 229 ? 126.884 137.275 128.997 1.00 19.52 ?  229 LEU B CG    1 
ATOM   7394  C  CD1   . LEU B 1 229 ? 125.790 138.238 128.581 1.00 20.88 ?  229 LEU B CD1   1 
ATOM   7395  C  CD2   . LEU B 1 229 ? 128.027 137.288 128.000 1.00 17.63 ?  229 LEU B CD2   1 
ATOM   7396  N  N     . LEU B 1 230 ? 127.698 137.508 133.485 1.00 21.75 ?  230 LEU B N     1 
ATOM   7397  C  CA    . LEU B 1 230 ? 128.150 138.087 134.744 1.00 17.81 ?  230 LEU B CA    1 
ATOM   7398  C  C     . LEU B 1 230 ? 128.957 137.084 135.554 1.00 17.83 ?  230 LEU B C     1 
ATOM   7399  O  O     . LEU B 1 230 ? 129.931 137.455 136.215 1.00 28.53 ?  230 LEU B O     1 
ATOM   7400  C  CB    . LEU B 1 230 ? 126.953 138.589 135.549 1.00 19.03 ?  230 LEU B CB    1 
ATOM   7401  C  CG    . LEU B 1 230 ? 126.244 139.830 135.006 1.00 23.50 ?  230 LEU B CG    1 
ATOM   7402  C  CD1   . LEU B 1 230 ? 124.914 140.031 135.712 1.00 24.96 ?  230 LEU B CD1   1 
ATOM   7403  C  CD2   . LEU B 1 230 ? 127.127 141.056 135.156 1.00 20.05 ?  230 LEU B CD2   1 
ATOM   7404  N  N     . ASP B 1 231 ? 128.562 135.812 135.526 1.00 21.74 ?  231 ASP B N     1 
ATOM   7405  C  CA    . ASP B 1 231 ? 129.312 134.783 136.235 1.00 24.81 ?  231 ASP B CA    1 
ATOM   7406  C  C     . ASP B 1 231 ? 130.723 134.656 135.680 1.00 26.22 ?  231 ASP B C     1 
ATOM   7407  O  O     . ASP B 1 231 ? 131.693 134.575 136.443 1.00 32.42 ?  231 ASP B O     1 
ATOM   7408  C  CB    . ASP B 1 231 ? 128.573 133.449 136.143 1.00 26.44 ?  231 ASP B CB    1 
ATOM   7409  C  CG    . ASP B 1 231 ? 129.305 132.328 136.846 1.00 35.82 ?  231 ASP B CG    1 
ATOM   7410  O  OD1   . ASP B 1 231 ? 129.697 132.518 138.014 1.00 38.60 ?  231 ASP B OD1   1 
ATOM   7411  O  OD2   . ASP B 1 231 ? 129.489 131.258 136.230 1.00 35.57 -1 231 ASP B OD2   1 
ATOM   7412  N  N     . ASN B 1 232 ? 130.860 134.657 134.353 1.00 29.25 ?  232 ASN B N     1 
ATOM   7413  C  CA    . ASN B 1 232 ? 132.193 134.612 133.759 1.00 26.54 ?  232 ASN B CA    1 
ATOM   7414  C  C     . ASN B 1 232 ? 132.979 135.882 134.054 1.00 23.51 ?  232 ASN B C     1 
ATOM   7415  O  O     . ASN B 1 232 ? 134.197 135.829 134.265 1.00 31.02 ?  232 ASN B O     1 
ATOM   7416  C  CB    . ASN B 1 232 ? 132.095 134.371 132.255 1.00 29.57 ?  232 ASN B CB    1 
ATOM   7417  C  CG    . ASN B 1 232 ? 132.998 133.251 131.790 1.00 31.72 ?  232 ASN B CG    1 
ATOM   7418  O  OD1   . ASN B 1 232 ? 132.531 132.243 131.263 1.00 31.09 ?  232 ASN B OD1   1 
ATOM   7419  N  ND2   . ASN B 1 232 ? 134.301 133.427 131.965 1.00 30.58 ?  232 ASN B ND2   1 
ATOM   7420  N  N     . ALA B 1 233 ? 132.305 137.035 134.070 1.00 22.25 ?  233 ALA B N     1 
ATOM   7421  C  CA    . ALA B 1 233 ? 132.983 138.287 134.386 1.00 19.36 ?  233 ALA B CA    1 
ATOM   7422  C  C     . ALA B 1 233 ? 133.517 138.284 135.813 1.00 30.42 ?  233 ALA B C     1 
ATOM   7423  O  O     . ALA B 1 233 ? 134.641 138.732 136.065 1.00 37.00 ?  233 ALA B O     1 
ATOM   7424  C  CB    . ALA B 1 233 ? 132.032 139.462 134.170 1.00 21.32 ?  233 ALA B CB    1 
ATOM   7425  N  N     . PHE B 1 234 ? 132.721 137.786 136.761 1.00 26.24 ?  234 PHE B N     1 
ATOM   7426  C  CA    . PHE B 1 234 ? 133.164 137.718 138.148 1.00 18.46 ?  234 PHE B CA    1 
ATOM   7427  C  C     . PHE B 1 234 ? 134.238 136.658 138.341 1.00 23.57 ?  234 PHE B C     1 
ATOM   7428  O  O     . PHE B 1 234 ? 135.123 136.823 139.188 1.00 30.29 ?  234 PHE B O     1 
ATOM   7429  C  CB    . PHE B 1 234 ? 131.973 137.453 139.069 1.00 25.09 ?  234 PHE B CB    1 
ATOM   7430  C  CG    . PHE B 1 234 ? 131.106 138.659 139.295 1.00 21.29 ?  234 PHE B CG    1 
ATOM   7431  C  CD1   . PHE B 1 234 ? 131.622 139.794 139.888 1.00 22.20 ?  234 PHE B CD1   1 
ATOM   7432  C  CD2   . PHE B 1 234 ? 129.778 138.658 138.913 1.00 20.87 ?  234 PHE B CD2   1 
ATOM   7433  C  CE1   . PHE B 1 234 ? 130.831 140.904 140.093 1.00 20.21 ?  234 PHE B CE1   1 
ATOM   7434  C  CE2   . PHE B 1 234 ? 128.984 139.768 139.114 1.00 20.94 ?  234 PHE B CE2   1 
ATOM   7435  C  CZ    . PHE B 1 234 ? 129.511 140.890 139.706 1.00 20.90 ?  234 PHE B CZ    1 
ATOM   7436  N  N     . ARG B 1 235 ? 134.175 135.563 137.579 1.00 29.56 ?  235 ARG B N     1 
ATOM   7437  C  CA    . ARG B 1 235 ? 135.252 134.581 137.613 1.00 26.83 ?  235 ARG B CA    1 
ATOM   7438  C  C     . ARG B 1 235 ? 136.557 135.184 137.114 1.00 28.32 ?  235 ARG B C     1 
ATOM   7439  O  O     . ARG B 1 235 ? 137.624 134.936 137.687 1.00 36.66 ?  235 ARG B O     1 
ATOM   7440  C  CB    . ARG B 1 235 ? 134.877 133.358 136.776 1.00 24.84 ?  235 ARG B CB    1 
ATOM   7441  C  CG    . ARG B 1 235 ? 134.413 132.170 137.591 1.00 32.99 ?  235 ARG B CG    1 
ATOM   7442  C  CD    . ARG B 1 235 ? 134.135 130.966 136.709 1.00 30.46 ?  235 ARG B CD    1 
ATOM   7443  N  NE    . ARG B 1 235 ? 132.766 130.956 136.207 1.00 34.53 ?  235 ARG B NE    1 
ATOM   7444  C  CZ    . ARG B 1 235 ? 132.443 130.915 134.921 1.00 36.67 ?  235 ARG B CZ    1 
ATOM   7445  N  NH1   . ARG B 1 235 ? 133.368 130.888 133.976 1.00 35.53 1  235 ARG B NH1   1 
ATOM   7446  N  NH2   . ARG B 1 235 ? 131.159 130.901 134.576 1.00 32.65 ?  235 ARG B NH2   1 
ATOM   7447  N  N     . TYR B 1 236 ? 136.492 135.981 136.046 1.00 24.71 ?  236 TYR B N     1 
ATOM   7448  C  CA    . TYR B 1 236 ? 137.701 136.577 135.492 1.00 25.51 ?  236 TYR B CA    1 
ATOM   7449  C  C     . TYR B 1 236 ? 138.275 137.630 136.433 1.00 27.63 ?  236 TYR B C     1 
ATOM   7450  O  O     . TYR B 1 236 ? 139.482 137.645 136.702 1.00 28.35 ?  236 TYR B O     1 
ATOM   7451  C  CB    . TYR B 1 236 ? 137.401 137.184 134.123 1.00 22.47 ?  236 TYR B CB    1 
ATOM   7452  C  CG    . TYR B 1 236 ? 138.618 137.743 133.430 1.00 23.31 ?  236 TYR B CG    1 
ATOM   7453  C  CD1   . TYR B 1 236 ? 139.561 136.897 132.867 1.00 21.64 ?  236 TYR B CD1   1 
ATOM   7454  C  CD2   . TYR B 1 236 ? 138.825 139.112 133.339 1.00 24.88 ?  236 TYR B CD2   1 
ATOM   7455  C  CE1   . TYR B 1 236 ? 140.674 137.395 132.233 1.00 24.32 ?  236 TYR B CE1   1 
ATOM   7456  C  CE2   . TYR B 1 236 ? 139.940 139.620 132.703 1.00 17.73 ?  236 TYR B CE2   1 
ATOM   7457  C  CZ    . TYR B 1 236 ? 140.859 138.755 132.153 1.00 20.63 ?  236 TYR B CZ    1 
ATOM   7458  O  OH    . TYR B 1 236 ? 141.973 139.244 131.518 1.00 30.59 ?  236 TYR B OH    1 
ATOM   7459  N  N     . ALA B 1 237 ? 137.425 138.522 136.938 1.00 29.98 ?  237 ALA B N     1 
ATOM   7460  C  CA    . ALA B 1 237 ? 137.848 139.566 137.872 1.00 29.43 ?  237 ALA B CA    1 
ATOM   7461  C  C     . ALA B 1 237 ? 137.694 139.017 139.283 1.00 36.88 ?  237 ALA B C     1 
ATOM   7462  O  O     . ALA B 1 237 ? 136.654 139.169 139.925 1.00 39.03 ?  237 ALA B O     1 
ATOM   7463  C  CB    . ALA B 1 237 ? 137.038 140.838 137.663 1.00 30.69 ?  237 ALA B CB    1 
ATOM   7464  N  N     . ASP B 1 238 ? 138.751 138.373 139.776 1.00 50.17 ?  238 ASP B N     1 
ATOM   7465  C  CA    . ASP B 1 238 ? 138.706 137.718 141.077 1.00 53.56 ?  238 ASP B CA    1 
ATOM   7466  C  C     . ASP B 1 238 ? 139.764 138.279 142.020 1.00 57.82 ?  238 ASP B C     1 
ATOM   7467  O  O     . ASP B 1 238 ? 140.501 137.515 142.654 1.00 57.80 ?  238 ASP B O     1 
ATOM   7468  C  CB    . ASP B 1 238 ? 138.879 136.204 140.919 1.00 52.95 ?  238 ASP B CB    1 
ATOM   7469  C  CG    . ASP B 1 238 ? 140.151 135.833 140.181 1.00 57.45 ?  238 ASP B CG    1 
ATOM   7470  O  OD1   . ASP B 1 238 ? 140.694 136.694 139.457 1.00 57.54 ?  238 ASP B OD1   1 
ATOM   7471  O  OD2   . ASP B 1 238 ? 140.611 134.682 140.331 1.00 56.42 -1 238 ASP B OD2   1 
ATOM   7472  N  N     . GLN B 1 239 ? 139.853 139.607 142.105 1.00 63.48 ?  239 GLN B N     1 
ATOM   7473  C  CA    . GLN B 1 239 ? 140.788 140.287 143.005 1.00 64.82 ?  239 GLN B CA    1 
ATOM   7474  C  C     . GLN B 1 239 ? 142.219 139.800 142.792 1.00 67.35 ?  239 GLN B C     1 
ATOM   7475  O  O     . GLN B 1 239 ? 142.946 139.492 143.739 1.00 66.69 ?  239 GLN B O     1 
ATOM   7476  C  CB    . GLN B 1 239 ? 140.370 140.115 144.466 1.00 64.62 ?  239 GLN B CB    1 
ATOM   7477  C  CG    . GLN B 1 239 ? 139.358 141.131 144.955 1.00 63.82 ?  239 GLN B CG    1 
ATOM   7478  C  CD    . GLN B 1 239 ? 139.592 141.527 146.401 1.00 66.05 ?  239 GLN B CD    1 
ATOM   7479  O  OE1   . GLN B 1 239 ? 138.666 141.551 147.210 1.00 65.31 ?  239 GLN B OE1   1 
ATOM   7480  N  NE2   . GLN B 1 239 ? 140.839 141.840 146.733 1.00 65.72 ?  239 GLN B NE2   1 
ATOM   7481  N  N     . MET B 1 240 ? 142.618 139.730 141.520 1.00 69.45 ?  240 MET B N     1 
ATOM   7482  C  CA    . MET B 1 240 ? 143.950 139.266 141.131 1.00 68.65 ?  240 MET B CA    1 
ATOM   7483  C  C     . MET B 1 240 ? 144.235 137.858 141.649 1.00 69.19 ?  240 MET B C     1 
ATOM   7484  O  O     . MET B 1 240 ? 145.374 137.526 141.985 1.00 69.12 ?  240 MET B O     1 
ATOM   7485  C  CB    . MET B 1 240 ? 145.037 140.240 141.598 1.00 68.32 ?  240 MET B CB    1 
ATOM   7486  C  CG    . MET B 1 240 ? 144.976 141.613 140.941 1.00 68.69 ?  240 MET B CG    1 
ATOM   7487  S  SD    . MET B 1 240 ? 143.323 142.332 140.905 1.00 73.09 ?  240 MET B SD    1 
ATOM   7488  C  CE    . MET B 1 240 ? 143.668 143.932 140.181 1.00 67.85 ?  240 MET B CE    1 
ATOM   7489  N  N     . GLY B 1 241 ? 143.201 137.021 141.717 1.00 67.80 ?  241 GLY B N     1 
ATOM   7490  C  CA    . GLY B 1 241 ? 143.363 135.643 142.128 1.00 68.08 ?  241 GLY B CA    1 
ATOM   7491  C  C     . GLY B 1 241 ? 143.478 135.413 143.618 1.00 70.85 ?  241 GLY B C     1 
ATOM   7492  O  O     . GLY B 1 241 ? 143.745 134.278 144.031 1.00 70.98 ?  241 GLY B O     1 
ATOM   7493  N  N     . GLN B 1 242 ? 143.285 136.444 144.440 1.00 75.83 ?  242 GLN B N     1 
ATOM   7494  C  CA    . GLN B 1 242 ? 143.382 136.287 145.887 1.00 75.30 ?  242 GLN B CA    1 
ATOM   7495  C  C     . GLN B 1 242 ? 142.057 135.845 146.501 1.00 76.57 ?  242 GLN B C     1 
ATOM   7496  O  O     . GLN B 1 242 ? 141.997 134.813 147.176 1.00 76.27 ?  242 GLN B O     1 
ATOM   7497  C  CB    . GLN B 1 242 ? 143.852 137.595 146.527 1.00 74.11 ?  242 GLN B CB    1 
ATOM   7498  C  CG    . GLN B 1 242 ? 145.303 137.940 146.233 1.00 76.09 ?  242 GLN B CG    1 
ATOM   7499  C  CD    . GLN B 1 242 ? 145.872 138.953 147.206 1.00 77.11 ?  242 GLN B CD    1 
ATOM   7500  O  OE1   . GLN B 1 242 ? 145.256 139.269 148.224 1.00 76.41 ?  242 GLN B OE1   1 
ATOM   7501  N  NE2   . GLN B 1 242 ? 147.057 139.468 146.897 1.00 75.63 ?  242 GLN B NE2   1 
ATOM   7502  N  N     . ARG B 1 243 ? 140.994 136.611 146.276 1.00 64.77 ?  243 ARG B N     1 
ATOM   7503  C  CA    . ARG B 1 243 ? 139.658 136.276 146.750 1.00 64.67 ?  243 ARG B CA    1 
ATOM   7504  C  C     . ARG B 1 243 ? 138.763 136.034 145.544 1.00 63.62 ?  243 ARG B C     1 
ATOM   7505  O  O     . ARG B 1 243 ? 138.758 136.834 144.604 1.00 62.13 ?  243 ARG B O     1 
ATOM   7506  C  CB    . ARG B 1 243 ? 139.086 137.395 147.629 1.00 63.04 ?  243 ARG B CB    1 
ATOM   7507  C  CG    . ARG B 1 243 ? 137.569 137.524 147.582 1.00 63.91 ?  243 ARG B CG    1 
ATOM   7508  C  CD    . ARG B 1 243 ? 137.136 138.742 146.776 1.00 63.15 ?  243 ARG B CD    1 
ATOM   7509  N  NE    . ARG B 1 243 ? 135.769 139.147 147.083 1.00 65.04 ?  243 ARG B NE    1 
ATOM   7510  C  CZ    . ARG B 1 243 ? 135.094 140.073 146.414 1.00 62.89 ?  243 ARG B CZ    1 
ATOM   7511  N  NH1   . ARG B 1 243 ? 135.630 140.713 145.387 1.00 59.40 1  243 ARG B NH1   1 
ATOM   7512  N  NH2   . ARG B 1 243 ? 133.850 140.362 146.784 1.00 60.40 ?  243 ARG B NH2   1 
ATOM   7513  N  N     . GLN B 1 244 ? 138.014 134.933 145.574 1.00 61.88 ?  244 GLN B N     1 
ATOM   7514  C  CA    . GLN B 1 244 ? 137.133 134.598 144.462 1.00 62.67 ?  244 GLN B CA    1 
ATOM   7515  C  C     . GLN B 1 244 ? 136.142 135.727 144.210 1.00 61.97 ?  244 GLN B C     1 
ATOM   7516  O  O     . GLN B 1 244 ? 135.540 136.261 145.146 1.00 61.07 ?  244 GLN B O     1 
ATOM   7517  C  CB    . GLN B 1 244 ? 136.386 133.296 144.755 1.00 59.38 ?  244 GLN B CB    1 
ATOM   7518  C  CG    . GLN B 1 244 ? 137.263 132.056 144.744 1.00 59.03 ?  244 GLN B CG    1 
ATOM   7519  C  CD    . GLN B 1 244 ? 136.466 130.783 144.534 1.00 60.67 ?  244 GLN B CD    1 
ATOM   7520  O  OE1   . GLN B 1 244 ? 135.388 130.611 145.103 1.00 61.69 ?  244 GLN B OE1   1 
ATOM   7521  N  NE2   . GLN B 1 244 ? 136.994 129.882 143.715 1.00 59.63 ?  244 GLN B NE2   1 
ATOM   7522  N  N     . GLY B 1 245 ? 135.986 136.096 142.941 1.00 50.30 ?  245 GLY B N     1 
ATOM   7523  C  CA    . GLY B 1 245 ? 135.049 137.137 142.572 1.00 47.08 ?  245 GLY B CA    1 
ATOM   7524  C  C     . GLY B 1 245 ? 133.626 136.776 142.939 1.00 46.51 ?  245 GLY B C     1 
ATOM   7525  O  O     . GLY B 1 245 ? 133.105 135.749 142.495 1.00 46.35 ?  245 GLY B O     1 
ATOM   7526  N  N     . SER B 1 246 ? 132.989 137.611 143.752 1.00 41.79 ?  246 SER B N     1 
ATOM   7527  C  CA    . SER B 1 246 ? 131.654 137.345 144.269 1.00 37.18 ?  246 SER B CA    1 
ATOM   7528  C  C     . SER B 1 246 ? 130.678 138.345 143.666 1.00 35.91 ?  246 SER B C     1 
ATOM   7529  O  O     . SER B 1 246 ? 130.872 139.560 143.785 1.00 30.02 ?  246 SER B O     1 
ATOM   7530  C  CB    . SER B 1 246 ? 131.632 137.425 145.795 1.00 37.49 ?  246 SER B CB    1 
ATOM   7531  O  OG    . SER B 1 246 ? 132.357 136.353 146.371 1.00 43.74 ?  246 SER B OG    1 
ATOM   7532  N  N     . GLY B 1 247 ? 129.631 137.829 143.026 1.00 25.68 ?  247 GLY B N     1 
ATOM   7533  C  CA    . GLY B 1 247 ? 128.593 138.668 142.478 1.00 8.74  ?  247 GLY B CA    1 
ATOM   7534  C  C     . GLY B 1 247 ? 127.229 138.189 142.928 1.00 13.22 ?  247 GLY B C     1 
ATOM   7535  O  O     . GLY B 1 247 ? 127.048 137.047 143.349 1.00 20.58 ?  247 GLY B O     1 
ATOM   7536  N  N     . ALA B 1 248 ? 126.266 139.097 142.844 1.00 14.03 ?  248 ALA B N     1 
ATOM   7537  C  CA    . ALA B 1 248 ? 124.883 138.801 143.174 1.00 14.28 ?  248 ALA B CA    1 
ATOM   7538  C  C     . ALA B 1 248 ? 123.990 139.267 142.037 1.00 10.37 ?  248 ALA B C     1 
ATOM   7539  O  O     . ALA B 1 248 ? 124.207 140.337 141.466 1.00 17.81 ?  248 ALA B O     1 
ATOM   7540  C  CB    . ALA B 1 248 ? 124.459 139.469 144.486 1.00 9.00  ?  248 ALA B CB    1 
ATOM   7541  N  N     . ALA B 1 249 ? 123.000 138.450 141.701 1.00 12.61 ?  249 ALA B N     1 
ATOM   7542  C  CA    . ALA B 1 249 ? 121.967 138.813 140.743 1.00 12.36 ?  249 ALA B CA    1 
ATOM   7543  C  C     . ALA B 1 249 ? 120.631 138.822 141.464 1.00 8.88  ?  249 ALA B C     1 
ATOM   7544  O  O     . ALA B 1 249 ? 120.308 137.878 142.191 1.00 16.83 ?  249 ALA B O     1 
ATOM   7545  C  CB    . ALA B 1 249 ? 121.932 137.841 139.561 1.00 14.14 ?  249 ALA B CB    1 
ATOM   7546  N  N     . TYR B 1 250 ? 119.865 139.890 141.279 1.00 8.30  ?  250 TYR B N     1 
ATOM   7547  C  CA    . TYR B 1 250 ? 118.553 140.020 141.891 1.00 8.18  ?  250 TYR B CA    1 
ATOM   7548  C  C     . TYR B 1 250 ? 117.499 140.074 140.798 1.00 7.77  ?  250 TYR B C     1 
ATOM   7549  O  O     . TYR B 1 250 ? 117.654 140.806 139.815 1.00 13.56 ?  250 TYR B O     1 
ATOM   7550  C  CB    . TYR B 1 250 ? 118.474 141.264 142.774 1.00 7.54  ?  250 TYR B CB    1 
ATOM   7551  C  CG    . TYR B 1 250 ? 118.980 141.041 144.177 1.00 15.50 ?  250 TYR B CG    1 
ATOM   7552  C  CD1   . TYR B 1 250 ? 120.341 140.955 144.436 1.00 3.04  ?  250 TYR B CD1   1 
ATOM   7553  C  CD2   . TYR B 1 250 ? 118.102 140.915 145.243 1.00 12.49 ?  250 TYR B CD2   1 
ATOM   7554  C  CE1   . TYR B 1 250 ? 120.812 140.752 145.713 1.00 0.74  ?  250 TYR B CE1   1 
ATOM   7555  C  CE2   . TYR B 1 250 ? 118.564 140.710 146.527 1.00 7.28  ?  250 TYR B CE2   1 
ATOM   7556  C  CZ    . TYR B 1 250 ? 119.921 140.630 146.756 1.00 8.49  ?  250 TYR B CZ    1 
ATOM   7557  O  OH    . TYR B 1 250 ? 120.390 140.426 148.032 1.00 12.85 ?  250 TYR B OH    1 
ATOM   7558  N  N     . LEU B 1 251 ? 116.440 139.294 140.968 1.00 12.99 ?  251 LEU B N     1 
ATOM   7559  C  CA    . LEU B 1 251 ? 115.335 139.263 140.024 1.00 14.29 ?  251 LEU B CA    1 
ATOM   7560  C  C     . LEU B 1 251 ? 114.023 139.359 140.782 1.00 12.54 ?  251 LEU B C     1 
ATOM   7561  O  O     . LEU B 1 251 ? 113.858 138.735 141.834 1.00 15.58 ?  251 LEU B O     1 
ATOM   7562  C  CB    . LEU B 1 251 ? 115.357 137.987 139.180 1.00 15.25 ?  251 LEU B CB    1 
ATOM   7563  C  CG    . LEU B 1 251 ? 114.534 138.046 137.895 1.00 11.75 ?  251 LEU B CG    1 
ATOM   7564  C  CD1   . LEU B 1 251 ? 115.169 139.010 136.913 1.00 12.25 ?  251 LEU B CD1   1 
ATOM   7565  C  CD2   . LEU B 1 251 ? 114.391 136.669 137.282 1.00 7.68  ?  251 LEU B CD2   1 
ATOM   7566  N  N     . ASN B 1 252 ? 113.097 140.148 140.250 1.00 11.64 ?  252 ASN B N     1 
ATOM   7567  C  CA    . ASN B 1 252 ? 111.762 140.209 140.822 1.00 10.65 ?  252 ASN B CA    1 
ATOM   7568  C  C     . ASN B 1 252 ? 111.050 138.879 140.623 1.00 15.17 ?  252 ASN B C     1 
ATOM   7569  O  O     . ASN B 1 252 ? 111.217 138.213 139.598 1.00 23.08 ?  252 ASN B O     1 
ATOM   7570  C  CB    . ASN B 1 252 ? 110.959 141.343 140.189 1.00 12.48 ?  252 ASN B CB    1 
ATOM   7571  C  CG    . ASN B 1 252 ? 109.881 141.873 141.109 1.00 20.70 ?  252 ASN B CG    1 
ATOM   7572  O  OD1   . ASN B 1 252 ? 108.871 141.213 141.346 1.00 30.12 ?  252 ASN B OD1   1 
ATOM   7573  N  ND2   . ASN B 1 252 ? 110.094 143.070 141.640 1.00 20.44 ?  252 ASN B ND2   1 
ATOM   7574  N  N     . ILE B 1 253 ? 110.255 138.486 141.621 1.00 13.68 ?  253 ILE B N     1 
ATOM   7575  C  CA    . ILE B 1 253 ? 109.559 137.209 141.555 1.00 17.48 ?  253 ILE B CA    1 
ATOM   7576  C  C     . ILE B 1 253 ? 108.477 137.205 140.482 1.00 20.96 ?  253 ILE B C     1 
ATOM   7577  O  O     . ILE B 1 253 ? 108.005 136.133 140.086 1.00 23.60 ?  253 ILE B O     1 
ATOM   7578  C  CB    . ILE B 1 253 ? 108.973 136.849 142.934 1.00 16.66 ?  253 ILE B CB    1 
ATOM   7579  C  CG1   . ILE B 1 253 ? 108.781 135.337 143.055 1.00 16.22 ?  253 ILE B CG1   1 
ATOM   7580  C  CG2   . ILE B 1 253 ? 107.668 137.589 143.178 1.00 13.72 ?  253 ILE B CG2   1 
ATOM   7581  C  CD1   . ILE B 1 253 ? 108.905 134.817 144.461 1.00 16.69 ?  253 ILE B CD1   1 
ATOM   7582  N  N     . PHE B 1 254 ? 108.073 138.375 139.993 1.00 19.04 ?  254 PHE B N     1 
ATOM   7583  C  CA    . PHE B 1 254 ? 107.086 138.470 138.928 1.00 16.79 ?  254 PHE B CA    1 
ATOM   7584  C  C     . PHE B 1 254 ? 107.716 138.471 137.541 1.00 18.10 ?  254 PHE B C     1 
ATOM   7585  O  O     . PHE B 1 254 ? 106.990 138.531 136.545 1.00 25.04 ?  254 PHE B O     1 
ATOM   7586  C  CB    . PHE B 1 254 ? 106.230 139.724 139.119 1.00 23.09 ?  254 PHE B CB    1 
ATOM   7587  C  CG    . PHE B 1 254 ? 105.167 139.569 140.167 1.00 22.28 ?  254 PHE B CG    1 
ATOM   7588  C  CD1   . PHE B 1 254 ? 104.091 138.727 139.959 1.00 22.04 ?  254 PHE B CD1   1 
ATOM   7589  C  CD2   . PHE B 1 254 ? 105.256 140.250 141.368 1.00 26.07 ?  254 PHE B CD2   1 
ATOM   7590  C  CE1   . PHE B 1 254 ? 103.115 138.576 140.924 1.00 24.80 ?  254 PHE B CE1   1 
ATOM   7591  C  CE2   . PHE B 1 254 ? 104.284 140.102 142.337 1.00 27.48 ?  254 PHE B CE2   1 
ATOM   7592  C  CZ    . PHE B 1 254 ? 103.211 139.265 142.114 1.00 21.77 ?  254 PHE B CZ    1 
ATOM   7593  N  N     . HIS B 1 255 ? 109.041 138.419 137.459 1.00 25.56 ?  255 HIS B N     1 
ATOM   7594  C  CA    . HIS B 1 255 ? 109.714 138.230 136.183 1.00 14.87 ?  255 HIS B CA    1 
ATOM   7595  C  C     . HIS B 1 255 ? 109.417 136.837 135.642 1.00 18.41 ?  255 HIS B C     1 
ATOM   7596  O  O     . HIS B 1 255 ? 109.331 135.868 136.399 1.00 27.28 ?  255 HIS B O     1 
ATOM   7597  C  CB    . HIS B 1 255 ? 111.220 138.421 136.356 1.00 17.20 ?  255 HIS B CB    1 
ATOM   7598  C  CG    . HIS B 1 255 ? 111.940 138.777 135.095 1.00 19.61 ?  255 HIS B CG    1 
ATOM   7599  N  ND1   . HIS B 1 255 ? 112.149 137.873 134.076 1.00 17.88 ?  255 HIS B ND1   1 
ATOM   7600  C  CD2   . HIS B 1 255 ? 112.518 139.935 134.696 1.00 14.91 ?  255 HIS B CD2   1 
ATOM   7601  C  CE1   . HIS B 1 255 ? 112.816 138.461 133.100 1.00 16.46 ?  255 HIS B CE1   1 
ATOM   7602  N  NE2   . HIS B 1 255 ? 113.054 139.711 133.451 1.00 11.54 ?  255 HIS B NE2   1 
ATOM   7603  N  N     . ARG B 1 256 ? 109.252 136.739 134.321 1.00 21.76 ?  256 ARG B N     1 
ATOM   7604  C  CA    . ARG B 1 256 ? 108.934 135.448 133.719 1.00 22.18 ?  256 ARG B CA    1 
ATOM   7605  C  C     . ARG B 1 256 ? 110.074 134.451 133.895 1.00 23.41 ?  256 ARG B C     1 
ATOM   7606  O  O     . ARG B 1 256 ? 109.831 133.245 134.017 1.00 25.13 ?  256 ARG B O     1 
ATOM   7607  C  CB    . ARG B 1 256 ? 108.605 135.623 132.237 1.00 22.61 ?  256 ARG B CB    1 
ATOM   7608  C  CG    . ARG B 1 256 ? 108.311 134.319 131.515 1.00 23.62 ?  256 ARG B CG    1 
ATOM   7609  C  CD    . ARG B 1 256 ? 109.212 134.132 130.308 1.00 25.89 ?  256 ARG B CD    1 
ATOM   7610  N  NE    . ARG B 1 256 ? 110.427 133.394 130.626 1.00 27.83 ?  256 ARG B NE    1 
ATOM   7611  C  CZ    . ARG B 1 256 ? 110.479 132.085 130.827 1.00 29.95 ?  256 ARG B CZ    1 
ATOM   7612  N  NH1   . ARG B 1 256 ? 109.395 131.329 130.754 1.00 28.67 1  256 ARG B NH1   1 
ATOM   7613  N  NH2   . ARG B 1 256 ? 111.649 131.517 131.109 1.00 27.86 ?  256 ARG B NH2   1 
ATOM   7614  N  N     . ASP B 1 257 ? 111.312 134.933 133.929 1.00 14.82 ?  257 ASP B N     1 
ATOM   7615  C  CA    . ASP B 1 257 ? 112.482 134.075 134.053 1.00 19.17 ?  257 ASP B CA    1 
ATOM   7616  C  C     . ASP B 1 257 ? 112.734 133.609 135.480 1.00 18.74 ?  257 ASP B C     1 
ATOM   7617  O  O     . ASP B 1 257 ? 113.751 132.948 135.719 1.00 24.95 ?  257 ASP B O     1 
ATOM   7618  C  CB    . ASP B 1 257 ? 113.721 134.803 133.534 1.00 23.39 ?  257 ASP B CB    1 
ATOM   7619  C  CG    . ASP B 1 257 ? 113.774 134.857 132.025 1.00 26.85 ?  257 ASP B CG    1 
ATOM   7620  O  OD1   . ASP B 1 257 ? 113.019 134.106 131.373 1.00 27.01 ?  257 ASP B OD1   1 
ATOM   7621  O  OD2   . ASP B 1 257 ? 114.576 135.649 131.492 1.00 31.26 -1 257 ASP B OD2   1 
ATOM   7622  N  N     . ILE B 1 258 ? 111.826 133.909 136.414 1.00 19.61 ?  258 ILE B N     1 
ATOM   7623  C  CA    . ILE B 1 258 ? 112.099 133.675 137.829 1.00 21.87 ?  258 ILE B CA    1 
ATOM   7624  C  C     . ILE B 1 258 ? 112.400 132.204 138.085 1.00 23.00 ?  258 ILE B C     1 
ATOM   7625  O  O     . ILE B 1 258 ? 113.259 131.868 138.907 1.00 32.37 ?  258 ILE B O     1 
ATOM   7626  C  CB    . ILE B 1 258 ? 110.930 134.182 138.698 1.00 23.55 ?  258 ILE B CB    1 
ATOM   7627  C  CG1   . ILE B 1 258 ? 111.281 134.080 140.184 1.00 21.31 ?  258 ILE B CG1   1 
ATOM   7628  C  CG2   . ILE B 1 258 ? 109.644 133.424 138.397 1.00 20.68 ?  258 ILE B CG2   1 
ATOM   7629  C  CD1   . ILE B 1 258 ? 112.477 134.911 140.584 1.00 19.07 ?  258 ILE B CD1   1 
ATOM   7630  N  N     . ASN B 1 259 ? 111.712 131.304 137.381 1.00 26.15 ?  259 ASN B N     1 
ATOM   7631  C  CA    . ASN B 1 259 ? 112.014 129.885 137.523 1.00 24.53 ?  259 ASN B CA    1 
ATOM   7632  C  C     . ASN B 1 259 ? 113.404 129.570 136.985 1.00 23.29 ?  259 ASN B C     1 
ATOM   7633  O  O     . ASN B 1 259 ? 114.228 128.966 137.682 1.00 26.89 ?  259 ASN B O     1 
ATOM   7634  C  CB    . ASN B 1 259 ? 110.950 129.050 136.812 1.00 24.70 ?  259 ASN B CB    1 
ATOM   7635  C  CG    . ASN B 1 259 ? 109.723 128.823 137.669 1.00 24.50 ?  259 ASN B CG    1 
ATOM   7636  O  OD1   . ASN B 1 259 ? 109.771 128.095 138.660 1.00 26.50 ?  259 ASN B OD1   1 
ATOM   7637  N  ND2   . ASN B 1 259 ? 108.616 129.452 137.295 1.00 30.54 ?  259 ASN B ND2   1 
ATOM   7638  N  N     . ASP B 1 260 ? 113.697 130.014 135.759 1.00 27.76 ?  260 ASP B N     1 
ATOM   7639  C  CA    . ASP B 1 260 ? 115.008 129.760 135.172 1.00 24.59 ?  260 ASP B CA    1 
ATOM   7640  C  C     . ASP B 1 260 ? 116.106 130.368 136.032 1.00 19.53 ?  260 ASP B C     1 
ATOM   7641  O  O     . ASP B 1 260 ? 117.133 129.730 136.295 1.00 27.97 ?  260 ASP B O     1 
ATOM   7642  C  CB    . ASP B 1 260 ? 115.063 130.318 133.750 1.00 23.49 ?  260 ASP B CB    1 
ATOM   7643  C  CG    . ASP B 1 260 ? 114.100 129.620 132.812 1.00 32.69 ?  260 ASP B CG    1 
ATOM   7644  O  OD1   . ASP B 1 260 ? 113.830 128.417 133.019 1.00 33.48 ?  260 ASP B OD1   1 
ATOM   7645  O  OD2   . ASP B 1 260 ? 113.613 130.275 131.866 1.00 33.86 -1 260 ASP B OD2   1 
ATOM   7646  N  N     . PHE B 1 261 ? 115.898 131.609 136.476 1.00 26.81 ?  261 PHE B N     1 
ATOM   7647  C  CA    . PHE B 1 261 ? 116.725 132.236 137.497 1.00 22.12 ?  261 PHE B CA    1 
ATOM   7648  C  C     . PHE B 1 261 ? 117.014 131.266 138.638 1.00 16.07 ?  261 PHE B C     1 
ATOM   7649  O  O     . PHE B 1 261 ? 118.173 130.934 138.916 1.00 21.75 ?  261 PHE B O     1 
ATOM   7650  C  CB    . PHE B 1 261 ? 116.004 133.493 138.002 1.00 10.28 ?  261 PHE B CB    1 
ATOM   7651  C  CG    . PHE B 1 261 ? 116.816 134.344 138.934 1.00 22.77 ?  261 PHE B CG    1 
ATOM   7652  C  CD1   . PHE B 1 261 ? 117.793 135.193 138.446 1.00 20.56 ?  261 PHE B CD1   1 
ATOM   7653  C  CD2   . PHE B 1 261 ? 116.571 134.326 140.297 1.00 23.60 ?  261 PHE B CD2   1 
ATOM   7654  C  CE1   . PHE B 1 261 ? 118.528 135.988 139.301 1.00 15.18 ?  261 PHE B CE1   1 
ATOM   7655  C  CE2   . PHE B 1 261 ? 117.302 135.119 141.154 1.00 15.89 ?  261 PHE B CE2   1 
ATOM   7656  C  CZ    . PHE B 1 261 ? 118.283 135.951 140.656 1.00 15.76 ?  261 PHE B CZ    1 
ATOM   7657  N  N     . LEU B 1 262 ? 115.952 130.760 139.271 1.00 23.93 ?  262 LEU B N     1 
ATOM   7658  C  CA    . LEU B 1 262 ? 116.130 129.824 140.374 1.00 23.77 ?  262 LEU B CA    1 
ATOM   7659  C  C     . LEU B 1 262 ? 116.821 128.552 139.904 1.00 28.49 ?  262 LEU B C     1 
ATOM   7660  O  O     . LEU B 1 262 ? 117.636 127.972 140.632 1.00 30.74 ?  262 LEU B O     1 
ATOM   7661  C  CB    . LEU B 1 262 ? 114.782 129.500 141.012 1.00 27.44 ?  262 LEU B CB    1 
ATOM   7662  C  CG    . LEU B 1 262 ? 114.067 130.674 141.677 1.00 24.56 ?  262 LEU B CG    1 
ATOM   7663  C  CD1   . LEU B 1 262 ? 112.695 130.252 142.167 1.00 26.12 ?  262 LEU B CD1   1 
ATOM   7664  C  CD2   . LEU B 1 262 ? 114.903 131.240 142.811 1.00 23.89 ?  262 LEU B CD2   1 
ATOM   7665  N  N     . ASP B 1 263 ? 116.534 128.123 138.674 1.00 34.07 ?  263 ASP B N     1 
ATOM   7666  C  CA    . ASP B 1 263 ? 117.159 126.918 138.150 1.00 25.65 ?  263 ASP B CA    1 
ATOM   7667  C  C     . ASP B 1 263 ? 118.664 127.068 137.995 1.00 29.95 ?  263 ASP B C     1 
ATOM   7668  O  O     . ASP B 1 263 ? 119.352 126.058 137.815 1.00 38.33 ?  263 ASP B O     1 
ATOM   7669  C  CB    . ASP B 1 263 ? 116.529 126.541 136.809 1.00 30.81 ?  263 ASP B CB    1 
ATOM   7670  C  CG    . ASP B 1 263 ? 115.111 126.026 136.958 1.00 37.05 ?  263 ASP B CG    1 
ATOM   7671  O  OD1   . ASP B 1 263 ? 114.743 125.608 138.076 1.00 36.66 ?  263 ASP B OD1   1 
ATOM   7672  O  OD2   . ASP B 1 263 ? 114.366 126.038 135.956 1.00 35.56 -1 263 ASP B OD2   1 
ATOM   7673  N  N     . THR B 1 264 ? 119.190 128.295 138.055 1.00 33.51 ?  264 THR B N     1 
ATOM   7674  C  CA    . THR B 1 264 ? 120.637 128.466 138.041 1.00 32.04 ?  264 THR B CA    1 
ATOM   7675  C  C     . THR B 1 264 ? 121.295 127.910 139.296 1.00 36.16 ?  264 THR B C     1 
ATOM   7676  O  O     . THR B 1 264 ? 122.488 127.592 139.264 1.00 36.90 ?  264 THR B O     1 
ATOM   7677  C  CB    . THR B 1 264 ? 120.996 129.943 137.877 1.00 33.04 ?  264 THR B CB    1 
ATOM   7678  O  OG1   . THR B 1 264 ? 120.438 130.696 138.961 1.00 36.48 ?  264 THR B OG1   1 
ATOM   7679  C  CG2   . THR B 1 264 ? 120.455 130.478 136.560 1.00 30.51 ?  264 THR B CG2   1 
ATOM   7680  N  N     . LYS B 1 265 ? 120.551 127.780 140.395 1.00 32.38 ?  265 LYS B N     1 
ATOM   7681  C  CA    . LYS B 1 265 ? 121.107 127.303 141.654 1.00 34.15 ?  265 LYS B CA    1 
ATOM   7682  C  C     . LYS B 1 265 ? 120.713 125.871 141.990 1.00 36.53 ?  265 LYS B C     1 
ATOM   7683  O  O     . LYS B 1 265 ? 121.145 125.355 143.025 1.00 39.20 ?  265 LYS B O     1 
ATOM   7684  C  CB    . LYS B 1 265 ? 120.695 128.231 142.800 1.00 33.86 ?  265 LYS B CB    1 
ATOM   7685  C  CG    . LYS B 1 265 ? 121.492 129.520 142.860 1.00 32.96 ?  265 LYS B CG    1 
ATOM   7686  C  CD    . LYS B 1 265 ? 122.983 129.243 142.850 1.00 35.96 ?  265 LYS B CD    1 
ATOM   7687  C  CE    . LYS B 1 265 ? 123.776 130.527 142.728 1.00 34.47 ?  265 LYS B CE    1 
ATOM   7688  N  NZ    . LYS B 1 265 ? 125.215 130.266 142.459 1.00 37.38 1  265 LYS B NZ    1 
ATOM   7689  N  N     . LYS B 1 266 ? 119.908 125.221 141.156 1.00 45.03 ?  266 LYS B N     1 
ATOM   7690  C  CA    . LYS B 1 266 ? 119.580 123.822 141.391 1.00 44.08 ?  266 LYS B CA    1 
ATOM   7691  C  C     . LYS B 1 266 ? 120.821 122.956 141.219 1.00 48.90 ?  266 LYS B C     1 
ATOM   7692  O  O     . LYS B 1 266 ? 121.627 123.170 140.308 1.00 50.53 ?  266 LYS B O     1 
ATOM   7693  C  CB    . LYS B 1 266 ? 118.476 123.362 140.440 1.00 44.10 ?  266 LYS B CB    1 
ATOM   7694  C  CG    . LYS B 1 266 ? 117.074 123.706 140.915 1.00 46.71 ?  266 LYS B CG    1 
ATOM   7695  C  CD    . LYS B 1 266 ? 116.015 123.078 140.025 1.00 48.45 ?  266 LYS B CD    1 
ATOM   7696  C  CE    . LYS B 1 266 ? 114.667 123.034 140.727 1.00 47.44 ?  266 LYS B CE    1 
ATOM   7697  N  NZ    . LYS B 1 266 ? 113.571 122.624 139.807 1.00 49.34 1  266 LYS B NZ    1 
ATOM   7698  N  N     . ILE B 1 267 ? 120.977 121.972 142.109 1.00 56.82 ?  267 ILE B N     1 
ATOM   7699  C  CA    . ILE B 1 267 ? 122.163 121.125 142.073 1.00 59.40 ?  267 ILE B CA    1 
ATOM   7700  C  C     . ILE B 1 267 ? 122.158 120.179 140.878 1.00 59.98 ?  267 ILE B C     1 
ATOM   7701  O  O     . ILE B 1 267 ? 123.198 119.600 140.546 1.00 58.71 ?  267 ILE B O     1 
ATOM   7702  C  CB    . ILE B 1 267 ? 122.316 120.367 143.409 1.00 60.41 ?  267 ILE B CB    1 
ATOM   7703  C  CG1   . ILE B 1 267 ? 120.967 119.886 143.971 1.00 59.80 ?  267 ILE B CG1   1 
ATOM   7704  C  CG2   . ILE B 1 267 ? 123.028 121.241 144.433 1.00 58.18 ?  267 ILE B CG2   1 
ATOM   7705  C  CD1   . ILE B 1 267 ? 120.196 118.895 143.118 1.00 57.74 ?  267 ILE B CD1   1 
ATOM   7706  N  N     . SER B 1 268 ? 121.013 120.008 140.219 1.00 62.10 ?  268 SER B N     1 
ATOM   7707  C  CA    . SER B 1 268 ? 120.897 119.163 139.039 1.00 64.31 ?  268 SER B CA    1 
ATOM   7708  C  C     . SER B 1 268 ? 120.928 119.963 137.743 1.00 65.31 ?  268 SER B C     1 
ATOM   7709  O  O     . SER B 1 268 ? 120.694 119.396 136.672 1.00 66.20 ?  268 SER B O     1 
ATOM   7710  C  CB    . SER B 1 268 ? 119.612 118.336 139.110 1.00 67.03 ?  268 SER B CB    1 
ATOM   7711  O  OG    . SER B 1 268 ? 118.482 119.169 139.306 1.00 64.20 ?  268 SER B OG    1 
ATOM   7712  N  N     . ALA B 1 269 ? 121.208 121.261 137.819 1.00 66.97 ?  269 ALA B N     1 
ATOM   7713  C  CA    . ALA B 1 269 ? 121.183 122.111 136.637 1.00 67.58 ?  269 ALA B CA    1 
ATOM   7714  C  C     . ALA B 1 269 ? 122.304 121.745 135.672 1.00 67.63 ?  269 ALA B C     1 
ATOM   7715  O  O     . ALA B 1 269 ? 123.405 121.359 136.075 1.00 65.97 ?  269 ALA B O     1 
ATOM   7716  C  CB    . ALA B 1 269 ? 121.298 123.581 137.036 1.00 65.51 ?  269 ALA B CB    1 
ATOM   7717  N  N     . ASP B 1 270 ? 122.011 121.872 134.381 1.00 73.26 ?  270 ASP B N     1 
ATOM   7718  C  CA    . ASP B 1 270 ? 123.004 121.617 133.352 1.00 73.45 ?  270 ASP B CA    1 
ATOM   7719  C  C     . ASP B 1 270 ? 124.052 122.729 133.336 1.00 73.74 ?  270 ASP B C     1 
ATOM   7720  O  O     . ASP B 1 270 ? 123.840 123.828 133.854 1.00 74.05 ?  270 ASP B O     1 
ATOM   7721  C  CB    . ASP B 1 270 ? 122.336 121.500 131.981 1.00 73.73 ?  270 ASP B CB    1 
ATOM   7722  C  CG    . ASP B 1 270 ? 123.141 120.664 131.008 1.00 75.07 ?  270 ASP B CG    1 
ATOM   7723  O  OD1   . ASP B 1 270 ? 124.296 121.037 130.713 1.00 75.22 ?  270 ASP B OD1   1 
ATOM   7724  O  OD2   . ASP B 1 270 ? 122.619 119.631 130.536 1.00 74.14 -1 270 ASP B OD2   1 
ATOM   7725  N  N     . GLU B 1 271 ? 125.201 122.424 132.728 1.00 73.75 ?  271 GLU B N     1 
ATOM   7726  C  CA    . GLU B 1 271 ? 126.306 123.377 132.713 1.00 73.72 ?  271 GLU B CA    1 
ATOM   7727  C  C     . GLU B 1 271 ? 125.964 124.639 131.927 1.00 72.95 ?  271 GLU B C     1 
ATOM   7728  O  O     . GLU B 1 271 ? 126.483 125.716 132.238 1.00 72.44 ?  271 GLU B O     1 
ATOM   7729  C  CB    . GLU B 1 271 ? 127.560 122.720 132.139 1.00 72.64 ?  271 GLU B CB    1 
ATOM   7730  C  CG    . GLU B 1 271 ? 128.280 121.808 133.119 1.00 73.86 ?  271 GLU B CG    1 
ATOM   7731  C  CD    . GLU B 1 271 ? 128.803 122.554 134.332 1.00 74.42 ?  271 GLU B CD    1 
ATOM   7732  O  OE1   . GLU B 1 271 ? 129.250 123.709 134.175 1.00 73.57 ?  271 GLU B OE1   1 
ATOM   7733  O  OE2   . GLU B 1 271 ? 128.766 121.984 135.442 1.00 73.53 -1 271 GLU B OE2   1 
ATOM   7734  N  N     . ASP B 1 272 ? 125.101 124.530 130.916 1.00 69.22 ?  272 ASP B N     1 
ATOM   7735  C  CA    . ASP B 1 272 ? 124.710 125.704 130.144 1.00 70.00 ?  272 ASP B CA    1 
ATOM   7736  C  C     . ASP B 1 272 ? 123.759 126.620 130.903 1.00 69.56 ?  272 ASP B C     1 
ATOM   7737  O  O     . ASP B 1 272 ? 123.517 127.744 130.451 1.00 68.28 ?  272 ASP B O     1 
ATOM   7738  C  CB    . ASP B 1 272 ? 124.074 125.275 128.820 1.00 69.68 ?  272 ASP B CB    1 
ATOM   7739  C  CG    . ASP B 1 272 ? 122.683 124.698 128.997 1.00 72.04 ?  272 ASP B CG    1 
ATOM   7740  O  OD1   . ASP B 1 272 ? 122.413 124.096 130.058 1.00 71.80 ?  272 ASP B OD1   1 
ATOM   7741  O  OD2   . ASP B 1 272 ? 121.857 124.843 128.072 1.00 69.21 -1 272 ASP B OD2   1 
ATOM   7742  N  N     . VAL B 1 273 ? 123.213 126.169 132.034 1.00 62.08 ?  273 VAL B N     1 
ATOM   7743  C  CA    . VAL B 1 273 ? 122.318 126.968 132.856 1.00 62.78 ?  273 VAL B CA    1 
ATOM   7744  C  C     . VAL B 1 273 ? 122.915 127.259 134.227 1.00 61.16 ?  273 VAL B C     1 
ATOM   7745  O  O     . VAL B 1 273 ? 122.741 128.358 134.765 1.00 60.96 ?  273 VAL B O     1 
ATOM   7746  C  CB    . VAL B 1 273 ? 120.940 126.285 132.997 1.00 63.68 ?  273 VAL B CB    1 
ATOM   7747  C  CG1   . VAL B 1 273 ? 120.041 127.063 133.948 1.00 61.00 ?  273 VAL B CG1   1 
ATOM   7748  C  CG2   . VAL B 1 273 ? 120.280 126.139 131.635 1.00 62.41 ?  273 VAL B CG2   1 
ATOM   7749  N  N     . ARG B 1 274 ? 123.631 126.293 134.802 1.00 61.27 ?  274 ARG B N     1 
ATOM   7750  C  CA    . ARG B 1 274 ? 124.159 126.440 136.152 1.00 60.75 ?  274 ARG B CA    1 
ATOM   7751  C  C     . ARG B 1 274 ? 125.122 127.618 136.243 1.00 59.70 ?  274 ARG B C     1 
ATOM   7752  O  O     . ARG B 1 274 ? 125.982 127.813 135.379 1.00 62.45 ?  274 ARG B O     1 
ATOM   7753  C  CB    . ARG B 1 274 ? 124.864 125.152 136.584 1.00 62.89 ?  274 ARG B CB    1 
ATOM   7754  C  CG    . ARG B 1 274 ? 126.063 125.366 137.496 1.00 58.68 ?  274 ARG B CG    1 
ATOM   7755  C  CD    . ARG B 1 274 ? 126.171 124.276 138.548 1.00 61.77 ?  274 ARG B CD    1 
ATOM   7756  N  NE    . ARG B 1 274 ? 126.434 122.970 137.956 1.00 65.06 ?  274 ARG B NE    1 
ATOM   7757  C  CZ    . ARG B 1 274 ? 125.662 121.905 138.116 1.00 66.11 ?  274 ARG B CZ    1 
ATOM   7758  N  NH1   . ARG B 1 274 ? 124.565 121.950 138.855 1.00 63.75 1  274 ARG B NH1   1 
ATOM   7759  N  NH2   . ARG B 1 274 ? 125.998 120.764 137.521 1.00 63.75 ?  274 ARG B NH2   1 
ATOM   7760  N  N     . VAL B 1 275 ? 124.963 128.410 137.299 1.00 47.00 ?  275 VAL B N     1 
ATOM   7761  C  CA    . VAL B 1 275 ? 125.850 129.519 137.620 1.00 44.89 ?  275 VAL B CA    1 
ATOM   7762  C  C     . VAL B 1 275 ? 126.332 129.320 139.051 1.00 48.71 ?  275 VAL B C     1 
ATOM   7763  O  O     . VAL B 1 275 ? 125.517 129.108 139.957 1.00 51.14 ?  275 VAL B O     1 
ATOM   7764  C  CB    . VAL B 1 275 ? 125.139 130.875 137.459 1.00 45.84 ?  275 VAL B CB    1 
ATOM   7765  C  CG1   . VAL B 1 275 ? 125.926 131.958 138.141 1.00 45.29 ?  275 VAL B CG1   1 
ATOM   7766  C  CG2   . VAL B 1 275 ? 124.940 131.202 135.987 1.00 43.95 ?  275 VAL B CG2   1 
ATOM   7767  N  N     . LYS B 1 276 ? 127.650 129.387 139.257 1.00 46.32 ?  276 LYS B N     1 
ATOM   7768  C  CA    . LYS B 1 276 ? 128.236 128.952 140.517 1.00 47.39 ?  276 LYS B CA    1 
ATOM   7769  C  C     . LYS B 1 276 ? 128.944 130.039 141.317 1.00 45.61 ?  276 LYS B C     1 
ATOM   7770  O  O     . LYS B 1 276 ? 129.080 129.878 142.536 1.00 51.16 ?  276 LYS B O     1 
ATOM   7771  C  CB    . LYS B 1 276 ? 129.218 127.792 140.273 1.00 48.20 ?  276 LYS B CB    1 
ATOM   7772  C  CG    . LYS B 1 276 ? 130.596 128.213 139.802 1.00 47.46 ?  276 LYS B CG    1 
ATOM   7773  C  CD    . LYS B 1 276 ? 131.301 127.078 139.081 1.00 50.60 ?  276 LYS B CD    1 
ATOM   7774  C  CE    . LYS B 1 276 ? 130.561 126.703 137.809 1.00 49.82 ?  276 LYS B CE    1 
ATOM   7775  N  NZ    . LYS B 1 276 ? 130.180 127.910 137.025 1.00 48.35 1  276 LYS B NZ    1 
ATOM   7776  N  N     . THR B 1 277 ? 129.400 131.123 140.693 1.00 37.24 ?  277 THR B N     1 
ATOM   7777  C  CA    . THR B 1 277 ? 130.051 132.206 141.422 1.00 36.87 ?  277 THR B CA    1 
ATOM   7778  C  C     . THR B 1 277 ? 129.180 133.444 141.568 1.00 38.11 ?  277 THR B C     1 
ATOM   7779  O  O     . THR B 1 277 ? 129.668 134.475 142.043 1.00 42.20 ?  277 THR B O     1 
ATOM   7780  C  CB    . THR B 1 277 ? 131.375 132.600 140.750 1.00 39.89 ?  277 THR B CB    1 
ATOM   7781  O  OG1   . THR B 1 277 ? 131.131 133.607 139.760 1.00 37.56 ?  277 THR B OG1   1 
ATOM   7782  C  CG2   . THR B 1 277 ? 132.028 131.399 140.104 1.00 40.45 ?  277 THR B CG2   1 
ATOM   7783  N  N     . LEU B 1 278 ? 127.912 133.375 141.180 1.00 29.21 ?  278 LEU B N     1 
ATOM   7784  C  CA    . LEU B 1 278 ? 127.004 134.515 141.235 1.00 29.10 ?  278 LEU B CA    1 
ATOM   7785  C  C     . LEU B 1 278 ? 125.844 134.165 142.158 1.00 23.31 ?  278 LEU B C     1 
ATOM   7786  O  O     . LEU B 1 278 ? 125.014 133.312 141.824 1.00 29.21 ?  278 LEU B O     1 
ATOM   7787  C  CB    . LEU B 1 278 ? 126.512 134.881 139.837 1.00 26.18 ?  278 LEU B CB    1 
ATOM   7788  C  CG    . LEU B 1 278 ? 125.654 136.126 139.641 1.00 26.72 ?  278 LEU B CG    1 
ATOM   7789  C  CD1   . LEU B 1 278 ? 126.524 137.361 139.554 1.00 23.26 ?  278 LEU B CD1   1 
ATOM   7790  C  CD2   . LEU B 1 278 ? 124.813 135.976 138.386 1.00 23.82 ?  278 LEU B CD2   1 
ATOM   7791  N  N     . SER B 1 279 ? 125.790 134.821 143.312 1.00 23.24 ?  279 SER B N     1 
ATOM   7792  C  CA    . SER B 1 279 ? 124.672 134.640 144.226 1.00 18.49 ?  279 SER B CA    1 
ATOM   7793  C  C     . SER B 1 279 ? 123.390 135.165 143.595 1.00 19.07 ?  279 SER B C     1 
ATOM   7794  O  O     . SER B 1 279 ? 123.410 136.055 142.742 1.00 29.86 ?  279 SER B O     1 
ATOM   7795  C  CB    . SER B 1 279 ? 124.940 135.358 145.546 1.00 17.19 ?  279 SER B CB    1 
ATOM   7796  O  OG    . SER B 1 279 ? 126.115 134.867 146.163 1.00 23.76 ?  279 SER B OG    1 
ATOM   7797  N  N     . ILE B 1 280 ? 122.262 134.599 144.009 1.00 20.84 ?  280 ILE B N     1 
ATOM   7798  C  CA    . ILE B 1 280 ? 120.970 134.964 143.449 1.00 19.36 ?  280 ILE B CA    1 
ATOM   7799  C  C     . ILE B 1 280 ? 120.077 135.485 144.565 1.00 20.82 ?  280 ILE B C     1 
ATOM   7800  O  O     . ILE B 1 280 ? 120.113 134.983 145.694 1.00 24.93 ?  280 ILE B O     1 
ATOM   7801  C  CB    . ILE B 1 280 ? 120.305 133.785 142.705 1.00 16.70 ?  280 ILE B CB    1 
ATOM   7802  C  CG1   . ILE B 1 280 ? 119.844 132.694 143.667 1.00 22.49 ?  280 ILE B CG1   1 
ATOM   7803  C  CG2   . ILE B 1 280 ? 121.274 133.176 141.722 1.00 25.14 ?  280 ILE B CG2   1 
ATOM   7804  C  CD1   . ILE B 1 280 ? 118.774 131.799 143.079 1.00 21.68 ?  280 ILE B CD1   1 
ATOM   7805  N  N     . GLY B 1 281 ? 119.311 136.520 144.253 1.00 11.91 ?  281 GLY B N     1 
ATOM   7806  C  CA    . GLY B 1 281 ? 118.325 137.042 145.175 1.00 6.43  ?  281 GLY B CA    1 
ATOM   7807  C  C     . GLY B 1 281 ? 117.006 137.251 144.466 1.00 8.98  ?  281 GLY B C     1 
ATOM   7808  O  O     . GLY B 1 281 ? 116.957 137.560 143.277 1.00 18.68 ?  281 GLY B O     1 
ATOM   7809  N  N     . VAL B 1 282 ? 115.926 137.068 145.217 1.00 8.40  ?  282 VAL B N     1 
ATOM   7810  C  CA    . VAL B 1 282 ? 114.572 137.189 144.693 1.00 14.89 ?  282 VAL B CA    1 
ATOM   7811  C  C     . VAL B 1 282 ? 113.863 138.302 145.448 1.00 11.81 ?  282 VAL B C     1 
ATOM   7812  O  O     . VAL B 1 282 ? 113.863 138.321 146.683 1.00 18.21 ?  282 VAL B O     1 
ATOM   7813  C  CB    . VAL B 1 282 ? 113.799 135.862 144.807 1.00 13.09 ?  282 VAL B CB    1 
ATOM   7814  C  CG1   . VAL B 1 282 ? 112.317 136.090 144.594 1.00 15.57 ?  282 VAL B CG1   1 
ATOM   7815  C  CG2   . VAL B 1 282 ? 114.325 134.865 143.794 1.00 19.32 ?  282 VAL B CG2   1 
ATOM   7816  N  N     . VAL B 1 283 ? 113.273 139.231 144.704 1.00 7.35  ?  283 VAL B N     1 
ATOM   7817  C  CA    . VAL B 1 283 ? 112.536 140.352 145.271 1.00 10.05 ?  283 VAL B CA    1 
ATOM   7818  C  C     . VAL B 1 283 ? 111.053 140.020 145.203 1.00 12.37 ?  283 VAL B C     1 
ATOM   7819  O  O     . VAL B 1 283 ? 110.493 139.861 144.112 1.00 22.54 ?  283 VAL B O     1 
ATOM   7820  C  CB    . VAL B 1 283 ? 112.853 141.659 144.531 1.00 6.35  ?  283 VAL B CB    1 
ATOM   7821  C  CG1   . VAL B 1 283 ? 112.170 142.829 145.210 1.00 9.67  ?  283 VAL B CG1   1 
ATOM   7822  C  CG2   . VAL B 1 283 ? 114.355 141.870 144.471 1.00 8.67  ?  283 VAL B CG2   1 
ATOM   7823  N  N     . ILE B 1 284 ? 110.419 139.917 146.364 1.00 17.09 ?  284 ILE B N     1 
ATOM   7824  C  CA    . ILE B 1 284 ? 109.039 139.459 146.481 1.00 17.92 ?  284 ILE B CA    1 
ATOM   7825  C  C     . ILE B 1 284 ? 108.185 140.639 146.937 1.00 17.41 ?  284 ILE B C     1 
ATOM   7826  O  O     . ILE B 1 284 ? 108.280 141.062 148.100 1.00 19.60 ?  284 ILE B O     1 
ATOM   7827  C  CB    . ILE B 1 284 ? 108.917 138.280 147.454 1.00 12.85 ?  284 ILE B CB    1 
ATOM   7828  C  CG1   . ILE B 1 284 ? 109.942 137.199 147.113 1.00 13.68 ?  284 ILE B CG1   1 
ATOM   7829  C  CG2   . ILE B 1 284 ? 107.506 137.716 147.428 1.00 17.19 ?  284 ILE B CG2   1 
ATOM   7830  C  CD1   . ILE B 1 284 ? 109.796 135.937 147.928 1.00 15.71 ?  284 ILE B CD1   1 
ATOM   7831  N  N     . PRO B 1 285 ? 107.346 141.203 146.074 1.00 22.30 ?  285 PRO B N     1 
ATOM   7832  C  CA    . PRO B 1 285 ? 106.364 142.187 146.536 1.00 25.67 ?  285 PRO B CA    1 
ATOM   7833  C  C     . PRO B 1 285 ? 105.285 141.529 147.382 1.00 25.21 ?  285 PRO B C     1 
ATOM   7834  O  O     . PRO B 1 285 ? 105.131 140.307 147.407 1.00 24.82 ?  285 PRO B O     1 
ATOM   7835  C  CB    . PRO B 1 285 ? 105.781 142.753 145.236 1.00 23.16 ?  285 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 1 285 ? 106.767 142.389 144.173 1.00 19.61 ?  285 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 1 285 ? 107.367 141.091 144.607 1.00 16.49 ?  285 PRO B CD    1 
ATOM   7838  N  N     . ASP B 1 286 ? 104.533 142.372 148.094 1.00 29.11 ?  286 ASP B N     1 
ATOM   7839  C  CA    . ASP B 1 286 ? 103.425 141.873 148.902 1.00 23.66 ?  286 ASP B CA    1 
ATOM   7840  C  C     . ASP B 1 286 ? 102.347 141.214 148.056 1.00 30.67 ?  286 ASP B C     1 
ATOM   7841  O  O     . ASP B 1 286 ? 101.594 140.380 148.571 1.00 32.81 ?  286 ASP B O     1 
ATOM   7842  C  CB    . ASP B 1 286 ? 102.818 143.011 149.723 1.00 26.22 ?  286 ASP B CB    1 
ATOM   7843  C  CG    . ASP B 1 286 ? 103.271 142.994 151.168 1.00 37.25 ?  286 ASP B CG    1 
ATOM   7844  O  OD1   . ASP B 1 286 ? 104.456 142.688 151.416 1.00 38.58 ?  286 ASP B OD1   1 
ATOM   7845  O  OD2   . ASP B 1 286 ? 102.444 143.291 152.055 1.00 39.34 -1 286 ASP B OD2   1 
ATOM   7846  N  N     . LYS B 1 287 ? 102.255 141.571 146.771 1.00 33.03 ?  287 LYS B N     1 
ATOM   7847  C  CA    . LYS B 1 287 ? 101.263 140.957 145.897 1.00 25.93 ?  287 LYS B CA    1 
ATOM   7848  C  C     . LYS B 1 287 ? 101.498 139.458 145.756 1.00 26.93 ?  287 LYS B C     1 
ATOM   7849  O  O     . LYS B 1 287 ? 100.544 138.673 145.757 1.00 33.99 ?  287 LYS B O     1 
ATOM   7850  C  CB    . LYS B 1 287 ? 101.282 141.632 144.527 1.00 27.63 ?  287 LYS B CB    1 
ATOM   7851  C  CG    . LYS B 1 287 ? 100.116 141.243 143.635 1.00 27.80 ?  287 LYS B CG    1 
ATOM   7852  C  CD    . LYS B 1 287 ? 98.793  141.463 144.346 1.00 32.66 ?  287 LYS B CD    1 
ATOM   7853  C  CE    . LYS B 1 287 ? 97.618  141.206 143.422 1.00 31.91 ?  287 LYS B CE    1 
ATOM   7854  N  NZ    . LYS B 1 287 ? 96.325  141.567 144.064 1.00 33.82 1  287 LYS B NZ    1 
ATOM   7855  N  N     . PHE B 1 288 ? 102.759 139.043 145.623 1.00 26.58 ?  288 PHE B N     1 
ATOM   7856  C  CA    . PHE B 1 288 ? 103.053 137.619 145.490 1.00 23.20 ?  288 PHE B CA    1 
ATOM   7857  C  C     . PHE B 1 288 ? 102.667 136.854 146.749 1.00 22.50 ?  288 PHE B C     1 
ATOM   7858  O  O     . PHE B 1 288 ? 102.101 135.758 146.670 1.00 30.53 ?  288 PHE B O     1 
ATOM   7859  C  CB    . PHE B 1 288 ? 104.533 137.412 145.174 1.00 27.79 ?  288 PHE B CB    1 
ATOM   7860  C  CG    . PHE B 1 288 ? 104.896 135.981 144.904 1.00 26.67 ?  288 PHE B CG    1 
ATOM   7861  C  CD1   . PHE B 1 288 ? 104.711 135.432 143.648 1.00 23.90 ?  288 PHE B CD1   1 
ATOM   7862  C  CD2   . PHE B 1 288 ? 105.412 135.180 145.910 1.00 23.29 ?  288 PHE B CD2   1 
ATOM   7863  C  CE1   . PHE B 1 288 ? 105.038 134.116 143.397 1.00 28.59 ?  288 PHE B CE1   1 
ATOM   7864  C  CE2   . PHE B 1 288 ? 105.740 133.863 145.665 1.00 24.98 ?  288 PHE B CE2   1 
ATOM   7865  C  CZ    . PHE B 1 288 ? 105.555 133.331 144.407 1.00 26.34 ?  288 PHE B CZ    1 
ATOM   7866  N  N     . VAL B 1 289 ? 102.974 137.413 147.920 1.00 25.75 ?  289 VAL B N     1 
ATOM   7867  C  CA    . VAL B 1 289 ? 102.611 136.761 149.173 1.00 26.07 ?  289 VAL B CA    1 
ATOM   7868  C  C     . VAL B 1 289 ? 101.097 136.697 149.320 1.00 26.59 ?  289 VAL B C     1 
ATOM   7869  O  O     . VAL B 1 289 ? 100.550 135.707 149.818 1.00 29.88 ?  289 VAL B O     1 
ATOM   7870  C  CB    . VAL B 1 289 ? 103.268 137.484 150.361 1.00 31.81 ?  289 VAL B CB    1 
ATOM   7871  C  CG1   . VAL B 1 289 ? 103.040 136.710 151.648 1.00 23.07 ?  289 VAL B CG1   1 
ATOM   7872  C  CG2   . VAL B 1 289 ? 104.754 137.681 150.105 1.00 25.12 ?  289 VAL B CG2   1 
ATOM   7873  N  N     . GLU B 1 290 ? 100.398 137.749 148.893 1.00 34.76 ?  290 GLU B N     1 
ATOM   7874  C  CA    . GLU B 1 290 ? 98.939  137.740 148.938 1.00 30.92 ?  290 GLU B CA    1 
ATOM   7875  C  C     . GLU B 1 290 ? 98.363  136.667 148.020 1.00 34.54 ?  290 GLU B C     1 
ATOM   7876  O  O     . GLU B 1 290 ? 97.428  135.951 148.398 1.00 39.59 ?  290 GLU B O     1 
ATOM   7877  C  CB    . GLU B 1 290 ? 98.401  139.121 148.567 1.00 28.23 ?  290 GLU B CB    1 
ATOM   7878  C  CG    . GLU B 1 290 ? 97.045  139.111 147.883 1.00 37.04 ?  290 GLU B CG    1 
ATOM   7879  C  CD    . GLU B 1 290 ? 96.515  140.507 147.628 1.00 41.41 ?  290 GLU B CD    1 
ATOM   7880  O  OE1   . GLU B 1 290 ? 96.537  141.332 148.565 1.00 42.37 ?  290 GLU B OE1   1 
ATOM   7881  O  OE2   . GLU B 1 290 ? 96.079  140.781 146.491 1.00 38.39 -1 290 GLU B OE2   1 
ATOM   7882  N  N     . LEU B 1 291 ? 98.913  136.539 146.810 1.00 27.28 ?  291 LEU B N     1 
ATOM   7883  C  CA    . LEU B 1 291 ? 98.439  135.517 145.880 1.00 25.18 ?  291 LEU B CA    1 
ATOM   7884  C  C     . LEU B 1 291 ? 98.708  134.115 146.411 1.00 32.91 ?  291 LEU B C     1 
ATOM   7885  O  O     . LEU B 1 291 ? 97.855  133.227 146.292 1.00 37.34 ?  291 LEU B O     1 
ATOM   7886  C  CB    . LEU B 1 291 ? 99.097  135.704 144.512 1.00 29.43 ?  291 LEU B CB    1 
ATOM   7887  C  CG    . LEU B 1 291 ? 98.728  136.966 143.732 1.00 29.44 ?  291 LEU B CG    1 
ATOM   7888  C  CD1   . LEU B 1 291 ? 99.796  137.285 142.703 1.00 26.20 ?  291 LEU B CD1   1 
ATOM   7889  C  CD2   . LEU B 1 291 ? 97.371  136.813 143.070 1.00 32.36 ?  291 LEU B CD2   1 
ATOM   7890  N  N     . ALA B 1 292 ? 99.893  133.891 146.985 1.00 32.40 ?  292 ALA B N     1 
ATOM   7891  C  CA    . ALA B 1 292 ? 100.203 132.585 147.557 1.00 27.35 ?  292 ALA B CA    1 
ATOM   7892  C  C     . ALA B 1 292 ? 99.303  132.276 148.748 1.00 29.21 ?  292 ALA B C     1 
ATOM   7893  O  O     . ALA B 1 292 ? 98.873  131.131 148.928 1.00 36.30 ?  292 ALA B O     1 
ATOM   7894  C  CB    . ALA B 1 292 ? 101.674 132.525 147.963 1.00 27.19 ?  292 ALA B CB    1 
ATOM   7895  N  N     . ARG B 1 293 ? 99.015  133.284 149.573 1.00 28.11 ?  293 ARG B N     1 
ATOM   7896  C  CA    . ARG B 1 293 ? 98.153  133.083 150.732 1.00 28.07 ?  293 ARG B CA    1 
ATOM   7897  C  C     . ARG B 1 293 ? 96.746  132.678 150.314 1.00 35.25 ?  293 ARG B C     1 
ATOM   7898  O  O     . ARG B 1 293 ? 96.144  131.783 150.917 1.00 39.63 ?  293 ARG B O     1 
ATOM   7899  C  CB    . ARG B 1 293 ? 98.123  134.358 151.575 1.00 29.39 ?  293 ARG B CB    1 
ATOM   7900  C  CG    . ARG B 1 293 ? 96.995  134.432 152.586 1.00 31.61 ?  293 ARG B CG    1 
ATOM   7901  C  CD    . ARG B 1 293 ? 96.859  135.844 153.123 1.00 32.58 ?  293 ARG B CD    1 
ATOM   7902  N  NE    . ARG B 1 293 ? 98.154  136.407 153.485 1.00 38.76 ?  293 ARG B NE    1 
ATOM   7903  C  CZ    . ARG B 1 293 ? 98.614  137.570 153.047 1.00 37.05 ?  293 ARG B CZ    1 
ATOM   7904  N  NH1   . ARG B 1 293 ? 97.903  138.333 152.234 1.00 36.91 1  293 ARG B NH1   1 
ATOM   7905  N  NH2   . ARG B 1 293 ? 99.821  137.976 153.431 1.00 29.92 ?  293 ARG B NH2   1 
ATOM   7906  N  N     . GLU B 1 294 ? 96.211  133.318 149.278 1.00 44.02 ?  294 GLU B N     1 
ATOM   7907  C  CA    . GLU B 1 294 ? 94.875  133.017 148.785 1.00 41.02 ?  294 GLU B CA    1 
ATOM   7908  C  C     . GLU B 1 294 ? 94.847  131.826 147.836 1.00 42.10 ?  294 GLU B C     1 
ATOM   7909  O  O     . GLU B 1 294 ? 93.762  131.446 147.382 1.00 46.91 ?  294 GLU B O     1 
ATOM   7910  C  CB    . GLU B 1 294 ? 94.288  134.248 148.090 1.00 37.63 ?  294 GLU B CB    1 
ATOM   7911  C  CG    . GLU B 1 294 ? 94.193  135.471 148.986 1.00 42.57 ?  294 GLU B CG    1 
ATOM   7912  C  CD    . GLU B 1 294 ? 93.822  136.727 148.224 1.00 48.77 ?  294 GLU B CD    1 
ATOM   7913  O  OE1   . GLU B 1 294 ? 93.697  136.657 146.984 1.00 48.12 ?  294 GLU B OE1   1 
ATOM   7914  O  OE2   . GLU B 1 294 ? 93.656  137.786 148.865 1.00 45.21 -1 294 GLU B OE2   1 
ATOM   7915  N  N     . ASP B 1 295 ? 96.005  131.245 147.522 1.00 39.29 ?  295 ASP B N     1 
ATOM   7916  C  CA    . ASP B 1 295 ? 96.133  130.091 146.634 1.00 41.69 ?  295 ASP B CA    1 
ATOM   7917  C  C     . ASP B 1 295 ? 95.633  130.382 145.223 1.00 45.58 ?  295 ASP B C     1 
ATOM   7918  O  O     . ASP B 1 295 ? 95.372  129.454 144.450 1.00 46.25 ?  295 ASP B O     1 
ATOM   7919  C  CB    . ASP B 1 295 ? 95.414  128.862 147.206 1.00 45.70 ?  295 ASP B CB    1 
ATOM   7920  C  CG    . ASP B 1 295 ? 96.183  127.577 146.972 1.00 50.22 ?  295 ASP B CG    1 
ATOM   7921  O  OD1   . ASP B 1 295 ? 96.036  126.639 147.783 1.00 47.79 ?  295 ASP B OD1   1 
ATOM   7922  O  OD2   . ASP B 1 295 ? 96.936  127.506 145.978 1.00 47.83 -1 295 ASP B OD2   1 
ATOM   7923  N  N     . LYS B 1 296 ? 95.494  131.657 144.870 1.00 45.81 ?  296 LYS B N     1 
ATOM   7924  C  CA    . LYS B 1 296 ? 95.105  132.035 143.521 1.00 44.99 ?  296 LYS B CA    1 
ATOM   7925  C  C     . LYS B 1 296 ? 96.316  131.966 142.602 1.00 46.34 ?  296 LYS B C     1 
ATOM   7926  O  O     . LYS B 1 296 ? 97.395  132.457 142.948 1.00 48.28 ?  296 LYS B O     1 
ATOM   7927  C  CB    . LYS B 1 296 ? 94.509  133.442 143.513 1.00 45.13 ?  296 LYS B CB    1 
ATOM   7928  C  CG    . LYS B 1 296 ? 93.233  133.579 144.327 1.00 46.13 ?  296 LYS B CG    1 
ATOM   7929  C  CD    . LYS B 1 296 ? 92.727  135.011 144.327 1.00 46.16 ?  296 LYS B CD    1 
ATOM   7930  C  CE    . LYS B 1 296 ? 91.399  135.127 145.059 1.00 47.56 ?  296 LYS B CE    1 
ATOM   7931  N  NZ    . LYS B 1 296 ? 91.023  136.546 145.308 1.00 45.77 1  296 LYS B NZ    1 
ATOM   7932  N  N     . ALA B 1 297 ? 96.141  131.352 141.433 1.00 44.65 ?  297 ALA B N     1 
ATOM   7933  C  CA    . ALA B 1 297 ? 97.240  131.219 140.486 1.00 43.38 ?  297 ALA B CA    1 
ATOM   7934  C  C     . ALA B 1 297 ? 97.740  132.593 140.059 1.00 42.38 ?  297 ALA B C     1 
ATOM   7935  O  O     . ALA B 1 297 ? 96.953  133.470 139.692 1.00 44.72 ?  297 ALA B O     1 
ATOM   7936  C  CB    . ALA B 1 297 ? 96.795  130.413 139.268 1.00 42.71 ?  297 ALA B CB    1 
ATOM   7937  N  N     . ALA B 1 298 ? 99.055  132.776 140.109 1.00 34.57 ?  298 ALA B N     1 
ATOM   7938  C  CA    . ALA B 1 298 ? 99.658  134.061 139.807 1.00 33.18 ?  298 ALA B CA    1 
ATOM   7939  C  C     . ALA B 1 298 ? 100.146 134.093 138.364 1.00 35.87 ?  298 ALA B C     1 
ATOM   7940  O  O     . ALA B 1 298 ? 100.114 133.095 137.643 1.00 40.21 ?  298 ALA B O     1 
ATOM   7941  C  CB    . ALA B 1 298 ? 100.810 134.351 140.768 1.00 34.50 ?  298 ALA B CB    1 
ATOM   7942  N  N     . TYR B 1 299 ? 100.615 135.263 137.944 1.00 36.18 ?  299 TYR B N     1 
ATOM   7943  C  CA    . TYR B 1 299 ? 101.128 135.451 136.595 1.00 25.69 ?  299 TYR B CA    1 
ATOM   7944  C  C     . TYR B 1 299 ? 102.484 136.133 136.663 1.00 27.90 ?  299 TYR B C     1 
ATOM   7945  O  O     . TYR B 1 299 ? 102.619 137.195 137.279 1.00 34.61 ?  299 TYR B O     1 
ATOM   7946  C  CB    . TYR B 1 299 ? 100.161 136.281 135.747 1.00 30.33 ?  299 TYR B CB    1 
ATOM   7947  C  CG    . TYR B 1 299 ? 98.975  135.500 135.228 1.00 31.78 ?  299 TYR B CG    1 
ATOM   7948  C  CD1   . TYR B 1 299 ? 99.107  134.628 134.157 1.00 33.34 ?  299 TYR B CD1   1 
ATOM   7949  C  CD2   . TYR B 1 299 ? 97.720  135.645 135.804 1.00 32.79 ?  299 TYR B CD2   1 
ATOM   7950  C  CE1   . TYR B 1 299 ? 98.027  133.916 133.679 1.00 33.86 ?  299 TYR B CE1   1 
ATOM   7951  C  CE2   . TYR B 1 299 ? 96.632  134.937 135.332 1.00 33.08 ?  299 TYR B CE2   1 
ATOM   7952  C  CZ    . TYR B 1 299 ? 96.791  134.074 134.269 1.00 35.07 ?  299 TYR B CZ    1 
ATOM   7953  O  OH    . TYR B 1 299 ? 95.710  133.367 133.793 1.00 37.22 ?  299 TYR B OH    1 
ATOM   7954  N  N     . VAL B 1 300 ? 103.480 135.524 136.040 1.00 29.64 ?  300 VAL B N     1 
ATOM   7955  C  CA    . VAL B 1 300 ? 104.769 136.170 135.830 1.00 22.32 ?  300 VAL B CA    1 
ATOM   7956  C  C     . VAL B 1 300 ? 104.707 136.890 134.493 1.00 25.64 ?  300 VAL B C     1 
ATOM   7957  O  O     . VAL B 1 300 ? 103.975 136.483 133.589 1.00 30.12 ?  300 VAL B O     1 
ATOM   7958  C  CB    . VAL B 1 300 ? 105.932 135.159 135.885 1.00 24.45 ?  300 VAL B CB    1 
ATOM   7959  C  CG1   . VAL B 1 300 ? 106.195 134.737 137.320 1.00 23.16 ?  300 VAL B CG1   1 
ATOM   7960  C  CG2   . VAL B 1 300 ? 105.630 133.951 135.014 1.00 26.14 ?  300 VAL B CG2   1 
ATOM   7961  N  N     . PHE B 1 301 ? 105.466 137.969 134.357 1.00 25.84 ?  301 PHE B N     1 
ATOM   7962  C  CA    . PHE B 1 301 ? 105.278 138.879 133.242 1.00 20.81 ?  301 PHE B CA    1 
ATOM   7963  C  C     . PHE B 1 301 ? 106.545 139.017 132.412 1.00 28.11 ?  301 PHE B C     1 
ATOM   7964  O  O     . PHE B 1 301 ? 107.663 138.823 132.896 1.00 29.52 ?  301 PHE B O     1 
ATOM   7965  C  CB    . PHE B 1 301 ? 104.829 140.258 133.736 1.00 24.66 ?  301 PHE B CB    1 
ATOM   7966  C  CG    . PHE B 1 301 ? 103.555 140.227 134.522 1.00 27.51 ?  301 PHE B CG    1 
ATOM   7967  C  CD1   . PHE B 1 301 ? 102.344 140.014 133.890 1.00 26.92 ?  301 PHE B CD1   1 
ATOM   7968  C  CD2   . PHE B 1 301 ? 103.568 140.404 135.894 1.00 25.39 ?  301 PHE B CD2   1 
ATOM   7969  C  CE1   . PHE B 1 301 ? 101.170 139.977 134.610 1.00 27.62 ?  301 PHE B CE1   1 
ATOM   7970  C  CE2   . PHE B 1 301 ? 102.398 140.370 136.618 1.00 28.97 ?  301 PHE B CE2   1 
ATOM   7971  C  CZ    . PHE B 1 301 ? 101.196 140.159 135.975 1.00 28.06 ?  301 PHE B CZ    1 
ATOM   7972  N  N     . TYR B 1 302 ? 106.340 139.356 131.139 1.00 25.95 ?  302 TYR B N     1 
ATOM   7973  C  CA    . TYR B 1 302 ? 107.434 139.677 130.237 1.00 26.54 ?  302 TYR B CA    1 
ATOM   7974  C  C     . TYR B 1 302 ? 107.727 141.164 130.366 1.00 29.50 ?  302 TYR B C     1 
ATOM   7975  O  O     . TYR B 1 302 ? 106.856 141.984 130.037 1.00 30.63 ?  302 TYR B O     1 
ATOM   7976  C  CB    . TYR B 1 302 ? 107.068 139.325 128.802 1.00 25.74 ?  302 TYR B CB    1 
ATOM   7977  C  CG    . TYR B 1 302 ? 107.032 137.841 128.522 1.00 27.02 ?  302 TYR B CG    1 
ATOM   7978  C  CD1   . TYR B 1 302 ? 105.985 137.053 128.979 1.00 25.03 ?  302 TYR B CD1   1 
ATOM   7979  C  CD2   . TYR B 1 302 ? 108.043 137.228 127.798 1.00 27.54 ?  302 TYR B CD2   1 
ATOM   7980  C  CE1   . TYR B 1 302 ? 105.947 135.699 128.724 1.00 25.70 ?  302 TYR B CE1   1 
ATOM   7981  C  CE2   . TYR B 1 302 ? 108.014 135.874 127.536 1.00 26.81 ?  302 TYR B CE2   1 
ATOM   7982  C  CZ    . TYR B 1 302 ? 106.963 135.115 128.002 1.00 30.33 ?  302 TYR B CZ    1 
ATOM   7983  O  OH    . TYR B 1 302 ? 106.933 133.764 127.745 1.00 33.17 ?  302 TYR B OH    1 
ATOM   7984  N  N     . PRO B 1 303 ? 108.904 141.560 130.852 1.00 28.05 ?  303 PRO B N     1 
ATOM   7985  C  CA    . PRO B 1 303 ? 109.153 142.989 131.103 1.00 25.48 ?  303 PRO B CA    1 
ATOM   7986  C  C     . PRO B 1 303 ? 109.059 143.864 129.867 1.00 29.88 ?  303 PRO B C     1 
ATOM   7987  O  O     . PRO B 1 303 ? 108.621 145.016 129.972 1.00 30.10 ?  303 PRO B O     1 
ATOM   7988  C  CB    . PRO B 1 303 ? 110.573 142.998 131.686 1.00 23.10 ?  303 PRO B CB    1 
ATOM   7989  C  CG    . PRO B 1 303 ? 110.779 141.628 132.211 1.00 25.78 ?  303 PRO B CG    1 
ATOM   7990  C  CD    . PRO B 1 303 ? 110.023 140.717 131.301 1.00 22.71 ?  303 PRO B CD    1 
ATOM   7991  N  N     . HIS B 1 304 ? 109.460 143.358 128.698 1.00 29.63 ?  304 HIS B N     1 
ATOM   7992  C  CA    . HIS B 1 304 ? 109.506 144.214 127.516 1.00 29.90 ?  304 HIS B CA    1 
ATOM   7993  C  C     . HIS B 1 304 ? 108.108 144.572 127.032 1.00 31.79 ?  304 HIS B C     1 
ATOM   7994  O  O     . HIS B 1 304 ? 107.880 145.692 126.563 1.00 37.64 ?  304 HIS B O     1 
ATOM   7995  C  CB    . HIS B 1 304 ? 110.300 143.543 126.400 1.00 27.70 ?  304 HIS B CB    1 
ATOM   7996  C  CG    . HIS B 1 304 ? 110.533 144.429 125.218 1.00 28.80 ?  304 HIS B CG    1 
ATOM   7997  N  ND1   . HIS B 1 304 ? 110.878 145.757 125.343 1.00 27.07 ?  304 HIS B ND1   1 
ATOM   7998  C  CD2   . HIS B 1 304 ? 110.466 144.181 123.889 1.00 35.59 ?  304 HIS B CD2   1 
ATOM   7999  C  CE1   . HIS B 1 304 ? 111.016 146.288 124.142 1.00 30.15 ?  304 HIS B CE1   1 
ATOM   8000  N  NE2   . HIS B 1 304 ? 110.772 145.354 123.242 1.00 35.61 ?  304 HIS B NE2   1 
ATOM   8001  N  N     . THR B 1 305 ? 107.161 143.637 127.124 1.00 28.56 ?  305 THR B N     1 
ATOM   8002  C  CA    . THR B 1 305 ? 105.786 143.947 126.749 1.00 32.68 ?  305 THR B CA    1 
ATOM   8003  C  C     . THR B 1 305 ? 105.198 145.016 127.659 1.00 29.26 ?  305 THR B C     1 
ATOM   8004  O  O     . THR B 1 305 ? 104.515 145.937 127.193 1.00 34.96 ?  305 THR B O     1 
ATOM   8005  C  CB    . THR B 1 305 ? 104.933 142.679 126.788 1.00 30.45 ?  305 THR B CB    1 
ATOM   8006  O  OG1   . THR B 1 305 ? 104.860 142.192 128.133 1.00 28.12 ?  305 THR B OG1   1 
ATOM   8007  C  CG2   . THR B 1 305 ? 105.538 141.607 125.901 1.00 31.29 ?  305 THR B CG2   1 
ATOM   8008  N  N     . ILE B 1 306 ? 105.466 144.917 128.962 1.00 29.89 ?  306 ILE B N     1 
ATOM   8009  C  CA    . ILE B 1 306 ? 104.990 145.922 129.906 1.00 30.13 ?  306 ILE B CA    1 
ATOM   8010  C  C     . ILE B 1 306 ? 105.628 147.273 129.610 1.00 29.22 ?  306 ILE B C     1 
ATOM   8011  O  O     . ILE B 1 306 ? 104.961 148.314 129.657 1.00 34.03 ?  306 ILE B O     1 
ATOM   8012  C  CB    . ILE B 1 306 ? 105.265 145.464 131.349 1.00 26.76 ?  306 ILE B CB    1 
ATOM   8013  C  CG1   . ILE B 1 306 ? 104.342 144.307 131.721 1.00 26.49 ?  306 ILE B CG1   1 
ATOM   8014  C  CG2   . ILE B 1 306 ? 105.096 146.612 132.320 1.00 29.75 ?  306 ILE B CG2   1 
ATOM   8015  C  CD1   . ILE B 1 306 ? 104.591 143.757 133.094 1.00 28.94 ?  306 ILE B CD1   1 
ATOM   8016  N  N     . TYR B 1 307 ? 106.926 147.280 129.305 1.00 30.63 ?  307 TYR B N     1 
ATOM   8017  C  CA    . TYR B 1 307 ? 107.601 148.533 128.984 1.00 27.67 ?  307 TYR B CA    1 
ATOM   8018  C  C     . TYR B 1 307 ? 107.039 149.150 127.709 1.00 31.63 ?  307 TYR B C     1 
ATOM   8019  O  O     . TYR B 1 307 ? 106.874 150.371 127.624 1.00 35.31 ?  307 TYR B O     1 
ATOM   8020  C  CB    . TYR B 1 307 ? 109.108 148.300 128.866 1.00 24.46 ?  307 TYR B CB    1 
ATOM   8021  C  CG    . TYR B 1 307 ? 109.912 149.544 128.552 1.00 31.21 ?  307 TYR B CG    1 
ATOM   8022  C  CD1   . TYR B 1 307 ? 110.048 150.003 127.246 1.00 31.54 ?  307 TYR B CD1   1 
ATOM   8023  C  CD2   . TYR B 1 307 ? 110.520 150.270 129.566 1.00 26.86 ?  307 TYR B CD2   1 
ATOM   8024  C  CE1   . TYR B 1 307 ? 110.774 151.139 126.963 1.00 31.01 ?  307 TYR B CE1   1 
ATOM   8025  C  CE2   . TYR B 1 307 ? 111.247 151.408 129.292 1.00 29.82 ?  307 TYR B CE2   1 
ATOM   8026  C  CZ    . TYR B 1 307 ? 111.371 151.838 127.989 1.00 34.47 ?  307 TYR B CZ    1 
ATOM   8027  O  OH    . TYR B 1 307 ? 112.096 152.973 127.709 1.00 36.60 ?  307 TYR B OH    1 
ATOM   8028  N  N     . LYS B 1 308 ? 106.753 148.322 126.703 1.00 34.42 ?  308 LYS B N     1 
ATOM   8029  C  CA    . LYS B 1 308 ? 106.162 148.826 125.469 1.00 31.88 ?  308 LYS B CA    1 
ATOM   8030  C  C     . LYS B 1 308 ? 104.780 149.412 125.719 1.00 31.61 ?  308 LYS B C     1 
ATOM   8031  O  O     . LYS B 1 308 ? 104.441 150.474 125.183 1.00 36.40 ?  308 LYS B O     1 
ATOM   8032  C  CB    . LYS B 1 308 ? 106.086 147.706 124.432 1.00 32.36 ?  308 LYS B CB    1 
ATOM   8033  C  CG    . LYS B 1 308 ? 107.378 147.470 123.667 1.00 33.85 ?  308 LYS B CG    1 
ATOM   8034  C  CD    . LYS B 1 308 ? 107.522 146.018 123.219 1.00 35.89 ?  308 LYS B CD    1 
ATOM   8035  C  CE    . LYS B 1 308 ? 106.204 145.259 123.275 1.00 36.98 ?  308 LYS B CE    1 
ATOM   8036  N  NZ    . LYS B 1 308 ? 106.172 144.124 122.313 1.00 35.60 1  308 LYS B NZ    1 
ATOM   8037  N  N     . GLU B 1 309 ? 103.967 148.736 126.533 1.00 29.97 ?  309 GLU B N     1 
ATOM   8038  C  CA    . GLU B 1 309 ? 102.595 149.186 126.740 1.00 34.83 ?  309 GLU B CA    1 
ATOM   8039  C  C     . GLU B 1 309 ? 102.532 150.438 127.607 1.00 35.03 ?  309 GLU B C     1 
ATOM   8040  O  O     . GLU B 1 309 ? 101.774 151.368 127.306 1.00 37.16 ?  309 GLU B O     1 
ATOM   8041  C  CB    . GLU B 1 309 ? 101.765 148.064 127.360 1.00 32.85 ?  309 GLU B CB    1 
ATOM   8042  C  CG    . GLU B 1 309 ? 100.417 148.520 127.887 1.00 35.09 ?  309 GLU B CG    1 
ATOM   8043  C  CD    . GLU B 1 309 ? 99.465  148.951 126.788 1.00 40.22 ?  309 GLU B CD    1 
ATOM   8044  O  OE1   . GLU B 1 309 ? 99.694  148.585 125.617 1.00 40.62 ?  309 GLU B OE1   1 
ATOM   8045  O  OE2   . GLU B 1 309 ? 98.485  149.659 127.098 1.00 39.65 -1 309 GLU B OE2   1 
ATOM   8046  N  N     . TYR B 1 310 ? 103.316 150.487 128.683 1.00 33.44 ?  310 TYR B N     1 
ATOM   8047  C  CA    . TYR B 1 310 ? 103.193 151.548 129.672 1.00 33.04 ?  310 TYR B CA    1 
ATOM   8048  C  C     . TYR B 1 310 ? 104.319 152.570 129.627 1.00 31.90 ?  310 TYR B C     1 
ATOM   8049  O  O     . TYR B 1 310 ? 104.171 153.649 130.211 1.00 31.87 ?  310 TYR B O     1 
ATOM   8050  C  CB    . TYR B 1 310 ? 103.119 150.946 131.083 1.00 31.08 ?  310 TYR B CB    1 
ATOM   8051  C  CG    . TYR B 1 310 ? 101.949 150.010 131.282 1.00 32.59 ?  310 TYR B CG    1 
ATOM   8052  C  CD1   . TYR B 1 310 ? 100.698 150.497 131.641 1.00 31.36 ?  310 TYR B CD1   1 
ATOM   8053  C  CD2   . TYR B 1 310 ? 102.091 148.640 131.105 1.00 32.26 ?  310 TYR B CD2   1 
ATOM   8054  C  CE1   . TYR B 1 310 ? 99.626  149.646 131.821 1.00 33.04 ?  310 TYR B CE1   1 
ATOM   8055  C  CE2   . TYR B 1 310 ? 101.023 147.782 131.281 1.00 32.17 ?  310 TYR B CE2   1 
ATOM   8056  C  CZ    . TYR B 1 310 ? 99.795  148.290 131.642 1.00 33.62 ?  310 TYR B CZ    1 
ATOM   8057  O  OH    . TYR B 1 310 ? 98.730  147.439 131.820 1.00 34.39 ?  310 TYR B OH    1 
ATOM   8058  N  N     . GLY B 1 311 ? 105.428 152.272 128.957 1.00 29.63 ?  311 GLY B N     1 
ATOM   8059  C  CA    . GLY B 1 311 ? 106.558 153.173 128.931 1.00 29.67 ?  311 GLY B CA    1 
ATOM   8060  C  C     . GLY B 1 311 ? 107.466 153.091 130.136 1.00 34.53 ?  311 GLY B C     1 
ATOM   8061  O  O     . GLY B 1 311 ? 108.464 153.820 130.189 1.00 36.90 ?  311 GLY B O     1 
ATOM   8062  N  N     . GLN B 1 312 ? 107.156 152.232 131.103 1.00 31.52 ?  312 GLN B N     1 
ATOM   8063  C  CA    . GLN B 1 312 ? 107.968 152.059 132.296 1.00 29.78 ?  312 GLN B CA    1 
ATOM   8064  C  C     . GLN B 1 312 ? 108.260 150.579 132.498 1.00 32.31 ?  312 GLN B C     1 
ATOM   8065  O  O     . GLN B 1 312 ? 107.524 149.709 132.025 1.00 39.23 ?  312 GLN B O     1 
ATOM   8066  C  CB    . GLN B 1 312 ? 107.279 152.629 133.544 1.00 32.47 ?  312 GLN B CB    1 
ATOM   8067  C  CG    . GLN B 1 312 ? 106.283 153.739 133.262 1.00 31.94 ?  312 GLN B CG    1 
ATOM   8068  C  CD    . GLN B 1 312 ? 105.331 153.973 134.416 1.00 35.90 ?  312 GLN B CD    1 
ATOM   8069  O  OE1   . GLN B 1 312 ? 105.725 154.475 135.469 1.00 38.51 ?  312 GLN B OE1   1 
ATOM   8070  N  NE2   . GLN B 1 312 ? 104.069 153.610 134.226 1.00 33.65 ?  312 GLN B NE2   1 
ATOM   8071  N  N     . HIS B 1 313 ? 109.348 150.305 133.210 1.00 29.23 ?  313 HIS B N     1 
ATOM   8072  C  CA    . HIS B 1 313 ? 109.727 148.933 133.496 1.00 29.45 ?  313 HIS B CA    1 
ATOM   8073  C  C     . HIS B 1 313 ? 108.782 148.318 134.525 1.00 32.07 ?  313 HIS B C     1 
ATOM   8074  O  O     . HIS B 1 313 ? 108.123 149.015 135.301 1.00 32.39 ?  313 HIS B O     1 
ATOM   8075  C  CB    . HIS B 1 313 ? 111.170 148.872 133.994 1.00 26.13 ?  313 HIS B CB    1 
ATOM   8076  C  CG    . HIS B 1 313 ? 112.164 149.431 133.024 1.00 27.87 ?  313 HIS B CG    1 
ATOM   8077  N  ND1   . HIS B 1 313 ? 112.657 148.701 131.963 1.00 30.95 ?  313 HIS B ND1   1 
ATOM   8078  C  CD2   . HIS B 1 313 ? 112.754 150.646 132.951 1.00 29.49 ?  313 HIS B CD2   1 
ATOM   8079  C  CE1   . HIS B 1 313 ? 113.509 149.444 131.280 1.00 28.56 ?  313 HIS B CE1   1 
ATOM   8080  N  NE2   . HIS B 1 313 ? 113.586 150.628 131.858 1.00 30.09 ?  313 HIS B NE2   1 
ATOM   8081  N  N     . MET B 1 314 ? 108.718 146.984 134.517 1.00 35.31 ?  314 MET B N     1 
ATOM   8082  C  CA    . MET B 1 314 ? 107.817 146.279 135.424 1.00 30.43 ?  314 MET B CA    1 
ATOM   8083  C  C     . MET B 1 314 ? 108.191 146.526 136.880 1.00 37.07 ?  314 MET B C     1 
ATOM   8084  O  O     . MET B 1 314 ? 107.313 146.708 137.731 1.00 39.69 ?  314 MET B O     1 
ATOM   8085  C  CB    . MET B 1 314 ? 107.823 144.783 135.116 1.00 28.98 ?  314 MET B CB    1 
ATOM   8086  C  CG    . MET B 1 314 ? 106.815 143.993 135.933 1.00 29.54 ?  314 MET B CG    1 
ATOM   8087  S  SD    . MET B 1 314 ? 107.266 142.271 136.207 1.00 45.32 ?  314 MET B SD    1 
ATOM   8088  C  CE    . MET B 1 314 ? 108.423 142.000 134.873 1.00 30.08 ?  314 MET B CE    1 
ATOM   8089  N  N     . ASP B 1 315 ? 109.486 146.536 137.187 1.00 30.29 ?  315 ASP B N     1 
ATOM   8090  C  CA    . ASP B 1 315 ? 109.943 146.795 138.546 1.00 34.42 ?  315 ASP B CA    1 
ATOM   8091  C  C     . ASP B 1 315 ? 110.014 148.281 138.872 1.00 30.20 ?  315 ASP B C     1 
ATOM   8092  O  O     . ASP B 1 315 ? 110.367 148.634 140.001 1.00 36.93 ?  315 ASP B O     1 
ATOM   8093  C  CB    . ASP B 1 315 ? 111.312 146.147 138.775 1.00 33.18 ?  315 ASP B CB    1 
ATOM   8094  C  CG    . ASP B 1 315 ? 112.392 146.745 137.900 1.00 32.79 ?  315 ASP B CG    1 
ATOM   8095  O  OD1   . ASP B 1 315 ? 112.059 147.249 136.808 1.00 36.65 ?  315 ASP B OD1   1 
ATOM   8096  O  OD2   . ASP B 1 315 ? 113.571 146.712 138.304 1.00 29.78 -1 315 ASP B OD2   1 
ATOM   8097  N  N     . GLU B 1 316 ? 109.692 149.153 137.916 1.00 28.38 ?  316 GLU B N     1 
ATOM   8098  C  CA    . GLU B 1 316 ? 109.694 150.589 138.151 1.00 29.96 ?  316 GLU B CA    1 
ATOM   8099  C  C     . GLU B 1 316 ? 108.403 151.092 138.785 1.00 35.54 ?  316 GLU B C     1 
ATOM   8100  O  O     . GLU B 1 316 ? 108.356 152.250 139.211 1.00 39.07 ?  316 GLU B O     1 
ATOM   8101  C  CB    . GLU B 1 316 ? 109.932 151.335 136.835 1.00 36.44 ?  316 GLU B CB    1 
ATOM   8102  C  CG    . GLU B 1 316 ? 111.384 151.688 136.558 1.00 34.69 ?  316 GLU B CG    1 
ATOM   8103  C  CD    . GLU B 1 316 ? 112.148 152.075 137.807 1.00 36.36 ?  316 GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 1 316 ? 111.726 153.028 138.497 1.00 38.09 ?  316 GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 1 316 ? 113.175 151.430 138.096 1.00 41.39 -1 316 GLU B OE2   1 
ATOM   8106  N  N     . MET B 1 317 ? 107.365 150.264 138.854 1.00 38.06 ?  317 MET B N     1 
ATOM   8107  C  CA    . MET B 1 317 ? 106.080 150.669 139.401 1.00 38.40 ?  317 MET B CA    1 
ATOM   8108  C  C     . MET B 1 317 ? 105.584 149.628 140.395 1.00 37.91 ?  317 MET B C     1 
ATOM   8109  O  O     . MET B 1 317 ? 106.135 148.532 140.517 1.00 37.39 ?  317 MET B O     1 
ATOM   8110  C  CB    . MET B 1 317 ? 105.042 150.894 138.293 1.00 40.05 ?  317 MET B CB    1 
ATOM   8111  C  CG    . MET B 1 317 ? 105.180 149.968 137.101 1.00 34.68 ?  317 MET B CG    1 
ATOM   8112  S  SD    . MET B 1 317 ? 104.615 150.775 135.591 1.00 48.10 ?  317 MET B SD    1 
ATOM   8113  C  CE    . MET B 1 317 ? 104.928 149.496 134.383 1.00 33.99 ?  317 MET B CE    1 
ATOM   8114  N  N     . ASP B 1 318 ? 104.518 149.992 141.106 1.00 40.30 ?  318 ASP B N     1 
ATOM   8115  C  CA    . ASP B 1 318 ? 103.989 149.185 142.200 1.00 38.45 ?  318 ASP B CA    1 
ATOM   8116  C  C     . ASP B 1 318 ? 103.183 148.025 141.633 1.00 38.44 ?  318 ASP B C     1 
ATOM   8117  O  O     . ASP B 1 318 ? 102.177 148.233 140.946 1.00 41.14 ?  318 ASP B O     1 
ATOM   8118  C  CB    . ASP B 1 318 ? 103.134 150.050 143.122 1.00 37.95 ?  318 ASP B CB    1 
ATOM   8119  C  CG    . ASP B 1 318 ? 102.569 149.275 144.293 1.00 46.03 ?  318 ASP B CG    1 
ATOM   8120  O  OD1   . ASP B 1 318 ? 103.347 148.902 145.197 1.00 42.17 ?  318 ASP B OD1   1 
ATOM   8121  O  OD2   . ASP B 1 318 ? 101.344 149.040 144.311 1.00 44.77 -1 318 ASP B OD2   1 
ATOM   8122  N  N     . MET B 1 319 ? 103.624 146.797 141.917 1.00 39.69 ?  319 MET B N     1 
ATOM   8123  C  CA    . MET B 1 319 ? 102.881 145.623 141.474 1.00 35.15 ?  319 MET B CA    1 
ATOM   8124  C  C     . MET B 1 319 ? 101.574 145.457 142.239 1.00 36.04 ?  319 MET B C     1 
ATOM   8125  O  O     . MET B 1 319 ? 100.609 144.915 141.694 1.00 38.25 ?  319 MET B O     1 
ATOM   8126  C  CB    . MET B 1 319 ? 103.738 144.365 141.617 1.00 36.87 ?  319 MET B CB    1 
ATOM   8127  C  CG    . MET B 1 319 ? 103.192 143.152 140.875 1.00 37.09 ?  319 MET B CG    1 
ATOM   8128  S  SD    . MET B 1 319 ? 103.638 143.054 139.128 1.00 44.18 ?  319 MET B SD    1 
ATOM   8129  C  CE    . MET B 1 319 ? 105.024 144.184 139.045 1.00 38.47 ?  319 MET B CE    1 
ATOM   8130  N  N     . ASN B 1 320 ? 101.518 145.926 143.487 1.00 38.47 ?  320 ASN B N     1 
ATOM   8131  C  CA    . ASN B 1 320 ? 100.305 145.765 144.283 1.00 38.98 ?  320 ASN B CA    1 
ATOM   8132  C  C     . ASN B 1 320 ? 99.123  146.495 143.662 1.00 40.89 ?  320 ASN B C     1 
ATOM   8133  O  O     . ASN B 1 320 ? 97.969  146.112 143.887 1.00 41.47 ?  320 ASN B O     1 
ATOM   8134  C  CB    . ASN B 1 320 ? 100.545 146.260 145.709 1.00 37.46 ?  320 ASN B CB    1 
ATOM   8135  C  CG    . ASN B 1 320 ? 101.582 145.436 146.441 1.00 42.30 ?  320 ASN B CG    1 
ATOM   8136  O  OD1   . ASN B 1 320 ? 102.717 145.297 145.985 1.00 37.80 ?  320 ASN B OD1   1 
ATOM   8137  N  ND2   . ASN B 1 320 ? 101.197 144.884 147.583 1.00 41.25 ?  320 ASN B ND2   1 
ATOM   8138  N  N     . GLU B 1 321 ? 99.383  147.542 142.881 1.00 42.19 ?  321 GLU B N     1 
ATOM   8139  C  CA    . GLU B 1 321 ? 98.330  148.301 142.226 1.00 40.34 ?  321 GLU B CA    1 
ATOM   8140  C  C     . GLU B 1 321 ? 98.267  148.080 140.722 1.00 40.01 ?  321 GLU B C     1 
ATOM   8141  O  O     . GLU B 1 321 ? 97.264  148.455 140.103 1.00 46.31 ?  321 GLU B O     1 
ATOM   8142  C  CB    . GLU B 1 321 ? 98.506  149.802 142.507 1.00 42.72 ?  321 GLU B CB    1 
ATOM   8143  C  CG    . GLU B 1 321 ? 99.344  150.533 141.471 1.00 39.85 ?  321 GLU B CG    1 
ATOM   8144  C  CD    . GLU B 1 321 ? 100.072 151.730 142.048 1.00 45.15 ?  321 GLU B CD    1 
ATOM   8145  O  OE1   . GLU B 1 321 ? 100.015 151.924 143.280 1.00 45.47 ?  321 GLU B OE1   1 
ATOM   8146  O  OE2   . GLU B 1 321 ? 100.708 152.472 141.271 1.00 45.61 -1 321 GLU B OE2   1 
ATOM   8147  N  N     . MET B 1 322 ? 99.292  147.483 140.116 1.00 34.71 ?  322 MET B N     1 
ATOM   8148  C  CA    . MET B 1 322 ? 99.345  147.327 138.671 1.00 32.82 ?  322 MET B CA    1 
ATOM   8149  C  C     . MET B 1 322 ? 99.289  145.873 138.223 1.00 33.10 ?  322 MET B C     1 
ATOM   8150  O  O     . MET B 1 322 ? 99.293  145.615 137.016 1.00 39.54 ?  322 MET B O     1 
ATOM   8151  C  CB    . MET B 1 322 ? 100.614 147.984 138.116 1.00 33.39 ?  322 MET B CB    1 
ATOM   8152  C  CG    . MET B 1 322 ? 100.564 149.508 138.066 1.00 35.60 ?  322 MET B CG    1 
ATOM   8153  S  SD    . MET B 1 322 ? 99.753  150.234 136.627 1.00 45.22 ?  322 MET B SD    1 
ATOM   8154  C  CE    . MET B 1 322 ? 99.923  148.932 135.417 1.00 36.56 ?  322 MET B CE    1 
ATOM   8155  N  N     . TYR B 1 323 ? 99.248  144.917 139.156 1.00 32.48 ?  323 TYR B N     1 
ATOM   8156  C  CA    . TYR B 1 323 ? 99.221  143.506 138.779 1.00 28.69 ?  323 TYR B CA    1 
ATOM   8157  C  C     . TYR B 1 323 ? 97.941  143.153 138.033 1.00 29.49 ?  323 TYR B C     1 
ATOM   8158  O  O     . TYR B 1 323 ? 97.980  142.436 137.025 1.00 33.38 ?  323 TYR B O     1 
ATOM   8159  C  CB    . TYR B 1 323 ? 99.376  142.631 140.025 1.00 32.87 ?  323 TYR B CB    1 
ATOM   8160  C  CG    . TYR B 1 323 ? 99.244  141.149 139.758 1.00 30.91 ?  323 TYR B CG    1 
ATOM   8161  C  CD1   . TYR B 1 323 ? 100.336 140.398 139.350 1.00 27.40 ?  323 TYR B CD1   1 
ATOM   8162  C  CD2   . TYR B 1 323 ? 98.027  140.499 139.919 1.00 30.40 ?  323 TYR B CD2   1 
ATOM   8163  C  CE1   . TYR B 1 323 ? 100.219 139.046 139.104 1.00 29.80 ?  323 TYR B CE1   1 
ATOM   8164  C  CE2   . TYR B 1 323 ? 97.901  139.149 139.675 1.00 25.97 ?  323 TYR B CE2   1 
ATOM   8165  C  CZ    . TYR B 1 323 ? 99.000  138.427 139.269 1.00 31.28 ?  323 TYR B CZ    1 
ATOM   8166  O  OH    . TYR B 1 323 ? 98.880  137.081 139.024 1.00 30.96 ?  323 TYR B OH    1 
ATOM   8167  N  N     . ASP B 1 324 ? 96.798  143.639 138.517 1.00 36.10 ?  324 ASP B N     1 
ATOM   8168  C  CA    . ASP B 1 324 ? 95.536  143.362 137.842 1.00 34.38 ?  324 ASP B CA    1 
ATOM   8169  C  C     . ASP B 1 324 ? 95.498  144.006 136.462 1.00 38.34 ?  324 ASP B C     1 
ATOM   8170  O  O     . ASP B 1 324 ? 94.962  143.423 135.513 1.00 41.12 ?  324 ASP B O     1 
ATOM   8171  C  CB    . ASP B 1 324 ? 94.368  143.844 138.700 1.00 38.72 ?  324 ASP B CB    1 
ATOM   8172  C  CG    . ASP B 1 324 ? 94.022  142.866 139.806 1.00 40.69 ?  324 ASP B CG    1 
ATOM   8173  O  OD1   . ASP B 1 324 ? 94.316  141.663 139.649 1.00 40.70 ?  324 ASP B OD1   1 
ATOM   8174  O  OD2   . ASP B 1 324 ? 93.458  143.301 140.833 1.00 42.71 -1 324 ASP B OD2   1 
ATOM   8175  N  N     . LYS B 1 325 ? 96.057  145.212 136.332 1.00 33.53 ?  325 LYS B N     1 
ATOM   8176  C  CA    . LYS B 1 325 ? 96.129  145.856 135.025 1.00 31.34 ?  325 LYS B CA    1 
ATOM   8177  C  C     . LYS B 1 325 ? 97.034  145.080 134.075 1.00 32.90 ?  325 LYS B C     1 
ATOM   8178  O  O     . LYS B 1 325 ? 96.726  144.952 132.885 1.00 40.84 ?  325 LYS B O     1 
ATOM   8179  C  CB    . LYS B 1 325 ? 96.610  147.296 135.179 1.00 36.26 ?  325 LYS B CB    1 
ATOM   8180  C  CG    . LYS B 1 325 ? 95.649  148.175 135.958 1.00 34.78 ?  325 LYS B CG    1 
ATOM   8181  C  CD    . LYS B 1 325 ? 96.305  149.474 136.381 1.00 34.18 ?  325 LYS B CD    1 
ATOM   8182  C  CE    . LYS B 1 325 ? 95.269  150.552 136.642 1.00 36.84 ?  325 LYS B CE    1 
ATOM   8183  N  NZ    . LYS B 1 325 ? 93.913  149.977 136.853 1.00 36.00 1  325 LYS B NZ    1 
ATOM   8184  N  N     . PHE B 1 326 ? 98.154  144.558 134.581 1.00 35.11 ?  326 PHE B N     1 
ATOM   8185  C  CA    . PHE B 1 326 ? 99.009  143.695 133.769 1.00 33.24 ?  326 PHE B CA    1 
ATOM   8186  C  C     . PHE B 1 326 ? 98.261  142.451 133.308 1.00 29.94 ?  326 PHE B C     1 
ATOM   8187  O  O     . PHE B 1 326 ? 98.373  142.042 132.147 1.00 36.57 ?  326 PHE B O     1 
ATOM   8188  C  CB    . PHE B 1 326 ? 100.255 143.289 134.558 1.00 30.23 ?  326 PHE B CB    1 
ATOM   8189  C  CG    . PHE B 1 326 ? 101.220 144.408 134.809 1.00 30.01 ?  326 PHE B CG    1 
ATOM   8190  C  CD1   . PHE B 1 326 ? 101.194 145.557 134.041 1.00 33.25 ?  326 PHE B CD1   1 
ATOM   8191  C  CD2   . PHE B 1 326 ? 102.158 144.307 135.823 1.00 33.29 ?  326 PHE B CD2   1 
ATOM   8192  C  CE1   . PHE B 1 326 ? 102.092 146.579 134.275 1.00 30.86 ?  326 PHE B CE1   1 
ATOM   8193  C  CE2   . PHE B 1 326 ? 103.052 145.328 136.063 1.00 33.97 ?  326 PHE B CE2   1 
ATOM   8194  C  CZ    . PHE B 1 326 ? 103.018 146.467 135.290 1.00 35.34 ?  326 PHE B CZ    1 
ATOM   8195  N  N     . VAL B 1 327 ? 97.501  141.829 134.211 1.00 31.40 ?  327 VAL B N     1 
ATOM   8196  C  CA    . VAL B 1 327 ? 96.822  140.580 133.877 1.00 34.99 ?  327 VAL B CA    1 
ATOM   8197  C  C     . VAL B 1 327 ? 95.706  140.824 132.867 1.00 36.86 ?  327 VAL B C     1 
ATOM   8198  O  O     . VAL B 1 327 ? 95.540  140.059 131.909 1.00 41.34 ?  327 VAL B O     1 
ATOM   8199  C  CB    . VAL B 1 327 ? 96.297  139.902 135.156 1.00 32.98 ?  327 VAL B CB    1 
ATOM   8200  C  CG1   . VAL B 1 327 ? 95.333  138.779 134.811 1.00 35.22 ?  327 VAL B CG1   1 
ATOM   8201  C  CG2   . VAL B 1 327 ? 97.456  139.375 135.986 1.00 29.82 ?  327 VAL B CG2   1 
ATOM   8202  N  N     . ASP B 1 328 ? 94.933  141.893 133.052 1.00 36.62 ?  328 ASP B N     1 
ATOM   8203  C  CA    . ASP B 1 328 ? 93.808  142.183 132.173 1.00 36.77 ?  328 ASP B CA    1 
ATOM   8204  C  C     . ASP B 1 328 ? 94.222  142.836 130.861 1.00 40.53 ?  328 ASP B C     1 
ATOM   8205  O  O     . ASP B 1 328 ? 93.371  143.014 129.984 1.00 43.97 ?  328 ASP B O     1 
ATOM   8206  C  CB    . ASP B 1 328 ? 92.800  143.082 132.895 1.00 38.73 ?  328 ASP B CB    1 
ATOM   8207  C  CG    . ASP B 1 328 ? 92.266  142.452 134.165 1.00 45.21 ?  328 ASP B CG    1 
ATOM   8208  O  OD1   . ASP B 1 328 ? 91.670  143.181 134.986 1.00 46.00 ?  328 ASP B OD1   1 
ATOM   8209  O  OD2   . ASP B 1 328 ? 92.443  141.228 134.344 1.00 44.15 -1 328 ASP B OD2   1 
ATOM   8210  N  N     . ASN B 1 329 ? 95.493  143.194 130.706 1.00 36.19 ?  329 ASN B N     1 
ATOM   8211  C  CA    . ASN B 1 329 ? 95.959  143.858 129.496 1.00 35.52 ?  329 ASN B CA    1 
ATOM   8212  C  C     . ASN B 1 329 ? 96.351  142.806 128.466 1.00 39.38 ?  329 ASN B C     1 
ATOM   8213  O  O     . ASN B 1 329 ? 97.296  142.043 128.709 1.00 39.32 ?  329 ASN B O     1 
ATOM   8214  C  CB    . ASN B 1 329 ? 97.145  144.756 129.809 1.00 35.64 ?  329 ASN B CB    1 
ATOM   8215  C  CG    . ASN B 1 329 ? 97.410  145.792 128.732 1.00 39.66 ?  329 ASN B CG    1 
ATOM   8216  O  OD1   . ASN B 1 329 ? 98.048  146.809 128.992 1.00 37.91 ?  329 ASN B OD1   1 
ATOM   8217  N  ND2   . ASN B 1 329 ? 96.925  145.545 127.524 1.00 42.21 ?  329 ASN B ND2   1 
ATOM   8218  N  N     . PRO B 1 330 ? 95.665  142.723 127.321 1.00 43.55 ?  330 PRO B N     1 
ATOM   8219  C  CA    . PRO B 1 330 ? 96.065  141.733 126.309 1.00 40.99 ?  330 PRO B CA    1 
ATOM   8220  C  C     . PRO B 1 330 ? 97.406  142.035 125.665 1.00 37.31 ?  330 PRO B C     1 
ATOM   8221  O  O     . PRO B 1 330 ? 98.061  141.109 125.170 1.00 39.57 ?  330 PRO B O     1 
ATOM   8222  C  CB    . PRO B 1 330 ? 94.919  141.794 125.290 1.00 41.98 ?  330 PRO B CB    1 
ATOM   8223  C  CG    . PRO B 1 330 ? 94.354  143.164 125.447 1.00 37.44 ?  330 PRO B CG    1 
ATOM   8224  C  CD    . PRO B 1 330 ? 94.482  143.496 126.906 1.00 40.19 ?  330 PRO B CD    1 
ATOM   8225  N  N     . ARG B 1 331 ? 97.838  143.296 125.653 1.00 38.79 ?  331 ARG B N     1 
ATOM   8226  C  CA    . ARG B 1 331 ? 99.122  143.654 125.064 1.00 42.17 ?  331 ARG B CA    1 
ATOM   8227  C  C     . ARG B 1 331 ? 100.299 143.332 125.973 1.00 40.20 ?  331 ARG B C     1 
ATOM   8228  O  O     . ARG B 1 331 ? 101.449 143.490 125.551 1.00 38.14 ?  331 ARG B O     1 
ATOM   8229  C  CB    . ARG B 1 331 ? 99.137  145.140 124.699 1.00 39.65 ?  331 ARG B CB    1 
ATOM   8230  C  CG    . ARG B 1 331 ? 98.246  145.488 123.517 1.00 38.38 ?  331 ARG B CG    1 
ATOM   8231  C  CD    . ARG B 1 331 ? 97.925  146.974 123.468 1.00 40.13 ?  331 ARG B CD    1 
ATOM   8232  N  NE    . ARG B 1 331 ? 97.183  147.426 124.640 1.00 42.43 ?  331 ARG B NE    1 
ATOM   8233  C  CZ    . ARG B 1 331 ? 95.917  147.121 124.895 1.00 42.33 ?  331 ARG B CZ    1 
ATOM   8234  N  NH1   . ARG B 1 331 ? 95.211  146.355 124.078 1.00 41.73 1  331 ARG B NH1   1 
ATOM   8235  N  NH2   . ARG B 1 331 ? 95.344  147.601 125.994 1.00 40.55 ?  331 ARG B NH2   1 
ATOM   8236  N  N     . VAL B 1 332 ? 100.041 142.894 127.202 1.00 38.10 ?  332 VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? 101.079 142.443 128.119 1.00 33.72 ?  332 VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? 101.127 140.923 128.066 1.00 34.64 ?  332 VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? 100.092 140.258 128.189 1.00 37.29 ?  332 VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? 100.811 142.939 129.551 1.00 33.18 ?  332 VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? 101.667 142.177 130.550 1.00 33.55 ?  332 VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? 101.067 144.434 129.648 1.00 33.28 ?  332 VAL B CG2   1 
ATOM   8243  N  N     . LYS B 1 333 ? 102.320 140.373 127.862 1.00 31.25 ?  333 LYS B N     1 
ATOM   8244  C  CA    . LYS B 1 333 ? 102.503 138.931 127.810 1.00 31.37 ?  333 LYS B CA    1 
ATOM   8245  C  C     . LYS B 1 333 ? 102.824 138.398 129.200 1.00 33.26 ?  333 LYS B C     1 
ATOM   8246  O  O     . LYS B 1 333 ? 103.618 138.991 129.937 1.00 34.81 ?  333 LYS B O     1 
ATOM   8247  C  CB    . LYS B 1 333 ? 103.619 138.564 126.832 1.00 26.23 ?  333 LYS B CB    1 
ATOM   8248  C  CG    . LYS B 1 333 ? 103.569 137.129 126.338 1.00 32.17 ?  333 LYS B CG    1 
ATOM   8249  C  CD    . LYS B 1 333 ? 104.762 136.811 125.452 1.00 34.40 ?  333 LYS B CD    1 
ATOM   8250  C  CE    . LYS B 1 333 ? 104.811 135.334 125.100 1.00 35.85 ?  333 LYS B CE    1 
ATOM   8251  N  NZ    . LYS B 1 333 ? 105.976 135.010 124.233 1.00 37.67 1  333 LYS B NZ    1 
ATOM   8252  N  N     . LYS B 1 334 ? 102.202 137.276 129.555 1.00 32.05 ?  334 LYS B N     1 
ATOM   8253  C  CA    . LYS B 1 334 ? 102.376 136.710 130.884 1.00 29.36 ?  334 LYS B CA    1 
ATOM   8254  C  C     . LYS B 1 334 ? 102.238 135.197 130.821 1.00 33.55 ?  334 LYS B C     1 
ATOM   8255  O  O     . LYS B 1 334 ? 101.678 134.639 129.875 1.00 35.10 ?  334 LYS B O     1 
ATOM   8256  C  CB    . LYS B 1 334 ? 101.364 137.289 131.880 1.00 31.14 ?  334 LYS B CB    1 
ATOM   8257  C  CG    . LYS B 1 334 ? 99.934  136.846 131.639 1.00 35.88 ?  334 LYS B CG    1 
ATOM   8258  C  CD    . LYS B 1 334 ? 98.953  137.974 131.891 1.00 32.50 ?  334 LYS B CD    1 
ATOM   8259  C  CE    . LYS B 1 334 ? 98.865  138.895 130.692 1.00 33.97 ?  334 LYS B CE    1 
ATOM   8260  N  NZ    . LYS B 1 334 ? 97.543  139.568 130.597 1.00 34.33 1  334 LYS B NZ    1 
ATOM   8261  N  N     . GLU B 1 335 ? 102.764 134.542 131.853 1.00 33.86 ?  335 GLU B N     1 
ATOM   8262  C  CA    . GLU B 1 335 ? 102.696 133.097 132.009 1.00 33.23 ?  335 GLU B CA    1 
ATOM   8263  C  C     . GLU B 1 335 ? 102.083 132.762 133.360 1.00 34.05 ?  335 GLU B C     1 
ATOM   8264  O  O     . GLU B 1 335 ? 102.352 133.436 134.358 1.00 40.53 ?  335 GLU B O     1 
ATOM   8265  C  CB    . GLU B 1 335 ? 104.083 132.453 131.896 1.00 29.97 ?  335 GLU B CB    1 
ATOM   8266  C  CG    . GLU B 1 335 ? 104.949 133.023 130.791 1.00 37.48 ?  335 GLU B CG    1 
ATOM   8267  C  CD    . GLU B 1 335 ? 105.731 131.956 130.053 1.00 41.55 ?  335 GLU B CD    1 
ATOM   8268  O  OE1   . GLU B 1 335 ? 106.631 131.345 130.668 1.00 36.02 ?  335 GLU B OE1   1 
ATOM   8269  O  OE2   . GLU B 1 335 ? 105.446 131.729 128.859 1.00 36.24 -1 335 GLU B OE2   1 
ATOM   8270  N  N     . LYS B 1 336 ? 101.264 131.715 133.386 1.00 33.34 ?  336 LYS B N     1 
ATOM   8271  C  CA    . LYS B 1 336 ? 100.628 131.281 134.620 1.00 29.33 ?  336 LYS B CA    1 
ATOM   8272  C  C     . LYS B 1 336 ? 101.607 130.490 135.476 1.00 35.73 ?  336 LYS B C     1 
ATOM   8273  O  O     . LYS B 1 336 ? 102.341 129.632 134.979 1.00 37.25 ?  336 LYS B O     1 
ATOM   8274  C  CB    . LYS B 1 336 ? 99.398  130.426 134.314 1.00 37.44 ?  336 LYS B CB    1 
ATOM   8275  C  CG    . LYS B 1 336 ? 98.313  130.495 135.375 1.00 41.25 ?  336 LYS B CG    1 
ATOM   8276  C  CD    . LYS B 1 336 ? 97.132  129.612 135.012 1.00 38.03 ?  336 LYS B CD    1 
ATOM   8277  C  CE    . LYS B 1 336 ? 95.829  130.392 135.035 1.00 39.22 ?  336 LYS B CE    1 
ATOM   8278  N  NZ    . LYS B 1 336 ? 95.751  131.306 136.207 1.00 39.13 1  336 LYS B NZ    1 
ATOM   8279  N  N     . ILE B 1 337 ? 101.618 130.789 136.777 1.00 36.47 ?  337 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 337 ? 102.436 130.079 137.749 1.00 34.68 ?  337 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 337 ? 101.598 129.829 138.993 1.00 35.24 ?  337 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 337 ? 100.562 130.460 139.212 1.00 39.38 ?  337 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 337 ? 103.721 130.851 138.130 1.00 33.50 ?  337 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 337 ? 103.367 132.243 138.660 1.00 33.10 ?  337 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 337 ? 104.670 130.944 136.946 1.00 35.27 ?  337 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 337 ? 104.247 132.703 139.798 1.00 31.75 ?  337 ILE B CD1   1 
ATOM   8287  N  N     . ASN B 1 338 ? 102.059 128.888 139.813 1.00 35.06 ?  338 ASN B N     1 
ATOM   8288  C  CA    . ASN B 1 338 ? 101.459 128.663 141.117 1.00 34.44 ?  338 ASN B CA    1 
ATOM   8289  C  C     . ASN B 1 338 ? 102.317 129.357 142.160 1.00 34.15 ?  338 ASN B C     1 
ATOM   8290  O  O     . ASN B 1 338 ? 103.448 128.914 142.409 1.00 37.77 ?  338 ASN B O     1 
ATOM   8291  C  CB    . ASN B 1 338 ? 101.351 127.170 141.417 1.00 32.16 ?  338 ASN B CB    1 
ATOM   8292  C  CG    . ASN B 1 338 ? 100.370 126.867 142.534 1.00 35.79 ?  338 ASN B CG    1 
ATOM   8293  O  OD1   . ASN B 1 338 ? 100.238 125.723 142.965 1.00 38.49 ?  338 ASN B OD1   1 
ATOM   8294  N  ND2   . ASN B 1 338 ? 99.673  127.894 143.005 1.00 37.38 ?  338 ASN B ND2   1 
ATOM   8295  N  N     . PRO B 1 339 ? 101.847 130.444 142.779 1.00 33.80 ?  339 PRO B N     1 
ATOM   8296  C  CA    . PRO B 1 339 ? 102.689 131.146 143.762 1.00 28.56 ?  339 PRO B CA    1 
ATOM   8297  C  C     . PRO B 1 339 ? 103.090 130.283 144.944 1.00 32.53 ?  339 PRO B C     1 
ATOM   8298  O  O     . PRO B 1 339 ? 104.201 130.445 145.464 1.00 35.56 ?  339 PRO B O     1 
ATOM   8299  C  CB    . PRO B 1 339 ? 101.812 132.330 144.194 1.00 29.85 ?  339 PRO B CB    1 
ATOM   8300  C  CG    . PRO B 1 339 ? 100.421 131.935 143.831 1.00 33.77 ?  339 PRO B CG    1 
ATOM   8301  C  CD    . PRO B 1 339 ? 100.540 131.094 142.603 1.00 33.82 ?  339 PRO B CD    1 
ATOM   8302  N  N     . ARG B 1 340 ? 102.225 129.367 145.387 1.00 31.45 ?  340 ARG B N     1 
ATOM   8303  C  CA    . ARG B 1 340 ? 102.606 128.464 146.467 1.00 28.07 ?  340 ARG B CA    1 
ATOM   8304  C  C     . ARG B 1 340 ? 103.683 127.487 146.014 1.00 31.70 ?  340 ARG B C     1 
ATOM   8305  O  O     . ARG B 1 340 ? 104.606 127.176 146.774 1.00 34.63 ?  340 ARG B O     1 
ATOM   8306  C  CB    . ARG B 1 340 ? 101.380 127.719 146.989 1.00 31.53 ?  340 ARG B CB    1 
ATOM   8307  C  CG    . ARG B 1 340 ? 100.483 128.576 147.859 1.00 29.55 ?  340 ARG B CG    1 
ATOM   8308  C  CD    . ARG B 1 340 ? 99.637  127.745 148.803 1.00 28.13 ?  340 ARG B CD    1 
ATOM   8309  N  NE    . ARG B 1 340 ? 98.694  128.580 149.538 1.00 31.78 ?  340 ARG B NE    1 
ATOM   8310  C  CZ    . ARG B 1 340 ? 97.812  128.125 150.416 1.00 34.23 ?  340 ARG B CZ    1 
ATOM   8311  N  NH1   . ARG B 1 340 ? 97.724  126.837 150.702 1.00 34.73 1  340 ARG B NH1   1 
ATOM   8312  N  NH2   . ARG B 1 340 ? 96.998  128.984 151.021 1.00 34.57 ?  340 ARG B NH2   1 
ATOM   8313  N  N     . LYS B 1 341 ? 103.586 126.997 144.776 1.00 30.60 ?  341 LYS B N     1 
ATOM   8314  C  CA    . LYS B 1 341 ? 104.645 126.147 144.243 1.00 27.34 ?  341 LYS B CA    1 
ATOM   8315  C  C     . LYS B 1 341 ? 105.952 126.914 144.102 1.00 30.08 ?  341 LYS B C     1 
ATOM   8316  O  O     . LYS B 1 341 ? 107.025 126.356 144.344 1.00 29.73 ?  341 LYS B O     1 
ATOM   8317  C  CB    . LYS B 1 341 ? 104.230 125.555 142.895 1.00 35.91 ?  341 LYS B CB    1 
ATOM   8318  C  CG    . LYS B 1 341 ? 103.208 124.425 142.972 1.00 37.10 ?  341 LYS B CG    1 
ATOM   8319  C  CD    . LYS B 1 341 ? 103.140 123.794 144.354 1.00 34.20 ?  341 LYS B CD    1 
ATOM   8320  C  CE    . LYS B 1 341 ? 102.669 122.350 144.279 1.00 36.14 ?  341 LYS B CE    1 
ATOM   8321  N  NZ    . LYS B 1 341 ? 101.337 122.231 143.623 1.00 33.97 1  341 LYS B NZ    1 
ATOM   8322  N  N     . LEU B 1 342 ? 105.883 128.190 143.718 1.00 29.26 ?  342 LEU B N     1 
ATOM   8323  C  CA    . LEU B 1 342 ? 107.093 129.003 143.643 1.00 26.52 ?  342 LEU B CA    1 
ATOM   8324  C  C     . LEU B 1 342 ? 107.697 129.222 145.025 1.00 30.91 ?  342 LEU B C     1 
ATOM   8325  O  O     . LEU B 1 342 ? 108.922 129.194 145.184 1.00 37.75 ?  342 LEU B O     1 
ATOM   8326  C  CB    . LEU B 1 342 ? 106.787 130.337 142.966 1.00 30.07 ?  342 LEU B CB    1 
ATOM   8327  C  CG    . LEU B 1 342 ? 107.991 131.137 142.466 1.00 27.23 ?  342 LEU B CG    1 
ATOM   8328  C  CD1   . LEU B 1 342 ? 109.002 130.224 141.793 1.00 25.62 ?  342 LEU B CD1   1 
ATOM   8329  C  CD2   . LEU B 1 342 ? 107.543 132.234 141.516 1.00 26.81 ?  342 LEU B CD2   1 
ATOM   8330  N  N     . LEU B 1 343 ? 106.855 129.441 146.038 1.00 29.53 ?  343 LEU B N     1 
ATOM   8331  C  CA    . LEU B 1 343 ? 107.352 129.564 147.405 1.00 26.59 ?  343 LEU B CA    1 
ATOM   8332  C  C     . LEU B 1 343 ? 108.013 128.273 147.872 1.00 28.70 ?  343 LEU B C     1 
ATOM   8333  O  O     . LEU B 1 343 ? 109.065 128.302 148.522 1.00 33.74 ?  343 LEU B O     1 
ATOM   8334  C  CB    . LEU B 1 343 ? 106.210 129.944 148.345 1.00 30.61 ?  343 LEU B CB    1 
ATOM   8335  C  CG    . LEU B 1 343 ? 106.041 131.429 148.657 1.00 30.70 ?  343 LEU B CG    1 
ATOM   8336  C  CD1   . LEU B 1 343 ? 104.973 131.624 149.720 1.00 27.27 ?  343 LEU B CD1   1 
ATOM   8337  C  CD2   . LEU B 1 343 ? 107.362 132.036 149.097 1.00 30.33 ?  343 LEU B CD2   1 
ATOM   8338  N  N     . GLU B 1 344 ? 107.402 127.129 147.559 1.00 30.95 ?  344 GLU B N     1 
ATOM   8339  C  CA    . GLU B 1 344 ? 107.999 125.849 147.925 1.00 28.52 ?  344 GLU B CA    1 
ATOM   8340  C  C     . GLU B 1 344 ? 109.316 125.627 147.193 1.00 29.40 ?  344 GLU B C     1 
ATOM   8341  O  O     . GLU B 1 344 ? 110.256 125.060 147.758 1.00 34.84 ?  344 GLU B O     1 
ATOM   8342  C  CB    . GLU B 1 344 ? 107.020 124.711 147.639 1.00 30.80 ?  344 GLU B CB    1 
ATOM   8343  C  CG    . GLU B 1 344 ? 105.792 124.718 148.534 1.00 33.67 ?  344 GLU B CG    1 
ATOM   8344  C  CD    . GLU B 1 344 ? 104.667 123.867 147.984 1.00 38.15 ?  344 GLU B CD    1 
ATOM   8345  O  OE1   . GLU B 1 344 ? 104.902 123.141 146.996 1.00 39.86 ?  344 GLU B OE1   1 
ATOM   8346  O  OE2   . GLU B 1 344 ? 103.548 123.928 148.535 1.00 37.98 -1 344 GLU B OE2   1 
ATOM   8347  N  N     . LYS B 1 345 ? 109.400 126.064 145.935 1.00 29.24 ?  345 LYS B N     1 
ATOM   8348  C  CA    . LYS B 1 345 ? 110.661 125.988 145.205 1.00 27.16 ?  345 LYS B CA    1 
ATOM   8349  C  C     . LYS B 1 345 ? 111.723 126.865 145.854 1.00 30.72 ?  345 LYS B C     1 
ATOM   8350  O  O     . LYS B 1 345 ? 112.891 126.471 145.947 1.00 32.03 ?  345 LYS B O     1 
ATOM   8351  C  CB    . LYS B 1 345 ? 110.450 126.390 143.746 1.00 26.14 ?  345 LYS B CB    1 
ATOM   8352  C  CG    . LYS B 1 345 ? 111.703 126.299 142.895 1.00 29.85 ?  345 LYS B CG    1 
ATOM   8353  C  CD    . LYS B 1 345 ? 111.417 126.629 141.442 1.00 30.37 ?  345 LYS B CD    1 
ATOM   8354  C  CE    . LYS B 1 345 ? 112.670 126.490 140.595 1.00 30.62 ?  345 LYS B CE    1 
ATOM   8355  N  NZ    . LYS B 1 345 ? 112.423 126.838 139.170 1.00 31.25 1  345 LYS B NZ    1 
ATOM   8356  N  N     . LEU B 1 346 ? 111.338 128.062 146.303 1.00 29.75 ?  346 LEU B N     1 
ATOM   8357  C  CA    . LEU B 1 346 ? 112.271 128.926 147.019 1.00 23.48 ?  346 LEU B CA    1 
ATOM   8358  C  C     . LEU B 1 346 ? 112.777 128.248 148.285 1.00 27.62 ?  346 LEU B C     1 
ATOM   8359  O  O     . LEU B 1 346 ? 113.978 128.266 148.579 1.00 30.54 ?  346 LEU B O     1 
ATOM   8360  C  CB    . LEU B 1 346 ? 111.602 130.256 147.369 1.00 24.10 ?  346 LEU B CB    1 
ATOM   8361  C  CG    . LEU B 1 346 ? 111.163 131.201 146.251 1.00 26.77 ?  346 LEU B CG    1 
ATOM   8362  C  CD1   . LEU B 1 346 ? 110.411 132.384 146.834 1.00 28.15 ?  346 LEU B CD1   1 
ATOM   8363  C  CD2   . LEU B 1 346 ? 112.354 131.676 145.453 1.00 26.32 ?  346 LEU B CD2   1 
ATOM   8364  N  N     . ALA B 1 347 ? 111.866 127.640 149.048 1.00 26.89 ?  347 ALA B N     1 
ATOM   8365  C  CA    . ALA B 1 347 ? 112.260 126.968 150.284 1.00 20.29 ?  347 ALA B CA    1 
ATOM   8366  C  C     . ALA B 1 347 ? 113.175 125.782 150.005 1.00 29.91 ?  347 ALA B C     1 
ATOM   8367  O  O     . ALA B 1 347 ? 114.165 125.577 150.716 1.00 35.16 ?  347 ALA B O     1 
ATOM   8368  C  CB    . ALA B 1 347 ? 111.020 126.521 151.055 1.00 22.69 ?  347 ALA B CB    1 
ATOM   8369  N  N     . MET B 1 348 ? 112.861 124.993 148.976 1.00 31.69 ?  348 MET B N     1 
ATOM   8370  C  CA    . MET B 1 348 ? 113.709 123.860 148.619 1.00 29.01 ?  348 MET B CA    1 
ATOM   8371  C  C     . MET B 1 348 ? 115.091 124.323 148.178 1.00 31.20 ?  348 MET B C     1 
ATOM   8372  O  O     . MET B 1 348 ? 116.105 123.734 148.570 1.00 35.64 ?  348 MET B O     1 
ATOM   8373  C  CB    . MET B 1 348 ? 113.040 123.037 147.518 1.00 31.96 ?  348 MET B CB    1 
ATOM   8374  C  CG    . MET B 1 348 ? 113.969 122.067 146.805 1.00 38.36 ?  348 MET B CG    1 
ATOM   8375  S  SD    . MET B 1 348 ? 114.299 122.554 145.100 1.00 53.07 ?  348 MET B SD    1 
ATOM   8376  C  CE    . MET B 1 348 ? 112.645 122.530 144.415 1.00 37.32 ?  348 MET B CE    1 
ATOM   8377  N  N     . LEU B 1 349 ? 115.152 125.381 147.368 1.00 28.67 ?  349 LEU B N     1 
ATOM   8378  C  CA    . LEU B 1 349 ? 116.439 125.905 146.923 1.00 25.58 ?  349 LEU B CA    1 
ATOM   8379  C  C     . LEU B 1 349 ? 117.258 126.422 148.096 1.00 25.72 ?  349 LEU B C     1 
ATOM   8380  O  O     . LEU B 1 349 ? 118.475 126.214 148.150 1.00 30.40 ?  349 LEU B O     1 
ATOM   8381  C  CB    . LEU B 1 349 ? 116.223 127.014 145.895 1.00 30.48 ?  349 LEU B CB    1 
ATOM   8382  C  CG    . LEU B 1 349 ? 116.630 126.725 144.452 1.00 31.43 ?  349 LEU B CG    1 
ATOM   8383  C  CD1   . LEU B 1 349 ? 115.546 125.942 143.731 1.00 31.89 ?  349 LEU B CD1   1 
ATOM   8384  C  CD2   . LEU B 1 349 ? 116.929 128.027 143.735 1.00 28.13 ?  349 LEU B CD2   1 
ATOM   8385  N  N     . ARG B 1 350 ? 116.613 127.112 149.039 1.00 25.07 ?  350 ARG B N     1 
ATOM   8386  C  CA    . ARG B 1 350 ? 117.334 127.610 150.204 1.00 25.84 ?  350 ARG B CA    1 
ATOM   8387  C  C     . ARG B 1 350 ? 117.800 126.475 151.104 1.00 28.68 ?  350 ARG B C     1 
ATOM   8388  O  O     . ARG B 1 350 ? 118.871 126.570 151.714 1.00 33.54 ?  350 ARG B O     1 
ATOM   8389  C  CB    . ARG B 1 350 ? 116.460 128.594 150.981 1.00 22.89 ?  350 ARG B CB    1 
ATOM   8390  C  CG    . ARG B 1 350 ? 116.180 129.887 150.235 1.00 23.30 ?  350 ARG B CG    1 
ATOM   8391  C  CD    . ARG B 1 350 ? 115.124 130.720 150.938 1.00 23.06 ?  350 ARG B CD    1 
ATOM   8392  N  NE    . ARG B 1 350 ? 115.497 131.015 152.315 1.00 34.99 ?  350 ARG B NE    1 
ATOM   8393  C  CZ    . ARG B 1 350 ? 116.393 131.925 152.673 1.00 31.12 ?  350 ARG B CZ    1 
ATOM   8394  N  NH1   . ARG B 1 350 ? 117.026 132.663 151.776 1.00 26.96 1  350 ARG B NH1   1 
ATOM   8395  N  NH2   . ARG B 1 350 ? 116.661 132.098 153.963 1.00 27.93 ?  350 ARG B NH2   1 
ATOM   8396  N  N     . SER B 1 351 ? 117.015 125.403 151.212 1.00 28.79 ?  351 SER B N     1 
ATOM   8397  C  CA    . SER B 1 351 ? 117.466 124.236 151.961 1.00 29.95 ?  351 SER B CA    1 
ATOM   8398  C  C     . SER B 1 351 ? 118.671 123.584 151.295 1.00 33.63 ?  351 SER B C     1 
ATOM   8399  O  O     . SER B 1 351 ? 119.623 123.184 151.975 1.00 40.76 ?  351 SER B O     1 
ATOM   8400  C  CB    . SER B 1 351 ? 116.325 123.231 152.107 1.00 31.21 ?  351 SER B CB    1 
ATOM   8401  O  OG    . SER B 1 351 ? 115.189 123.832 152.704 1.00 36.59 ?  351 SER B OG    1 
ATOM   8402  N  N     . GLU B 1 352 ? 118.650 123.471 149.966 1.00 31.55 ?  352 GLU B N     1 
ATOM   8403  C  CA    . GLU B 1 352 ? 119.730 122.782 149.266 1.00 30.05 ?  352 GLU B CA    1 
ATOM   8404  C  C     . GLU B 1 352 ? 121.015 123.605 149.247 1.00 35.96 ?  352 GLU B C     1 
ATOM   8405  O  O     . GLU B 1 352 ? 122.099 123.071 149.506 1.00 39.68 ?  352 GLU B O     1 
ATOM   8406  C  CB    . GLU B 1 352 ? 119.299 122.432 147.842 1.00 34.33 ?  352 GLU B CB    1 
ATOM   8407  C  CG    . GLU B 1 352 ? 118.114 121.486 147.763 1.00 36.76 ?  352 GLU B CG    1 
ATOM   8408  C  CD    . GLU B 1 352 ? 117.619 121.290 146.345 1.00 41.55 ?  352 GLU B CD    1 
ATOM   8409  O  OE1   . GLU B 1 352 ? 117.768 122.222 145.527 1.00 38.58 ?  352 GLU B OE1   1 
ATOM   8410  O  OE2   . GLU B 1 352 ? 117.079 120.204 146.048 1.00 41.64 -1 352 GLU B OE2   1 
ATOM   8411  N  N     . SER B 1 353 ? 120.920 124.903 148.946 1.00 34.01 ?  353 SER B N     1 
ATOM   8412  C  CA    . SER B 1 353 ? 122.107 125.714 148.713 1.00 35.75 ?  353 SER B CA    1 
ATOM   8413  C  C     . SER B 1 353 ? 122.123 127.048 149.447 1.00 31.83 ?  353 SER B C     1 
ATOM   8414  O  O     . SER B 1 353 ? 123.119 127.772 149.346 1.00 34.71 ?  353 SER B O     1 
ATOM   8415  C  CB    . SER B 1 353 ? 122.280 125.977 147.209 1.00 35.48 ?  353 SER B CB    1 
ATOM   8416  O  OG    . SER B 1 353 ? 121.225 126.776 146.707 1.00 36.62 ?  353 SER B OG    1 
ATOM   8417  N  N     . GLY B 1 354 ? 121.065 127.400 150.174 1.00 22.19 ?  354 GLY B N     1 
ATOM   8418  C  CA    . GLY B 1 354 ? 121.012 128.678 150.851 1.00 23.41 ?  354 GLY B CA    1 
ATOM   8419  C  C     . GLY B 1 354 ? 120.579 129.844 149.991 1.00 21.72 ?  354 GLY B C     1 
ATOM   8420  O  O     . GLY B 1 354 ? 120.500 130.969 150.498 1.00 28.76 ?  354 GLY B O     1 
ATOM   8421  N  N     . TYR B 1 355 ? 120.295 129.614 148.718 1.00 25.60 ?  355 TYR B N     1 
ATOM   8422  C  CA    . TYR B 1 355 ? 119.841 130.620 147.778 1.00 17.85 ?  355 TYR B CA    1 
ATOM   8423  C  C     . TYR B 1 355 ? 118.386 130.369 147.408 1.00 20.21 ?  355 TYR B C     1 
ATOM   8424  O  O     . TYR B 1 355 ? 117.905 129.235 147.492 1.00 28.32 ?  355 TYR B O     1 
ATOM   8425  C  CB    . TYR B 1 355 ? 120.712 130.600 146.515 1.00 22.73 ?  355 TYR B CB    1 
ATOM   8426  C  CG    . TYR B 1 355 ? 122.123 131.080 146.741 1.00 25.91 ?  355 TYR B CG    1 
ATOM   8427  C  CD1   . TYR B 1 355 ? 122.371 132.315 147.322 1.00 23.53 ?  355 TYR B CD1   1 
ATOM   8428  C  CD2   . TYR B 1 355 ? 123.211 130.296 146.378 1.00 26.75 ?  355 TYR B CD2   1 
ATOM   8429  C  CE1   . TYR B 1 355 ? 123.658 132.757 147.534 1.00 26.24 ?  355 TYR B CE1   1 
ATOM   8430  C  CE2   . TYR B 1 355 ? 124.503 130.731 146.586 1.00 28.07 ?  355 TYR B CE2   1 
ATOM   8431  C  CZ    . TYR B 1 355 ? 124.721 131.963 147.164 1.00 29.17 ?  355 TYR B CZ    1 
ATOM   8432  O  OH    . TYR B 1 355 ? 126.006 132.403 147.374 1.00 30.83 ?  355 TYR B OH    1 
ATOM   8433  N  N     . PRO B 1 356 ? 117.646 131.400 146.982 1.00 21.44 ?  356 PRO B N     1 
ATOM   8434  C  CA    . PRO B 1 356 ? 118.028 132.804 146.789 1.00 17.78 ?  356 PRO B CA    1 
ATOM   8435  C  C     . PRO B 1 356 ? 117.968 133.656 148.046 1.00 17.32 ?  356 PRO B C     1 
ATOM   8436  O  O     . PRO B 1 356 ? 117.393 133.269 149.058 1.00 20.04 ?  356 PRO B O     1 
ATOM   8437  C  CB    . PRO B 1 356 ? 116.994 133.285 145.769 1.00 16.77 ?  356 PRO B CB    1 
ATOM   8438  C  CG    . PRO B 1 356 ? 115.761 132.538 146.162 1.00 19.79 ?  356 PRO B CG    1 
ATOM   8439  C  CD    . PRO B 1 356 ? 116.248 131.169 146.579 1.00 17.79 ?  356 PRO B CD    1 
ATOM   8440  N  N     . TYR B 1 357 ? 118.574 134.839 147.993 1.00 23.57 ?  357 TYR B N     1 
ATOM   8441  C  CA    . TYR B 1 357 ? 118.246 135.877 148.955 1.00 11.38 ?  357 TYR B CA    1 
ATOM   8442  C  C     . TYR B 1 357 ? 116.800 136.304 148.748 1.00 17.94 ?  357 TYR B C     1 
ATOM   8443  O  O     . TYR B 1 357 ? 116.315 136.376 147.616 1.00 26.55 ?  357 TYR B O     1 
ATOM   8444  C  CB    . TYR B 1 357 ? 119.175 137.081 148.795 1.00 16.41 ?  357 TYR B CB    1 
ATOM   8445  C  CG    . TYR B 1 357 ? 120.649 136.748 148.766 1.00 21.16 ?  357 TYR B CG    1 
ATOM   8446  C  CD1   . TYR B 1 357 ? 121.155 135.687 149.497 1.00 15.33 ?  357 TYR B CD1   1 
ATOM   8447  C  CD2   . TYR B 1 357 ? 121.536 137.500 148.007 1.00 20.38 ?  357 TYR B CD2   1 
ATOM   8448  C  CE1   . TYR B 1 357 ? 122.498 135.381 149.480 1.00 20.34 ?  357 TYR B CE1   1 
ATOM   8449  C  CE2   . TYR B 1 357 ? 122.882 137.200 147.979 1.00 15.32 ?  357 TYR B CE2   1 
ATOM   8450  C  CZ    . TYR B 1 357 ? 123.358 136.139 148.719 1.00 21.33 ?  357 TYR B CZ    1 
ATOM   8451  O  OH    . TYR B 1 357 ? 124.698 135.834 148.700 1.00 31.57 ?  357 TYR B OH    1 
ATOM   8452  N  N     . ILE B 1 358 ? 116.104 136.580 149.843 1.00 15.26 ?  358 ILE B N     1 
ATOM   8453  C  CA    . ILE B 1 358 ? 114.706 136.984 149.796 1.00 14.09 ?  358 ILE B CA    1 
ATOM   8454  C  C     . ILE B 1 358 ? 114.630 138.447 150.201 1.00 15.26 ?  358 ILE B C     1 
ATOM   8455  O  O     . ILE B 1 358 ? 115.068 138.819 151.295 1.00 24.51 ?  358 ILE B O     1 
ATOM   8456  C  CB    . ILE B 1 358 ? 113.830 136.112 150.707 1.00 23.12 ?  358 ILE B CB    1 
ATOM   8457  C  CG1   . ILE B 1 358 ? 113.862 134.655 150.245 1.00 15.21 ?  358 ILE B CG1   1 
ATOM   8458  C  CG2   . ILE B 1 358 ? 112.403 136.633 150.721 1.00 16.12 ?  358 ILE B CG2   1 
ATOM   8459  C  CD1   . ILE B 1 358 ? 113.373 134.453 148.830 1.00 19.53 ?  358 ILE B CD1   1 
ATOM   8460  N  N     . MET B 1 359 ? 114.081 139.275 149.317 1.00 17.72 ?  359 MET B N     1 
ATOM   8461  C  CA    . MET B 1 359 ? 113.863 140.693 149.587 1.00 7.28  ?  359 MET B CA    1 
ATOM   8462  C  C     . MET B 1 359 ? 112.368 140.962 149.518 1.00 9.30  ?  359 MET B C     1 
ATOM   8463  O  O     . MET B 1 359 ? 111.766 140.882 148.442 1.00 20.49 ?  359 MET B O     1 
ATOM   8464  C  CB    . MET B 1 359 ? 114.622 141.571 148.595 1.00 8.65  ?  359 MET B CB    1 
ATOM   8465  C  CG    . MET B 1 359 ? 114.579 143.050 148.936 1.00 9.10  ?  359 MET B CG    1 
ATOM   8466  S  SD    . MET B 1 359 ? 114.633 144.110 147.485 1.00 32.53 ?  359 MET B SD    1 
ATOM   8467  C  CE    . MET B 1 359 ? 113.680 145.509 148.055 1.00 9.56  ?  359 MET B CE    1 
ATOM   8468  N  N     . PHE B 1 360 ? 111.769 141.274 150.662 1.00 10.36 ?  360 PHE B N     1 
ATOM   8469  C  CA    . PHE B 1 360 ? 110.352 141.621 150.718 1.00 10.65 ?  360 PHE B CA    1 
ATOM   8470  C  C     . PHE B 1 360 ? 110.224 143.089 150.338 1.00 16.04 ?  360 PHE B C     1 
ATOM   8471  O  O     . PHE B 1 360 ? 110.413 143.978 151.170 1.00 19.76 ?  360 PHE B O     1 
ATOM   8472  C  CB    . PHE B 1 360 ? 109.787 141.333 152.102 1.00 12.02 ?  360 PHE B CB    1 
ATOM   8473  C  CG    . PHE B 1 360 ? 109.798 139.875 152.460 1.00 15.34 ?  360 PHE B CG    1 
ATOM   8474  C  CD1   . PHE B 1 360 ? 109.068 138.961 151.721 1.00 15.19 ?  360 PHE B CD1   1 
ATOM   8475  C  CD2   . PHE B 1 360 ? 110.554 139.417 153.526 1.00 14.96 ?  360 PHE B CD2   1 
ATOM   8476  C  CE1   . PHE B 1 360 ? 109.084 137.618 152.045 1.00 13.79 ?  360 PHE B CE1   1 
ATOM   8477  C  CE2   . PHE B 1 360 ? 110.573 138.076 153.853 1.00 14.37 ?  360 PHE B CE2   1 
ATOM   8478  C  CZ    . PHE B 1 360 ? 109.836 137.176 153.112 1.00 17.05 ?  360 PHE B CZ    1 
ATOM   8479  N  N     . GLN B 1 361 ? 109.892 143.337 149.067 1.00 16.85 ?  361 GLN B N     1 
ATOM   8480  C  CA    . GLN B 1 361 ? 109.959 144.687 148.514 1.00 9.93  ?  361 GLN B CA    1 
ATOM   8481  C  C     . GLN B 1 361 ? 109.041 145.649 149.255 1.00 13.61 ?  361 GLN B C     1 
ATOM   8482  O  O     . GLN B 1 361 ? 109.427 146.788 149.547 1.00 15.15 ?  361 GLN B O     1 
ATOM   8483  C  CB    . GLN B 1 361 ? 109.603 144.650 147.028 1.00 15.59 ?  361 GLN B CB    1 
ATOM   8484  C  CG    . GLN B 1 361 ? 109.737 145.979 146.315 1.00 15.46 ?  361 GLN B CG    1 
ATOM   8485  C  CD    . GLN B 1 361 ? 109.938 145.816 144.825 1.00 17.89 ?  361 GLN B CD    1 
ATOM   8486  O  OE1   . GLN B 1 361 ? 109.348 144.935 144.202 1.00 27.70 ?  361 GLN B OE1   1 
ATOM   8487  N  NE2   . GLN B 1 361 ? 110.778 146.663 144.243 1.00 18.34 ?  361 GLN B NE2   1 
ATOM   8488  N  N     . ASP B 1 362 ? 107.817 145.216 149.562 1.00 20.04 ?  362 ASP B N     1 
ATOM   8489  C  CA    . ASP B 1 362 ? 106.880 146.102 150.242 1.00 15.90 ?  362 ASP B CA    1 
ATOM   8490  C  C     . ASP B 1 362 ? 107.313 146.387 151.673 1.00 16.17 ?  362 ASP B C     1 
ATOM   8491  O  O     . ASP B 1 362 ? 107.109 147.500 152.167 1.00 23.66 ?  362 ASP B O     1 
ATOM   8492  C  CB    . ASP B 1 362 ? 105.476 145.506 150.214 1.00 22.13 ?  362 ASP B CB    1 
ATOM   8493  C  CG    . ASP B 1 362 ? 104.777 145.737 148.891 1.00 29.34 ?  362 ASP B CG    1 
ATOM   8494  O  OD1   . ASP B 1 362 ? 105.112 145.041 147.910 1.00 29.39 ?  362 ASP B OD1   1 
ATOM   8495  O  OD2   . ASP B 1 362 ? 103.892 146.616 148.830 1.00 30.44 -1 362 ASP B OD2   1 
ATOM   8496  N  N     . ASN B 1 363 ? 107.917 145.407 152.349 1.00 21.55 ?  363 ASN B N     1 
ATOM   8497  C  CA    . ASN B 1 363 ? 108.465 145.661 153.677 1.00 10.88 ?  363 ASN B CA    1 
ATOM   8498  C  C     . ASN B 1 363 ? 109.578 146.696 153.628 1.00 14.86 ?  363 ASN B C     1 
ATOM   8499  O  O     . ASN B 1 363 ? 109.724 147.498 154.558 1.00 25.42 ?  363 ASN B O     1 
ATOM   8500  C  CB    . ASN B 1 363 ? 108.981 144.359 154.291 1.00 12.50 ?  363 ASN B CB    1 
ATOM   8501  C  CG    . ASN B 1 363 ? 107.864 143.459 154.771 1.00 16.62 ?  363 ASN B CG    1 
ATOM   8502  O  OD1   . ASN B 1 363 ? 106.750 143.914 155.020 1.00 21.40 ?  363 ASN B OD1   1 
ATOM   8503  N  ND2   . ASN B 1 363 ? 108.158 142.172 154.903 1.00 15.52 ?  363 ASN B ND2   1 
ATOM   8504  N  N     . VAL B 1 364 ? 110.376 146.690 152.559 1.00 14.12 ?  364 VAL B N     1 
ATOM   8505  C  CA    . VAL B 1 364 ? 111.431 147.685 152.409 1.00 9.03  ?  364 VAL B CA    1 
ATOM   8506  C  C     . VAL B 1 364 ? 110.839 149.059 152.122 1.00 16.84 ?  364 VAL B C     1 
ATOM   8507  O  O     . VAL B 1 364 ? 111.280 150.068 152.684 1.00 18.99 ?  364 VAL B O     1 
ATOM   8508  C  CB    . VAL B 1 364 ? 112.413 147.256 151.304 1.00 2.44  ?  364 VAL B CB    1 
ATOM   8509  C  CG1   . VAL B 1 364 ? 113.553 148.248 151.198 1.00 6.38  ?  364 VAL B CG1   1 
ATOM   8510  C  CG2   . VAL B 1 364 ? 112.940 145.863 151.578 1.00 9.06  ?  364 VAL B CG2   1 
ATOM   8511  N  N     . ASN B 1 365 ? 109.835 149.125 151.249 1.00 18.91 ?  365 ASN B N     1 
ATOM   8512  C  CA    . ASN B 1 365 ? 109.362 150.402 150.735 1.00 7.74  ?  365 ASN B CA    1 
ATOM   8513  C  C     . ASN B 1 365 ? 108.247 151.030 151.561 1.00 15.37 ?  365 ASN B C     1 
ATOM   8514  O  O     . ASN B 1 365 ? 107.912 152.194 151.321 1.00 22.95 ?  365 ASN B O     1 
ATOM   8515  C  CB    . ASN B 1 365 ? 108.890 150.242 149.287 1.00 11.88 ?  365 ASN B CB    1 
ATOM   8516  C  CG    . ASN B 1 365 ? 110.038 150.051 148.321 1.00 13.44 ?  365 ASN B CG    1 
ATOM   8517  O  OD1   . ASN B 1 365 ? 110.993 150.825 148.316 1.00 15.79 ?  365 ASN B OD1   1 
ATOM   8518  N  ND2   . ASN B 1 365 ? 109.952 149.016 147.499 1.00 19.25 ?  365 ASN B ND2   1 
ATOM   8519  N  N     . LYS B 1 366 ? 107.664 150.307 152.518 1.00 15.39 ?  366 LYS B N     1 
ATOM   8520  C  CA    . LYS B 1 366 ? 106.666 150.921 153.384 1.00 17.04 ?  366 LYS B CA    1 
ATOM   8521  C  C     . LYS B 1 366 ? 107.292 151.840 154.422 1.00 19.24 ?  366 LYS B C     1 
ATOM   8522  O  O     . LYS B 1 366 ? 106.603 152.718 154.951 1.00 26.94 ?  366 LYS B O     1 
ATOM   8523  C  CB    . LYS B 1 366 ? 105.828 149.846 154.079 1.00 18.92 ?  366 LYS B CB    1 
ATOM   8524  C  CG    . LYS B 1 366 ? 106.622 148.915 154.982 1.00 22.26 ?  366 LYS B CG    1 
ATOM   8525  C  CD    . LYS B 1 366 ? 105.726 148.232 156.008 1.00 24.45 ?  366 LYS B CD    1 
ATOM   8526  C  CE    . LYS B 1 366 ? 104.385 147.828 155.411 1.00 24.01 ?  366 LYS B CE    1 
ATOM   8527  N  NZ    . LYS B 1 366 ? 104.500 146.642 154.518 1.00 24.16 1  366 LYS B NZ    1 
ATOM   8528  N  N     . VAL B 1 367 ? 108.576 151.657 154.719 1.00 24.11 ?  367 VAL B N     1 
ATOM   8529  C  CA    . VAL B 1 367 ? 109.317 152.530 155.618 1.00 14.42 ?  367 VAL B CA    1 
ATOM   8530  C  C     . VAL B 1 367 ? 110.496 153.198 154.933 1.00 16.80 ?  367 VAL B C     1 
ATOM   8531  O  O     . VAL B 1 367 ? 111.263 153.905 155.594 1.00 22.49 ?  367 VAL B O     1 
ATOM   8532  C  CB    . VAL B 1 367 ? 109.789 151.773 156.876 1.00 12.46 ?  367 VAL B CB    1 
ATOM   8533  C  CG1   . VAL B 1 367 ? 108.594 151.282 157.675 1.00 19.88 ?  367 VAL B CG1   1 
ATOM   8534  C  CG2   . VAL B 1 367 ? 110.681 150.612 156.485 1.00 9.76  ?  367 VAL B CG2   1 
ATOM   8535  N  N     . HIS B 1 368 ? 110.666 152.989 153.630 1.00 20.92 ?  368 HIS B N     1 
ATOM   8536  C  CA    . HIS B 1 368 ? 111.745 153.627 152.889 1.00 5.32  ?  368 HIS B CA    1 
ATOM   8537  C  C     . HIS B 1 368 ? 111.543 155.137 152.867 1.00 15.48 ?  368 HIS B C     1 
ATOM   8538  O  O     . HIS B 1 368 ? 110.465 155.627 152.518 1.00 25.96 ?  368 HIS B O     1 
ATOM   8539  C  CB    . HIS B 1 368 ? 111.796 153.072 151.467 1.00 13.01 ?  368 HIS B CB    1 
ATOM   8540  C  CG    . HIS B 1 368 ? 112.933 153.597 150.650 1.00 10.56 ?  368 HIS B CG    1 
ATOM   8541  N  ND1   . HIS B 1 368 ? 112.834 153.807 149.292 1.00 14.86 ?  368 HIS B ND1   1 
ATOM   8542  C  CD2   . HIS B 1 368 ? 114.193 153.948 150.994 1.00 7.35  ?  368 HIS B CD2   1 
ATOM   8543  C  CE1   . HIS B 1 368 ? 113.985 154.267 148.836 1.00 14.41 ?  368 HIS B CE1   1 
ATOM   8544  N  NE2   . HIS B 1 368 ? 114.827 154.362 149.849 1.00 10.81 ?  368 HIS B NE2   1 
ATOM   8545  N  N     . ALA B 1 369 ? 112.587 155.875 153.241 1.00 20.22 ?  369 ALA B N     1 
ATOM   8546  C  CA    . ALA B 1 369 ? 112.491 157.321 153.368 1.00 10.07 ?  369 ALA B CA    1 
ATOM   8547  C  C     . ALA B 1 369 ? 112.703 158.060 152.055 1.00 17.57 ?  369 ALA B C     1 
ATOM   8548  O  O     . ALA B 1 369 ? 112.425 159.261 151.993 1.00 26.04 ?  369 ALA B O     1 
ATOM   8549  C  CB    . ALA B 1 369 ? 113.501 157.820 154.401 1.00 10.84 ?  369 ALA B CB    1 
ATOM   8550  N  N     . ASN B 1 370 ? 113.177 157.384 151.012 1.00 16.15 ?  370 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 370 ? 113.521 158.026 149.750 1.00 14.72 ?  370 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 370 ? 112.776 157.390 148.584 1.00 12.00 ?  370 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 370 ? 113.340 157.167 147.511 1.00 18.38 ?  370 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 370 ? 115.029 157.982 149.517 1.00 11.27 ?  370 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 370 ? 115.806 158.680 150.613 1.00 11.90 ?  370 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 370 ? 115.622 159.872 150.856 1.00 26.54 ?  370 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 370 ? 116.677 157.940 151.285 1.00 16.28 ?  370 ASN B ND2   1 
ATOM   8558  N  N     . ASN B 1 371 ? 111.492 157.088 148.783 1.00 20.31 ?  371 ASN B N     1 
ATOM   8559  C  CA    . ASN B 1 371 ? 110.678 156.546 147.703 1.00 10.79 ?  371 ASN B CA    1 
ATOM   8560  C  C     . ASN B 1 371 ? 110.487 157.541 146.567 1.00 16.41 ?  371 ASN B C     1 
ATOM   8561  O  O     . ASN B 1 371 ? 110.241 157.125 145.431 1.00 19.64 ?  371 ASN B O     1 
ATOM   8562  C  CB    . ASN B 1 371 ? 109.315 156.106 148.239 1.00 6.58  ?  371 ASN B CB    1 
ATOM   8563  C  CG    . ASN B 1 371 ? 109.336 154.702 148.800 1.00 16.28 ?  371 ASN B CG    1 
ATOM   8564  O  OD1   . ASN B 1 371 ? 110.181 153.887 148.432 1.00 20.36 ?  371 ASN B OD1   1 
ATOM   8565  N  ND2   . ASN B 1 371 ? 108.402 154.410 149.696 1.00 19.92 ?  371 ASN B ND2   1 
ATOM   8566  N  N     . HIS B 1 372 ? 110.587 158.841 146.853 1.00 21.65 ?  372 HIS B N     1 
ATOM   8567  C  CA    . HIS B 1 372 ? 110.463 159.847 145.804 1.00 17.77 ?  372 HIS B CA    1 
ATOM   8568  C  C     . HIS B 1 372 ? 111.581 159.716 144.777 1.00 20.25 ?  372 HIS B C     1 
ATOM   8569  O  O     . HIS B 1 372 ? 111.341 159.829 143.570 1.00 26.17 ?  372 HIS B O     1 
ATOM   8570  C  CB    . HIS B 1 372 ? 110.462 161.245 146.423 1.00 19.55 ?  372 HIS B CB    1 
ATOM   8571  C  CG    . HIS B 1 372 ? 111.753 161.610 147.085 1.00 19.08 ?  372 HIS B CG    1 
ATOM   8572  N  ND1   . HIS B 1 372 ? 112.265 160.907 148.154 1.00 22.10 ?  372 HIS B ND1   1 
ATOM   8573  C  CD2   . HIS B 1 372 ? 112.641 162.597 146.824 1.00 20.71 ?  372 HIS B CD2   1 
ATOM   8574  C  CE1   . HIS B 1 372 ? 113.413 161.447 148.523 1.00 17.13 ?  372 HIS B CE1   1 
ATOM   8575  N  NE2   . HIS B 1 372 ? 113.660 162.477 147.734 1.00 24.73 ?  372 HIS B NE2   1 
ATOM   8576  N  N     . ILE B 1 373 ? 112.813 159.488 145.239 1.00 16.01 ?  373 ILE B N     1 
ATOM   8577  C  CA    . ILE B 1 373 ? 113.924 159.268 144.318 1.00 18.41 ?  373 ILE B CA    1 
ATOM   8578  C  C     . ILE B 1 373 ? 113.691 157.996 143.517 1.00 18.51 ?  373 ILE B C     1 
ATOM   8579  O  O     . ILE B 1 373 ? 113.750 157.995 142.281 1.00 28.73 ?  373 ILE B O     1 
ATOM   8580  C  CB    . ILE B 1 373 ? 115.254 159.205 145.090 1.00 20.64 ?  373 ILE B CB    1 
ATOM   8581  C  CG1   . ILE B 1 373 ? 115.508 160.522 145.819 1.00 18.92 ?  373 ILE B CG1   1 
ATOM   8582  C  CG2   . ILE B 1 373 ? 116.405 158.876 144.151 1.00 19.25 ?  373 ILE B CG2   1 
ATOM   8583  C  CD1   . ILE B 1 373 ? 116.618 160.454 146.835 1.00 14.77 ?  373 ILE B CD1   1 
ATOM   8584  N  N     . SER B 1 374 ? 113.399 156.902 144.216 1.00 17.14 ?  374 SER B N     1 
ATOM   8585  C  CA    . SER B 1 374 ? 113.134 155.606 143.610 1.00 6.86  ?  374 SER B CA    1 
ATOM   8586  C  C     . SER B 1 374 ? 112.733 154.620 144.696 1.00 13.56 ?  374 SER B C     1 
ATOM   8587  O  O     . SER B 1 374 ? 113.110 154.788 145.859 1.00 16.95 ?  374 SER B O     1 
ATOM   8588  C  CB    . SER B 1 374 ? 114.360 155.093 142.855 1.00 18.97 ?  374 SER B CB    1 
ATOM   8589  O  OG    . SER B 1 374 ? 114.000 154.105 141.908 1.00 32.64 ?  374 SER B OG    1 
ATOM   8590  N  N     . LYS B 1 375 ? 111.967 153.598 144.337 1.00 24.02 ?  375 LYS B N     1 
ATOM   8591  C  CA    . LYS B 1 375 ? 111.720 152.504 145.258 1.00 14.13 ?  375 LYS B CA    1 
ATOM   8592  C  C     . LYS B 1 375 ? 112.916 151.562 145.269 1.00 15.05 ?  375 LYS B C     1 
ATOM   8593  O  O     . LYS B 1 375 ? 113.653 151.450 144.286 1.00 23.95 ?  375 LYS B O     1 
ATOM   8594  C  CB    . LYS B 1 375 ? 110.456 151.738 144.870 1.00 11.94 ?  375 LYS B CB    1 
ATOM   8595  C  CG    . LYS B 1 375 ? 109.196 152.580 144.868 1.00 17.96 ?  375 LYS B CG    1 
ATOM   8596  C  CD    . LYS B 1 375 ? 108.288 152.210 146.025 1.00 17.81 ?  375 LYS B CD    1 
ATOM   8597  C  CE    . LYS B 1 375 ? 107.001 153.012 145.989 1.00 16.98 ?  375 LYS B CE    1 
ATOM   8598  N  NZ    . LYS B 1 375 ? 107.230 154.404 145.516 1.00 23.96 1  375 LYS B NZ    1 
ATOM   8599  N  N     . VAL B 1 376 ? 113.115 150.890 146.397 1.00 9.75  ?  376 VAL B N     1 
ATOM   8600  C  CA    . VAL B 1 376 ? 114.182 149.903 146.501 1.00 13.73 ?  376 VAL B CA    1 
ATOM   8601  C  C     . VAL B 1 376 ? 113.738 148.645 145.768 1.00 16.12 ?  376 VAL B C     1 
ATOM   8602  O  O     . VAL B 1 376 ? 112.761 147.998 146.162 1.00 23.12 ?  376 VAL B O     1 
ATOM   8603  C  CB    . VAL B 1 376 ? 114.525 149.604 147.966 1.00 11.90 ?  376 VAL B CB    1 
ATOM   8604  C  CG1   . VAL B 1 376 ? 115.678 148.621 148.042 1.00 10.55 ?  376 VAL B CG1   1 
ATOM   8605  C  CG2   . VAL B 1 376 ? 114.865 150.886 148.702 1.00 6.92  ?  376 VAL B CG2   1 
ATOM   8606  N  N     . LYS B 1 377 ? 114.448 148.298 144.696 1.00 14.55 ?  377 LYS B N     1 
ATOM   8607  C  CA    . LYS B 1 377 ? 114.060 147.173 143.859 1.00 9.58  ?  377 LYS B CA    1 
ATOM   8608  C  C     . LYS B 1 377 ? 114.924 145.939 144.060 1.00 9.63  ?  377 LYS B C     1 
ATOM   8609  O  O     . LYS B 1 377 ? 114.543 144.861 143.596 1.00 24.47 ?  377 LYS B O     1 
ATOM   8610  C  CB    . LYS B 1 377 ? 114.104 147.564 142.379 1.00 13.22 ?  377 LYS B CB    1 
ATOM   8611  C  CG    . LYS B 1 377 ? 113.433 148.879 142.062 1.00 9.80  ?  377 LYS B CG    1 
ATOM   8612  C  CD    . LYS B 1 377 ? 114.176 149.591 140.955 1.00 18.20 ?  377 LYS B CD    1 
ATOM   8613  C  CE    . LYS B 1 377 ? 114.070 151.090 141.101 1.00 20.76 ?  377 LYS B CE    1 
ATOM   8614  N  NZ    . LYS B 1 377 ? 115.057 151.789 140.234 1.00 19.82 1  377 LYS B NZ    1 
ATOM   8615  N  N     . PHE B 1 378 ? 116.071 146.066 144.719 1.00 11.14 ?  378 PHE B N     1 
ATOM   8616  C  CA    . PHE B 1 378 ? 116.953 144.930 144.951 1.00 8.11  ?  378 PHE B CA    1 
ATOM   8617  C  C     . PHE B 1 378 ? 117.899 145.281 146.091 1.00 7.41  ?  378 PHE B C     1 
ATOM   8618  O  O     . PHE B 1 378 ? 117.923 146.413 146.580 1.00 16.36 ?  378 PHE B O     1 
ATOM   8619  C  CB    . PHE B 1 378 ? 117.701 144.538 143.673 1.00 4.29  ?  378 PHE B CB    1 
ATOM   8620  C  CG    . PHE B 1 378 ? 118.782 145.500 143.267 1.00 4.17  ?  378 PHE B CG    1 
ATOM   8621  C  CD1   . PHE B 1 378 ? 118.482 146.815 142.958 1.00 10.59 ?  378 PHE B CD1   1 
ATOM   8622  C  CD2   . PHE B 1 378 ? 120.096 145.079 143.173 1.00 3.19  ?  378 PHE B CD2   1 
ATOM   8623  C  CE1   . PHE B 1 378 ? 119.472 147.694 142.580 1.00 7.65  ?  378 PHE B CE1   1 
ATOM   8624  C  CE2   . PHE B 1 378 ? 121.088 145.954 142.793 1.00 10.18 ?  378 PHE B CE2   1 
ATOM   8625  C  CZ    . PHE B 1 378 ? 120.775 147.264 142.495 1.00 11.71 ?  378 PHE B CZ    1 
ATOM   8626  N  N     . SER B 1 379 ? 118.676 144.293 146.518 1.00 2.13  ?  379 SER B N     1 
ATOM   8627  C  CA    . SER B 1 379 ? 119.612 144.437 147.624 1.00 0.54  ?  379 SER B CA    1 
ATOM   8628  C  C     . SER B 1 379 ? 121.024 144.118 147.139 1.00 4.59  ?  379 SER B C     1 
ATOM   8629  O  O     . SER B 1 379 ? 121.263 143.899 145.949 1.00 7.64  ?  379 SER B O     1 
ATOM   8630  C  CB    . SER B 1 379 ? 119.199 143.545 148.795 1.00 10.27 ?  379 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 379 ? 119.601 144.114 150.027 1.00 10.56 ?  379 SER B OG    1 
ATOM   8632  N  N     . ASN B 1 380 ? 121.967 144.102 148.075 1.00 11.08 ?  380 ASN B N     1 
ATOM   8633  C  CA    . ASN B 1 380 ? 123.369 143.887 147.768 1.00 7.33  ?  380 ASN B CA    1 
ATOM   8634  C  C     . ASN B 1 380 ? 123.715 142.406 147.904 1.00 13.50 ?  380 ASN B C     1 
ATOM   8635  O  O     . ASN B 1 380 ? 122.841 141.549 148.067 1.00 16.85 ?  380 ASN B O     1 
ATOM   8636  C  CB    . ASN B 1 380 ? 124.244 144.763 148.667 1.00 8.68  ?  380 ASN B CB    1 
ATOM   8637  C  CG    . ASN B 1 380 ? 124.196 144.342 150.118 1.00 6.85  ?  380 ASN B CG    1 
ATOM   8638  O  OD1   . ASN B 1 380 ? 123.125 144.100 150.671 1.00 19.12 ?  380 ASN B OD1   1 
ATOM   8639  N  ND2   . ASN B 1 380 ? 125.361 144.254 150.744 1.00 13.32 ?  380 ASN B ND2   1 
ATOM   8640  N  N     . LEU B 1 381 ? 125.010 142.095 147.824 1.00 18.23 ?  381 LEU B N     1 
ATOM   8641  C  CA    . LEU B 1 381 ? 125.466 140.715 147.917 1.00 11.49 ?  381 LEU B CA    1 
ATOM   8642  C  C     . LEU B 1 381 ? 125.217 140.116 149.296 1.00 7.62  ?  381 LEU B C     1 
ATOM   8643  O  O     . LEU B 1 381 ? 125.076 138.894 149.411 1.00 18.28 ?  381 LEU B O     1 
ATOM   8644  C  CB    . LEU B 1 381 ? 126.954 140.644 147.562 1.00 17.87 ?  381 LEU B CB    1 
ATOM   8645  C  CG    . LEU B 1 381 ? 127.701 139.315 147.689 1.00 19.37 ?  381 LEU B CG    1 
ATOM   8646  C  CD1   . LEU B 1 381 ? 127.225 138.318 146.647 1.00 15.88 ?  381 LEU B CD1   1 
ATOM   8647  C  CD2   . LEU B 1 381 ? 129.196 139.543 147.572 1.00 17.74 ?  381 LEU B CD2   1 
ATOM   8648  N  N     . CYS B 1 382 ? 125.147 140.941 150.337 1.00 11.63 ?  382 CYS B N     1 
ATOM   8649  C  CA    . CYS B 1 382 ? 124.835 140.475 151.680 1.00 5.10  ?  382 CYS B CA    1 
ATOM   8650  C  C     . CYS B 1 382 ? 123.395 140.764 152.081 1.00 8.11  ?  382 CYS B C     1 
ATOM   8651  O  O     . CYS B 1 382 ? 123.019 140.490 153.225 1.00 17.87 ?  382 CYS B O     1 
ATOM   8652  C  CB    . CYS B 1 382 ? 125.797 141.101 152.693 1.00 16.37 ?  382 CYS B CB    1 
ATOM   8653  S  SG    . CYS B 1 382 ? 127.544 140.953 152.252 1.00 31.70 ?  382 CYS B SG    1 
ATOM   8654  N  N     . SER B 1 383 ? 122.587 141.307 151.168 1.00 10.35 ?  383 SER B N     1 
ATOM   8655  C  CA    . SER B 1 383 ? 121.153 141.523 151.375 1.00 9.66  ?  383 SER B CA    1 
ATOM   8656  C  C     . SER B 1 383 ? 120.873 142.362 152.620 1.00 12.91 ?  383 SER B C     1 
ATOM   8657  O  O     . SER B 1 383 ? 119.979 142.060 153.411 1.00 23.55 ?  383 SER B O     1 
ATOM   8658  C  CB    . SER B 1 383 ? 120.398 140.194 151.439 1.00 13.23 ?  383 SER B CB    1 
ATOM   8659  O  OG    . SER B 1 383 ? 120.842 139.400 152.520 1.00 18.79 ?  383 SER B OG    1 
ATOM   8660  N  N     . GLU B 1 384 ? 121.651 143.428 152.802 1.00 7.46  ?  384 GLU B N     1 
ATOM   8661  C  CA    . GLU B 1 384 ? 121.381 144.391 153.859 1.00 8.37  ?  384 GLU B CA    1 
ATOM   8662  C  C     . GLU B 1 384 ? 121.345 145.831 153.371 1.00 13.49 ?  384 GLU B C     1 
ATOM   8663  O  O     . GLU B 1 384 ? 120.869 146.701 154.110 1.00 23.85 ?  384 GLU B O     1 
ATOM   8664  C  CB    . GLU B 1 384 ? 122.413 144.260 154.993 1.00 6.60  ?  384 GLU B CB    1 
ATOM   8665  C  CG    . GLU B 1 384 ? 123.500 145.322 155.030 1.00 10.32 ?  384 GLU B CG    1 
ATOM   8666  C  CD    . GLU B 1 384 ? 124.625 145.045 154.060 1.00 19.47 ?  384 GLU B CD    1 
ATOM   8667  O  OE1   . GLU B 1 384 ? 124.704 143.910 153.554 1.00 13.01 ?  384 GLU B OE1   1 
ATOM   8668  O  OE2   . GLU B 1 384 ? 125.440 145.958 153.819 1.00 26.60 -1 384 GLU B OE2   1 
ATOM   8669  N  N     . VAL B 1 385 ? 121.808 146.110 152.159 1.00 10.47 ?  385 VAL B N     1 
ATOM   8670  C  CA    . VAL B 1 385 ? 121.749 147.449 151.590 1.00 6.73  ?  385 VAL B CA    1 
ATOM   8671  C  C     . VAL B 1 385 ? 120.444 147.585 150.820 1.00 15.55 ?  385 VAL B C     1 
ATOM   8672  O  O     . VAL B 1 385 ? 120.190 146.828 149.877 1.00 24.31 ?  385 VAL B O     1 
ATOM   8673  C  CB    . VAL B 1 385 ? 122.955 147.721 150.682 1.00 6.60  ?  385 VAL B CB    1 
ATOM   8674  C  CG1   . VAL B 1 385 ? 122.782 149.042 149.975 1.00 6.70  ?  385 VAL B CG1   1 
ATOM   8675  C  CG2   . VAL B 1 385 ? 124.227 147.720 151.493 1.00 11.92 ?  385 VAL B CG2   1 
ATOM   8676  N  N     . LEU B 1 386 ? 119.614 148.546 151.223 1.00 12.50 ?  386 LEU B N     1 
ATOM   8677  C  CA    . LEU B 1 386 ? 118.297 148.766 150.626 1.00 2.08  ?  386 LEU B CA    1 
ATOM   8678  C  C     . LEU B 1 386 ? 118.138 150.262 150.384 1.00 5.19  ?  386 LEU B C     1 
ATOM   8679  O  O     . LEU B 1 386 ? 117.702 151.002 151.269 1.00 11.17 ?  386 LEU B O     1 
ATOM   8680  C  CB    . LEU B 1 386 ? 117.199 148.212 151.519 1.00 5.06  ?  386 LEU B CB    1 
ATOM   8681  C  CG    . LEU B 1 386 ? 117.240 146.692 151.674 1.00 5.85  ?  386 LEU B CG    1 
ATOM   8682  C  CD1   . LEU B 1 386 ? 116.358 146.261 152.813 1.00 10.23 ?  386 LEU B CD1   1 
ATOM   8683  C  CD2   . LEU B 1 386 ? 116.824 146.009 150.382 1.00 8.67  ?  386 LEU B CD2   1 
ATOM   8684  N  N     . GLN B 1 387 ? 118.494 150.701 149.180 1.00 11.72 ?  387 GLN B N     1 
ATOM   8685  C  CA    . GLN B 1 387 ? 118.527 152.117 148.850 1.00 9.78  ?  387 GLN B CA    1 
ATOM   8686  C  C     . GLN B 1 387 ? 117.869 152.349 147.499 1.00 11.25 ?  387 GLN B C     1 
ATOM   8687  O  O     . GLN B 1 387 ? 117.724 151.433 146.686 1.00 19.86 ?  387 GLN B O     1 
ATOM   8688  C  CB    . GLN B 1 387 ? 119.963 152.652 148.833 1.00 4.43  ?  387 GLN B CB    1 
ATOM   8689  C  CG    . GLN B 1 387 ? 120.735 152.387 150.108 1.00 6.44  ?  387 GLN B CG    1 
ATOM   8690  C  CD    . GLN B 1 387 ? 122.118 152.982 150.076 1.00 10.27 ?  387 GLN B CD    1 
ATOM   8691  O  OE1   . GLN B 1 387 ? 122.418 153.827 149.235 1.00 21.83 ?  387 GLN B OE1   1 
ATOM   8692  N  NE2   . GLN B 1 387 ? 122.974 152.548 150.990 1.00 10.90 ?  387 GLN B NE2   1 
ATOM   8693  N  N     . ALA B 1 388 ? 117.457 153.593 147.276 1.00 13.59 ?  388 ALA B N     1 
ATOM   8694  C  CA    . ALA B 1 388 ? 116.894 153.982 145.992 1.00 10.79 ?  388 ALA B CA    1 
ATOM   8695  C  C     . ALA B 1 388 ? 117.964 153.945 144.909 1.00 17.73 ?  388 ALA B C     1 
ATOM   8696  O  O     . ALA B 1 388 ? 119.099 154.378 145.117 1.00 23.67 ?  388 ALA B O     1 
ATOM   8697  C  CB    . ALA B 1 388 ? 116.287 155.380 146.080 1.00 9.43  ?  388 ALA B CB    1 
ATOM   8698  N  N     . SER B 1 389 ? 117.596 153.419 143.745 1.00 21.15 ?  389 SER B N     1 
ATOM   8699  C  CA    . SER B 1 389 ? 118.494 153.366 142.604 1.00 8.55  ?  389 SER B CA    1 
ATOM   8700  C  C     . SER B 1 389 ? 117.734 153.745 141.345 1.00 16.13 ?  389 SER B C     1 
ATOM   8701  O  O     . SER B 1 389 ? 116.583 153.342 141.159 1.00 23.96 ?  389 SER B O     1 
ATOM   8702  C  CB    . SER B 1 389 ? 119.117 151.975 142.437 1.00 14.47 ?  389 SER B CB    1 
ATOM   8703  O  OG    . SER B 1 389 ? 118.121 150.967 142.424 1.00 24.83 ?  389 SER B OG    1 
ATOM   8704  N  N     . GLN B 1 390 ? 118.383 154.524 140.487 1.00 17.90 ?  390 GLN B N     1 
ATOM   8705  C  CA    . GLN B 1 390 ? 117.847 154.888 139.186 1.00 11.04 ?  390 GLN B CA    1 
ATOM   8706  C  C     . GLN B 1 390 ? 118.705 154.243 138.110 1.00 12.59 ?  390 GLN B C     1 
ATOM   8707  O  O     . GLN B 1 390 ? 119.935 154.361 138.139 1.00 26.82 ?  390 GLN B O     1 
ATOM   8708  C  CB    . GLN B 1 390 ? 117.811 156.409 139.013 1.00 16.03 ?  390 GLN B CB    1 
ATOM   8709  C  CG    . GLN B 1 390 ? 116.805 157.103 139.917 1.00 18.30 ?  390 GLN B CG    1 
ATOM   8710  C  CD    . GLN B 1 390 ? 116.930 158.612 139.887 1.00 22.91 ?  390 GLN B CD    1 
ATOM   8711  O  OE1   . GLN B 1 390 ? 117.860 159.158 139.297 1.00 25.83 ?  390 GLN B OE1   1 
ATOM   8712  N  NE2   . GLN B 1 390 ? 115.987 159.296 140.527 1.00 18.30 ?  390 GLN B NE2   1 
ATOM   8713  N  N     . VAL B 1 391 ? 118.059 153.551 137.172 1.00 22.98 ?  391 VAL B N     1 
ATOM   8714  C  CA    . VAL B 1 391 ? 118.796 152.842 136.135 1.00 20.87 ?  391 VAL B CA    1 
ATOM   8715  C  C     . VAL B 1 391 ? 119.466 153.844 135.202 1.00 23.00 ?  391 VAL B C     1 
ATOM   8716  O  O     . VAL B 1 391 ? 118.978 154.963 134.991 1.00 21.34 ?  391 VAL B O     1 
ATOM   8717  C  CB    . VAL B 1 391 ? 117.869 151.881 135.367 1.00 15.39 ?  391 VAL B CB    1 
ATOM   8718  C  CG1   . VAL B 1 391 ? 117.013 152.635 134.360 1.00 20.83 ?  391 VAL B CG1   1 
ATOM   8719  C  CG2   . VAL B 1 391 ? 118.677 150.789 134.683 1.00 17.46 ?  391 VAL B CG2   1 
ATOM   8720  N  N     . SER B 1 392 ? 120.609 153.448 134.654 1.00 28.78 ?  392 SER B N     1 
ATOM   8721  C  CA    . SER B 1 392 ? 121.360 154.277 133.726 1.00 21.82 ?  392 SER B CA    1 
ATOM   8722  C  C     . SER B 1 392 ? 121.063 153.861 132.292 1.00 28.18 ?  392 SER B C     1 
ATOM   8723  O  O     . SER B 1 392 ? 120.827 152.686 132.002 1.00 31.29 ?  392 SER B O     1 
ATOM   8724  C  CB    . SER B 1 392 ? 122.864 154.178 133.994 1.00 20.84 ?  392 SER B CB    1 
ATOM   8725  O  OG    . SER B 1 392 ? 123.176 154.577 135.316 1.00 30.03 ?  392 SER B OG    1 
ATOM   8726  N  N     . SER B 1 393 ? 121.075 154.842 131.397 1.00 25.65 ?  393 SER B N     1 
ATOM   8727  C  CA    . SER B 1 393 ? 120.872 154.613 129.970 1.00 23.85 ?  393 SER B CA    1 
ATOM   8728  C  C     . SER B 1 393 ? 122.234 154.736 129.293 1.00 25.99 ?  393 SER B C     1 
ATOM   8729  O  O     . SER B 1 393 ? 122.634 155.817 128.860 1.00 31.14 ?  393 SER B O     1 
ATOM   8730  C  CB    . SER B 1 393 ? 119.862 155.598 129.388 1.00 28.94 ?  393 SER B CB    1 
ATOM   8731  O  OG    . SER B 1 393 ? 118.688 155.650 130.179 1.00 31.30 ?  393 SER B OG    1 
ATOM   8732  N  N     . TYR B 1 394 ? 122.948 153.617 129.216 1.00 28.75 ?  394 TYR B N     1 
ATOM   8733  C  CA    . TYR B 1 394 ? 124.226 153.571 128.514 1.00 26.75 ?  394 TYR B CA    1 
ATOM   8734  C  C     . TYR B 1 394 ? 123.942 153.419 127.025 1.00 26.39 ?  394 TYR B C     1 
ATOM   8735  O  O     . TYR B 1 394 ? 123.468 152.369 126.579 1.00 29.18 ?  394 TYR B O     1 
ATOM   8736  C  CB    . TYR B 1 394 ? 125.085 152.427 129.038 1.00 24.95 ?  394 TYR B CB    1 
ATOM   8737  C  CG    . TYR B 1 394 ? 125.451 152.565 130.499 1.00 23.85 ?  394 TYR B CG    1 
ATOM   8738  C  CD1   . TYR B 1 394 ? 126.291 153.580 130.932 1.00 23.65 ?  394 TYR B CD1   1 
ATOM   8739  C  CD2   . TYR B 1 394 ? 124.949 151.682 131.446 1.00 25.91 ?  394 TYR B CD2   1 
ATOM   8740  C  CE1   . TYR B 1 394 ? 126.627 153.710 132.266 1.00 28.58 ?  394 TYR B CE1   1 
ATOM   8741  C  CE2   . TYR B 1 394 ? 125.278 151.802 132.781 1.00 26.75 ?  394 TYR B CE2   1 
ATOM   8742  C  CZ    . TYR B 1 394 ? 126.117 152.819 133.185 1.00 30.68 ?  394 TYR B CZ    1 
ATOM   8743  O  OH    . TYR B 1 394 ? 126.447 152.944 134.515 1.00 34.71 ?  394 TYR B OH    1 
ATOM   8744  N  N     . THR B 1 395 ? 124.219 154.465 126.260 1.00 31.26 ?  395 THR B N     1 
ATOM   8745  C  CA    . THR B 1 395 ? 123.869 154.522 124.854 1.00 30.91 ?  395 THR B CA    1 
ATOM   8746  C  C     . THR B 1 395 ? 125.029 154.016 124.001 1.00 32.44 ?  395 THR B C     1 
ATOM   8747  O  O     . THR B 1 395 ? 126.021 153.481 124.507 1.00 32.19 ?  395 THR B O     1 
ATOM   8748  C  CB    . THR B 1 395 ? 123.466 155.949 124.481 1.00 30.55 ?  395 THR B CB    1 
ATOM   8749  O  OG1   . THR B 1 395 ? 124.537 156.847 124.798 1.00 32.79 ?  395 THR B OG1   1 
ATOM   8750  C  CG2   . THR B 1 395 ? 122.223 156.366 125.250 1.00 30.29 ?  395 THR B CG2   1 
ATOM   8751  N  N     . ASP B 1 396 ? 124.906 154.181 122.688 1.00 33.29 ?  396 ASP B N     1 
ATOM   8752  C  CA    . ASP B 1 396 ? 125.949 153.754 121.771 1.00 31.68 ?  396 ASP B CA    1 
ATOM   8753  C  C     . ASP B 1 396 ? 127.197 154.614 121.941 1.00 34.49 ?  396 ASP B C     1 
ATOM   8754  O  O     . ASP B 1 396 ? 127.177 155.673 122.573 1.00 40.59 ?  396 ASP B O     1 
ATOM   8755  C  CB    . ASP B 1 396 ? 125.462 153.831 120.325 1.00 33.18 ?  396 ASP B CB    1 
ATOM   8756  C  CG    . ASP B 1 396 ? 124.322 152.876 120.038 1.00 36.09 ?  396 ASP B CG    1 
ATOM   8757  O  OD1   . ASP B 1 396 ? 124.179 151.878 120.774 1.00 39.61 ?  396 ASP B OD1   1 
ATOM   8758  O  OD2   . ASP B 1 396 ? 123.571 153.122 119.072 1.00 36.46 -1 396 ASP B OD2   1 
ATOM   8759  N  N     . TYR B 1 397 ? 128.299 154.136 121.371 1.00 32.92 ?  397 TYR B N     1 
ATOM   8760  C  CA    . TYR B 1 397 ? 129.521 154.924 121.349 1.00 32.88 ?  397 TYR B CA    1 
ATOM   8761  C  C     . TYR B 1 397 ? 129.298 156.206 120.555 1.00 38.23 ?  397 TYR B C     1 
ATOM   8762  O  O     . TYR B 1 397 ? 128.514 156.243 119.602 1.00 43.77 ?  397 TYR B O     1 
ATOM   8763  C  CB    . TYR B 1 397 ? 130.671 154.116 120.748 1.00 31.40 ?  397 TYR B CB    1 
ATOM   8764  C  CG    . TYR B 1 397 ? 132.039 154.582 121.188 1.00 31.29 ?  397 TYR B CG    1 
ATOM   8765  C  CD1   . TYR B 1 397 ? 132.683 155.623 120.534 1.00 34.49 ?  397 TYR B CD1   1 
ATOM   8766  C  CD2   . TYR B 1 397 ? 132.685 153.982 122.260 1.00 32.36 ?  397 TYR B CD2   1 
ATOM   8767  C  CE1   . TYR B 1 397 ? 133.932 156.052 120.933 1.00 33.49 ?  397 TYR B CE1   1 
ATOM   8768  C  CE2   . TYR B 1 397 ? 133.935 154.404 122.666 1.00 29.46 ?  397 TYR B CE2   1 
ATOM   8769  C  CZ    . TYR B 1 397 ? 134.553 155.439 121.999 1.00 31.74 ?  397 TYR B CZ    1 
ATOM   8770  O  OH    . TYR B 1 397 ? 135.798 155.864 122.399 1.00 35.13 ?  397 TYR B OH    1 
ATOM   8771  N  N     . ASP B 1 398 ? 129.983 157.270 120.976 1.00 35.77 ?  398 ASP B N     1 
ATOM   8772  C  CA    . ASP B 1 398 ? 129.842 158.628 120.455 1.00 40.56 ?  398 ASP B CA    1 
ATOM   8773  C  C     . ASP B 1 398 ? 128.495 159.246 120.800 1.00 41.34 ?  398 ASP B C     1 
ATOM   8774  O  O     . ASP B 1 398 ? 128.144 160.299 120.252 1.00 39.21 ?  398 ASP B O     1 
ATOM   8775  C  CB    . ASP B 1 398 ? 130.063 158.695 118.938 1.00 39.07 ?  398 ASP B CB    1 
ATOM   8776  C  CG    . ASP B 1 398 ? 131.415 159.270 118.571 1.00 44.22 ?  398 ASP B CG    1 
ATOM   8777  O  OD1   . ASP B 1 398 ? 131.594 159.674 117.402 1.00 42.46 ?  398 ASP B OD1   1 
ATOM   8778  O  OD2   . ASP B 1 398 ? 132.302 159.320 119.450 1.00 45.23 -1 398 ASP B OD2   1 
ATOM   8779  N  N     . GLU B 1 399 ? 127.730 158.625 121.693 1.00 44.70 ?  399 GLU B N     1 
ATOM   8780  C  CA    . GLU B 1 399 ? 126.473 159.168 122.184 1.00 41.11 ?  399 GLU B CA    1 
ATOM   8781  C  C     . GLU B 1 399 ? 126.566 159.345 123.692 1.00 44.21 ?  399 GLU B C     1 
ATOM   8782  O  O     . GLU B 1 399 ? 127.155 158.513 124.389 1.00 39.66 ?  399 GLU B O     1 
ATOM   8783  C  CB    . GLU B 1 399 ? 125.293 158.254 121.834 1.00 37.86 ?  399 GLU B CB    1 
ATOM   8784  C  CG    . GLU B 1 399 ? 125.044 158.104 120.343 1.00 43.97 ?  399 GLU B CG    1 
ATOM   8785  C  CD    . GLU B 1 399 ? 124.501 159.370 119.712 1.00 47.43 ?  399 GLU B CD    1 
ATOM   8786  O  OE1   . GLU B 1 399 ? 123.630 160.019 120.330 1.00 47.85 ?  399 GLU B OE1   1 
ATOM   8787  O  OE2   . GLU B 1 399 ? 124.944 159.718 118.597 1.00 46.53 -1 399 GLU B OE2   1 
ATOM   8788  N  N     . GLU B 1 400 ? 125.990 160.436 124.192 1.00 45.70 ?  400 GLU B N     1 
ATOM   8789  C  CA    . GLU B 1 400 ? 126.027 160.708 125.622 1.00 39.54 ?  400 GLU B CA    1 
ATOM   8790  C  C     . GLU B 1 400 ? 125.164 159.704 126.374 1.00 40.22 ?  400 GLU B C     1 
ATOM   8791  O  O     . GLU B 1 400 ? 124.042 159.397 125.959 1.00 39.36 ?  400 GLU B O     1 
ATOM   8792  C  CB    . GLU B 1 400 ? 125.551 162.131 125.904 1.00 40.02 ?  400 GLU B CB    1 
ATOM   8793  C  CG    . GLU B 1 400 ? 126.631 163.187 125.741 1.00 44.35 ?  400 GLU B CG    1 
ATOM   8794  C  CD    . GLU B 1 400 ? 127.893 162.853 126.510 1.00 47.31 ?  400 GLU B CD    1 
ATOM   8795  O  OE1   . GLU B 1 400 ? 127.820 162.736 127.751 1.00 46.59 ?  400 GLU B OE1   1 
ATOM   8796  O  OE2   . GLU B 1 400 ? 128.958 162.707 125.875 1.00 45.60 -1 400 GLU B OE2   1 
ATOM   8797  N  N     . ASP B 1 401 ? 125.692 159.190 127.481 1.00 35.64 ?  401 ASP B N     1 
ATOM   8798  C  CA    . ASP B 1 401 ? 124.965 158.249 128.320 1.00 31.88 ?  401 ASP B CA    1 
ATOM   8799  C  C     . ASP B 1 401 ? 124.196 158.993 129.402 1.00 32.92 ?  401 ASP B C     1 
ATOM   8800  O  O     . ASP B 1 401 ? 124.682 159.982 129.958 1.00 38.51 ?  401 ASP B O     1 
ATOM   8801  C  CB    . ASP B 1 401 ? 125.922 157.244 128.962 1.00 31.73 ?  401 ASP B CB    1 
ATOM   8802  C  CG    . ASP B 1 401 ? 126.751 156.492 127.943 1.00 36.42 ?  401 ASP B CG    1 
ATOM   8803  O  OD1   . ASP B 1 401 ? 126.345 156.439 126.763 1.00 38.79 ?  401 ASP B OD1   1 
ATOM   8804  O  OD2   . ASP B 1 401 ? 127.810 155.952 128.322 1.00 38.06 -1 401 ASP B OD2   1 
ATOM   8805  N  N     . GLU B 1 402 ? 122.990 158.513 129.695 1.00 29.52 ?  402 GLU B N     1 
ATOM   8806  C  CA    . GLU B 1 402 ? 122.190 159.042 130.798 1.00 27.64 ?  402 GLU B CA    1 
ATOM   8807  C  C     . GLU B 1 402 ? 122.580 158.274 132.053 1.00 29.15 ?  402 GLU B C     1 
ATOM   8808  O  O     . GLU B 1 402 ? 122.184 157.121 132.239 1.00 30.97 ?  402 GLU B O     1 
ATOM   8809  C  CB    . GLU B 1 402 ? 120.702 158.922 130.498 1.00 29.73 ?  402 GLU B CB    1 
ATOM   8810  C  CG    . GLU B 1 402 ? 120.206 159.864 129.414 1.00 33.82 ?  402 GLU B CG    1 
ATOM   8811  C  CD    . GLU B 1 402 ? 120.767 161.266 129.556 1.00 39.10 ?  402 GLU B CD    1 
ATOM   8812  O  OE1   . GLU B 1 402 ? 120.368 161.975 130.503 1.00 35.36 ?  402 GLU B OE1   1 
ATOM   8813  O  OE2   . GLU B 1 402 ? 121.609 161.658 128.721 1.00 36.60 -1 402 GLU B OE2   1 
ATOM   8814  N  N     . ILE B 1 403 ? 123.358 158.914 132.916 1.00 29.66 ?  403 ILE B N     1 
ATOM   8815  C  CA    . ILE B 1 403 ? 123.910 158.268 134.102 1.00 24.05 ?  403 ILE B CA    1 
ATOM   8816  C  C     . ILE B 1 403 ? 122.877 158.327 135.219 1.00 25.63 ?  403 ILE B C     1 
ATOM   8817  O  O     . ILE B 1 403 ? 122.415 159.409 135.595 1.00 30.61 ?  403 ILE B O     1 
ATOM   8818  C  CB    . ILE B 1 403 ? 125.227 158.929 134.530 1.00 21.38 ?  403 ILE B CB    1 
ATOM   8819  C  CG1   . ILE B 1 403 ? 126.303 158.709 133.465 1.00 23.71 ?  403 ILE B CG1   1 
ATOM   8820  C  CG2   . ILE B 1 403 ? 125.683 158.387 135.871 1.00 20.95 ?  403 ILE B CG2   1 
ATOM   8821  C  CD1   . ILE B 1 403 ? 126.468 157.266 133.053 1.00 27.98 ?  403 ILE B CD1   1 
ATOM   8822  N  N     . GLY B 1 404 ? 122.518 157.166 135.749 1.00 22.24 ?  404 GLY B N     1 
ATOM   8823  C  CA    . GLY B 1 404 ? 121.578 157.060 136.845 1.00 10.85 ?  404 GLY B CA    1 
ATOM   8824  C  C     . GLY B 1 404 ? 122.267 156.994 138.189 1.00 19.17 ?  404 GLY B C     1 
ATOM   8825  O  O     . GLY B 1 404 ? 123.346 157.558 138.393 1.00 26.62 ?  404 GLY B O     1 
ATOM   8826  N  N     . LEU B 1 405 ? 121.634 156.292 139.124 1.00 23.93 ?  405 LEU B N     1 
ATOM   8827  C  CA    . LEU B 1 405 ? 122.149 156.134 140.477 1.00 10.66 ?  405 LEU B CA    1 
ATOM   8828  C  C     . LEU B 1 405 ? 122.338 154.652 140.763 1.00 13.07 ?  405 LEU B C     1 
ATOM   8829  O  O     . LEU B 1 405 ? 121.367 153.889 140.762 1.00 14.56 ?  405 LEU B O     1 
ATOM   8830  C  CB    . LEU B 1 405 ? 121.203 156.763 141.501 1.00 17.18 ?  405 LEU B CB    1 
ATOM   8831  C  CG    . LEU B 1 405 ? 120.930 158.261 141.354 1.00 17.59 ?  405 LEU B CG    1 
ATOM   8832  C  CD1   . LEU B 1 405 ? 119.721 158.663 142.176 1.00 20.83 ?  405 LEU B CD1   1 
ATOM   8833  C  CD2   . LEU B 1 405 ? 122.146 159.077 141.754 1.00 16.71 ?  405 LEU B CD2   1 
ATOM   8834  N  N     . ASP B 1 406 ? 123.581 154.249 141.009 1.00 24.08 ?  406 ASP B N     1 
ATOM   8835  C  CA    . ASP B 1 406 ? 123.907 152.883 141.394 1.00 17.26 ?  406 ASP B CA    1 
ATOM   8836  C  C     . ASP B 1 406 ? 124.356 152.873 142.847 1.00 18.11 ?  406 ASP B C     1 
ATOM   8837  O  O     . ASP B 1 406 ? 125.288 153.591 143.220 1.00 27.75 ?  406 ASP B O     1 
ATOM   8838  C  CB    . ASP B 1 406 ? 124.997 152.298 140.496 1.00 17.89 ?  406 ASP B CB    1 
ATOM   8839  C  CG    . ASP B 1 406 ? 124.440 151.680 139.229 1.00 29.59 ?  406 ASP B CG    1 
ATOM   8840  O  OD1   . ASP B 1 406 ? 123.211 151.470 139.156 1.00 31.46 ?  406 ASP B OD1   1 
ATOM   8841  O  OD2   . ASP B 1 406 ? 125.232 151.400 138.306 1.00 31.03 -1 406 ASP B OD2   1 
ATOM   8842  N  N     . ILE B 1 407 ? 123.701 152.042 143.657 1.00 18.55 ?  407 ILE B N     1 
ATOM   8843  C  CA    . ILE B 1 407 ? 123.870 152.107 145.102 1.00 14.68 ?  407 ILE B CA    1 
ATOM   8844  C  C     . ILE B 1 407 ? 125.290 151.717 145.499 1.00 15.53 ?  407 ILE B C     1 
ATOM   8845  O  O     . ILE B 1 407 ? 125.909 150.817 144.914 1.00 21.25 ?  407 ILE B O     1 
ATOM   8846  C  CB    . ILE B 1 407 ? 122.833 151.207 145.797 1.00 15.58 ?  407 ILE B CB    1 
ATOM   8847  C  CG1   . ILE B 1 407 ? 121.417 151.584 145.365 1.00 3.84  ?  407 ILE B CG1   1 
ATOM   8848  C  CG2   . ILE B 1 407 ? 122.968 151.298 147.293 1.00 13.32 ?  407 ILE B CG2   1 
ATOM   8849  C  CD1   . ILE B 1 407 ? 120.464 150.420 145.377 1.00 11.74 ?  407 ILE B CD1   1 
ATOM   8850  N  N     . SER B 1 408 ? 125.812 152.413 146.507 1.00 26.34 ?  408 SER B N     1 
ATOM   8851  C  CA    . SER B 1 408 ? 127.105 152.105 147.104 1.00 23.56 ?  408 SER B CA    1 
ATOM   8852  C  C     . SER B 1 408 ? 127.171 152.801 148.453 1.00 27.78 ?  408 SER B C     1 
ATOM   8853  O  O     . SER B 1 408 ? 126.947 154.012 148.534 1.00 38.28 ?  408 SER B O     1 
ATOM   8854  C  CB    . SER B 1 408 ? 128.256 152.565 146.203 1.00 29.16 ?  408 SER B CB    1 
ATOM   8855  O  OG    . SER B 1 408 ? 129.375 152.967 146.970 1.00 27.58 ?  408 SER B OG    1 
ATOM   8856  N  N     . CYS B 1 409 ? 127.461 152.042 149.507 1.00 23.83 ?  409 CYS B N     1 
ATOM   8857  C  CA    . CYS B 1 409 ? 127.572 152.603 150.844 1.00 30.39 ?  409 CYS B CA    1 
ATOM   8858  C  C     . CYS B 1 409 ? 128.793 152.027 151.547 1.00 28.90 ?  409 CYS B C     1 
ATOM   8859  O  O     . CYS B 1 409 ? 129.269 150.935 151.224 1.00 26.96 ?  409 CYS B O     1 
ATOM   8860  C  CB    . CYS B 1 409 ? 126.309 152.346 151.681 1.00 25.10 ?  409 CYS B CB    1 
ATOM   8861  S  SG    . CYS B 1 409 ? 126.146 150.669 152.324 1.00 45.46 ?  409 CYS B SG    1 
ATOM   8862  N  N     . ASN B 1 410 ? 129.294 152.786 152.515 1.00 22.93 ?  410 ASN B N     1 
ATOM   8863  C  CA    . ASN B 1 410 ? 130.460 152.405 153.300 1.00 20.91 ?  410 ASN B CA    1 
ATOM   8864  C  C     . ASN B 1 410 ? 129.999 151.770 154.602 1.00 25.91 ?  410 ASN B C     1 
ATOM   8865  O  O     . ASN B 1 410 ? 129.098 152.291 155.267 1.00 28.35 ?  410 ASN B O     1 
ATOM   8866  C  CB    . ASN B 1 410 ? 131.341 153.620 153.584 1.00 24.20 ?  410 ASN B CB    1 
ATOM   8867  C  CG    . ASN B 1 410 ? 131.222 154.678 152.514 1.00 32.33 ?  410 ASN B CG    1 
ATOM   8868  O  OD1   . ASN B 1 410 ? 130.674 155.752 152.751 1.00 34.43 ?  410 ASN B OD1   1 
ATOM   8869  N  ND2   . ASN B 1 410 ? 131.732 154.379 151.325 1.00 34.92 ?  410 ASN B ND2   1 
ATOM   8870  N  N     . LEU B 1 411 ? 130.615 150.653 154.961 1.00 19.65 ?  411 LEU B N     1 
ATOM   8871  C  CA    . LEU B 1 411 ? 130.202 149.873 156.116 1.00 10.94 ?  411 LEU B CA    1 
ATOM   8872  C  C     . LEU B 1 411 ? 131.054 150.212 157.332 1.00 11.69 ?  411 LEU B C     1 
ATOM   8873  O  O     . LEU B 1 411 ? 132.244 150.516 157.221 1.00 22.88 ?  411 LEU B O     1 
ATOM   8874  C  CB    . LEU B 1 411 ? 130.294 148.375 155.822 1.00 19.20 ?  411 LEU B CB    1 
ATOM   8875  C  CG    . LEU B 1 411 ? 129.125 147.674 155.129 1.00 17.67 ?  411 LEU B CG    1 
ATOM   8876  C  CD1   . LEU B 1 411 ? 128.934 148.170 153.708 1.00 18.06 ?  411 LEU B CD1   1 
ATOM   8877  C  CD2   . LEU B 1 411 ? 129.356 146.175 155.140 1.00 23.52 ?  411 LEU B CD2   1 
ATOM   8878  N  N     . GLY B 1 412 ? 130.420 150.165 158.497 1.00 17.26 ?  412 GLY B N     1 
ATOM   8879  C  CA    . GLY B 1 412 ? 131.094 150.332 159.768 1.00 11.56 ?  412 GLY B CA    1 
ATOM   8880  C  C     . GLY B 1 412 ? 130.206 149.816 160.878 1.00 10.58 ?  412 GLY B C     1 
ATOM   8881  O  O     . GLY B 1 412 ? 129.005 150.091 160.878 1.00 27.55 ?  412 GLY B O     1 
ATOM   8882  N  N     . SER B 1 413 ? 130.763 149.063 161.820 1.00 11.05 ?  413 SER B N     1 
ATOM   8883  C  CA    . SER B 1 413 ? 129.960 148.380 162.823 1.00 11.98 ?  413 SER B CA    1 
ATOM   8884  C  C     . SER B 1 413 ? 130.277 148.889 164.220 1.00 19.09 ?  413 SER B C     1 
ATOM   8885  O  O     . SER B 1 413 ? 131.444 149.046 164.588 1.00 20.96 ?  413 SER B O     1 
ATOM   8886  C  CB    . SER B 1 413 ? 130.189 146.869 162.765 1.00 13.26 ?  413 SER B CB    1 
ATOM   8887  O  OG    . SER B 1 413 ? 129.700 146.334 161.549 1.00 31.25 ?  413 SER B OG    1 
ATOM   8888  N  N     . LEU B 1 414 ? 129.232 149.132 165.000 1.00 20.36 ?  414 LEU B N     1 
ATOM   8889  C  CA    . LEU B 1 414 ? 129.385 149.404 166.418 1.00 13.08 ?  414 LEU B CA    1 
ATOM   8890  C  C     . LEU B 1 414 ? 129.501 148.089 167.173 1.00 21.50 ?  414 LEU B C     1 
ATOM   8891  O  O     . LEU B 1 414 ? 128.744 147.149 166.924 1.00 25.61 ?  414 LEU B O     1 
ATOM   8892  C  CB    . LEU B 1 414 ? 128.196 150.203 166.953 1.00 22.88 ?  414 LEU B CB    1 
ATOM   8893  C  CG    . LEU B 1 414 ? 127.768 151.446 166.179 1.00 21.75 ?  414 LEU B CG    1 
ATOM   8894  C  CD1   . LEU B 1 414 ? 126.498 152.009 166.779 1.00 22.36 ?  414 LEU B CD1   1 
ATOM   8895  C  CD2   . LEU B 1 414 ? 128.873 152.486 166.190 1.00 24.62 ?  414 LEU B CD2   1 
ATOM   8896  N  N     . ASN B 1 415 ? 130.459 148.025 168.090 1.00 29.80 ?  415 ASN B N     1 
ATOM   8897  C  CA    . ASN B 1 415 ? 130.561 146.889 168.997 1.00 27.12 ?  415 ASN B CA    1 
ATOM   8898  C  C     . ASN B 1 415 ? 129.645 147.162 170.181 1.00 25.14 ?  415 ASN B C     1 
ATOM   8899  O  O     . ASN B 1 415 ? 129.956 147.998 171.035 1.00 29.23 ?  415 ASN B O     1 
ATOM   8900  C  CB    . ASN B 1 415 ? 132.006 146.681 169.437 1.00 22.71 ?  415 ASN B CB    1 
ATOM   8901  C  CG    . ASN B 1 415 ? 132.237 145.327 170.074 1.00 28.99 ?  415 ASN B CG    1 
ATOM   8902  O  OD1   . ASN B 1 415 ? 131.439 144.862 170.885 1.00 34.87 ?  415 ASN B OD1   1 
ATOM   8903  N  ND2   . ASN B 1 415 ? 133.340 144.685 169.708 1.00 29.53 ?  415 ASN B ND2   1 
ATOM   8904  N  N     . ILE B 1 416 ? 128.513 146.456 170.230 1.00 20.40 ?  416 ILE B N     1 
ATOM   8905  C  CA    . ILE B 1 416 ? 127.468 146.776 171.200 1.00 23.03 ?  416 ILE B CA    1 
ATOM   8906  C  C     . ILE B 1 416 ? 127.984 146.615 172.624 1.00 30.00 ?  416 ILE B C     1 
ATOM   8907  O  O     . ILE B 1 416 ? 127.714 147.452 173.494 1.00 30.28 ?  416 ILE B O     1 
ATOM   8908  C  CB    . ILE B 1 416 ? 126.223 145.910 170.938 1.00 22.35 ?  416 ILE B CB    1 
ATOM   8909  C  CG1   . ILE B 1 416 ? 125.566 146.326 169.620 1.00 22.82 ?  416 ILE B CG1   1 
ATOM   8910  C  CG2   . ILE B 1 416 ? 125.233 146.032 172.079 1.00 17.29 ?  416 ILE B CG2   1 
ATOM   8911  C  CD1   . ILE B 1 416 ? 124.419 145.443 169.193 1.00 21.61 ?  416 ILE B CD1   1 
ATOM   8912  N  N     . LEU B 1 417 ? 128.742 145.548 172.883 1.00 24.98 ?  417 LEU B N     1 
ATOM   8913  C  CA    . LEU B 1 417 ? 129.271 145.325 174.225 1.00 27.55 ?  417 LEU B CA    1 
ATOM   8914  C  C     . LEU B 1 417 ? 130.203 146.453 174.646 1.00 28.75 ?  417 LEU B C     1 
ATOM   8915  O  O     . LEU B 1 417 ? 130.086 146.990 175.754 1.00 34.00 ?  417 LEU B O     1 
ATOM   8916  C  CB    . LEU B 1 417 ? 129.995 143.980 174.285 1.00 28.61 ?  417 LEU B CB    1 
ATOM   8917  C  CG    . LEU B 1 417 ? 130.532 143.578 175.658 1.00 29.91 ?  417 LEU B CG    1 
ATOM   8918  C  CD1   . LEU B 1 417 ? 129.897 142.281 176.113 1.00 27.31 ?  417 LEU B CD1   1 
ATOM   8919  C  CD2   . LEU B 1 417 ? 132.045 143.453 175.624 1.00 32.64 ?  417 LEU B CD2   1 
ATOM   8920  N  N     . ASN B 1 418 ? 131.131 146.836 173.768 1.00 34.08 ?  418 ASN B N     1 
ATOM   8921  C  CA    . ASN B 1 418 ? 132.079 147.888 174.112 1.00 29.41 ?  418 ASN B CA    1 
ATOM   8922  C  C     . ASN B 1 418 ? 131.417 149.259 174.141 1.00 29.20 ?  418 ASN B C     1 
ATOM   8923  O  O     . ASN B 1 418 ? 131.785 150.106 174.962 1.00 35.03 ?  418 ASN B O     1 
ATOM   8924  C  CB    . ASN B 1 418 ? 133.250 147.878 173.132 1.00 27.06 ?  418 ASN B CB    1 
ATOM   8925  C  CG    . ASN B 1 418 ? 134.116 146.645 173.278 1.00 28.65 ?  418 ASN B CG    1 
ATOM   8926  O  OD1   . ASN B 1 418 ? 134.371 146.183 174.389 1.00 36.71 ?  418 ASN B OD1   1 
ATOM   8927  N  ND2   . ASN B 1 418 ? 134.569 146.102 172.156 1.00 30.28 ?  418 ASN B ND2   1 
ATOM   8928  N  N     . VAL B 1 419 ? 130.448 149.498 173.254 1.00 31.16 ?  419 VAL B N     1 
ATOM   8929  C  CA    . VAL B 1 419 ? 129.747 150.778 173.245 1.00 31.46 ?  419 VAL B CA    1 
ATOM   8930  C  C     . VAL B 1 419 ? 128.945 150.960 174.528 1.00 29.36 ?  419 VAL B C     1 
ATOM   8931  O  O     . VAL B 1 419 ? 128.971 152.029 175.148 1.00 36.08 ?  419 VAL B O     1 
ATOM   8932  C  CB    . VAL B 1 419 ? 128.856 150.890 171.994 1.00 26.47 ?  419 VAL B CB    1 
ATOM   8933  C  CG1   . VAL B 1 419 ? 127.815 151.969 172.178 1.00 28.15 ?  419 VAL B CG1   1 
ATOM   8934  C  CG2   . VAL B 1 419 ? 129.701 151.185 170.772 1.00 25.84 ?  419 VAL B CG2   1 
ATOM   8935  N  N     . MET B 1 420 ? 128.226 149.918 174.953 1.00 31.99 ?  420 MET B N     1 
ATOM   8936  C  CA    . MET B 1 420 ? 127.412 150.037 176.157 1.00 34.66 ?  420 MET B CA    1 
ATOM   8937  C  C     . MET B 1 420 ? 128.247 149.979 177.429 1.00 33.26 ?  420 MET B C     1 
ATOM   8938  O  O     . MET B 1 420 ? 127.869 150.587 178.437 1.00 35.93 ?  420 MET B O     1 
ATOM   8939  C  CB    . MET B 1 420 ? 126.334 148.953 176.182 1.00 32.45 ?  420 MET B CB    1 
ATOM   8940  C  CG    . MET B 1 420 ? 125.332 149.068 175.049 1.00 30.51 ?  420 MET B CG    1 
ATOM   8941  S  SD    . MET B 1 420 ? 123.809 149.888 175.551 1.00 43.53 ?  420 MET B SD    1 
ATOM   8942  C  CE    . MET B 1 420 ? 123.520 149.149 177.154 1.00 31.04 ?  420 MET B CE    1 
ATOM   8943  N  N     . GLU B 1 421 ? 129.370 149.258 177.411 1.00 37.77 ?  421 GLU B N     1 
ATOM   8944  C  CA    . GLU B 1 421 ? 130.262 149.256 178.567 1.00 34.78 ?  421 GLU B CA    1 
ATOM   8945  C  C     . GLU B 1 421 ? 130.843 150.642 178.808 1.00 38.51 ?  421 GLU B C     1 
ATOM   8946  O  O     . GLU B 1 421 ? 130.965 151.084 179.956 1.00 41.72 ?  421 GLU B O     1 
ATOM   8947  C  CB    . GLU B 1 421 ? 131.374 148.227 178.366 1.00 34.46 ?  421 GLU B CB    1 
ATOM   8948  C  CG    . GLU B 1 421 ? 132.589 148.435 179.254 1.00 42.35 ?  421 GLU B CG    1 
ATOM   8949  C  CD    . GLU B 1 421 ? 133.892 148.256 178.503 1.00 44.83 ?  421 GLU B CD    1 
ATOM   8950  O  OE1   . GLU B 1 421 ? 133.845 147.946 177.293 1.00 43.17 ?  421 GLU B OE1   1 
ATOM   8951  O  OE2   . GLU B 1 421 ? 134.965 148.427 179.120 1.00 41.27 -1 421 GLU B OE2   1 
ATOM   8952  N  N     . HIS B 1 422 ? 131.196 151.348 177.736 1.00 34.24 ?  422 HIS B N     1 
ATOM   8953  C  CA    . HIS B 1 422 ? 131.710 152.707 177.839 1.00 35.44 ?  422 HIS B CA    1 
ATOM   8954  C  C     . HIS B 1 422 ? 130.607 153.748 177.965 1.00 38.64 ?  422 HIS B C     1 
ATOM   8955  O  O     . HIS B 1 422 ? 130.919 154.931 178.141 1.00 41.12 ?  422 HIS B O     1 
ATOM   8956  C  CB    . HIS B 1 422 ? 132.586 153.027 176.625 1.00 32.69 ?  422 HIS B CB    1 
ATOM   8957  C  CG    . HIS B 1 422 ? 133.867 152.253 176.583 1.00 35.81 ?  422 HIS B CG    1 
ATOM   8958  N  ND1   . HIS B 1 422 ? 133.967 151.015 175.986 1.00 36.57 ?  422 HIS B ND1   1 
ATOM   8959  C  CD2   . HIS B 1 422 ? 135.098 152.539 177.066 1.00 37.01 ?  422 HIS B CD2   1 
ATOM   8960  C  CE1   . HIS B 1 422 ? 135.206 150.572 176.103 1.00 39.80 ?  422 HIS B CE1   1 
ATOM   8961  N  NE2   . HIS B 1 422 ? 135.912 151.478 176.754 1.00 39.81 ?  422 HIS B NE2   1 
ATOM   8962  N  N     . LYS B 1 423 ? 129.338 153.339 177.885 1.00 40.97 ?  423 LYS B N     1 
ATOM   8963  C  CA    . LYS B 1 423 ? 128.198 154.252 177.992 1.00 42.37 ?  423 LYS B CA    1 
ATOM   8964  C  C     . LYS B 1 423 ? 128.319 155.399 176.992 1.00 43.69 ?  423 LYS B C     1 
ATOM   8965  O  O     . LYS B 1 423 ? 128.087 156.565 177.317 1.00 46.33 ?  423 LYS B O     1 
ATOM   8966  C  CB    . LYS B 1 423 ? 128.056 154.786 179.418 1.00 40.41 ?  423 LYS B CB    1 
ATOM   8967  C  CG    . LYS B 1 423 ? 127.454 153.794 180.397 1.00 42.43 ?  423 LYS B CG    1 
ATOM   8968  C  CD    . LYS B 1 423 ? 127.521 154.319 181.821 1.00 43.32 ?  423 LYS B CD    1 
ATOM   8969  C  CE    . LYS B 1 423 ? 128.623 153.630 182.612 1.00 45.85 ?  423 LYS B CE    1 
ATOM   8970  N  NZ    . LYS B 1 423 ? 128.087 152.887 183.786 1.00 43.92 1  423 LYS B NZ    1 
ATOM   8971  N  N     . SER B 1 424 ? 128.684 155.061 175.759 1.00 31.73 ?  424 SER B N     1 
ATOM   8972  C  CA    . SER B 1 424 ? 129.031 156.047 174.743 1.00 33.97 ?  424 SER B CA    1 
ATOM   8973  C  C     . SER B 1 424 ? 128.333 155.741 173.427 1.00 34.09 ?  424 SER B C     1 
ATOM   8974  O  O     . SER B 1 424 ? 128.951 155.718 172.362 1.00 32.55 ?  424 SER B O     1 
ATOM   8975  C  CB    . SER B 1 424 ? 130.541 156.097 174.542 1.00 35.65 ?  424 SER B CB    1 
ATOM   8976  O  OG    . SER B 1 424 ? 131.001 154.918 173.905 1.00 32.02 ?  424 SER B OG    1 
ATOM   8977  N  N     . ILE B 1 425 ? 127.023 155.493 173.481 1.00 33.46 ?  425 ILE B N     1 
ATOM   8978  C  CA    . ILE B 1 425 ? 126.264 155.296 172.248 1.00 26.93 ?  425 ILE B CA    1 
ATOM   8979  C  C     . ILE B 1 425 ? 126.336 156.546 171.381 1.00 32.03 ?  425 ILE B C     1 
ATOM   8980  O  O     . ILE B 1 425 ? 126.627 156.477 170.182 1.00 35.69 ?  425 ILE B O     1 
ATOM   8981  C  CB    . ILE B 1 425 ? 124.805 154.915 172.562 1.00 32.10 ?  425 ILE B CB    1 
ATOM   8982  C  CG1   . ILE B 1 425 ? 124.711 153.462 173.023 1.00 32.37 ?  425 ILE B CG1   1 
ATOM   8983  C  CG2   . ILE B 1 425 ? 123.923 155.128 171.342 1.00 27.48 ?  425 ILE B CG2   1 
ATOM   8984  C  CD1   . ILE B 1 425 ? 123.328 153.065 173.485 1.00 33.35 ?  425 ILE B CD1   1 
ATOM   8985  N  N     . GLU B 1 426 ? 126.099 157.712 171.986 1.00 27.69 ?  426 GLU B N     1 
ATOM   8986  C  CA    . GLU B 1 426 ? 126.058 158.954 171.222 1.00 23.51 ?  426 GLU B CA    1 
ATOM   8987  C  C     . GLU B 1 426 ? 127.405 159.259 170.581 1.00 26.23 ?  426 GLU B C     1 
ATOM   8988  O  O     . GLU B 1 426 ? 127.490 159.492 169.369 1.00 34.59 ?  426 GLU B O     1 
ATOM   8989  C  CB    . GLU B 1 426 ? 125.622 160.106 172.126 1.00 26.59 ?  426 GLU B CB    1 
ATOM   8990  C  CG    . GLU B 1 426 ? 125.916 161.481 171.556 1.00 29.01 ?  426 GLU B CG    1 
ATOM   8991  C  CD    . GLU B 1 426 ? 125.450 162.600 172.464 1.00 33.93 ?  426 GLU B CD    1 
ATOM   8992  O  OE1   . GLU B 1 426 ? 125.032 162.310 173.603 1.00 33.66 ?  426 GLU B OE1   1 
ATOM   8993  O  OE2   . GLU B 1 426 ? 125.503 163.773 172.037 1.00 36.80 -1 426 GLU B OE2   1 
ATOM   8994  N  N     . LYS B 1 427 ? 128.473 159.263 171.382 1.00 33.18 ?  427 LYS B N     1 
ATOM   8995  C  CA    . LYS B 1 427 ? 129.786 159.630 170.862 1.00 27.99 ?  427 LYS B CA    1 
ATOM   8996  C  C     . LYS B 1 427 ? 130.257 158.642 169.803 1.00 28.32 ?  427 LYS B C     1 
ATOM   8997  O  O     . LYS B 1 427 ? 130.772 159.045 168.753 1.00 32.78 ?  427 LYS B O     1 
ATOM   8998  C  CB    . LYS B 1 427 ? 130.795 159.721 172.005 1.00 28.87 ?  427 LYS B CB    1 
ATOM   8999  C  CG    . LYS B 1 427 ? 132.242 159.821 171.553 1.00 32.24 ?  427 LYS B CG    1 
ATOM   9000  C  CD    . LYS B 1 427 ? 133.201 159.722 172.727 1.00 33.02 ?  427 LYS B CD    1 
ATOM   9001  C  CE    . LYS B 1 427 ? 133.111 158.368 173.411 1.00 31.84 ?  427 LYS B CE    1 
ATOM   9002  N  NZ    . LYS B 1 427 ? 133.026 157.249 172.433 1.00 33.99 1  427 LYS B NZ    1 
ATOM   9003  N  N     . THR B 1 428 ? 130.078 157.344 170.057 1.00 30.09 ?  428 THR B N     1 
ATOM   9004  C  CA    . THR B 1 428 ? 130.498 156.340 169.088 1.00 24.75 ?  428 THR B CA    1 
ATOM   9005  C  C     . THR B 1 428 ? 129.710 156.462 167.792 1.00 24.98 ?  428 THR B C     1 
ATOM   9006  O  O     . THR B 1 428 ? 130.286 156.377 166.703 1.00 32.34 ?  428 THR B O     1 
ATOM   9007  C  CB    . THR B 1 428 ? 130.343 154.937 169.671 1.00 24.64 ?  428 THR B CB    1 
ATOM   9008  O  OG1   . THR B 1 428 ? 130.926 154.895 170.979 1.00 26.31 ?  428 THR B OG1   1 
ATOM   9009  C  CG2   . THR B 1 428 ? 131.035 153.920 168.782 1.00 25.22 ?  428 THR B CG2   1 
ATOM   9010  N  N     . VAL B 1 429 ? 128.394 156.667 167.888 1.00 23.05 ?  429 VAL B N     1 
ATOM   9011  C  CA    . VAL B 1 429 ? 127.578 156.783 166.684 1.00 22.40 ?  429 VAL B CA    1 
ATOM   9012  C  C     . VAL B 1 429 ? 127.991 158.003 165.873 1.00 27.00 ?  429 VAL B C     1 
ATOM   9013  O  O     . VAL B 1 429 ? 128.140 157.927 164.648 1.00 28.05 ?  429 VAL B O     1 
ATOM   9014  C  CB    . VAL B 1 429 ? 126.081 156.821 167.047 1.00 25.19 ?  429 VAL B CB    1 
ATOM   9015  C  CG1   . VAL B 1 429 ? 125.271 157.351 165.882 1.00 22.74 ?  429 VAL B CG1   1 
ATOM   9016  C  CG2   . VAL B 1 429 ? 125.594 155.437 167.423 1.00 26.03 ?  429 VAL B CG2   1 
ATOM   9017  N  N     . LYS B 1 430 ? 128.191 159.145 166.537 1.00 25.79 ?  430 LYS B N     1 
ATOM   9018  C  CA    . LYS B 1 430 ? 128.563 160.355 165.806 1.00 20.82 ?  430 LYS B CA    1 
ATOM   9019  C  C     . LYS B 1 430 ? 129.941 160.224 165.166 1.00 23.73 ?  430 LYS B C     1 
ATOM   9020  O  O     . LYS B 1 430 ? 130.132 160.619 164.009 1.00 30.67 ?  430 LYS B O     1 
ATOM   9021  C  CB    . LYS B 1 430 ? 128.509 161.571 166.732 1.00 23.66 ?  430 LYS B CB    1 
ATOM   9022  C  CG    . LYS B 1 430 ? 127.166 161.765 167.415 1.00 25.85 ?  430 LYS B CG    1 
ATOM   9023  C  CD    . LYS B 1 430 ? 126.542 163.105 167.088 1.00 27.12 ?  430 LYS B CD    1 
ATOM   9024  C  CE    . LYS B 1 430 ? 125.371 163.395 168.010 1.00 29.17 ?  430 LYS B CE    1 
ATOM   9025  N  NZ    . LYS B 1 430 ? 124.952 164.820 167.949 1.00 32.65 1  430 LYS B NZ    1 
ATOM   9026  N  N     . LEU B 1 431 ? 130.911 159.664 165.892 1.00 25.57 ?  431 LEU B N     1 
ATOM   9027  C  CA    . LEU B 1 431 ? 132.246 159.500 165.325 1.00 21.63 ?  431 LEU B CA    1 
ATOM   9028  C  C     . LEU B 1 431 ? 132.243 158.501 164.174 1.00 24.56 ?  431 LEU B C     1 
ATOM   9029  O  O     . LEU B 1 431 ? 132.938 158.701 163.170 1.00 28.94 ?  431 LEU B O     1 
ATOM   9030  C  CB    . LEU B 1 431 ? 133.226 159.070 166.412 1.00 26.72 ?  431 LEU B CB    1 
ATOM   9031  C  CG    . LEU B 1 431 ? 133.957 160.194 167.146 1.00 29.74 ?  431 LEU B CG    1 
ATOM   9032  C  CD1   . LEU B 1 431 ? 134.753 159.635 168.310 1.00 27.85 ?  431 LEU B CD1   1 
ATOM   9033  C  CD2   . LEU B 1 431 ? 134.858 160.958 166.191 1.00 28.68 ?  431 LEU B CD2   1 
ATOM   9034  N  N     . ALA B 1 432 ? 131.470 157.419 164.298 1.00 26.78 ?  432 ALA B N     1 
ATOM   9035  C  CA    . ALA B 1 432 ? 131.360 156.456 163.209 1.00 15.82 ?  432 ALA B CA    1 
ATOM   9036  C  C     . ALA B 1 432 ? 130.693 157.077 161.991 1.00 25.44 ?  432 ALA B C     1 
ATOM   9037  O  O     . ALA B 1 432 ? 131.092 156.808 160.852 1.00 27.92 ?  432 ALA B O     1 
ATOM   9038  C  CB    . ALA B 1 432 ? 130.584 155.227 163.677 1.00 17.76 ?  432 ALA B CB    1 
ATOM   9039  N  N     . THR B 1 433 ? 129.670 157.906 162.210 1.00 25.72 ?  433 THR B N     1 
ATOM   9040  C  CA    . THR B 1 433 ? 129.035 158.606 161.101 1.00 19.97 ?  433 THR B CA    1 
ATOM   9041  C  C     . THR B 1 433 ? 130.020 159.538 160.410 1.00 23.21 ?  433 THR B C     1 
ATOM   9042  O  O     . THR B 1 433 ? 130.048 159.620 159.179 1.00 32.64 ?  433 THR B O     1 
ATOM   9043  C  CB    . THR B 1 433 ? 127.817 159.384 161.602 1.00 22.90 ?  433 THR B CB    1 
ATOM   9044  O  OG1   . THR B 1 433 ? 126.910 158.485 162.252 1.00 31.80 ?  433 THR B OG1   1 
ATOM   9045  C  CG2   . THR B 1 433 ? 127.101 160.067 160.446 1.00 22.05 ?  433 THR B CG2   1 
ATOM   9046  N  N     . ASP B 1 434 ? 130.843 160.242 161.190 1.00 23.10 ?  434 ASP B N     1 
ATOM   9047  C  CA    . ASP B 1 434 ? 131.858 161.110 160.598 1.00 23.64 ?  434 ASP B CA    1 
ATOM   9048  C  C     . ASP B 1 434 ? 132.877 160.311 159.794 1.00 20.53 ?  434 ASP B C     1 
ATOM   9049  O  O     . ASP B 1 434 ? 133.273 160.720 158.696 1.00 25.07 ?  434 ASP B O     1 
ATOM   9050  C  CB    . ASP B 1 434 ? 132.553 161.922 161.689 1.00 26.42 ?  434 ASP B CB    1 
ATOM   9051  C  CG    . ASP B 1 434 ? 131.629 162.919 162.349 1.00 32.91 ?  434 ASP B CG    1 
ATOM   9052  O  OD1   . ASP B 1 434 ? 130.755 163.470 161.648 1.00 34.35 ?  434 ASP B OD1   1 
ATOM   9053  O  OD2   . ASP B 1 434 ? 131.773 163.151 163.567 1.00 33.39 -1 434 ASP B OD2   1 
ATOM   9054  N  N     . SER B 1 435 ? 133.316 159.168 160.326 1.00 23.60 ?  435 SER B N     1 
ATOM   9055  C  CA    . SER B 1 435 ? 134.280 158.339 159.609 1.00 18.43 ?  435 SER B CA    1 
ATOM   9056  C  C     . SER B 1 435 ? 133.692 157.794 158.312 1.00 22.69 ?  435 SER B C     1 
ATOM   9057  O  O     . SER B 1 435 ? 134.369 157.771 157.276 1.00 32.06 ?  435 SER B O     1 
ATOM   9058  C  CB    . SER B 1 435 ? 134.756 157.196 160.503 1.00 22.49 ?  435 SER B CB    1 
ATOM   9059  O  OG    . SER B 1 435 ? 133.748 156.214 160.656 1.00 23.75 ?  435 SER B OG    1 
ATOM   9060  N  N     . LEU B 1 436 ? 132.433 157.357 158.345 1.00 21.95 ?  436 LEU B N     1 
ATOM   9061  C  CA    . LEU B 1 436 ? 131.793 156.852 157.134 1.00 13.09 ?  436 LEU B CA    1 
ATOM   9062  C  C     . LEU B 1 436 ? 131.568 157.968 156.122 1.00 18.56 ?  436 LEU B C     1 
ATOM   9063  O  O     . LEU B 1 436 ? 131.687 157.751 154.911 1.00 23.01 ?  436 LEU B O     1 
ATOM   9064  C  CB    . LEU B 1 436 ? 130.476 156.163 157.488 1.00 22.43 ?  436 LEU B CB    1 
ATOM   9065  C  CG    . LEU B 1 436 ? 130.599 154.890 158.328 1.00 21.08 ?  436 LEU B CG    1 
ATOM   9066  C  CD1   . LEU B 1 436 ? 129.261 154.513 158.939 1.00 18.38 ?  436 LEU B CD1   1 
ATOM   9067  C  CD2   . LEU B 1 436 ? 131.152 153.750 157.494 1.00 18.57 ?  436 LEU B CD2   1 
ATOM   9068  N  N     . THR B 1 437 ? 131.246 159.171 156.602 1.00 21.16 ?  437 THR B N     1 
ATOM   9069  C  CA    . THR B 1 437 ? 131.132 160.319 155.710 1.00 20.15 ?  437 THR B CA    1 
ATOM   9070  C  C     . THR B 1 437 ? 132.466 160.625 155.044 1.00 22.83 ?  437 THR B C     1 
ATOM   9071  O  O     . THR B 1 437 ? 132.517 160.926 153.846 1.00 29.74 ?  437 THR B O     1 
ATOM   9072  C  CB    . THR B 1 437 ? 130.632 161.536 156.488 1.00 20.41 ?  437 THR B CB    1 
ATOM   9073  O  OG1   . THR B 1 437 ? 129.426 161.197 157.182 1.00 23.40 ?  437 THR B OG1   1 
ATOM   9074  C  CG2   . THR B 1 437 ? 130.362 162.695 155.551 1.00 20.77 ?  437 THR B CG2   1 
ATOM   9075  N  N     . HIS B 1 438 ? 133.558 160.549 155.805 1.00 21.30 ?  438 HIS B N     1 
ATOM   9076  C  CA    . HIS B 1 438 ? 134.881 160.750 155.222 1.00 21.63 ?  438 HIS B CA    1 
ATOM   9077  C  C     . HIS B 1 438 ? 135.191 159.683 154.181 1.00 23.01 ?  438 HIS B C     1 
ATOM   9078  O  O     . HIS B 1 438 ? 135.727 159.988 153.107 1.00 32.46 ?  438 HIS B O     1 
ATOM   9079  C  CB    . HIS B 1 438 ? 135.943 160.753 156.321 1.00 26.49 ?  438 HIS B CB    1 
ATOM   9080  C  CG    . HIS B 1 438 ? 137.344 160.850 155.803 1.00 27.67 ?  438 HIS B CG    1 
ATOM   9081  N  ND1   . HIS B 1 438 ? 137.914 162.045 155.422 1.00 25.54 ?  438 HIS B ND1   1 
ATOM   9082  C  CD2   . HIS B 1 438 ? 138.285 159.900 155.594 1.00 28.00 ?  438 HIS B CD2   1 
ATOM   9083  C  CE1   . HIS B 1 438 ? 139.150 161.828 155.007 1.00 30.66 ?  438 HIS B CE1   1 
ATOM   9084  N  NE2   . HIS B 1 438 ? 139.399 160.534 155.100 1.00 31.16 ?  438 HIS B NE2   1 
ATOM   9085  N  N     . VAL B 1 439 ? 134.861 158.424 154.479 1.00 21.40 ?  439 VAL B N     1 
ATOM   9086  C  CA    . VAL B 1 439 ? 135.119 157.342 153.530 1.00 19.11 ?  439 VAL B CA    1 
ATOM   9087  C  C     . VAL B 1 439 ? 134.333 157.564 152.245 1.00 28.84 ?  439 VAL B C     1 
ATOM   9088  O  O     . VAL B 1 439 ? 134.843 157.343 151.140 1.00 32.53 ?  439 VAL B O     1 
ATOM   9089  C  CB    . VAL B 1 439 ? 134.793 155.979 154.167 1.00 23.77 ?  439 VAL B CB    1 
ATOM   9090  C  CG1   . VAL B 1 439 ? 134.830 154.876 153.119 1.00 20.70 ?  439 VAL B CG1   1 
ATOM   9091  C  CG2   . VAL B 1 439 ? 135.768 155.676 155.282 1.00 21.77 ?  439 VAL B CG2   1 
ATOM   9092  N  N     . SER B 1 440 ? 133.078 158.004 152.367 1.00 24.41 ?  440 SER B N     1 
ATOM   9093  C  CA    . SER B 1 440 ? 132.287 158.321 151.182 1.00 20.03 ?  440 SER B CA    1 
ATOM   9094  C  C     . SER B 1 440 ? 132.896 159.483 150.405 1.00 25.90 ?  440 SER B C     1 
ATOM   9095  O  O     . SER B 1 440 ? 132.957 159.449 149.171 1.00 31.54 ?  440 SER B O     1 
ATOM   9096  C  CB    . SER B 1 440 ? 130.847 158.641 151.583 1.00 22.41 ?  440 SER B CB    1 
ATOM   9097  O  OG    . SER B 1 440 ? 130.009 158.740 150.445 1.00 31.27 ?  440 SER B OG    1 
ATOM   9098  N  N     . GLU B 1 441 ? 133.348 160.520 151.112 1.00 26.70 ?  441 GLU B N     1 
ATOM   9099  C  CA    . GLU B 1 441 ? 133.867 161.711 150.446 1.00 24.82 ?  441 GLU B CA    1 
ATOM   9100  C  C     . GLU B 1 441 ? 135.155 161.418 149.686 1.00 32.63 ?  441 GLU B C     1 
ATOM   9101  O  O     . GLU B 1 441 ? 135.353 161.925 148.577 1.00 40.05 ?  441 GLU B O     1 
ATOM   9102  C  CB    . GLU B 1 441 ? 134.087 162.827 151.464 1.00 27.11 ?  441 GLU B CB    1 
ATOM   9103  C  CG    . GLU B 1 441 ? 132.827 163.605 151.801 1.00 27.69 ?  441 GLU B CG    1 
ATOM   9104  C  CD    . GLU B 1 441 ? 132.862 164.204 153.193 1.00 35.39 ?  441 GLU B CD    1 
ATOM   9105  O  OE1   . GLU B 1 441 ? 133.848 163.968 153.922 1.00 37.20 ?  441 GLU B OE1   1 
ATOM   9106  O  OE2   . GLU B 1 441 ? 131.900 164.911 153.558 1.00 36.45 -1 441 GLU B OE2   1 
ATOM   9107  N  N     . THR B 1 442 ? 136.042 160.606 150.259 1.00 31.61 ?  442 THR B N     1 
ATOM   9108  C  CA    . THR B 1 442 ? 137.300 160.281 149.597 1.00 30.94 ?  442 THR B CA    1 
ATOM   9109  C  C     . THR B 1 442 ? 137.180 159.125 148.613 1.00 29.64 ?  442 THR B C     1 
ATOM   9110  O  O     . THR B 1 442 ? 138.188 158.733 148.018 1.00 34.42 ?  442 THR B O     1 
ATOM   9111  C  CB    . THR B 1 442 ? 138.391 159.963 150.627 1.00 29.54 ?  442 THR B CB    1 
ATOM   9112  O  OG1   . THR B 1 442 ? 138.237 158.618 151.099 1.00 31.14 ?  442 THR B OG1   1 
ATOM   9113  C  CG2   . THR B 1 442 ? 138.340 160.937 151.788 1.00 31.60 ?  442 THR B CG2   1 
ATOM   9114  N  N     . THR B 1 443 ? 135.986 158.572 148.427 1.00 30.24 ?  443 THR B N     1 
ATOM   9115  C  CA    . THR B 1 443 ? 135.769 157.525 147.439 1.00 34.71 ?  443 THR B CA    1 
ATOM   9116  C  C     . THR B 1 443 ? 135.452 158.153 146.089 1.00 35.60 ?  443 THR B C     1 
ATOM   9117  O  O     . THR B 1 443 ? 134.518 158.952 145.972 1.00 36.53 ?  443 THR B O     1 
ATOM   9118  C  CB    . THR B 1 443 ? 134.633 156.595 147.867 1.00 33.90 ?  443 THR B CB    1 
ATOM   9119  O  OG1   . THR B 1 443 ? 135.042 155.829 149.006 1.00 39.26 ?  443 THR B OG1   1 
ATOM   9120  C  CG2   . THR B 1 443 ? 134.266 155.653 146.732 1.00 27.95 ?  443 THR B CG2   1 
ATOM   9121  N  N     . ASP B 1 444 ? 136.232 157.789 145.073 1.00 39.02 ?  444 ASP B N     1 
ATOM   9122  C  CA    . ASP B 1 444 ? 136.023 158.270 143.710 1.00 38.94 ?  444 ASP B CA    1 
ATOM   9123  C  C     . ASP B 1 444 ? 136.363 157.132 142.758 1.00 39.94 ?  444 ASP B C     1 
ATOM   9124  O  O     . ASP B 1 444 ? 137.539 156.802 142.578 1.00 40.16 ?  444 ASP B O     1 
ATOM   9125  C  CB    . ASP B 1 444 ? 136.876 159.505 143.419 1.00 41.00 ?  444 ASP B CB    1 
ATOM   9126  C  CG    . ASP B 1 444 ? 136.244 160.420 142.389 1.00 46.45 ?  444 ASP B CG    1 
ATOM   9127  O  OD1   . ASP B 1 444 ? 135.117 160.902 142.631 1.00 44.63 ?  444 ASP B OD1   1 
ATOM   9128  O  OD2   . ASP B 1 444 ? 136.875 160.660 141.338 1.00 43.46 -1 444 ASP B OD2   1 
ATOM   9129  N  N     . ILE B 1 445 ? 135.341 156.538 142.152 1.00 37.64 ?  445 ILE B N     1 
ATOM   9130  C  CA    . ILE B 1 445 ? 135.506 155.401 141.255 1.00 36.46 ?  445 ILE B CA    1 
ATOM   9131  C  C     . ILE B 1 445 ? 135.381 155.904 139.825 1.00 37.15 ?  445 ILE B C     1 
ATOM   9132  O  O     . ILE B 1 445 ? 134.341 156.446 139.435 1.00 42.66 ?  445 ILE B O     1 
ATOM   9133  C  CB    . ILE B 1 445 ? 134.477 154.301 141.553 1.00 32.65 ?  445 ILE B CB    1 
ATOM   9134  C  CG1   . ILE B 1 445 ? 134.828 153.602 142.865 1.00 33.55 ?  445 ILE B CG1   1 
ATOM   9135  C  CG2   . ILE B 1 445 ? 134.433 153.293 140.419 1.00 35.35 ?  445 ILE B CG2   1 
ATOM   9136  C  CD1   . ILE B 1 445 ? 133.677 152.862 143.481 1.00 35.02 ?  445 ILE B CD1   1 
ATOM   9137  N  N     . ARG B 1 446 ? 136.440 155.719 139.040 1.00 36.82 ?  446 ARG B N     1 
ATOM   9138  C  CA    . ARG B 1 446 ? 136.545 156.320 137.719 1.00 39.43 ?  446 ARG B CA    1 
ATOM   9139  C  C     . ARG B 1 446 ? 136.017 155.428 136.603 1.00 40.16 ?  446 ARG B C     1 
ATOM   9140  O  O     . ARG B 1 446 ? 136.038 155.844 135.440 1.00 37.10 ?  446 ARG B O     1 
ATOM   9141  C  CB    . ARG B 1 446 ? 138.003 156.694 137.431 1.00 37.35 ?  446 ARG B CB    1 
ATOM   9142  C  CG    . ARG B 1 446 ? 138.820 156.977 138.682 1.00 37.48 ?  446 ARG B CG    1 
ATOM   9143  C  CD    . ARG B 1 446 ? 138.549 158.369 139.230 1.00 39.79 ?  446 ARG B CD    1 
ATOM   9144  N  NE    . ARG B 1 446 ? 138.497 159.379 138.181 1.00 40.67 ?  446 ARG B NE    1 
ATOM   9145  C  CZ    . ARG B 1 446 ? 138.666 160.678 138.385 1.00 40.52 ?  446 ARG B CZ    1 
ATOM   9146  N  NH1   . ARG B 1 446 ? 138.899 161.163 139.593 1.00 37.72 1  446 ARG B NH1   1 
ATOM   9147  N  NH2   . ARG B 1 446 ? 138.596 161.512 137.351 1.00 39.59 ?  446 ARG B NH2   1 
ATOM   9148  N  N     . ASN B 1 447 ? 135.542 154.223 136.918 1.00 33.35 ?  447 ASN B N     1 
ATOM   9149  C  CA    . ASN B 1 447 ? 135.024 153.314 135.907 1.00 25.93 ?  447 ASN B CA    1 
ATOM   9150  C  C     . ASN B 1 447 ? 133.574 152.919 136.138 1.00 30.51 ?  447 ASN B C     1 
ATOM   9151  O  O     . ASN B 1 447 ? 133.011 152.183 135.319 1.00 37.20 ?  447 ASN B O     1 
ATOM   9152  C  CB    . ASN B 1 447 ? 135.892 152.051 135.830 1.00 31.43 ?  447 ASN B CB    1 
ATOM   9153  C  CG    . ASN B 1 447 ? 137.001 152.174 134.809 1.00 30.80 ?  447 ASN B CG    1 
ATOM   9154  O  OD1   . ASN B 1 447 ? 136.747 152.324 133.617 1.00 34.38 ?  447 ASN B OD1   1 
ATOM   9155  N  ND2   . ASN B 1 447 ? 138.243 152.115 135.274 1.00 29.87 ?  447 ASN B ND2   1 
ATOM   9156  N  N     . ALA B 1 448 ? 132.954 153.380 137.223 1.00 31.55 ?  448 ALA B N     1 
ATOM   9157  C  CA    . ALA B 1 448 ? 131.532 153.175 137.488 1.00 26.92 ?  448 ALA B CA    1 
ATOM   9158  C  C     . ALA B 1 448 ? 130.891 154.551 137.607 1.00 27.73 ?  448 ALA B C     1 
ATOM   9159  O  O     . ALA B 1 448 ? 130.933 155.174 138.679 1.00 29.36 ?  448 ALA B O     1 
ATOM   9160  C  CB    . ALA B 1 448 ? 131.314 152.342 138.747 1.00 26.31 ?  448 ALA B CB    1 
ATOM   9161  N  N     . PRO B 1 449 ? 130.298 155.069 136.529 1.00 27.20 ?  449 PRO B N     1 
ATOM   9162  C  CA    . PRO B 1 449 ? 129.780 156.445 136.585 1.00 24.21 ?  449 PRO B CA    1 
ATOM   9163  C  C     . PRO B 1 449 ? 128.552 156.583 137.461 1.00 24.86 ?  449 PRO B C     1 
ATOM   9164  O  O     . PRO B 1 449 ? 128.435 157.565 138.206 1.00 21.81 ?  449 PRO B O     1 
ATOM   9165  C  CB    . PRO B 1 449 ? 129.463 156.766 135.115 1.00 21.18 ?  449 PRO B CB    1 
ATOM   9166  C  CG    . PRO B 1 449 ? 129.962 155.595 134.316 1.00 25.67 ?  449 PRO B CG    1 
ATOM   9167  C  CD    . PRO B 1 449 ? 130.040 154.431 135.230 1.00 25.18 ?  449 PRO B CD    1 
ATOM   9168  N  N     . ALA B 1 450 ? 127.623 155.629 137.388 1.00 28.94 ?  450 ALA B N     1 
ATOM   9169  C  CA    . ALA B 1 450 ? 126.434 155.692 138.227 1.00 19.52 ?  450 ALA B CA    1 
ATOM   9170  C  C     . ALA B 1 450 ? 126.792 155.531 139.698 1.00 23.03 ?  450 ALA B C     1 
ATOM   9171  O  O     . ALA B 1 450 ? 126.208 156.197 140.559 1.00 24.84 ?  450 ALA B O     1 
ATOM   9172  C  CB    . ALA B 1 450 ? 125.427 154.631 137.791 1.00 19.72 ?  450 ALA B CB    1 
ATOM   9173  N  N     . VAL B 1 451 ? 127.757 154.661 140.005 1.00 26.08 ?  451 VAL B N     1 
ATOM   9174  C  CA    . VAL B 1 451 ? 128.212 154.510 141.384 1.00 19.47 ?  451 VAL B CA    1 
ATOM   9175  C  C     . VAL B 1 451 ? 128.828 155.809 141.887 1.00 19.53 ?  451 VAL B C     1 
ATOM   9176  O  O     . VAL B 1 451 ? 128.565 156.241 143.014 1.00 26.05 ?  451 VAL B O     1 
ATOM   9177  C  CB    . VAL B 1 451 ? 129.201 153.333 141.501 1.00 22.52 ?  451 VAL B CB    1 
ATOM   9178  C  CG1   . VAL B 1 451 ? 129.847 153.311 142.875 1.00 25.41 ?  451 VAL B CG1   1 
ATOM   9179  C  CG2   . VAL B 1 451 ? 128.497 152.018 141.224 1.00 19.90 ?  451 VAL B CG2   1 
ATOM   9180  N  N     . ARG B 1 452 ? 129.655 156.453 141.061 1.00 21.20 ?  452 ARG B N     1 
ATOM   9181  C  CA    . ARG B 1 452 ? 130.275 157.713 141.460 1.00 23.42 ?  452 ARG B CA    1 
ATOM   9182  C  C     . ARG B 1 452 ? 129.224 158.793 141.693 1.00 24.60 ?  452 ARG B C     1 
ATOM   9183  O  O     . ARG B 1 452 ? 129.270 159.518 142.696 1.00 30.17 ?  452 ARG B O     1 
ATOM   9184  C  CB    . ARG B 1 452 ? 131.279 158.159 140.396 1.00 20.90 ?  452 ARG B CB    1 
ATOM   9185  C  CG    . ARG B 1 452 ? 131.843 159.548 140.627 1.00 24.84 ?  452 ARG B CG    1 
ATOM   9186  C  CD    . ARG B 1 452 ? 133.285 159.645 140.168 1.00 27.79 ?  452 ARG B CD    1 
ATOM   9187  N  NE    . ARG B 1 452 ? 133.395 160.298 138.870 1.00 33.94 ?  452 ARG B NE    1 
ATOM   9188  C  CZ    . ARG B 1 452 ? 134.434 160.177 138.055 1.00 38.90 ?  452 ARG B CZ    1 
ATOM   9189  N  NH1   . ARG B 1 452 ? 135.478 159.431 138.374 1.00 31.79 1  452 ARG B NH1   1 
ATOM   9190  N  NH2   . ARG B 1 452 ? 134.425 160.821 136.892 1.00 34.38 ?  452 ARG B NH2   1 
ATOM   9191  N  N     . ARG B 1 453 ? 128.264 158.910 140.774 1.00 22.40 ?  453 ARG B N     1 
ATOM   9192  C  CA    . ARG B 1 453 ? 127.227 159.927 140.911 1.00 20.83 ?  453 ARG B CA    1 
ATOM   9193  C  C     . ARG B 1 453 ? 126.365 159.673 142.141 1.00 23.25 ?  453 ARG B C     1 
ATOM   9194  O  O     . ARG B 1 453 ? 126.015 160.611 142.866 1.00 25.88 ?  453 ARG B O     1 
ATOM   9195  C  CB    . ARG B 1 453 ? 126.369 159.973 139.645 1.00 20.64 ?  453 ARG B CB    1 
ATOM   9196  C  CG    . ARG B 1 453 ? 125.039 160.681 139.815 1.00 20.05 ?  453 ARG B CG    1 
ATOM   9197  C  CD    . ARG B 1 453 ? 124.445 161.073 138.474 1.00 20.46 ?  453 ARG B CD    1 
ATOM   9198  N  NE    . ARG B 1 453 ? 123.077 160.596 138.325 1.00 22.82 ?  453 ARG B NE    1 
ATOM   9199  C  CZ    . ARG B 1 453 ? 122.006 161.247 138.755 1.00 26.10 ?  453 ARG B CZ    1 
ATOM   9200  N  NH1   . ARG B 1 453 ? 122.106 162.414 139.369 1.00 28.13 1  453 ARG B NH1   1 
ATOM   9201  N  NH2   . ARG B 1 453 ? 120.802 160.713 138.566 1.00 25.07 ?  453 ARG B NH2   1 
ATOM   9202  N  N     . ALA B 1 454 ? 126.017 158.410 142.399 1.00 23.91 ?  454 ALA B N     1 
ATOM   9203  C  CA    . ALA B 1 454 ? 125.214 158.088 143.572 1.00 17.46 ?  454 ALA B CA    1 
ATOM   9204  C  C     . ALA B 1 454 ? 125.989 158.325 144.861 1.00 21.92 ?  454 ALA B C     1 
ATOM   9205  O  O     . ALA B 1 454 ? 125.414 158.765 145.859 1.00 24.78 ?  454 ALA B O     1 
ATOM   9206  C  CB    . ALA B 1 454 ? 124.728 156.643 143.494 1.00 19.55 ?  454 ALA B CB    1 
ATOM   9207  N  N     . ASN B 1 455 ? 127.289 158.032 144.870 1.00 23.90 ?  455 ASN B N     1 
ATOM   9208  C  CA    . ASN B 1 455 ? 128.097 158.331 146.045 1.00 20.72 ?  455 ASN B CA    1 
ATOM   9209  C  C     . ASN B 1 455 ? 128.152 159.831 146.299 1.00 26.36 ?  455 ASN B C     1 
ATOM   9210  O  O     . ASN B 1 455 ? 128.072 160.280 147.448 1.00 30.59 ?  455 ASN B O     1 
ATOM   9211  C  CB    . ASN B 1 455 ? 129.505 157.763 145.876 1.00 20.52 ?  455 ASN B CB    1 
ATOM   9212  C  CG    . ASN B 1 455 ? 130.336 157.884 147.135 1.00 24.75 ?  455 ASN B CG    1 
ATOM   9213  O  OD1   . ASN B 1 455 ? 130.131 157.149 148.099 1.00 30.97 ?  455 ASN B OD1   1 
ATOM   9214  N  ND2   . ASN B 1 455 ? 131.279 158.817 147.134 1.00 27.07 ?  455 ASN B ND2   1 
ATOM   9215  N  N     . LYS B 1 456 ? 128.286 160.624 145.234 1.00 27.25 ?  456 LYS B N     1 
ATOM   9216  C  CA    . LYS B 1 456 ? 128.363 162.071 145.395 1.00 25.06 ?  456 LYS B CA    1 
ATOM   9217  C  C     . LYS B 1 456 ? 127.025 162.675 145.809 1.00 23.96 ?  456 LYS B C     1 
ATOM   9218  O  O     . LYS B 1 456 ? 126.999 163.663 146.549 1.00 32.65 ?  456 LYS B O     1 
ATOM   9219  C  CB    . LYS B 1 456 ? 128.854 162.717 144.099 1.00 26.81 ?  456 LYS B CB    1 
ATOM   9220  C  CG    . LYS B 1 456 ? 130.024 163.668 144.282 1.00 30.51 ?  456 LYS B CG    1 
ATOM   9221  C  CD    . LYS B 1 456 ? 130.639 164.048 142.945 1.00 33.74 ?  456 LYS B CD    1 
ATOM   9222  C  CE    . LYS B 1 456 ? 131.114 162.821 142.184 1.00 33.23 ?  456 LYS B CE    1 
ATOM   9223  N  NZ    . LYS B 1 456 ? 132.323 162.212 142.802 1.00 28.20 1  456 LYS B NZ    1 
ATOM   9224  N  N     . ALA B 1 457 ? 125.912 162.105 145.346 1.00 24.59 ?  457 ALA B N     1 
ATOM   9225  C  CA    . ALA B 1 457 ? 124.597 162.697 145.572 1.00 18.66 ?  457 ALA B CA    1 
ATOM   9226  C  C     . ALA B 1 457 ? 123.919 162.143 146.823 1.00 26.26 ?  457 ALA B C     1 
ATOM   9227  O  O     . ALA B 1 457 ? 123.544 162.902 147.722 1.00 32.54 ?  457 ALA B O     1 
ATOM   9228  C  CB    . ALA B 1 457 ? 123.713 162.471 144.340 1.00 18.26 ?  457 ALA B CB    1 
ATOM   9229  N  N     . MET B 1 458 ? 123.741 160.823 146.879 1.00 24.94 ?  458 MET B N     1 
ATOM   9230  C  CA    . MET B 1 458 ? 123.072 160.195 148.012 1.00 16.55 ?  458 MET B CA    1 
ATOM   9231  C  C     . MET B 1 458 ? 123.855 160.388 149.305 1.00 21.35 ?  458 MET B C     1 
ATOM   9232  O  O     . MET B 1 458 ? 123.262 160.605 150.368 1.00 30.53 ?  458 MET B O     1 
ATOM   9233  C  CB    . MET B 1 458 ? 122.871 158.705 147.733 1.00 22.58 ?  458 MET B CB    1 
ATOM   9234  C  CG    . MET B 1 458 ? 122.267 158.395 146.376 1.00 21.89 ?  458 MET B CG    1 
ATOM   9235  S  SD    . MET B 1 458 ? 120.773 159.341 146.051 1.00 29.65 ?  458 MET B SD    1 
ATOM   9236  C  CE    . MET B 1 458 ? 119.657 158.583 147.225 1.00 23.61 ?  458 MET B CE    1 
ATOM   9237  N  N     . LYS B 1 459 ? 125.184 160.292 149.236 1.00 19.92 ?  459 LYS B N     1 
ATOM   9238  C  CA    . LYS B 1 459 ? 126.048 160.349 150.418 1.00 17.97 ?  459 LYS B CA    1 
ATOM   9239  C  C     . LYS B 1 459 ? 125.664 159.268 151.425 1.00 20.01 ?  459 LYS B C     1 
ATOM   9240  O  O     . LYS B 1 459 ? 125.754 159.461 152.638 1.00 26.61 ?  459 LYS B O     1 
ATOM   9241  C  CB    . LYS B 1 459 ? 126.016 161.732 151.071 1.00 20.12 ?  459 LYS B CB    1 
ATOM   9242  C  CG    . LYS B 1 459 ? 126.646 162.833 150.242 1.00 24.69 ?  459 LYS B CG    1 
ATOM   9243  C  CD    . LYS B 1 459 ? 125.921 164.151 150.447 1.00 25.09 ?  459 LYS B CD    1 
ATOM   9244  C  CE    . LYS B 1 459 ? 126.179 165.107 149.299 1.00 25.13 ?  459 LYS B CE    1 
ATOM   9245  N  NZ    . LYS B 1 459 ? 127.632 165.377 149.122 1.00 27.84 1  459 LYS B NZ    1 
ATOM   9246  N  N     . SER B 1 460 ? 125.232 158.119 150.915 1.00 24.04 ?  460 SER B N     1 
ATOM   9247  C  CA    . SER B 1 460 ? 124.738 157.047 151.762 1.00 13.89 ?  460 SER B CA    1 
ATOM   9248  C  C     . SER B 1 460 ? 125.883 156.335 152.467 1.00 13.09 ?  460 SER B C     1 
ATOM   9249  O  O     . SER B 1 460 ? 126.927 156.058 151.871 1.00 26.30 ?  460 SER B O     1 
ATOM   9250  C  CB    . SER B 1 460 ? 123.934 156.046 150.937 1.00 15.88 ?  460 SER B CB    1 
ATOM   9251  O  OG    . SER B 1 460 ? 124.055 154.743 151.476 1.00 26.50 ?  460 SER B OG    1 
ATOM   9252  N  N     . ILE B 1 461 ? 125.677 156.038 153.750 1.00 10.69 ?  461 ILE B N     1 
ATOM   9253  C  CA    . ILE B 1 461 ? 126.633 155.292 154.552 1.00 19.56 ?  461 ILE B CA    1 
ATOM   9254  C  C     . ILE B 1 461 ? 125.891 154.157 155.241 1.00 16.81 ?  461 ILE B C     1 
ATOM   9255  O  O     . ILE B 1 461 ? 124.667 154.172 155.374 1.00 20.02 ?  461 ILE B O     1 
ATOM   9256  C  CB    . ILE B 1 461 ? 127.346 156.179 155.595 1.00 14.38 ?  461 ILE B CB    1 
ATOM   9257  C  CG1   . ILE B 1 461 ? 126.335 156.743 156.594 1.00 10.83 ?  461 ILE B CG1   1 
ATOM   9258  C  CG2   . ILE B 1 461 ? 128.114 157.301 154.911 1.00 17.22 ?  461 ILE B CG2   1 
ATOM   9259  C  CD1   . ILE B 1 461 ? 126.964 157.467 157.759 1.00 14.55 ?  461 ILE B CD1   1 
ATOM   9260  N  N     . GLY B 1 462 ? 126.651 153.151 155.661 1.00 15.87 ?  462 GLY B N     1 
ATOM   9261  C  CA    . GLY B 1 462 ? 126.075 152.064 156.424 1.00 6.58  ?  462 GLY B CA    1 
ATOM   9262  C  C     . GLY B 1 462 ? 126.745 151.881 157.768 1.00 11.82 ?  462 GLY B C     1 
ATOM   9263  O  O     . GLY B 1 462 ? 127.900 151.455 157.837 1.00 26.95 ?  462 GLY B O     1 
ATOM   9264  N  N     . LEU B 1 463 ? 126.028 152.191 158.842 1.00 12.36 ?  463 LEU B N     1 
ATOM   9265  C  CA    . LEU B 1 463 ? 126.539 152.029 160.198 1.00 11.25 ?  463 LEU B CA    1 
ATOM   9266  C  C     . LEU B 1 463 ? 125.860 150.814 160.817 1.00 13.98 ?  463 LEU B C     1 
ATOM   9267  O  O     . LEU B 1 463 ? 124.679 150.867 161.171 1.00 25.51 ?  463 LEU B O     1 
ATOM   9268  C  CB    . LEU B 1 463 ? 126.295 153.287 161.029 1.00 19.67 ?  463 LEU B CB    1 
ATOM   9269  C  CG    . LEU B 1 463 ? 126.720 153.227 162.499 1.00 18.45 ?  463 LEU B CG    1 
ATOM   9270  C  CD1   . LEU B 1 463 ? 128.148 152.730 162.622 1.00 6.51  ?  463 LEU B CD1   1 
ATOM   9271  C  CD2   . LEU B 1 463 ? 126.563 154.587 163.157 1.00 14.56 ?  463 LEU B CD2   1 
ATOM   9272  N  N     . GLY B 1 464 ? 126.609 149.719 160.940 1.00 14.85 ?  464 GLY B N     1 
ATOM   9273  C  CA    . GLY B 1 464 ? 126.089 148.482 161.476 1.00 13.86 ?  464 GLY B CA    1 
ATOM   9274  C  C     . GLY B 1 464 ? 126.369 148.326 162.960 1.00 13.07 ?  464 GLY B C     1 
ATOM   9275  O  O     . GLY B 1 464 ? 126.774 149.258 163.657 1.00 15.05 ?  464 GLY B O     1 
ATOM   9276  N  N     . ALA B 1 465 ? 126.142 147.108 163.442 1.00 15.16 ?  465 ALA B N     1 
ATOM   9277  C  CA    . ALA B 1 465 ? 126.379 146.776 164.837 1.00 12.37 ?  465 ALA B CA    1 
ATOM   9278  C  C     . ALA B 1 465 ? 126.800 145.320 164.931 1.00 14.17 ?  465 ALA B C     1 
ATOM   9279  O  O     . ALA B 1 465 ? 126.330 144.479 164.159 1.00 28.53 ?  465 ALA B O     1 
ATOM   9280  C  CB    . ALA B 1 465 ? 125.136 147.029 165.696 1.00 19.00 ?  465 ALA B CB    1 
ATOM   9281  N  N     . MET B 1 466 ? 127.694 145.032 165.872 1.00 20.66 ?  466 MET B N     1 
ATOM   9282  C  CA    . MET B 1 466 ? 128.158 143.682 166.143 1.00 20.75 ?  466 MET B CA    1 
ATOM   9283  C  C     . MET B 1 466 ? 128.068 143.418 167.639 1.00 20.58 ?  466 MET B C     1 
ATOM   9284  O  O     . MET B 1 466 ? 127.859 144.333 168.442 1.00 26.81 ?  466 MET B O     1 
ATOM   9285  C  CB    . MET B 1 466 ? 129.596 143.466 165.648 1.00 27.19 ?  466 MET B CB    1 
ATOM   9286  C  CG    . MET B 1 466 ? 130.577 144.532 166.109 1.00 22.89 ?  466 MET B CG    1 
ATOM   9287  S  SD    . MET B 1 466 ? 132.263 144.259 165.534 1.00 38.02 ?  466 MET B SD    1 
ATOM   9288  C  CE    . MET B 1 466 ? 131.993 143.912 163.800 1.00 29.36 ?  466 MET B CE    1 
ATOM   9289  N  N     . ASN B 1 467 ? 128.215 142.144 168.005 1.00 19.96 ?  467 ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 467 ? 128.269 141.711 169.403 1.00 19.55 ?  467 ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 467 ? 126.951 141.963 170.132 1.00 20.51 ?  467 ASN B C     1 
ATOM   9292  O  O     . ASN B 1 467 ? 126.941 142.303 171.315 1.00 27.46 ?  467 ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 467 ? 129.427 142.374 170.152 1.00 21.54 ?  467 ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 467 ? 130.140 141.419 171.082 1.00 24.57 ?  467 ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 467 ? 129.895 140.214 171.062 1.00 28.94 ?  467 ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 467 ? 131.033 141.952 171.905 1.00 28.00 ?  467 ASN B ND2   1 
ATOM   9297  N  N     . LEU B 1 468 ? 125.829 141.807 169.426 1.00 19.53 ?  468 LEU B N     1 
ATOM   9298  C  CA    . LEU B 1 468 ? 124.539 141.833 170.108 1.00 18.12 ?  468 LEU B CA    1 
ATOM   9299  C  C     . LEU B 1 468 ? 124.371 140.602 170.987 1.00 22.01 ?  468 LEU B C     1 
ATOM   9300  O  O     . LEU B 1 468 ? 124.055 140.711 172.179 1.00 25.58 ?  468 LEU B O     1 
ATOM   9301  C  CB    . LEU B 1 468 ? 123.404 141.923 169.090 1.00 24.55 ?  468 LEU B CB    1 
ATOM   9302  C  CG    . LEU B 1 468 ? 122.003 141.740 169.677 1.00 20.38 ?  468 LEU B CG    1 
ATOM   9303  C  CD1   . LEU B 1 468 ? 121.668 142.876 170.629 1.00 17.94 ?  468 LEU B CD1   1 
ATOM   9304  C  CD2   . LEU B 1 468 ? 120.956 141.624 168.584 1.00 15.41 ?  468 LEU B CD2   1 
ATOM   9305  N  N     . HIS B 1 469 ? 124.609 139.419 170.419 1.00 25.31 ?  469 HIS B N     1 
ATOM   9306  C  CA    . HIS B 1 469 ? 124.481 138.190 171.192 1.00 16.96 ?  469 HIS B CA    1 
ATOM   9307  C  C     . HIS B 1 469 ? 125.559 138.102 172.262 1.00 26.08 ?  469 HIS B C     1 
ATOM   9308  O  O     . HIS B 1 469 ? 125.307 137.592 173.356 1.00 38.87 ?  469 HIS B O     1 
ATOM   9309  C  CB    . HIS B 1 469 ? 124.539 136.972 170.273 1.00 20.40 ?  469 HIS B CB    1 
ATOM   9310  C  CG    . HIS B 1 469 ? 124.030 135.716 170.909 1.00 24.73 ?  469 HIS B CG    1 
ATOM   9311  N  ND1   . HIS B 1 469 ? 124.143 134.480 170.314 1.00 28.72 ?  469 HIS B ND1   1 
ATOM   9312  C  CD2   . HIS B 1 469 ? 123.404 135.508 172.092 1.00 25.30 ?  469 HIS B CD2   1 
ATOM   9313  C  CE1   . HIS B 1 469 ? 123.610 133.564 171.101 1.00 22.84 ?  469 HIS B CE1   1 
ATOM   9314  N  NE2   . HIS B 1 469 ? 123.155 134.161 172.187 1.00 25.44 ?  469 HIS B NE2   1 
ATOM   9315  N  N     . GLY B 1 470 ? 126.765 138.584 171.962 1.00 21.78 ?  470 GLY B N     1 
ATOM   9316  C  CA    . GLY B 1 470 ? 127.807 138.604 172.975 1.00 18.71 ?  470 GLY B CA    1 
ATOM   9317  C  C     . GLY B 1 470 ? 127.433 139.462 174.166 1.00 19.99 ?  470 GLY B C     1 
ATOM   9318  O  O     . GLY B 1 470 ? 127.599 139.055 175.318 1.00 34.01 ?  470 GLY B O     1 
ATOM   9319  N  N     . TYR B 1 471 ? 126.907 140.660 173.902 1.00 22.88 ?  471 TYR B N     1 
ATOM   9320  C  CA    . TYR B 1 471 ? 126.481 141.532 174.991 1.00 25.52 ?  471 TYR B CA    1 
ATOM   9321  C  C     . TYR B 1 471 ? 125.333 140.912 175.776 1.00 27.96 ?  471 TYR B C     1 
ATOM   9322  O  O     . TYR B 1 471 ? 125.314 140.971 177.011 1.00 32.88 ?  471 TYR B O     1 
ATOM   9323  C  CB    . TYR B 1 471 ? 126.071 142.901 174.448 1.00 24.23 ?  471 TYR B CB    1 
ATOM   9324  C  CG    . TYR B 1 471 ? 125.684 143.882 175.531 1.00 26.56 ?  471 TYR B CG    1 
ATOM   9325  C  CD1   . TYR B 1 471 ? 126.646 144.436 176.365 1.00 28.31 ?  471 TYR B CD1   1 
ATOM   9326  C  CD2   . TYR B 1 471 ? 124.358 144.234 175.737 1.00 18.57 ?  471 TYR B CD2   1 
ATOM   9327  C  CE1   . TYR B 1 471 ? 126.301 145.327 177.358 1.00 28.21 ?  471 TYR B CE1   1 
ATOM   9328  C  CE2   . TYR B 1 471 ? 124.004 145.122 176.732 1.00 21.27 ?  471 TYR B CE2   1 
ATOM   9329  C  CZ    . TYR B 1 471 ? 124.979 145.665 177.538 1.00 27.48 ?  471 TYR B CZ    1 
ATOM   9330  O  OH    . TYR B 1 471 ? 124.634 146.549 178.533 1.00 32.99 ?  471 TYR B OH    1 
ATOM   9331  N  N     . LEU B 1 472 ? 124.363 140.315 175.077 1.00 26.27 ?  472 LEU B N     1 
ATOM   9332  C  CA    . LEU B 1 472 ? 123.215 139.735 175.766 1.00 23.87 ?  472 LEU B CA    1 
ATOM   9333  C  C     . LEU B 1 472 ? 123.618 138.536 176.618 1.00 25.52 ?  472 LEU B C     1 
ATOM   9334  O  O     . LEU B 1 472 ? 123.142 138.384 177.748 1.00 31.23 ?  472 LEU B O     1 
ATOM   9335  C  CB    . LEU B 1 472 ? 122.139 139.338 174.755 1.00 28.13 ?  472 LEU B CB    1 
ATOM   9336  C  CG    . LEU B 1 472 ? 121.484 140.474 173.969 1.00 27.42 ?  472 LEU B CG    1 
ATOM   9337  C  CD1   . LEU B 1 472 ? 120.654 139.919 172.822 1.00 24.49 ?  472 LEU B CD1   1 
ATOM   9338  C  CD2   . LEU B 1 472 ? 120.636 141.345 174.880 1.00 19.86 ?  472 LEU B CD2   1 
ATOM   9339  N  N     . ALA B 1 473 ? 124.491 137.671 176.094 1.00 25.93 ?  473 ALA B N     1 
ATOM   9340  C  CA    . ALA B 1 473 ? 124.898 136.484 176.835 1.00 26.31 ?  473 ALA B CA    1 
ATOM   9341  C  C     . ALA B 1 473 ? 125.819 136.839 177.993 1.00 33.22 ?  473 ALA B C     1 
ATOM   9342  O  O     . ALA B 1 473 ? 125.746 136.223 179.062 1.00 38.99 ?  473 ALA B O     1 
ATOM   9343  C  CB    . ALA B 1 473 ? 125.574 135.489 175.893 1.00 26.76 ?  473 ALA B CB    1 
ATOM   9344  N  N     . GLN B 1 474 ? 126.695 137.827 177.804 1.00 27.75 ?  474 GLN B N     1 
ATOM   9345  C  CA    . GLN B 1 474 ? 127.581 138.256 178.877 1.00 28.56 ?  474 GLN B CA    1 
ATOM   9346  C  C     . GLN B 1 474 ? 126.861 139.064 179.946 1.00 29.18 ?  474 GLN B C     1 
ATOM   9347  O  O     . GLN B 1 474 ? 127.448 139.324 181.002 1.00 36.85 ?  474 GLN B O     1 
ATOM   9348  C  CB    . GLN B 1 474 ? 128.743 139.069 178.303 1.00 28.71 ?  474 GLN B CB    1 
ATOM   9349  C  CG    . GLN B 1 474 ? 129.785 138.221 177.595 1.00 28.77 ?  474 GLN B CG    1 
ATOM   9350  C  CD    . GLN B 1 474 ? 130.839 139.052 176.899 1.00 33.70 ?  474 GLN B CD    1 
ATOM   9351  O  OE1   . GLN B 1 474 ? 131.650 139.714 177.545 1.00 36.08 ?  474 GLN B OE1   1 
ATOM   9352  N  NE2   . GLN B 1 474 ? 130.835 139.024 175.571 1.00 33.97 ?  474 GLN B NE2   1 
ATOM   9353  N  N     . ASN B 1 475 ? 125.616 139.467 179.700 1.00 31.43 ?  475 ASN B N     1 
ATOM   9354  C  CA    . ASN B 1 475 ? 124.805 140.173 180.681 1.00 31.52 ?  475 ASN B CA    1 
ATOM   9355  C  C     . ASN B 1 475 ? 123.651 139.325 181.195 1.00 31.77 ?  475 ASN B C     1 
ATOM   9356  O  O     . ASN B 1 475 ? 122.742 139.857 181.839 1.00 34.96 ?  475 ASN B O     1 
ATOM   9357  C  CB    . ASN B 1 475 ? 124.277 141.479 180.085 1.00 30.74 ?  475 ASN B CB    1 
ATOM   9358  C  CG    . ASN B 1 475 ? 125.356 142.532 179.956 1.00 30.26 ?  475 ASN B CG    1 
ATOM   9359  O  OD1   . ASN B 1 475 ? 125.548 143.356 180.850 1.00 38.24 ?  475 ASN B OD1   1 
ATOM   9360  N  ND2   . ASN B 1 475 ? 126.077 142.504 178.843 1.00 28.97 ?  475 ASN B ND2   1 
ATOM   9361  N  N     . GLY B 1 476 ? 123.665 138.024 180.927 1.00 31.06 ?  476 GLY B N     1 
ATOM   9362  C  CA    . GLY B 1 476 ? 122.621 137.135 181.403 1.00 30.18 ?  476 GLY B CA    1 
ATOM   9363  C  C     . GLY B 1 476 ? 121.254 137.378 180.801 1.00 35.17 ?  476 GLY B C     1 
ATOM   9364  O  O     . GLY B 1 476 ? 120.248 137.326 181.519 1.00 37.39 ?  476 GLY B O     1 
ATOM   9365  N  N     . ILE B 1 477 ? 121.191 137.649 179.501 1.00 32.15 ?  477 ILE B N     1 
ATOM   9366  C  CA    . ILE B 1 477 ? 119.932 137.851 178.793 1.00 27.50 ?  477 ILE B CA    1 
ATOM   9367  C  C     . ILE B 1 477 ? 119.874 136.859 177.641 1.00 31.33 ?  477 ILE B C     1 
ATOM   9368  O  O     . ILE B 1 477 ? 120.779 136.827 176.797 1.00 36.33 ?  477 ILE B O     1 
ATOM   9369  C  CB    . ILE B 1 477 ? 119.784 139.291 178.282 1.00 26.02 ?  477 ILE B CB    1 
ATOM   9370  C  CG1   . ILE B 1 477 ? 119.910 140.286 179.436 1.00 29.49 ?  477 ILE B CG1   1 
ATOM   9371  C  CG2   . ILE B 1 477 ? 118.452 139.468 177.577 1.00 30.20 ?  477 ILE B CG2   1 
ATOM   9372  C  CD1   . ILE B 1 477 ? 120.267 141.681 178.992 1.00 32.35 ?  477 ILE B CD1   1 
ATOM   9373  N  N     . ALA B 1 478 ? 118.817 136.052 177.608 1.00 33.41 ?  478 ALA B N     1 
ATOM   9374  C  CA    . ALA B 1 478 ? 118.626 135.116 176.508 1.00 27.28 ?  478 ALA B CA    1 
ATOM   9375  C  C     . ALA B 1 478 ? 118.297 135.878 175.231 1.00 32.74 ?  478 ALA B C     1 
ATOM   9376  O  O     . ALA B 1 478 ? 117.482 136.805 175.244 1.00 34.41 ?  478 ALA B O     1 
ATOM   9377  C  CB    . ALA B 1 478 ? 117.513 134.126 176.842 1.00 27.73 ?  478 ALA B CB    1 
ATOM   9378  N  N     . TYR B 1 479 ? 118.934 135.482 174.126 1.00 30.56 ?  479 TYR B N     1 
ATOM   9379  C  CA    . TYR B 1 479 ? 118.742 136.183 172.860 1.00 23.51 ?  479 TYR B CA    1 
ATOM   9380  C  C     . TYR B 1 479 ? 117.287 136.144 172.408 1.00 26.65 ?  479 TYR B C     1 
ATOM   9381  O  O     . TYR B 1 479 ? 116.808 137.095 171.782 1.00 32.90 ?  479 TYR B O     1 
ATOM   9382  C  CB    . TYR B 1 479 ? 119.657 135.578 171.794 1.00 18.58 ?  479 TYR B CB    1 
ATOM   9383  C  CG    . TYR B 1 479 ? 119.623 136.260 170.442 1.00 26.64 ?  479 TYR B CG    1 
ATOM   9384  C  CD1   . TYR B 1 479 ? 118.692 135.896 169.477 1.00 24.92 ?  479 TYR B CD1   1 
ATOM   9385  C  CD2   . TYR B 1 479 ? 120.537 137.256 170.125 1.00 25.29 ?  479 TYR B CD2   1 
ATOM   9386  C  CE1   . TYR B 1 479 ? 118.663 136.514 168.242 1.00 22.84 ?  479 TYR B CE1   1 
ATOM   9387  C  CE2   . TYR B 1 479 ? 120.518 137.877 168.891 1.00 22.12 ?  479 TYR B CE2   1 
ATOM   9388  C  CZ    . TYR B 1 479 ? 119.580 137.503 167.954 1.00 28.95 ?  479 TYR B CZ    1 
ATOM   9389  O  OH    . TYR B 1 479 ? 119.560 138.121 166.725 1.00 29.93 ?  479 TYR B OH    1 
ATOM   9390  N  N     . GLU B 1 480 ? 116.572 135.064 172.712 1.00 28.98 ?  480 GLU B N     1 
ATOM   9391  C  CA    . GLU B 1 480 ? 115.169 134.947 172.339 1.00 28.27 ?  480 GLU B CA    1 
ATOM   9392  C  C     . GLU B 1 480 ? 114.227 135.587 173.348 1.00 27.46 ?  480 GLU B C     1 
ATOM   9393  O  O     . GLU B 1 480 ? 113.023 135.668 173.080 1.00 33.76 ?  480 GLU B O     1 
ATOM   9394  C  CB    . GLU B 1 480 ? 114.785 133.475 172.169 1.00 30.32 ?  480 GLU B CB    1 
ATOM   9395  C  CG    . GLU B 1 480 ? 115.528 132.747 171.067 1.00 28.24 ?  480 GLU B CG    1 
ATOM   9396  C  CD    . GLU B 1 480 ? 115.287 131.252 171.112 1.00 36.35 ?  480 GLU B CD    1 
ATOM   9397  O  OE1   . GLU B 1 480 ? 114.162 130.821 170.784 1.00 36.92 ?  480 GLU B OE1   1 
ATOM   9398  O  OE2   . GLU B 1 480 ? 116.217 130.507 171.484 1.00 36.74 -1 480 GLU B OE2   1 
ATOM   9399  N  N     . SER B 1 481 ? 114.736 136.041 174.489 1.00 26.14 ?  481 SER B N     1 
ATOM   9400  C  CA    . SER B 1 481 ? 113.875 136.576 175.528 1.00 26.98 ?  481 SER B CA    1 
ATOM   9401  C  C     . SER B 1 481 ? 113.295 137.926 175.109 1.00 28.79 ?  481 SER B C     1 
ATOM   9402  O  O     . SER B 1 481 ? 113.887 138.642 174.297 1.00 29.80 ?  481 SER B O     1 
ATOM   9403  C  CB    . SER B 1 481 ? 114.651 136.729 176.832 1.00 28.32 ?  481 SER B CB    1 
ATOM   9404  O  OG    . SER B 1 481 ? 115.288 137.991 176.900 1.00 32.20 ?  481 SER B OG    1 
ATOM   9405  N  N     . PRO B 1 482 ? 112.124 138.288 175.639 1.00 36.02 ?  482 PRO B N     1 
ATOM   9406  C  CA    . PRO B 1 482 ? 111.602 139.641 175.392 1.00 32.05 ?  482 PRO B CA    1 
ATOM   9407  C  C     . PRO B 1 482 ? 112.507 140.737 175.922 1.00 31.69 ?  482 PRO B C     1 
ATOM   9408  O  O     . PRO B 1 482 ? 112.487 141.853 175.389 1.00 31.35 ?  482 PRO B O     1 
ATOM   9409  C  CB    . PRO B 1 482 ? 110.245 139.629 176.110 1.00 30.81 ?  482 PRO B CB    1 
ATOM   9410  C  CG    . PRO B 1 482 ? 109.878 138.190 176.210 1.00 31.49 ?  482 PRO B CG    1 
ATOM   9411  C  CD    . PRO B 1 482 ? 111.168 137.454 176.385 1.00 33.90 ?  482 PRO B CD    1 
ATOM   9412  N  N     . GLU B 1 483 ? 113.292 140.458 176.966 1.00 34.74 ?  483 GLU B N     1 
ATOM   9413  C  CA    . GLU B 1 483 ? 114.230 141.453 177.476 1.00 33.51 ?  483 GLU B CA    1 
ATOM   9414  C  C     . GLU B 1 483 ? 115.298 141.784 176.442 1.00 33.18 ?  483 GLU B C     1 
ATOM   9415  O  O     . GLU B 1 483 ? 115.705 142.944 176.308 1.00 38.65 ?  483 GLU B O     1 
ATOM   9416  C  CB    . GLU B 1 483 ? 114.874 140.953 178.769 1.00 36.12 ?  483 GLU B CB    1 
ATOM   9417  C  CG    . GLU B 1 483 ? 113.961 141.012 179.978 1.00 37.22 ?  483 GLU B CG    1 
ATOM   9418  C  CD    . GLU B 1 483 ? 113.257 139.697 180.240 1.00 41.25 ?  483 GLU B CD    1 
ATOM   9419  O  OE1   . GLU B 1 483 ? 112.870 139.022 179.262 1.00 39.62 ?  483 GLU B OE1   1 
ATOM   9420  O  OE2   . GLU B 1 483 ? 113.089 139.337 181.424 1.00 40.92 -1 483 GLU B OE2   1 
ATOM   9421  N  N     . ALA B 1 484 ? 115.772 140.774 175.710 1.00 26.92 ?  484 ALA B N     1 
ATOM   9422  C  CA    . ALA B 1 484 ? 116.746 141.018 174.654 1.00 25.36 ?  484 ALA B CA    1 
ATOM   9423  C  C     . ALA B 1 484 ? 116.159 141.887 173.549 1.00 27.63 ?  484 ALA B C     1 
ATOM   9424  O  O     . ALA B 1 484 ? 116.830 142.790 173.036 1.00 27.44 ?  484 ALA B O     1 
ATOM   9425  C  CB    . ALA B 1 484 ? 117.244 139.690 174.090 1.00 24.44 ?  484 ALA B CB    1 
ATOM   9426  N  N     . ARG B 1 485 ? 114.908 141.625 173.162 1.00 29.59 ?  485 ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 485 ? 114.265 142.455 172.150 1.00 22.93 ?  485 ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 485 ? 114.035 143.873 172.655 1.00 23.94 ?  485 ARG B C     1 
ATOM   9429  O  O     . ARG B 1 485 ? 114.152 144.828 171.883 1.00 33.77 ?  485 ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 485 ? 112.949 141.822 171.707 1.00 28.90 ?  485 ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 485 ? 113.122 140.528 170.933 1.00 27.03 ?  485 ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 485 ? 111.812 140.074 170.319 1.00 27.04 ?  485 ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 485 ? 110.768 139.896 171.321 1.00 27.22 ?  485 ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 485 ? 110.552 138.771 171.987 1.00 27.87 ?  485 ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 485 ? 111.303 137.698 171.793 1.00 25.07 1  485 ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 485 ? 109.559 138.719 172.869 1.00 30.16 ?  485 ARG B NH2   1 
ATOM   9437  N  N     . ASP B 1 486 ? 113.713 144.027 173.940 1.00 30.99 ?  486 ASP B N     1 
ATOM   9438  C  CA    . ASP B 1 486 ? 113.593 145.358 174.525 1.00 27.43 ?  486 ASP B CA    1 
ATOM   9439  C  C     . ASP B 1 486 ? 114.922 146.102 174.480 1.00 26.61 ?  486 ASP B C     1 
ATOM   9440  O  O     . ASP B 1 486 ? 114.970 147.294 174.139 1.00 33.37 ?  486 ASP B O     1 
ATOM   9441  C  CB    . ASP B 1 486 ? 113.087 145.241 175.962 1.00 32.56 ?  486 ASP B CB    1 
ATOM   9442  C  CG    . ASP B 1 486 ? 112.791 146.582 176.591 1.00 40.37 ?  486 ASP B CG    1 
ATOM   9443  O  OD1   . ASP B 1 486 ? 112.058 147.383 175.977 1.00 37.86 ?  486 ASP B OD1   1 
ATOM   9444  O  OD2   . ASP B 1 486 ? 113.292 146.827 177.707 1.00 37.16 -1 486 ASP B OD2   1 
ATOM   9445  N  N     . PHE B 1 487 ? 116.013 145.411 174.816 1.00 25.12 ?  487 PHE B N     1 
ATOM   9446  C  CA    . PHE B 1 487 ? 117.330 146.031 174.732 1.00 24.05 ?  487 PHE B CA    1 
ATOM   9447  C  C     . PHE B 1 487 ? 117.653 146.435 173.302 1.00 23.70 ?  487 PHE B C     1 
ATOM   9448  O  O     . PHE B 1 487 ? 118.189 147.519 173.062 1.00 29.55 ?  487 PHE B O     1 
ATOM   9449  C  CB    . PHE B 1 487 ? 118.413 145.095 175.258 1.00 25.33 ?  487 PHE B CB    1 
ATOM   9450  C  CG    . PHE B 1 487 ? 119.790 145.491 174.817 1.00 27.57 ?  487 PHE B CG    1 
ATOM   9451  C  CD1   . PHE B 1 487 ? 120.437 146.555 175.419 1.00 22.50 ?  487 PHE B CD1   1 
ATOM   9452  C  CD2   . PHE B 1 487 ? 120.419 144.835 173.771 1.00 29.01 ?  487 PHE B CD2   1 
ATOM   9453  C  CE1   . PHE B 1 487 ? 121.690 146.943 175.005 1.00 24.30 ?  487 PHE B CE1   1 
ATOM   9454  C  CE2   . PHE B 1 487 ? 121.673 145.221 173.353 1.00 25.24 ?  487 PHE B CE2   1 
ATOM   9455  C  CZ    . PHE B 1 487 ? 122.309 146.277 173.972 1.00 27.43 ?  487 PHE B CZ    1 
ATOM   9456  N  N     . ALA B 1 488 ? 117.371 145.553 172.343 1.00 24.45 ?  488 ALA B N     1 
ATOM   9457  C  CA    . ALA B 1 488 ? 117.645 145.876 170.948 1.00 19.89 ?  488 ALA B CA    1 
ATOM   9458  C  C     . ALA B 1 488 ? 116.831 147.081 170.501 1.00 26.39 ?  488 ALA B C     1 
ATOM   9459  O  O     . ALA B 1 488 ? 117.353 147.982 169.838 1.00 31.88 ?  488 ALA B O     1 
ATOM   9460  C  CB    . ALA B 1 488 ? 117.356 144.669 170.059 1.00 20.17 ?  488 ALA B CB    1 
ATOM   9461  N  N     . ASN B 1 489 ? 115.553 147.122 170.882 1.00 25.22 ?  489 ASN B N     1 
ATOM   9462  C  CA    . ASN B 1 489 ? 114.702 148.258 170.553 1.00 24.36 ?  489 ASN B CA    1 
ATOM   9463  C  C     . ASN B 1 489 ? 115.300 149.556 171.073 1.00 23.95 ?  489 ASN B C     1 
ATOM   9464  O  O     . ASN B 1 489 ? 115.488 150.514 170.316 1.00 24.39 ?  489 ASN B O     1 
ATOM   9465  C  CB    . ASN B 1 489 ? 113.305 148.038 171.134 1.00 21.91 ?  489 ASN B CB    1 
ATOM   9466  C  CG    . ASN B 1 489 ? 112.300 149.050 170.637 1.00 27.14 ?  489 ASN B CG    1 
ATOM   9467  O  OD1   . ASN B 1 489 ? 112.239 149.349 169.447 1.00 33.77 ?  489 ASN B OD1   1 
ATOM   9468  N  ND2   . ASN B 1 489 ? 111.498 149.581 171.551 1.00 30.58 ?  489 ASN B ND2   1 
ATOM   9469  N  N     . THR B 1 490 ? 115.638 149.593 172.364 1.00 27.27 ?  490 THR B N     1 
ATOM   9470  C  CA    . THR B 1 490 ? 116.159 150.825 172.947 1.00 22.97 ?  490 THR B CA    1 
ATOM   9471  C  C     . THR B 1 490 ? 117.508 151.203 172.343 1.00 24.75 ?  490 THR B C     1 
ATOM   9472  O  O     . THR B 1 490 ? 117.727 152.359 171.962 1.00 25.78 ?  490 THR B O     1 
ATOM   9473  C  CB    . THR B 1 490 ? 116.274 150.684 174.464 1.00 28.98 ?  490 THR B CB    1 
ATOM   9474  O  OG1   . THR B 1 490 ? 115.006 150.295 175.007 1.00 32.64 ?  490 THR B OG1   1 
ATOM   9475  C  CG2   . THR B 1 490 ? 116.707 152.002 175.083 1.00 26.06 ?  490 THR B CG2   1 
ATOM   9476  N  N     . PHE B 1 491 ? 118.422 150.235 172.239 1.00 24.63 ?  491 PHE B N     1 
ATOM   9477  C  CA    . PHE B 1 491 ? 119.767 150.521 171.756 1.00 19.07 ?  491 PHE B CA    1 
ATOM   9478  C  C     . PHE B 1 491 ? 119.745 151.019 170.320 1.00 19.39 ?  491 PHE B C     1 
ATOM   9479  O  O     . PHE B 1 491 ? 120.430 151.992 169.983 1.00 28.67 ?  491 PHE B O     1 
ATOM   9480  C  CB    . PHE B 1 491 ? 120.640 149.271 171.876 1.00 25.23 ?  491 PHE B CB    1 
ATOM   9481  C  CG    . PHE B 1 491 ? 121.998 149.414 171.248 1.00 23.98 ?  491 PHE B CG    1 
ATOM   9482  C  CD1   . PHE B 1 491 ? 123.049 149.958 171.964 1.00 19.94 ?  491 PHE B CD1   1 
ATOM   9483  C  CD2   . PHE B 1 491 ? 122.227 148.998 169.946 1.00 19.44 ?  491 PHE B CD2   1 
ATOM   9484  C  CE1   . PHE B 1 491 ? 124.298 150.093 171.395 1.00 16.87 ?  491 PHE B CE1   1 
ATOM   9485  C  CE2   . PHE B 1 491 ? 123.472 149.134 169.371 1.00 17.20 ?  491 PHE B CE2   1 
ATOM   9486  C  CZ    . PHE B 1 491 ? 124.509 149.682 170.098 1.00 23.78 ?  491 PHE B CZ    1 
ATOM   9487  N  N     . PHE B 1 492 ? 118.966 150.374 169.454 1.00 17.42 ?  492 PHE B N     1 
ATOM   9488  C  CA    . PHE B 1 492 ? 118.945 150.786 168.063 1.00 12.24 ?  492 PHE B CA    1 
ATOM   9489  C  C     . PHE B 1 492 ? 118.097 152.027 167.832 1.00 13.03 ?  492 PHE B C     1 
ATOM   9490  O  O     . PHE B 1 492 ? 118.364 152.765 166.883 1.00 24.31 ?  492 PHE B O     1 
ATOM   9491  C  CB    . PHE B 1 492 ? 118.486 149.622 167.189 1.00 17.91 ?  492 PHE B CB    1 
ATOM   9492  C  CG    . PHE B 1 492 ? 119.536 148.560 167.026 1.00 20.42 ?  492 PHE B CG    1 
ATOM   9493  C  CD1   . PHE B 1 492 ? 120.616 148.763 166.185 1.00 14.94 ?  492 PHE B CD1   1 
ATOM   9494  C  CD2   . PHE B 1 492 ? 119.466 147.379 167.742 1.00 19.18 ?  492 PHE B CD2   1 
ATOM   9495  C  CE1   . PHE B 1 492 ? 121.592 147.797 166.045 1.00 10.03 ?  492 PHE B CE1   1 
ATOM   9496  C  CE2   . PHE B 1 492 ? 120.438 146.411 167.607 1.00 15.06 ?  492 PHE B CE2   1 
ATOM   9497  C  CZ    . PHE B 1 492 ? 121.502 146.620 166.757 1.00 15.00 ?  492 PHE B CZ    1 
ATOM   9498  N  N     . MET B 1 493 ? 117.120 152.311 168.700 1.00 16.96 ?  493 MET B N     1 
ATOM   9499  C  CA    . MET B 1 493 ? 116.486 153.623 168.654 1.00 17.53 ?  493 MET B CA    1 
ATOM   9500  C  C     . MET B 1 493 ? 117.484 154.715 169.015 1.00 17.63 ?  493 MET B C     1 
ATOM   9501  O  O     . MET B 1 493 ? 117.501 155.776 168.386 1.00 26.01 ?  493 MET B O     1 
ATOM   9502  C  CB    . MET B 1 493 ? 115.265 153.652 169.578 1.00 17.60 ?  493 MET B CB    1 
ATOM   9503  C  CG    . MET B 1 493 ? 114.683 155.037 169.873 1.00 20.72 ?  493 MET B CG    1 
ATOM   9504  S  SD    . MET B 1 493 ? 115.513 155.972 171.176 1.00 30.63 ?  493 MET B SD    1 
ATOM   9505  C  CE    . MET B 1 493 ? 115.383 154.821 172.538 1.00 24.03 ?  493 MET B CE    1 
ATOM   9506  N  N     . MET B 1 494 ? 118.326 154.470 170.024 1.00 21.86 ?  494 MET B N     1 
ATOM   9507  C  CA    . MET B 1 494 ? 119.385 155.423 170.355 1.00 16.39 ?  494 MET B CA    1 
ATOM   9508  C  C     . MET B 1 494 ? 120.356 155.600 169.194 1.00 19.03 ?  494 MET B C     1 
ATOM   9509  O  O     . MET B 1 494 ? 120.763 156.726 168.876 1.00 22.87 ?  494 MET B O     1 
ATOM   9510  C  CB    . MET B 1 494 ? 120.139 154.959 171.602 1.00 20.19 ?  494 MET B CB    1 
ATOM   9511  C  CG    . MET B 1 494 ? 119.313 154.908 172.873 1.00 20.19 ?  494 MET B CG    1 
ATOM   9512  S  SD    . MET B 1 494 ? 120.355 154.952 174.343 1.00 37.53 ?  494 MET B SD    1 
ATOM   9513  C  CE    . MET B 1 494 ? 120.852 156.669 174.363 1.00 30.33 ?  494 MET B CE    1 
ATOM   9514  N  N     . VAL B 1 495 ? 120.746 154.494 168.560 1.00 19.01 ?  495 VAL B N     1 
ATOM   9515  C  CA    . VAL B 1 495 ? 121.664 154.562 167.427 1.00 17.66 ?  495 VAL B CA    1 
ATOM   9516  C  C     . VAL B 1 495 ? 121.047 155.362 166.288 1.00 17.55 ?  495 VAL B C     1 
ATOM   9517  O  O     . VAL B 1 495 ? 121.706 156.215 165.687 1.00 28.72 ?  495 VAL B O     1 
ATOM   9518  C  CB    . VAL B 1 495 ? 122.063 153.145 166.975 1.00 15.28 ?  495 VAL B CB    1 
ATOM   9519  C  CG1   . VAL B 1 495 ? 122.788 153.195 165.640 1.00 10.14 ?  495 VAL B CG1   1 
ATOM   9520  C  CG2   . VAL B 1 495 ? 122.933 152.481 168.024 1.00 19.24 ?  495 VAL B CG2   1 
ATOM   9521  N  N     . ASN B 1 496 ? 119.774 155.105 165.977 1.00 19.18 ?  496 ASN B N     1 
ATOM   9522  C  CA    . ASN B 1 496 ? 119.098 155.855 164.925 1.00 12.13 ?  496 ASN B CA    1 
ATOM   9523  C  C     . ASN B 1 496 ? 118.986 157.330 165.279 1.00 19.26 ?  496 ASN B C     1 
ATOM   9524  O  O     . ASN B 1 496 ? 119.200 158.199 164.426 1.00 30.91 ?  496 ASN B O     1 
ATOM   9525  C  CB    . ASN B 1 496 ? 117.713 155.262 164.666 1.00 16.23 ?  496 ASN B CB    1 
ATOM   9526  C  CG    . ASN B 1 496 ? 117.134 155.696 163.338 1.00 16.08 ?  496 ASN B CG    1 
ATOM   9527  O  OD1   . ASN B 1 496 ? 117.866 155.964 162.387 1.00 24.74 ?  496 ASN B OD1   1 
ATOM   9528  N  ND2   . ASN B 1 496 ? 115.811 155.773 163.267 1.00 15.35 ?  496 ASN B ND2   1 
ATOM   9529  N  N     . PHE B 1 497 ? 118.654 157.634 166.535 1.00 20.27 ?  497 PHE B N     1 
ATOM   9530  C  CA    . PHE B 1 497 ? 118.528 159.021 166.965 1.00 15.60 ?  497 PHE B CA    1 
ATOM   9531  C  C     . PHE B 1 497 ? 119.841 159.765 166.785 1.00 19.24 ?  497 PHE B C     1 
ATOM   9532  O  O     . PHE B 1 497 ? 119.877 160.857 166.208 1.00 26.32 ?  497 PHE B O     1 
ATOM   9533  C  CB    . PHE B 1 497 ? 118.077 159.069 168.426 1.00 17.84 ?  497 PHE B CB    1 
ATOM   9534  C  CG    . PHE B 1 497 ? 117.965 160.457 168.990 1.00 20.97 ?  497 PHE B CG    1 
ATOM   9535  C  CD1   . PHE B 1 497 ? 119.052 161.064 169.600 1.00 21.66 ?  497 PHE B CD1   1 
ATOM   9536  C  CD2   . PHE B 1 497 ? 116.771 161.152 168.920 1.00 21.23 ?  497 PHE B CD2   1 
ATOM   9537  C  CE1   . PHE B 1 497 ? 118.949 162.338 170.118 1.00 22.63 ?  497 PHE B CE1   1 
ATOM   9538  C  CE2   . PHE B 1 497 ? 116.664 162.426 169.438 1.00 20.87 ?  497 PHE B CE2   1 
ATOM   9539  C  CZ    . PHE B 1 497 ? 117.755 163.019 170.038 1.00 23.33 ?  497 PHE B CZ    1 
ATOM   9540  N  N     . TYR B 1 498 ? 120.938 159.179 167.260 1.00 26.89 ?  498 TYR B N     1 
ATOM   9541  C  CA    . TYR B 1 498 ? 122.213 159.878 167.186 1.00 18.43 ?  498 TYR B CA    1 
ATOM   9542  C  C     . TYR B 1 498 ? 122.779 159.884 165.772 1.00 18.27 ?  498 TYR B C     1 
ATOM   9543  O  O     . TYR B 1 498 ? 123.478 160.831 165.401 1.00 26.71 ?  498 TYR B O     1 
ATOM   9544  C  CB    . TYR B 1 498 ? 123.197 159.270 168.183 1.00 18.97 ?  498 TYR B CB    1 
ATOM   9545  C  CG    . TYR B 1 498 ? 122.829 159.608 169.609 1.00 22.61 ?  498 TYR B CG    1 
ATOM   9546  C  CD1   . TYR B 1 498 ? 122.713 160.931 170.016 1.00 23.34 ?  498 TYR B CD1   1 
ATOM   9547  C  CD2   . TYR B 1 498 ? 122.571 158.611 170.540 1.00 26.29 ?  498 TYR B CD2   1 
ATOM   9548  C  CE1   . TYR B 1 498 ? 122.365 161.251 171.311 1.00 24.09 ?  498 TYR B CE1   1 
ATOM   9549  C  CE2   . TYR B 1 498 ? 122.222 158.923 171.839 1.00 25.24 ?  498 TYR B CE2   1 
ATOM   9550  C  CZ    . TYR B 1 498 ? 122.120 160.244 172.219 1.00 29.24 ?  498 TYR B CZ    1 
ATOM   9551  O  OH    . TYR B 1 498 ? 121.776 160.563 173.511 1.00 35.73 ?  498 TYR B OH    1 
ATOM   9552  N  N     . SER B 1 499 ? 122.457 158.879 164.955 1.00 19.26 ?  499 SER B N     1 
ATOM   9553  C  CA    . SER B 1 499 ? 122.858 158.913 163.554 1.00 13.36 ?  499 SER B CA    1 
ATOM   9554  C  C     . SER B 1 499 ? 122.126 160.015 162.800 1.00 18.33 ?  499 SER B C     1 
ATOM   9555  O  O     . SER B 1 499 ? 122.735 160.738 162.005 1.00 20.27 ?  499 SER B O     1 
ATOM   9556  C  CB    . SER B 1 499 ? 122.606 157.553 162.904 1.00 14.93 ?  499 SER B CB    1 
ATOM   9557  O  OG    . SER B 1 499 ? 123.334 157.425 161.696 1.00 19.27 ?  499 SER B OG    1 
ATOM   9558  N  N     . ILE B 1 500 ? 120.821 160.165 163.044 1.00 18.14 ?  500 ILE B N     1 
ATOM   9559  C  CA    . ILE B 1 500 ? 120.066 161.251 162.426 1.00 20.90 ?  500 ILE B CA    1 
ATOM   9560  C  C     . ILE B 1 500 ? 120.585 162.596 162.911 1.00 19.50 ?  500 ILE B C     1 
ATOM   9561  O  O     . ILE B 1 500 ? 120.708 163.549 162.131 1.00 26.97 ?  500 ILE B O     1 
ATOM   9562  C  CB    . ILE B 1 500 ? 118.562 161.089 162.711 1.00 23.62 ?  500 ILE B CB    1 
ATOM   9563  C  CG1   . ILE B 1 500 ? 118.010 159.856 162.001 1.00 18.38 ?  500 ILE B CG1   1 
ATOM   9564  C  CG2   . ILE B 1 500 ? 117.793 162.323 162.277 1.00 18.21 ?  500 ILE B CG2   1 
ATOM   9565  C  CD1   . ILE B 1 500 ? 116.658 159.439 162.501 1.00 22.35 ?  500 ILE B CD1   1 
ATOM   9566  N  N     . GLN B 1 501 ? 120.894 162.698 164.205 1.00 20.82 ?  501 GLN B N     1 
ATOM   9567  C  CA    . GLN B 1 501 ? 121.425 163.945 164.742 1.00 22.83 ?  501 GLN B CA    1 
ATOM   9568  C  C     . GLN B 1 501 ? 122.760 164.298 164.098 1.00 24.83 ?  501 GLN B C     1 
ATOM   9569  O  O     . GLN B 1 501 ? 122.983 165.452 163.718 1.00 30.68 ?  501 GLN B O     1 
ATOM   9570  C  CB    . GLN B 1 501 ? 121.567 163.843 166.259 1.00 27.35 ?  501 GLN B CB    1 
ATOM   9571  C  CG    . GLN B 1 501 ? 121.519 165.181 166.973 1.00 24.19 ?  501 GLN B CG    1 
ATOM   9572  C  CD    . GLN B 1 501 ? 121.384 165.032 168.472 1.00 28.90 ?  501 GLN B CD    1 
ATOM   9573  O  OE1   . GLN B 1 501 ? 122.128 164.284 169.104 1.00 34.53 ?  501 GLN B OE1   1 
ATOM   9574  N  NE2   . GLN B 1 501 ? 120.427 165.746 169.053 1.00 31.97 ?  501 GLN B NE2   1 
ATOM   9575  N  N     . ARG B 1 502 ? 123.656 163.319 163.960 1.00 23.90 ?  502 ARG B N     1 
ATOM   9576  C  CA    . ARG B 1 502 ? 124.941 163.581 163.322 1.00 20.10 ?  502 ARG B CA    1 
ATOM   9577  C  C     . ARG B 1 502 ? 124.772 163.932 161.849 1.00 22.90 ?  502 ARG B C     1 
ATOM   9578  O  O     . ARG B 1 502 ? 125.475 164.806 161.335 1.00 30.30 ?  502 ARG B O     1 
ATOM   9579  C  CB    . ARG B 1 502 ? 125.870 162.380 163.481 1.00 23.30 ?  502 ARG B CB    1 
ATOM   9580  C  CG    . ARG B 1 502 ? 127.317 162.694 163.143 1.00 26.41 ?  502 ARG B CG    1 
ATOM   9581  C  CD    . ARG B 1 502 ? 127.776 163.961 163.842 1.00 26.01 ?  502 ARG B CD    1 
ATOM   9582  N  NE    . ARG B 1 502 ? 129.049 164.442 163.320 1.00 24.91 ?  502 ARG B NE    1 
ATOM   9583  C  CZ    . ARG B 1 502 ? 129.370 165.722 163.193 1.00 23.93 ?  502 ARG B CZ    1 
ATOM   9584  N  NH1   . ARG B 1 502 ? 128.535 166.683 163.551 1.00 30.63 1  502 ARG B NH1   1 
ATOM   9585  N  NH2   . ARG B 1 502 ? 130.559 166.046 162.693 1.00 28.82 ?  502 ARG B NH2   1 
ATOM   9586  N  N     . SER B 1 503 ? 123.857 163.256 161.152 1.00 23.38 ?  503 SER B N     1 
ATOM   9587  C  CA    . SER B 1 503 ? 123.618 163.577 159.748 1.00 22.11 ?  503 SER B CA    1 
ATOM   9588  C  C     . SER B 1 503 ? 123.108 165.004 159.594 1.00 23.05 ?  503 SER B C     1 
ATOM   9589  O  O     . SER B 1 503 ? 123.564 165.746 158.716 1.00 28.92 ?  503 SER B O     1 
ATOM   9590  C  CB    . SER B 1 503 ? 122.628 162.580 159.148 1.00 18.74 ?  503 SER B CB    1 
ATOM   9591  O  OG    . SER B 1 503 ? 122.785 162.478 157.745 1.00 24.69 ?  503 SER B OG    1 
ATOM   9592  N  N     . ALA B 1 504 ? 122.178 165.413 160.459 1.00 23.24 ?  504 ALA B N     1 
ATOM   9593  C  CA    . ALA B 1 504 ? 121.667 166.778 160.410 1.00 25.89 ?  504 ALA B CA    1 
ATOM   9594  C  C     . ALA B 1 504 ? 122.744 167.789 160.783 1.00 27.48 ?  504 ALA B C     1 
ATOM   9595  O  O     . ALA B 1 504 ? 122.807 168.877 160.201 1.00 34.08 ?  504 ALA B O     1 
ATOM   9596  C  CB    . ALA B 1 504 ? 120.454 166.913 161.328 1.00 26.38 ?  504 ALA B CB    1 
ATOM   9597  N  N     . GLU B 1 505 ? 123.604 167.449 161.746 1.00 25.13 ?  505 GLU B N     1 
ATOM   9598  C  CA    . GLU B 1 505 ? 124.689 168.350 162.124 1.00 25.65 ?  505 GLU B CA    1 
ATOM   9599  C  C     . GLU B 1 505 ? 125.698 168.510 160.994 1.00 26.97 ?  505 GLU B C     1 
ATOM   9600  O  O     . GLU B 1 505 ? 126.205 169.612 160.761 1.00 31.65 ?  505 GLU B O     1 
ATOM   9601  C  CB    . GLU B 1 505 ? 125.376 167.840 163.390 1.00 26.13 ?  505 GLU B CB    1 
ATOM   9602  C  CG    . GLU B 1 505 ? 124.575 168.059 164.660 1.00 27.47 ?  505 GLU B CG    1 
ATOM   9603  C  CD    . GLU B 1 505 ? 125.010 167.145 165.784 1.00 32.39 ?  505 GLU B CD    1 
ATOM   9604  O  OE1   . GLU B 1 505 ? 125.987 166.391 165.593 1.00 31.08 ?  505 GLU B OE1   1 
ATOM   9605  O  OE2   . GLU B 1 505 ? 124.378 167.179 166.860 1.00 34.66 -1 505 GLU B OE2   1 
ATOM   9606  N  N     . ILE B 1 506 ? 126.008 167.422 160.288 1.00 26.20 ?  506 ILE B N     1 
ATOM   9607  C  CA    . ILE B 1 506 ? 126.895 167.509 159.132 1.00 26.19 ?  506 ILE B CA    1 
ATOM   9608  C  C     . ILE B 1 506 ? 126.254 168.342 158.031 1.00 26.67 ?  506 ILE B C     1 
ATOM   9609  O  O     . ILE B 1 506 ? 126.921 169.156 157.381 1.00 33.16 ?  506 ILE B O     1 
ATOM   9610  C  CB    . ILE B 1 506 ? 127.272 166.101 158.637 1.00 25.49 ?  506 ILE B CB    1 
ATOM   9611  C  CG1   . ILE B 1 506 ? 128.077 165.357 159.702 1.00 28.34 ?  506 ILE B CG1   1 
ATOM   9612  C  CG2   . ILE B 1 506 ? 128.068 166.179 157.348 1.00 24.77 ?  506 ILE B CG2   1 
ATOM   9613  C  CD1   . ILE B 1 506 ? 128.238 163.881 159.424 1.00 21.69 ?  506 ILE B CD1   1 
ATOM   9614  N  N     . ALA B 1 507 ? 124.951 168.158 157.803 1.00 26.64 ?  507 ALA B N     1 
ATOM   9615  C  CA    . ALA B 1 507 ? 124.253 168.970 156.811 1.00 28.48 ?  507 ALA B CA    1 
ATOM   9616  C  C     . ALA B 1 507 ? 124.290 170.447 157.184 1.00 32.25 ?  507 ALA B C     1 
ATOM   9617  O  O     . ALA B 1 507 ? 124.442 171.312 156.315 1.00 36.65 ?  507 ALA B O     1 
ATOM   9618  C  CB    . ALA B 1 507 ? 122.811 168.489 156.662 1.00 24.25 ?  507 ALA B CB    1 
ATOM   9619  N  N     . LYS B 1 508 ? 124.143 170.751 158.475 1.00 32.69 ?  508 LYS B N     1 
ATOM   9620  C  CA    . LYS B 1 508 ? 124.209 172.135 158.933 1.00 30.69 ?  508 LYS B CA    1 
ATOM   9621  C  C     . LYS B 1 508 ? 125.610 172.713 158.769 1.00 36.95 ?  508 LYS B C     1 
ATOM   9622  O  O     . LYS B 1 508 ? 125.769 173.852 158.315 1.00 43.58 ?  508 LYS B O     1 
ATOM   9623  C  CB    . LYS B 1 508 ? 123.764 172.214 160.393 1.00 34.62 ?  508 LYS B CB    1 
ATOM   9624  C  CG    . LYS B 1 508 ? 123.911 173.585 161.027 1.00 35.60 ?  508 LYS B CG    1 
ATOM   9625  C  CD    . LYS B 1 508 ? 123.717 173.506 162.532 1.00 34.74 ?  508 LYS B CD    1 
ATOM   9626  C  CE    . LYS B 1 508 ? 123.559 174.885 163.147 1.00 36.44 ?  508 LYS B CE    1 
ATOM   9627  N  NZ    . LYS B 1 508 ? 122.707 174.851 164.367 1.00 38.05 1  508 LYS B NZ    1 
ATOM   9628  N  N     . GLU B 1 509 ? 126.637 171.941 159.132 1.00 34.40 ?  509 GLU B N     1 
ATOM   9629  C  CA    . GLU B 1 509 ? 128.004 172.450 159.087 1.00 35.15 ?  509 GLU B CA    1 
ATOM   9630  C  C     . GLU B 1 509 ? 128.516 172.577 157.658 1.00 36.28 ?  509 GLU B C     1 
ATOM   9631  O  O     . GLU B 1 509 ? 129.394 173.404 157.389 1.00 39.64 ?  509 GLU B O     1 
ATOM   9632  C  CB    . GLU B 1 509 ? 128.922 171.548 159.916 1.00 35.08 ?  509 GLU B CB    1 
ATOM   9633  C  CG    . GLU B 1 509 ? 129.712 170.529 159.112 1.00 32.91 ?  509 GLU B CG    1 
ATOM   9634  C  CD    . GLU B 1 509 ? 130.215 169.379 159.963 1.00 41.57 ?  509 GLU B CD    1 
ATOM   9635  O  OE1   . GLU B 1 509 ? 130.102 169.461 161.204 1.00 40.77 ?  509 GLU B OE1   1 
ATOM   9636  O  OE2   . GLU B 1 509 ? 130.721 168.391 159.390 1.00 40.46 -1 509 GLU B OE2   1 
ATOM   9637  N  N     . LYS B 1 510 ? 127.987 171.777 156.733 1.00 32.33 ?  510 LYS B N     1 
ATOM   9638  C  CA    . LYS B 1 510 ? 128.380 171.854 155.334 1.00 31.26 ?  510 LYS B CA    1 
ATOM   9639  C  C     . LYS B 1 510 ? 127.388 172.627 154.477 1.00 35.37 ?  510 LYS B C     1 
ATOM   9640  O  O     . LYS B 1 510 ? 127.691 172.911 153.314 1.00 39.87 ?  510 LYS B O     1 
ATOM   9641  C  CB    . LYS B 1 510 ? 128.561 170.444 154.756 1.00 30.84 ?  510 LYS B CB    1 
ATOM   9642  C  CG    . LYS B 1 510 ? 129.546 169.588 155.528 1.00 32.21 ?  510 LYS B CG    1 
ATOM   9643  C  CD    . LYS B 1 510 ? 129.980 168.377 154.725 1.00 31.73 ?  510 LYS B CD    1 
ATOM   9644  C  CE    . LYS B 1 510 ? 131.057 167.593 155.455 1.00 33.69 ?  510 LYS B CE    1 
ATOM   9645  N  NZ    . LYS B 1 510 ? 132.049 167.007 154.516 1.00 32.53 1  510 LYS B NZ    1 
ATOM   9646  N  N     . GLY B 1 511 ? 126.222 172.973 155.019 1.00 32.71 ?  511 GLY B N     1 
ATOM   9647  C  CA    . GLY B 1 511 ? 125.228 173.702 154.261 1.00 32.43 ?  511 GLY B CA    1 
ATOM   9648  C  C     . GLY B 1 511 ? 124.604 172.937 153.118 1.00 36.03 ?  511 GLY B C     1 
ATOM   9649  O  O     . GLY B 1 511 ? 123.937 173.546 152.277 1.00 39.42 ?  511 GLY B O     1 
ATOM   9650  N  N     . GLU B 1 512 ? 124.799 171.622 153.057 1.00 33.04 ?  512 GLU B N     1 
ATOM   9651  C  CA    . GLU B 1 512 ? 124.281 170.805 151.971 1.00 29.38 ?  512 GLU B CA    1 
ATOM   9652  C  C     . GLU B 1 512 ? 123.665 169.530 152.524 1.00 31.47 ?  512 GLU B C     1 
ATOM   9653  O  O     . GLU B 1 512 ? 124.161 168.958 153.499 1.00 32.91 ?  512 GLU B O     1 
ATOM   9654  C  CB    . GLU B 1 512 ? 125.383 170.455 150.962 1.00 31.29 ?  512 GLU B CB    1 
ATOM   9655  C  CG    . GLU B 1 512 ? 126.620 169.830 151.580 1.00 31.45 ?  512 GLU B CG    1 
ATOM   9656  C  CD    . GLU B 1 512 ? 127.397 168.979 150.594 1.00 36.04 ?  512 GLU B CD    1 
ATOM   9657  O  OE1   . GLU B 1 512 ? 126.765 168.370 149.707 1.00 32.30 ?  512 GLU B OE1   1 
ATOM   9658  O  OE2   . GLU B 1 512 ? 128.640 168.918 150.708 1.00 36.73 -1 512 GLU B OE2   1 
ATOM   9659  N  N     . THR B 1 513 ? 122.578 169.097 151.899 1.00 31.96 ?  513 THR B N     1 
ATOM   9660  C  CA    . THR B 1 513 ? 121.927 167.830 152.186 1.00 26.26 ?  513 THR B CA    1 
ATOM   9661  C  C     . THR B 1 513 ? 122.195 166.862 151.038 1.00 27.02 ?  513 THR B C     1 
ATOM   9662  O  O     . THR B 1 513 ? 122.864 167.197 150.058 1.00 34.08 ?  513 THR B O     1 
ATOM   9663  C  CB    . THR B 1 513 ? 120.425 168.032 152.401 1.00 27.27 ?  513 THR B CB    1 
ATOM   9664  O  OG1   . THR B 1 513 ? 119.830 168.515 151.191 1.00 29.20 ?  513 THR B OG1   1 
ATOM   9665  C  CG2   . THR B 1 513 ? 120.181 169.039 153.510 1.00 24.46 ?  513 THR B CG2   1 
ATOM   9666  N  N     . PHE B 1 514 ? 121.669 165.648 151.162 1.00 21.67 ?  514 PHE B N     1 
ATOM   9667  C  CA    . PHE B 1 514 ? 121.781 164.725 150.047 1.00 22.78 ?  514 PHE B CA    1 
ATOM   9668  C  C     . PHE B 1 514 ? 120.790 165.107 148.953 1.00 22.05 ?  514 PHE B C     1 
ATOM   9669  O  O     . PHE B 1 514 ? 119.794 165.794 149.195 1.00 26.25 ?  514 PHE B O     1 
ATOM   9670  C  CB    . PHE B 1 514 ? 121.568 163.276 150.499 1.00 19.13 ?  514 PHE B CB    1 
ATOM   9671  C  CG    . PHE B 1 514 ? 120.187 162.981 151.016 1.00 19.25 ?  514 PHE B CG    1 
ATOM   9672  C  CD1   . PHE B 1 514 ? 119.879 163.161 152.352 1.00 17.52 ?  514 PHE B CD1   1 
ATOM   9673  C  CD2   . PHE B 1 514 ? 119.205 162.490 150.169 1.00 19.76 ?  514 PHE B CD2   1 
ATOM   9674  C  CE1   . PHE B 1 514 ? 118.617 162.874 152.830 1.00 20.16 ?  514 PHE B CE1   1 
ATOM   9675  C  CE2   . PHE B 1 514 ? 117.943 162.204 150.642 1.00 14.93 ?  514 PHE B CE2   1 
ATOM   9676  C  CZ    . PHE B 1 514 ? 117.648 162.397 151.975 1.00 21.93 ?  514 PHE B CZ    1 
ATOM   9677  N  N     . ASP B 1 515 ? 121.084 164.666 147.734 1.00 25.10 ?  515 ASP B N     1 
ATOM   9678  C  CA    . ASP B 1 515 ? 120.277 165.057 146.589 1.00 26.53 ?  515 ASP B CA    1 
ATOM   9679  C  C     . ASP B 1 515 ? 118.845 164.563 146.740 1.00 31.04 ?  515 ASP B C     1 
ATOM   9680  O  O     . ASP B 1 515 ? 118.602 163.429 147.162 1.00 40.44 ?  515 ASP B O     1 
ATOM   9681  C  CB    . ASP B 1 515 ? 120.889 164.515 145.298 1.00 29.27 ?  515 ASP B CB    1 
ATOM   9682  C  CG    . ASP B 1 515 ? 121.910 165.459 144.698 1.00 33.63 ?  515 ASP B CG    1 
ATOM   9683  O  OD1   . ASP B 1 515 ? 122.380 166.364 145.419 1.00 32.53 ?  515 ASP B OD1   1 
ATOM   9684  O  OD2   . ASP B 1 515 ? 122.242 165.298 143.506 1.00 38.46 -1 515 ASP B OD2   1 
ATOM   9685  N  N     . GLN B 1 516 ? 117.896 165.436 146.396 1.00 28.92 ?  516 GLN B N     1 
ATOM   9686  C  CA    . GLN B 1 516 ? 116.465 165.147 146.489 1.00 26.49 ?  516 GLN B CA    1 
ATOM   9687  C  C     . GLN B 1 516 ? 116.036 164.849 147.923 1.00 27.05 ?  516 GLN B C     1 
ATOM   9688  O  O     . GLN B 1 516 ? 115.125 164.053 148.153 1.00 32.99 ?  516 GLN B O     1 
ATOM   9689  C  CB    . GLN B 1 516 ? 116.066 163.994 145.565 1.00 26.22 ?  516 GLN B CB    1 
ATOM   9690  C  CG    . GLN B 1 516 ? 116.384 164.219 144.100 1.00 29.62 ?  516 GLN B CG    1 
ATOM   9691  C  CD    . GLN B 1 516 ? 116.199 162.964 143.272 1.00 32.34 ?  516 GLN B CD    1 
ATOM   9692  O  OE1   . GLN B 1 516 ? 115.074 162.548 142.997 1.00 29.80 ?  516 GLN B OE1   1 
ATOM   9693  N  NE2   . GLN B 1 516 ? 117.306 162.350 142.873 1.00 32.48 ?  516 GLN B NE2   1 
ATOM   9694  N  N     . TYR B 1 517 ? 116.686 165.482 148.901 1.00 24.80 ?  517 TYR B N     1 
ATOM   9695  C  CA    . TYR B 1 517 ? 116.269 165.298 150.287 1.00 22.80 ?  517 TYR B CA    1 
ATOM   9696  C  C     . TYR B 1 517 ? 114.899 165.911 150.546 1.00 29.59 ?  517 TYR B C     1 
ATOM   9697  O  O     . TYR B 1 517 ? 114.161 165.432 151.415 1.00 35.82 ?  517 TYR B O     1 
ATOM   9698  C  CB    . TYR B 1 517 ? 117.306 165.898 151.240 1.00 18.52 ?  517 TYR B CB    1 
ATOM   9699  C  CG    . TYR B 1 517 ? 116.715 166.398 152.540 1.00 28.00 ?  517 TYR B CG    1 
ATOM   9700  C  CD1   . TYR B 1 517 ? 116.458 165.525 153.589 1.00 23.79 ?  517 TYR B CD1   1 
ATOM   9701  C  CD2   . TYR B 1 517 ? 116.407 167.742 152.714 1.00 29.52 ?  517 TYR B CD2   1 
ATOM   9702  C  CE1   . TYR B 1 517 ? 115.913 165.976 154.774 1.00 27.50 ?  517 TYR B CE1   1 
ATOM   9703  C  CE2   . TYR B 1 517 ? 115.860 168.199 153.894 1.00 24.93 ?  517 TYR B CE2   1 
ATOM   9704  C  CZ    . TYR B 1 517 ? 115.614 167.313 154.920 1.00 27.75 ?  517 TYR B CZ    1 
ATOM   9705  O  OH    . TYR B 1 517 ? 115.072 167.768 156.098 1.00 36.93 ?  517 TYR B OH    1 
ATOM   9706  N  N     . GLU B 1 518 ? 114.538 166.957 149.799 1.00 28.16 ?  518 GLU B N     1 
ATOM   9707  C  CA    . GLU B 1 518 ? 113.315 167.700 150.085 1.00 30.08 ?  518 GLU B CA    1 
ATOM   9708  C  C     . GLU B 1 518 ? 112.070 166.837 149.923 1.00 34.42 ?  518 GLU B C     1 
ATOM   9709  O  O     . GLU B 1 518 ? 111.074 167.055 150.623 1.00 35.10 ?  518 GLU B O     1 
ATOM   9710  C  CB    . GLU B 1 518 ? 113.225 168.933 149.185 1.00 29.58 ?  518 GLU B CB    1 
ATOM   9711  C  CG    . GLU B 1 518 ? 114.347 169.945 149.384 1.00 34.09 ?  518 GLU B CG    1 
ATOM   9712  C  CD    . GLU B 1 518 ? 115.642 169.534 148.705 1.00 41.01 ?  518 GLU B CD    1 
ATOM   9713  O  OE1   . GLU B 1 518 ? 115.576 168.867 147.651 1.00 38.63 ?  518 GLU B OE1   1 
ATOM   9714  O  OE2   . GLU B 1 518 ? 116.724 169.878 149.226 1.00 38.53 -1 518 GLU B OE2   1 
ATOM   9715  N  N     . GLY B 1 519 ? 112.098 165.869 149.014 1.00 23.98 ?  519 GLY B N     1 
ATOM   9716  C  CA    . GLY B 1 519 ? 110.991 164.956 148.842 1.00 20.26 ?  519 GLY B CA    1 
ATOM   9717  C  C     . GLY B 1 519 ? 110.986 163.768 149.771 1.00 19.74 ?  519 GLY B C     1 
ATOM   9718  O  O     . GLY B 1 519 ? 110.034 162.981 149.750 1.00 28.28 ?  519 GLY B O     1 
ATOM   9719  N  N     . SER B 1 520 ? 112.020 163.610 150.591 1.00 21.17 ?  520 SER B N     1 
ATOM   9720  C  CA    . SER B 1 520 ? 112.129 162.464 151.477 1.00 22.77 ?  520 SER B CA    1 
ATOM   9721  C  C     . SER B 1 520 ? 111.218 162.624 152.689 1.00 22.36 ?  520 SER B C     1 
ATOM   9722  O  O     . SER B 1 520 ? 110.731 163.715 152.999 1.00 24.18 ?  520 SER B O     1 
ATOM   9723  C  CB    . SER B 1 520 ? 113.576 162.272 151.931 1.00 18.69 ?  520 SER B CB    1 
ATOM   9724  O  OG    . SER B 1 520 ? 114.024 163.382 152.685 1.00 23.96 ?  520 SER B OG    1 
ATOM   9725  N  N     . THR B 1 521 ? 110.987 161.504 153.378 1.00 21.97 ?  521 THR B N     1 
ATOM   9726  C  CA    . THR B 1 521 ? 110.192 161.533 154.598 1.00 18.95 ?  521 THR B CA    1 
ATOM   9727  C  C     . THR B 1 521 ? 110.925 162.217 155.743 1.00 25.21 ?  521 THR B C     1 
ATOM   9728  O  O     . THR B 1 521 ? 110.288 162.597 156.730 1.00 26.86 ?  521 THR B O     1 
ATOM   9729  C  CB    . THR B 1 521 ? 109.795 160.114 155.004 1.00 24.09 ?  521 THR B CB    1 
ATOM   9730  O  OG1   . THR B 1 521 ? 110.938 159.422 155.520 1.00 29.44 ?  521 THR B OG1   1 
ATOM   9731  C  CG2   . THR B 1 521 ? 109.250 159.354 153.810 1.00 15.63 ?  521 THR B CG2   1 
ATOM   9732  N  N     . TYR B 1 522 ? 112.247 162.374 155.639 1.00 25.01 ?  522 TYR B N     1 
ATOM   9733  C  CA    . TYR B 1 522 ? 112.973 163.174 156.619 1.00 20.83 ?  522 TYR B CA    1 
ATOM   9734  C  C     . TYR B 1 522 ? 112.568 164.639 156.536 1.00 25.33 ?  522 TYR B C     1 
ATOM   9735  O  O     . TYR B 1 522 ? 112.394 165.303 157.563 1.00 24.25 ?  522 TYR B O     1 
ATOM   9736  C  CB    . TYR B 1 522 ? 114.480 163.030 156.408 1.00 18.01 ?  522 TYR B CB    1 
ATOM   9737  C  CG    . TYR B 1 522 ? 115.021 161.640 156.647 1.00 24.21 ?  522 TYR B CG    1 
ATOM   9738  C  CD1   . TYR B 1 522 ? 114.990 161.067 157.911 1.00 24.70 ?  522 TYR B CD1   1 
ATOM   9739  C  CD2   . TYR B 1 522 ? 115.580 160.907 155.610 1.00 22.12 ?  522 TYR B CD2   1 
ATOM   9740  C  CE1   . TYR B 1 522 ? 115.490 159.801 158.132 1.00 24.61 ?  522 TYR B CE1   1 
ATOM   9741  C  CE2   . TYR B 1 522 ? 116.084 159.641 155.822 1.00 20.99 ?  522 TYR B CE2   1 
ATOM   9742  C  CZ    . TYR B 1 522 ? 116.035 159.092 157.084 1.00 22.49 ?  522 TYR B CZ    1 
ATOM   9743  O  OH    . TYR B 1 522 ? 116.535 157.830 157.297 1.00 28.05 ?  522 TYR B OH    1 
ATOM   9744  N  N     . ALA B 1 523 ? 112.416 165.160 155.316 1.00 27.79 ?  523 ALA B N     1 
ATOM   9745  C  CA    . ALA B 1 523 ? 112.066 166.566 155.142 1.00 30.41 ?  523 ALA B CA    1 
ATOM   9746  C  C     . ALA B 1 523 ? 110.622 166.834 155.542 1.00 29.48 ?  523 ALA B C     1 
ATOM   9747  O  O     . ALA B 1 523 ? 110.321 167.871 156.145 1.00 28.29 ?  523 ALA B O     1 
ATOM   9748  C  CB    . ALA B 1 523 ? 112.310 166.990 153.696 1.00 27.66 ?  523 ALA B CB    1 
ATOM   9749  N  N     . THR B 1 524 ? 109.714 165.915 155.215 1.00 26.48 ?  524 THR B N     1 
ATOM   9750  C  CA    . THR B 1 524 ? 108.304 166.092 155.528 1.00 27.99 ?  524 THR B CA    1 
ATOM   9751  C  C     . THR B 1 524 ? 107.968 165.769 156.978 1.00 33.26 ?  524 THR B C     1 
ATOM   9752  O  O     . THR B 1 524 ? 106.856 166.079 157.420 1.00 38.05 ?  524 THR B O     1 
ATOM   9753  C  CB    . THR B 1 524 ? 107.444 165.223 154.604 1.00 28.49 ?  524 THR B CB    1 
ATOM   9754  O  OG1   . THR B 1 524 ? 107.643 163.841 154.922 1.00 32.57 ?  524 THR B OG1   1 
ATOM   9755  C  CG2   . THR B 1 524 ? 107.818 165.463 153.150 1.00 27.48 ?  524 THR B CG2   1 
ATOM   9756  N  N     . GLY B 1 525 ? 108.890 165.163 157.722 1.00 25.50 ?  525 GLY B N     1 
ATOM   9757  C  CA    . GLY B 1 525 ? 108.646 164.804 159.102 1.00 23.63 ?  525 GLY B CA    1 
ATOM   9758  C  C     . GLY B 1 525 ? 107.908 163.502 159.307 1.00 26.91 ?  525 GLY B C     1 
ATOM   9759  O  O     . GLY B 1 525 ? 107.677 163.116 160.459 1.00 31.03 ?  525 GLY B O     1 
ATOM   9760  N  N     . GLU B 1 526 ? 107.527 162.813 158.228 1.00 31.40 ?  526 GLU B N     1 
ATOM   9761  C  CA    . GLU B 1 526 ? 106.816 161.546 158.368 1.00 30.90 ?  526 GLU B CA    1 
ATOM   9762  C  C     . GLU B 1 526 ? 107.697 160.486 159.016 1.00 31.91 ?  526 GLU B C     1 
ATOM   9763  O  O     . GLU B 1 526 ? 107.218 159.676 159.819 1.00 36.63 ?  526 GLU B O     1 
ATOM   9764  C  CB    . GLU B 1 526 ? 106.318 161.081 156.999 1.00 29.22 ?  526 GLU B CB    1 
ATOM   9765  C  CG    . GLU B 1 526 ? 105.854 159.636 156.951 1.00 33.58 ?  526 GLU B CG    1 
ATOM   9766  C  CD    . GLU B 1 526 ? 105.754 159.105 155.535 1.00 39.33 ?  526 GLU B CD    1 
ATOM   9767  O  OE1   . GLU B 1 526 ? 105.292 159.854 154.649 1.00 39.85 ?  526 GLU B OE1   1 
ATOM   9768  O  OE2   . GLU B 1 526 ? 106.140 157.939 155.307 1.00 35.42 -1 526 GLU B OE2   1 
ATOM   9769  N  N     . TYR B 1 527 ? 108.994 160.489 158.690 1.00 33.11 ?  527 TYR B N     1 
ATOM   9770  C  CA    . TYR B 1 527 ? 109.909 159.478 159.210 1.00 22.71 ?  527 TYR B CA    1 
ATOM   9771  C  C     . TYR B 1 527 ? 109.901 159.439 160.732 1.00 25.58 ?  527 TYR B C     1 
ATOM   9772  O  O     . TYR B 1 527 ? 110.048 158.372 161.337 1.00 30.15 ?  527 TYR B O     1 
ATOM   9773  C  CB    . TYR B 1 527 ? 111.325 159.745 158.698 1.00 18.10 ?  527 TYR B CB    1 
ATOM   9774  C  CG    . TYR B 1 527 ? 112.350 158.746 159.184 1.00 26.66 ?  527 TYR B CG    1 
ATOM   9775  C  CD1   . TYR B 1 527 ? 112.595 157.580 158.473 1.00 26.45 ?  527 TYR B CD1   1 
ATOM   9776  C  CD2   . TYR B 1 527 ? 113.066 158.962 160.353 1.00 24.18 ?  527 TYR B CD2   1 
ATOM   9777  C  CE1   . TYR B 1 527 ? 113.524 156.662 158.908 1.00 23.64 ?  527 TYR B CE1   1 
ATOM   9778  C  CE2   . TYR B 1 527 ? 113.995 158.047 160.798 1.00 19.65 ?  527 TYR B CE2   1 
ATOM   9779  C  CZ    . TYR B 1 527 ? 114.221 156.900 160.071 1.00 20.98 ?  527 TYR B CZ    1 
ATOM   9780  O  OH    . TYR B 1 527 ? 115.150 155.985 160.509 1.00 30.81 ?  527 TYR B OH    1 
ATOM   9781  N  N     . PHE B 1 528 ? 109.733 160.594 161.367 1.00 29.04 ?  528 PHE B N     1 
ATOM   9782  C  CA    . PHE B 1 528 ? 109.784 160.701 162.817 1.00 26.61 ?  528 PHE B CA    1 
ATOM   9783  C  C     . PHE B 1 528 ? 108.454 160.390 163.488 1.00 33.94 ?  528 PHE B C     1 
ATOM   9784  O  O     . PHE B 1 528 ? 108.368 160.480 164.716 1.00 38.82 ?  528 PHE B O     1 
ATOM   9785  C  CB    . PHE B 1 528 ? 110.244 162.104 163.223 1.00 27.80 ?  528 PHE B CB    1 
ATOM   9786  C  CG    . PHE B 1 528 ? 111.553 162.513 162.614 1.00 29.99 ?  528 PHE B CG    1 
ATOM   9787  C  CD1   . PHE B 1 528 ? 112.747 162.227 163.251 1.00 26.60 ?  528 PHE B CD1   1 
ATOM   9788  C  CD2   . PHE B 1 528 ? 111.589 163.187 161.404 1.00 25.41 ?  528 PHE B CD2   1 
ATOM   9789  C  CE1   . PHE B 1 528 ? 113.953 162.603 162.693 1.00 28.91 ?  528 PHE B CE1   1 
ATOM   9790  C  CE2   . PHE B 1 528 ? 112.791 163.564 160.842 1.00 27.68 ?  528 PHE B CE2   1 
ATOM   9791  C  CZ    . PHE B 1 528 ? 113.974 163.271 161.487 1.00 27.60 ?  528 PHE B CZ    1 
ATOM   9792  N  N     . ASP B 1 529 ? 107.425 160.025 162.716 1.00 31.57 ?  529 ASP B N     1 
ATOM   9793  C  CA    . ASP B 1 529 ? 106.092 159.815 163.277 1.00 31.29 ?  529 ASP B CA    1 
ATOM   9794  C  C     . ASP B 1 529 ? 106.125 158.838 164.448 1.00 32.79 ?  529 ASP B C     1 
ATOM   9795  O  O     . ASP B 1 529 ? 105.811 159.201 165.589 1.00 37.04 ?  529 ASP B O     1 
ATOM   9796  C  CB    . ASP B 1 529 ? 105.147 159.313 162.185 1.00 31.85 ?  529 ASP B CB    1 
ATOM   9797  C  CG    . ASP B 1 529 ? 104.629 160.433 161.305 1.00 33.93 ?  529 ASP B CG    1 
ATOM   9798  O  OD1   . ASP B 1 529 ? 104.895 161.610 161.624 1.00 36.54 ?  529 ASP B OD1   1 
ATOM   9799  O  OD2   . ASP B 1 529 ? 103.958 160.133 160.295 1.00 36.46 -1 529 ASP B OD2   1 
ATOM   9800  N  N     . LYS B 1 530 ? 106.542 157.597 164.188 1.00 34.54 ?  530 LYS B N     1 
ATOM   9801  C  CA    . LYS B 1 530 ? 106.596 156.597 165.247 1.00 34.43 ?  530 LYS B CA    1 
ATOM   9802  C  C     . LYS B 1 530 ? 107.552 156.992 166.362 1.00 36.06 ?  530 LYS B C     1 
ATOM   9803  O  O     . LYS B 1 530 ? 107.451 156.457 167.470 1.00 36.80 ?  530 LYS B O     1 
ATOM   9804  C  CB    . LYS B 1 530 ? 107.003 155.239 164.673 1.00 33.22 ?  530 LYS B CB    1 
ATOM   9805  C  CG    . LYS B 1 530 ? 108.494 154.957 164.750 1.00 31.06 ?  530 LYS B CG    1 
ATOM   9806  C  CD    . LYS B 1 530 ? 108.890 153.812 163.844 1.00 32.94 ?  530 LYS B CD    1 
ATOM   9807  C  CE    . LYS B 1 530 ? 110.357 153.475 164.010 1.00 31.12 ?  530 LYS B CE    1 
ATOM   9808  N  NZ    . LYS B 1 530 ? 111.053 153.390 162.698 1.00 37.43 1  530 LYS B NZ    1 
ATOM   9809  N  N     . TYR B 1 531 ? 108.475 157.914 166.097 1.00 35.29 ?  531 TYR B N     1 
ATOM   9810  C  CA    . TYR B 1 531 ? 109.405 158.364 167.119 1.00 28.42 ?  531 TYR B CA    1 
ATOM   9811  C  C     . TYR B 1 531 ? 108.870 159.525 167.940 1.00 29.68 ?  531 TYR B C     1 
ATOM   9812  O  O     . TYR B 1 531 ? 109.390 159.782 169.033 1.00 33.16 ?  531 TYR B O     1 
ATOM   9813  C  CB    . TYR B 1 531 ? 110.735 158.759 166.477 1.00 27.04 ?  531 TYR B CB    1 
ATOM   9814  C  CG    . TYR B 1 531 ? 111.567 157.581 166.032 1.00 28.11 ?  531 TYR B CG    1 
ATOM   9815  C  CD1   . TYR B 1 531 ? 111.936 156.591 166.930 1.00 25.95 ?  531 TYR B CD1   1 
ATOM   9816  C  CD2   . TYR B 1 531 ? 111.983 157.458 164.713 1.00 27.49 ?  531 TYR B CD2   1 
ATOM   9817  C  CE1   . TYR B 1 531 ? 112.697 155.513 166.531 1.00 28.69 ?  531 TYR B CE1   1 
ATOM   9818  C  CE2   . TYR B 1 531 ? 112.744 156.382 164.304 1.00 23.66 ?  531 TYR B CE2   1 
ATOM   9819  C  CZ    . TYR B 1 531 ? 113.098 155.413 165.217 1.00 28.29 ?  531 TYR B CZ    1 
ATOM   9820  O  OH    . TYR B 1 531 ? 113.856 154.340 164.815 1.00 32.32 ?  531 TYR B OH    1 
ATOM   9821  N  N     . VAL B 1 532 ? 107.846 160.230 167.453 1.00 33.72 ?  532 VAL B N     1 
ATOM   9822  C  CA    . VAL B 1 532 ? 107.261 161.336 168.203 1.00 31.71 ?  532 VAL B CA    1 
ATOM   9823  C  C     . VAL B 1 532 ? 105.948 160.954 168.866 1.00 34.87 ?  532 VAL B C     1 
ATOM   9824  O  O     . VAL B 1 532 ? 105.282 161.821 169.448 1.00 40.13 ?  532 VAL B O     1 
ATOM   9825  C  CB    . VAL B 1 532 ? 107.067 162.579 167.309 1.00 34.38 ?  532 VAL B CB    1 
ATOM   9826  C  CG1   . VAL B 1 532 ? 108.399 163.038 166.740 1.00 32.64 ?  532 VAL B CG1   1 
ATOM   9827  C  CG2   . VAL B 1 532 ? 106.071 162.294 166.197 1.00 34.61 ?  532 VAL B CG2   1 
ATOM   9828  N  N     . SER B 1 533 ? 105.555 159.683 168.798 1.00 40.20 ?  533 SER B N     1 
ATOM   9829  C  CA    . SER B 1 533 ? 104.300 159.237 169.387 1.00 39.75 ?  533 SER B CA    1 
ATOM   9830  C  C     . SER B 1 533 ? 104.515 158.011 170.265 1.00 40.09 ?  533 SER B C     1 
ATOM   9831  O  O     . SER B 1 533 ? 103.744 157.765 171.199 1.00 44.55 ?  533 SER B O     1 
ATOM   9832  C  CB    . SER B 1 533 ? 103.278 158.933 168.292 1.00 41.09 ?  533 SER B CB    1 
ATOM   9833  O  OG    . SER B 1 533 ? 103.623 157.753 167.589 1.00 42.45 ?  533 SER B OG    1 
ATOM   9834  N  N     . THR B 1 534 ? 105.557 157.238 169.975 1.00 39.24 ?  534 THR B N     1 
ATOM   9835  C  CA    . THR B 1 534 ? 105.864 156.020 170.709 1.00 38.89 ?  534 THR B CA    1 
ATOM   9836  C  C     . THR B 1 534 ? 107.168 156.190 171.475 1.00 37.46 ?  534 THR B C     1 
ATOM   9837  O  O     . THR B 1 534 ? 108.148 156.722 170.944 1.00 43.15 ?  534 THR B O     1 
ATOM   9838  C  CB    . THR B 1 534 ? 105.968 154.816 169.768 1.00 39.21 ?  534 THR B CB    1 
ATOM   9839  O  OG1   . THR B 1 534 ? 104.825 154.782 168.904 1.00 40.92 ?  534 THR B OG1   1 
ATOM   9840  C  CG2   . THR B 1 534 ? 106.040 153.518 170.558 1.00 40.55 ?  534 THR B CG2   1 
ATOM   9841  N  N     . ASP B 1 535 ? 107.172 155.735 172.724 1.00 42.63 ?  535 ASP B N     1 
ATOM   9842  C  CA    . ASP B 1 535 ? 108.358 155.786 173.567 1.00 41.49 ?  535 ASP B CA    1 
ATOM   9843  C  C     . ASP B 1 535 ? 109.104 154.462 173.477 1.00 41.07 ?  535 ASP B C     1 
ATOM   9844  O  O     . ASP B 1 535 ? 108.510 153.393 173.654 1.00 42.97 ?  535 ASP B O     1 
ATOM   9845  C  CB    . ASP B 1 535 ? 107.972 156.086 175.016 1.00 38.42 ?  535 ASP B CB    1 
ATOM   9846  C  CG    . ASP B 1 535 ? 109.146 155.984 175.965 1.00 44.29 ?  535 ASP B CG    1 
ATOM   9847  O  OD1   . ASP B 1 535 ? 109.891 156.978 176.103 1.00 47.58 ?  535 ASP B OD1   1 
ATOM   9848  O  OD2   . ASP B 1 535 ? 109.320 154.910 176.575 1.00 46.27 -1 535 ASP B OD2   1 
ATOM   9849  N  N     . PHE B 1 536 ? 110.406 154.536 173.200 1.00 32.24 ?  536 PHE B N     1 
ATOM   9850  C  CA    . PHE B 1 536 ? 111.235 153.352 173.028 1.00 32.66 ?  536 PHE B CA    1 
ATOM   9851  C  C     . PHE B 1 536 ? 112.191 153.142 174.197 1.00 33.90 ?  536 PHE B C     1 
ATOM   9852  O  O     . PHE B 1 536 ? 113.211 152.462 174.046 1.00 35.05 ?  536 PHE B O     1 
ATOM   9853  C  CB    . PHE B 1 536 ? 112.004 153.432 171.709 1.00 29.99 ?  536 PHE B CB    1 
ATOM   9854  C  CG    . PHE B 1 536 ? 111.120 153.411 170.496 1.00 27.01 ?  536 PHE B CG    1 
ATOM   9855  C  CD1   . PHE B 1 536 ? 110.766 152.213 169.901 1.00 28.60 ?  536 PHE B CD1   1 
ATOM   9856  C  CD2   . PHE B 1 536 ? 110.636 154.590 169.954 1.00 30.83 ?  536 PHE B CD2   1 
ATOM   9857  C  CE1   . PHE B 1 536 ? 109.950 152.190 168.787 1.00 30.63 ?  536 PHE B CE1   1 
ATOM   9858  C  CE2   . PHE B 1 536 ? 109.819 154.573 168.841 1.00 35.58 ?  536 PHE B CE2   1 
ATOM   9859  C  CZ    . PHE B 1 536 ? 109.477 153.372 168.256 1.00 32.38 ?  536 PHE B CZ    1 
ATOM   9860  N  N     . SER B 1 537 ? 111.882 153.714 175.356 1.00 35.74 ?  537 SER B N     1 
ATOM   9861  C  CA    . SER B 1 537 ? 112.654 153.435 176.553 1.00 33.49 ?  537 SER B CA    1 
ATOM   9862  C  C     . SER B 1 537 ? 112.426 151.989 176.988 1.00 37.92 ?  537 SER B C     1 
ATOM   9863  O  O     . SER B 1 537 ? 111.379 151.404 176.696 1.00 39.77 ?  537 SER B O     1 
ATOM   9864  C  CB    . SER B 1 537 ? 112.262 154.391 177.676 1.00 35.62 ?  537 SER B CB    1 
ATOM   9865  O  OG    . SER B 1 537 ? 112.401 155.740 177.267 1.00 41.80 ?  537 SER B OG    1 
ATOM   9866  N  N     . PRO B 1 538 ? 113.396 151.382 177.671 1.00 35.53 ?  538 PRO B N     1 
ATOM   9867  C  CA    . PRO B 1 538 ? 113.251 149.973 178.055 1.00 34.54 ?  538 PRO B CA    1 
ATOM   9868  C  C     . PRO B 1 538 ? 112.042 149.748 178.950 1.00 38.77 ?  538 PRO B C     1 
ATOM   9869  O  O     . PRO B 1 538 ? 111.765 150.526 179.865 1.00 41.83 ?  538 PRO B O     1 
ATOM   9870  C  CB    . PRO B 1 538 ? 114.561 149.670 178.792 1.00 36.06 ?  538 PRO B CB    1 
ATOM   9871  C  CG    . PRO B 1 538 ? 115.516 150.711 178.323 1.00 37.65 ?  538 PRO B CG    1 
ATOM   9872  C  CD    . PRO B 1 538 ? 114.692 151.934 178.096 1.00 35.67 ?  538 PRO B CD    1 
ATOM   9873  N  N     . LYS B 1 539 ? 111.321 148.661 178.675 1.00 41.02 ?  539 LYS B N     1 
ATOM   9874  C  CA    . LYS B 1 539 ? 110.167 148.270 179.471 1.00 41.05 ?  539 LYS B CA    1 
ATOM   9875  C  C     . LYS B 1 539 ? 110.529 147.357 180.633 1.00 44.29 ?  539 LYS B C     1 
ATOM   9876  O  O     . LYS B 1 539 ? 109.675 147.101 181.488 1.00 47.25 ?  539 LYS B O     1 
ATOM   9877  C  CB    . LYS B 1 539 ? 109.127 147.575 178.587 1.00 42.03 ?  539 LYS B CB    1 
ATOM   9878  C  CG    . LYS B 1 539 ? 109.008 148.164 177.192 1.00 42.44 ?  539 LYS B CG    1 
ATOM   9879  C  CD    . LYS B 1 539 ? 107.846 149.139 177.103 1.00 42.09 ?  539 LYS B CD    1 
ATOM   9880  C  CE    . LYS B 1 539 ? 107.713 149.710 175.702 1.00 44.54 ?  539 LYS B CE    1 
ATOM   9881  N  NZ    . LYS B 1 539 ? 109.024 150.173 175.166 1.00 45.96 1  539 LYS B NZ    1 
ATOM   9882  N  N     . TYR B 1 540 ? 111.763 146.867 180.685 1.00 42.27 ?  540 TYR B N     1 
ATOM   9883  C  CA    . TYR B 1 540 ? 112.222 145.986 181.747 1.00 39.72 ?  540 TYR B CA    1 
ATOM   9884  C  C     . TYR B 1 540 ? 113.256 146.707 182.600 1.00 46.19 ?  540 TYR B C     1 
ATOM   9885  O  O     . TYR B 1 540 ? 114.061 147.491 182.087 1.00 47.07 ?  540 TYR B O     1 
ATOM   9886  C  CB    . TYR B 1 540 ? 112.815 144.696 181.172 1.00 41.89 ?  540 TYR B CB    1 
ATOM   9887  C  CG    . TYR B 1 540 ? 111.801 143.826 180.467 1.00 45.05 ?  540 TYR B CG    1 
ATOM   9888  C  CD1   . TYR B 1 540 ? 111.521 144.006 179.118 1.00 42.64 ?  540 TYR B CD1   1 
ATOM   9889  C  CD2   . TYR B 1 540 ? 111.116 142.832 181.151 1.00 45.24 ?  540 TYR B CD2   1 
ATOM   9890  C  CE1   . TYR B 1 540 ? 110.592 143.214 178.470 1.00 42.42 ?  540 TYR B CE1   1 
ATOM   9891  C  CE2   . TYR B 1 540 ? 110.186 142.037 180.512 1.00 42.26 ?  540 TYR B CE2   1 
ATOM   9892  C  CZ    . TYR B 1 540 ? 109.928 142.231 179.172 1.00 43.92 ?  540 TYR B CZ    1 
ATOM   9893  O  OH    . TYR B 1 540 ? 109.001 141.440 178.534 1.00 46.28 ?  540 TYR B OH    1 
ATOM   9894  N  N     . GLU B 1 541 ? 113.222 146.443 183.908 1.00 49.66 ?  541 GLU B N     1 
ATOM   9895  C  CA    . GLU B 1 541 ? 114.133 147.119 184.825 1.00 45.98 ?  541 GLU B CA    1 
ATOM   9896  C  C     . GLU B 1 541 ? 115.583 146.743 184.546 1.00 46.37 ?  541 GLU B C     1 
ATOM   9897  O  O     . GLU B 1 541 ? 116.483 147.582 184.673 1.00 45.04 ?  541 GLU B O     1 
ATOM   9898  C  CB    . GLU B 1 541 ? 113.763 146.791 186.272 1.00 46.69 ?  541 GLU B CB    1 
ATOM   9899  C  CG    . GLU B 1 541 ? 114.435 147.691 187.295 1.00 48.66 ?  541 GLU B CG    1 
ATOM   9900  C  CD    . GLU B 1 541 ? 114.340 149.159 186.932 1.00 50.84 ?  541 GLU B CD    1 
ATOM   9901  O  OE1   . GLU B 1 541 ? 113.209 149.655 186.747 1.00 50.80 ?  541 GLU B OE1   1 
ATOM   9902  O  OE2   . GLU B 1 541 ? 115.396 149.818 186.828 1.00 52.89 -1 541 GLU B OE2   1 
ATOM   9903  N  N     . LYS B 1 542 ? 115.832 145.484 184.179 1.00 42.48 ?  542 LYS B N     1 
ATOM   9904  C  CA    . LYS B 1 542 ? 117.198 145.053 183.892 1.00 39.80 ?  542 LYS B CA    1 
ATOM   9905  C  C     . LYS B 1 542 ? 117.780 145.812 182.706 1.00 42.82 ?  542 LYS B C     1 
ATOM   9906  O  O     . LYS B 1 542 ? 118.937 146.248 182.744 1.00 44.21 ?  542 LYS B O     1 
ATOM   9907  C  CB    . LYS B 1 542 ? 117.224 143.546 183.634 1.00 38.45 ?  542 LYS B CB    1 
ATOM   9908  C  CG    . LYS B 1 542 ? 118.613 142.977 183.402 1.00 43.63 ?  542 LYS B CG    1 
ATOM   9909  C  CD    . LYS B 1 542 ? 118.569 141.466 183.258 1.00 42.93 ?  542 LYS B CD    1 
ATOM   9910  C  CE    . LYS B 1 542 ? 119.968 140.879 183.183 1.00 43.45 ?  542 LYS B CE    1 
ATOM   9911  N  NZ    . LYS B 1 542 ? 119.954 139.393 183.255 1.00 41.95 1  542 LYS B NZ    1 
ATOM   9912  N  N     . ILE B 1 543 ? 116.990 145.994 181.648 1.00 39.40 ?  543 ILE B N     1 
ATOM   9913  C  CA    . ILE B 1 543 ? 117.468 146.730 180.482 1.00 37.20 ?  543 ILE B CA    1 
ATOM   9914  C  C     . ILE B 1 543 ? 117.684 148.199 180.825 1.00 36.34 ?  543 ILE B C     1 
ATOM   9915  O  O     . ILE B 1 543 ? 118.658 148.818 180.379 1.00 39.33 ?  543 ILE B O     1 
ATOM   9916  C  CB    . ILE B 1 543 ? 116.487 146.555 179.309 1.00 36.93 ?  543 ILE B CB    1 
ATOM   9917  C  CG1   . ILE B 1 543 ? 116.190 145.071 179.077 1.00 36.34 ?  543 ILE B CG1   1 
ATOM   9918  C  CG2   . ILE B 1 543 ? 117.051 147.187 178.055 1.00 35.21 ?  543 ILE B CG2   1 
ATOM   9919  C  CD1   . ILE B 1 543 ? 117.428 144.220 178.883 1.00 34.56 ?  543 ILE B CD1   1 
ATOM   9920  N  N     . ALA B 1 544 ? 116.780 148.782 181.617 1.00 37.78 ?  544 ALA B N     1 
ATOM   9921  C  CA    . ALA B 1 544 ? 116.952 150.169 182.036 1.00 40.15 ?  544 ALA B CA    1 
ATOM   9922  C  C     . ALA B 1 544 ? 118.230 150.344 182.845 1.00 39.96 ?  544 ALA B C     1 
ATOM   9923  O  O     . ALA B 1 544 ? 118.949 151.337 182.679 1.00 42.67 ?  544 ALA B O     1 
ATOM   9924  C  CB    . ALA B 1 544 ? 115.737 150.628 182.842 1.00 41.98 ?  544 ALA B CB    1 
ATOM   9925  N  N     . ASN B 1 545 ? 118.529 149.390 183.730 1.00 43.77 ?  545 ASN B N     1 
ATOM   9926  C  CA    . ASN B 1 545 ? 119.791 149.423 184.460 1.00 47.64 ?  545 ASN B CA    1 
ATOM   9927  C  C     . ASN B 1 545 ? 120.975 149.282 183.513 1.00 45.05 ?  545 ASN B C     1 
ATOM   9928  O  O     . ASN B 1 545 ? 122.014 149.923 183.704 1.00 46.84 ?  545 ASN B O     1 
ATOM   9929  C  CB    . ASN B 1 545 ? 119.815 148.322 185.520 1.00 44.49 ?  545 ASN B CB    1 
ATOM   9930  C  CG    . ASN B 1 545 ? 118.792 148.546 186.613 1.00 47.52 ?  545 ASN B CG    1 
ATOM   9931  O  OD1   . ASN B 1 545 ? 118.354 149.672 186.847 1.00 49.39 ?  545 ASN B OD1   1 
ATOM   9932  N  ND2   . ASN B 1 545 ? 118.404 147.472 187.290 1.00 44.45 ?  545 ASN B ND2   1 
ATOM   9933  N  N     . LEU B 1 546 ? 120.839 148.431 182.493 1.00 38.60 ?  546 LEU B N     1 
ATOM   9934  C  CA    . LEU B 1 546 ? 121.878 148.318 181.475 1.00 39.55 ?  546 LEU B CA    1 
ATOM   9935  C  C     . LEU B 1 546 ? 122.126 149.648 180.779 1.00 39.47 ?  546 LEU B C     1 
ATOM   9936  O  O     . LEU B 1 546 ? 123.265 149.957 180.413 1.00 39.00 ?  546 LEU B O     1 
ATOM   9937  C  CB    . LEU B 1 546 ? 121.495 147.249 180.452 1.00 36.75 ?  546 LEU B CB    1 
ATOM   9938  C  CG    . LEU B 1 546 ? 121.818 145.800 180.810 1.00 39.09 ?  546 LEU B CG    1 
ATOM   9939  C  CD1   . LEU B 1 546 ? 121.797 144.938 179.563 1.00 37.33 ?  546 LEU B CD1   1 
ATOM   9940  C  CD2   . LEU B 1 546 ? 123.165 145.704 181.509 1.00 38.77 ?  546 LEU B CD2   1 
ATOM   9941  N  N     . PHE B 1 547 ? 121.078 150.448 180.593 1.00 40.07 ?  547 PHE B N     1 
ATOM   9942  C  CA    . PHE B 1 547 ? 121.191 151.746 179.941 1.00 37.64 ?  547 PHE B CA    1 
ATOM   9943  C  C     . PHE B 1 547 ? 121.436 152.889 180.918 1.00 39.81 ?  547 PHE B C     1 
ATOM   9944  O  O     . PHE B 1 547 ? 121.318 154.054 180.526 1.00 43.53 ?  547 PHE B O     1 
ATOM   9945  C  CB    . PHE B 1 547 ? 119.932 152.034 179.120 1.00 35.49 ?  547 PHE B CB    1 
ATOM   9946  C  CG    . PHE B 1 547 ? 119.898 151.335 177.796 1.00 36.65 ?  547 PHE B CG    1 
ATOM   9947  C  CD1   . PHE B 1 547 ? 120.622 151.824 176.723 1.00 35.91 ?  547 PHE B CD1   1 
ATOM   9948  C  CD2   . PHE B 1 547 ? 119.143 150.189 177.620 1.00 35.72 ?  547 PHE B CD2   1 
ATOM   9949  C  CE1   . PHE B 1 547 ? 120.593 151.184 175.502 1.00 34.64 ?  547 PHE B CE1   1 
ATOM   9950  C  CE2   . PHE B 1 547 ? 119.112 149.546 176.402 1.00 36.03 ?  547 PHE B CE2   1 
ATOM   9951  C  CZ    . PHE B 1 547 ? 119.839 150.043 175.342 1.00 35.01 ?  547 PHE B CZ    1 
ATOM   9952  N  N     . GLU B 1 548 ? 121.767 152.590 182.171 1.00 47.04 ?  548 GLU B N     1 
ATOM   9953  C  CA    . GLU B 1 548 ? 122.027 153.642 183.144 1.00 47.44 ?  548 GLU B CA    1 
ATOM   9954  C  C     . GLU B 1 548 ? 123.298 154.406 182.791 1.00 47.26 ?  548 GLU B C     1 
ATOM   9955  O  O     . GLU B 1 548 ? 124.238 153.861 182.206 1.00 50.56 ?  548 GLU B O     1 
ATOM   9956  C  CB    . GLU B 1 548 ? 122.142 153.062 184.553 1.00 46.82 ?  548 GLU B CB    1 
ATOM   9957  C  CG    . GLU B 1 548 ? 120.807 152.789 185.226 1.00 48.12 ?  548 GLU B CG    1 
ATOM   9958  C  CD    . GLU B 1 548 ? 119.954 154.038 185.380 1.00 50.79 ?  548 GLU B CD    1 
ATOM   9959  O  OE1   . GLU B 1 548 ? 120.519 155.150 185.445 1.00 48.80 ?  548 GLU B OE1   1 
ATOM   9960  O  OE2   . GLU B 1 548 ? 118.714 153.904 185.438 1.00 50.91 -1 548 GLU B OE2   1 
ATOM   9961  N  N     . GLY B 1 549 ? 123.316 155.685 183.155 1.00 45.31 ?  549 GLY B N     1 
ATOM   9962  C  CA    . GLY B 1 549 ? 124.406 156.564 182.799 1.00 44.97 ?  549 GLY B CA    1 
ATOM   9963  C  C     . GLY B 1 549 ? 124.340 157.114 181.394 1.00 46.10 ?  549 GLY B C     1 
ATOM   9964  O  O     . GLY B 1 549 ? 125.274 157.809 180.973 1.00 47.53 ?  549 GLY B O     1 
ATOM   9965  N  N     . MET B 1 550 ? 123.271 156.826 180.656 1.00 45.44 ?  550 MET B N     1 
ATOM   9966  C  CA    . MET B 1 550 ? 123.109 157.273 179.281 1.00 44.20 ?  550 MET B CA    1 
ATOM   9967  C  C     . MET B 1 550 ? 121.710 157.843 179.113 1.00 44.33 ?  550 MET B C     1 
ATOM   9968  O  O     . MET B 1 550 ? 120.736 157.250 179.586 1.00 46.15 ?  550 MET B O     1 
ATOM   9969  C  CB    . MET B 1 550 ? 123.339 156.119 178.302 1.00 43.15 ?  550 MET B CB    1 
ATOM   9970  C  CG    . MET B 1 550 ? 124.629 156.227 177.517 1.00 48.10 ?  550 MET B CG    1 
ATOM   9971  S  SD    . MET B 1 550 ? 124.692 155.060 176.150 1.00 54.89 ?  550 MET B SD    1 
ATOM   9972  C  CE    . MET B 1 550 ? 124.559 153.502 177.021 1.00 44.40 ?  550 MET B CE    1 
ATOM   9973  N  N     . HIS B 1 551 ? 121.611 158.986 178.440 1.00 40.63 ?  551 HIS B N     1 
ATOM   9974  C  CA    . HIS B 1 551 ? 120.329 159.658 178.254 1.00 40.60 ?  551 HIS B CA    1 
ATOM   9975  C  C     . HIS B 1 551 ? 119.575 159.004 177.103 1.00 40.33 ?  551 HIS B C     1 
ATOM   9976  O  O     . HIS B 1 551 ? 119.888 159.242 175.932 1.00 41.37 ?  551 HIS B O     1 
ATOM   9977  C  CB    . HIS B 1 551 ? 120.533 161.146 177.989 1.00 39.84 ?  551 HIS B CB    1 
ATOM   9978  C  CG    . HIS B 1 551 ? 119.303 161.840 177.498 1.00 41.55 ?  551 HIS B CG    1 
ATOM   9979  N  ND1   . HIS B 1 551 ? 118.201 162.055 178.296 1.00 44.88 ?  551 HIS B ND1   1 
ATOM   9980  C  CD2   . HIS B 1 551 ? 118.996 162.358 176.285 1.00 41.27 ?  551 HIS B CD2   1 
ATOM   9981  C  CE1   . HIS B 1 551 ? 117.269 162.679 177.598 1.00 43.33 ?  551 HIS B CE1   1 
ATOM   9982  N  NE2   . HIS B 1 551 ? 117.726 162.875 176.375 1.00 40.71 ?  551 HIS B NE2   1 
ATOM   9983  N  N     . ILE B 1 552 ? 118.574 158.195 177.432 1.00 35.98 ?  552 ILE B N     1 
ATOM   9984  C  CA    . ILE B 1 552 ? 117.737 157.543 176.428 1.00 32.38 ?  552 ILE B CA    1 
ATOM   9985  C  C     . ILE B 1 552 ? 116.800 158.585 175.831 1.00 33.83 ?  552 ILE B C     1 
ATOM   9986  O  O     . ILE B 1 552 ? 116.033 159.220 176.568 1.00 38.54 ?  552 ILE B O     1 
ATOM   9987  C  CB    . ILE B 1 552 ? 116.953 156.370 177.036 1.00 35.25 ?  552 ILE B CB    1 
ATOM   9988  C  CG1   . ILE B 1 552 ? 117.913 155.366 177.674 1.00 34.38 ?  552 ILE B CG1   1 
ATOM   9989  C  CG2   . ILE B 1 552 ? 116.098 155.697 175.979 1.00 35.00 ?  552 ILE B CG2   1 
ATOM   9990  C  CD1   . ILE B 1 552 ? 117.249 154.435 178.656 1.00 33.66 ?  552 ILE B CD1   1 
ATOM   9991  N  N     . PRO B 1 553 ? 116.833 158.804 174.516 1.00 37.53 ?  553 PRO B N     1 
ATOM   9992  C  CA    . PRO B 1 553 ? 115.962 159.822 173.917 1.00 34.70 ?  553 PRO B CA    1 
ATOM   9993  C  C     . PRO B 1 553 ? 114.491 159.484 174.110 1.00 35.12 ?  553 PRO B C     1 
ATOM   9994  O  O     . PRO B 1 553 ? 114.071 158.335 173.962 1.00 37.86 ?  553 PRO B O     1 
ATOM   9995  C  CB    . PRO B 1 553 ? 116.354 159.798 172.435 1.00 32.01 ?  553 PRO B CB    1 
ATOM   9996  C  CG    . PRO B 1 553 ? 117.716 159.186 172.406 1.00 30.36 ?  553 PRO B CG    1 
ATOM   9997  C  CD    . PRO B 1 553 ? 117.735 158.196 173.525 1.00 32.54 ?  553 PRO B CD    1 
ATOM   9998  N  N     . THR B 1 554 ? 113.710 160.504 174.440 1.00 39.81 ?  554 THR B N     1 
ATOM   9999  C  CA    . THR B 1 554 ? 112.276 160.374 174.615 1.00 38.48 ?  554 THR B CA    1 
ATOM   10000 C  C     . THR B 1 554 ? 111.563 160.963 173.401 1.00 36.43 ?  554 THR B C     1 
ATOM   10001 O  O     . THR B 1 554 ? 112.189 161.333 172.403 1.00 36.73 ?  554 THR B O     1 
ATOM   10002 C  CB    . THR B 1 554 ? 111.840 161.049 175.917 1.00 38.13 ?  554 THR B CB    1 
ATOM   10003 O  OG1   . THR B 1 554 ? 112.133 162.450 175.852 1.00 37.11 ?  554 THR B OG1   1 
ATOM   10004 C  CG2   . THR B 1 554 ? 112.573 160.439 177.103 1.00 36.24 ?  554 THR B CG2   1 
ATOM   10005 N  N     . THR B 1 555 ? 110.233 161.050 173.477 1.00 39.09 ?  555 THR B N     1 
ATOM   10006 C  CA    . THR B 1 555 ? 109.479 161.651 172.384 1.00 36.65 ?  555 THR B CA    1 
ATOM   10007 C  C     . THR B 1 555 ? 109.794 163.133 172.231 1.00 39.53 ?  555 THR B C     1 
ATOM   10008 O  O     . THR B 1 555 ? 109.727 163.666 171.119 1.00 40.35 ?  555 THR B O     1 
ATOM   10009 C  CB    . THR B 1 555 ? 107.978 161.451 172.599 1.00 38.95 ?  555 THR B CB    1 
ATOM   10010 O  OG1   . THR B 1 555 ? 107.602 161.974 173.878 1.00 44.10 ?  555 THR B OG1   1 
ATOM   10011 C  CG2   . THR B 1 555 ? 107.626 159.972 172.533 1.00 39.39 ?  555 THR B CG2   1 
ATOM   10012 N  N     . GLU B 1 556 ? 110.142 163.813 173.327 1.00 37.71 ?  556 GLU B N     1 
ATOM   10013 C  CA    . GLU B 1 556 ? 110.504 165.225 173.237 1.00 37.73 ?  556 GLU B CA    1 
ATOM   10014 C  C     . GLU B 1 556 ? 111.842 165.410 172.529 1.00 40.49 ?  556 GLU B C     1 
ATOM   10015 O  O     . GLU B 1 556 ? 111.992 166.314 171.697 1.00 41.86 ?  556 GLU B O     1 
ATOM   10016 C  CB    . GLU B 1 556 ? 110.545 165.845 174.632 1.00 39.97 ?  556 GLU B CB    1 
ATOM   10017 C  CG    . GLU B 1 556 ? 109.177 166.043 175.263 1.00 41.23 ?  556 GLU B CG    1 
ATOM   10018 C  CD    . GLU B 1 556 ? 108.145 166.543 174.274 1.00 44.19 ?  556 GLU B CD    1 
ATOM   10019 O  OE1   . GLU B 1 556 ? 108.261 167.703 173.826 1.00 42.40 ?  556 GLU B OE1   1 
ATOM   10020 O  OE2   . GLU B 1 556 ? 107.215 165.776 173.943 1.00 44.24 -1 556 GLU B OE2   1 
ATOM   10021 N  N     . ASP B 1 557 ? 112.828 164.569 172.850 1.00 40.06 ?  557 ASP B N     1 
ATOM   10022 C  CA    . ASP B 1 557 ? 114.105 164.626 172.146 1.00 34.63 ?  557 ASP B CA    1 
ATOM   10023 C  C     . ASP B 1 557 ? 113.925 164.313 170.668 1.00 36.07 ?  557 ASP B C     1 
ATOM   10024 O  O     . ASP B 1 557 ? 114.564 164.931 169.810 1.00 38.98 ?  557 ASP B O     1 
ATOM   10025 C  CB    . ASP B 1 557 ? 115.104 163.659 172.781 1.00 32.74 ?  557 ASP B CB    1 
ATOM   10026 C  CG    . ASP B 1 557 ? 115.031 163.658 174.294 1.00 41.14 ?  557 ASP B CG    1 
ATOM   10027 O  OD1   . ASP B 1 557 ? 113.943 163.375 174.837 1.00 44.16 ?  557 ASP B OD1   1 
ATOM   10028 O  OD2   . ASP B 1 557 ? 116.063 163.938 174.940 1.00 42.26 -1 557 ASP B OD2   1 
ATOM   10029 N  N     . TRP B 1 558 ? 113.050 163.356 170.350 1.00 32.21 ?  558 TRP B N     1 
ATOM   10030 C  CA    . TRP B 1 558 ? 112.783 163.035 168.954 1.00 26.34 ?  558 TRP B CA    1 
ATOM   10031 C  C     . TRP B 1 558 ? 112.065 164.177 168.245 1.00 31.81 ?  558 TRP B C     1 
ATOM   10032 O  O     . TRP B 1 558 ? 112.314 164.429 167.063 1.00 38.07 ?  558 TRP B O     1 
ATOM   10033 C  CB    . TRP B 1 558 ? 111.974 161.745 168.862 1.00 27.19 ?  558 TRP B CB    1 
ATOM   10034 C  CG    . TRP B 1 558 ? 112.826 160.522 168.752 1.00 27.01 ?  558 TRP B CG    1 
ATOM   10035 C  CD1   . TRP B 1 558 ? 113.035 159.579 169.713 1.00 26.33 ?  558 TRP B CD1   1 
ATOM   10036 C  CD2   . TRP B 1 558 ? 113.579 160.104 167.608 1.00 27.89 ?  558 TRP B CD2   1 
ATOM   10037 N  NE1   . TRP B 1 558 ? 113.874 158.601 169.240 1.00 30.65 ?  558 TRP B NE1   1 
ATOM   10038 C  CE2   . TRP B 1 558 ? 114.220 158.898 167.949 1.00 28.06 ?  558 TRP B CE2   1 
ATOM   10039 C  CE3   . TRP B 1 558 ? 113.769 160.630 166.327 1.00 31.92 ?  558 TRP B CE3   1 
ATOM   10040 C  CZ2   . TRP B 1 558 ? 115.039 158.212 167.056 1.00 25.09 ?  558 TRP B CZ2   1 
ATOM   10041 C  CZ3   . TRP B 1 558 ? 114.583 159.949 165.444 1.00 26.96 ?  558 TRP B CZ3   1 
ATOM   10042 C  CH2   . TRP B 1 558 ? 115.208 158.753 165.812 1.00 21.83 ?  558 TRP B CH2   1 
ATOM   10043 N  N     . LYS B 1 559 ? 111.170 164.881 168.944 1.00 36.75 ?  559 LYS B N     1 
ATOM   10044 C  CA    . LYS B 1 559 ? 110.530 166.053 168.353 1.00 31.12 ?  559 LYS B CA    1 
ATOM   10045 C  C     . LYS B 1 559 ? 111.544 167.157 168.082 1.00 34.26 ?  559 LYS B C     1 
ATOM   10046 O  O     . LYS B 1 559 ? 111.501 167.810 167.031 1.00 34.78 ?  559 LYS B O     1 
ATOM   10047 C  CB    . LYS B 1 559 ? 109.418 166.561 169.271 1.00 35.39 ?  559 LYS B CB    1 
ATOM   10048 C  CG    . LYS B 1 559 ? 108.124 165.772 169.181 1.00 37.52 ?  559 LYS B CG    1 
ATOM   10049 C  CD    . LYS B 1 559 ? 107.204 166.092 170.346 1.00 36.46 ?  559 LYS B CD    1 
ATOM   10050 C  CE    . LYS B 1 559 ? 106.183 164.989 170.565 1.00 37.55 ?  559 LYS B CE    1 
ATOM   10051 N  NZ    . LYS B 1 559 ? 105.653 164.992 171.957 1.00 36.41 1  559 LYS B NZ    1 
ATOM   10052 N  N     . LYS B 1 560 ? 112.465 167.378 169.022 1.00 31.68 ?  560 LYS B N     1 
ATOM   10053 C  CA    . LYS B 1 560 ? 113.520 168.363 168.808 1.00 30.42 ?  560 LYS B CA    1 
ATOM   10054 C  C     . LYS B 1 560 ? 114.406 167.970 167.634 1.00 34.62 ?  560 LYS B C     1 
ATOM   10055 O  O     . LYS B 1 560 ? 114.799 168.822 166.829 1.00 36.67 ?  560 LYS B O     1 
ATOM   10056 C  CB    . LYS B 1 560 ? 114.351 168.529 170.080 1.00 30.64 ?  560 LYS B CB    1 
ATOM   10057 C  CG    . LYS B 1 560 ? 113.659 169.320 171.175 1.00 35.01 ?  560 LYS B CG    1 
ATOM   10058 C  CD    . LYS B 1 560 ? 114.574 169.517 172.371 1.00 37.36 ?  560 LYS B CD    1 
ATOM   10059 C  CE    . LYS B 1 560 ? 113.783 169.848 173.626 1.00 35.42 ?  560 LYS B CE    1 
ATOM   10060 N  NZ    . LYS B 1 560 ? 113.061 168.659 174.157 1.00 37.29 1  560 LYS B NZ    1 
ATOM   10061 N  N     . LEU B 1 561 ? 114.730 166.680 167.518 1.00 31.74 ?  561 LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 561 ? 115.528 166.211 166.391 1.00 27.68 ?  561 LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 561 ? 114.775 166.367 165.075 1.00 31.16 ?  561 LEU B C     1 
ATOM   10064 O  O     . LEU B 1 561 ? 115.374 166.697 164.047 1.00 33.36 ?  561 LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 561 ? 115.936 164.754 166.606 1.00 29.77 ?  561 LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 561 ? 116.769 164.132 165.485 1.00 28.99 ?  561 LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 561 ? 117.996 164.982 165.205 1.00 25.20 ?  561 LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 561 ? 117.167 162.713 165.833 1.00 26.50 ?  561 LEU B CD2   1 
ATOM   10069 N  N     . LYS B 1 562 ? 113.464 166.121 165.086 1.00 31.63 ?  562 LYS B N     1 
ATOM   10070 C  CA    . LYS B 1 562 ? 112.657 166.318 163.887 1.00 29.39 ?  562 LYS B CA    1 
ATOM   10071 C  C     . LYS B 1 562 ? 112.657 167.778 163.459 1.00 31.00 ?  562 LYS B C     1 
ATOM   10072 O  O     . LYS B 1 562 ? 112.787 168.087 162.269 1.00 35.93 ?  562 LYS B O     1 
ATOM   10073 C  CB    . LYS B 1 562 ? 111.232 165.825 164.138 1.00 27.01 ?  562 LYS B CB    1 
ATOM   10074 C  CG    . LYS B 1 562 ? 110.230 166.200 163.062 1.00 29.64 ?  562 LYS B CG    1 
ATOM   10075 C  CD    . LYS B 1 562 ? 108.827 165.772 163.457 1.00 30.78 ?  562 LYS B CD    1 
ATOM   10076 C  CE    . LYS B 1 562 ? 107.804 166.178 162.410 1.00 32.17 ?  562 LYS B CE    1 
ATOM   10077 N  NZ    . LYS B 1 562 ? 106.527 165.429 162.569 1.00 32.25 1  562 LYS B NZ    1 
ATOM   10078 N  N     . ALA B 1 563 ? 112.521 168.695 164.421 1.00 31.70 ?  563 ALA B N     1 
ATOM   10079 C  CA    . ALA B 1 563 ? 112.593 170.118 164.100 1.00 32.22 ?  563 ALA B CA    1 
ATOM   10080 C  C     . ALA B 1 563 ? 113.973 170.495 163.573 1.00 32.55 ?  563 ALA B C     1 
ATOM   10081 O  O     . ALA B 1 563 ? 114.094 171.281 162.625 1.00 36.45 ?  563 ALA B O     1 
ATOM   10082 C  CB    . ALA B 1 563 ? 112.240 170.952 165.331 1.00 32.53 ?  563 ALA B CB    1 
ATOM   10083 N  N     . PHE B 1 564 ? 115.026 169.938 164.176 1.00 32.33 ?  564 PHE B N     1 
ATOM   10084 C  CA    . PHE B 1 564 ? 116.386 170.217 163.726 1.00 27.46 ?  564 PHE B CA    1 
ATOM   10085 C  C     . PHE B 1 564 ? 116.604 169.729 162.298 1.00 30.75 ?  564 PHE B C     1 
ATOM   10086 O  O     . PHE B 1 564 ? 117.241 170.413 161.489 1.00 33.53 ?  564 PHE B O     1 
ATOM   10087 C  CB    . PHE B 1 564 ? 117.383 169.563 164.682 1.00 28.79 ?  564 PHE B CB    1 
ATOM   10088 C  CG    . PHE B 1 564 ? 118.797 170.028 164.502 1.00 32.18 ?  564 PHE B CG    1 
ATOM   10089 C  CD1   . PHE B 1 564 ? 119.234 171.201 165.091 1.00 31.86 ?  564 PHE B CD1   1 
ATOM   10090 C  CD2   . PHE B 1 564 ? 119.695 169.285 163.756 1.00 33.00 ?  564 PHE B CD2   1 
ATOM   10091 C  CE1   . PHE B 1 564 ? 120.538 171.628 164.932 1.00 34.64 ?  564 PHE B CE1   1 
ATOM   10092 C  CE2   . PHE B 1 564 ? 120.998 169.706 163.592 1.00 32.71 ?  564 PHE B CE2   1 
ATOM   10093 C  CZ    . PHE B 1 564 ? 121.421 170.879 164.181 1.00 34.29 ?  564 PHE B CZ    1 
ATOM   10094 N  N     . VAL B 1 565 ? 116.085 168.544 161.973 1.00 31.07 ?  565 VAL B N     1 
ATOM   10095 C  CA    . VAL B 1 565 ? 116.197 168.016 160.617 1.00 27.20 ?  565 VAL B CA    1 
ATOM   10096 C  C     . VAL B 1 565 ? 115.403 168.876 159.642 1.00 32.84 ?  565 VAL B C     1 
ATOM   10097 O  O     . VAL B 1 565 ? 115.868 169.172 158.536 1.00 34.16 ?  565 VAL B O     1 
ATOM   10098 C  CB    . VAL B 1 565 ? 115.745 166.546 160.578 1.00 27.17 ?  565 VAL B CB    1 
ATOM   10099 C  CG1   . VAL B 1 565 ? 115.604 166.068 159.143 1.00 27.37 ?  565 VAL B CG1   1 
ATOM   10100 C  CG2   . VAL B 1 565 ? 116.733 165.673 161.327 1.00 29.85 ?  565 VAL B CG2   1 
ATOM   10101 N  N     . ALA B 1 566 ? 114.197 169.292 160.033 1.00 34.96 ?  566 ALA B N     1 
ATOM   10102 C  CA    . ALA B 1 566 ? 113.402 170.155 159.166 1.00 34.18 ?  566 ALA B CA    1 
ATOM   10103 C  C     . ALA B 1 566 ? 114.120 171.469 158.892 1.00 36.19 ?  566 ALA B C     1 
ATOM   10104 O  O     . ALA B 1 566 ? 114.043 172.009 157.782 1.00 38.31 ?  566 ALA B O     1 
ATOM   10105 C  CB    . ALA B 1 566 ? 112.031 170.409 159.793 1.00 33.11 ?  566 ALA B CB    1 
ATOM   10106 N  N     . GLU B 1 567 ? 114.824 172.000 159.893 1.00 36.81 ?  567 GLU B N     1 
ATOM   10107 C  CA    . GLU B 1 567 ? 115.530 173.263 159.707 1.00 35.87 ?  567 GLU B CA    1 
ATOM   10108 C  C     . GLU B 1 567 ? 116.790 173.086 158.862 1.00 38.64 ?  567 GLU B C     1 
ATOM   10109 O  O     . GLU B 1 567 ? 117.067 173.906 157.977 1.00 44.38 ?  567 GLU B O     1 
ATOM   10110 C  CB    . GLU B 1 567 ? 115.874 173.873 161.066 1.00 34.73 ?  567 GLU B CB    1 
ATOM   10111 C  CG    . GLU B 1 567 ? 117.144 174.704 161.078 1.00 37.84 ?  567 GLU B CG    1 
ATOM   10112 C  CD    . GLU B 1 567 ? 117.067 175.872 162.041 1.00 42.89 ?  567 GLU B CD    1 
ATOM   10113 O  OE1   . GLU B 1 567 ? 118.042 176.647 162.115 1.00 42.59 ?  567 GLU B OE1   1 
ATOM   10114 O  OE2   . GLU B 1 567 ? 116.029 176.014 162.721 1.00 42.45 -1 567 GLU B OE2   1 
ATOM   10115 N  N     . HIS B 1 568 ? 117.559 172.022 159.106 1.00 34.94 ?  568 HIS B N     1 
ATOM   10116 C  CA    . HIS B 1 568 ? 118.875 171.875 158.500 1.00 31.70 ?  568 HIS B CA    1 
ATOM   10117 C  C     . HIS B 1 568 ? 118.976 170.768 157.461 1.00 32.49 ?  568 HIS B C     1 
ATOM   10118 O  O     . HIS B 1 568 ? 119.893 170.807 156.636 1.00 37.18 ?  568 HIS B O     1 
ATOM   10119 C  CB    . HIS B 1 568 ? 119.932 171.620 159.584 1.00 31.46 ?  568 HIS B CB    1 
ATOM   10120 C  CG    . HIS B 1 568 ? 120.137 172.776 160.510 1.00 35.80 ?  568 HIS B CG    1 
ATOM   10121 N  ND1   . HIS B 1 568 ? 119.950 172.681 161.871 1.00 36.83 ?  568 HIS B ND1   1 
ATOM   10122 C  CD2   . HIS B 1 568 ? 120.511 174.055 160.269 1.00 34.09 ?  568 HIS B CD2   1 
ATOM   10123 C  CE1   . HIS B 1 568 ? 120.202 173.852 162.430 1.00 32.59 ?  568 HIS B CE1   1 
ATOM   10124 N  NE2   . HIS B 1 568 ? 120.544 174.702 161.481 1.00 39.37 ?  568 HIS B NE2   1 
ATOM   10125 N  N     . GLY B 1 569 ? 118.075 169.795 157.474 1.00 28.65 ?  569 GLY B N     1 
ATOM   10126 C  CA    . GLY B 1 569 ? 118.171 168.688 156.547 1.00 27.61 ?  569 GLY B CA    1 
ATOM   10127 C  C     . GLY B 1 569 ? 119.081 167.586 157.054 1.00 29.72 ?  569 GLY B C     1 
ATOM   10128 O  O     . GLY B 1 569 ? 119.588 167.614 158.177 1.00 33.19 ?  569 GLY B O     1 
ATOM   10129 N  N     . MET B 1 570 ? 119.279 166.587 156.197 1.00 26.84 ?  570 MET B N     1 
ATOM   10130 C  CA    . MET B 1 570 ? 120.143 165.455 156.501 1.00 24.33 ?  570 MET B CA    1 
ATOM   10131 C  C     . MET B 1 570 ? 121.205 165.318 155.424 1.00 26.64 ?  570 MET B C     1 
ATOM   10132 O  O     . MET B 1 570 ? 120.909 165.425 154.231 1.00 30.44 ?  570 MET B O     1 
ATOM   10133 C  CB    . MET B 1 570 ? 119.349 164.151 156.611 1.00 25.96 ?  570 MET B CB    1 
ATOM   10134 C  CG    . MET B 1 570 ? 118.346 164.122 157.745 1.00 23.78 ?  570 MET B CG    1 
ATOM   10135 S  SD    . MET B 1 570 ? 118.592 162.701 158.818 1.00 38.72 ?  570 MET B SD    1 
ATOM   10136 C  CE    . MET B 1 570 ? 118.625 161.376 157.618 1.00 28.81 ?  570 MET B CE    1 
ATOM   10137 N  N     . TYR B 1 571 ? 122.444 165.079 155.852 1.00 19.73 ?  571 TYR B N     1 
ATOM   10138 C  CA    . TYR B 1 571 ? 123.539 164.922 154.904 1.00 11.33 ?  571 TYR B CA    1 
ATOM   10139 C  C     . TYR B 1 571 ? 123.512 163.570 154.205 1.00 18.37 ?  571 TYR B C     1 
ATOM   10140 O  O     . TYR B 1 571 ? 123.947 163.467 153.053 1.00 22.60 ?  571 TYR B O     1 
ATOM   10141 C  CB    . TYR B 1 571 ? 124.880 165.108 155.611 1.00 19.31 ?  571 TYR B CB    1 
ATOM   10142 C  CG    . TYR B 1 571 ? 126.042 165.276 154.663 1.00 20.16 ?  571 TYR B CG    1 
ATOM   10143 C  CD1   . TYR B 1 571 ? 126.209 166.450 153.943 1.00 23.18 ?  571 TYR B CD1   1 
ATOM   10144 C  CD2   . TYR B 1 571 ? 126.969 164.258 154.481 1.00 18.13 ?  571 TYR B CD2   1 
ATOM   10145 C  CE1   . TYR B 1 571 ? 127.267 166.608 153.073 1.00 23.37 ?  571 TYR B CE1   1 
ATOM   10146 C  CE2   . TYR B 1 571 ? 128.030 164.409 153.612 1.00 22.50 ?  571 TYR B CE2   1 
ATOM   10147 C  CZ    . TYR B 1 571 ? 128.175 165.585 152.911 1.00 27.73 ?  571 TYR B CZ    1 
ATOM   10148 O  OH    . TYR B 1 571 ? 129.232 165.739 152.045 1.00 26.73 ?  571 TYR B OH    1 
ATOM   10149 N  N     . HIS B 1 572 ? 123.015 162.533 154.871 1.00 20.02 ?  572 HIS B N     1 
ATOM   10150 C  CA    . HIS B 1 572 ? 123.059 161.173 154.354 1.00 13.85 ?  572 HIS B CA    1 
ATOM   10151 C  C     . HIS B 1 572 ? 121.652 160.697 154.025 1.00 22.03 ?  572 HIS B C     1 
ATOM   10152 O  O     . HIS B 1 572 ? 120.748 160.793 154.863 1.00 26.66 ?  572 HIS B O     1 
ATOM   10153 C  CB    . HIS B 1 572 ? 123.706 160.223 155.364 1.00 13.30 ?  572 HIS B CB    1 
ATOM   10154 C  CG    . HIS B 1 572 ? 124.993 160.732 155.932 1.00 14.70 ?  572 HIS B CG    1 
ATOM   10155 N  ND1   . HIS B 1 572 ? 125.056 161.444 157.110 1.00 18.30 ?  572 HIS B ND1   1 
ATOM   10156 C  CD2   . HIS B 1 572 ? 126.267 160.632 155.485 1.00 16.96 ?  572 HIS B CD2   1 
ATOM   10157 C  CE1   . HIS B 1 572 ? 126.313 161.761 157.364 1.00 19.14 ?  572 HIS B CE1   1 
ATOM   10158 N  NE2   . HIS B 1 572 ? 127.068 161.280 156.394 1.00 26.58 ?  572 HIS B NE2   1 
ATOM   10159 N  N     . SER B 1 573 ? 121.472 160.189 152.805 1.00 13.21 ?  573 SER B N     1 
ATOM   10160 C  CA    . SER B 1 573 ? 120.203 159.571 152.442 1.00 7.91  ?  573 SER B CA    1 
ATOM   10161 C  C     . SER B 1 573 ? 119.962 158.304 153.251 1.00 14.44 ?  573 SER B C     1 
ATOM   10162 O  O     . SER B 1 573 ? 118.827 158.022 153.654 1.00 21.39 ?  573 SER B O     1 
ATOM   10163 C  CB    . SER B 1 573 ? 120.177 159.267 150.946 1.00 14.15 ?  573 SER B CB    1 
ATOM   10164 O  OG    . SER B 1 573 ? 121.369 158.617 150.544 1.00 22.11 ?  573 SER B OG    1 
ATOM   10165 N  N     . TYR B 1 574 ? 121.015 157.528 153.490 1.00 14.03 ?  574 TYR B N     1 
ATOM   10166 C  CA    . TYR B 1 574 ? 120.936 156.300 154.264 1.00 7.35  ?  574 TYR B CA    1 
ATOM   10167 C  C     . TYR B 1 574 ? 122.105 156.267 155.233 1.00 8.48  ?  574 TYR B C     1 
ATOM   10168 O  O     . TYR B 1 574 ? 123.222 156.653 154.879 1.00 18.38 ?  574 TYR B O     1 
ATOM   10169 C  CB    . TYR B 1 574 ? 120.950 155.065 153.356 1.00 10.15 ?  574 TYR B CB    1 
ATOM   10170 C  CG    . TYR B 1 574 ? 119.884 155.098 152.287 1.00 7.41  ?  574 TYR B CG    1 
ATOM   10171 C  CD1   . TYR B 1 574 ? 120.116 155.724 151.070 1.00 9.48  ?  574 TYR B CD1   1 
ATOM   10172 C  CD2   . TYR B 1 574 ? 118.644 154.511 152.495 1.00 7.15  ?  574 TYR B CD2   1 
ATOM   10173 C  CE1   . TYR B 1 574 ? 119.145 155.767 150.093 1.00 9.78  ?  574 TYR B CE1   1 
ATOM   10174 C  CE2   . TYR B 1 574 ? 117.668 154.546 151.522 1.00 9.31  ?  574 TYR B CE2   1 
ATOM   10175 C  CZ    . TYR B 1 574 ? 117.924 155.176 150.324 1.00 4.50  ?  574 TYR B CZ    1 
ATOM   10176 O  OH    . TYR B 1 574 ? 116.957 155.212 149.349 1.00 17.16 ?  574 TYR B OH    1 
ATOM   10177 N  N     . ARG B 1 575 ? 121.843 155.816 156.454 1.00 10.32 ?  575 ARG B N     1 
ATOM   10178 C  CA    . ARG B 1 575 ? 122.836 155.878 157.519 1.00 4.99  ?  575 ARG B CA    1 
ATOM   10179 C  C     . ARG B 1 575 ? 123.153 154.530 158.144 1.00 12.76 ?  575 ARG B C     1 
ATOM   10180 O  O     . ARG B 1 575 ? 124.322 154.246 158.412 1.00 18.56 ?  575 ARG B O     1 
ATOM   10181 C  CB    . ARG B 1 575 ? 122.360 156.837 158.616 1.00 13.95 ?  575 ARG B CB    1 
ATOM   10182 C  CG    . ARG B 1 575 ? 122.133 158.260 158.144 1.00 6.32  ?  575 ARG B CG    1 
ATOM   10183 C  CD    . ARG B 1 575 ? 121.127 158.968 159.030 1.00 13.67 ?  575 ARG B CD    1 
ATOM   10184 N  NE    . ARG B 1 575 ? 119.788 158.411 158.888 1.00 18.22 ?  575 ARG B NE    1 
ATOM   10185 C  CZ    . ARG B 1 575 ? 119.225 157.580 159.754 1.00 13.40 ?  575 ARG B CZ    1 
ATOM   10186 N  NH1   . ARG B 1 575 ? 119.863 157.178 160.840 1.00 12.95 1  575 ARG B NH1   1 
ATOM   10187 N  NH2   . ARG B 1 575 ? 117.991 157.141 159.526 1.00 11.24 ?  575 ARG B NH2   1 
ATOM   10188 N  N     . LEU B 1 576 ? 122.151 153.691 158.383 1.00 20.40 ?  576 LEU B N     1 
ATOM   10189 C  CA    . LEU B 1 576 ? 122.324 152.462 159.142 1.00 10.53 ?  576 LEU B CA    1 
ATOM   10190 C  C     . LEU B 1 576 ? 122.039 151.257 158.260 1.00 5.36  ?  576 LEU B C     1 
ATOM   10191 O  O     . LEU B 1 576 ? 120.964 151.160 157.662 1.00 15.05 ?  576 LEU B O     1 
ATOM   10192 C  CB    . LEU B 1 576 ? 121.405 152.442 160.366 1.00 6.04  ?  576 LEU B CB    1 
ATOM   10193 C  CG    . LEU B 1 576 ? 121.459 153.657 161.291 1.00 7.13  ?  576 LEU B CG    1 
ATOM   10194 C  CD1   . LEU B 1 576 ? 120.391 153.550 162.366 1.00 13.51 ?  576 LEU B CD1   1 
ATOM   10195 C  CD2   . LEU B 1 576 ? 122.832 153.796 161.913 1.00 10.43 ?  576 LEU B CD2   1 
ATOM   10196 N  N     . CYS B 1 577 ? 123.005 150.345 158.182 1.00 14.04 ?  577 CYS B N     1 
ATOM   10197 C  CA    . CYS B 1 577 ? 122.808 149.044 157.559 1.00 8.07  ?  577 CYS B CA    1 
ATOM   10198 C  C     . CYS B 1 577 ? 123.679 148.046 158.305 1.00 14.92 ?  577 CYS B C     1 
ATOM   10199 O  O     . CYS B 1 577 ? 124.854 148.317 158.563 1.00 21.80 ?  577 CYS B O     1 
ATOM   10200 C  CB    . CYS B 1 577 ? 123.142 149.073 156.059 1.00 5.93  ?  577 CYS B CB    1 
ATOM   10201 S  SG    . CYS B 1 577 ? 124.859 148.741 155.593 1.00 35.18 ?  577 CYS B SG    1 
ATOM   10202 N  N     . ILE B 1 578 ? 123.095 146.911 158.675 1.00 16.01 ?  578 ILE B N     1 
ATOM   10203 C  CA    . ILE B 1 578 ? 123.759 145.927 159.520 1.00 12.46 ?  578 ILE B CA    1 
ATOM   10204 C  C     . ILE B 1 578 ? 124.298 144.827 158.611 1.00 9.65  ?  578 ILE B C     1 
ATOM   10205 O  O     . ILE B 1 578 ? 123.566 143.926 158.195 1.00 18.17 ?  578 ILE B O     1 
ATOM   10206 C  CB    . ILE B 1 578 ? 122.818 145.378 160.595 1.00 9.77  ?  578 ILE B CB    1 
ATOM   10207 C  CG1   . ILE B 1 578 ? 122.300 146.523 161.466 1.00 8.00  ?  578 ILE B CG1   1 
ATOM   10208 C  CG2   . ILE B 1 578 ? 123.532 144.358 161.457 1.00 9.50  ?  578 ILE B CG2   1 
ATOM   10209 C  CD1   . ILE B 1 578 ? 121.519 146.066 162.667 1.00 8.95  ?  578 ILE B CD1   1 
ATOM   10210 N  N     . ALA B 1 579 ? 125.588 144.911 158.303 1.00 17.09 ?  579 ALA B N     1 
ATOM   10211 C  CA    . ALA B 1 579 ? 126.281 143.938 157.479 1.00 7.33  ?  579 ALA B CA    1 
ATOM   10212 C  C     . ALA B 1 579 ? 126.578 142.669 158.275 1.00 21.03 ?  579 ALA B C     1 
ATOM   10213 O  O     . ALA B 1 579 ? 126.513 142.670 159.506 1.00 28.62 ?  579 ALA B O     1 
ATOM   10214 C  CB    . ALA B 1 579 ? 127.573 144.544 156.943 1.00 11.73 ?  579 ALA B CB    1 
ATOM   10215 N  N     . PRO B 1 580 ? 126.880 141.560 157.592 1.00 25.04 ?  580 PRO B N     1 
ATOM   10216 C  CA    . PRO B 1 580 ? 127.228 140.328 158.321 1.00 22.61 ?  580 PRO B CA    1 
ATOM   10217 C  C     . PRO B 1 580 ? 128.459 140.454 159.206 1.00 25.92 ?  580 PRO B C     1 
ATOM   10218 O  O     . PRO B 1 580 ? 128.517 139.793 160.251 1.00 32.85 ?  580 PRO B O     1 
ATOM   10219 C  CB    . PRO B 1 580 ? 127.440 139.299 157.200 1.00 22.52 ?  580 PRO B CB    1 
ATOM   10220 C  CG    . PRO B 1 580 ? 127.546 140.090 155.938 1.00 21.75 ?  580 PRO B CG    1 
ATOM   10221 C  CD    . PRO B 1 580 ? 126.734 141.317 156.148 1.00 19.76 ?  580 PRO B CD    1 
ATOM   10222 N  N     . THR B 1 581 ? 129.439 141.278 158.826 1.00 21.55 ?  581 THR B N     1 
ATOM   10223 C  CA    . THR B 1 581 ? 130.682 141.465 159.584 1.00 29.18 ?  581 THR B CA    1 
ATOM   10224 C  C     . THR B 1 581 ? 131.350 140.119 159.886 1.00 28.51 ?  581 THR B C     1 
ATOM   10225 O  O     . THR B 1 581 ? 131.484 139.693 161.032 1.00 27.81 ?  581 THR B O     1 
ATOM   10226 C  CB    . THR B 1 581 ? 130.445 142.251 160.879 1.00 28.11 ?  581 THR B CB    1 
ATOM   10227 O  OG1   . THR B 1 581 ? 130.102 141.348 161.938 1.00 27.66 ?  581 THR B OG1   1 
ATOM   10228 C  CG2   . THR B 1 581 ? 129.346 143.287 160.707 1.00 30.44 ?  581 THR B CG2   1 
ATOM   10229 N  N     . GLY B 1 582 ? 131.774 139.463 158.809 1.00 31.48 ?  582 GLY B N     1 
ATOM   10230 C  CA    . GLY B 1 582 ? 132.274 138.107 158.899 1.00 33.44 ?  582 GLY B CA    1 
ATOM   10231 C  C     . GLY B 1 582 ? 133.572 137.930 159.661 1.00 37.00 ?  582 GLY B C     1 
ATOM   10232 O  O     . GLY B 1 582 ? 133.582 137.326 160.739 1.00 38.24 ?  582 GLY B O     1 
ATOM   10233 N  N     . SER B 1 583 ? 134.677 138.450 159.123 1.00 31.25 ?  583 SER B N     1 
ATOM   10234 C  CA    . SER B 1 583 ? 135.991 138.175 159.688 1.00 33.74 ?  583 SER B CA    1 
ATOM   10235 C  C     . SER B 1 583 ? 136.509 139.275 160.604 1.00 35.09 ?  583 SER B C     1 
ATOM   10236 O  O     . SER B 1 583 ? 137.352 138.993 161.463 1.00 37.38 ?  583 SER B O     1 
ATOM   10237 C  CB    . SER B 1 583 ? 137.011 137.940 158.567 1.00 37.87 ?  583 SER B CB    1 
ATOM   10238 O  OG    . SER B 1 583 ? 136.983 136.592 158.134 1.00 41.00 ?  583 SER B OG    1 
ATOM   10239 N  N     . ILE B 1 584 ? 136.031 140.511 160.449 1.00 33.94 ?  584 ILE B N     1 
ATOM   10240 C  CA    . ILE B 1 584 ? 136.474 141.583 161.329 1.00 27.57 ?  584 ILE B CA    1 
ATOM   10241 C  C     . ILE B 1 584 ? 135.859 141.461 162.717 1.00 26.21 ?  584 ILE B C     1 
ATOM   10242 O  O     . ILE B 1 584 ? 136.315 142.127 163.654 1.00 29.85 ?  584 ILE B O     1 
ATOM   10243 C  CB    . ILE B 1 584 ? 136.163 142.953 160.698 1.00 31.69 ?  584 ILE B CB    1 
ATOM   10244 C  CG1   . ILE B 1 584 ? 137.137 144.011 161.215 1.00 28.37 ?  584 ILE B CG1   1 
ATOM   10245 C  CG2   . ILE B 1 584 ? 134.724 143.360 160.978 1.00 29.13 ?  584 ILE B CG2   1 
ATOM   10246 C  CD1   . ILE B 1 584 ? 138.587 143.675 161.014 1.00 31.61 ?  584 ILE B CD1   1 
ATOM   10247 N  N     . SER B 1 585 ? 134.832 140.623 162.877 1.00 31.58 ?  585 SER B N     1 
ATOM   10248 C  CA    . SER B 1 585 ? 134.279 140.385 164.204 1.00 30.22 ?  585 SER B CA    1 
ATOM   10249 C  C     . SER B 1 585 ? 135.245 139.592 165.073 1.00 28.05 ?  585 SER B C     1 
ATOM   10250 O  O     . SER B 1 585 ? 135.179 139.673 166.305 1.00 26.72 ?  585 SER B O     1 
ATOM   10251 C  CB    . SER B 1 585 ? 132.938 139.659 164.096 1.00 25.61 ?  585 SER B CB    1 
ATOM   10252 O  OG    . SER B 1 585 ? 133.092 138.396 163.474 1.00 30.23 ?  585 SER B OG    1 
ATOM   10253 N  N     . TYR B 1 586 ? 136.136 138.816 164.452 1.00 31.10 ?  586 TYR B N     1 
ATOM   10254 C  CA    . TYR B 1 586 ? 137.154 138.093 165.205 1.00 32.10 ?  586 TYR B CA    1 
ATOM   10255 C  C     . TYR B 1 586 ? 138.098 139.058 165.911 1.00 31.26 ?  586 TYR B C     1 
ATOM   10256 O  O     . TYR B 1 586 ? 138.401 138.893 167.098 1.00 34.53 ?  586 TYR B O     1 
ATOM   10257 C  CB    . TYR B 1 586 ? 137.938 137.177 164.268 1.00 28.08 ?  586 TYR B CB    1 
ATOM   10258 C  CG    . TYR B 1 586 ? 137.207 135.917 163.875 1.00 31.07 ?  586 TYR B CG    1 
ATOM   10259 C  CD1   . TYR B 1 586 ? 136.827 134.985 164.828 1.00 31.09 ?  586 TYR B CD1   1 
ATOM   10260 C  CD2   . TYR B 1 586 ? 136.895 135.664 162.547 1.00 31.81 ?  586 TYR B CD2   1 
ATOM   10261 C  CE1   . TYR B 1 586 ? 136.159 133.834 164.469 1.00 33.96 ?  586 TYR B CE1   1 
ATOM   10262 C  CE2   . TYR B 1 586 ? 136.226 134.516 162.179 1.00 30.57 ?  586 TYR B CE2   1 
ATOM   10263 C  CZ    . TYR B 1 586 ? 135.861 133.605 163.143 1.00 34.73 ?  586 TYR B CZ    1 
ATOM   10264 O  OH    . TYR B 1 586 ? 135.194 132.459 162.778 1.00 37.76 ?  586 TYR B OH    1 
ATOM   10265 N  N     . VAL B 1 587 ? 138.563 140.082 165.190 1.00 28.11 ?  587 VAL B N     1 
ATOM   10266 C  CA    . VAL B 1 587 ? 139.537 141.018 165.745 1.00 24.65 ?  587 VAL B CA    1 
ATOM   10267 C  C     . VAL B 1 587 ? 138.936 141.793 166.909 1.00 29.14 ?  587 VAL B C     1 
ATOM   10268 O  O     . VAL B 1 587 ? 139.616 142.083 167.900 1.00 35.72 ?  587 VAL B O     1 
ATOM   10269 C  CB    . VAL B 1 587 ? 140.051 141.963 164.643 1.00 30.15 ?  587 VAL B CB    1 
ATOM   10270 C  CG1   . VAL B 1 587 ? 141.203 142.806 165.160 1.00 30.11 ?  587 VAL B CG1   1 
ATOM   10271 C  CG2   . VAL B 1 587 ? 140.468 141.170 163.415 1.00 28.67 ?  587 VAL B CG2   1 
ATOM   10272 N  N     . GLN B 1 588 ? 137.655 142.135 166.812 1.00 31.14 ?  588 GLN B N     1 
ATOM   10273 C  CA    . GLN B 1 588 ? 136.983 142.907 167.847 1.00 24.26 ?  588 GLN B CA    1 
ATOM   10274 C  C     . GLN B 1 588 ? 136.526 142.055 169.021 1.00 25.55 ?  588 GLN B C     1 
ATOM   10275 O  O     . GLN B 1 588 ? 135.972 142.605 169.979 1.00 32.76 ?  588 GLN B O     1 
ATOM   10276 C  CB    . GLN B 1 588 ? 135.782 143.646 167.254 1.00 25.03 ?  588 GLN B CB    1 
ATOM   10277 C  CG    . GLN B 1 588 ? 136.153 144.840 166.397 1.00 28.82 ?  588 GLN B CG    1 
ATOM   10278 C  CD    . GLN B 1 588 ? 136.078 146.145 167.163 1.00 24.32 ?  588 GLN B CD    1 
ATOM   10279 O  OE1   . GLN B 1 588 ? 135.101 146.413 167.859 1.00 29.94 ?  588 GLN B OE1   1 
ATOM   10280 N  NE2   . GLN B 1 588 ? 137.113 146.966 167.036 1.00 26.90 ?  588 GLN B NE2   1 
ATOM   10281 N  N     . SER B 1 589 ? 136.752 140.742 168.973 1.00 30.06 ?  589 SER B N     1 
ATOM   10282 C  CA    . SER B 1 589 ? 136.270 139.809 169.989 1.00 27.12 ?  589 SER B CA    1 
ATOM   10283 C  C     . SER B 1 589 ? 134.766 139.979 170.185 1.00 26.93 ?  589 SER B C     1 
ATOM   10284 O  O     . SER B 1 589 ? 134.270 140.251 171.279 1.00 28.72 ?  589 SER B O     1 
ATOM   10285 C  CB    . SER B 1 589 ? 137.030 139.985 171.306 1.00 32.57 ?  589 SER B CB    1 
ATOM   10286 O  OG    . SER B 1 589 ? 138.399 139.666 171.146 1.00 36.64 ?  589 SER B OG    1 
ATOM   10287 N  N     . SER B 1 590 ? 134.043 139.821 169.080 1.00 25.89 ?  590 SER B N     1 
ATOM   10288 C  CA    . SER B 1 590 ? 132.617 140.090 169.039 1.00 22.92 ?  590 SER B CA    1 
ATOM   10289 C  C     . SER B 1 590 ? 131.916 139.010 168.233 1.00 25.94 ?  590 SER B C     1 
ATOM   10290 O  O     . SER B 1 590 ? 132.502 138.407 167.330 1.00 29.51 ?  590 SER B O     1 
ATOM   10291 C  CB    . SER B 1 590 ? 132.332 141.467 168.427 1.00 21.98 ?  590 SER B CB    1 
ATOM   10292 O  OG    . SER B 1 590 ? 132.135 141.373 167.029 1.00 31.28 ?  590 SER B OG    1 
ATOM   10293 N  N     . THR B 1 591 ? 130.655 138.765 168.574 1.00 25.52 ?  591 THR B N     1 
ATOM   10294 C  CA    . THR B 1 591 ? 129.827 137.882 167.768 1.00 21.76 ?  591 THR B CA    1 
ATOM   10295 C  C     . THR B 1 591 ? 129.445 138.571 166.464 1.00 24.15 ?  591 THR B C     1 
ATOM   10296 O  O     . THR B 1 591 ? 129.287 139.793 166.403 1.00 22.75 ?  591 THR B O     1 
ATOM   10297 C  CB    . THR B 1 591 ? 128.574 137.466 168.534 1.00 22.02 ?  591 THR B CB    1 
ATOM   10298 O  OG1   . THR B 1 591 ? 127.668 138.574 168.613 1.00 29.69 ?  591 THR B OG1   1 
ATOM   10299 C  CG2   . THR B 1 591 ? 128.940 137.017 169.937 1.00 20.22 ?  591 THR B CG2   1 
ATOM   10300 N  N     . ALA B 1 592 ? 129.302 137.770 165.412 1.00 22.71 ?  592 ALA B N     1 
ATOM   10301 C  CA    . ALA B 1 592 ? 129.094 138.308 164.074 1.00 20.11 ?  592 ALA B CA    1 
ATOM   10302 C  C     . ALA B 1 592 ? 127.745 139.010 163.981 1.00 19.32 ?  592 ALA B C     1 
ATOM   10303 O  O     . ALA B 1 592 ? 126.695 138.372 164.105 1.00 27.49 ?  592 ALA B O     1 
ATOM   10304 C  CB    . ALA B 1 592 ? 129.186 137.190 163.039 1.00 24.99 ?  592 ALA B CB    1 
ATOM   10305 N  N     . SER B 1 593 ? 127.782 140.323 163.772 1.00 25.09 ?  593 SER B N     1 
ATOM   10306 C  CA    . SER B 1 593 ? 126.596 141.135 163.469 1.00 14.55 ?  593 SER B CA    1 
ATOM   10307 C  C     . SER B 1 593 ? 125.609 141.033 164.633 1.00 16.18 ?  593 SER B C     1 
ATOM   10308 O  O     . SER B 1 593 ? 126.001 140.779 165.780 1.00 27.98 ?  593 SER B O     1 
ATOM   10309 C  CB    . SER B 1 593 ? 126.035 140.713 162.123 1.00 27.06 ?  593 SER B CB    1 
ATOM   10310 O  OG    . SER B 1 593 ? 125.042 141.613 161.673 1.00 23.36 ?  593 SER B OG    1 
ATOM   10311 N  N     . VAL B 1 594 ? 124.321 141.234 164.350 1.00 19.65 ?  594 VAL B N     1 
ATOM   10312 C  CA    . VAL B 1 594 ? 123.265 141.041 165.334 1.00 19.52 ?  594 VAL B CA    1 
ATOM   10313 C  C     . VAL B 1 594 ? 122.709 139.622 165.287 1.00 18.59 ?  594 VAL B C     1 
ATOM   10314 O  O     . VAL B 1 594 ? 121.733 139.317 165.978 1.00 18.18 ?  594 VAL B O     1 
ATOM   10315 C  CB    . VAL B 1 594 ? 122.143 142.075 165.152 1.00 17.07 ?  594 VAL B CB    1 
ATOM   10316 C  CG1   . VAL B 1 594 ? 122.677 143.480 165.376 1.00 12.24 ?  594 VAL B CG1   1 
ATOM   10317 C  CG2   . VAL B 1 594 ? 121.524 141.951 163.771 1.00 19.04 ?  594 VAL B CG2   1 
ATOM   10318 N  N     . MET B 1 595 ? 123.309 138.748 164.484 1.00 23.61 ?  595 MET B N     1 
ATOM   10319 C  CA    . MET B 1 595 ? 122.877 137.366 164.418 1.00 19.01 ?  595 MET B CA    1 
ATOM   10320 C  C     . MET B 1 595 ? 123.293 136.618 165.683 1.00 26.69 ?  595 MET B C     1 
ATOM   10321 O  O     . MET B 1 595 ? 124.304 136.951 166.308 1.00 29.65 ?  595 MET B O     1 
ATOM   10322 C  CB    . MET B 1 595 ? 123.478 136.673 163.198 1.00 18.08 ?  595 MET B CB    1 
ATOM   10323 C  CG    . MET B 1 595 ? 122.727 136.885 161.891 1.00 24.07 ?  595 MET B CG    1 
ATOM   10324 S  SD    . MET B 1 595 ? 120.960 137.170 162.093 1.00 29.78 ?  595 MET B SD    1 
ATOM   10325 C  CE    . MET B 1 595 ? 120.884 138.931 161.789 1.00 22.55 ?  595 MET B CE    1 
ATOM   10326 N  N     . PRO B 1 596 ? 122.530 135.606 166.084 1.00 29.56 ?  596 PRO B N     1 
ATOM   10327 C  CA    . PRO B 1 596 ? 122.980 134.732 167.170 1.00 19.09 ?  596 PRO B CA    1 
ATOM   10328 C  C     . PRO B 1 596 ? 124.130 133.845 166.718 1.00 25.93 ?  596 PRO B C     1 
ATOM   10329 O  O     . PRO B 1 596 ? 124.309 133.562 165.532 1.00 30.62 ?  596 PRO B O     1 
ATOM   10330 C  CB    . PRO B 1 596 ? 121.735 133.909 167.506 1.00 20.74 ?  596 PRO B CB    1 
ATOM   10331 C  CG    . PRO B 1 596 ? 120.934 133.911 166.254 1.00 23.25 ?  596 PRO B CG    1 
ATOM   10332 C  CD    . PRO B 1 596 ? 121.203 135.222 165.571 1.00 25.77 ?  596 PRO B CD    1 
ATOM   10333 N  N     . ILE B 1 597 ? 124.924 133.409 167.698 1.00 28.44 ?  597 ILE B N     1 
ATOM   10334 C  CA    . ILE B 1 597 ? 126.130 132.646 167.405 1.00 31.03 ?  597 ILE B CA    1 
ATOM   10335 C  C     . ILE B 1 597 ? 125.764 131.302 166.790 1.00 34.42 ?  597 ILE B C     1 
ATOM   10336 O  O     . ILE B 1 597 ? 124.788 130.653 167.193 1.00 37.08 ?  597 ILE B O     1 
ATOM   10337 C  CB    . ILE B 1 597 ? 126.976 132.463 168.676 1.00 32.17 ?  597 ILE B CB    1 
ATOM   10338 C  CG1   . ILE B 1 597 ? 126.202 131.669 169.729 1.00 30.45 ?  597 ILE B CG1   1 
ATOM   10339 C  CG2   . ILE B 1 597 ? 127.396 133.811 169.228 1.00 29.22 ?  597 ILE B CG2   1 
ATOM   10340 C  CD1   . ILE B 1 597 ? 127.075 130.829 170.626 1.00 29.18 ?  597 ILE B CD1   1 
ATOM   10341 N  N     . MET B 1 598 ? 126.541 130.886 165.789 1.00 40.22 ?  598 MET B N     1 
ATOM   10342 C  CA    . MET B 1 598 ? 126.328 129.575 165.186 1.00 38.65 ?  598 MET B CA    1 
ATOM   10343 C  C     . MET B 1 598 ? 126.741 128.459 166.137 1.00 36.48 ?  598 MET B C     1 
ATOM   10344 O  O     . MET B 1 598 ? 126.037 127.451 166.264 1.00 42.09 ?  598 MET B O     1 
ATOM   10345 C  CB    . MET B 1 598 ? 127.100 129.472 163.872 1.00 38.14 ?  598 MET B CB    1 
ATOM   10346 C  CG    . MET B 1 598 ? 126.381 130.082 162.684 1.00 35.63 ?  598 MET B CG    1 
ATOM   10347 S  SD    . MET B 1 598 ? 127.500 130.557 161.355 1.00 53.34 ?  598 MET B SD    1 
ATOM   10348 C  CE    . MET B 1 598 ? 128.659 131.596 162.241 1.00 40.76 ?  598 MET B CE    1 
ATOM   10349 N  N     . GLU B 1 599 ? 127.874 128.623 166.814 1.00 37.86 ?  599 GLU B N     1 
ATOM   10350 C  CA    . GLU B 1 599 ? 128.373 127.624 167.744 1.00 37.80 ?  599 GLU B CA    1 
ATOM   10351 C  C     . GLU B 1 599 ? 129.094 128.328 168.882 1.00 34.97 ?  599 GLU B C     1 
ATOM   10352 O  O     . GLU B 1 599 ? 129.622 129.430 168.711 1.00 40.23 ?  599 GLU B O     1 
ATOM   10353 C  CB    . GLU B 1 599 ? 129.313 126.631 167.051 1.00 39.85 ?  599 GLU B CB    1 
ATOM   10354 C  CG    . GLU B 1 599 ? 130.381 127.294 166.203 1.00 37.81 ?  599 GLU B CG    1 
ATOM   10355 C  CD    . GLU B 1 599 ? 130.673 126.530 164.927 1.00 43.29 ?  599 GLU B CD    1 
ATOM   10356 O  OE1   . GLU B 1 599 ? 130.483 125.295 164.917 1.00 44.64 ?  599 GLU B OE1   1 
ATOM   10357 O  OE2   . GLU B 1 599 ? 131.093 127.163 163.937 1.00 43.83 -1 599 GLU B OE2   1 
ATOM   10358 N  N     . ARG B 1 600 ? 129.109 127.681 170.048 1.00 36.52 ?  600 ARG B N     1 
ATOM   10359 C  CA    . ARG B 1 600 ? 129.792 128.257 171.201 1.00 32.88 ?  600 ARG B CA    1 
ATOM   10360 C  C     . ARG B 1 600 ? 131.300 128.268 170.996 1.00 33.71 ?  600 ARG B C     1 
ATOM   10361 O  O     . ARG B 1 600 ? 131.961 129.288 171.218 1.00 39.87 ?  600 ARG B O     1 
ATOM   10362 C  CB    . ARG B 1 600 ? 129.421 127.484 172.465 1.00 35.62 ?  600 ARG B CB    1 
ATOM   10363 C  CG    . ARG B 1 600 ? 128.030 127.788 172.974 1.00 33.67 ?  600 ARG B CG    1 
ATOM   10364 C  CD    . ARG B 1 600 ? 127.811 127.200 174.348 1.00 31.09 ?  600 ARG B CD    1 
ATOM   10365 N  NE    . ARG B 1 600 ? 126.437 127.369 174.802 1.00 32.40 ?  600 ARG B NE    1 
ATOM   10366 C  CZ    . ARG B 1 600 ? 125.427 126.593 174.435 1.00 34.59 ?  600 ARG B CZ    1 
ATOM   10367 N  NH1   . ARG B 1 600 ? 125.598 125.588 173.593 1.00 33.92 1  600 ARG B NH1   1 
ATOM   10368 N  NH2   . ARG B 1 600 ? 124.214 126.833 174.926 1.00 35.08 ?  600 ARG B NH2   1 
ATOM   10369 N  N     . ILE B 1 601 ? 131.863 127.139 170.577 1.00 38.78 ?  601 ILE B N     1 
ATOM   10370 C  CA    . ILE B 1 601 ? 133.274 127.030 170.231 1.00 37.26 ?  601 ILE B CA    1 
ATOM   10371 C  C     . ILE B 1 601 ? 133.353 126.525 168.800 1.00 37.70 ?  601 ILE B C     1 
ATOM   10372 O  O     . ILE B 1 601 ? 132.811 125.458 168.483 1.00 42.98 ?  601 ILE B O     1 
ATOM   10373 C  CB    . ILE B 1 601 ? 134.032 126.094 171.186 1.00 39.69 ?  601 ILE B CB    1 
ATOM   10374 C  CG1   . ILE B 1 601 ? 133.688 126.417 172.640 1.00 40.45 ?  601 ILE B CG1   1 
ATOM   10375 C  CG2   . ILE B 1 601 ? 135.530 126.201 170.956 1.00 37.99 ?  601 ILE B CG2   1 
ATOM   10376 C  CD1   . ILE B 1 601 ? 134.222 125.410 173.633 1.00 39.25 ?  601 ILE B CD1   1 
ATOM   10377 N  N     . GLU B 1 602 ? 134.023 127.282 167.938 1.00 45.48 ?  602 GLU B N     1 
ATOM   10378 C  CA    . GLU B 1 602 ? 134.143 126.928 166.532 1.00 46.01 ?  602 GLU B CA    1 
ATOM   10379 C  C     . GLU B 1 602 ? 135.530 126.372 166.246 1.00 47.78 ?  602 GLU B C     1 
ATOM   10380 O  O     . GLU B 1 602 ? 136.542 126.967 166.625 1.00 47.96 ?  602 GLU B O     1 
ATOM   10381 C  CB    . GLU B 1 602 ? 133.872 128.136 165.635 1.00 44.80 ?  602 GLU B CB    1 
ATOM   10382 C  CG    . GLU B 1 602 ? 134.469 129.433 166.138 1.00 47.22 ?  602 GLU B CG    1 
ATOM   10383 C  CD    . GLU B 1 602 ? 134.582 130.477 165.049 1.00 50.05 ?  602 GLU B CD    1 
ATOM   10384 O  OE1   . GLU B 1 602 ? 133.537 131.019 164.630 1.00 48.81 ?  602 GLU B OE1   1 
ATOM   10385 O  OE2   . GLU B 1 602 ? 135.716 130.751 164.607 1.00 49.61 -1 602 GLU B OE2   1 
ATOM   10386 N  N     . GLU B 1 603 ? 135.571 125.224 165.574 1.00 53.84 ?  603 GLU B N     1 
ATOM   10387 C  CA    . GLU B 1 603 ? 136.820 124.569 165.203 1.00 54.70 ?  603 GLU B CA    1 
ATOM   10388 C  C     . GLU B 1 603 ? 137.125 124.908 163.749 1.00 53.81 ?  603 GLU B C     1 
ATOM   10389 O  O     . GLU B 1 603 ? 136.395 124.498 162.841 1.00 54.77 ?  603 GLU B O     1 
ATOM   10390 C  CB    . GLU B 1 603 ? 136.726 123.060 165.413 1.00 54.03 ?  603 GLU B CB    1 
ATOM   10391 C  CG    . GLU B 1 603 ? 137.980 122.297 165.021 1.00 56.11 ?  603 GLU B CG    1 
ATOM   10392 C  CD    . GLU B 1 603 ? 137.731 120.810 164.863 1.00 58.17 ?  603 GLU B CD    1 
ATOM   10393 O  OE1   . GLU B 1 603 ? 137.600 120.114 165.892 1.00 57.94 ?  603 GLU B OE1   1 
ATOM   10394 O  OE2   . GLU B 1 603 ? 137.665 120.336 163.709 1.00 56.54 -1 603 GLU B OE2   1 
ATOM   10395 N  N     . ARG B 1 604 ? 138.204 125.656 163.533 1.00 55.14 ?  604 ARG B N     1 
ATOM   10396 C  CA    . ARG B 1 604 ? 138.612 126.092 162.207 1.00 55.62 ?  604 ARG B CA    1 
ATOM   10397 C  C     . ARG B 1 604 ? 139.998 125.545 161.897 1.00 56.99 ?  604 ARG B C     1 
ATOM   10398 O  O     . ARG B 1 604 ? 140.895 125.584 162.744 1.00 58.94 ?  604 ARG B O     1 
ATOM   10399 C  CB    . ARG B 1 604 ? 138.619 127.621 162.106 1.00 57.20 ?  604 ARG B CB    1 
ATOM   10400 C  CG    . ARG B 1 604 ? 137.242 128.251 161.958 1.00 57.77 ?  604 ARG B CG    1 
ATOM   10401 C  CD    . ARG B 1 604 ? 136.359 127.457 161.012 1.00 56.81 ?  604 ARG B CD    1 
ATOM   10402 N  NE    . ARG B 1 604 ? 135.264 126.796 161.712 1.00 59.20 ?  604 ARG B NE    1 
ATOM   10403 C  CZ    . ARG B 1 604 ? 134.121 127.382 162.039 1.00 59.01 ?  604 ARG B CZ    1 
ATOM   10404 N  NH1   . ARG B 1 604 ? 133.887 128.651 161.748 1.00 56.40 1  604 ARG B NH1   1 
ATOM   10405 N  NH2   . ARG B 1 604 ? 133.188 126.676 162.672 1.00 56.67 ?  604 ARG B NH2   1 
ATOM   10406 N  N     . THR B 1 605 ? 140.175 125.045 160.679 1.00 63.74 ?  605 THR B N     1 
ATOM   10407 C  CA    . THR B 1 605 ? 141.440 124.462 160.254 1.00 64.57 ?  605 THR B CA    1 
ATOM   10408 C  C     . THR B 1 605 ? 142.240 125.504 159.481 1.00 64.75 ?  605 THR B C     1 
ATOM   10409 O  O     . THR B 1 605 ? 141.780 126.006 158.449 1.00 64.19 ?  605 THR B O     1 
ATOM   10410 C  CB    . THR B 1 605 ? 141.209 123.219 159.395 1.00 64.44 ?  605 THR B CB    1 
ATOM   10411 O  OG1   . THR B 1 605 ? 140.496 122.236 160.156 1.00 64.01 ?  605 THR B OG1   1 
ATOM   10412 C  CG2   . THR B 1 605 ? 142.537 122.635 158.941 1.00 64.39 ?  605 THR B CG2   1 
ATOM   10413 N  N     . TYR B 1 606 ? 143.428 125.825 159.984 1.00 64.82 ?  606 TYR B N     1 
ATOM   10414 C  CA    . TYR B 1 606 ? 144.351 126.736 159.320 1.00 66.48 ?  606 TYR B CA    1 
ATOM   10415 C  C     . TYR B 1 606 ? 145.655 125.999 159.058 1.00 67.41 ?  606 TYR B C     1 
ATOM   10416 O  O     . TYR B 1 606 ? 146.242 125.422 159.981 1.00 65.23 ?  606 TYR B O     1 
ATOM   10417 C  CB    . TYR B 1 606 ? 144.597 127.991 160.163 1.00 64.43 ?  606 TYR B CB    1 
ATOM   10418 C  CG    . TYR B 1 606 ? 143.341 128.784 160.449 1.00 65.10 ?  606 TYR B CG    1 
ATOM   10419 C  CD1   . TYR B 1 606 ? 142.723 129.523 159.449 1.00 64.08 ?  606 TYR B CD1   1 
ATOM   10420 C  CD2   . TYR B 1 606 ? 142.774 128.793 161.717 1.00 63.67 ?  606 TYR B CD2   1 
ATOM   10421 C  CE1   . TYR B 1 606 ? 141.576 130.248 159.704 1.00 64.22 ?  606 TYR B CE1   1 
ATOM   10422 C  CE2   . TYR B 1 606 ? 141.627 129.515 161.980 1.00 62.41 ?  606 TYR B CE2   1 
ATOM   10423 C  CZ    . TYR B 1 606 ? 141.032 130.241 160.970 1.00 65.40 ?  606 TYR B CZ    1 
ATOM   10424 O  OH    . TYR B 1 606 ? 139.889 130.962 161.228 1.00 66.17 ?  606 TYR B OH    1 
ATOM   10425 N  N     . GLY B 1 607 ? 146.103 126.023 157.806 1.00 74.58 ?  607 GLY B N     1 
ATOM   10426 C  CA    . GLY B 1 607 ? 147.262 125.231 157.433 1.00 74.32 ?  607 GLY B CA    1 
ATOM   10427 C  C     . GLY B 1 607 ? 147.001 123.762 157.699 1.00 75.00 ?  607 GLY B C     1 
ATOM   10428 O  O     . GLY B 1 607 ? 145.960 123.213 157.320 1.00 73.95 ?  607 GLY B O     1 
ATOM   10429 N  N     . ASN B 1 608 ? 147.953 123.111 158.362 1.00 78.45 ?  608 ASN B N     1 
ATOM   10430 C  CA    . ASN B 1 608 ? 147.790 121.737 158.811 1.00 78.79 ?  608 ASN B CA    1 
ATOM   10431 C  C     . ASN B 1 608 ? 147.350 121.652 160.265 1.00 78.89 ?  608 ASN B C     1 
ATOM   10432 O  O     . ASN B 1 608 ? 147.239 120.547 160.807 1.00 79.13 ?  608 ASN B O     1 
ATOM   10433 C  CB    . ASN B 1 608 ? 149.090 120.956 158.607 1.00 78.58 ?  608 ASN B CB    1 
ATOM   10434 C  CG    . ASN B 1 608 ? 149.343 120.619 157.151 1.00 79.08 ?  608 ASN B CG    1 
ATOM   10435 O  OD1   . ASN B 1 608 ? 148.440 120.696 156.319 1.00 78.71 ?  608 ASN B OD1   1 
ATOM   10436 N  ND2   . ASN B 1 608 ? 150.577 120.241 156.837 1.00 78.97 ?  608 ASN B ND2   1 
ATOM   10437 N  N     . SER B 1 609 ? 147.097 122.788 160.908 1.00 72.52 ?  609 SER B N     1 
ATOM   10438 C  CA    . SER B 1 609 ? 146.706 122.833 162.307 1.00 71.89 ?  609 SER B CA    1 
ATOM   10439 C  C     . SER B 1 609 ? 145.223 123.155 162.433 1.00 70.62 ?  609 SER B C     1 
ATOM   10440 O  O     . SER B 1 609 ? 144.587 123.652 161.501 1.00 71.68 ?  609 SER B O     1 
ATOM   10441 C  CB    . SER B 1 609 ? 147.532 123.869 163.073 1.00 69.93 ?  609 SER B CB    1 
ATOM   10442 O  OG    . SER B 1 609 ? 147.229 125.183 162.637 1.00 69.72 ?  609 SER B OG    1 
ATOM   10443 N  N     . LYS B 1 610 ? 144.675 122.855 163.606 1.00 61.32 ?  610 LYS B N     1 
ATOM   10444 C  CA    . LYS B 1 610 ? 143.292 123.163 163.930 1.00 61.43 ?  610 LYS B CA    1 
ATOM   10445 C  C     . LYS B 1 610 ? 143.250 124.035 165.177 1.00 61.84 ?  610 LYS B C     1 
ATOM   10446 O  O     . LYS B 1 610 ? 144.030 123.836 166.113 1.00 59.72 ?  610 LYS B O     1 
ATOM   10447 C  CB    . LYS B 1 610 ? 142.470 121.883 164.132 1.00 62.88 ?  610 LYS B CB    1 
ATOM   10448 C  CG    . LYS B 1 610 ? 142.860 121.055 165.346 1.00 61.41 ?  610 LYS B CG    1 
ATOM   10449 C  CD    . LYS B 1 610 ? 141.837 119.966 165.637 1.00 61.32 ?  610 LYS B CD    1 
ATOM   10450 C  CE    . LYS B 1 610 ? 141.119 119.507 164.376 1.00 61.36 ?  610 LYS B CE    1 
ATOM   10451 N  NZ    . LYS B 1 610 ? 140.070 118.492 164.669 1.00 60.10 1  610 LYS B NZ    1 
ATOM   10452 N  N     . THR B 1 611 ? 142.355 125.020 165.172 1.00 60.71 ?  611 THR B N     1 
ATOM   10453 C  CA    . THR B 1 611 ? 142.218 125.966 166.265 1.00 57.67 ?  611 THR B CA    1 
ATOM   10454 C  C     . THR B 1 611 ? 140.766 126.015 166.708 1.00 54.85 ?  611 THR B C     1 
ATOM   10455 O  O     . THR B 1 611 ? 139.850 125.782 165.915 1.00 57.03 ?  611 THR B O     1 
ATOM   10456 C  CB    . THR B 1 611 ? 142.675 127.373 165.858 1.00 58.17 ?  611 THR B CB    1 
ATOM   10457 O  OG1   . THR B 1 611 ? 141.897 127.822 164.743 1.00 58.82 ?  611 THR B OG1   1 
ATOM   10458 C  CG2   . THR B 1 611 ? 144.142 127.370 165.473 1.00 55.74 ?  611 THR B CG2   1 
ATOM   10459 N  N     . TYR B 1 612 ? 140.560 126.308 167.988 1.00 49.86 ?  612 TYR B N     1 
ATOM   10460 C  CA    . TYR B 1 612 ? 139.224 126.440 168.552 1.00 50.17 ?  612 TYR B CA    1 
ATOM   10461 C  C     . TYR B 1 612 ? 139.040 127.861 169.058 1.00 50.25 ?  612 TYR B C     1 
ATOM   10462 O  O     . TYR B 1 612 ? 139.813 128.331 169.899 1.00 51.80 ?  612 TYR B O     1 
ATOM   10463 C  CB    . TYR B 1 612 ? 138.978 125.429 169.675 1.00 52.03 ?  612 TYR B CB    1 
ATOM   10464 C  CG    . TYR B 1 612 ? 139.272 123.992 169.301 1.00 54.51 ?  612 TYR B CG    1 
ATOM   10465 C  CD1   . TYR B 1 612 ? 140.577 123.524 169.206 1.00 53.62 ?  612 TYR B CD1   1 
ATOM   10466 C  CD2   . TYR B 1 612 ? 138.239 123.112 169.010 1.00 54.03 ?  612 TYR B CD2   1 
ATOM   10467 C  CE1   . TYR B 1 612 ? 140.840 122.213 168.859 1.00 55.62 ?  612 TYR B CE1   1 
ATOM   10468 C  CE2   . TYR B 1 612 ? 138.492 121.802 168.663 1.00 54.22 ?  612 TYR B CE2   1 
ATOM   10469 C  CZ    . TYR B 1 612 ? 139.794 121.357 168.588 1.00 55.61 ?  612 TYR B CZ    1 
ATOM   10470 O  OH    . TYR B 1 612 ? 140.047 120.052 168.240 1.00 55.81 ?  612 TYR B OH    1 
ATOM   10471 N  N     . TYR B 1 613 ? 138.019 128.536 168.544 1.00 42.10 ?  613 TYR B N     1 
ATOM   10472 C  CA    . TYR B 1 613 ? 137.664 129.880 168.979 1.00 38.05 ?  613 TYR B CA    1 
ATOM   10473 C  C     . TYR B 1 613 ? 136.397 129.820 169.814 1.00 38.01 ?  613 TYR B C     1 
ATOM   10474 O  O     . TYR B 1 613 ? 135.318 129.531 169.270 1.00 36.70 ?  613 TYR B O     1 
ATOM   10475 C  CB    . TYR B 1 613 ? 137.468 130.806 167.778 1.00 38.76 ?  613 TYR B CB    1 
ATOM   10476 C  CG    . TYR B 1 613 ? 137.011 132.199 168.146 1.00 35.14 ?  613 TYR B CG    1 
ATOM   10477 C  CD1   . TYR B 1 613 ? 137.781 133.008 168.971 1.00 36.58 ?  613 TYR B CD1   1 
ATOM   10478 C  CD2   . TYR B 1 613 ? 135.812 132.708 167.667 1.00 36.96 ?  613 TYR B CD2   1 
ATOM   10479 C  CE1   . TYR B 1 613 ? 137.371 134.281 169.307 1.00 38.78 ?  613 TYR B CE1   1 
ATOM   10480 C  CE2   . TYR B 1 613 ? 135.393 133.981 167.999 1.00 39.76 ?  613 TYR B CE2   1 
ATOM   10481 C  CZ    . TYR B 1 613 ? 136.177 134.762 168.820 1.00 41.14 ?  613 TYR B CZ    1 
ATOM   10482 O  OH    . TYR B 1 613 ? 135.767 136.032 169.153 1.00 40.64 ?  613 TYR B OH    1 
ATOM   10483 N  N     . PRO B 1 614 ? 136.476 130.018 171.127 1.00 35.86 ?  614 PRO B N     1 
ATOM   10484 C  CA    . PRO B 1 614 ? 135.255 130.180 171.918 1.00 34.87 ?  614 PRO B CA    1 
ATOM   10485 C  C     . PRO B 1 614 ? 134.616 131.531 171.648 1.00 38.36 ?  614 PRO B C     1 
ATOM   10486 O  O     . PRO B 1 614 ? 135.286 132.498 171.276 1.00 39.87 ?  614 PRO B O     1 
ATOM   10487 C  CB    . PRO B 1 614 ? 135.747 130.077 173.368 1.00 33.93 ?  614 PRO B CB    1 
ATOM   10488 C  CG    . PRO B 1 614 ? 137.153 129.549 173.282 1.00 36.88 ?  614 PRO B CG    1 
ATOM   10489 C  CD    . PRO B 1 614 ? 137.682 130.010 171.967 1.00 35.12 ?  614 PRO B CD    1 
ATOM   10490 N  N     . MET B 1 615 ? 133.304 131.588 171.834 1.00 32.85 ?  615 MET B N     1 
ATOM   10491 C  CA    . MET B 1 615 ? 132.601 132.851 171.682 1.00 29.77 ?  615 MET B CA    1 
ATOM   10492 C  C     . MET B 1 615 ? 133.089 133.842 172.735 1.00 36.44 ?  615 MET B C     1 
ATOM   10493 O  O     . MET B 1 615 ? 133.444 133.440 173.849 1.00 40.66 ?  615 MET B O     1 
ATOM   10494 C  CB    . MET B 1 615 ? 131.092 132.643 171.796 1.00 30.91 ?  615 MET B CB    1 
ATOM   10495 C  CG    . MET B 1 615 ? 130.426 132.116 170.527 1.00 35.52 ?  615 MET B CG    1 
ATOM   10496 S  SD    . MET B 1 615 ? 131.169 132.687 168.981 1.00 41.17 ?  615 MET B SD    1 
ATOM   10497 C  CE    . MET B 1 615 ? 132.256 131.325 168.557 1.00 34.86 ?  615 MET B CE    1 
ATOM   10498 N  N     . PRO B 1 616 ? 133.137 135.135 172.415 1.00 37.15 ?  616 PRO B N     1 
ATOM   10499 C  CA    . PRO B 1 616 ? 133.713 136.116 173.350 1.00 33.00 ?  616 PRO B CA    1 
ATOM   10500 C  C     . PRO B 1 616 ? 132.957 136.151 174.668 1.00 35.01 ?  616 PRO B C     1 
ATOM   10501 O  O     . PRO B 1 616 ? 131.750 136.393 174.707 1.00 37.07 ?  616 PRO B O     1 
ATOM   10502 C  CB    . PRO B 1 616 ? 133.587 137.440 172.589 1.00 34.26 ?  616 PRO B CB    1 
ATOM   10503 C  CG    . PRO B 1 616 ? 133.456 137.047 171.155 1.00 33.99 ?  616 PRO B CG    1 
ATOM   10504 C  CD    . PRO B 1 616 ? 132.713 135.758 171.152 1.00 33.29 ?  616 PRO B CD    1 
ATOM   10505 N  N     . GLY B 1 617 ? 133.684 135.916 175.756 1.00 35.39 ?  617 GLY B N     1 
ATOM   10506 C  CA    . GLY B 1 617 ? 133.084 135.894 177.072 1.00 33.60 ?  617 GLY B CA    1 
ATOM   10507 C  C     . GLY B 1 617 ? 132.431 134.588 177.459 1.00 38.16 ?  617 GLY B C     1 
ATOM   10508 O  O     . GLY B 1 617 ? 131.779 134.531 178.507 1.00 41.04 ?  617 GLY B O     1 
ATOM   10509 N  N     . LEU B 1 618 ? 132.576 133.543 176.647 1.00 38.93 ?  618 LEU B N     1 
ATOM   10510 C  CA    . LEU B 1 618 ? 131.998 132.251 176.987 1.00 33.74 ?  618 LEU B CA    1 
ATOM   10511 C  C     . LEU B 1 618 ? 132.661 131.686 178.236 1.00 36.51 ?  618 LEU B C     1 
ATOM   10512 O  O     . LEU B 1 618 ? 133.886 131.726 178.383 1.00 38.95 ?  618 LEU B O     1 
ATOM   10513 C  CB    . LEU B 1 618 ? 132.151 131.277 175.817 1.00 30.87 ?  618 LEU B CB    1 
ATOM   10514 C  CG    . LEU B 1 618 ? 131.573 129.872 176.004 1.00 35.47 ?  618 LEU B CG    1 
ATOM   10515 C  CD1   . LEU B 1 618 ? 130.066 129.926 176.194 1.00 36.01 ?  618 LEU B CD1   1 
ATOM   10516 C  CD2   . LEU B 1 618 ? 131.936 128.987 174.824 1.00 35.81 ?  618 LEU B CD2   1 
ATOM   10517 N  N     . ALA B 1 619 ? 131.844 131.158 179.137 1.00 42.84 ?  619 ALA B N     1 
ATOM   10518 C  CA    . ALA B 1 619 ? 132.321 130.610 180.400 1.00 42.21 ?  619 ALA B CA    1 
ATOM   10519 C  C     . ALA B 1 619 ? 131.262 129.651 180.930 1.00 43.92 ?  619 ALA B C     1 
ATOM   10520 O  O     . ALA B 1 619 ? 130.275 129.353 180.249 1.00 49.67 ?  619 ALA B O     1 
ATOM   10521 C  CB    . ALA B 1 619 ? 132.642 131.730 181.395 1.00 41.95 ?  619 ALA B CB    1 
ATOM   10522 N  N     . SER B 1 620 ? 131.470 129.162 182.154 1.00 47.85 ?  620 SER B N     1 
ATOM   10523 C  CA    . SER B 1 620 ? 130.517 128.232 182.749 1.00 49.40 ?  620 SER B CA    1 
ATOM   10524 C  C     . SER B 1 620 ? 129.211 128.927 183.113 1.00 49.40 ?  620 SER B C     1 
ATOM   10525 O  O     . SER B 1 620 ? 128.127 128.365 182.920 1.00 51.23 ?  620 SER B O     1 
ATOM   10526 C  CB    . SER B 1 620 ? 131.132 127.570 183.981 1.00 50.49 ?  620 SER B CB    1 
ATOM   10527 O  OG    . SER B 1 620 ? 132.521 127.356 183.805 1.00 53.13 ?  620 SER B OG    1 
ATOM   10528 N  N     . ASN B 1 621 ? 129.290 130.151 183.640 1.00 47.53 ?  621 ASN B N     1 
ATOM   10529 C  CA    . ASN B 1 621 ? 128.092 130.837 184.107 1.00 49.06 ?  621 ASN B CA    1 
ATOM   10530 C  C     . ASN B 1 621 ? 127.220 131.344 182.966 1.00 50.49 ?  621 ASN B C     1 
ATOM   10531 O  O     . ASN B 1 621 ? 126.013 131.519 183.160 1.00 51.11 ?  621 ASN B O     1 
ATOM   10532 C  CB    . ASN B 1 621 ? 128.475 132.002 185.022 1.00 48.58 ?  621 ASN B CB    1 
ATOM   10533 C  CG    . ASN B 1 621 ? 129.470 132.945 184.379 1.00 51.79 ?  621 ASN B CG    1 
ATOM   10534 O  OD1   . ASN B 1 621 ? 130.285 132.536 183.553 1.00 54.59 ?  621 ASN B OD1   1 
ATOM   10535 N  ND2   . ASN B 1 621 ? 129.409 134.216 184.756 1.00 50.11 ?  621 ASN B ND2   1 
ATOM   10536 N  N     . ASN B 1 622 ? 127.794 131.581 181.787 1.00 42.43 ?  622 ASN B N     1 
ATOM   10537 C  CA    . ASN B 1 622 ? 127.040 132.070 180.639 1.00 42.64 ?  622 ASN B CA    1 
ATOM   10538 C  C     . ASN B 1 622 ? 127.082 131.082 179.477 1.00 45.50 ?  622 ASN B C     1 
ATOM   10539 O  O     . ASN B 1 622 ? 126.953 131.475 178.315 1.00 48.48 ?  622 ASN B O     1 
ATOM   10540 C  CB    . ASN B 1 622 ? 127.545 133.446 180.200 1.00 42.25 ?  622 ASN B CB    1 
ATOM   10541 C  CG    . ASN B 1 622 ? 129.020 133.445 179.832 1.00 43.85 ?  622 ASN B CG    1 
ATOM   10542 O  OD1   . ASN B 1 622 ? 129.654 132.395 179.736 1.00 45.91 ?  622 ASN B OD1   1 
ATOM   10543 N  ND2   . ASN B 1 622 ? 129.572 134.634 179.623 1.00 41.49 ?  622 ASN B ND2   1 
ATOM   10544 N  N     . TRP B 1 623 ? 127.273 129.795 179.778 1.00 40.13 ?  623 TRP B N     1 
ATOM   10545 C  CA    . TRP B 1 623 ? 127.300 128.790 178.719 1.00 38.16 ?  623 TRP B CA    1 
ATOM   10546 C  C     . TRP B 1 623 ? 125.944 128.666 178.037 1.00 39.87 ?  623 TRP B C     1 
ATOM   10547 O  O     . TRP B 1 623 ? 125.864 128.617 176.804 1.00 42.48 ?  623 TRP B O     1 
ATOM   10548 C  CB    . TRP B 1 623 ? 127.742 127.441 179.288 1.00 42.24 ?  623 TRP B CB    1 
ATOM   10549 C  CG    . TRP B 1 623 ? 127.660 126.312 178.302 1.00 40.48 ?  623 TRP B CG    1 
ATOM   10550 C  CD1   . TRP B 1 623 ? 126.575 125.526 178.044 1.00 39.05 ?  623 TRP B CD1   1 
ATOM   10551 C  CD2   . TRP B 1 623 ? 128.707 125.845 177.443 1.00 39.60 ?  623 TRP B CD2   1 
ATOM   10552 N  NE1   . TRP B 1 623 ? 126.880 124.599 177.079 1.00 40.20 ?  623 TRP B NE1   1 
ATOM   10553 C  CE2   . TRP B 1 623 ? 128.183 124.772 176.694 1.00 39.80 ?  623 TRP B CE2   1 
ATOM   10554 C  CE3   . TRP B 1 623 ? 130.034 126.227 177.235 1.00 40.04 ?  623 TRP B CE3   1 
ATOM   10555 C  CZ2   . TRP B 1 623 ? 128.940 124.081 175.751 1.00 39.15 ?  623 TRP B CZ2   1 
ATOM   10556 C  CZ3   . TRP B 1 623 ? 130.784 125.539 176.299 1.00 39.84 ?  623 TRP B CZ3   1 
ATOM   10557 C  CH2   . TRP B 1 623 ? 130.235 124.478 175.569 1.00 39.02 ?  623 TRP B CH2   1 
ATOM   10558 N  N     . PHE B 1 624 ? 124.866 128.616 178.819 1.00 44.42 ?  624 PHE B N     1 
ATOM   10559 C  CA    . PHE B 1 624 ? 123.534 128.450 178.253 1.00 44.06 ?  624 PHE B CA    1 
ATOM   10560 C  C     . PHE B 1 624 ? 122.925 129.753 177.760 1.00 41.51 ?  624 PHE B C     1 
ATOM   10561 O  O     . PHE B 1 624 ? 121.944 129.711 177.009 1.00 46.26 ?  624 PHE B O     1 
ATOM   10562 C  CB    . PHE B 1 624 ? 122.608 127.791 179.277 1.00 42.66 ?  624 PHE B CB    1 
ATOM   10563 C  CG    . PHE B 1 624 ? 122.943 126.354 179.552 1.00 44.84 ?  624 PHE B CG    1 
ATOM   10564 C  CD1   . PHE B 1 624 ? 122.524 125.358 178.687 1.00 42.91 ?  624 PHE B CD1   1 
ATOM   10565 C  CD2   . PHE B 1 624 ? 123.685 126.001 180.665 1.00 45.60 ?  624 PHE B CD2   1 
ATOM   10566 C  CE1   . PHE B 1 624 ? 122.833 124.035 178.932 1.00 42.49 ?  624 PHE B CE1   1 
ATOM   10567 C  CE2   . PHE B 1 624 ? 123.998 124.679 180.915 1.00 45.60 ?  624 PHE B CE2   1 
ATOM   10568 C  CZ    . PHE B 1 624 ? 123.571 123.695 180.047 1.00 45.64 ?  624 PHE B CZ    1 
ATOM   10569 N  N     . PHE B 1 625 ? 123.470 130.903 178.159 1.00 37.19 ?  625 PHE B N     1 
ATOM   10570 C  CA    . PHE B 1 625 ? 123.066 132.157 177.536 1.00 32.73 ?  625 PHE B CA    1 
ATOM   10571 C  C     . PHE B 1 625 ? 123.659 132.308 176.144 1.00 30.95 ?  625 PHE B C     1 
ATOM   10572 O  O     . PHE B 1 625 ? 123.102 133.040 175.320 1.00 33.43 ?  625 PHE B O     1 
ATOM   10573 C  CB    . PHE B 1 625 ? 123.467 133.340 178.416 1.00 29.88 ?  625 PHE B CB    1 
ATOM   10574 C  CG    . PHE B 1 625 ? 122.571 133.538 179.603 1.00 32.89 ?  625 PHE B CG    1 
ATOM   10575 C  CD1   . PHE B 1 625 ? 121.242 133.887 179.433 1.00 33.41 ?  625 PHE B CD1   1 
ATOM   10576 C  CD2   . PHE B 1 625 ? 123.056 133.373 180.890 1.00 33.39 ?  625 PHE B CD2   1 
ATOM   10577 C  CE1   . PHE B 1 625 ? 120.414 134.069 180.523 1.00 33.55 ?  625 PHE B CE1   1 
ATOM   10578 C  CE2   . PHE B 1 625 ? 122.232 133.553 181.983 1.00 35.07 ?  625 PHE B CE2   1 
ATOM   10579 C  CZ    . PHE B 1 625 ? 120.909 133.902 181.799 1.00 35.94 ?  625 PHE B CZ    1 
ATOM   10580 N  N     . TYR B 1 626 ? 124.768 131.631 175.866 1.00 29.75 ?  626 TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 626 ? 125.337 131.571 174.521 1.00 29.27 ?  626 TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 626 ? 124.695 130.452 173.709 1.00 32.33 ?  626 TYR B C     1 
ATOM   10583 O  O     . TYR B 1 626 ? 125.369 129.595 173.142 1.00 35.80 ?  626 TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 626 ? 126.847 131.394 174.601 1.00 31.54 ?  626 TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 626 ? 127.614 132.684 174.460 1.00 29.75 ?  626 TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 626 ? 127.636 133.370 173.253 1.00 33.90 ?  626 TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 626 ? 128.315 133.219 175.531 1.00 28.57 ?  626 TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 626 ? 128.334 134.550 173.117 1.00 30.73 ?  626 TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 626 ? 129.017 134.399 175.405 1.00 31.89 ?  626 TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 626 ? 129.022 135.060 174.194 1.00 33.56 ?  626 TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 626 ? 129.718 136.236 174.059 1.00 36.80 ?  626 TYR B OH    1 
ATOM   10592 N  N     . LYS B 1 627 ? 123.365 130.463 173.661 1.00 33.36 ?  627 LYS B N     1 
ATOM   10593 C  CA    . LYS B 1 627 ? 122.627 129.437 172.940 1.00 31.32 ?  627 LYS B CA    1 
ATOM   10594 C  C     . LYS B 1 627 ? 122.957 129.491 171.454 1.00 31.42 ?  627 LYS B C     1 
ATOM   10595 O  O     . LYS B 1 627 ? 123.015 130.566 170.851 1.00 34.42 ?  627 LYS B O     1 
ATOM   10596 C  CB    . LYS B 1 627 ? 121.128 129.627 173.159 1.00 32.93 ?  627 LYS B CB    1 
ATOM   10597 C  CG    . LYS B 1 627 ? 120.255 128.531 172.581 1.00 33.39 ?  627 LYS B CG    1 
ATOM   10598 C  CD    . LYS B 1 627 ? 118.806 128.737 172.985 1.00 30.93 ?  627 LYS B CD    1 
ATOM   10599 C  CE    . LYS B 1 627 ? 117.900 127.692 172.364 1.00 36.51 ?  627 LYS B CE    1 
ATOM   10600 N  NZ    . LYS B 1 627 ? 116.468 127.957 172.676 1.00 36.73 1  627 LYS B NZ    1 
ATOM   10601 N  N     . GLU B 1 628 ? 123.184 128.321 170.866 1.00 33.49 ?  628 GLU B N     1 
ATOM   10602 C  CA    . GLU B 1 628 ? 123.506 128.256 169.449 1.00 33.47 ?  628 GLU B CA    1 
ATOM   10603 C  C     . GLU B 1 628 ? 122.290 128.619 168.608 1.00 35.41 ?  628 GLU B C     1 
ATOM   10604 O  O     . GLU B 1 628 ? 121.144 128.350 168.978 1.00 39.24 ?  628 GLU B O     1 
ATOM   10605 C  CB    . GLU B 1 628 ? 124.017 126.865 169.079 1.00 35.21 ?  628 GLU B CB    1 
ATOM   10606 C  CG    . GLU B 1 628 ? 125.403 126.566 169.622 1.00 33.53 ?  628 GLU B CG    1 
ATOM   10607 C  CD    . GLU B 1 628 ? 125.936 125.226 169.162 1.00 41.02 ?  628 GLU B CD    1 
ATOM   10608 O  OE1   . GLU B 1 628 ? 125.336 124.629 168.242 1.00 41.66 ?  628 GLU B OE1   1 
ATOM   10609 O  OE2   . GLU B 1 628 ? 126.958 124.770 169.715 1.00 38.10 -1 628 GLU B OE2   1 
ATOM   10610 N  N     . ALA B 1 629 ? 122.555 129.247 167.460 1.00 33.48 ?  629 ALA B N     1 
ATOM   10611 C  CA    . ALA B 1 629 ? 121.478 129.759 166.620 1.00 28.50 ?  629 ALA B CA    1 
ATOM   10612 C  C     . ALA B 1 629 ? 120.589 128.637 166.099 1.00 33.82 ?  629 ALA B C     1 
ATOM   10613 O  O     . ALA B 1 629 ? 119.366 128.796 166.010 1.00 41.85 ?  629 ALA B O     1 
ATOM   10614 C  CB    . ALA B 1 629 ? 122.060 130.563 165.460 1.00 29.76 ?  629 ALA B CB    1 
ATOM   10615 N  N     . TYR B 1 630 ? 121.185 127.499 165.737 1.00 39.39 ?  630 TYR B N     1 
ATOM   10616 C  CA    . TYR B 1 630 ? 120.400 126.393 165.200 1.00 37.06 ?  630 TYR B CA    1 
ATOM   10617 C  C     . TYR B 1 630 ? 119.431 125.834 166.233 1.00 39.49 ?  630 TYR B C     1 
ATOM   10618 O  O     . TYR B 1 630 ? 118.351 125.356 165.869 1.00 42.63 ?  630 TYR B O     1 
ATOM   10619 C  CB    . TYR B 1 630 ? 121.328 125.292 164.689 1.00 34.90 ?  630 TYR B CB    1 
ATOM   10620 C  CG    . TYR B 1 630 ? 122.292 125.763 163.626 1.00 37.14 ?  630 TYR B CG    1 
ATOM   10621 C  CD1   . TYR B 1 630 ? 121.879 125.922 162.310 1.00 33.86 ?  630 TYR B CD1   1 
ATOM   10622 C  CD2   . TYR B 1 630 ? 123.613 126.049 163.937 1.00 37.66 ?  630 TYR B CD2   1 
ATOM   10623 C  CE1   . TYR B 1 630 ? 122.755 126.353 161.335 1.00 37.39 ?  630 TYR B CE1   1 
ATOM   10624 C  CE2   . TYR B 1 630 ? 124.497 126.480 162.969 1.00 36.27 ?  630 TYR B CE2   1 
ATOM   10625 C  CZ    . TYR B 1 630 ? 124.062 126.630 161.669 1.00 39.87 ?  630 TYR B CZ    1 
ATOM   10626 O  OH    . TYR B 1 630 ? 124.938 127.059 160.700 1.00 43.03 ?  630 TYR B OH    1 
ATOM   10627 N  N     . ASP B 1 631 ? 119.788 125.889 167.515 1.00 36.75 ?  631 ASP B N     1 
ATOM   10628 C  CA    . ASP B 1 631 ? 118.902 125.426 168.574 1.00 32.70 ?  631 ASP B CA    1 
ATOM   10629 C  C     . ASP B 1 631 ? 117.807 126.429 168.911 1.00 37.19 ?  631 ASP B C     1 
ATOM   10630 O  O     . ASP B 1 631 ? 116.906 126.100 169.689 1.00 39.80 ?  631 ASP B O     1 
ATOM   10631 C  CB    . ASP B 1 631 ? 119.711 125.115 169.835 1.00 34.41 ?  631 ASP B CB    1 
ATOM   10632 C  CG    . ASP B 1 631 ? 120.778 124.064 169.598 1.00 41.11 ?  631 ASP B CG    1 
ATOM   10633 O  OD1   . ASP B 1 631 ? 120.491 123.068 168.902 1.00 43.19 ?  631 ASP B OD1   1 
ATOM   10634 O  OD2   . ASP B 1 631 ? 121.906 124.236 170.107 1.00 42.19 -1 631 ASP B OD2   1 
ATOM   10635 N  N     . MET B 1 632 ? 117.859 127.630 168.345 1.00 36.47 ?  632 MET B N     1 
ATOM   10636 C  CA    . MET B 1 632 ? 116.920 128.689 168.678 1.00 32.57 ?  632 MET B CA    1 
ATOM   10637 C  C     . MET B 1 632 ? 115.676 128.612 167.806 1.00 34.91 ?  632 MET B C     1 
ATOM   10638 O  O     . MET B 1 632 ? 115.701 128.081 166.692 1.00 34.50 ?  632 MET B O     1 
ATOM   10639 C  CB    . MET B 1 632 ? 117.573 130.060 168.504 1.00 31.54 ?  632 MET B CB    1 
ATOM   10640 C  CG    . MET B 1 632 ? 118.685 130.347 169.486 1.00 36.57 ?  632 MET B CG    1 
ATOM   10641 S  SD    . MET B 1 632 ? 119.398 131.978 169.244 1.00 39.71 ?  632 MET B SD    1 
ATOM   10642 C  CE    . MET B 1 632 ? 120.172 132.233 170.834 1.00 30.53 ?  632 MET B CE    1 
ATOM   10643 N  N     . ASP B 1 633 ? 114.579 129.153 168.329 1.00 33.36 ?  633 ASP B N     1 
ATOM   10644 C  CA    . ASP B 1 633 ? 113.365 129.312 167.541 1.00 26.12 ?  633 ASP B CA    1 
ATOM   10645 C  C     . ASP B 1 633 ? 113.568 130.428 166.527 1.00 31.27 ?  633 ASP B C     1 
ATOM   10646 O  O     . ASP B 1 633 ? 113.832 131.575 166.903 1.00 37.33 ?  633 ASP B O     1 
ATOM   10647 C  CB    . ASP B 1 633 ? 112.181 129.620 168.454 1.00 28.86 ?  633 ASP B CB    1 
ATOM   10648 C  CG    . ASP B 1 633 ? 110.852 129.560 167.728 1.00 36.59 ?  633 ASP B CG    1 
ATOM   10649 O  OD1   . ASP B 1 633 ? 110.829 129.132 166.556 1.00 39.85 ?  633 ASP B OD1   1 
ATOM   10650 O  OD2   . ASP B 1 633 ? 109.828 129.941 168.332 1.00 35.97 -1 633 ASP B OD2   1 
ATOM   10651 N  N     . MET B 1 634 ? 113.451 130.097 165.241 1.00 28.97 ?  634 MET B N     1 
ATOM   10652 C  CA    . MET B 1 634 ? 113.644 131.100 164.202 1.00 19.79 ?  634 MET B CA    1 
ATOM   10653 C  C     . MET B 1 634 ? 112.584 132.191 164.246 1.00 23.83 ?  634 MET B C     1 
ATOM   10654 O  O     . MET B 1 634 ? 112.831 133.293 163.749 1.00 30.66 ?  634 MET B O     1 
ATOM   10655 C  CB    . MET B 1 634 ? 113.654 130.441 162.823 1.00 24.77 ?  634 MET B CB    1 
ATOM   10656 C  CG    . MET B 1 634 ? 115.044 130.137 162.275 1.00 26.45 ?  634 MET B CG    1 
ATOM   10657 S  SD    . MET B 1 634 ? 116.263 131.418 162.631 1.00 40.68 ?  634 MET B SD    1 
ATOM   10658 C  CE    . MET B 1 634 ? 117.228 130.629 163.918 1.00 27.98 ?  634 MET B CE    1 
ATOM   10659 N  N     . PHE B 1 635 ? 111.417 131.914 164.830 1.00 22.81 ?  635 PHE B N     1 
ATOM   10660 C  CA    . PHE B 1 635 ? 110.388 132.944 164.944 1.00 23.82 ?  635 PHE B CA    1 
ATOM   10661 C  C     . PHE B 1 635 ? 110.815 134.046 165.906 1.00 20.23 ?  635 PHE B C     1 
ATOM   10662 O  O     . PHE B 1 635 ? 110.588 135.232 165.644 1.00 23.00 ?  635 PHE B O     1 
ATOM   10663 C  CB    . PHE B 1 635 ? 109.069 132.317 165.390 1.00 22.81 ?  635 PHE B CB    1 
ATOM   10664 C  CG    . PHE B 1 635 ? 108.206 131.850 164.253 1.00 23.55 ?  635 PHE B CG    1 
ATOM   10665 C  CD1   . PHE B 1 635 ? 108.763 131.182 163.176 1.00 25.61 ?  635 PHE B CD1   1 
ATOM   10666 C  CD2   . PHE B 1 635 ? 106.842 132.078 164.261 1.00 24.32 ?  635 PHE B CD2   1 
ATOM   10667 C  CE1   . PHE B 1 635 ? 107.975 130.751 162.127 1.00 22.74 ?  635 PHE B CE1   1 
ATOM   10668 C  CE2   . PHE B 1 635 ? 106.049 131.649 163.215 1.00 25.49 ?  635 PHE B CE2   1 
ATOM   10669 C  CZ    . PHE B 1 635 ? 106.617 130.984 162.146 1.00 23.57 ?  635 PHE B CZ    1 
ATOM   10670 N  N     . LYS B 1 636 ? 111.454 133.679 167.018 1.00 26.75 ?  636 LYS B N     1 
ATOM   10671 C  CA    . LYS B 1 636 ? 111.934 134.683 167.958 1.00 29.79 ?  636 LYS B CA    1 
ATOM   10672 C  C     . LYS B 1 636 ? 113.146 135.433 167.416 1.00 26.40 ?  636 LYS B C     1 
ATOM   10673 O  O     . LYS B 1 636 ? 113.315 136.624 167.704 1.00 29.33 ?  636 LYS B O     1 
ATOM   10674 C  CB    . LYS B 1 636 ? 112.256 134.026 169.299 1.00 27.22 ?  636 LYS B CB    1 
ATOM   10675 C  CG    . LYS B 1 636 ? 111.043 133.387 169.957 1.00 27.67 ?  636 LYS B CG    1 
ATOM   10676 C  CD    . LYS B 1 636 ? 111.343 132.930 171.371 1.00 33.78 ?  636 LYS B CD    1 
ATOM   10677 C  CE    . LYS B 1 636 ? 110.163 132.186 171.972 1.00 33.82 ?  636 LYS B CE    1 
ATOM   10678 N  NZ    . LYS B 1 636 ? 110.501 131.585 173.291 1.00 35.15 1  636 LYS B NZ    1 
ATOM   10679 N  N     . VAL B 1 637 ? 113.981 134.768 166.617 1.00 22.60 ?  637 VAL B N     1 
ATOM   10680 C  CA    . VAL B 1 637 ? 115.052 135.478 165.926 1.00 19.51 ?  637 VAL B CA    1 
ATOM   10681 C  C     . VAL B 1 637 ? 114.469 136.466 164.923 1.00 25.77 ?  637 VAL B C     1 
ATOM   10682 O  O     . VAL B 1 637 ? 114.979 137.581 164.763 1.00 26.46 ?  637 VAL B O     1 
ATOM   10683 C  CB    . VAL B 1 637 ? 116.010 134.478 165.253 1.00 19.65 ?  637 VAL B CB    1 
ATOM   10684 C  CG1   . VAL B 1 637 ? 117.220 135.200 164.688 1.00 20.23 ?  637 VAL B CG1   1 
ATOM   10685 C  CG2   . VAL B 1 637 ? 116.442 133.412 166.246 1.00 24.93 ?  637 VAL B CG2   1 
ATOM   10686 N  N     . VAL B 1 638 ? 113.390 136.079 164.238 1.00 20.68 ?  638 VAL B N     1 
ATOM   10687 C  CA    . VAL B 1 638 ? 112.698 137.002 163.342 1.00 20.02 ?  638 VAL B CA    1 
ATOM   10688 C  C     . VAL B 1 638 ? 112.145 138.185 164.124 1.00 20.80 ?  638 VAL B C     1 
ATOM   10689 O  O     . VAL B 1 638 ? 112.197 139.332 163.665 1.00 28.07 ?  638 VAL B O     1 
ATOM   10690 C  CB    . VAL B 1 638 ? 111.582 136.267 162.572 1.00 22.27 ?  638 VAL B CB    1 
ATOM   10691 C  CG1   . VAL B 1 638 ? 110.599 137.258 161.975 1.00 16.86 ?  638 VAL B CG1   1 
ATOM   10692 C  CG2   . VAL B 1 638 ? 112.169 135.388 161.484 1.00 18.92 ?  638 VAL B CG2   1 
ATOM   10693 N  N     . ASP B 1 639 ? 111.596 137.924 165.312 1.00 21.40 ?  639 ASP B N     1 
ATOM   10694 C  CA    . ASP B 1 639 ? 111.099 139.006 166.156 1.00 16.39 ?  639 ASP B CA    1 
ATOM   10695 C  C     . ASP B 1 639 ? 112.217 139.971 166.532 1.00 22.64 ?  639 ASP B C     1 
ATOM   10696 O  O     . ASP B 1 639 ? 112.039 141.193 166.472 1.00 31.87 ?  639 ASP B O     1 
ATOM   10697 C  CB    . ASP B 1 639 ? 110.448 138.431 167.413 1.00 20.16 ?  639 ASP B CB    1 
ATOM   10698 C  CG    . ASP B 1 639 ? 109.061 137.890 167.154 1.00 30.99 ?  639 ASP B CG    1 
ATOM   10699 O  OD1   . ASP B 1 639 ? 108.333 138.487 166.334 1.00 30.17 ?  639 ASP B OD1   1 
ATOM   10700 O  OD2   . ASP B 1 639 ? 108.695 136.870 167.773 1.00 33.70 -1 639 ASP B OD2   1 
ATOM   10701 N  N     . MET B 1 640 ? 113.378 139.437 166.918 1.00 20.10 ?  640 MET B N     1 
ATOM   10702 C  CA    . MET B 1 640 ? 114.526 140.288 167.223 1.00 16.85 ?  640 MET B CA    1 
ATOM   10703 C  C     . MET B 1 640 ? 114.944 141.114 166.014 1.00 18.80 ?  640 MET B C     1 
ATOM   10704 O  O     . MET B 1 640 ? 115.212 142.318 166.128 1.00 24.56 ?  640 MET B O     1 
ATOM   10705 C  CB    . MET B 1 640 ? 115.700 139.439 167.705 1.00 18.97 ?  640 MET B CB    1 
ATOM   10706 C  CG    . MET B 1 640 ? 116.938 140.265 168.014 1.00 23.29 ?  640 MET B CG    1 
ATOM   10707 S  SD    . MET B 1 640 ? 116.877 141.118 169.593 1.00 26.94 ?  640 MET B SD    1 
ATOM   10708 C  CE    . MET B 1 640 ? 117.680 139.908 170.627 1.00 20.08 ?  640 MET B CE    1 
ATOM   10709 N  N     . ILE B 1 641 ? 115.021 140.479 164.845 1.00 22.96 ?  641 ILE B N     1 
ATOM   10710 C  CA    . ILE B 1 641 ? 115.500 141.183 163.663 1.00 18.61 ?  641 ILE B CA    1 
ATOM   10711 C  C     . ILE B 1 641 ? 114.508 142.258 163.244 1.00 17.77 ?  641 ILE B C     1 
ATOM   10712 O  O     . ILE B 1 641 ? 114.902 143.335 162.801 1.00 25.68 ?  641 ILE B O     1 
ATOM   10713 C  CB    . ILE B 1 641 ? 115.798 140.191 162.522 1.00 23.86 ?  641 ILE B CB    1 
ATOM   10714 C  CG1   . ILE B 1 641 ? 116.888 139.209 162.950 1.00 22.05 ?  641 ILE B CG1   1 
ATOM   10715 C  CG2   . ILE B 1 641 ? 116.261 140.930 161.281 1.00 13.33 ?  641 ILE B CG2   1 
ATOM   10716 C  CD1   . ILE B 1 641 ? 118.029 139.852 163.707 1.00 20.77 ?  641 ILE B CD1   1 
ATOM   10717 N  N     . ALA B 1 642 ? 113.207 141.996 163.399 1.00 9.77  ?  642 ALA B N     1 
ATOM   10718 C  CA    . ALA B 1 642 ? 112.204 143.017 163.105 1.00 17.35 ?  642 ALA B CA    1 
ATOM   10719 C  C     . ALA B 1 642 ? 112.277 144.170 164.099 1.00 19.47 ?  642 ALA B C     1 
ATOM   10720 O  O     . ALA B 1 642 ? 112.128 145.341 163.719 1.00 29.13 ?  642 ALA B O     1 
ATOM   10721 C  CB    . ALA B 1 642 ? 110.809 142.395 163.106 1.00 23.44 ?  642 ALA B CB    1 
ATOM   10722 N  N     . THR B 1 643 ? 112.508 143.857 165.376 1.00 13.83 ?  643 THR B N     1 
ATOM   10723 C  CA    . THR B 1 643 ? 112.663 144.901 166.382 1.00 15.50 ?  643 THR B CA    1 
ATOM   10724 C  C     . THR B 1 643 ? 113.848 145.801 166.060 1.00 18.38 ?  643 THR B C     1 
ATOM   10725 O  O     . THR B 1 643 ? 113.762 147.027 166.194 1.00 22.78 ?  643 THR B O     1 
ATOM   10726 C  CB    . THR B 1 643 ? 112.828 144.271 167.765 1.00 18.85 ?  643 THR B CB    1 
ATOM   10727 O  OG1   . THR B 1 643 ? 111.688 143.456 168.061 1.00 23.42 ?  643 THR B OG1   1 
ATOM   10728 C  CG2   . THR B 1 643 ? 112.963 145.342 168.828 1.00 17.01 ?  643 THR B CG2   1 
ATOM   10729 N  N     . ILE B 1 644 ? 114.964 145.210 165.637 1.00 16.84 ?  644 ILE B N     1 
ATOM   10730 C  CA    . ILE B 1 644 ? 116.110 146.016 165.227 1.00 12.86 ?  644 ILE B CA    1 
ATOM   10731 C  C     . ILE B 1 644 ? 115.802 146.769 163.936 1.00 16.93 ?  644 ILE B C     1 
ATOM   10732 O  O     . ILE B 1 644 ? 116.174 147.937 163.777 1.00 23.05 ?  644 ILE B O     1 
ATOM   10733 C  CB    . ILE B 1 644 ? 117.361 145.133 165.082 1.00 14.99 ?  644 ILE B CB    1 
ATOM   10734 C  CG1   . ILE B 1 644 ? 117.661 144.412 166.395 1.00 15.83 ?  644 ILE B CG1   1 
ATOM   10735 C  CG2   . ILE B 1 644 ? 118.548 145.968 164.650 1.00 10.19 ?  644 ILE B CG2   1 
ATOM   10736 C  CD1   . ILE B 1 644 ? 118.668 143.298 166.254 1.00 18.65 ?  644 ILE B CD1   1 
ATOM   10737 N  N     . GLN B 1 645 ? 115.104 146.116 163.004 1.00 7.72  ?  645 GLN B N     1 
ATOM   10738 C  CA    . GLN B 1 645 ? 114.865 146.668 161.678 1.00 14.27 ?  645 GLN B CA    1 
ATOM   10739 C  C     . GLN B 1 645 ? 113.974 147.897 161.730 1.00 20.95 ?  645 GLN B C     1 
ATOM   10740 O  O     . GLN B 1 645 ? 114.091 148.783 160.875 1.00 28.01 ?  645 GLN B O     1 
ATOM   10741 C  CB    . GLN B 1 645 ? 114.238 145.596 160.787 1.00 12.79 ?  645 GLN B CB    1 
ATOM   10742 C  CG    . GLN B 1 645 ? 113.992 146.024 159.358 1.00 10.57 ?  645 GLN B CG    1 
ATOM   10743 C  CD    . GLN B 1 645 ? 115.239 145.926 158.512 1.00 15.11 ?  645 GLN B CD    1 
ATOM   10744 O  OE1   . GLN B 1 645 ? 115.989 146.888 158.386 1.00 8.69  ?  645 GLN B OE1   1 
ATOM   10745 N  NE2   . GLN B 1 645 ? 115.469 144.756 157.928 1.00 17.69 ?  645 GLN B NE2   1 
ATOM   10746 N  N     . GLN B 1 646 ? 113.080 147.967 162.716 1.00 18.85 ?  646 GLN B N     1 
ATOM   10747 C  CA    . GLN B 1 646 ? 112.224 149.142 162.830 1.00 16.53 ?  646 GLN B CA    1 
ATOM   10748 C  C     . GLN B 1 646 ? 113.025 150.421 163.059 1.00 13.75 ?  646 GLN B C     1 
ATOM   10749 O  O     . GLN B 1 646 ? 112.509 151.513 162.803 1.00 21.39 ?  646 GLN B O     1 
ATOM   10750 C  CB    . GLN B 1 646 ? 111.203 148.938 163.950 1.00 19.98 ?  646 GLN B CB    1 
ATOM   10751 C  CG    . GLN B 1 646 ? 111.714 149.259 165.334 1.00 21.39 ?  646 GLN B CG    1 
ATOM   10752 C  CD    . GLN B 1 646 ? 110.696 148.949 166.410 1.00 27.82 ?  646 GLN B CD    1 
ATOM   10753 O  OE1   . GLN B 1 646 ? 110.911 148.079 167.253 1.00 25.23 ?  646 GLN B OE1   1 
ATOM   10754 N  NE2   . GLN B 1 646 ? 109.575 149.661 166.386 1.00 27.04 ?  646 GLN B NE2   1 
ATOM   10755 N  N     . HIS B 1 647 ? 114.275 150.313 163.508 1.00 22.19 ?  647 HIS B N     1 
ATOM   10756 C  CA    . HIS B 1 647 ? 115.136 151.469 163.720 1.00 19.27 ?  647 HIS B CA    1 
ATOM   10757 C  C     . HIS B 1 647 ? 116.261 151.579 162.700 1.00 16.97 ?  647 HIS B C     1 
ATOM   10758 O  O     . HIS B 1 647 ? 117.069 152.508 162.790 1.00 22.98 ?  647 HIS B O     1 
ATOM   10759 C  CB    . HIS B 1 647 ? 115.732 151.434 165.131 1.00 13.76 ?  647 HIS B CB    1 
ATOM   10760 C  CG    . HIS B 1 647 ? 114.709 151.302 166.214 1.00 17.51 ?  647 HIS B CG    1 
ATOM   10761 N  ND1   . HIS B 1 647 ? 113.776 152.280 166.478 1.00 13.19 ?  647 HIS B ND1   1 
ATOM   10762 C  CD2   . HIS B 1 647 ? 114.474 150.307 167.101 1.00 16.95 ?  647 HIS B CD2   1 
ATOM   10763 C  CE1   . HIS B 1 647 ? 113.009 151.894 167.480 1.00 19.01 ?  647 HIS B CE1   1 
ATOM   10764 N  NE2   . HIS B 1 647 ? 113.411 150.701 167.877 1.00 21.98 ?  647 HIS B NE2   1 
ATOM   10765 N  N     . ILE B 1 648 ? 116.338 150.665 161.737 1.00 12.68 ?  648 ILE B N     1 
ATOM   10766 C  CA    . ILE B 1 648 ? 117.377 150.668 160.714 1.00 11.44 ?  648 ILE B CA    1 
ATOM   10767 C  C     . ILE B 1 648 ? 116.735 151.059 159.390 1.00 16.81 ?  648 ILE B C     1 
ATOM   10768 O  O     . ILE B 1 648 ? 115.762 150.429 158.957 1.00 27.46 ?  648 ILE B O     1 
ATOM   10769 C  CB    . ILE B 1 648 ? 118.070 149.298 160.613 1.00 13.28 ?  648 ILE B CB    1 
ATOM   10770 C  CG1   . ILE B 1 648 ? 118.640 148.884 161.970 1.00 16.65 ?  648 ILE B CG1   1 
ATOM   10771 C  CG2   . ILE B 1 648 ? 119.169 149.328 159.569 1.00 5.40  ?  648 ILE B CG2   1 
ATOM   10772 C  CD1   . ILE B 1 648 ? 119.712 149.809 162.493 1.00 8.73  ?  648 ILE B CD1   1 
ATOM   10773 N  N     . ASP B 1 649 ? 117.272 152.101 158.752 1.00 12.87 ?  649 ASP B N     1 
ATOM   10774 C  CA    . ASP B 1 649 ? 116.680 152.594 157.511 1.00 7.33  ?  649 ASP B CA    1 
ATOM   10775 C  C     . ASP B 1 649 ? 116.956 151.656 156.342 1.00 10.36 ?  649 ASP B C     1 
ATOM   10776 O  O     . ASP B 1 649 ? 116.094 151.470 155.478 1.00 29.65 ?  649 ASP B O     1 
ATOM   10777 C  CB    . ASP B 1 649 ? 117.188 154.003 157.206 1.00 16.59 ?  649 ASP B CB    1 
ATOM   10778 C  CG    . ASP B 1 649 ? 118.672 154.153 157.450 1.00 16.75 ?  649 ASP B CG    1 
ATOM   10779 O  OD1   . ASP B 1 649 ? 119.138 153.732 158.526 1.00 20.57 ?  649 ASP B OD1   1 
ATOM   10780 O  OD2   . ASP B 1 649 ? 119.369 154.697 156.573 1.00 15.48 -1 649 ASP B OD2   1 
ATOM   10781 N  N     . GLN B 1 650 ? 118.145 151.069 156.292 1.00 12.34 ?  650 GLN B N     1 
ATOM   10782 C  CA    . GLN B 1 650 ? 118.449 150.032 155.317 1.00 3.46  ?  650 GLN B CA    1 
ATOM   10783 C  C     . GLN B 1 650 ? 118.115 148.676 155.939 1.00 7.97  ?  650 GLN B C     1 
ATOM   10784 O  O     . GLN B 1 650 ? 117.436 148.605 156.966 1.00 18.13 ?  650 GLN B O     1 
ATOM   10785 C  CB    . GLN B 1 650 ? 119.905 150.144 154.862 1.00 7.16  ?  650 GLN B CB    1 
ATOM   10786 C  CG    . GLN B 1 650 ? 120.253 151.478 154.238 1.00 8.51  ?  650 GLN B CG    1 
ATOM   10787 C  CD    . GLN B 1 650 ? 121.689 151.534 153.771 1.00 13.48 ?  650 GLN B CD    1 
ATOM   10788 O  OE1   . GLN B 1 650 ? 122.049 150.927 152.765 1.00 18.42 ?  650 GLN B OE1   1 
ATOM   10789 N  NE2   . GLN B 1 650 ? 122.519 152.269 154.499 1.00 6.77  ?  650 GLN B NE2   1 
ATOM   10790 N  N     . GLY B 1 651 ? 118.567 147.586 155.323 1.00 7.27  ?  651 GLY B N     1 
ATOM   10791 C  CA    . GLY B 1 651 ? 118.239 146.261 155.798 1.00 8.37  ?  651 GLY B CA    1 
ATOM   10792 C  C     . GLY B 1 651 ? 119.273 145.689 156.749 1.00 7.98  ?  651 GLY B C     1 
ATOM   10793 O  O     . GLY B 1 651 ? 120.262 146.323 157.114 1.00 12.97 ?  651 GLY B O     1 
ATOM   10794 N  N     . ILE B 1 652 ? 119.013 144.452 157.160 1.00 12.55 ?  652 ILE B N     1 
ATOM   10795 C  CA    . ILE B 1 652 ? 119.886 143.690 158.042 1.00 11.63 ?  652 ILE B CA    1 
ATOM   10796 C  C     . ILE B 1 652 ? 120.146 142.346 157.382 1.00 14.25 ?  652 ILE B C     1 
ATOM   10797 O  O     . ILE B 1 652 ? 119.208 141.692 156.915 1.00 25.45 ?  652 ILE B O     1 
ATOM   10798 C  CB    . ILE B 1 652 ? 119.262 143.490 159.435 1.00 6.36  ?  652 ILE B CB    1 
ATOM   10799 C  CG1   . ILE B 1 652 ? 118.861 144.831 160.048 1.00 6.35  ?  652 ILE B CG1   1 
ATOM   10800 C  CG2   . ILE B 1 652 ? 120.215 142.740 160.348 1.00 10.09 ?  652 ILE B CG2   1 
ATOM   10801 C  CD1   . ILE B 1 652 ? 117.988 144.695 161.269 1.00 9.76  ?  652 ILE B CD1   1 
ATOM   10802 N  N     . SER B 1 653 ? 121.409 141.934 157.342 1.00 5.70  ?  653 SER B N     1 
ATOM   10803 C  CA    . SER B 1 653 ? 121.754 140.636 156.772 1.00 12.44 ?  653 SER B CA    1 
ATOM   10804 C  C     . SER B 1 653 ? 121.263 139.556 157.724 1.00 19.34 ?  653 SER B C     1 
ATOM   10805 O  O     . SER B 1 653 ? 121.940 139.200 158.690 1.00 23.48 ?  653 SER B O     1 
ATOM   10806 C  CB    . SER B 1 653 ? 123.255 140.532 156.539 1.00 12.43 ?  653 SER B CB    1 
ATOM   10807 O  OG    . SER B 1 653 ? 123.611 141.099 155.291 1.00 21.12 ?  653 SER B OG    1 
ATOM   10808 N  N     . PHE B 1 654 ? 120.072 139.034 157.451 1.00 19.33 ?  654 PHE B N     1 
ATOM   10809 C  CA    . PHE B 1 654 ? 119.390 138.097 158.335 1.00 12.91 ?  654 PHE B CA    1 
ATOM   10810 C  C     . PHE B 1 654 ? 119.592 136.688 157.788 1.00 16.26 ?  654 PHE B C     1 
ATOM   10811 O  O     . PHE B 1 654 ? 118.953 136.289 156.812 1.00 25.36 ?  654 PHE B O     1 
ATOM   10812 C  CB    . PHE B 1 654 ? 117.913 138.456 158.446 1.00 13.27 ?  654 PHE B CB    1 
ATOM   10813 C  CG    . PHE B 1 654 ? 117.142 137.594 159.402 1.00 16.91 ?  654 PHE B CG    1 
ATOM   10814 C  CD1   . PHE B 1 654 ? 117.786 136.874 160.393 1.00 18.96 ?  654 PHE B CD1   1 
ATOM   10815 C  CD2   . PHE B 1 654 ? 115.767 137.508 159.307 1.00 17.86 ?  654 PHE B CD2   1 
ATOM   10816 C  CE1   . PHE B 1 654 ? 117.072 136.083 161.266 1.00 19.71 ?  654 PHE B CE1   1 
ATOM   10817 C  CE2   . PHE B 1 654 ? 115.049 136.721 160.177 1.00 17.55 ?  654 PHE B CE2   1 
ATOM   10818 C  CZ    . PHE B 1 654 ? 115.702 136.008 161.159 1.00 16.60 ?  654 PHE B CZ    1 
ATOM   10819 N  N     . THR B 1 655 ? 120.477 135.934 158.430 1.00 21.60 ?  655 THR B N     1 
ATOM   10820 C  CA    . THR B 1 655 ? 120.709 134.542 158.082 1.00 22.15 ?  655 THR B CA    1 
ATOM   10821 C  C     . THR B 1 655 ? 119.775 133.655 158.893 1.00 22.47 ?  655 THR B C     1 
ATOM   10822 O  O     . THR B 1 655 ? 119.680 133.798 160.116 1.00 27.99 ?  655 THR B O     1 
ATOM   10823 C  CB    . THR B 1 655 ? 122.166 134.156 158.342 1.00 24.56 ?  655 THR B CB    1 
ATOM   10824 O  OG1   . THR B 1 655 ? 123.021 134.881 157.450 1.00 31.42 ?  655 THR B OG1   1 
ATOM   10825 C  CG2   . THR B 1 655 ? 122.374 132.664 158.132 1.00 24.12 ?  655 THR B CG2   1 
ATOM   10826 N  N     . LEU B 1 656 ? 119.077 132.754 158.211 1.00 28.74 ?  656 LEU B N     1 
ATOM   10827 C  CA    . LEU B 1 656 ? 118.238 131.767 158.874 1.00 31.33 ?  656 LEU B CA    1 
ATOM   10828 C  C     . LEU B 1 656 ? 119.087 130.561 159.244 1.00 24.98 ?  656 LEU B C     1 
ATOM   10829 O  O     . LEU B 1 656 ? 119.896 130.095 158.438 1.00 30.77 ?  656 LEU B O     1 
ATOM   10830 C  CB    . LEU B 1 656 ? 117.074 131.347 157.978 1.00 28.54 ?  656 LEU B CB    1 
ATOM   10831 C  CG    . LEU B 1 656 ? 116.047 132.440 157.680 1.00 29.96 ?  656 LEU B CG    1 
ATOM   10832 C  CD1   . LEU B 1 656 ? 114.890 131.883 156.872 1.00 27.74 ?  656 LEU B CD1   1 
ATOM   10833 C  CD2   . LEU B 1 656 ? 115.551 133.083 158.966 1.00 26.15 ?  656 LEU B CD2   1 
ATOM   10834 N  N     . PHE B 1 657 ? 118.922 130.079 160.470 1.00 25.49 ?  657 PHE B N     1 
ATOM   10835 C  CA    . PHE B 1 657 ? 119.688 128.951 160.989 1.00 29.93 ?  657 PHE B CA    1 
ATOM   10836 C  C     . PHE B 1 657 ? 118.722 127.797 161.209 1.00 34.81 ?  657 PHE B C     1 
ATOM   10837 O  O     . PHE B 1 657 ? 117.899 127.836 162.130 1.00 38.68 ?  657 PHE B O     1 
ATOM   10838 C  CB    . PHE B 1 657 ? 120.412 129.338 162.274 1.00 28.95 ?  657 PHE B CB    1 
ATOM   10839 C  CG    . PHE B 1 657 ? 121.308 130.531 162.120 1.00 33.74 ?  657 PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 1 657 ? 122.597 130.388 161.639 1.00 32.30 ?  657 PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 1 657 ? 120.858 131.801 162.446 1.00 33.75 ?  657 PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 1 657 ? 123.421 131.487 161.490 1.00 32.19 ?  657 PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 1 657 ? 121.678 132.900 162.303 1.00 31.68 ?  657 PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 1 657 ? 122.962 132.744 161.824 1.00 31.73 ?  657 PHE B CZ    1 
ATOM   10845 N  N     . LEU B 1 658 ? 118.823 126.774 160.368 1.00 35.52 ?  658 LEU B N     1 
ATOM   10846 C  CA    . LEU B 1 658 ? 117.829 125.719 160.297 1.00 38.84 ?  658 LEU B CA    1 
ATOM   10847 C  C     . LEU B 1 658 ? 118.438 124.390 160.722 1.00 42.86 ?  658 LEU B C     1 
ATOM   10848 O  O     . LEU B 1 658 ? 119.646 124.172 160.596 1.00 42.45 ?  658 LEU B O     1 
ATOM   10849 C  CB    . LEU B 1 658 ? 117.276 125.596 158.876 1.00 38.92 ?  658 LEU B CB    1 
ATOM   10850 C  CG    . LEU B 1 658 ? 116.815 126.901 158.221 1.00 36.73 ?  658 LEU B CG    1 
ATOM   10851 C  CD1   . LEU B 1 658 ? 116.957 126.794 156.713 1.00 36.74 ?  658 LEU B CD1   1 
ATOM   10852 C  CD2   . LEU B 1 658 ? 115.401 127.286 158.609 1.00 34.53 ?  658 LEU B CD2   1 
ATOM   10853 N  N     . LYS B 1 659 ? 117.591 123.512 161.246 1.00 46.82 ?  659 LYS B N     1 
ATOM   10854 C  CA    . LYS B 1 659 ? 117.984 122.143 161.537 1.00 45.01 ?  659 LYS B CA    1 
ATOM   10855 C  C     . LYS B 1 659 ? 117.668 121.247 160.347 1.00 47.48 ?  659 LYS B C     1 
ATOM   10856 O  O     . LYS B 1 659 ? 116.786 121.543 159.537 1.00 49.57 ?  659 LYS B O     1 
ATOM   10857 C  CB    . LYS B 1 659 ? 117.273 121.624 162.787 1.00 45.65 ?  659 LYS B CB    1 
ATOM   10858 C  CG    . LYS B 1 659 ? 117.640 122.357 164.064 1.00 46.86 ?  659 LYS B CG    1 
ATOM   10859 C  CD    . LYS B 1 659 ? 117.039 121.671 165.280 1.00 49.12 ?  659 LYS B CD    1 
ATOM   10860 C  CE    . LYS B 1 659 ? 117.448 122.367 166.567 1.00 46.79 ?  659 LYS B CE    1 
ATOM   10861 N  NZ    . LYS B 1 659 ? 117.152 121.540 167.769 1.00 49.98 1  659 LYS B NZ    1 
ATOM   10862 N  N     . ASP B 1 660 ? 118.410 120.142 160.245 1.00 53.65 ?  660 ASP B N     1 
ATOM   10863 C  CA    . ASP B 1 660 ? 118.188 119.194 159.159 1.00 52.62 ?  660 ASP B CA    1 
ATOM   10864 C  C     . ASP B 1 660 ? 116.833 118.506 159.258 1.00 51.96 ?  660 ASP B C     1 
ATOM   10865 O  O     . ASP B 1 660 ? 116.289 118.082 158.233 1.00 51.23 ?  660 ASP B O     1 
ATOM   10866 C  CB    . ASP B 1 660 ? 119.302 118.146 159.145 1.00 53.34 ?  660 ASP B CB    1 
ATOM   10867 C  CG    . ASP B 1 660 ? 120.321 118.392 158.050 1.00 55.56 ?  660 ASP B CG    1 
ATOM   10868 O  OD1   . ASP B 1 660 ? 119.956 118.998 157.022 1.00 54.48 ?  660 ASP B OD1   1 
ATOM   10869 O  OD2   . ASP B 1 660 ? 121.488 117.981 158.218 1.00 53.90 -1 660 ASP B OD2   1 
ATOM   10870 N  N     . THR B 1 661 ? 116.276 118.389 160.466 1.00 52.85 ?  661 THR B N     1 
ATOM   10871 C  CA    . THR B 1 661 ? 115.018 117.669 160.640 1.00 52.27 ?  661 THR B CA    1 
ATOM   10872 C  C     . THR B 1 661 ? 113.847 118.425 160.023 1.00 52.80 ?  661 THR B C     1 
ATOM   10873 O  O     . THR B 1 661 ? 112.920 117.811 159.484 1.00 55.96 ?  661 THR B O     1 
ATOM   10874 C  CB    . THR B 1 661 ? 114.761 117.412 162.124 1.00 53.12 ?  661 THR B CB    1 
ATOM   10875 O  OG1   . THR B 1 661 ? 114.830 118.650 162.844 1.00 54.39 ?  661 THR B OG1   1 
ATOM   10876 C  CG2   . THR B 1 661 ? 115.796 116.448 162.684 1.00 52.13 ?  661 THR B CG2   1 
ATOM   10877 N  N     . MET B 1 662 ? 113.868 119.753 160.096 1.00 51.33 ?  662 MET B N     1 
ATOM   10878 C  CA    . MET B 1 662 ? 112.737 120.542 159.630 1.00 52.61 ?  662 MET B CA    1 
ATOM   10879 C  C     . MET B 1 662 ? 112.635 120.511 158.108 1.00 51.05 ?  662 MET B C     1 
ATOM   10880 O  O     . MET B 1 662 ? 113.621 120.302 157.397 1.00 52.14 ?  662 MET B O     1 
ATOM   10881 C  CB    . MET B 1 662 ? 112.853 121.981 160.133 1.00 51.42 ?  662 MET B CB    1 
ATOM   10882 C  CG    . MET B 1 662 ? 113.735 122.881 159.296 1.00 49.54 ?  662 MET B CG    1 
ATOM   10883 S  SD    . MET B 1 662 ? 113.804 124.542 159.985 1.00 59.95 ?  662 MET B SD    1 
ATOM   10884 C  CE    . MET B 1 662 ? 113.696 124.195 161.739 1.00 49.08 ?  662 MET B CE    1 
ATOM   10885 N  N     . THR B 1 663 ? 111.417 120.718 157.615 1.00 43.99 ?  663 THR B N     1 
ATOM   10886 C  CA    . THR B 1 663 ? 111.093 120.564 156.207 1.00 44.61 ?  663 THR B CA    1 
ATOM   10887 C  C     . THR B 1 663 ? 111.098 121.921 155.506 1.00 44.35 ?  663 THR B C     1 
ATOM   10888 O  O     . THR B 1 663 ? 111.317 122.969 156.117 1.00 47.40 ?  663 THR B O     1 
ATOM   10889 C  CB    . THR B 1 663 ? 109.733 119.880 156.051 1.00 44.65 ?  663 THR B CB    1 
ATOM   10890 O  OG1   . THR B 1 663 ? 108.717 120.697 156.642 1.00 46.81 ?  663 THR B OG1   1 
ATOM   10891 C  CG2   . THR B 1 663 ? 109.741 118.527 156.740 1.00 45.09 ?  663 THR B CG2   1 
ATOM   10892 N  N     . THR B 1 664 ? 110.856 121.893 154.192 1.00 36.56 ?  664 THR B N     1 
ATOM   10893 C  CA    . THR B 1 664 ? 110.734 123.138 153.440 1.00 37.93 ?  664 THR B CA    1 
ATOM   10894 C  C     . THR B 1 664 ? 109.504 123.926 153.867 1.00 36.91 ?  664 THR B C     1 
ATOM   10895 O  O     . THR B 1 664 ? 109.459 125.148 153.694 1.00 39.76 ?  664 THR B O     1 
ATOM   10896 C  CB    . THR B 1 664 ? 110.678 122.854 151.938 1.00 37.84 ?  664 THR B CB    1 
ATOM   10897 O  OG1   . THR B 1 664 ? 109.463 122.161 151.626 1.00 38.33 ?  664 THR B OG1   1 
ATOM   10898 C  CG2   . THR B 1 664 ? 111.866 122.008 151.509 1.00 37.08 ?  664 THR B CG2   1 
ATOM   10899 N  N     . ARG B 1 665 ? 108.496 123.246 154.417 1.00 39.50 ?  665 ARG B N     1 
ATOM   10900 C  CA    . ARG B 1 665 ? 107.326 123.942 154.940 1.00 37.27 ?  665 ARG B CA    1 
ATOM   10901 C  C     . ARG B 1 665 ? 107.693 124.809 156.137 1.00 40.60 ?  665 ARG B C     1 
ATOM   10902 O  O     . ARG B 1 665 ? 107.171 125.917 156.289 1.00 42.67 ?  665 ARG B O     1 
ATOM   10903 C  CB    . ARG B 1 665 ? 106.244 122.928 155.307 1.00 39.03 ?  665 ARG B CB    1 
ATOM   10904 C  CG    . ARG B 1 665 ? 104.922 123.522 155.765 1.00 36.25 ?  665 ARG B CG    1 
ATOM   10905 C  CD    . ARG B 1 665 ? 104.654 123.176 157.219 1.00 39.06 ?  665 ARG B CD    1 
ATOM   10906 N  NE    . ARG B 1 665 ? 103.229 123.027 157.491 1.00 42.59 ?  665 ARG B NE    1 
ATOM   10907 C  CZ    . ARG B 1 665 ? 102.590 123.607 158.498 1.00 42.49 ?  665 ARG B CZ    1 
ATOM   10908 N  NH1   . ARG B 1 665 ? 103.223 124.381 159.363 1.00 43.20 1  665 ARG B NH1   1 
ATOM   10909 N  NH2   . ARG B 1 665 ? 101.284 123.403 158.641 1.00 41.16 ?  665 ARG B NH2   1 
ATOM   10910 N  N     . ASP B 1 666 ? 108.594 124.325 156.995 1.00 40.52 ?  666 ASP B N     1 
ATOM   10911 C  CA    . ASP B 1 666 ? 109.067 125.141 158.108 1.00 36.31 ?  666 ASP B CA    1 
ATOM   10912 C  C     . ASP B 1 666 ? 109.833 126.362 157.610 1.00 40.69 ?  666 ASP B C     1 
ATOM   10913 O  O     . ASP B 1 666 ? 109.681 127.462 158.155 1.00 43.81 ?  666 ASP B O     1 
ATOM   10914 C  CB    . ASP B 1 666 ? 109.939 124.301 159.040 1.00 39.39 ?  666 ASP B CB    1 
ATOM   10915 C  CG    . ASP B 1 666 ? 109.160 123.197 159.726 1.00 46.56 ?  666 ASP B CG    1 
ATOM   10916 O  OD1   . ASP B 1 666 ? 108.087 123.490 160.293 1.00 46.49 ?  666 ASP B OD1   1 
ATOM   10917 O  OD2   . ASP B 1 666 ? 109.618 122.036 159.696 1.00 46.36 -1 666 ASP B OD2   1 
ATOM   10918 N  N     . LEU B 1 667 ? 110.661 126.186 156.579 1.00 34.44 ?  667 LEU B N     1 
ATOM   10919 C  CA    . LEU B 1 667 ? 111.378 127.318 155.999 1.00 29.98 ?  667 LEU B CA    1 
ATOM   10920 C  C     . LEU B 1 667 ? 110.410 128.332 155.401 1.00 28.63 ?  667 LEU B C     1 
ATOM   10921 O  O     . LEU B 1 667 ? 110.590 129.546 155.564 1.00 35.33 ?  667 LEU B O     1 
ATOM   10922 C  CB    . LEU B 1 667 ? 112.361 126.818 154.940 1.00 33.52 ?  667 LEU B CB    1 
ATOM   10923 C  CG    . LEU B 1 667 ? 113.368 127.821 154.380 1.00 32.74 ?  667 LEU B CG    1 
ATOM   10924 C  CD1   . LEU B 1 667 ? 113.947 128.673 155.492 1.00 34.04 ?  667 LEU B CD1   1 
ATOM   10925 C  CD2   . LEU B 1 667 ? 114.470 127.094 153.633 1.00 31.27 ?  667 LEU B CD2   1 
ATOM   10926 N  N     . ASN B 1 668 ? 109.374 127.853 154.710 1.00 29.56 ?  668 ASN B N     1 
ATOM   10927 C  CA    . ASN B 1 668 ? 108.370 128.755 154.158 1.00 24.89 ?  668 ASN B CA    1 
ATOM   10928 C  C     . ASN B 1 668 ? 107.614 129.482 155.263 1.00 26.58 ?  668 ASN B C     1 
ATOM   10929 O  O     . ASN B 1 668 ? 107.305 130.669 155.129 1.00 28.91 ?  668 ASN B O     1 
ATOM   10930 C  CB    . ASN B 1 668 ? 107.402 127.983 153.263 1.00 28.31 ?  668 ASN B CB    1 
ATOM   10931 C  CG    . ASN B 1 668 ? 107.862 127.926 151.822 1.00 32.47 ?  668 ASN B CG    1 
ATOM   10932 O  OD1   . ASN B 1 668 ? 108.558 128.820 151.345 1.00 33.33 ?  668 ASN B OD1   1 
ATOM   10933 N  ND2   . ASN B 1 668 ? 107.474 126.868 151.121 1.00 33.17 ?  668 ASN B ND2   1 
ATOM   10934 N  N     . ARG B 1 669 ? 107.303 128.785 156.357 1.00 30.84 ?  669 ARG B N     1 
ATOM   10935 C  CA    . ARG B 1 669 ? 106.638 129.431 157.484 1.00 33.19 ?  669 ARG B CA    1 
ATOM   10936 C  C     . ARG B 1 669 ? 107.517 130.510 158.096 1.00 27.48 ?  669 ARG B C     1 
ATOM   10937 O  O     . ARG B 1 669 ? 107.029 131.585 158.459 1.00 28.14 ?  669 ARG B O     1 
ATOM   10938 C  CB    . ARG B 1 669 ? 106.260 128.394 158.540 1.00 31.40 ?  669 ARG B CB    1 
ATOM   10939 C  CG    . ARG B 1 669 ? 104.772 128.132 158.646 1.00 30.10 ?  669 ARG B CG    1 
ATOM   10940 C  CD    . ARG B 1 669 ? 104.447 127.329 159.896 1.00 32.17 ?  669 ARG B CD    1 
ATOM   10941 N  NE    . ARG B 1 669 ? 104.366 128.162 161.091 1.00 31.03 ?  669 ARG B NE    1 
ATOM   10942 C  CZ    . ARG B 1 669 ? 103.379 129.009 161.355 1.00 34.14 ?  669 ARG B CZ    1 
ATOM   10943 N  NH1   . ARG B 1 669 ? 102.359 129.162 160.528 1.00 33.10 1  669 ARG B NH1   1 
ATOM   10944 N  NH2   . ARG B 1 669 ? 103.415 129.716 162.481 1.00 34.56 ?  669 ARG B NH2   1 
ATOM   10945 N  N     . ILE B 1 670 ? 108.817 130.239 158.229 1.00 24.89 ?  670 ILE B N     1 
ATOM   10946 C  CA    . ILE B 1 670 ? 109.734 131.248 158.754 1.00 28.67 ?  670 ILE B CA    1 
ATOM   10947 C  C     . ILE B 1 670 ? 109.789 132.452 157.824 1.00 27.42 ?  670 ILE B C     1 
ATOM   10948 O  O     . ILE B 1 670 ? 109.769 133.604 158.273 1.00 27.35 ?  670 ILE B O     1 
ATOM   10949 C  CB    . ILE B 1 670 ? 111.130 130.641 158.985 1.00 28.82 ?  670 ILE B CB    1 
ATOM   10950 C  CG1   . ILE B 1 670 ? 111.079 129.593 160.099 1.00 28.87 ?  670 ILE B CG1   1 
ATOM   10951 C  CG2   . ILE B 1 670 ? 112.132 131.725 159.336 1.00 26.47 ?  670 ILE B CG2   1 
ATOM   10952 C  CD1   . ILE B 1 670 ? 112.211 128.593 160.046 1.00 28.03 ?  670 ILE B CD1   1 
ATOM   10953 N  N     . ASP B 1 671 ? 109.850 132.206 156.512 1.00 27.88 ?  671 ASP B N     1 
ATOM   10954 C  CA    . ASP B 1 671 ? 109.878 133.304 155.549 1.00 21.61 ?  671 ASP B CA    1 
ATOM   10955 C  C     . ASP B 1 671 ? 108.604 134.139 155.621 1.00 22.57 ?  671 ASP B C     1 
ATOM   10956 O  O     . ASP B 1 671 ? 108.655 135.374 155.582 1.00 26.72 ?  671 ASP B O     1 
ATOM   10957 C  CB    . ASP B 1 671 ? 110.073 132.754 154.135 1.00 22.56 ?  671 ASP B CB    1 
ATOM   10958 C  CG    . ASP B 1 671 ? 111.461 132.192 153.913 1.00 32.56 ?  671 ASP B CG    1 
ATOM   10959 O  OD1   . ASP B 1 671 ? 112.396 132.605 154.628 1.00 35.53 ?  671 ASP B OD1   1 
ATOM   10960 O  OD2   . ASP B 1 671 ? 111.619 131.333 153.020 1.00 33.40 -1 671 ASP B OD2   1 
ATOM   10961 N  N     . LEU B 1 672 ? 107.449 133.480 155.727 1.00 22.25 ?  672 LEU B N     1 
ATOM   10962 C  CA    . LEU B 1 672 ? 106.185 134.203 155.782 1.00 20.71 ?  672 LEU B CA    1 
ATOM   10963 C  C     . LEU B 1 672 ? 106.021 134.957 157.093 1.00 21.52 ?  672 LEU B C     1 
ATOM   10964 O  O     . LEU B 1 672 ? 105.421 136.037 157.112 1.00 26.69 ?  672 LEU B O     1 
ATOM   10965 C  CB    . LEU B 1 672 ? 105.019 133.238 155.571 1.00 24.45 ?  672 LEU B CB    1 
ATOM   10966 C  CG    . LEU B 1 672 ? 104.966 132.582 154.191 1.00 23.66 ?  672 LEU B CG    1 
ATOM   10967 C  CD1   . LEU B 1 672 ? 104.087 131.342 154.220 1.00 22.52 ?  672 LEU B CD1   1 
ATOM   10968 C  CD2   . LEU B 1 672 ? 104.489 133.572 153.141 1.00 20.82 ?  672 LEU B CD2   1 
ATOM   10969 N  N     . TYR B 1 673 ? 106.536 134.412 158.196 1.00 21.13 ?  673 TYR B N     1 
ATOM   10970 C  CA    . TYR B 1 673 ? 106.515 135.144 159.457 1.00 18.26 ?  673 TYR B CA    1 
ATOM   10971 C  C     . TYR B 1 673 ? 107.443 136.349 159.403 1.00 19.58 ?  673 TYR B C     1 
ATOM   10972 O  O     . TYR B 1 673 ? 107.130 137.406 159.961 1.00 27.13 ?  673 TYR B O     1 
ATOM   10973 C  CB    . TYR B 1 673 ? 106.902 134.220 160.610 1.00 18.99 ?  673 TYR B CB    1 
ATOM   10974 C  CG    . TYR B 1 673 ? 106.805 134.875 161.967 1.00 23.24 ?  673 TYR B CG    1 
ATOM   10975 C  CD1   . TYR B 1 673 ? 105.586 135.321 162.457 1.00 22.65 ?  673 TYR B CD1   1 
ATOM   10976 C  CD2   . TYR B 1 673 ? 107.932 135.050 162.757 1.00 16.57 ?  673 TYR B CD2   1 
ATOM   10977 C  CE1   . TYR B 1 673 ? 105.491 135.919 163.694 1.00 18.82 ?  673 TYR B CE1   1 
ATOM   10978 C  CE2   . TYR B 1 673 ? 107.847 135.649 163.997 1.00 19.29 ?  673 TYR B CE2   1 
ATOM   10979 C  CZ    . TYR B 1 673 ? 106.625 136.081 164.460 1.00 20.46 ?  673 TYR B CZ    1 
ATOM   10980 O  OH    . TYR B 1 673 ? 106.534 136.679 165.696 1.00 28.40 ?  673 TYR B OH    1 
ATOM   10981 N  N     . ALA B 1 674 ? 108.595 136.203 158.746 1.00 18.23 ?  674 ALA B N     1 
ATOM   10982 C  CA    . ALA B 1 674 ? 109.489 137.337 158.548 1.00 14.78 ?  674 ALA B CA    1 
ATOM   10983 C  C     . ALA B 1 674 ? 108.808 138.427 157.734 1.00 19.33 ?  674 ALA B C     1 
ATOM   10984 O  O     . ALA B 1 674 ? 108.884 139.614 158.073 1.00 23.74 ?  674 ALA B O     1 
ATOM   10985 C  CB    . ALA B 1 674 ? 110.775 136.871 157.864 1.00 13.81 ?  674 ALA B CB    1 
ATOM   10986 N  N     . HIS B 1 675 ? 108.122 138.038 156.658 1.00 18.20 ?  675 HIS B N     1 
ATOM   10987 C  CA    . HIS B 1 675 ? 107.379 139.011 155.865 1.00 19.37 ?  675 HIS B CA    1 
ATOM   10988 C  C     . HIS B 1 675 ? 106.278 139.667 156.691 1.00 18.72 ?  675 HIS B C     1 
ATOM   10989 O  O     . HIS B 1 675 ? 106.044 140.876 156.581 1.00 26.02 ?  675 HIS B O     1 
ATOM   10990 C  CB    . HIS B 1 675 ? 106.791 138.335 154.627 1.00 19.31 ?  675 HIS B CB    1 
ATOM   10991 C  CG    . HIS B 1 675 ? 105.815 139.190 153.883 1.00 17.26 ?  675 HIS B CG    1 
ATOM   10992 N  ND1   . HIS B 1 675 ? 104.452 139.089 154.058 1.00 24.61 ?  675 HIS B ND1   1 
ATOM   10993 C  CD2   . HIS B 1 675 ? 106.005 140.166 152.965 1.00 13.15 ?  675 HIS B CD2   1 
ATOM   10994 C  CE1   . HIS B 1 675 ? 103.844 139.963 153.277 1.00 22.93 ?  675 HIS B CE1   1 
ATOM   10995 N  NE2   . HIS B 1 675 ? 104.764 140.630 152.604 1.00 27.16 ?  675 HIS B NE2   1 
ATOM   10996 N  N     . HIS B 1 676 ? 105.589 138.881 157.520 1.00 18.21 ?  676 HIS B N     1 
ATOM   10997 C  CA    . HIS B 1 676 ? 104.528 139.419 158.364 1.00 18.52 ?  676 HIS B CA    1 
ATOM   10998 C  C     . HIS B 1 676 ? 105.077 140.392 159.399 1.00 23.94 ?  676 HIS B C     1 
ATOM   10999 O  O     . HIS B 1 676 ? 104.447 141.413 159.697 1.00 25.31 ?  676 HIS B O     1 
ATOM   11000 C  CB    . HIS B 1 676 ? 103.779 138.273 159.044 1.00 19.23 ?  676 HIS B CB    1 
ATOM   11001 C  CG    . HIS B 1 676 ? 102.908 138.707 160.181 1.00 20.47 ?  676 HIS B CG    1 
ATOM   11002 N  ND1   . HIS B 1 676 ? 101.742 139.420 159.996 1.00 25.04 ?  676 HIS B ND1   1 
ATOM   11003 C  CD2   . HIS B 1 676 ? 103.033 138.531 161.517 1.00 21.47 ?  676 HIS B CD2   1 
ATOM   11004 C  CE1   . HIS B 1 676 ? 101.186 139.662 161.169 1.00 26.61 ?  676 HIS B CE1   1 
ATOM   11005 N  NE2   . HIS B 1 676 ? 101.950 139.133 162.109 1.00 26.42 ?  676 HIS B NE2   1 
ATOM   11006 N  N     . ARG B 1 677 ? 106.247 140.094 159.956 1.00 22.89 ?  677 ARG B N     1 
ATOM   11007 C  CA    . ARG B 1 677 ? 106.828 140.911 161.015 1.00 19.61 ?  677 ARG B CA    1 
ATOM   11008 C  C     . ARG B 1 677 ? 107.565 142.135 160.491 1.00 21.29 ?  677 ARG B C     1 
ATOM   11009 O  O     . ARG B 1 677 ? 108.081 142.916 161.297 1.00 29.33 ?  677 ARG B O     1 
ATOM   11010 C  CB    . ARG B 1 677 ? 107.777 140.066 161.867 1.00 19.71 ?  677 ARG B CB    1 
ATOM   11011 C  CG    . ARG B 1 677 ? 107.073 139.078 162.772 1.00 23.45 ?  677 ARG B CG    1 
ATOM   11012 C  CD    . ARG B 1 677 ? 106.455 139.773 163.971 1.00 21.42 ?  677 ARG B CD    1 
ATOM   11013 N  NE    . ARG B 1 677 ? 107.466 140.322 164.867 1.00 28.85 ?  677 ARG B NE    1 
ATOM   11014 C  CZ    . ARG B 1 677 ? 107.684 141.617 165.048 1.00 35.20 ?  677 ARG B CZ    1 
ATOM   11015 N  NH1   . ARG B 1 677 ? 106.972 142.534 164.413 1.00 30.86 1  677 ARG B NH1   1 
ATOM   11016 N  NH2   . ARG B 1 677 ? 108.641 142.003 165.887 1.00 26.43 ?  677 ARG B NH2   1 
ATOM   11017 N  N     . GLY B 1 678 ? 107.628 142.324 159.178 1.00 20.57 ?  678 GLY B N     1 
ATOM   11018 C  CA    . GLY B 1 678 ? 108.292 143.476 158.613 1.00 13.88 ?  678 GLY B CA    1 
ATOM   11019 C  C     . GLY B 1 678 ? 109.742 143.274 158.248 1.00 12.96 ?  678 GLY B C     1 
ATOM   11020 O  O     . GLY B 1 678 ? 110.444 144.264 158.010 1.00 18.02 ?  678 GLY B O     1 
ATOM   11021 N  N     . ILE B 1 679 ? 110.220 142.028 158.203 1.00 15.56 ?  679 ILE B N     1 
ATOM   11022 C  CA    . ILE B 1 679 ? 111.600 141.777 157.813 1.00 15.82 ?  679 ILE B CA    1 
ATOM   11023 C  C     . ILE B 1 679 ? 111.793 142.205 156.369 1.00 13.14 ?  679 ILE B C     1 
ATOM   11024 O  O     . ILE B 1 679 ? 111.008 141.843 155.484 1.00 26.35 ?  679 ILE B O     1 
ATOM   11025 C  CB    . ILE B 1 679 ? 111.958 140.297 158.012 1.00 16.76 ?  679 ILE B CB    1 
ATOM   11026 C  CG1   . ILE B 1 679 ? 111.901 139.930 159.494 1.00 11.88 ?  679 ILE B CG1   1 
ATOM   11027 C  CG2   . ILE B 1 679 ? 113.327 139.994 157.430 1.00 14.34 ?  679 ILE B CG2   1 
ATOM   11028 C  CD1   . ILE B 1 679 ? 112.838 140.721 160.344 1.00 13.38 ?  679 ILE B CD1   1 
ATOM   11029 N  N     . LYS B 1 680 ? 112.839 142.991 156.124 1.00 9.64  ?  680 LYS B N     1 
ATOM   11030 C  CA    . LYS B 1 680 ? 113.066 143.515 154.784 1.00 9.10  ?  680 LYS B CA    1 
ATOM   11031 C  C     . LYS B 1 680 ? 113.742 142.483 153.890 1.00 6.32  ?  680 LYS B C     1 
ATOM   11032 O  O     . LYS B 1 680 ? 113.297 142.242 152.763 1.00 19.51 ?  680 LYS B O     1 
ATOM   11033 C  CB    . LYS B 1 680 ? 113.901 144.791 154.862 1.00 6.44  ?  680 LYS B CB    1 
ATOM   11034 C  CG    . LYS B 1 680 ? 113.162 145.977 155.446 1.00 0.00  ?  680 LYS B CG    1 
ATOM   11035 C  CD    . LYS B 1 680 ? 114.032 147.217 155.453 1.00 8.90  ?  680 LYS B CD    1 
ATOM   11036 C  CE    . LYS B 1 680 ? 113.439 148.300 156.327 1.00 9.68  ?  680 LYS B CE    1 
ATOM   11037 N  NZ    . LYS B 1 680 ? 114.279 149.524 156.346 1.00 17.63 1  680 LYS B NZ    1 
ATOM   11038 N  N     . THR B 1 681 ? 114.813 141.860 154.374 1.00 14.09 ?  681 THR B N     1 
ATOM   11039 C  CA    . THR B 1 681 ? 115.573 140.906 153.583 1.00 7.46  ?  681 THR B CA    1 
ATOM   11040 C  C     . THR B 1 681 ? 115.945 139.706 154.439 1.00 12.18 ?  681 THR B C     1 
ATOM   11041 O  O     . THR B 1 681 ? 116.082 139.809 155.660 1.00 19.65 ?  681 THR B O     1 
ATOM   11042 C  CB    . THR B 1 681 ? 116.852 141.530 153.002 1.00 12.38 ?  681 THR B CB    1 
ATOM   11043 O  OG1   . THR B 1 681 ? 117.571 142.208 154.041 1.00 23.17 ?  681 THR B OG1   1 
ATOM   11044 C  CG2   . THR B 1 681 ? 116.518 142.518 151.899 1.00 8.64  ?  681 THR B CG2   1 
ATOM   11045 N  N     . ILE B 1 682 ? 116.109 138.562 153.779 1.00 12.38 ?  682 ILE B N     1 
ATOM   11046 C  CA    . ILE B 1 682 ? 116.604 137.341 154.400 1.00 9.09  ?  682 ILE B CA    1 
ATOM   11047 C  C     . ILE B 1 682 ? 117.871 136.929 153.665 1.00 15.98 ?  682 ILE B C     1 
ATOM   11048 O  O     . ILE B 1 682 ? 117.864 136.800 152.435 1.00 19.54 ?  682 ILE B O     1 
ATOM   11049 C  CB    . ILE B 1 682 ? 115.555 136.217 154.365 1.00 11.04 ?  682 ILE B CB    1 
ATOM   11050 C  CG1   . ILE B 1 682 ? 114.209 136.731 154.876 1.00 17.16 ?  682 ILE B CG1   1 
ATOM   11051 C  CG2   . ILE B 1 682 ? 116.018 135.047 155.198 1.00 19.66 ?  682 ILE B CG2   1 
ATOM   11052 C  CD1   . ILE B 1 682 ? 113.108 135.704 154.839 1.00 18.91 ?  682 ILE B CD1   1 
ATOM   11053 N  N     . TYR B 1 683 ? 118.958 136.736 154.413 1.00 13.01 ?  683 TYR B N     1 
ATOM   11054 C  CA    . TYR B 1 683 ? 120.260 136.526 153.782 1.00 12.37 ?  683 TYR B CA    1 
ATOM   11055 C  C     . TYR B 1 683 ? 120.471 135.071 153.372 1.00 20.43 ?  683 TYR B C     1 
ATOM   11056 O  O     . TYR B 1 683 ? 120.548 134.753 152.183 1.00 33.65 ?  683 TYR B O     1 
ATOM   11057 C  CB    . TYR B 1 683 ? 121.372 136.988 154.730 1.00 19.94 ?  683 TYR B CB    1 
ATOM   11058 C  CG    . TYR B 1 683 ? 122.756 136.987 154.122 1.00 16.76 ?  683 TYR B CG    1 
ATOM   11059 C  CD1   . TYR B 1 683 ? 122.936 137.045 152.746 1.00 10.05 ?  683 TYR B CD1   1 
ATOM   11060 C  CD2   . TYR B 1 683 ? 123.885 136.940 154.927 1.00 14.57 ?  683 TYR B CD2   1 
ATOM   11061 C  CE1   . TYR B 1 683 ? 124.195 137.047 152.191 1.00 17.35 ?  683 TYR B CE1   1 
ATOM   11062 C  CE2   . TYR B 1 683 ? 125.152 136.944 154.380 1.00 20.79 ?  683 TYR B CE2   1 
ATOM   11063 C  CZ    . TYR B 1 683 ? 125.301 136.998 153.011 1.00 21.07 ?  683 TYR B CZ    1 
ATOM   11064 O  OH    . TYR B 1 683 ? 126.561 137.002 152.462 1.00 18.47 ?  683 TYR B OH    1 
ATOM   11065 N  N     . TYR B 1 684 ? 120.542 134.169 154.343 1.00 28.72 ?  684 TYR B N     1 
ATOM   11066 C  CA    . TYR B 1 684 ? 120.957 132.805 154.062 1.00 22.47 ?  684 TYR B CA    1 
ATOM   11067 C  C     . TYR B 1 684 ? 120.087 131.828 154.831 1.00 33.54 ?  684 TYR B C     1 
ATOM   11068 O  O     . TYR B 1 684 ? 119.534 132.154 155.884 1.00 33.94 ?  684 TYR B O     1 
ATOM   11069 C  CB    . TYR B 1 684 ? 122.429 132.573 154.429 1.00 23.90 ?  684 TYR B CB    1 
ATOM   11070 C  CG    . TYR B 1 684 ? 123.382 132.683 153.262 1.00 25.15 ?  684 TYR B CG    1 
ATOM   11071 C  CD1   . TYR B 1 684 ? 123.195 131.928 152.113 1.00 28.20 ?  684 TYR B CD1   1 
ATOM   11072 C  CD2   . TYR B 1 684 ? 124.475 133.537 153.315 1.00 27.14 ?  684 TYR B CD2   1 
ATOM   11073 C  CE1   . TYR B 1 684 ? 124.068 132.025 151.046 1.00 30.33 ?  684 TYR B CE1   1 
ATOM   11074 C  CE2   . TYR B 1 684 ? 125.351 133.642 152.254 1.00 27.12 ?  684 TYR B CE2   1 
ATOM   11075 C  CZ    . TYR B 1 684 ? 125.144 132.885 151.122 1.00 30.90 ?  684 TYR B CZ    1 
ATOM   11076 O  OH    . TYR B 1 684 ? 126.017 132.988 150.065 1.00 33.34 ?  684 TYR B OH    1 
ATOM   11077 N  N     . ALA B 1 685 ? 119.974 130.625 154.286 1.00 32.23 ?  685 ALA B N     1 
ATOM   11078 C  CA    . ALA B 1 685 ? 119.349 129.496 154.961 1.00 31.89 ?  685 ALA B CA    1 
ATOM   11079 C  C     . ALA B 1 685 ? 120.454 128.470 155.199 1.00 34.11 ?  685 ALA B C     1 
ATOM   11080 O  O     . ALA B 1 685 ? 120.661 127.560 154.396 1.00 41.93 ?  685 ALA B O     1 
ATOM   11081 C  CB    . ALA B 1 685 ? 118.206 128.926 154.134 1.00 30.04 ?  685 ALA B CB    1 
ATOM   11082 N  N     . ARG B 1 686 ? 121.169 128.631 156.309 1.00 31.14 ?  686 ARG B N     1 
ATOM   11083 C  CA    . ARG B 1 686 ? 122.243 127.716 156.671 1.00 35.59 ?  686 ARG B CA    1 
ATOM   11084 C  C     . ARG B 1 686 ? 121.665 126.571 157.490 1.00 40.36 ?  686 ARG B C     1 
ATOM   11085 O  O     . ARG B 1 686 ? 121.074 126.796 158.550 1.00 39.37 ?  686 ARG B O     1 
ATOM   11086 C  CB    . ARG B 1 686 ? 123.322 128.450 157.463 1.00 35.54 ?  686 ARG B CB    1 
ATOM   11087 C  CG    . ARG B 1 686 ? 124.082 129.492 156.666 1.00 39.12 ?  686 ARG B CG    1 
ATOM   11088 C  CD    . ARG B 1 686 ? 125.218 130.084 157.483 1.00 40.12 ?  686 ARG B CD    1 
ATOM   11089 N  NE    . ARG B 1 686 ? 125.749 129.132 158.451 1.00 42.56 ?  686 ARG B NE    1 
ATOM   11090 C  CZ    . ARG B 1 686 ? 126.944 128.563 158.363 1.00 41.73 ?  686 ARG B CZ    1 
ATOM   11091 N  NH1   . ARG B 1 686 ? 127.763 128.829 157.359 1.00 40.57 1  686 ARG B NH1   1 
ATOM   11092 N  NH2   . ARG B 1 686 ? 127.327 127.708 159.306 1.00 38.17 ?  686 ARG B NH2   1 
ATOM   11093 N  N     . THR B 1 687 ? 121.841 125.346 157.005 1.00 42.20 ?  687 THR B N     1 
ATOM   11094 C  CA    . THR B 1 687 ? 121.314 124.161 157.664 1.00 45.25 ?  687 THR B CA    1 
ATOM   11095 C  C     . THR B 1 687 ? 122.434 123.447 158.407 1.00 45.70 ?  687 THR B C     1 
ATOM   11096 O  O     . THR B 1 687 ? 123.527 123.253 157.867 1.00 45.26 ?  687 THR B O     1 
ATOM   11097 C  CB    . THR B 1 687 ? 120.664 123.212 156.654 1.00 43.73 ?  687 THR B CB    1 
ATOM   11098 O  OG1   . THR B 1 687 ? 119.850 123.963 155.746 1.00 43.79 ?  687 THR B OG1   1 
ATOM   11099 C  CG2   . THR B 1 687 ? 119.796 122.194 157.373 1.00 42.22 ?  687 THR B CG2   1 
ATOM   11100 N  N     . LYS B 1 688 ? 122.153 123.060 159.646 1.00 40.87 ?  688 LYS B N     1 
ATOM   11101 C  CA    . LYS B 1 688 ? 123.147 122.405 160.487 1.00 43.33 ?  688 LYS B CA    1 
ATOM   11102 C  C     . LYS B 1 688 ? 123.402 120.974 160.022 1.00 48.17 ?  688 LYS B C     1 
ATOM   11103 O  O     . LYS B 1 688 ? 122.552 120.099 160.179 1.00 48.97 ?  688 LYS B O     1 
ATOM   11104 C  CB    . LYS B 1 688 ? 122.700 122.415 161.949 1.00 42.70 ?  688 LYS B CB    1 
ATOM   11105 C  CG    . LYS B 1 688 ? 123.712 121.826 162.914 1.00 41.41 ?  688 LYS B CG    1 
ATOM   11106 C  CD    . LYS B 1 688 ? 123.272 122.015 164.354 1.00 44.48 ?  688 LYS B CD    1 
ATOM   11107 C  CE    . LYS B 1 688 ? 124.364 121.595 165.323 1.00 46.73 ?  688 LYS B CE    1 
ATOM   11108 N  NZ    . LYS B 1 688 ? 123.959 121.810 166.739 1.00 44.27 ?  688 LYS B NZ    1 
ATOM   11109 N  N     . ASP C 2 37  ? 123.819 82.073  110.663 1.00 45.99 ?  16  ASP C N     1 
ATOM   11110 C  CA    . ASP C 2 37  ? 124.032 82.837  109.430 1.00 45.47 ?  16  ASP C CA    1 
ATOM   11111 C  C     . ASP C 2 37  ? 123.583 84.297  109.502 1.00 44.13 ?  16  ASP C C     1 
ATOM   11112 O  O     . ASP C 2 37  ? 123.802 85.058  108.557 1.00 44.46 ?  16  ASP C O     1 
ATOM   11113 C  CB    . ASP C 2 37  ? 123.317 82.148  108.265 1.00 45.90 ?  16  ASP C CB    1 
ATOM   11114 C  CG    . ASP C 2 37  ? 123.630 80.673  108.188 1.00 47.25 ?  16  ASP C CG    1 
ATOM   11115 O  OD1   . ASP C 2 37  ? 124.796 80.296  108.430 1.00 47.99 ?  16  ASP C OD1   1 
ATOM   11116 O  OD2   . ASP C 2 37  ? 122.704 79.892  107.887 1.00 49.50 -1 16  ASP C OD2   1 
ATOM   11117 N  N     . PHE C 2 38  ? 122.963 84.690  110.611 1.00 42.17 ?  17  PHE C N     1 
ATOM   11118 C  CA    . PHE C 2 38  ? 122.297 85.996  110.673 1.00 40.67 ?  17  PHE C CA    1 
ATOM   11119 C  C     . PHE C 2 38  ? 122.557 86.864  111.911 1.00 39.46 ?  17  PHE C C     1 
ATOM   11120 O  O     . PHE C 2 38  ? 122.410 88.086  111.842 1.00 39.17 ?  17  PHE C O     1 
ATOM   11121 C  CB    . PHE C 2 38  ? 120.783 85.829  110.455 1.00 40.24 ?  17  PHE C CB    1 
ATOM   11122 C  CG    . PHE C 2 38  ? 120.127 84.851  111.400 1.00 39.58 ?  17  PHE C CG    1 
ATOM   11123 C  CD1   . PHE C 2 38  ? 119.669 85.267  112.651 1.00 38.78 ?  17  PHE C CD1   1 
ATOM   11124 C  CD2   . PHE C 2 38  ? 119.952 83.515  111.034 1.00 39.43 ?  17  PHE C CD2   1 
ATOM   11125 C  CE1   . PHE C 2 38  ? 119.053 84.371  113.525 1.00 38.07 ?  17  PHE C CE1   1 
ATOM   11126 C  CE2   . PHE C 2 38  ? 119.336 82.609  111.904 1.00 39.10 ?  17  PHE C CE2   1 
ATOM   11127 C  CZ    . PHE C 2 38  ? 118.888 83.039  113.153 1.00 38.63 ?  17  PHE C CZ    1 
ATOM   11128 N  N     . THR C 2 39  ? 122.931 86.246  113.033 1.00 38.22 ?  18  THR C N     1 
ATOM   11129 C  CA    . THR C 2 39  ? 123.057 86.985  114.301 1.00 37.09 ?  18  THR C CA    1 
ATOM   11130 C  C     . THR C 2 39  ? 124.027 88.175  114.211 1.00 36.84 ?  18  THR C C     1 
ATOM   11131 O  O     . THR C 2 39  ? 123.701 89.281  114.672 1.00 36.13 ?  18  THR C O     1 
ATOM   11132 C  CB    . THR C 2 39  ? 123.364 86.059  115.515 1.00 36.59 ?  18  THR C CB    1 
ATOM   11133 O  OG1   . THR C 2 39  ? 122.179 85.337  115.863 1.00 36.50 ?  18  THR C OG1   1 
ATOM   11134 C  CG2   . THR C 2 39  ? 123.782 86.866  116.728 1.00 36.06 ?  18  THR C CG2   1 
ATOM   11135 N  N     . GLN C 2 40  ? 125.195 87.952  113.601 1.00 37.01 ?  19  GLN C N     1 
ATOM   11136 C  CA    . GLN C 2 40  ? 126.208 89.011  113.470 1.00 37.33 ?  19  GLN C CA    1 
ATOM   11137 C  C     . GLN C 2 40  ? 125.697 90.239  112.736 1.00 36.63 ?  19  GLN C C     1 
ATOM   11138 O  O     . GLN C 2 40  ? 125.958 91.366  113.155 1.00 36.10 ?  19  GLN C O     1 
ATOM   11139 C  CB    . GLN C 2 40  ? 127.489 88.502  112.811 1.00 38.24 ?  19  GLN C CB    1 
ATOM   11140 C  CG    . GLN C 2 40  ? 128.417 87.813  113.786 1.00 41.33 ?  19  GLN C CG    1 
ATOM   11141 C  CD    . GLN C 2 40  ? 129.884 88.056  113.488 1.00 45.15 ?  19  GLN C CD    1 
ATOM   11142 O  OE1   . GLN C 2 40  ? 130.289 88.180  112.326 1.00 47.33 ?  19  GLN C OE1   1 
ATOM   11143 N  NE2   . GLN C 2 40  ? 130.694 88.124  114.543 1.00 46.51 ?  19  GLN C NE2   1 
ATOM   11144 N  N     . MET C 2 41  ? 124.959 90.019  111.652 1.00 36.23 ?  20  MET C N     1 
ATOM   11145 C  CA    . MET C 2 41  ? 124.392 91.133  110.904 1.00 36.40 ?  20  MET C CA    1 
ATOM   11146 C  C     . MET C 2 41  ? 123.264 91.835  111.682 1.00 34.93 ?  20  MET C C     1 
ATOM   11147 O  O     . MET C 2 41  ? 123.126 93.053  111.596 1.00 34.20 ?  20  MET C O     1 
ATOM   11148 C  CB    . MET C 2 41  ? 124.014 90.728  109.462 1.00 37.35 ?  20  MET C CB    1 
ATOM   11149 C  CG    . MET C 2 41  ? 122.636 90.136  109.233 1.00 40.49 ?  20  MET C CG    1 
ATOM   11150 S  SD    . MET C 2 41  ? 122.311 89.941  107.452 1.00 48.68 ?  20  MET C SD    1 
ATOM   11151 C  CE    . MET C 2 41  ? 123.030 88.324  107.132 1.00 47.17 ?  20  MET C CE    1 
ATOM   11152 N  N     . PHE C 2 42  ? 122.500 91.079  112.475 1.00 33.75 ?  21  PHE C N     1 
ATOM   11153 C  CA    . PHE C 2 42  ? 121.514 91.693  113.377 1.00 32.62 ?  21  PHE C CA    1 
ATOM   11154 C  C     . PHE C 2 42  ? 122.177 92.458  114.517 1.00 32.59 ?  21  PHE C C     1 
ATOM   11155 O  O     . PHE C 2 42  ? 121.715 93.539  114.896 1.00 32.23 ?  21  PHE C O     1 
ATOM   11156 C  CB    . PHE C 2 42  ? 120.514 90.666  113.907 1.00 32.12 ?  21  PHE C CB    1 
ATOM   11157 C  CG    . PHE C 2 42  ? 119.398 90.369  112.950 1.00 31.04 ?  21  PHE C CG    1 
ATOM   11158 C  CD1   . PHE C 2 42  ? 118.187 91.055  113.037 1.00 30.75 ?  21  PHE C CD1   1 
ATOM   11159 C  CD2   . PHE C 2 42  ? 119.555 89.411  111.955 1.00 30.99 ?  21  PHE C CD2   1 
ATOM   11160 C  CE1   . PHE C 2 42  ? 117.144 90.785  112.143 1.00 30.30 ?  21  PHE C CE1   1 
ATOM   11161 C  CE2   . PHE C 2 42  ? 118.518 89.131  111.050 1.00 30.74 ?  21  PHE C CE2   1 
ATOM   11162 C  CZ    . PHE C 2 42  ? 117.313 89.819  111.146 1.00 30.48 ?  21  PHE C CZ    1 
ATOM   11163 N  N     . TYR C 2 43  ? 123.263 91.902  115.051 1.00 32.33 ?  22  TYR C N     1 
ATOM   11164 C  CA    . TYR C 2 43  ? 124.052 92.597  116.065 1.00 32.50 ?  22  TYR C CA    1 
ATOM   11165 C  C     . TYR C 2 43  ? 124.505 93.959  115.544 1.00 33.01 ?  22  TYR C C     1 
ATOM   11166 O  O     . TYR C 2 43  ? 124.298 94.981  116.204 1.00 32.50 ?  22  TYR C O     1 
ATOM   11167 C  CB    . TYR C 2 43  ? 125.257 91.759  116.533 1.00 32.53 ?  22  TYR C CB    1 
ATOM   11168 C  CG    . TYR C 2 43  ? 126.215 92.562  117.396 1.00 33.27 ?  22  TYR C CG    1 
ATOM   11169 C  CD1   . TYR C 2 43  ? 125.959 92.767  118.754 1.00 32.34 ?  22  TYR C CD1   1 
ATOM   11170 C  CD2   . TYR C 2 43  ? 127.354 93.149  116.841 1.00 33.71 ?  22  TYR C CD2   1 
ATOM   11171 C  CE1   . TYR C 2 43  ? 126.825 93.523  119.544 1.00 33.58 ?  22  TYR C CE1   1 
ATOM   11172 C  CE2   . TYR C 2 43  ? 128.226 93.914  117.619 1.00 35.12 ?  22  TYR C CE2   1 
ATOM   11173 C  CZ    . TYR C 2 43  ? 127.958 94.092  118.970 1.00 35.30 ?  22  TYR C CZ    1 
ATOM   11174 O  OH    . TYR C 2 43  ? 128.820 94.845  119.736 1.00 36.54 ?  22  TYR C OH    1 
ATOM   11175 N  N     . ASN C 2 44  ? 125.107 93.964  114.352 1.00 33.80 ?  23  ASN C N     1 
ATOM   11176 C  CA    . ASN C 2 44  ? 125.609 95.189  113.743 1.00 34.80 ?  23  ASN C CA    1 
ATOM   11177 C  C     . ASN C 2 44  ? 124.489 96.185  113.450 1.00 34.40 ?  23  ASN C C     1 
ATOM   11178 O  O     . ASN C 2 44  ? 124.639 97.376  113.703 1.00 33.99 ?  23  ASN C O     1 
ATOM   11179 C  CB    . ASN C 2 44  ? 126.418 94.885  112.472 1.00 35.46 ?  23  ASN C CB    1 
ATOM   11180 C  CG    . ASN C 2 44  ? 127.679 94.053  112.747 1.00 38.28 ?  23  ASN C CG    1 
ATOM   11181 O  OD1   . ASN C 2 44  ? 128.219 94.039  113.863 1.00 41.01 ?  23  ASN C OD1   1 
ATOM   11182 N  ND2   . ASN C 2 44  ? 128.156 93.359  111.714 1.00 39.13 ?  23  ASN C ND2   1 
ATOM   11183 N  N     . GLN C 2 45  ? 123.363 95.689  112.935 1.00 34.49 ?  24  GLN C N     1 
ATOM   11184 C  CA    . GLN C 2 45  ? 122.216 96.539  112.638 1.00 34.81 ?  24  GLN C CA    1 
ATOM   11185 C  C     . GLN C 2 45  ? 121.619 97.149  113.912 1.00 34.68 ?  24  GLN C C     1 
ATOM   11186 O  O     . GLN C 2 45  ? 121.327 98.347  113.953 1.00 34.59 ?  24  GLN C O     1 
ATOM   11187 C  CB    . GLN C 2 45  ? 121.158 95.768  111.842 1.00 34.83 ?  24  GLN C CB    1 
ATOM   11188 C  CG    . GLN C 2 45  ? 120.106 96.647  111.160 1.00 36.14 ?  24  GLN C CG    1 
ATOM   11189 C  CD    . GLN C 2 45  ? 120.693 97.618  110.132 1.00 38.04 ?  24  GLN C CD    1 
ATOM   11190 O  OE1   . GLN C 2 45  ? 121.727 97.350  109.513 1.00 38.57 ?  24  GLN C OE1   1 
ATOM   11191 N  NE2   . GLN C 2 45  ? 120.028 98.760  109.954 1.00 38.67 ?  24  GLN C NE2   1 
ATOM   11192 N  N     . ASN C 2 46  ? 121.456 96.337  114.953 1.00 34.71 ?  25  ASN C N     1 
ATOM   11193 C  CA    . ASN C 2 46  ? 120.910 96.836  116.215 1.00 34.99 ?  25  ASN C CA    1 
ATOM   11194 C  C     . ASN C 2 46  ? 121.777 97.924  116.847 1.00 35.69 ?  25  ASN C C     1 
ATOM   11195 O  O     . ASN C 2 46  ? 121.273 98.985  117.231 1.00 35.41 ?  25  ASN C O     1 
ATOM   11196 C  CB    . ASN C 2 46  ? 120.643 95.693  117.202 1.00 34.64 ?  25  ASN C CB    1 
ATOM   11197 C  CG    . ASN C 2 46  ? 119.328 94.993  116.932 1.00 34.71 ?  25  ASN C CG    1 
ATOM   11198 O  OD1   . ASN C 2 46  ? 118.306 95.350  117.510 1.00 35.68 ?  25  ASN C OD1   1 
ATOM   11199 N  ND2   . ASN C 2 46  ? 119.338 94.015  116.021 1.00 34.71 ?  25  ASN C ND2   1 
ATOM   11200 N  N     . VAL C 2 47  ? 123.082 97.680  116.931 1.00 36.69 ?  26  VAL C N     1 
ATOM   11201 C  CA    . VAL C 2 47  ? 123.973 98.656  117.560 1.00 38.00 ?  26  VAL C CA    1 
ATOM   11202 C  C     . VAL C 2 47  ? 124.141 99.935  116.729 1.00 38.90 ?  26  VAL C C     1 
ATOM   11203 O  O     . VAL C 2 47  ? 124.332 101.009 117.291 1.00 39.46 ?  26  VAL C O     1 
ATOM   11204 C  CB    . VAL C 2 47  ? 125.345 98.058  117.974 1.00 38.16 ?  26  VAL C CB    1 
ATOM   11205 C  CG1   . VAL C 2 47  ? 125.142 96.899  118.930 1.00 37.75 ?  26  VAL C CG1   1 
ATOM   11206 C  CG2   . VAL C 2 47  ? 126.166 97.636  116.757 1.00 38.81 ?  26  VAL C CG2   1 
ATOM   11207 N  N     . LYS C 2 48  ? 124.035 99.825  115.405 1.00 39.67 ?  27  LYS C N     1 
ATOM   11208 C  CA    . LYS C 2 48  ? 124.132 101.004 114.540 1.00 40.50 ?  27  LYS C CA    1 
ATOM   11209 C  C     . LYS C 2 48  ? 122.834 101.823 114.545 1.00 40.02 ?  27  LYS C C     1 
ATOM   11210 O  O     . LYS C 2 48  ? 122.813 102.975 114.107 1.00 40.55 ?  27  LYS C O     1 
ATOM   11211 C  CB    . LYS C 2 48  ? 124.545 100.621 113.107 1.00 41.23 ?  27  LYS C CB    1 
ATOM   11212 C  CG    . LYS C 2 48  ? 123.398 100.176 112.201 1.00 42.50 ?  27  LYS C CG    1 
ATOM   11213 C  CD    . LYS C 2 48  ? 123.860 99.871  110.768 1.00 44.92 ?  27  LYS C CD    1 
ATOM   11214 C  CE    . LYS C 2 48  ? 124.029 101.139 109.934 1.00 46.66 ?  27  LYS C CE    1 
ATOM   11215 N  NZ    . LYS C 2 48  ? 122.753 101.903 109.806 1.00 47.26 1  27  LYS C NZ    1 
ATOM   11216 N  N     . GLN C 2 49  ? 121.754 101.223 115.031 1.00 39.10 ?  28  GLN C N     1 
ATOM   11217 C  CA    . GLN C 2 49  ? 120.490 101.922 115.129 1.00 38.22 ?  28  GLN C CA    1 
ATOM   11218 C  C     . GLN C 2 49  ? 120.322 102.603 116.486 1.00 37.23 ?  28  GLN C C     1 
ATOM   11219 O  O     . GLN C 2 49  ? 119.304 103.252 116.714 1.00 37.40 ?  28  GLN C O     1 
ATOM   11220 C  CB    . GLN C 2 49  ? 119.309 100.982 114.829 1.00 38.69 ?  28  GLN C CB    1 
ATOM   11221 C  CG    . GLN C 2 49  ? 119.157 100.625 113.342 1.00 39.57 ?  28  GLN C CG    1 
ATOM   11222 C  CD    . GLN C 2 49  ? 117.879 99.854  113.020 1.00 41.20 ?  28  GLN C CD    1 
ATOM   11223 O  OE1   . GLN C 2 49  ? 117.674 99.441  111.878 1.00 42.94 ?  28  GLN C OE1   1 
ATOM   11224 N  NE2   . GLN C 2 49  ? 117.016 99.660  114.021 1.00 41.23 ?  28  GLN C NE2   1 
ATOM   11225 N  N     . PHE C 2 50  ? 121.319 102.479 117.369 1.00 35.83 ?  29  PHE C N     1 
ATOM   11226 C  CA    . PHE C 2 50  ? 121.209 103.031 118.727 1.00 34.51 ?  29  PHE C CA    1 
ATOM   11227 C  C     . PHE C 2 50  ? 120.861 104.522 118.745 1.00 33.81 ?  29  PHE C C     1 
ATOM   11228 O  O     . PHE C 2 50  ? 121.452 105.310 118.005 1.00 33.66 ?  29  PHE C O     1 
ATOM   11229 C  CB    . PHE C 2 50  ? 122.463 102.772 119.566 1.00 34.59 ?  29  PHE C CB    1 
ATOM   11230 C  CG    . PHE C 2 50  ? 122.362 103.302 120.986 1.00 34.59 ?  29  PHE C CG    1 
ATOM   11231 C  CD1   . PHE C 2 50  ? 121.542 102.672 121.929 1.00 34.34 ?  29  PHE C CD1   1 
ATOM   11232 C  CD2   . PHE C 2 50  ? 123.068 104.441 121.372 1.00 35.49 ?  29  PHE C CD2   1 
ATOM   11233 C  CE1   . PHE C 2 50  ? 121.438 103.162 123.240 1.00 33.88 ?  29  PHE C CE1   1 
ATOM   11234 C  CE2   . PHE C 2 50  ? 122.972 104.945 122.682 1.00 34.12 ?  29  PHE C CE2   1 
ATOM   11235 C  CZ    . PHE C 2 50  ? 122.157 104.305 123.615 1.00 33.87 ?  29  PHE C CZ    1 
ATOM   11236 N  N     . TRP C 2 51  ? 119.905 104.888 119.601 1.00 32.24 ?  30  TRP C N     1 
ATOM   11237 C  CA    . TRP C 2 51  ? 119.440 106.268 119.725 1.00 31.28 ?  30  TRP C CA    1 
ATOM   11238 C  C     . TRP C 2 51  ? 118.885 106.556 121.122 1.00 31.12 ?  30  TRP C C     1 
ATOM   11239 O  O     . TRP C 2 51  ? 118.608 105.625 121.887 1.00 30.71 ?  30  TRP C O     1 
ATOM   11240 C  CB    . TRP C 2 51  ? 118.388 106.580 118.652 1.00 30.85 ?  30  TRP C CB    1 
ATOM   11241 C  CG    . TRP C 2 51  ? 117.136 105.743 118.753 1.00 29.31 ?  30  TRP C CG    1 
ATOM   11242 C  CD1   . TRP C 2 51  ? 116.951 104.475 118.272 1.00 29.07 ?  30  TRP C CD1   1 
ATOM   11243 C  CD2   . TRP C 2 51  ? 115.910 106.110 119.392 1.00 28.33 ?  30  TRP C CD2   1 
ATOM   11244 N  NE1   . TRP C 2 51  ? 115.683 104.036 118.564 1.00 28.01 ?  30  TRP C NE1   1 
ATOM   11245 C  CE2   . TRP C 2 51  ? 115.021 105.019 119.251 1.00 27.67 ?  30  TRP C CE2   1 
ATOM   11246 C  CE3   . TRP C 2 51  ? 115.474 107.254 120.076 1.00 27.27 ?  30  TRP C CE3   1 
ATOM   11247 C  CZ2   . TRP C 2 51  ? 113.725 105.038 119.765 1.00 26.54 ?  30  TRP C CZ2   1 
ATOM   11248 C  CZ3   . TRP C 2 51  ? 114.180 107.277 120.579 1.00 27.07 ?  30  TRP C CZ3   1 
ATOM   11249 C  CH2   . TRP C 2 51  ? 113.323 106.171 120.427 1.00 26.52 ?  30  TRP C CH2   1 
ATOM   11250 N  N     . LEU C 2 52  ? 118.732 107.844 121.441 1.00 30.65 ?  31  LEU C N     1 
ATOM   11251 C  CA    . LEU C 2 52  ? 118.088 108.302 122.675 1.00 30.38 ?  31  LEU C CA    1 
ATOM   11252 C  C     . LEU C 2 52  ? 117.059 109.380 122.345 1.00 30.51 ?  31  LEU C C     1 
ATOM   11253 O  O     . LEU C 2 52  ? 117.309 110.206 121.466 1.00 30.77 ?  31  LEU C O     1 
ATOM   11254 C  CB    . LEU C 2 52  ? 119.127 108.859 123.662 1.00 30.45 ?  31  LEU C CB    1 
ATOM   11255 C  CG    . LEU C 2 52  ? 120.145 107.848 124.199 1.00 30.29 ?  31  LEU C CG    1 
ATOM   11256 C  CD1   . LEU C 2 52  ? 121.393 108.530 124.776 1.00 30.69 ?  31  LEU C CD1   1 
ATOM   11257 C  CD2   . LEU C 2 52  ? 119.496 106.900 125.221 1.00 29.91 ?  31  LEU C CD2   1 
ATOM   11258 N  N     . PRO C 2 53  ? 115.904 109.387 123.049 1.00 30.73 ?  32  PRO C N     1 
ATOM   11259 C  CA    . PRO C 2 53  ? 114.852 110.375 122.756 1.00 31.17 ?  32  PRO C CA    1 
ATOM   11260 C  C     . PRO C 2 53  ? 115.325 111.823 122.866 1.00 32.18 ?  32  PRO C C     1 
ATOM   11261 O  O     . PRO C 2 53  ? 114.820 112.691 122.135 1.00 32.66 ?  32  PRO C O     1 
ATOM   11262 C  CB    . PRO C 2 53  ? 113.781 110.087 123.814 1.00 30.99 ?  32  PRO C CB    1 
ATOM   11263 C  CG    . PRO C 2 53  ? 114.468 109.246 124.864 1.00 30.50 ?  32  PRO C CG    1 
ATOM   11264 C  CD    . PRO C 2 53  ? 115.493 108.459 124.121 1.00 30.46 ?  32  PRO C CD    1 
ATOM   11265 N  N     . GLU C 2 54  ? 116.293 112.072 123.752 1.00 32.62 ?  33  GLU C N     1 
ATOM   11266 C  CA    . GLU C 2 54  ? 116.853 113.419 123.954 1.00 33.44 ?  33  GLU C CA    1 
ATOM   11267 C  C     . GLU C 2 54  ? 117.536 113.996 122.708 1.00 33.59 ?  33  GLU C C     1 
ATOM   11268 O  O     . GLU C 2 54  ? 117.778 115.199 122.643 1.00 34.05 ?  33  GLU C O     1 
ATOM   11269 C  CB    . GLU C 2 54  ? 117.828 113.450 125.145 1.00 33.72 ?  33  GLU C CB    1 
ATOM   11270 C  CG    . GLU C 2 54  ? 117.166 113.336 126.532 1.00 34.53 ?  33  GLU C CG    1 
ATOM   11271 C  CD    . GLU C 2 54  ? 116.693 111.918 126.857 1.00 35.09 ?  33  GLU C CD    1 
ATOM   11272 O  OE1   . GLU C 2 54  ? 117.220 110.946 126.257 1.00 34.38 ?  33  GLU C OE1   1 
ATOM   11273 O  OE2   . GLU C 2 54  ? 115.790 111.779 127.713 1.00 35.53 -1 33  GLU C OE2   1 
ATOM   11274 N  N     . GLU C 2 55  ? 117.844 113.141 121.731 1.00 33.82 ?  34  GLU C N     1 
ATOM   11275 C  CA    . GLU C 2 55  ? 118.405 113.584 120.451 1.00 34.19 ?  34  GLU C CA    1 
ATOM   11276 C  C     . GLU C 2 55  ? 117.388 114.401 119.641 1.00 33.83 ?  34  GLU C C     1 
ATOM   11277 O  O     . GLU C 2 55  ? 117.767 115.164 118.754 1.00 33.93 ?  34  GLU C O     1 
ATOM   11278 C  CB    . GLU C 2 55  ? 118.880 112.390 119.603 1.00 34.52 ?  34  GLU C CB    1 
ATOM   11279 C  CG    . GLU C 2 55  ? 120.007 111.550 120.199 1.00 36.50 ?  34  GLU C CG    1 
ATOM   11280 C  CD    . GLU C 2 55  ? 120.598 110.572 119.188 1.00 40.03 ?  34  GLU C CD    1 
ATOM   11281 O  OE1   . GLU C 2 55  ? 121.492 110.972 118.410 1.00 42.43 ?  34  GLU C OE1   1 
ATOM   11282 O  OE2   . GLU C 2 55  ? 120.177 109.399 119.173 1.00 39.35 -1 34  GLU C OE2   1 
ATOM   11283 N  N     . ILE C 2 56  ? 116.104 114.203 119.939 1.00 33.31 ?  35  ILE C N     1 
ATOM   11284 C  CA    . ILE C 2 56  ? 114.993 114.853 119.241 1.00 33.14 ?  35  ILE C CA    1 
ATOM   11285 C  C     . ILE C 2 56  ? 114.372 115.908 120.162 1.00 32.58 ?  35  ILE C C     1 
ATOM   11286 O  O     . ILE C 2 56  ? 113.857 115.574 121.223 1.00 32.12 ?  35  ILE C O     1 
ATOM   11287 C  CB    . ILE C 2 56  ? 113.888 113.812 118.848 1.00 33.03 ?  35  ILE C CB    1 
ATOM   11288 C  CG1   . ILE C 2 56  ? 114.477 112.600 118.092 1.00 34.76 ?  35  ILE C CG1   1 
ATOM   11289 C  CG2   . ILE C 2 56  ? 112.743 114.470 118.068 1.00 33.61 ?  35  ILE C CG2   1 
ATOM   11290 C  CD1   . ILE C 2 56  ? 115.033 112.892 116.696 1.00 36.75 ?  35  ILE C CD1   1 
ATOM   11291 N  N     . ALA C 2 57  ? 114.433 117.178 119.764 1.00 32.36 ?  36  ALA C N     1 
ATOM   11292 C  CA    . ALA C 2 57  ? 113.789 118.250 120.529 1.00 32.17 ?  36  ALA C CA    1 
ATOM   11293 C  C     . ALA C 2 57  ? 112.280 118.251 120.257 1.00 31.76 ?  36  ALA C C     1 
ATOM   11294 O  O     . ALA C 2 57  ? 111.852 118.198 119.103 1.00 31.95 ?  36  ALA C O     1 
ATOM   11295 C  CB    . ALA C 2 57  ? 114.400 119.596 120.174 1.00 33.01 ?  36  ALA C CB    1 
ATOM   11296 N  N     . LEU C 2 58  ? 111.479 118.314 121.316 1.00 30.68 ?  37  LEU C N     1 
ATOM   11297 C  CA    . LEU C 2 58  ? 110.043 118.074 121.187 1.00 30.14 ?  37  LEU C CA    1 
ATOM   11298 C  C     . LEU C 2 58  ? 109.170 119.323 121.252 1.00 30.21 ?  37  LEU C C     1 
ATOM   11299 O  O     . LEU C 2 58  ? 107.975 119.263 120.933 1.00 29.91 ?  37  LEU C O     1 
ATOM   11300 C  CB    . LEU C 2 58  ? 109.580 117.041 122.221 1.00 29.46 ?  37  LEU C CB    1 
ATOM   11301 C  CG    . LEU C 2 58  ? 110.111 115.615 122.018 1.00 29.08 ?  37  LEU C CG    1 
ATOM   11302 C  CD1   . LEU C 2 58  ? 109.739 114.728 123.192 1.00 29.23 ?  37  LEU C CD1   1 
ATOM   11303 C  CD2   . LEU C 2 58  ? 109.600 115.009 120.711 1.00 28.84 ?  37  LEU C CD2   1 
ATOM   11304 N  N     . ASN C 2 59  ? 109.767 120.446 121.639 1.00 30.50 ?  38  ASN C N     1 
ATOM   11305 C  CA    . ASN C 2 59  ? 109.023 121.700 121.791 1.00 31.23 ?  38  ASN C CA    1 
ATOM   11306 C  C     . ASN C 2 59  ? 108.379 122.208 120.490 1.00 31.03 ?  38  ASN C C     1 
ATOM   11307 O  O     . ASN C 2 59  ? 107.435 122.990 120.529 1.00 30.82 ?  38  ASN C O     1 
ATOM   11308 C  CB    . ASN C 2 59  ? 109.882 122.782 122.472 1.00 31.98 ?  38  ASN C CB    1 
ATOM   11309 C  CG    . ASN C 2 59  ? 111.165 123.089 121.717 1.00 33.59 ?  38  ASN C CG    1 
ATOM   11310 O  OD1   . ASN C 2 59  ? 111.970 122.192 121.437 1.00 36.48 ?  38  ASN C OD1   1 
ATOM   11311 N  ND2   . ASN C 2 59  ? 111.371 124.363 121.394 1.00 34.77 ?  38  ASN C ND2   1 
ATOM   11312 N  N     . GLY C 2 60  ? 108.875 121.727 119.352 1.00 30.88 ?  39  GLY C N     1 
ATOM   11313 C  CA    . GLY C 2 60  ? 108.279 122.016 118.042 1.00 31.37 ?  39  GLY C CA    1 
ATOM   11314 C  C     . GLY C 2 60  ? 106.877 121.459 117.819 1.00 31.05 ?  39  GLY C C     1 
ATOM   11315 O  O     . GLY C 2 60  ? 106.123 122.015 117.033 1.00 31.21 ?  39  GLY C O     1 
ATOM   11316 N  N     . ASP C 2 61  ? 106.523 120.373 118.512 1.00 30.63 ?  40  ASP C N     1 
ATOM   11317 C  CA    . ASP C 2 61  ? 105.155 119.823 118.469 1.00 30.65 ?  40  ASP C CA    1 
ATOM   11318 C  C     . ASP C 2 61  ? 104.127 120.582 119.316 1.00 31.00 ?  40  ASP C C     1 
ATOM   11319 O  O     . ASP C 2 61  ? 102.934 120.289 119.227 1.00 30.91 ?  40  ASP C O     1 
ATOM   11320 C  CB    . ASP C 2 61  ? 105.134 118.359 118.924 1.00 30.00 ?  40  ASP C CB    1 
ATOM   11321 C  CG    . ASP C 2 61  ? 105.851 117.431 117.972 1.00 30.88 ?  40  ASP C CG    1 
ATOM   11322 O  OD1   . ASP C 2 61  ? 106.401 117.899 116.946 1.00 30.42 ?  40  ASP C OD1   1 
ATOM   11323 O  OD2   . ASP C 2 61  ? 105.868 116.217 118.266 1.00 31.17 -1 40  ASP C OD2   1 
ATOM   11324 N  N     . LEU C 2 62  ? 104.580 121.526 120.139 1.00 31.54 ?  41  LEU C N     1 
ATOM   11325 C  CA    . LEU C 2 62  ? 103.703 122.193 121.115 1.00 32.47 ?  41  LEU C CA    1 
ATOM   11326 C  C     . LEU C 2 62  ? 102.450 122.815 120.507 1.00 33.21 ?  41  LEU C C     1 
ATOM   11327 O  O     . LEU C 2 62  ? 101.358 122.704 121.075 1.00 32.84 ?  41  LEU C O     1 
ATOM   11328 C  CB    . LEU C 2 62  ? 104.464 123.248 121.920 1.00 33.14 ?  41  LEU C CB    1 
ATOM   11329 C  CG    . LEU C 2 62  ? 105.241 122.775 123.149 1.00 34.44 ?  41  LEU C CG    1 
ATOM   11330 C  CD1   . LEU C 2 62  ? 106.169 123.880 123.633 1.00 35.04 ?  41  LEU C CD1   1 
ATOM   11331 C  CD2   . LEU C 2 62  ? 104.282 122.333 124.261 1.00 35.52 ?  41  LEU C CD2   1 
ATOM   11332 N  N     . LEU C 2 63  ? 102.611 123.461 119.354 1.00 33.75 ?  42  LEU C N     1 
ATOM   11333 C  CA    . LEU C 2 63  ? 101.488 124.118 118.700 1.00 34.79 ?  42  LEU C CA    1 
ATOM   11334 C  C     . LEU C 2 63  ? 100.520 123.180 117.980 1.00 34.66 ?  42  LEU C C     1 
ATOM   11335 O  O     . LEU C 2 63  ? 99.312  123.326 118.150 1.00 34.67 ?  42  LEU C O     1 
ATOM   11336 C  CB    . LEU C 2 63  ? 101.955 125.247 117.778 1.00 35.27 ?  42  LEU C CB    1 
ATOM   11337 C  CG    . LEU C 2 63  ? 102.235 126.564 118.513 1.00 36.82 ?  42  LEU C CG    1 
ATOM   11338 C  CD1   . LEU C 2 63  ? 102.733 127.609 117.522 1.00 37.93 ?  42  LEU C CD1   1 
ATOM   11339 C  CD2   . LEU C 2 63  ? 101.001 127.085 119.248 1.00 37.85 ?  42  LEU C CD2   1 
ATOM   11340 N  N     . THR C 2 64  ? 101.025 122.230 117.188 1.00 34.70 ?  43  THR C N     1 
ATOM   11341 C  CA    . THR C 2 64  ? 100.120 121.268 116.536 1.00 35.10 ?  43  THR C CA    1 
ATOM   11342 C  C     . THR C 2 64  ? 99.368  120.402 117.560 1.00 34.78 ?  43  THR C C     1 
ATOM   11343 O  O     . THR C 2 64  ? 98.269  119.936 117.281 1.00 35.04 ?  43  THR C O     1 
ATOM   11344 C  CB    . THR C 2 64  ? 100.793 120.394 115.431 1.00 35.30 ?  43  THR C CB    1 
ATOM   11345 O  OG1   . THR C 2 64  ? 101.931 119.696 115.958 1.00 36.01 ?  43  THR C OG1   1 
ATOM   11346 C  CG2   . THR C 2 64  ? 101.215 121.251 114.238 1.00 35.96 ?  43  THR C CG2   1 
ATOM   11347 N  N     . TRP C 2 65  ? 99.947  120.223 118.749 1.00 34.63 ?  44  TRP C N     1 
ATOM   11348 C  CA    . TRP C 2 65  ? 99.279  119.506 119.844 1.00 34.37 ?  44  TRP C CA    1 
ATOM   11349 C  C     . TRP C 2 65  ? 98.147  120.341 120.442 1.00 35.13 ?  44  TRP C C     1 
ATOM   11350 O  O     . TRP C 2 65  ? 97.017  119.861 120.604 1.00 34.98 ?  44  TRP C O     1 
ATOM   11351 C  CB    . TRP C 2 65  ? 100.283 119.136 120.934 1.00 33.95 ?  44  TRP C CB    1 
ATOM   11352 C  CG    . TRP C 2 65  ? 99.656  118.594 122.178 1.00 33.26 ?  44  TRP C CG    1 
ATOM   11353 C  CD1   . TRP C 2 65  ? 99.472  119.254 123.362 1.00 32.51 ?  44  TRP C CD1   1 
ATOM   11354 C  CD2   . TRP C 2 65  ? 99.132  117.272 122.368 1.00 30.93 ?  44  TRP C CD2   1 
ATOM   11355 N  NE1   . TRP C 2 65  ? 98.870  118.421 124.280 1.00 31.66 ?  44  TRP C NE1   1 
ATOM   11356 C  CE2   . TRP C 2 65  ? 98.649  117.200 123.696 1.00 30.39 ?  44  TRP C CE2   1 
ATOM   11357 C  CE3   . TRP C 2 65  ? 99.029  116.141 121.546 1.00 30.36 ?  44  TRP C CE3   1 
ATOM   11358 C  CZ2   . TRP C 2 65  ? 98.063  116.045 124.218 1.00 29.16 ?  44  TRP C CZ2   1 
ATOM   11359 C  CZ3   . TRP C 2 65  ? 98.447  114.985 122.068 1.00 28.84 ?  44  TRP C CZ3   1 
ATOM   11360 C  CH2   . TRP C 2 65  ? 97.978  114.947 123.393 1.00 29.34 ?  44  TRP C CH2   1 
ATOM   11361 N  N     . LYS C 2 66  ? 98.474  121.586 120.783 1.00 35.69 ?  45  LYS C N     1 
ATOM   11362 C  CA    . LYS C 2 66  ? 97.509  122.550 121.290 1.00 36.38 ?  45  LYS C CA    1 
ATOM   11363 C  C     . LYS C 2 66  ? 96.260  122.641 120.406 1.00 36.24 ?  45  LYS C C     1 
ATOM   11364 O  O     . LYS C 2 66  ? 95.165  122.841 120.917 1.00 36.78 ?  45  LYS C O     1 
ATOM   11365 C  CB    . LYS C 2 66  ? 98.182  123.920 121.392 1.00 37.14 ?  45  LYS C CB    1 
ATOM   11366 C  CG    . LYS C 2 66  ? 97.318  125.035 121.954 1.00 38.91 ?  45  LYS C CG    1 
ATOM   11367 C  CD    . LYS C 2 66  ? 98.007  126.387 121.769 1.00 41.12 ?  45  LYS C CD    1 
ATOM   11368 C  CE    . LYS C 2 66  ? 97.345  127.462 122.616 1.00 43.00 ?  45  LYS C CE    1 
ATOM   11369 N  NZ    . LYS C 2 66  ? 97.170  127.013 124.031 1.00 44.38 1  45  LYS C NZ    1 
ATOM   11370 N  N     . TYR C 2 67  ? 96.443  122.451 119.095 1.00 36.03 ?  46  TYR C N     1 
ATOM   11371 C  CA    . TYR C 2 67  ? 95.397  122.637 118.076 1.00 36.03 ?  46  TYR C CA    1 
ATOM   11372 C  C     . TYR C 2 67  ? 94.468  121.435 117.861 1.00 35.25 ?  46  TYR C C     1 
ATOM   11373 O  O     . TYR C 2 67  ? 93.441  121.550 117.184 1.00 35.32 ?  46  TYR C O     1 
ATOM   11374 C  CB    . TYR C 2 67  ? 96.028  123.005 116.721 1.00 36.60 ?  46  TYR C CB    1 
ATOM   11375 C  CG    . TYR C 2 67  ? 96.812  124.311 116.691 1.00 37.85 ?  46  TYR C CG    1 
ATOM   11376 C  CD1   . TYR C 2 67  ? 96.693  125.248 117.717 1.00 38.97 ?  46  TYR C CD1   1 
ATOM   11377 C  CD2   . TYR C 2 67  ? 97.664  124.611 115.618 1.00 40.06 ?  46  TYR C CD2   1 
ATOM   11378 C  CE1   . TYR C 2 67  ? 97.414  126.440 117.698 1.00 40.36 ?  46  TYR C CE1   1 
ATOM   11379 C  CE2   . TYR C 2 67  ? 98.391  125.811 115.586 1.00 40.53 ?  46  TYR C CE2   1 
ATOM   11380 C  CZ    . TYR C 2 67  ? 98.255  126.721 116.634 1.00 41.43 ?  46  TYR C CZ    1 
ATOM   11381 O  OH    . TYR C 2 67  ? 98.949  127.918 116.630 1.00 41.48 ?  46  TYR C OH    1 
ATOM   11382 N  N     . LEU C 2 68  ? 94.838  120.282 118.412 1.00 33.80 ?  47  LEU C N     1 
ATOM   11383 C  CA    . LEU C 2 68  ? 94.012  119.086 118.289 1.00 32.77 ?  47  LEU C CA    1 
ATOM   11384 C  C     . LEU C 2 68  ? 92.796  119.189 119.199 1.00 31.84 ?  47  LEU C C     1 
ATOM   11385 O  O     . LEU C 2 68  ? 92.858  119.812 120.256 1.00 31.90 ?  47  LEU C O     1 
ATOM   11386 C  CB    . LEU C 2 68  ? 94.812  117.833 118.651 1.00 32.39 ?  47  LEU C CB    1 
ATOM   11387 C  CG    . LEU C 2 68  ? 96.015  117.385 117.819 1.00 32.68 ?  47  LEU C CG    1 
ATOM   11388 C  CD1   . LEU C 2 68  ? 96.608  116.121 118.432 1.00 33.03 ?  47  LEU C CD1   1 
ATOM   11389 C  CD2   . LEU C 2 68  ? 95.658  117.153 116.347 1.00 32.78 ?  47  LEU C CD2   1 
ATOM   11390 N  N     . GLY C 2 69  ? 91.698  118.560 118.795 1.00 30.99 ?  48  GLY C N     1 
ATOM   11391 C  CA    . GLY C 2 69  ? 90.518  118.461 119.653 1.00 30.58 ?  48  GLY C CA    1 
ATOM   11392 C  C     . GLY C 2 69  ? 90.780  117.641 120.910 1.00 29.87 ?  48  GLY C C     1 
ATOM   11393 O  O     . GLY C 2 69  ? 91.741  116.876 120.971 1.00 28.79 ?  48  GLY C O     1 
ATOM   11394 N  N     . LYS C 2 70  ? 89.931  117.810 121.918 1.00 29.89 ?  49  LYS C N     1 
ATOM   11395 C  CA    . LYS C 2 70  ? 90.068  117.057 123.164 1.00 29.49 ?  49  LYS C CA    1 
ATOM   11396 C  C     . LYS C 2 70  ? 90.002  115.536 122.931 1.00 28.74 ?  49  LYS C C     1 
ATOM   11397 O  O     . LYS C 2 70  ? 90.762  114.780 123.551 1.00 27.27 ?  49  LYS C O     1 
ATOM   11398 C  CB    . LYS C 2 70  ? 89.042  117.524 124.201 1.00 30.67 ?  49  LYS C CB    1 
ATOM   11399 C  CG    . LYS C 2 70  ? 89.453  118.840 124.907 1.00 33.73 ?  49  LYS C CG    1 
ATOM   11400 C  CD    . LYS C 2 70  ? 88.282  119.532 125.626 1.00 38.93 ?  49  LYS C CD    1 
ATOM   11401 C  CE    . LYS C 2 70  ? 87.936  118.893 126.978 1.00 41.04 ?  49  LYS C CE    1 
ATOM   11402 N  NZ    . LYS C 2 70  ? 88.947  119.168 128.042 1.00 42.21 1  49  LYS C NZ    1 
ATOM   11403 N  N     . ASN C 2 71  ? 89.112  115.111 122.029 1.00 27.54 ?  50  ASN C N     1 
ATOM   11404 C  CA    . ASN C 2 71  ? 89.005  113.705 121.632 1.00 27.00 ?  50  ASN C CA    1 
ATOM   11405 C  C     . ASN C 2 71  ? 90.305  113.161 121.038 1.00 26.19 ?  50  ASN C C     1 
ATOM   11406 O  O     . ASN C 2 71  ? 90.726  112.028 121.351 1.00 25.38 ?  50  ASN C O     1 
ATOM   11407 C  CB    . ASN C 2 71  ? 87.839  113.492 120.640 1.00 27.08 ?  50  ASN C CB    1 
ATOM   11408 C  CG    . ASN C 2 71  ? 87.984  114.308 119.333 1.00 28.69 ?  50  ASN C CG    1 
ATOM   11409 O  OD1   . ASN C 2 71  ? 88.340  115.502 119.340 1.00 30.45 ?  50  ASN C OD1   1 
ATOM   11410 N  ND2   . ASN C 2 71  ? 87.674  113.658 118.200 1.00 29.42 ?  50  ASN C ND2   1 
ATOM   11411 N  N     . GLU C 2 72  ? 90.932  113.971 120.187 1.00 24.91 ?  51  GLU C N     1 
ATOM   11412 C  CA    . GLU C 2 72  ? 92.166  113.581 119.517 1.00 24.97 ?  51  GLU C CA    1 
ATOM   11413 C  C     . GLU C 2 72  ? 93.326  113.450 120.510 1.00 24.45 ?  51  GLU C C     1 
ATOM   11414 O  O     . GLU C 2 72  ? 94.091  112.474 120.462 1.00 23.90 ?  51  GLU C O     1 
ATOM   11415 C  CB    . GLU C 2 72  ? 92.510  114.579 118.410 1.00 25.27 ?  51  GLU C CB    1 
ATOM   11416 C  CG    . GLU C 2 72  ? 91.511  114.595 117.254 1.00 26.16 ?  51  GLU C CG    1 
ATOM   11417 C  CD    . GLU C 2 72  ? 91.870  115.640 116.206 1.00 28.70 ?  51  GLU C CD    1 
ATOM   11418 O  OE1   . GLU C 2 72  ? 91.623  116.838 116.453 1.00 28.70 ?  51  GLU C OE1   1 
ATOM   11419 O  OE2   . GLU C 2 72  ? 92.397  115.264 115.136 1.00 28.92 -1 51  GLU C OE2   1 
ATOM   11420 N  N     . GLN C 2 73  ? 93.433  114.421 121.416 1.00 23.75 ?  52  GLN C N     1 
ATOM   11421 C  CA    . GLN C 2 73  ? 94.473  114.402 122.442 1.00 23.94 ?  52  GLN C CA    1 
ATOM   11422 C  C     . GLN C 2 73  ? 94.297  113.207 123.381 1.00 23.36 ?  52  GLN C C     1 
ATOM   11423 O  O     . GLN C 2 73  ? 95.276  112.589 123.783 1.00 22.95 ?  52  GLN C O     1 
ATOM   11424 C  CB    . GLN C 2 73  ? 94.465  115.702 123.260 1.00 24.28 ?  52  GLN C CB    1 
ATOM   11425 C  CG    . GLN C 2 73  ? 95.005  116.946 122.527 1.00 25.22 ?  52  GLN C CG    1 
ATOM   11426 C  CD    . GLN C 2 73  ? 95.064  118.191 123.420 1.00 29.02 ?  52  GLN C CD    1 
ATOM   11427 O  OE1   . GLN C 2 73  ? 94.693  118.148 124.591 1.00 32.08 ?  52  GLN C OE1   1 
ATOM   11428 N  NE2   . GLN C 2 73  ? 95.534  119.300 122.862 1.00 29.13 ?  52  GLN C NE2   1 
ATOM   11429 N  N     . ASP C 2 74  ? 93.047  112.916 123.745 1.00 23.02 ?  53  ASP C N     1 
ATOM   11430 C  CA    . ASP C 2 74  ? 92.729  111.799 124.624 1.00 23.44 ?  53  ASP C CA    1 
ATOM   11431 C  C     . ASP C 2 74  ? 93.167  110.471 123.992 1.00 23.00 ?  53  ASP C C     1 
ATOM   11432 O  O     . ASP C 2 74  ? 93.838  109.671 124.636 1.00 22.96 ?  53  ASP C O     1 
ATOM   11433 C  CB    . ASP C 2 74  ? 91.226  111.762 124.933 1.00 23.31 ?  53  ASP C CB    1 
ATOM   11434 C  CG    . ASP C 2 74  ? 90.869  110.726 125.979 1.00 25.80 ?  53  ASP C CG    1 
ATOM   11435 O  OD1   . ASP C 2 74  ? 91.369  110.823 127.129 1.00 27.95 ?  53  ASP C OD1   1 
ATOM   11436 O  OD2   . ASP C 2 74  ? 90.079  109.818 125.653 1.00 26.30 -1 53  ASP C OD2   1 
ATOM   11437 N  N     . THR C 2 75  ? 92.769  110.249 122.741 1.00 22.20 ?  54  THR C N     1 
ATOM   11438 C  CA    . THR C 2 75  ? 93.133  109.038 122.019 1.00 21.84 ?  54  THR C CA    1 
ATOM   11439 C  C     . THR C 2 75  ? 94.649  108.931 121.887 1.00 22.09 ?  54  THR C C     1 
ATOM   11440 O  O     . THR C 2 75  ? 95.217  107.870 122.122 1.00 21.88 ?  54  THR C O     1 
ATOM   11441 C  CB    . THR C 2 75  ? 92.441  108.958 120.629 1.00 21.74 ?  54  THR C CB    1 
ATOM   11442 O  OG1   . THR C 2 75  ? 91.032  108.834 120.827 1.00 22.09 ?  54  THR C OG1   1 
ATOM   11443 C  CG2   . THR C 2 75  ? 92.918  107.730 119.842 1.00 19.76 ?  54  THR C CG2   1 
ATOM   11444 N  N     . TYR C 2 76  ? 95.296  110.036 121.528 1.00 22.38 ?  55  TYR C N     1 
ATOM   11445 C  CA    . TYR C 2 76  ? 96.751  110.055 121.393 1.00 22.85 ?  55  TYR C CA    1 
ATOM   11446 C  C     . TYR C 2 76  ? 97.479  109.657 122.689 1.00 22.56 ?  55  TYR C C     1 
ATOM   11447 O  O     . TYR C 2 76  ? 98.386  108.830 122.646 1.00 21.97 ?  55  TYR C O     1 
ATOM   11448 C  CB    . TYR C 2 76  ? 97.219  111.424 120.918 1.00 23.57 ?  55  TYR C CB    1 
ATOM   11449 C  CG    . TYR C 2 76  ? 98.629  111.462 120.368 1.00 25.59 ?  55  TYR C CG    1 
ATOM   11450 C  CD1   . TYR C 2 76  ? 98.873  111.276 119.003 1.00 27.49 ?  55  TYR C CD1   1 
ATOM   11451 C  CD2   . TYR C 2 76  ? 99.716  111.719 121.204 1.00 27.70 ?  55  TYR C CD2   1 
ATOM   11452 C  CE1   . TYR C 2 76  ? 100.174 111.336 118.488 1.00 30.28 ?  55  TYR C CE1   1 
ATOM   11453 C  CE2   . TYR C 2 76  ? 101.023 111.775 120.701 1.00 30.38 ?  55  TYR C CE2   1 
ATOM   11454 C  CZ    . TYR C 2 76  ? 101.242 111.581 119.343 1.00 31.39 ?  55  TYR C CZ    1 
ATOM   11455 O  OH    . TYR C 2 76  ? 102.529 111.650 118.844 1.00 32.67 ?  55  TYR C OH    1 
ATOM   11456 N  N     . MET C 2 77  ? 97.087  110.248 123.820 1.00 23.14 ?  56  MET C N     1 
ATOM   11457 C  CA    . MET C 2 77  ? 97.702  109.938 125.125 1.00 23.90 ?  56  MET C CA    1 
ATOM   11458 C  C     . MET C 2 77  ? 97.540  108.462 125.463 1.00 23.24 ?  56  MET C C     1 
ATOM   11459 O  O     . MET C 2 77  ? 98.469  107.807 125.951 1.00 22.47 ?  56  MET C O     1 
ATOM   11460 C  CB    . MET C 2 77  ? 97.056  110.754 126.251 1.00 24.38 ?  56  MET C CB    1 
ATOM   11461 C  CG    . MET C 2 77  ? 97.251  112.261 126.184 1.00 28.52 ?  56  MET C CG    1 
ATOM   11462 S  SD    . MET C 2 77  ? 98.896  112.771 126.667 1.00 34.32 ?  56  MET C SD    1 
ATOM   11463 C  CE    . MET C 2 77  ? 98.925  112.318 128.405 1.00 33.84 ?  56  MET C CE    1 
ATOM   11464 N  N     . LYS C 2 78  ? 96.339  107.950 125.209 1.00 23.25 ?  57  LYS C N     1 
ATOM   11465 C  CA    . LYS C 2 78  ? 95.986  106.597 125.619 1.00 22.98 ?  57  LYS C CA    1 
ATOM   11466 C  C     . LYS C 2 78  ? 96.728  105.583 124.762 1.00 22.77 ?  57  LYS C C     1 
ATOM   11467 O  O     . LYS C 2 78  ? 97.258  104.601 125.274 1.00 22.56 ?  57  LYS C O     1 
ATOM   11468 C  CB    . LYS C 2 78  ? 94.465  106.406 125.579 1.00 22.99 ?  57  LYS C CB    1 
ATOM   11469 C  CG    . LYS C 2 78  ? 93.758  107.074 126.761 1.00 24.86 ?  57  LYS C CG    1 
ATOM   11470 C  CD    . LYS C 2 78  ? 92.235  107.052 126.623 1.00 27.37 ?  57  LYS C CD    1 
ATOM   11471 C  CE    . LYS C 2 78  ? 91.560  107.501 127.924 1.00 28.99 ?  57  LYS C CE    1 
ATOM   11472 N  NZ    . LYS C 2 78  ? 90.092  107.663 127.704 1.00 29.82 1  57  LYS C NZ    1 
ATOM   11473 N  N     . VAL C 2 79  ? 96.774  105.856 123.459 1.00 22.70 ?  58  VAL C N     1 
ATOM   11474 C  CA    . VAL C 2 79  ? 97.523  105.071 122.481 1.00 23.48 ?  58  VAL C CA    1 
ATOM   11475 C  C     . VAL C 2 79  ? 99.004  104.908 122.901 1.00 23.04 ?  58  VAL C C     1 
ATOM   11476 O  O     . VAL C 2 79  ? 99.525  103.776 122.968 1.00 22.83 ?  58  VAL C O     1 
ATOM   11477 C  CB    . VAL C 2 79  ? 97.330  105.721 121.075 1.00 24.24 ?  58  VAL C CB    1 
ATOM   11478 C  CG1   . VAL C 2 79  ? 98.572  105.648 120.205 1.00 25.71 ?  58  VAL C CG1   1 
ATOM   11479 C  CG2   . VAL C 2 79  ? 96.077  105.136 120.385 1.00 25.04 ?  58  VAL C CG2   1 
ATOM   11480 N  N     . LEU C 2 80  ? 99.657  106.018 123.232 1.00 22.84 ?  59  LEU C N     1 
ATOM   11481 C  CA    . LEU C 2 80  ? 101.061 105.979 123.646 1.00 23.35 ?  59  LEU C CA    1 
ATOM   11482 C  C     . LEU C 2 80  ? 101.231 105.283 125.001 1.00 22.75 ?  59  LEU C C     1 
ATOM   11483 O  O     . LEU C 2 80  ? 102.235 104.611 125.225 1.00 22.75 ?  59  LEU C O     1 
ATOM   11484 C  CB    . LEU C 2 80  ? 101.688 107.380 123.683 1.00 23.91 ?  59  LEU C CB    1 
ATOM   11485 C  CG    . LEU C 2 80  ? 101.920 108.219 122.411 1.00 26.63 ?  59  LEU C CG    1 
ATOM   11486 C  CD1   . LEU C 2 80  ? 102.930 109.321 122.692 1.00 26.99 ?  59  LEU C CD1   1 
ATOM   11487 C  CD2   . LEU C 2 80  ? 102.385 107.393 121.224 1.00 27.23 ?  59  LEU C CD2   1 
ATOM   11488 N  N     . ALA C 2 81  ? 100.240 105.425 125.884 1.00 22.28 ?  60  ALA C N     1 
ATOM   11489 C  CA    . ALA C 2 81  ? 100.255 104.749 127.185 1.00 22.21 ?  60  ALA C CA    1 
ATOM   11490 C  C     . ALA C 2 81  ? 100.180 103.227 127.026 1.00 22.07 ?  60  ALA C C     1 
ATOM   11491 O  O     . ALA C 2 81  ? 100.894 102.506 127.715 1.00 21.97 ?  60  ALA C O     1 
ATOM   11492 C  CB    . ALA C 2 81  ? 99.129  105.281 128.097 1.00 22.38 ?  60  ALA C CB    1 
ATOM   11493 N  N     . GLY C 2 82  ? 99.347  102.760 126.087 1.00 21.67 ?  61  GLY C N     1 
ATOM   11494 C  CA    . GLY C 2 82  ? 99.245  101.346 125.735 1.00 21.74 ?  61  GLY C CA    1 
ATOM   11495 C  C     . GLY C 2 82  ? 100.553 100.804 125.184 1.00 21.79 ?  61  GLY C C     1 
ATOM   11496 O  O     . GLY C 2 82  ? 100.956 99.672  125.491 1.00 21.93 ?  61  GLY C O     1 
ATOM   11497 N  N     . LEU C 2 83  ? 101.226 101.628 124.383 1.00 21.54 ?  62  LEU C N     1 
ATOM   11498 C  CA    . LEU C 2 83  ? 102.551 101.299 123.860 1.00 21.12 ?  62  LEU C CA    1 
ATOM   11499 C  C     . LEU C 2 83  ? 103.577 101.223 124.982 1.00 20.89 ?  62  LEU C C     1 
ATOM   11500 O  O     . LEU C 2 83  ? 104.403 100.309 124.997 1.00 20.84 ?  62  LEU C O     1 
ATOM   11501 C  CB    . LEU C 2 83  ? 103.010 102.319 122.812 1.00 21.23 ?  62  LEU C CB    1 
ATOM   11502 C  CG    . LEU C 2 83  ? 102.248 102.425 121.484 1.00 21.98 ?  62  LEU C CG    1 
ATOM   11503 C  CD1   . LEU C 2 83  ? 102.754 103.604 120.649 1.00 24.12 ?  62  LEU C CD1   1 
ATOM   11504 C  CD2   . LEU C 2 83  ? 102.332 101.145 120.675 1.00 22.03 ?  62  LEU C CD2   1 
ATOM   11505 N  N     . THR C 2 84  ? 103.521 102.184 125.906 1.00 19.93 ?  63  THR C N     1 
ATOM   11506 C  CA    . THR C 2 84  ? 104.439 102.220 127.041 1.00 19.71 ?  63  THR C CA    1 
ATOM   11507 C  C     . THR C 2 84  ? 104.341 100.941 127.856 1.00 19.63 ?  63  THR C C     1 
ATOM   11508 O  O     . THR C 2 84  ? 105.364 100.394 128.278 1.00 19.62 ?  63  THR C O     1 
ATOM   11509 C  CB    . THR C 2 84  ? 104.170 103.438 127.959 1.00 20.22 ?  63  THR C CB    1 
ATOM   11510 O  OG1   . THR C 2 84  ? 104.128 104.640 127.171 1.00 19.37 ?  63  THR C OG1   1 
ATOM   11511 C  CG2   . THR C 2 84  ? 105.238 103.548 129.021 1.00 19.45 ?  63  THR C CG2   1 
ATOM   11512 N  N     . LEU C 2 85  ? 103.116 100.473 128.080 1.00 19.66 ?  64  LEU C N     1 
ATOM   11513 C  CA    . LEU C 2 85  ? 102.886 99.252  128.847 1.00 20.51 ?  64  LEU C CA    1 
ATOM   11514 C  C     . LEU C 2 85  ? 103.532 98.044  128.161 1.00 20.84 ?  64  LEU C C     1 
ATOM   11515 O  O     . LEU C 2 85  ? 104.272 97.288  128.794 1.00 21.30 ?  64  LEU C O     1 
ATOM   11516 C  CB    . LEU C 2 85  ? 101.387 99.015  129.100 1.00 20.03 ?  64  LEU C CB    1 
ATOM   11517 C  CG    . LEU C 2 85  ? 101.074 97.716  129.878 1.00 21.43 ?  64  LEU C CG    1 
ATOM   11518 C  CD1   . LEU C 2 85  ? 101.616 97.756  131.326 1.00 21.61 ?  64  LEU C CD1   1 
ATOM   11519 C  CD2   . LEU C 2 85  ? 99.584  97.383  129.885 1.00 20.99 ?  64  LEU C CD2   1 
ATOM   11520 N  N     . LEU C 2 86  ? 103.260 97.884  126.871 1.00 21.37 ?  65  LEU C N     1 
ATOM   11521 C  CA    . LEU C 2 86  ? 103.852 96.808  126.072 1.00 21.92 ?  65  LEU C CA    1 
ATOM   11522 C  C     . LEU C 2 86  ? 105.388 96.798  126.128 1.00 21.76 ?  65  LEU C C     1 
ATOM   11523 O  O     . LEU C 2 86  ? 105.989 95.748  126.358 1.00 21.72 ?  65  LEU C O     1 
ATOM   11524 C  CB    . LEU C 2 86  ? 103.375 96.886  124.614 1.00 22.42 ?  65  LEU C CB    1 
ATOM   11525 C  CG    . LEU C 2 86  ? 101.907 96.589  124.241 1.00 24.26 ?  65  LEU C CG    1 
ATOM   11526 C  CD1   . LEU C 2 86  ? 101.685 96.873  122.756 1.00 24.67 ?  65  LEU C CD1   1 
ATOM   11527 C  CD2   . LEU C 2 86  ? 101.525 95.154  124.563 1.00 25.60 ?  65  LEU C CD2   1 
ATOM   11528 N  N     . ASP C 2 87  ? 106.015 97.957  125.916 1.00 21.75 ?  66  ASP C N     1 
ATOM   11529 C  CA    . ASP C 2 87  ? 107.484 98.078  125.998 1.00 21.99 ?  66  ASP C CA    1 
ATOM   11530 C  C     . ASP C 2 87  ? 108.051 97.853  127.404 1.00 21.76 ?  66  ASP C C     1 
ATOM   11531 O  O     . ASP C 2 87  ? 109.162 97.326  127.558 1.00 21.65 ?  66  ASP C O     1 
ATOM   11532 C  CB    . ASP C 2 87  ? 107.950 99.449  125.501 1.00 22.23 ?  66  ASP C CB    1 
ATOM   11533 C  CG    . ASP C 2 87  ? 108.331 99.439  124.047 1.00 24.59 ?  66  ASP C CG    1 
ATOM   11534 O  OD1   . ASP C 2 87  ? 109.002 98.480  123.602 1.00 27.46 ?  66  ASP C OD1   1 
ATOM   11535 O  OD2   . ASP C 2 87  ? 107.964 100.406 123.348 1.00 27.98 -1 66  ASP C OD2   1 
ATOM   11536 N  N     . THR C 2 88  ? 107.305 98.285  128.418 1.00 21.50 ?  67  THR C N     1 
ATOM   11537 C  CA    . THR C 2 88  ? 107.670 98.021  129.805 1.00 21.80 ?  67  THR C CA    1 
ATOM   11538 C  C     . THR C 2 88  ? 107.832 96.507  130.043 1.00 22.04 ?  67  THR C C     1 
ATOM   11539 O  O     . THR C 2 88  ? 108.844 96.063  130.603 1.00 22.21 ?  67  THR C O     1 
ATOM   11540 C  CB    . THR C 2 88  ? 106.644 98.633  130.774 1.00 22.15 ?  67  THR C CB    1 
ATOM   11541 O  OG1   . THR C 2 88  ? 106.594 100.046 130.569 1.00 22.23 ?  67  THR C OG1   1 
ATOM   11542 C  CG2   . THR C 2 88  ? 107.013 98.360  132.236 1.00 21.19 ?  67  THR C CG2   1 
ATOM   11543 N  N     . GLU C 2 89  ? 106.856 95.728  129.587 1.00 21.55 ?  68  GLU C N     1 
ATOM   11544 C  CA    . GLU C 2 89  ? 106.880 94.288  129.809 1.00 21.81 ?  68  GLU C CA    1 
ATOM   11545 C  C     . GLU C 2 89  ? 107.845 93.568  128.853 1.00 21.35 ?  68  GLU C C     1 
ATOM   11546 O  O     . GLU C 2 89  ? 108.489 92.594  129.236 1.00 21.34 ?  68  GLU C O     1 
ATOM   11547 C  CB    . GLU C 2 89  ? 105.462 93.707  129.773 1.00 22.25 ?  68  GLU C CB    1 
ATOM   11548 C  CG    . GLU C 2 89  ? 104.682 93.941  131.099 1.00 24.02 ?  68  GLU C CG    1 
ATOM   11549 C  CD    . GLU C 2 89  ? 105.452 93.460  132.331 1.00 25.78 ?  68  GLU C CD    1 
ATOM   11550 O  OE1   . GLU C 2 89  ? 106.003 92.339  132.305 1.00 26.69 ?  68  GLU C OE1   1 
ATOM   11551 O  OE2   . GLU C 2 89  ? 105.508 94.204  133.338 1.00 28.98 -1 68  GLU C OE2   1 
ATOM   11552 N  N     . GLN C 2 90  ? 107.983 94.083  127.633 1.00 20.82 ?  69  GLN C N     1 
ATOM   11553 C  CA    . GLN C 2 90  ? 108.939 93.533  126.679 1.00 21.28 ?  69  GLN C CA    1 
ATOM   11554 C  C     . GLN C 2 90  ? 110.376 93.724  127.174 1.00 21.24 ?  69  GLN C C     1 
ATOM   11555 O  O     . GLN C 2 90  ? 111.219 92.839  126.996 1.00 20.99 ?  69  GLN C O     1 
ATOM   11556 C  CB    . GLN C 2 90  ? 108.743 94.147  125.281 1.00 21.86 ?  69  GLN C CB    1 
ATOM   11557 C  CG    . GLN C 2 90  ? 109.461 93.377  124.150 1.00 24.29 ?  69  GLN C CG    1 
ATOM   11558 C  CD    . GLN C 2 90  ? 108.834 92.008  123.864 1.00 27.14 ?  69  GLN C CD    1 
ATOM   11559 O  OE1   . GLN C 2 90  ? 108.138 91.441  124.711 1.00 27.13 ?  69  GLN C OE1   1 
ATOM   11560 N  NE2   . GLN C 2 90  ? 109.098 91.468  122.671 1.00 27.69 ?  69  GLN C NE2   1 
ATOM   11561 N  N     . GLY C 2 91  ? 110.634 94.861  127.824 1.00 20.62 ?  70  GLY C N     1 
ATOM   11562 C  CA    . GLY C 2 91  ? 111.959 95.173  128.368 1.00 22.00 ?  70  GLY C CA    1 
ATOM   11563 C  C     . GLY C 2 91  ? 112.241 94.508  129.701 1.00 22.45 ?  70  GLY C C     1 
ATOM   11564 O  O     . GLY C 2 91  ? 113.330 93.975  129.895 1.00 23.53 ?  70  GLY C O     1 
ATOM   11565 N  N     . ASN C 2 92  ? 111.265 94.540  130.611 1.00 22.79 ?  71  ASN C N     1 
ATOM   11566 C  CA    . ASN C 2 92  ? 111.417 93.960  131.955 1.00 23.85 ?  71  ASN C CA    1 
ATOM   11567 C  C     . ASN C 2 92  ? 111.437 92.436  131.938 1.00 24.33 ?  71  ASN C C     1 
ATOM   11568 O  O     . ASN C 2 92  ? 112.143 91.812  132.739 1.00 24.17 ?  71  ASN C O     1 
ATOM   11569 C  CB    . ASN C 2 92  ? 110.271 94.390  132.879 1.00 23.74 ?  71  ASN C CB    1 
ATOM   11570 C  CG    . ASN C 2 92  ? 110.310 95.863  133.249 1.00 24.38 ?  71  ASN C CG    1 
ATOM   11571 O  OD1   . ASN C 2 92  ? 111.176 96.627  132.803 1.00 25.16 ?  71  ASN C OD1   1 
ATOM   11572 N  ND2   . ASN C 2 92  ? 109.355 96.271  134.068 1.00 24.07 ?  71  ASN C ND2   1 
ATOM   11573 N  N     . THR C 2 93  ? 110.665 91.844  131.025 1.00 23.97 ?  72  THR C N     1 
ATOM   11574 C  CA    . THR C 2 93  ? 110.318 90.420  131.132 1.00 24.97 ?  72  THR C CA    1 
ATOM   11575 C  C     . THR C 2 93  ? 110.615 89.644  129.857 1.00 24.52 ?  72  THR C C     1 
ATOM   11576 O  O     . THR C 2 93  ? 111.393 88.698  129.881 1.00 25.39 ?  72  THR C O     1 
ATOM   11577 C  CB    . THR C 2 93  ? 108.825 90.227  131.513 1.00 24.54 ?  72  THR C CB    1 
ATOM   11578 O  OG1   . THR C 2 93  ? 108.531 90.969  132.704 1.00 26.43 ?  72  THR C OG1   1 
ATOM   11579 C  CG2   . THR C 2 93  ? 108.505 88.761  131.757 1.00 26.83 ?  72  THR C CG2   1 
ATOM   11580 N  N     . GLY C 2 94  ? 109.998 90.058  128.760 1.00 24.37 ?  73  GLY C N     1 
ATOM   11581 C  CA    . GLY C 2 94  ? 110.014 89.305  127.496 1.00 24.24 ?  73  GLY C CA    1 
ATOM   11582 C  C     . GLY C 2 94  ? 111.395 89.075  126.920 1.00 24.94 ?  73  GLY C C     1 
ATOM   11583 O  O     . GLY C 2 94  ? 111.826 87.929  126.759 1.00 25.86 ?  73  GLY C O     1 
ATOM   11584 N  N     . MET C 2 95  ? 112.093 90.161  126.607 1.00 24.07 ?  74  MET C N     1 
ATOM   11585 C  CA    . MET C 2 95  ? 113.426 90.034  126.033 1.00 24.35 ?  74  MET C CA    1 
ATOM   11586 C  C     . MET C 2 95  ? 114.473 89.389  126.962 1.00 23.52 ?  74  MET C C     1 
ATOM   11587 O  O     . MET C 2 95  ? 115.212 88.530  126.493 1.00 23.40 ?  74  MET C O     1 
ATOM   11588 C  CB    . MET C 2 95  ? 113.911 91.359  125.444 1.00 24.38 ?  74  MET C CB    1 
ATOM   11589 C  CG    . MET C 2 95  ? 113.176 91.777  124.170 1.00 27.47 ?  74  MET C CG    1 
ATOM   11590 S  SD    . MET C 2 95  ? 113.440 90.569  122.843 1.00 32.54 ?  74  MET C SD    1 
ATOM   11591 C  CE    . MET C 2 95  ? 115.123 90.883  122.446 1.00 34.32 ?  74  MET C CE    1 
ATOM   11592 N  N     . PRO C 2 96  ? 114.537 89.788  128.265 1.00 23.36 ?  75  PRO C N     1 
ATOM   11593 C  CA    . PRO C 2 96  ? 115.472 89.120  129.196 1.00 23.27 ?  75  PRO C CA    1 
ATOM   11594 C  C     . PRO C 2 96  ? 115.228 87.625  129.367 1.00 23.77 ?  75  PRO C C     1 
ATOM   11595 O  O     . PRO C 2 96  ? 116.187 86.856  129.415 1.00 23.46 ?  75  PRO C O     1 
ATOM   11596 C  CB    . PRO C 2 96  ? 115.211 89.825  130.537 1.00 23.55 ?  75  PRO C CB    1 
ATOM   11597 C  CG    . PRO C 2 96  ? 114.704 91.175  130.160 1.00 23.85 ?  75  PRO C CG    1 
ATOM   11598 C  CD    . PRO C 2 96  ? 113.870 90.935  128.912 1.00 22.76 ?  75  PRO C CD    1 
ATOM   11599 N  N     . ILE C 2 97  ? 113.962 87.214  129.480 1.00 23.81 ?  76  ILE C N     1 
ATOM   11600 C  CA    . ILE C 2 97  ? 113.640 85.794  129.641 1.00 24.52 ?  76  ILE C CA    1 
ATOM   11601 C  C     . ILE C 2 97  ? 113.982 84.950  128.394 1.00 23.92 ?  76  ILE C C     1 
ATOM   11602 O  O     . ILE C 2 97  ? 114.532 83.846  128.511 1.00 23.99 ?  76  ILE C O     1 
ATOM   11603 C  CB    . ILE C 2 97  ? 112.177 85.577  130.124 1.00 24.49 ?  76  ILE C CB    1 
ATOM   11604 C  CG1   . ILE C 2 97  ? 112.034 84.220  130.808 1.00 27.08 ?  76  ILE C CG1   1 
ATOM   11605 C  CG2   . ILE C 2 97  ? 111.157 85.714  128.974 1.00 26.06 ?  76  ILE C CG2   1 
ATOM   11606 C  CD1   . ILE C 2 97  ? 110.880 84.175  131.798 1.00 31.37 ?  76  ILE C CD1   1 
ATOM   11607 N  N     . VAL C 2 98  ? 113.689 85.478  127.210 1.00 23.97 ?  77  VAL C N     1 
ATOM   11608 C  CA    . VAL C 2 98  ? 114.099 84.816  125.963 1.00 24.01 ?  77  VAL C CA    1 
ATOM   11609 C  C     . VAL C 2 98  ? 115.640 84.756  125.883 1.00 25.23 ?  77  VAL C C     1 
ATOM   11610 O  O     . VAL C 2 98  ? 116.208 83.712  125.546 1.00 25.77 ?  77  VAL C O     1 
ATOM   11611 C  CB    . VAL C 2 98  ? 113.477 85.501  124.720 1.00 23.98 ?  77  VAL C CB    1 
ATOM   11612 C  CG1   . VAL C 2 98  ? 114.119 84.995  123.430 1.00 23.17 ?  77  VAL C CG1   1 
ATOM   11613 C  CG2   . VAL C 2 98  ? 111.962 85.260  124.696 1.00 22.55 ?  77  VAL C CG2   1 
ATOM   11614 N  N     . ALA C 2 99  ? 116.309 85.851  126.247 1.00 25.42 ?  78  ALA C N     1 
ATOM   11615 C  CA    . ALA C 2 99  ? 117.782 85.863  126.286 1.00 26.72 ?  78  ALA C CA    1 
ATOM   11616 C  C     . ALA C 2 99  ? 118.326 84.744  127.179 1.00 27.46 ?  78  ALA C C     1 
ATOM   11617 O  O     . ALA C 2 99  ? 119.286 84.066  126.813 1.00 28.07 ?  78  ALA C O     1 
ATOM   11618 C  CB    . ALA C 2 99  ? 118.305 87.210  126.748 1.00 26.52 ?  78  ALA C CB    1 
ATOM   11619 N  N     . GLU C 2 100 ? 117.682 84.532  128.325 1.00 28.33 ?  79  GLU C N     1 
ATOM   11620 C  CA    . GLU C 2 100 ? 118.115 83.512  129.285 1.00 29.60 ?  79  GLU C CA    1 
ATOM   11621 C  C     . GLU C 2 100 ? 118.093 82.102  128.689 1.00 29.64 ?  79  GLU C C     1 
ATOM   11622 O  O     . GLU C 2 100 ? 118.974 81.281  128.973 1.00 29.72 ?  79  GLU C O     1 
ATOM   11623 C  CB    . GLU C 2 100 ? 117.263 83.572  130.553 1.00 29.70 ?  79  GLU C CB    1 
ATOM   11624 C  CG    . GLU C 2 100 ? 117.697 82.592  131.643 1.00 33.58 ?  79  GLU C CG    1 
ATOM   11625 C  CD    . GLU C 2 100 ? 116.773 82.568  132.844 1.00 37.83 ?  79  GLU C CD    1 
ATOM   11626 O  OE1   . GLU C 2 100 ? 115.858 83.421  132.946 1.00 40.64 ?  79  GLU C OE1   1 
ATOM   11627 O  OE2   . GLU C 2 100 ? 116.960 81.674  133.697 1.00 41.40 -1 79  GLU C OE2   1 
ATOM   11628 N  N     . HIS C 2 101 ? 117.099 81.828  127.847 1.00 29.43 ?  80  HIS C N     1 
ATOM   11629 C  CA    . HIS C 2 101 ? 116.877 80.475  127.356 1.00 29.74 ?  80  HIS C CA    1 
ATOM   11630 C  C     . HIS C 2 101 ? 117.506 80.166  125.996 1.00 30.18 ?  80  HIS C C     1 
ATOM   11631 O  O     . HIS C 2 101 ? 117.645 79.005  125.631 1.00 30.30 ?  80  HIS C O     1 
ATOM   11632 C  CB    . HIS C 2 101 ? 115.379 80.131  127.404 1.00 29.21 ?  80  HIS C CB    1 
ATOM   11633 C  CG    . HIS C 2 101 ? 114.856 79.977  128.799 1.00 29.60 ?  80  HIS C CG    1 
ATOM   11634 N  ND1   . HIS C 2 101 ? 114.313 81.025  129.513 1.00 30.06 ?  80  HIS C ND1   1 
ATOM   11635 C  CD2   . HIS C 2 101 ? 114.836 78.907  129.628 1.00 29.49 ?  80  HIS C CD2   1 
ATOM   11636 C  CE1   . HIS C 2 101 ? 113.968 80.604  130.718 1.00 29.56 ?  80  HIS C CE1   1 
ATOM   11637 N  NE2   . HIS C 2 101 ? 114.273 79.322  130.812 1.00 30.20 ?  80  HIS C NE2   1 
ATOM   11638 N  N     . VAL C 2 102 ? 117.897 81.205  125.263 1.00 30.70 ?  81  VAL C N     1 
ATOM   11639 C  CA    . VAL C 2 102 ? 118.538 81.044  123.961 1.00 31.47 ?  81  VAL C CA    1 
ATOM   11640 C  C     . VAL C 2 102 ? 120.039 80.838  124.152 1.00 32.45 ?  81  VAL C C     1 
ATOM   11641 O  O     . VAL C 2 102 ? 120.681 81.599  124.887 1.00 32.50 ?  81  VAL C O     1 
ATOM   11642 C  CB    . VAL C 2 102 ? 118.281 82.261  123.033 1.00 31.18 ?  81  VAL C CB    1 
ATOM   11643 C  CG1   . VAL C 2 102 ? 119.125 82.176  121.760 1.00 31.20 ?  81  VAL C CG1   1 
ATOM   11644 C  CG2   . VAL C 2 102 ? 116.806 82.345  122.666 1.00 31.28 ?  81  VAL C CG2   1 
ATOM   11645 N  N     . ASP C 2 103 ? 120.585 79.820  123.483 1.00 33.38 ?  82  ASP C N     1 
ATOM   11646 C  CA    . ASP C 2 103 ? 122.006 79.475  123.591 1.00 34.82 ?  82  ASP C CA    1 
ATOM   11647 C  C     . ASP C 2 103 ? 122.890 80.260  122.629 1.00 34.74 ?  82  ASP C C     1 
ATOM   11648 O  O     . ASP C 2 103 ? 122.509 80.509  121.479 1.00 35.00 ?  82  ASP C O     1 
ATOM   11649 C  CB    . ASP C 2 103 ? 122.217 77.969  123.373 1.00 35.82 ?  82  ASP C CB    1 
ATOM   11650 C  CG    . ASP C 2 103 ? 121.747 77.129  124.557 1.00 38.29 ?  82  ASP C CG    1 
ATOM   11651 O  OD1   . ASP C 2 103 ? 121.829 77.601  125.717 1.00 41.49 ?  82  ASP C OD1   1 
ATOM   11652 O  OD2   . ASP C 2 103 ? 121.296 75.990  124.329 1.00 41.10 -1 82  ASP C OD2   1 
ATOM   11653 N  N     . GLY C 2 104 ? 124.073 80.639  123.112 1.00 34.89 ?  83  GLY C N     1 
ATOM   11654 C  CA    . GLY C 2 104 ? 125.078 81.329  122.296 1.00 35.11 ?  83  GLY C CA    1 
ATOM   11655 C  C     . GLY C 2 104 ? 125.278 82.775  122.704 1.00 34.96 ?  83  GLY C C     1 
ATOM   11656 O  O     . GLY C 2 104 ? 124.325 83.558  122.705 1.00 34.57 ?  83  GLY C O     1 
ATOM   11657 N  N     . HIS C 2 105 ? 126.522 83.131  123.035 1.00 35.02 ?  84  HIS C N     1 
ATOM   11658 C  CA    . HIS C 2 105 ? 126.849 84.465  123.557 1.00 34.83 ?  84  HIS C CA    1 
ATOM   11659 C  C     . HIS C 2 105 ? 126.476 85.611  122.627 1.00 33.77 ?  84  HIS C C     1 
ATOM   11660 O  O     . HIS C 2 105 ? 126.067 86.678  123.090 1.00 33.25 ?  84  HIS C O     1 
ATOM   11661 C  CB    . HIS C 2 105 ? 128.325 84.563  123.962 1.00 36.09 ?  84  HIS C CB    1 
ATOM   11662 C  CG    . HIS C 2 105 ? 128.640 83.862  125.249 1.00 39.17 ?  84  HIS C CG    1 
ATOM   11663 N  ND1   . HIS C 2 105 ? 129.851 83.242  125.484 1.00 43.00 ?  84  HIS C ND1   1 
ATOM   11664 C  CD2   . HIS C 2 105 ? 127.893 83.663  126.363 1.00 41.84 ?  84  HIS C CD2   1 
ATOM   11665 C  CE1   . HIS C 2 105 ? 129.838 82.701  126.691 1.00 43.47 ?  84  HIS C CE1   1 
ATOM   11666 N  NE2   . HIS C 2 105 ? 128.662 82.943  127.245 1.00 43.10 ?  84  HIS C NE2   1 
ATOM   11667 N  N     . GLN C 2 106 ? 126.596 85.390  121.323 1.00 32.84 ?  85  GLN C N     1 
ATOM   11668 C  CA    . GLN C 2 106 ? 126.229 86.425  120.360 1.00 32.29 ?  85  GLN C CA    1 
ATOM   11669 C  C     . GLN C 2 106 ? 124.710 86.602  120.250 1.00 30.88 ?  85  GLN C C     1 
ATOM   11670 O  O     . GLN C 2 106 ? 124.222 87.735  120.165 1.00 30.44 ?  85  GLN C O     1 
ATOM   11671 C  CB    . GLN C 2 106 ? 126.838 86.142  118.996 1.00 32.85 ?  85  GLN C CB    1 
ATOM   11672 C  CG    . GLN C 2 106 ? 128.360 86.215  118.981 1.00 35.55 ?  85  GLN C CG    1 
ATOM   11673 C  CD    . GLN C 2 106 ? 128.933 85.824  117.644 1.00 38.12 ?  85  GLN C CD    1 
ATOM   11674 O  OE1   . GLN C 2 106 ? 128.366 86.141  116.599 1.00 39.96 ?  85  GLN C OE1   1 
ATOM   11675 N  NE2   . GLN C 2 106 ? 130.069 85.130  117.667 1.00 40.39 ?  85  GLN C NE2   1 
ATOM   11676 N  N     . ARG C 2 107 ? 123.974 85.492  120.246 1.00 29.75 ?  86  ARG C N     1 
ATOM   11677 C  CA    . ARG C 2 107 ? 122.507 85.553  120.247 1.00 28.87 ?  86  ARG C CA    1 
ATOM   11678 C  C     . ARG C 2 107 ? 122.028 86.254  121.511 1.00 28.16 ?  86  ARG C C     1 
ATOM   11679 O  O     . ARG C 2 107 ? 121.126 87.089  121.453 1.00 27.55 ?  86  ARG C O     1 
ATOM   11680 C  CB    . ARG C 2 107 ? 121.889 84.160  120.151 1.00 28.48 ?  86  ARG C CB    1 
ATOM   11681 C  CG    . ARG C 2 107 ? 122.042 83.527  118.779 1.00 29.86 ?  86  ARG C CG    1 
ATOM   11682 C  CD    . ARG C 2 107 ? 121.452 82.128  118.720 1.00 30.23 ?  86  ARG C CD    1 
ATOM   11683 N  NE    . ARG C 2 107 ? 121.219 81.771  117.326 1.00 33.04 ?  86  ARG C NE    1 
ATOM   11684 C  CZ    . ARG C 2 107 ? 120.409 80.810  116.915 1.00 31.54 ?  86  ARG C CZ    1 
ATOM   11685 N  NH1   . ARG C 2 107 ? 119.747 80.068  117.790 1.00 31.85 1  86  ARG C NH1   1 
ATOM   11686 N  NH2   . ARG C 2 107 ? 120.274 80.594  115.617 1.00 34.74 ?  86  ARG C NH2   1 
ATOM   11687 N  N     . LYS C 2 108 ? 122.645 85.924  122.644 1.00 27.65 ?  87  LYS C N     1 
ATOM   11688 C  CA    . LYS C 2 108 ? 122.309 86.576  123.914 1.00 27.96 ?  87  LYS C CA    1 
ATOM   11689 C  C     . LYS C 2 108 ? 122.625 88.065  123.914 1.00 27.75 ?  87  LYS C C     1 
ATOM   11690 O  O     . LYS C 2 108 ? 121.873 88.851  124.489 1.00 28.29 ?  87  LYS C O     1 
ATOM   11691 C  CB    . LYS C 2 108 ? 123.000 85.901  125.098 1.00 27.80 ?  87  LYS C CB    1 
ATOM   11692 C  CG    . LYS C 2 108 ? 122.473 84.514  125.402 1.00 29.04 ?  87  LYS C CG    1 
ATOM   11693 C  CD    . LYS C 2 108 ? 123.197 83.937  126.611 1.00 31.15 ?  87  LYS C CD    1 
ATOM   11694 C  CE    . LYS C 2 108 ? 122.855 82.473  126.815 1.00 32.05 ?  87  LYS C CE    1 
ATOM   11695 N  NZ    . LYS C 2 108 ? 121.515 82.326  127.438 1.00 30.88 1  87  LYS C NZ    1 
ATOM   11696 N  N     . ALA C 2 109 ? 123.728 88.452  123.274 1.00 27.69 ?  88  ALA C N     1 
ATOM   11697 C  CA    . ALA C 2 109 ? 124.099 89.870  123.174 1.00 27.46 ?  88  ALA C CA    1 
ATOM   11698 C  C     . ALA C 2 109 ? 123.081 90.691  122.378 1.00 26.87 ?  88  ALA C C     1 
ATOM   11699 O  O     . ALA C 2 109 ? 122.780 91.828  122.739 1.00 26.47 ?  88  ALA C O     1 
ATOM   11700 C  CB    . ALA C 2 109 ? 125.481 90.020  122.571 1.00 27.98 ?  88  ALA C CB    1 
ATOM   11701 N  N     . VAL C 2 110 ? 122.571 90.118  121.290 1.00 25.98 ?  89  VAL C N     1 
ATOM   11702 C  CA    . VAL C 2 110 ? 121.536 90.766  120.481 1.00 25.46 ?  89  VAL C CA    1 
ATOM   11703 C  C     . VAL C 2 110 ? 120.252 90.916  121.302 1.00 24.57 ?  89  VAL C C     1 
ATOM   11704 O  O     . VAL C 2 110 ? 119.684 92.009  121.388 1.00 23.62 ?  89  VAL C O     1 
ATOM   11705 C  CB    . VAL C 2 110 ? 121.266 89.984  119.171 1.00 25.80 ?  89  VAL C CB    1 
ATOM   11706 C  CG1   . VAL C 2 110 ? 120.023 90.517  118.444 1.00 25.44 ?  89  VAL C CG1   1 
ATOM   11707 C  CG2   . VAL C 2 110 ? 122.490 90.041  118.258 1.00 26.23 ?  89  VAL C CG2   1 
ATOM   11708 N  N     . LEU C 2 111 ? 119.823 89.826  121.933 1.00 24.33 ?  90  LEU C N     1 
ATOM   11709 C  CA    . LEU C 2 111 ? 118.601 89.853  122.738 1.00 23.93 ?  90  LEU C CA    1 
ATOM   11710 C  C     . LEU C 2 111 ? 118.696 90.793  123.940 1.00 23.77 ?  90  LEU C C     1 
ATOM   11711 O  O     . LEU C 2 111 ? 117.722 91.470  124.269 1.00 23.04 ?  90  LEU C O     1 
ATOM   11712 C  CB    . LEU C 2 111 ? 118.179 88.445  123.166 1.00 23.73 ?  90  LEU C CB    1 
ATOM   11713 C  CG    . LEU C 2 111 ? 117.805 87.509  122.013 1.00 24.50 ?  90  LEU C CG    1 
ATOM   11714 C  CD1   . LEU C 2 111 ? 117.863 86.055  122.451 1.00 24.02 ?  90  LEU C CD1   1 
ATOM   11715 C  CD2   . LEU C 2 111 ? 116.432 87.852  121.430 1.00 25.38 ?  90  LEU C CD2   1 
ATOM   11716 N  N     . ASN C 2 112 ? 119.861 90.823  124.597 1.00 24.24 ?  91  ASN C N     1 
ATOM   11717 C  CA    . ASN C 2 112 ? 120.113 91.791  125.675 1.00 24.95 ?  91  ASN C CA    1 
ATOM   11718 C  C     . ASN C 2 112 ? 120.056 93.243  125.208 1.00 24.25 ?  91  ASN C C     1 
ATOM   11719 O  O     . ASN C 2 112 ? 119.529 94.102  125.914 1.00 23.99 ?  91  ASN C O     1 
ATOM   11720 C  CB    . ASN C 2 112 ? 121.467 91.541  126.347 1.00 25.81 ?  91  ASN C CB    1 
ATOM   11721 C  CG    . ASN C 2 112 ? 121.383 90.517  127.445 1.00 29.96 ?  91  ASN C CG    1 
ATOM   11722 O  OD1   . ASN C 2 112 ? 121.164 90.864  128.608 1.00 35.44 ?  91  ASN C OD1   1 
ATOM   11723 N  ND2   . ASN C 2 112 ? 121.552 89.242  127.094 1.00 32.37 ?  91  ASN C ND2   1 
ATOM   11724 N  N     . PHE C 2 113 ? 120.632 93.515  124.038 1.00 23.60 ?  92  PHE C N     1 
ATOM   11725 C  CA    . PHE C 2 113 ? 120.572 94.849  123.452 1.00 23.32 ?  92  PHE C CA    1 
ATOM   11726 C  C     . PHE C 2 113 ? 119.124 95.261  123.149 1.00 22.63 ?  92  PHE C C     1 
ATOM   11727 O  O     . PHE C 2 113 ? 118.722 96.384  123.456 1.00 21.94 ?  92  PHE C O     1 
ATOM   11728 C  CB    . PHE C 2 113 ? 121.395 94.932  122.158 1.00 23.27 ?  92  PHE C CB    1 
ATOM   11729 C  CG    . PHE C 2 113 ? 121.570 96.338  121.653 1.00 24.66 ?  92  PHE C CG    1 
ATOM   11730 C  CD1   . PHE C 2 113 ? 122.653 97.117  122.083 1.00 25.72 ?  92  PHE C CD1   1 
ATOM   11731 C  CD2   . PHE C 2 113 ? 120.647 96.896  120.773 1.00 25.36 ?  92  PHE C CD2   1 
ATOM   11732 C  CE1   . PHE C 2 113 ? 122.811 98.428  121.633 1.00 25.92 ?  92  PHE C CE1   1 
ATOM   11733 C  CE2   . PHE C 2 113 ? 120.794 98.212  120.315 1.00 25.82 ?  92  PHE C CE2   1 
ATOM   11734 C  CZ    . PHE C 2 113 ? 121.876 98.980  120.751 1.00 25.80 ?  92  PHE C CZ    1 
ATOM   11735 N  N     . MET C 2 114 ? 118.367 94.354  122.526 1.00 22.03 ?  93  MET C N     1 
ATOM   11736 C  CA    . MET C 2 114 ? 116.944 94.589  122.242 1.00 22.14 ?  93  MET C CA    1 
ATOM   11737 C  C     . MET C 2 114 ? 116.137 94.864  123.523 1.00 21.64 ?  93  MET C C     1 
ATOM   11738 O  O     . MET C 2 114 ? 115.308 95.781  123.547 1.00 21.59 ?  93  MET C O     1 
ATOM   11739 C  CB    . MET C 2 114 ? 116.349 93.415  121.474 1.00 22.46 ?  93  MET C CB    1 
ATOM   11740 C  CG    . MET C 2 114 ? 116.883 93.278  120.056 1.00 23.80 ?  93  MET C CG    1 
ATOM   11741 S  SD    . MET C 2 114 ? 116.300 91.771  119.248 1.00 28.07 ?  93  MET C SD    1 
ATOM   11742 C  CE    . MET C 2 114 ? 116.818 92.125  117.548 1.00 26.42 ?  93  MET C CE    1 
ATOM   11743 N  N     . ALA C 2 115 ? 116.405 94.096  124.584 1.00 20.98 ?  94  ALA C N     1 
ATOM   11744 C  CA    . ALA C 2 115 ? 115.788 94.323  125.905 1.00 20.58 ?  94  ALA C CA    1 
ATOM   11745 C  C     . ALA C 2 115 ? 116.055 95.722  126.456 1.00 21.01 ?  94  ALA C C     1 
ATOM   11746 O  O     . ALA C 2 115 ? 115.151 96.381  127.002 1.00 21.06 ?  94  ALA C O     1 
ATOM   11747 C  CB    . ALA C 2 115 ? 116.268 93.250  126.911 1.00 20.83 ?  94  ALA C CB    1 
ATOM   11748 N  N     . MET C 2 116 ? 117.308 96.163  126.348 1.00 20.36 ?  95  MET C N     1 
ATOM   11749 C  CA    . MET C 2 116 ? 117.685 97.493  126.790 1.00 20.83 ?  95  MET C CA    1 
ATOM   11750 C  C     . MET C 2 116 ? 116.898 98.561  126.014 1.00 20.55 ?  95  MET C C     1 
ATOM   11751 O  O     . MET C 2 116 ? 116.366 99.500  126.603 1.00 20.70 ?  95  MET C O     1 
ATOM   11752 C  CB    . MET C 2 116 ? 119.200 97.683  126.638 1.00 20.64 ?  95  MET C CB    1 
ATOM   11753 C  CG    . MET C 2 116 ? 119.718 99.087  126.951 1.00 21.42 ?  95  MET C CG    1 
ATOM   11754 S  SD    . MET C 2 116 ? 119.472 100.230 125.577 1.00 22.51 ?  95  MET C SD    1 
ATOM   11755 C  CE    . MET C 2 116 ? 120.430 99.448  124.278 1.00 20.66 ?  95  MET C CE    1 
ATOM   11756 N  N     . MET C 2 117 ? 116.809 98.395  124.698 1.00 20.50 ?  96  MET C N     1 
ATOM   11757 C  CA    . MET C 2 117 ? 116.068 99.333  123.866 1.00 21.22 ?  96  MET C CA    1 
ATOM   11758 C  C     . MET C 2 117 ? 114.614 99.452  124.321 1.00 21.11 ?  96  MET C C     1 
ATOM   11759 O  O     . MET C 2 117 ? 114.091 100.565 124.418 1.00 20.71 ?  96  MET C O     1 
ATOM   11760 C  CB    . MET C 2 117 ? 116.153 98.950  122.382 1.00 21.35 ?  96  MET C CB    1 
ATOM   11761 C  CG    . MET C 2 117 ? 117.540 99.202  121.712 1.00 22.54 ?  96  MET C CG    1 
ATOM   11762 S  SD    . MET C 2 117 ? 118.192 100.882 121.855 1.00 24.89 ?  96  MET C SD    1 
ATOM   11763 C  CE    . MET C 2 117 ? 117.172 101.756 120.667 1.00 24.95 ?  96  MET C CE    1 
ATOM   11764 N  N     . GLU C 2 118 ? 113.985 98.315  124.620 1.00 21.18 ?  97  GLU C N     1 
ATOM   11765 C  CA    . GLU C 2 118 ? 112.585 98.282  125.055 1.00 21.99 ?  97  GLU C CA    1 
ATOM   11766 C  C     . GLU C 2 118 ? 112.318 99.189  126.258 1.00 22.10 ?  97  GLU C C     1 
ATOM   11767 O  O     . GLU C 2 118 ? 111.449 100.062 126.199 1.00 22.22 ?  97  GLU C O     1 
ATOM   11768 C  CB    . GLU C 2 118 ? 112.111 96.854  125.373 1.00 22.01 ?  97  GLU C CB    1 
ATOM   11769 C  CG    . GLU C 2 118 ? 112.313 95.790  124.287 1.00 24.38 ?  97  GLU C CG    1 
ATOM   11770 C  CD    . GLU C 2 118 ? 111.600 96.068  122.958 1.00 26.32 ?  97  GLU C CD    1 
ATOM   11771 O  OE1   . GLU C 2 118 ? 111.431 97.233  122.570 1.00 29.86 ?  97  GLU C OE1   1 
ATOM   11772 O  OE2   . GLU C 2 118 ? 111.248 95.100  122.264 1.00 29.19 -1 97  GLU C OE2   1 
ATOM   11773 N  N     . ASN C 2 119 ? 113.057 98.990  127.348 1.00 22.26 ?  98  ASN C N     1 
ATOM   11774 C  CA    . ASN C 2 119 ? 112.751 99.731  128.572 1.00 21.91 ?  98  ASN C CA    1 
ATOM   11775 C  C     . ASN C 2 119 ? 113.602 100.976 128.861 1.00 22.41 ?  98  ASN C C     1 
ATOM   11776 O  O     . ASN C 2 119 ? 113.125 101.911 129.502 1.00 23.07 ?  98  ASN C O     1 
ATOM   11777 C  CB    . ASN C 2 119 ? 112.569 98.806  129.795 1.00 21.93 ?  98  ASN C CB    1 
ATOM   11778 C  CG    . ASN C 2 119 ? 113.821 98.041  130.165 1.00 21.31 ?  98  ASN C CG    1 
ATOM   11779 O  OD1   . ASN C 2 119 ? 114.858 98.143  129.506 1.00 21.88 ?  98  ASN C OD1   1 
ATOM   11780 N  ND2   . ASN C 2 119 ? 113.733 97.268  131.246 1.00 21.73 ?  98  ASN C ND2   1 
ATOM   11781 N  N     . ALA C 2 120 ? 114.852 100.981 128.405 1.00 22.75 ?  99  ALA C N     1 
ATOM   11782 C  CA    . ALA C 2 120 ? 115.737 102.128 128.607 1.00 23.12 ?  99  ALA C CA    1 
ATOM   11783 C  C     . ALA C 2 120 ? 115.587 103.186 127.532 1.00 23.60 ?  99  ALA C C     1 
ATOM   11784 O  O     . ALA C 2 120 ? 115.906 104.353 127.778 1.00 24.14 ?  99  ALA C O     1 
ATOM   11785 C  CB    . ALA C 2 120 ? 117.210 101.689 128.736 1.00 23.28 ?  99  ALA C CB    1 
ATOM   11786 N  N     . VAL C 2 121 ? 115.101 102.795 126.349 1.00 23.23 ?  100 VAL C N     1 
ATOM   11787 C  CA    . VAL C 2 121 ? 114.933 103.767 125.252 1.00 23.74 ?  100 VAL C CA    1 
ATOM   11788 C  C     . VAL C 2 121 ? 113.476 103.989 124.844 1.00 23.62 ?  100 VAL C C     1 
ATOM   11789 O  O     . VAL C 2 121 ? 112.993 105.115 124.906 1.00 24.51 ?  100 VAL C O     1 
ATOM   11790 C  CB    . VAL C 2 121 ? 115.793 103.419 124.017 1.00 23.19 ?  100 VAL C CB    1 
ATOM   11791 C  CG1   . VAL C 2 121 ? 115.550 104.427 122.879 1.00 24.10 ?  100 VAL C CG1   1 
ATOM   11792 C  CG2   . VAL C 2 121 ? 117.281 103.387 124.400 1.00 23.48 ?  100 VAL C CG2   1 
ATOM   11793 N  N     . HIS C 2 122 ? 112.788 102.922 124.442 1.00 23.45 ?  101 HIS C N     1 
ATOM   11794 C  CA    . HIS C 2 122 ? 111.422 103.036 123.926 1.00 23.81 ?  101 HIS C CA    1 
ATOM   11795 C  C     . HIS C 2 122 ? 110.420 103.479 124.971 1.00 24.33 ?  101 HIS C C     1 
ATOM   11796 O  O     . HIS C 2 122 ? 109.736 104.488 124.774 1.00 24.80 ?  101 HIS C O     1 
ATOM   11797 C  CB    . HIS C 2 122 ? 110.938 101.730 123.303 1.00 23.30 ?  101 HIS C CB    1 
ATOM   11798 C  CG    . HIS C 2 122 ? 111.736 101.289 122.118 1.00 22.96 ?  101 HIS C CG    1 
ATOM   11799 N  ND1   . HIS C 2 122 ? 111.534 100.072 121.500 1.00 22.78 ?  101 HIS C ND1   1 
ATOM   11800 C  CD2   . HIS C 2 122 ? 112.759 101.884 121.460 1.00 23.25 ?  101 HIS C CD2   1 
ATOM   11801 C  CE1   . HIS C 2 122 ? 112.388 99.946  120.502 1.00 22.57 ?  101 HIS C CE1   1 
ATOM   11802 N  NE2   . HIS C 2 122 ? 113.141 101.029 120.455 1.00 21.75 ?  101 HIS C NE2   1 
ATOM   11803 N  N     . ALA C 2 123 ? 110.308 102.713 126.060 1.00 24.40 ?  102 ALA C N     1 
ATOM   11804 C  CA    . ALA C 2 123 ? 109.337 103.025 127.111 1.00 24.00 ?  102 ALA C CA    1 
ATOM   11805 C  C     . ALA C 2 123 ? 109.571 104.435 127.656 1.00 24.05 ?  102 ALA C C     1 
ATOM   11806 O  O     . ALA C 2 123 ? 108.617 105.168 127.905 1.00 23.89 ?  102 ALA C O     1 
ATOM   11807 C  CB    . ALA C 2 123 ? 109.383 101.985 128.229 1.00 23.73 ?  102 ALA C CB    1 
ATOM   11808 N  N     . LYS C 2 124 ? 110.839 104.813 127.817 1.00 24.36 ?  103 LYS C N     1 
ATOM   11809 C  CA    . LYS C 2 124 ? 111.197 106.141 128.330 1.00 24.31 ?  103 LYS C CA    1 
ATOM   11810 C  C     . LYS C 2 124 ? 110.846 107.295 127.383 1.00 23.84 ?  103 LYS C C     1 
ATOM   11811 O  O     . LYS C 2 124 ? 110.401 108.356 127.840 1.00 24.21 ?  103 LYS C O     1 
ATOM   11812 C  CB    . LYS C 2 124 ? 112.667 106.208 128.755 1.00 24.93 ?  103 LYS C CB    1 
ATOM   11813 C  CG    . LYS C 2 124 ? 113.017 107.505 129.500 1.00 26.37 ?  103 LYS C CG    1 
ATOM   11814 C  CD    . LYS C 2 124 ? 114.425 107.477 130.072 1.00 29.42 ?  103 LYS C CD    1 
ATOM   11815 C  CE    . LYS C 2 124 ? 114.802 108.843 130.654 1.00 31.51 ?  103 LYS C CE    1 
ATOM   11816 N  NZ    . LYS C 2 124 ? 114.877 109.904 129.605 1.00 32.37 1  103 LYS C NZ    1 
ATOM   11817 N  N     . SER C 2 125 ? 111.030 107.087 126.077 1.00 23.52 ?  104 SER C N     1 
ATOM   11818 C  CA    . SER C 2 125 ? 110.690 108.091 125.063 0.50 23.23 ?  104 SER C CA    1 
ATOM   11819 C  C     . SER C 2 125 ? 109.241 108.565 125.183 1.00 22.91 ?  104 SER C C     1 
ATOM   11820 O  O     . SER C 2 125 ? 108.940 109.727 124.946 1.00 22.33 ?  104 SER C O     1 
ATOM   11821 C  CB    . SER C 2 125 ? 110.925 107.541 123.651 0.50 23.25 ?  104 SER C CB    1 
ATOM   11822 O  OG    . SER C 2 125 ? 112.277 107.170 123.456 0.50 24.57 ?  104 SER C OG    1 
ATOM   11823 N  N     . TYR C 2 126 ? 108.336 107.655 125.536 1.00 22.72 ?  105 TYR C N     1 
ATOM   11824 C  CA    . TYR C 2 126 ? 106.931 108.038 125.673 1.00 23.34 ?  105 TYR C CA    1 
ATOM   11825 C  C     . TYR C 2 126 ? 106.734 109.037 126.788 1.00 23.32 ?  105 TYR C C     1 
ATOM   11826 O  O     . TYR C 2 126 ? 105.903 109.924 126.661 1.00 23.17 ?  105 TYR C O     1 
ATOM   11827 C  CB    . TYR C 2 126 ? 106.006 106.839 125.889 1.00 23.45 ?  105 TYR C CB    1 
ATOM   11828 C  CG    . TYR C 2 126 ? 106.091 105.789 124.806 1.00 25.16 ?  105 TYR C CG    1 
ATOM   11829 C  CD1   . TYR C 2 126 ? 105.763 106.085 123.485 1.00 26.75 ?  105 TYR C CD1   1 
ATOM   11830 C  CD2   . TYR C 2 126 ? 106.502 104.492 125.111 1.00 26.36 ?  105 TYR C CD2   1 
ATOM   11831 C  CE1   . TYR C 2 126 ? 105.859 105.109 122.486 1.00 28.22 ?  105 TYR C CE1   1 
ATOM   11832 C  CE2   . TYR C 2 126 ? 106.602 103.519 124.129 1.00 27.17 ?  105 TYR C CE2   1 
ATOM   11833 C  CZ    . TYR C 2 126 ? 106.266 103.828 122.824 1.00 29.26 ?  105 TYR C CZ    1 
ATOM   11834 O  OH    . TYR C 2 126 ? 106.353 102.853 121.851 1.00 30.76 ?  105 TYR C OH    1 
ATOM   11835 N  N     . SER C 2 127 ? 107.500 108.886 127.872 1.00 23.61 ?  106 SER C N     1 
ATOM   11836 C  CA    . SER C 2 127 ? 107.464 109.841 128.973 1.00 24.40 ?  106 SER C CA    1 
ATOM   11837 C  C     . SER C 2 127 ? 108.019 111.195 128.550 1.00 24.55 ?  106 SER C C     1 
ATOM   11838 O  O     . SER C 2 127 ? 107.552 112.215 129.032 1.00 24.74 ?  106 SER C O     1 
ATOM   11839 C  CB    . SER C 2 127 ? 108.203 109.323 130.206 1.00 24.54 ?  106 SER C CB    1 
ATOM   11840 O  OG    . SER C 2 127 ? 107.417 108.364 130.903 1.00 24.69 ?  106 SER C OG    1 
ATOM   11841 N  N     . ASN C 2 128 ? 109.014 111.199 127.664 1.00 25.28 ?  107 ASN C N     1 
ATOM   11842 C  CA    . ASN C 2 128 ? 109.537 112.454 127.114 1.00 25.88 ?  107 ASN C CA    1 
ATOM   11843 C  C     . ASN C 2 128 ? 108.439 113.173 126.341 1.00 25.48 ?  107 ASN C C     1 
ATOM   11844 O  O     . ASN C 2 128 ? 108.253 114.380 126.484 1.00 25.23 ?  107 ASN C O     1 
ATOM   11845 C  CB    . ASN C 2 128 ? 110.750 112.217 126.205 1.00 26.40 ?  107 ASN C CB    1 
ATOM   11846 C  CG    . ASN C 2 128 ? 112.032 111.936 126.980 1.00 27.90 ?  107 ASN C CG    1 
ATOM   11847 O  OD1   . ASN C 2 128 ? 112.008 111.365 128.072 1.00 30.62 ?  107 ASN C OD1   1 
ATOM   11848 N  ND2   . ASN C 2 128 ? 113.163 112.326 126.401 1.00 27.91 ?  107 ASN C ND2   1 
ATOM   11849 N  N     . ILE C 2 129 ? 107.707 112.418 125.529 1.00 25.44 ?  108 ILE C N     1 
ATOM   11850 C  CA    . ILE C 2 129 ? 106.574 112.981 124.795 1.00 25.48 ?  108 ILE C CA    1 
ATOM   11851 C  C     . ILE C 2 129 ? 105.503 113.499 125.768 1.00 25.93 ?  108 ILE C C     1 
ATOM   11852 O  O     . ILE C 2 129 ? 105.086 114.657 125.661 1.00 25.54 ?  108 ILE C O     1 
ATOM   11853 C  CB    . ILE C 2 129 ? 106.005 112.000 123.738 1.00 25.21 ?  108 ILE C CB    1 
ATOM   11854 C  CG1   . ILE C 2 129 ? 107.085 111.680 122.691 1.00 25.96 ?  108 ILE C CG1   1 
ATOM   11855 C  CG2   . ILE C 2 129 ? 104.742 112.587 123.072 1.00 24.43 ?  108 ILE C CG2   1 
ATOM   11856 C  CD1   . ILE C 2 129 ? 106.761 110.519 121.751 1.00 26.11 ?  108 ILE C CD1   1 
ATOM   11857 N  N     . PHE C 2 130 ? 105.080 112.661 126.720 1.00 26.04 ?  109 PHE C N     1 
ATOM   11858 C  CA    . PHE C 2 130 ? 104.073 113.064 127.720 1.00 26.66 ?  109 PHE C CA    1 
ATOM   11859 C  C     . PHE C 2 130 ? 104.477 114.329 128.482 1.00 27.38 ?  109 PHE C C     1 
ATOM   11860 O  O     . PHE C 2 130 ? 103.658 115.242 128.672 1.00 27.22 ?  109 PHE C O     1 
ATOM   11861 C  CB    . PHE C 2 130 ? 103.812 111.940 128.747 1.00 26.98 ?  109 PHE C CB    1 
ATOM   11862 C  CG    . PHE C 2 130 ? 103.066 110.747 128.203 1.00 27.46 ?  109 PHE C CG    1 
ATOM   11863 C  CD1   . PHE C 2 130 ? 102.167 110.873 127.150 1.00 28.57 ?  109 PHE C CD1   1 
ATOM   11864 C  CD2   . PHE C 2 130 ? 103.256 109.487 128.770 1.00 28.51 ?  109 PHE C CD2   1 
ATOM   11865 C  CE1   . PHE C 2 130 ? 101.483 109.762 126.657 1.00 29.17 ?  109 PHE C CE1   1 
ATOM   11866 C  CE2   . PHE C 2 130 ? 102.569 108.364 128.289 1.00 29.27 ?  109 PHE C CE2   1 
ATOM   11867 C  CZ    . PHE C 2 130 ? 101.678 108.500 127.235 1.00 28.83 ?  109 PHE C CZ    1 
ATOM   11868 N  N     . MET C 2 131 ? 105.736 114.387 128.918 1.00 27.52 ?  110 MET C N     1 
ATOM   11869 C  CA    . MET C 2 131 ? 106.206 115.503 129.747 1.00 29.07 ?  110 MET C CA    1 
ATOM   11870 C  C     . MET C 2 131 ? 106.260 116.824 129.000 1.00 29.58 ?  110 MET C C     1 
ATOM   11871 O  O     . MET C 2 131 ? 106.150 117.888 129.608 1.00 30.07 ?  110 MET C O     1 
ATOM   11872 C  CB    . MET C 2 131 ? 107.561 115.201 130.381 1.00 28.96 ?  110 MET C CB    1 
ATOM   11873 C  CG    . MET C 2 131 ? 107.461 114.318 131.607 1.00 31.09 ?  110 MET C CG    1 
ATOM   11874 S  SD    . MET C 2 131 ? 109.059 113.906 132.345 1.00 35.43 ?  110 MET C SD    1 
ATOM   11875 C  CE    . MET C 2 131 ? 109.816 112.898 131.074 1.00 33.13 ?  110 MET C CE    1 
ATOM   11876 N  N     . THR C 2 132 ? 106.424 116.744 127.685 1.00 30.25 ?  111 THR C N     1 
ATOM   11877 C  CA    . THR C 2 132 ? 106.405 117.917 126.817 1.00 30.97 ?  111 THR C CA    1 
ATOM   11878 C  C     . THR C 2 132 ? 104.978 118.428 126.588 1.00 31.36 ?  111 THR C C     1 
ATOM   11879 O  O     . THR C 2 132 ? 104.687 119.613 126.798 1.00 31.60 ?  111 THR C O     1 
ATOM   11880 C  CB    . THR C 2 132 ? 107.091 117.594 125.459 1.00 30.88 ?  111 THR C CB    1 
ATOM   11881 O  OG1   . THR C 2 132 ? 108.462 117.257 125.696 1.00 29.86 ?  111 THR C OG1   1 
ATOM   11882 C  CG2   . THR C 2 132 ? 107.032 118.786 124.490 1.00 31.44 ?  111 THR C CG2   1 
ATOM   11883 N  N     . LEU C 2 133 ? 104.095 117.526 126.171 1.00 31.34 ?  112 LEU C N     1 
ATOM   11884 C  CA    . LEU C 2 133 ? 102.758 117.905 125.709 1.00 31.68 ?  112 LEU C CA    1 
ATOM   11885 C  C     . LEU C 2 133 ? 101.689 118.071 126.793 1.00 31.96 ?  112 LEU C C     1 
ATOM   11886 O  O     . LEU C 2 133 ? 100.774 118.880 126.643 1.00 31.69 ?  112 LEU C O     1 
ATOM   11887 C  CB    . LEU C 2 133 ? 102.265 116.904 124.669 1.00 31.35 ?  112 LEU C CB    1 
ATOM   11888 C  CG    . LEU C 2 133 ? 103.181 116.621 123.474 1.00 32.14 ?  112 LEU C CG    1 
ATOM   11889 C  CD1   . LEU C 2 133 ? 102.550 115.559 122.605 1.00 32.15 ?  112 LEU C CD1   1 
ATOM   11890 C  CD2   . LEU C 2 133 ? 103.461 117.891 122.674 1.00 32.39 ?  112 LEU C CD2   1 
ATOM   11891 N  N     . ALA C 2 134 ? 101.803 117.310 127.876 1.00 32.12 ?  113 ALA C N     1 
ATOM   11892 C  CA    . ALA C 2 134 ? 100.712 117.199 128.836 1.00 32.53 ?  113 ALA C CA    1 
ATOM   11893 C  C     . ALA C 2 134 ? 101.083 117.663 130.238 1.00 33.15 ?  113 ALA C C     1 
ATOM   11894 O  O     . ALA C 2 134 ? 102.225 117.502 130.662 1.00 32.47 ?  113 ALA C O     1 
ATOM   11895 C  CB    . ALA C 2 134 ? 100.185 115.759 128.871 1.00 32.20 ?  113 ALA C CB    1 
ATOM   11896 N  N     . PRO C 2 135 ? 100.101 118.228 130.970 1.00 34.27 ?  114 PRO C N     1 
ATOM   11897 C  CA    . PRO C 2 135 ? 100.310 118.555 132.375 1.00 35.35 ?  114 PRO C CA    1 
ATOM   11898 C  C     . PRO C 2 135 ? 100.328 117.287 133.222 1.00 36.17 ?  114 PRO C C     1 
ATOM   11899 O  O     . PRO C 2 135 ? 99.762  116.267 132.822 1.00 35.92 ?  114 PRO C O     1 
ATOM   11900 C  CB    . PRO C 2 135 ? 99.107  119.441 132.722 1.00 35.48 ?  114 PRO C CB    1 
ATOM   11901 C  CG    . PRO C 2 135 ? 98.059  119.091 131.738 1.00 34.94 ?  114 PRO C CG    1 
ATOM   11902 C  CD    . PRO C 2 135 ? 98.743  118.573 130.507 1.00 34.50 ?  114 PRO C CD    1 
ATOM   11903 N  N     . THR C 2 136 ? 100.986 117.358 134.374 1.00 37.30 ?  115 THR C N     1 
ATOM   11904 C  CA    . THR C 2 136 ? 101.192 116.201 135.252 1.00 38.49 ?  115 THR C CA    1 
ATOM   11905 C  C     . THR C 2 136 ? 99.923  115.398 135.575 1.00 38.48 ?  115 THR C C     1 
ATOM   11906 O  O     . THR C 2 136 ? 99.976  114.165 135.639 1.00 38.74 ?  115 THR C O     1 
ATOM   11907 C  CB    . THR C 2 136 ? 101.881 116.628 136.564 1.00 38.95 ?  115 THR C CB    1 
ATOM   11908 O  OG1   . THR C 2 136 ? 103.057 117.376 136.247 1.00 40.08 ?  115 THR C OG1   1 
ATOM   11909 C  CG2   . THR C 2 136 ? 102.271 115.415 137.411 1.00 39.82 ?  115 THR C CG2   1 
ATOM   11910 N  N     . GLU C 2 137 ? 98.800  116.092 135.769 1.00 38.89 ?  116 GLU C N     1 
ATOM   11911 C  CA    . GLU C 2 137 ? 97.536  115.444 136.145 1.00 38.65 ?  116 GLU C CA    1 
ATOM   11912 C  C     . GLU C 2 137 ? 96.998  114.556 135.028 1.00 37.38 ?  116 GLU C C     1 
ATOM   11913 O  O     . GLU C 2 137 ? 96.462  113.480 135.288 1.00 37.22 ?  116 GLU C O     1 
ATOM   11914 C  CB    . GLU C 2 137 ? 96.468  116.462 136.603 1.00 39.52 ?  116 GLU C CB    1 
ATOM   11915 C  CG    . GLU C 2 137 ? 95.872  117.375 135.507 1.00 41.90 ?  116 GLU C CG    1 
ATOM   11916 C  CD    . GLU C 2 137 ? 96.096  118.877 135.751 1.00 46.43 ?  116 GLU C CD    1 
ATOM   11917 O  OE1   . GLU C 2 137 ? 96.902  119.247 136.639 1.00 47.84 ?  116 GLU C OE1   1 
ATOM   11918 O  OE2   . GLU C 2 137 ? 95.457  119.695 135.045 1.00 47.52 -1 116 GLU C OE2   1 
ATOM   11919 N  N     . THR C 2 138 ? 97.159  115.013 133.790 1.00 36.05 ?  117 THR C N     1 
ATOM   11920 C  CA    . THR C 2 138 ? 96.750  114.251 132.621 1.00 34.88 ?  117 THR C CA    1 
ATOM   11921 C  C     . THR C 2 138 ? 97.660  113.039 132.451 1.00 33.58 ?  117 THR C C     1 
ATOM   11922 O  O     . THR C 2 138 ? 97.192  111.959 132.078 1.00 33.61 ?  117 THR C O     1 
ATOM   11923 C  CB    . THR C 2 138 ? 96.765  115.118 131.355 1.00 34.85 ?  117 THR C CB    1 
ATOM   11924 O  OG1   . THR C 2 138 ? 96.013  116.313 131.601 1.00 35.98 ?  117 THR C OG1   1 
ATOM   11925 C  CG2   . THR C 2 138 ? 96.151  114.375 130.178 1.00 34.92 ?  117 THR C CG2   1 
ATOM   11926 N  N     . ILE C 2 139 ? 98.949  113.224 132.729 1.00 32.29 ?  118 ILE C N     1 
ATOM   11927 C  CA    . ILE C 2 139 ? 99.909  112.121 132.714 1.00 31.19 ?  118 ILE C CA    1 
ATOM   11928 C  C     . ILE C 2 139 ? 99.553  111.078 133.790 1.00 30.85 ?  118 ILE C C     1 
ATOM   11929 O  O     . ILE C 2 139 ? 99.477  109.886 133.492 1.00 29.77 ?  118 ILE C O     1 
ATOM   11930 C  CB    . ILE C 2 139 ? 101.384 112.603 132.858 1.00 31.25 ?  118 ILE C CB    1 
ATOM   11931 C  CG1   . ILE C 2 139 ? 101.761 113.584 131.735 1.00 30.12 ?  118 ILE C CG1   1 
ATOM   11932 C  CG2   . ILE C 2 139 ? 102.354 111.411 132.864 1.00 30.21 ?  118 ILE C CG2   1 
ATOM   11933 C  CD1   . ILE C 2 139 ? 103.156 114.215 131.900 1.00 29.41 ?  118 ILE C CD1   1 
ATOM   11934 N  N     . ASN C 2 140 ? 99.317  111.535 135.025 1.00 31.17 ?  119 ASN C N     1 
ATOM   11935 C  CA    . ASN C 2 140 ? 98.906  110.647 136.125 1.00 31.76 ?  119 ASN C CA    1 
ATOM   11936 C  C     . ASN C 2 140 ? 97.640  109.854 135.782 1.00 31.25 ?  119 ASN C C     1 
ATOM   11937 O  O     . ASN C 2 140 ? 97.583  108.644 136.006 1.00 31.47 ?  119 ASN C O     1 
ATOM   11938 C  CB    . ASN C 2 140 ? 98.673  111.426 137.429 1.00 32.65 ?  119 ASN C CB    1 
ATOM   11939 C  CG    . ASN C 2 140 ? 99.960  111.937 138.066 1.00 35.14 ?  119 ASN C CG    1 
ATOM   11940 O  OD1   . ASN C 2 140 ? 101.044 111.371 137.887 1.00 36.75 ?  119 ASN C OD1   1 
ATOM   11941 N  ND2   . ASN C 2 140 ? 99.833  113.013 138.848 1.00 38.05 ?  119 ASN C ND2   1 
ATOM   11942 N  N     . GLU C 2 141 ? 96.645  110.547 135.232 1.00 30.96 ?  120 GLU C N     1 
ATOM   11943 C  CA    . GLU C 2 141 ? 95.372  109.945 134.841 1.00 30.36 ?  120 GLU C CA    1 
ATOM   11944 C  C     . GLU C 2 141 ? 95.535  108.862 133.771 1.00 28.60 ?  120 GLU C C     1 
ATOM   11945 O  O     . GLU C 2 141 ? 94.905  107.812 133.862 1.00 27.94 ?  120 GLU C O     1 
ATOM   11946 C  CB    . GLU C 2 141 ? 94.395  111.016 134.347 1.00 30.86 ?  120 GLU C CB    1 
ATOM   11947 C  CG    . GLU C 2 141 ? 93.744  111.842 135.452 1.00 34.89 ?  120 GLU C CG    1 
ATOM   11948 C  CD    . GLU C 2 141 ? 92.941  113.016 134.908 1.00 39.82 ?  120 GLU C CD    1 
ATOM   11949 O  OE1   . GLU C 2 141 ? 92.655  113.045 133.685 1.00 41.95 ?  120 GLU C OE1   1 
ATOM   11950 O  OE2   . GLU C 2 141 ? 92.589  113.911 135.704 1.00 41.94 -1 120 GLU C OE2   1 
ATOM   11951 N  N     . VAL C 2 142 ? 96.369  109.109 132.764 1.00 27.29 ?  121 VAL C N     1 
ATOM   11952 C  CA    . VAL C 2 142 ? 96.535  108.099 131.697 1.00 25.89 ?  121 VAL C CA    1 
ATOM   11953 C  C     . VAL C 2 142 ? 97.246  106.833 132.191 1.00 25.11 ?  121 VAL C C     1 
ATOM   11954 O  O     . VAL C 2 142 ? 96.938  105.730 131.741 1.00 24.23 ?  121 VAL C O     1 
ATOM   11955 C  CB    . VAL C 2 142 ? 97.158  108.673 130.378 1.00 25.99 ?  121 VAL C CB    1 
ATOM   11956 C  CG1   . VAL C 2 142 ? 98.689  108.693 130.411 1.00 25.21 ?  121 VAL C CG1   1 
ATOM   11957 C  CG2   . VAL C 2 142 ? 96.683  107.870 129.177 1.00 25.78 ?  121 VAL C CG2   1 
ATOM   11958 N  N     . PHE C 2 143 ? 98.181  106.979 133.124 1.00 24.69 ?  122 PHE C N     1 
ATOM   11959 C  CA    . PHE C 2 143 ? 98.831  105.796 133.708 1.00 24.77 ?  122 PHE C CA    1 
ATOM   11960 C  C     . PHE C 2 143 ? 97.875  105.021 134.632 1.00 24.99 ?  122 PHE C C     1 
ATOM   11961 O  O     . PHE C 2 143 ? 97.925  103.793 134.704 1.00 24.73 ?  122 PHE C O     1 
ATOM   11962 C  CB    . PHE C 2 143 ? 100.159 106.154 134.387 1.00 24.83 ?  122 PHE C CB    1 
ATOM   11963 C  CG    . PHE C 2 143 ? 101.293 106.353 133.405 1.00 25.12 ?  122 PHE C CG    1 
ATOM   11964 C  CD1   . PHE C 2 143 ? 101.871 105.263 132.757 1.00 26.58 ?  122 PHE C CD1   1 
ATOM   11965 C  CD2   . PHE C 2 143 ? 101.767 107.623 133.114 1.00 24.49 ?  122 PHE C CD2   1 
ATOM   11966 C  CE1   . PHE C 2 143 ? 102.910 105.445 131.835 1.00 26.96 ?  122 PHE C CE1   1 
ATOM   11967 C  CE2   . PHE C 2 143 ? 102.798 107.815 132.206 1.00 25.79 ?  122 PHE C CE2   1 
ATOM   11968 C  CZ    . PHE C 2 143 ? 103.373 106.725 131.559 1.00 26.45 ?  122 PHE C CZ    1 
ATOM   11969 N  N     . GLU C 2 144 ? 96.990  105.742 135.317 1.00 25.22 ?  123 GLU C N     1 
ATOM   11970 C  CA    . GLU C 2 144 ? 95.908  105.095 136.065 1.00 25.72 ?  123 GLU C CA    1 
ATOM   11971 C  C     . GLU C 2 144 ? 94.957  104.366 135.118 1.00 25.08 ?  123 GLU C C     1 
ATOM   11972 O  O     . GLU C 2 144 ? 94.512  103.254 135.408 1.00 24.67 ?  123 GLU C O     1 
ATOM   11973 C  CB    . GLU C 2 144 ? 95.159  106.104 136.931 1.00 26.23 ?  123 GLU C CB    1 
ATOM   11974 C  CG    . GLU C 2 144 ? 95.976  106.571 138.124 1.00 29.96 ?  123 GLU C CG    1 
ATOM   11975 C  CD    . GLU C 2 144 ? 96.499  105.409 138.952 1.00 33.82 ?  123 GLU C CD    1 
ATOM   11976 O  OE1   . GLU C 2 144 ? 95.670  104.689 139.549 1.00 36.54 ?  123 GLU C OE1   1 
ATOM   11977 O  OE2   . GLU C 2 144 ? 97.731  105.203 138.993 1.00 35.84 -1 123 GLU C OE2   1 
ATOM   11978 N  N     . TRP C 2 145 ? 94.678  104.987 133.975 1.00 24.21 ?  124 TRP C N     1 
ATOM   11979 C  CA    . TRP C 2 145 ? 93.830  104.388 132.946 1.00 23.99 ?  124 TRP C CA    1 
ATOM   11980 C  C     . TRP C 2 145 ? 94.389  103.076 132.376 1.00 23.95 ?  124 TRP C C     1 
ATOM   11981 O  O     . TRP C 2 145 ? 93.613  102.139 132.111 1.00 23.31 ?  124 TRP C O     1 
ATOM   11982 C  CB    . TRP C 2 145 ? 93.546  105.394 131.820 1.00 24.13 ?  124 TRP C CB    1 
ATOM   11983 C  CG    . TRP C 2 145 ? 92.930  104.766 130.590 1.00 24.37 ?  124 TRP C CG    1 
ATOM   11984 C  CD1   . TRP C 2 145 ? 91.593  104.576 130.336 1.00 24.76 ?  124 TRP C CD1   1 
ATOM   11985 C  CD2   . TRP C 2 145 ? 93.634  104.253 129.452 1.00 23.31 ?  124 TRP C CD2   1 
ATOM   11986 N  NE1   . TRP C 2 145 ? 91.431  103.966 129.105 1.00 24.97 ?  124 TRP C NE1   1 
ATOM   11987 C  CE2   . TRP C 2 145 ? 92.664  103.760 128.544 1.00 24.20 ?  124 TRP C CE2   1 
ATOM   11988 C  CE3   . TRP C 2 145 ? 94.990  104.151 129.114 1.00 23.76 ?  124 TRP C CE3   1 
ATOM   11989 C  CZ2   . TRP C 2 145 ? 93.013  103.179 127.317 1.00 23.41 ?  124 TRP C CZ2   1 
ATOM   11990 C  CZ3   . TRP C 2 145 ? 95.337  103.569 127.896 1.00 23.29 ?  124 TRP C CZ3   1 
ATOM   11991 C  CH2   . TRP C 2 145 ? 94.347  103.097 127.010 1.00 22.93 ?  124 TRP C CH2   1 
ATOM   11992 N  N     . VAL C 2 146 ? 95.708  102.985 132.172 1.00 23.35 ?  125 VAL C N     1 
ATOM   11993 C  CA    . VAL C 2 146 ? 96.259  101.683 131.715 1.00 23.53 ?  125 VAL C CA    1 
ATOM   11994 C  C     . VAL C 2 146 ? 96.001  100.555 132.721 1.00 23.73 ?  125 VAL C C     1 
ATOM   11995 O  O     . VAL C 2 146 ? 95.646  99.456  132.320 1.00 23.03 ?  125 VAL C O     1 
ATOM   11996 C  CB    . VAL C 2 146 ? 97.746  101.702 131.123 1.00 23.63 ?  125 VAL C CB    1 
ATOM   11997 C  CG1   . VAL C 2 146 ? 98.342  103.079 131.008 1.00 24.40 ?  125 VAL C CG1   1 
ATOM   11998 C  CG2   . VAL C 2 146 ? 98.701  100.700 131.799 1.00 22.97 ?  125 VAL C CG2   1 
ATOM   11999 N  N     . LYS C 2 147 ? 96.125  100.853 134.017 1.00 24.06 ?  126 LYS C N     1 
ATOM   12000 C  CA    . LYS C 2 147 ? 95.929  99.840  135.068 1.00 25.41 ?  126 LYS C CA    1 
ATOM   12001 C  C     . LYS C 2 147 ? 94.521  99.240  135.085 1.00 25.82 ?  126 LYS C C     1 
ATOM   12002 O  O     . LYS C 2 147 ? 94.355  98.066  135.424 1.00 26.08 ?  126 LYS C O     1 
ATOM   12003 C  CB    . LYS C 2 147 ? 96.232  100.420 136.452 1.00 25.49 ?  126 LYS C CB    1 
ATOM   12004 C  CG    . LYS C 2 147 ? 97.687  100.761 136.705 1.00 27.52 ?  126 LYS C CG    1 
ATOM   12005 C  CD    . LYS C 2 147 ? 97.818  101.406 138.079 1.00 30.43 ?  126 LYS C CD    1 
ATOM   12006 C  CE    . LYS C 2 147 ? 99.162  102.081 138.256 1.00 33.10 ?  126 LYS C CE    1 
ATOM   12007 N  NZ    . LYS C 2 147 ? 99.207  102.800 139.560 1.00 34.86 1  126 LYS C NZ    1 
ATOM   12008 N  N     . GLN C 2 148 ? 93.522  100.043 134.722 1.00 26.45 ?  127 GLN C N     1 
ATOM   12009 C  CA    . GLN C 2 148 ? 92.119  99.630  134.817 1.00 26.85 ?  127 GLN C CA    1 
ATOM   12010 C  C     . GLN C 2 148 ? 91.469  99.266  133.480 1.00 26.01 ?  127 GLN C C     1 
ATOM   12011 O  O     . GLN C 2 148 ? 90.328  98.802  133.460 1.00 26.12 ?  127 GLN C O     1 
ATOM   12012 C  CB    . GLN C 2 148 ? 91.278  100.690 135.554 1.00 28.08 ?  127 GLN C CB    1 
ATOM   12013 C  CG    . GLN C 2 148 ? 91.200  102.057 134.868 1.00 30.69 ?  127 GLN C CG    1 
ATOM   12014 C  CD    . GLN C 2 148 ? 90.273  102.073 133.655 1.00 34.64 ?  127 GLN C CD    1 
ATOM   12015 O  OE1   . GLN C 2 148 ? 90.722  102.266 132.511 1.00 33.80 ?  127 GLN C OE1   1 
ATOM   12016 N  NE2   . GLN C 2 148 ? 88.973  101.859 133.895 1.00 36.24 ?  127 GLN C NE2   1 
ATOM   12017 N  N     . ASN C 2 149 ? 92.183  99.483  132.372 1.00 24.97 ?  128 ASN C N     1 
ATOM   12018 C  CA    . ASN C 2 149 ? 91.655  99.163  131.049 1.00 24.03 ?  128 ASN C CA    1 
ATOM   12019 C  C     . ASN C 2 149 ? 91.690  97.663  130.804 1.00 24.13 ?  128 ASN C C     1 
ATOM   12020 O  O     . ASN C 2 149 ? 92.772  97.069  130.821 1.00 22.93 ?  128 ASN C O     1 
ATOM   12021 C  CB    . ASN C 2 149 ? 92.469  99.857  129.968 1.00 23.97 ?  128 ASN C CB    1 
ATOM   12022 C  CG    . ASN C 2 149 ? 91.876  99.666  128.593 1.00 23.94 ?  128 ASN C CG    1 
ATOM   12023 O  OD1   . ASN C 2 149 ? 92.192  98.704  127.896 1.00 24.85 ?  128 ASN C OD1   1 
ATOM   12024 N  ND2   . ASN C 2 149 ? 90.969  100.557 128.213 1.00 24.76 ?  128 ASN C ND2   1 
ATOM   12025 N  N     . LYS C 2 150 ? 90.525  97.061  130.550 1.00 24.32 ?  129 LYS C N     1 
ATOM   12026 C  CA    . LYS C 2 150 ? 90.419  95.590  130.501 1.00 24.77 ?  129 LYS C CA    1 
ATOM   12027 C  C     . LYS C 2 150 ? 91.112  94.920  129.311 1.00 24.54 ?  129 LYS C C     1 
ATOM   12028 O  O     . LYS C 2 150 ? 91.605  93.798  129.437 1.00 24.17 ?  129 LYS C O     1 
ATOM   12029 C  CB    . LYS C 2 150 ? 88.965  95.120  130.634 1.00 25.27 ?  129 LYS C CB    1 
ATOM   12030 C  CG    . LYS C 2 150 ? 88.025  95.566  129.534 1.00 28.72 ?  129 LYS C CG    1 
ATOM   12031 C  CD    . LYS C 2 150 ? 86.729  94.756  129.601 1.00 33.40 ?  129 LYS C CD    1 
ATOM   12032 C  CE    . LYS C 2 150 ? 85.589  95.478  128.910 1.00 36.77 ?  129 LYS C CE    1 
ATOM   12033 N  NZ    . LYS C 2 150 ? 84.295  94.777  129.175 1.00 39.66 1  129 LYS C NZ    1 
ATOM   12034 N  N     . TYR C 2 151 ? 91.142  95.605  128.163 1.00 23.92 ?  130 TYR C N     1 
ATOM   12035 C  CA    . TYR C 2 151 ? 91.799  95.071  126.963 1.00 24.12 ?  130 TYR C CA    1 
ATOM   12036 C  C     . TYR C 2 151 ? 93.315  95.092  127.076 1.00 23.54 ?  130 TYR C C     1 
ATOM   12037 O  O     . TYR C 2 151 ? 93.999  94.153  126.642 1.00 23.32 ?  130 TYR C O     1 
ATOM   12038 C  CB    . TYR C 2 151 ? 91.327  95.830  125.709 1.00 24.53 ?  130 TYR C CB    1 
ATOM   12039 C  CG    . TYR C 2 151 ? 89.829  96.045  125.699 1.00 25.83 ?  130 TYR C CG    1 
ATOM   12040 C  CD1   . TYR C 2 151 ? 88.954  94.960  125.633 1.00 26.57 ?  130 TYR C CD1   1 
ATOM   12041 C  CD2   . TYR C 2 151 ? 89.286  97.331  125.802 1.00 27.87 ?  130 TYR C CD2   1 
ATOM   12042 C  CE1   . TYR C 2 151 ? 87.575  95.143  125.645 1.00 29.65 ?  130 TYR C CE1   1 
ATOM   12043 C  CE2   . TYR C 2 151 ? 87.900  97.526  125.820 1.00 29.91 ?  130 TYR C CE2   1 
ATOM   12044 C  CZ    . TYR C 2 151 ? 87.056  96.427  125.742 1.00 31.19 ?  130 TYR C CZ    1 
ATOM   12045 O  OH    . TYR C 2 151 ? 85.687  96.600  125.756 1.00 34.44 ?  130 TYR C OH    1 
ATOM   12046 N  N     . LEU C 2 152 ? 93.836  96.165  127.662 1.00 23.38 ?  131 LEU C N     1 
ATOM   12047 C  CA    . LEU C 2 152 ? 95.264  96.308  127.879 1.00 23.43 ?  131 LEU C CA    1 
ATOM   12048 C  C     . LEU C 2 152 ? 95.733  95.313  128.946 1.00 23.37 ?  131 LEU C C     1 
ATOM   12049 O  O     . LEU C 2 152 ? 96.780  94.679  128.787 1.00 23.05 ?  131 LEU C O     1 
ATOM   12050 C  CB    . LEU C 2 152 ? 95.565  97.749  128.287 1.00 23.73 ?  131 LEU C CB    1 
ATOM   12051 C  CG    . LEU C 2 152 ? 96.702  98.594  127.726 1.00 24.71 ?  131 LEU C CG    1 
ATOM   12052 C  CD1   . LEU C 2 152 ? 97.286  98.108  126.388 1.00 21.63 ?  131 LEU C CD1   1 
ATOM   12053 C  CD2   . LEU C 2 152 ? 96.225  100.024 127.608 1.00 26.87 ?  131 LEU C CD2   1 
ATOM   12054 N  N     . GLN C 2 153 ? 94.965  95.172  130.031 1.00 22.80 ?  132 GLN C N     1 
ATOM   12055 C  CA    . GLN C 2 153 ? 95.273  94.131  131.025 1.00 22.70 ?  132 GLN C CA    1 
ATOM   12056 C  C     . GLN C 2 153 ? 95.203  92.712  130.455 1.00 22.54 ?  132 GLN C C     1 
ATOM   12057 O  O     . GLN C 2 153 ? 96.093  91.892  130.725 1.00 21.73 ?  132 GLN C O     1 
ATOM   12058 C  CB    . GLN C 2 153 ? 94.422  94.271  132.291 1.00 23.07 ?  132 GLN C CB    1 
ATOM   12059 C  CG    . GLN C 2 153 ? 94.697  95.570  133.049 1.00 21.83 ?  132 GLN C CG    1 
ATOM   12060 C  CD    . GLN C 2 153 ? 96.159  95.729  133.472 1.00 22.34 ?  132 GLN C CD    1 
ATOM   12061 O  OE1   . GLN C 2 153 ? 96.765  94.810  134.027 1.00 24.07 ?  132 GLN C OE1   1 
ATOM   12062 N  NE2   . GLN C 2 153 ? 96.721  96.904  133.223 1.00 22.26 ?  132 GLN C NE2   1 
ATOM   12063 N  N     . LYS C 2 154 ? 94.166  92.423  129.664 1.00 22.53 ?  133 LYS C N     1 
ATOM   12064 C  CA    . LYS C 2 154 ? 94.062  91.107  129.033 1.00 22.84 ?  133 LYS C CA    1 
ATOM   12065 C  C     . LYS C 2 154 ? 95.263  90.801  128.136 1.00 22.42 ?  133 LYS C C     1 
ATOM   12066 O  O     . LYS C 2 154 ? 95.811  89.708  128.213 1.00 21.90 ?  133 LYS C O     1 
ATOM   12067 C  CB    . LYS C 2 154 ? 92.730  90.909  128.272 1.00 22.96 ?  133 LYS C CB    1 
ATOM   12068 C  CG    . LYS C 2 154 ? 92.568  89.499  127.623 1.00 23.45 ?  133 LYS C CG    1 
ATOM   12069 C  CD    . LYS C 2 154 ? 92.499  88.352  128.655 1.00 26.74 ?  133 LYS C CD    1 
ATOM   12070 C  CE    . LYS C 2 154 ? 92.295  86.992  127.974 1.00 27.93 ?  133 LYS C CE    1 
ATOM   12071 N  NZ    . LYS C 2 154 ? 92.426  85.838  128.903 1.00 27.86 1  133 LYS C NZ    1 
ATOM   12072 N  N     . LYS C 2 155 ? 95.690  91.758  127.306 1.00 22.77 ?  134 LYS C N     1 
ATOM   12073 C  CA    . LYS C 2 155 ? 96.782  91.468  126.371 1.00 22.87 ?  134 LYS C CA    1 
ATOM   12074 C  C     . LYS C 2 155 ? 98.110  91.276  127.096 1.00 22.30 ?  134 LYS C C     1 
ATOM   12075 O  O     . LYS C 2 155 ? 98.870  90.353  126.756 1.00 21.89 ?  134 LYS C O     1 
ATOM   12076 C  CB    . LYS C 2 155 ? 96.862  92.469  125.195 1.00 23.33 ?  134 LYS C CB    1 
ATOM   12077 C  CG    . LYS C 2 155 ? 97.447  93.829  125.480 1.00 24.25 ?  134 LYS C CG    1 
ATOM   12078 C  CD    . LYS C 2 155 ? 97.472  94.701  124.213 1.00 26.87 ?  134 LYS C CD    1 
ATOM   12079 C  CE    . LYS C 2 155 ? 96.140  95.413  124.003 1.00 28.26 ?  134 LYS C CE    1 
ATOM   12080 N  NZ    . LYS C 2 155 ? 96.280  96.484  122.970 1.00 28.97 1  134 LYS C NZ    1 
ATOM   12081 N  N     . ALA C 2 156 ? 98.358  92.102  128.112 1.00 21.96 ?  135 ALA C N     1 
ATOM   12082 C  CA    . ALA C 2 156 ? 99.507  91.910  129.017 1.00 22.43 ?  135 ALA C CA    1 
ATOM   12083 C  C     . ALA C 2 156 ? 99.467  90.568  129.750 1.00 22.02 ?  135 ALA C C     1 
ATOM   12084 O  O     . ALA C 2 156 ? 100.487 89.892  129.852 1.00 22.60 ?  135 ALA C O     1 
ATOM   12085 C  CB    . ALA C 2 156 ? 99.614  93.060  130.041 1.00 22.05 ?  135 ALA C CB    1 
ATOM   12086 N  N     . GLN C 2 157 ? 98.299  90.194  130.274 1.00 21.97 ?  136 GLN C N     1 
ATOM   12087 C  CA    . GLN C 2 157 ? 98.144  88.907  130.965 1.00 22.10 ?  136 GLN C CA    1 
ATOM   12088 C  C     . GLN C 2 157 ? 98.535  87.753  130.064 1.00 21.87 ?  136 GLN C C     1 
ATOM   12089 O  O     . GLN C 2 157 ? 99.233  86.838  130.497 1.00 21.75 ?  136 GLN C O     1 
ATOM   12090 C  CB    . GLN C 2 157 ? 96.700  88.679  131.412 1.00 22.50 ?  136 GLN C CB    1 
ATOM   12091 C  CG    . GLN C 2 157 ? 96.299  89.398  132.692 1.00 23.55 ?  136 GLN C CG    1 
ATOM   12092 C  CD    . GLN C 2 157 ? 94.788  89.481  132.813 1.00 26.93 ?  136 GLN C CD    1 
ATOM   12093 O  OE1   . GLN C 2 157 ? 94.073  88.671  132.227 1.00 26.36 ?  136 GLN C OE1   1 
ATOM   12094 N  NE2   . GLN C 2 157 ? 94.297  90.472  133.547 1.00 28.09 ?  136 GLN C NE2   1 
ATOM   12095 N  N     . MET C 2 158 ? 98.062  87.803  128.820 1.00 21.38 ?  137 MET C N     1 
ATOM   12096 C  CA    . MET C 2 158 ? 98.276  86.726  127.865 1.00 22.08 ?  137 MET C CA    1 
ATOM   12097 C  C     . MET C 2 158 ? 99.731  86.624  127.423 1.00 21.70 ?  137 MET C C     1 
ATOM   12098 O  O     . MET C 2 158 ? 100.292 85.531  127.329 1.00 21.83 ?  137 MET C O     1 
ATOM   12099 C  CB    . MET C 2 158 ? 97.402  86.930  126.632 1.00 22.05 ?  137 MET C CB    1 
ATOM   12100 C  CG    . MET C 2 158 ? 95.917  86.609  126.845 1.00 23.93 ?  137 MET C CG    1 
ATOM   12101 S  SD    . MET C 2 158 ? 94.966  87.102  125.393 1.00 27.75 ?  137 MET C SD    1 
ATOM   12102 C  CE    . MET C 2 158 ? 95.558  85.878  124.214 1.00 26.00 ?  137 MET C CE    1 
ATOM   12103 N  N     . ILE C 2 159 ? 100.326 87.767  127.113 1.00 20.90 ?  138 ILE C N     1 
ATOM   12104 C  CA    . ILE C 2 159 ? 101.685 87.775  126.598 1.00 20.60 ?  138 ILE C CA    1 
ATOM   12105 C  C     . ILE C 2 159 ? 102.676 87.416  127.709 1.00 20.36 ?  138 ILE C C     1 
ATOM   12106 O  O     . ILE C 2 159 ? 103.515 86.531  127.525 1.00 19.65 ?  138 ILE C O     1 
ATOM   12107 C  CB    . ILE C 2 159 ? 102.033 89.130  125.913 1.00 20.17 ?  138 ILE C CB    1 
ATOM   12108 C  CG1   . ILE C 2 159 ? 101.190 89.328  124.640 1.00 20.66 ?  138 ILE C CG1   1 
ATOM   12109 C  CG2   . ILE C 2 159 ? 103.548 89.255  125.672 1.00 20.62 ?  138 ILE C CG2   1 
ATOM   12110 C  CD1   . ILE C 2 159 ? 101.420 88.340  123.492 1.00 22.17 ?  138 ILE C CD1   1 
ATOM   12111 N  N     . VAL C 2 160 ? 102.559 88.081  128.859 1.00 19.58 ?  139 VAL C N     1 
ATOM   12112 C  CA    . VAL C 2 160 ? 103.473 87.860  129.983 1.00 19.88 ?  139 VAL C CA    1 
ATOM   12113 C  C     . VAL C 2 160 ? 103.293 86.451  130.556 1.00 19.44 ?  139 VAL C C     1 
ATOM   12114 O  O     . VAL C 2 160 ? 104.243 85.848  131.044 1.00 19.88 ?  139 VAL C O     1 
ATOM   12115 C  CB    . VAL C 2 160 ? 103.306 88.932  131.120 1.00 19.52 ?  139 VAL C CB    1 
ATOM   12116 C  CG1   . VAL C 2 160 ? 104.216 88.613  132.320 1.00 20.75 ?  139 VAL C CG1   1 
ATOM   12117 C  CG2   . VAL C 2 160 ? 103.640 90.326  130.601 1.00 20.03 ?  139 VAL C CG2   1 
ATOM   12118 N  N     . GLY C 2 161 ? 102.074 85.926  130.488 1.00 19.13 ?  140 GLY C N     1 
ATOM   12119 C  CA    . GLY C 2 161 ? 101.823 84.576  130.968 1.00 18.05 ?  140 GLY C CA    1 
ATOM   12120 C  C     . GLY C 2 161 ? 102.652 83.580  130.198 1.00 17.86 ?  140 GLY C C     1 
ATOM   12121 O  O     . GLY C 2 161 ? 103.265 82.677  130.778 1.00 17.47 ?  140 GLY C O     1 
ATOM   12122 N  N     . LEU C 2 162 ? 102.661 83.735  128.879 1.00 17.92 ?  141 LEU C N     1 
ATOM   12123 C  CA    . LEU C 2 162 ? 103.470 82.874  128.022 1.00 18.32 ?  141 LEU C CA    1 
ATOM   12124 C  C     . LEU C 2 162 ? 104.985 83.024  128.281 1.00 18.55 ?  141 LEU C C     1 
ATOM   12125 O  O     . LEU C 2 162 ? 105.703 82.026  128.323 1.00 18.49 ?  141 LEU C O     1 
ATOM   12126 C  CB    . LEU C 2 162 ? 103.125 83.128  126.549 1.00 18.50 ?  141 LEU C CB    1 
ATOM   12127 C  CG    . LEU C 2 162 ? 101.738 82.623  126.141 1.00 19.32 ?  141 LEU C CG    1 
ATOM   12128 C  CD1   . LEU C 2 162 ? 101.313 83.239  124.813 1.00 20.38 ?  141 LEU C CD1   1 
ATOM   12129 C  CD2   . LEU C 2 162 ? 101.705 81.093  126.079 1.00 19.94 ?  141 LEU C CD2   1 
ATOM   12130 N  N     . TYR C 2 163 ? 105.462 84.249  128.488 1.00 19.16 ?  142 TYR C N     1 
ATOM   12131 C  CA    . TYR C 2 163 ? 106.871 84.465  128.874 1.00 20.16 ?  142 TYR C CA    1 
ATOM   12132 C  C     . TYR C 2 163 ? 107.234 83.725  130.149 1.00 20.78 ?  142 TYR C C     1 
ATOM   12133 O  O     . TYR C 2 163 ? 108.300 83.112  130.250 1.00 20.36 ?  142 TYR C O     1 
ATOM   12134 C  CB    . TYR C 2 163 ? 107.186 85.956  129.083 1.00 20.34 ?  142 TYR C CB    1 
ATOM   12135 C  CG    . TYR C 2 163 ? 107.087 86.820  127.834 1.00 22.46 ?  142 TYR C CG    1 
ATOM   12136 C  CD1   . TYR C 2 163 ? 107.223 86.272  126.562 1.00 23.88 ?  142 TYR C CD1   1 
ATOM   12137 C  CD2   . TYR C 2 163 ? 106.867 88.189  127.934 1.00 22.41 ?  142 TYR C CD2   1 
ATOM   12138 C  CE1   . TYR C 2 163 ? 107.129 87.078  125.413 1.00 25.93 ?  142 TYR C CE1   1 
ATOM   12139 C  CE2   . TYR C 2 163 ? 106.777 88.994  126.802 1.00 22.07 ?  142 TYR C CE2   1 
ATOM   12140 C  CZ    . TYR C 2 163 ? 106.916 88.438  125.553 1.00 25.19 ?  142 TYR C CZ    1 
ATOM   12141 O  OH    . TYR C 2 163 ? 106.820 89.259  124.448 1.00 27.43 ?  142 TYR C OH    1 
ATOM   12142 N  N     . LYS C 2 164 ? 106.340 83.781  131.129 1.00 21.39 ?  143 LYS C N     1 
ATOM   12143 C  CA    . LYS C 2 164 ? 106.647 83.203  132.427 1.00 22.49 ?  143 LYS C CA    1 
ATOM   12144 C  C     . LYS C 2 164 ? 106.413 81.695  132.472 1.00 22.49 ?  143 LYS C C     1 
ATOM   12145 O  O     . LYS C 2 164 ? 106.841 81.033  133.411 1.00 22.45 ?  143 LYS C O     1 
ATOM   12146 C  CB    . LYS C 2 164 ? 105.933 83.957  133.546 1.00 23.16 ?  143 LYS C CB    1 
ATOM   12147 C  CG    . LYS C 2 164 ? 106.488 85.371  133.707 1.00 26.08 ?  143 LYS C CG    1 
ATOM   12148 C  CD    . LYS C 2 164 ? 106.223 85.939  135.070 1.00 30.38 ?  143 LYS C CD    1 
ATOM   12149 C  CE    . LYS C 2 164 ? 106.946 87.251  135.255 1.00 32.69 ?  143 LYS C CE    1 
ATOM   12150 N  NZ    . LYS C 2 164 ? 106.635 87.827  136.592 1.00 35.60 1  143 LYS C NZ    1 
ATOM   12151 N  N     . ALA C 2 165 ? 105.804 81.152  131.416 1.00 22.02 ?  144 ALA C N     1 
ATOM   12152 C  CA    . ALA C 2 165 ? 105.609 79.718  131.314 1.00 22.69 ?  144 ALA C CA    1 
ATOM   12153 C  C     . ALA C 2 165 ? 106.812 78.986  130.695 1.00 23.20 ?  144 ALA C C     1 
ATOM   12154 O  O     . ALA C 2 165 ? 106.844 77.762  130.678 1.00 23.80 ?  144 ALA C O     1 
ATOM   12155 C  CB    . ALA C 2 165 ? 104.305 79.400  130.542 1.00 21.79 ?  144 ALA C CB    1 
ATOM   12156 N  N     . ILE C 2 166 ? 107.803 79.724  130.186 1.00 23.97 ?  145 ILE C N     1 
ATOM   12157 C  CA    . ILE C 2 166 ? 108.987 79.084  129.602 1.00 24.29 ?  145 ILE C CA    1 
ATOM   12158 C  C     . ILE C 2 166 ? 109.670 78.183  130.635 1.00 25.49 ?  145 ILE C C     1 
ATOM   12159 O  O     . ILE C 2 166 ? 109.883 78.586  131.774 1.00 25.82 ?  145 ILE C O     1 
ATOM   12160 C  CB    . ILE C 2 166 ? 110.017 80.107  129.042 1.00 24.22 ?  145 ILE C CB    1 
ATOM   12161 C  CG1   . ILE C 2 166 ? 109.399 80.963  127.941 1.00 23.45 ?  145 ILE C CG1   1 
ATOM   12162 C  CG2   . ILE C 2 166 ? 111.252 79.385  128.499 1.00 23.42 ?  145 ILE C CG2   1 
ATOM   12163 C  CD1   . ILE C 2 166 ? 110.252 82.201  127.564 1.00 21.99 ?  145 ILE C CD1   1 
ATOM   12164 N  N     . GLN C 2 167 ? 109.958 76.951  130.237 1.00 26.83 ?  146 GLN C N     1 
ATOM   12165 C  CA    . GLN C 2 167 ? 110.649 76.006  131.102 1.00 28.85 ?  146 GLN C CA    1 
ATOM   12166 C  C     . GLN C 2 167 ? 112.040 75.783  130.541 1.00 29.77 ?  146 GLN C C     1 
ATOM   12167 O  O     . GLN C 2 167 ? 112.210 75.645  129.325 1.00 29.74 ?  146 GLN C O     1 
ATOM   12168 C  CB    . GLN C 2 167 ? 109.891 74.672  131.191 1.00 28.99 ?  146 GLN C CB    1 
ATOM   12169 C  CG    . GLN C 2 167 ? 108.593 74.727  131.996 1.00 30.30 ?  146 GLN C CG    1 
ATOM   12170 C  CD    . GLN C 2 167 ? 108.826 74.896  133.492 1.00 33.32 ?  146 GLN C CD    1 
ATOM   12171 O  OE1   . GLN C 2 167 ? 109.956 74.786  133.972 1.00 34.63 ?  146 GLN C OE1   1 
ATOM   12172 N  NE2   . GLN C 2 167 ? 107.752 75.142  134.238 1.00 32.32 ?  146 GLN C NE2   1 
ATOM   12173 N  N     . LYS C 2 168 ? 113.028 75.754  131.426 1.00 31.29 ?  147 LYS C N     1 
ATOM   12174 C  CA    . LYS C 2 168 ? 114.417 75.531  131.024 1.00 33.14 ?  147 LYS C CA    1 
ATOM   12175 C  C     . LYS C 2 168 ? 114.508 74.252  130.204 1.00 33.79 ?  147 LYS C C     1 
ATOM   12176 O  O     . LYS C 2 168 ? 113.822 73.265  130.493 1.00 34.06 ?  147 LYS C O     1 
ATOM   12177 C  CB    . LYS C 2 168 ? 115.323 75.464  132.251 1.00 33.44 ?  147 LYS C CB    1 
ATOM   12178 C  CG    . LYS C 2 168 ? 116.803 75.739  131.990 1.00 35.61 ?  147 LYS C CG    1 
ATOM   12179 C  CD    . LYS C 2 168 ? 117.575 75.686  133.304 1.00 38.40 ?  147 LYS C CD    1 
ATOM   12180 C  CE    . LYS C 2 168 ? 118.990 76.223  133.175 1.00 40.48 ?  147 LYS C CE    1 
ATOM   12181 N  NZ    . LYS C 2 168 ? 119.961 75.113  132.984 1.00 41.56 1  147 LYS C NZ    1 
ATOM   12182 N  N     . ASP C 2 169 ? 115.319 74.298  129.151 1.00 35.10 ?  148 ASP C N     1 
ATOM   12183 C  CA    . ASP C 2 169 ? 115.531 73.152  128.251 1.00 36.27 ?  148 ASP C CA    1 
ATOM   12184 C  C     . ASP C 2 169 ? 114.268 72.608  127.581 1.00 36.29 ?  148 ASP C C     1 
ATOM   12185 O  O     . ASP C 2 169 ? 114.271 71.496  127.051 1.00 36.95 ?  148 ASP C O     1 
ATOM   12186 C  CB    . ASP C 2 169 ? 116.251 72.018  128.988 1.00 37.15 ?  148 ASP C CB    1 
ATOM   12187 C  CG    . ASP C 2 169 ? 117.684 72.349  129.306 1.00 38.94 ?  148 ASP C CG    1 
ATOM   12188 O  OD1   . ASP C 2 169 ? 118.263 73.235  128.635 1.00 41.71 ?  148 ASP C OD1   1 
ATOM   12189 O  OD2   . ASP C 2 169 ? 118.233 71.719  130.232 1.00 41.64 -1 148 ASP C OD2   1 
ATOM   12190 N  N     . ASP C 2 170 ? 113.189 73.381  127.605 1.00 35.87 ?  149 ASP C N     1 
ATOM   12191 C  CA    . ASP C 2 170 ? 111.955 72.966  126.951 1.00 35.24 ?  149 ASP C CA    1 
ATOM   12192 C  C     . ASP C 2 170 ? 111.695 73.929  125.801 1.00 34.12 ?  149 ASP C C     1 
ATOM   12193 O  O     . ASP C 2 170 ? 111.217 75.064  125.996 1.00 33.52 ?  149 ASP C O     1 
ATOM   12194 C  CB    . ASP C 2 170 ? 110.797 72.906  127.952 1.00 36.09 ?  149 ASP C CB    1 
ATOM   12195 C  CG    . ASP C 2 170 ? 109.440 72.663  127.290 1.00 38.39 ?  149 ASP C CG    1 
ATOM   12196 O  OD1   . ASP C 2 170 ? 109.375 72.260  126.105 1.00 42.06 ?  149 ASP C OD1   1 
ATOM   12197 O  OD2   . ASP C 2 170 ? 108.420 72.869  127.975 1.00 42.21 -1 149 ASP C OD2   1 
ATOM   12198 N  N     . GLU C 2 171 ? 112.038 73.460  124.605 1.00 32.48 ?  150 GLU C N     1 
ATOM   12199 C  CA    . GLU C 2 171 ? 112.020 74.279  123.406 1.00 30.93 ?  150 GLU C CA    1 
ATOM   12200 C  C     . GLU C 2 171 ? 110.602 74.665  122.974 1.00 29.37 ?  150 GLU C C     1 
ATOM   12201 O  O     . GLU C 2 171 ? 110.410 75.711  122.354 1.00 28.99 ?  150 GLU C O     1 
ATOM   12202 C  CB    . GLU C 2 171 ? 112.799 73.597  122.265 1.00 31.30 ?  150 GLU C CB    1 
ATOM   12203 C  CG    . GLU C 2 171 ? 112.139 72.352  121.625 1.00 33.64 ?  150 GLU C CG    1 
ATOM   12204 C  CD    . GLU C 2 171 ? 113.087 71.538  120.712 1.00 36.40 ?  150 GLU C CD    1 
ATOM   12205 O  OE1   . GLU C 2 171 ? 114.258 71.937  120.523 1.00 38.62 ?  150 GLU C OE1   1 
ATOM   12206 O  OE2   . GLU C 2 171 ? 112.660 70.489  120.178 1.00 37.42 -1 150 GLU C OE2   1 
ATOM   12207 N  N     . ILE C 2 172 ? 109.619 73.825  123.300 1.00 27.68 ?  151 ILE C N     1 
ATOM   12208 C  CA    . ILE C 2 172 ? 108.230 74.105  122.927 1.00 26.26 ?  151 ILE C CA    1 
ATOM   12209 C  C     . ILE C 2 172 ? 107.676 75.298  123.711 1.00 24.85 ?  151 ILE C C     1 
ATOM   12210 O  O     . ILE C 2 172 ? 107.036 76.167  123.122 1.00 23.53 ?  151 ILE C O     1 
ATOM   12211 C  CB    . ILE C 2 172 ? 107.314 72.859  123.060 1.00 26.53 ?  151 ILE C CB    1 
ATOM   12212 C  CG1   . ILE C 2 172 ? 107.791 71.732  122.128 1.00 27.59 ?  151 ILE C CG1   1 
ATOM   12213 C  CG2   . ILE C 2 172 ? 105.835 73.215  122.815 1.00 26.51 ?  151 ILE C CG2   1 
ATOM   12214 C  CD1   . ILE C 2 172 ? 107.659 72.016  120.626 1.00 26.91 ?  151 ILE C CD1   1 
ATOM   12215 N  N     . SER C 2 173 ? 107.928 75.352  125.021 1.00 23.58 ?  152 SER C N     1 
ATOM   12216 C  CA    . SER C 2 173 ? 107.471 76.501  125.800 1.00 22.36 ?  152 SER C CA    1 
ATOM   12217 C  C     . SER C 2 173 ? 108.172 77.777  125.331 1.00 21.79 ?  152 SER C C     1 
ATOM   12218 O  O     . SER C 2 173 ? 107.576 78.862  125.338 1.00 20.91 ?  152 SER C O     1 
ATOM   12219 C  CB    . SER C 2 173 ? 107.637 76.281  127.309 1.00 22.43 ?  152 SER C CB    1 
ATOM   12220 O  OG    . SER C 2 173 ? 108.996 76.081  127.665 1.00 24.02 ?  152 SER C OG    1 
ATOM   12221 N  N     . LEU C 2 174 ? 109.435 77.639  124.926 1.00 21.65 ?  153 LEU C N     1 
ATOM   12222 C  CA    . LEU C 2 174 ? 110.207 78.764  124.403 1.00 21.86 ?  153 LEU C CA    1 
ATOM   12223 C  C     . LEU C 2 174 ? 109.623 79.262  123.079 1.00 21.98 ?  153 LEU C C     1 
ATOM   12224 O  O     . LEU C 2 174 ? 109.447 80.470  122.907 1.00 21.64 ?  153 LEU C O     1 
ATOM   12225 C  CB    . LEU C 2 174 ? 111.705 78.420  124.270 1.00 21.71 ?  153 LEU C CB    1 
ATOM   12226 C  CG    . LEU C 2 174 ? 112.665 79.492  123.719 1.00 22.04 ?  153 LEU C CG    1 
ATOM   12227 C  CD1   . LEU C 2 174 ? 112.550 80.824  124.459 1.00 21.99 ?  153 LEU C CD1   1 
ATOM   12228 C  CD2   . LEU C 2 174 ? 114.107 78.975  123.768 1.00 23.37 ?  153 LEU C CD2   1 
ATOM   12229 N  N     . PHE C 2 175 ? 109.319 78.336  122.163 1.00 22.17 ?  154 PHE C N     1 
ATOM   12230 C  CA    . PHE C 2 175 ? 108.659 78.671  120.881 1.00 22.02 ?  154 PHE C CA    1 
ATOM   12231 C  C     . PHE C 2 175 ? 107.375 79.464  121.090 1.00 21.86 ?  154 PHE C C     1 
ATOM   12232 O  O     . PHE C 2 175 ? 107.112 80.445  120.383 1.00 21.62 ?  154 PHE C O     1 
ATOM   12233 C  CB    . PHE C 2 175 ? 108.323 77.397  120.089 1.00 22.08 ?  154 PHE C CB    1 
ATOM   12234 C  CG    . PHE C 2 175 ? 107.495 77.649  118.843 1.00 21.99 ?  154 PHE C CG    1 
ATOM   12235 C  CD1   . PHE C 2 175 ? 108.105 78.044  117.650 1.00 20.87 ?  154 PHE C CD1   1 
ATOM   12236 C  CD2   . PHE C 2 175 ? 106.100 77.504  118.872 1.00 20.82 ?  154 PHE C CD2   1 
ATOM   12237 C  CE1   . PHE C 2 175 ? 107.348 78.306  116.507 1.00 20.27 ?  154 PHE C CE1   1 
ATOM   12238 C  CE2   . PHE C 2 175 ? 105.327 77.751  117.734 1.00 20.19 ?  154 PHE C CE2   1 
ATOM   12239 C  CZ    . PHE C 2 175 ? 105.954 78.149  116.540 1.00 20.93 ?  154 PHE C CZ    1 
ATOM   12240 N  N     . LYS C 2 176 ? 106.558 79.004  122.038 1.00 21.98 ?  155 LYS C N     1 
ATOM   12241 C  CA    . LYS C 2 176 ? 105.277 79.654  122.329 1.00 21.79 ?  155 LYS C CA    1 
ATOM   12242 C  C     . LYS C 2 176 ? 105.476 81.102  122.789 1.00 21.70 ?  155 LYS C C     1 
ATOM   12243 O  O     . LYS C 2 176 ? 104.757 82.008  122.343 1.00 21.10 ?  155 LYS C O     1 
ATOM   12244 C  CB    . LYS C 2 176 ? 104.481 78.838  123.357 1.00 22.00 ?  155 LYS C CB    1 
ATOM   12245 C  CG    . LYS C 2 176 ? 104.021 77.479  122.846 1.00 21.93 ?  155 LYS C CG    1 
ATOM   12246 C  CD    . LYS C 2 176 ? 103.300 76.687  123.923 1.00 23.06 ?  155 LYS C CD    1 
ATOM   12247 C  CE    . LYS C 2 176 ? 102.789 75.364  123.390 1.00 24.91 ?  155 LYS C CE    1 
ATOM   12248 N  NZ    . LYS C 2 176 ? 102.376 74.448  124.505 1.00 25.16 1  155 LYS C NZ    1 
ATOM   12249 N  N     . ALA C 2 177 ? 106.455 81.315  123.674 1.00 21.49 ?  156 ALA C N     1 
ATOM   12250 C  CA    . ALA C 2 177 ? 106.807 82.666  124.102 1.00 20.60 ?  156 ALA C CA    1 
ATOM   12251 C  C     . ALA C 2 177 ? 107.377 83.537  122.960 1.00 20.37 ?  156 ALA C C     1 
ATOM   12252 O  O     . ALA C 2 177 ? 107.102 84.728  122.904 1.00 19.61 ?  156 ALA C O     1 
ATOM   12253 C  CB    . ALA C 2 177 ? 107.770 82.633  125.285 1.00 20.88 ?  156 ALA C CB    1 
ATOM   12254 N  N     . MET C 2 178 ? 108.150 82.938  122.055 1.00 20.70 ?  157 MET C N     1 
ATOM   12255 C  CA    . MET C 2 178 ? 108.682 83.670  120.892 1.00 21.06 ?  157 MET C CA    1 
ATOM   12256 C  C     . MET C 2 178 ? 107.584 84.067  119.925 1.00 20.83 ?  157 MET C C     1 
ATOM   12257 O  O     . MET C 2 178 ? 107.679 85.113  119.275 1.00 21.28 ?  157 MET C O     1 
ATOM   12258 C  CB    . MET C 2 178 ? 109.743 82.851  120.134 1.00 20.68 ?  157 MET C CB    1 
ATOM   12259 C  CG    . MET C 2 178 ? 111.063 82.628  120.869 1.00 21.61 ?  157 MET C CG    1 
ATOM   12260 S  SD    . MET C 2 178 ? 112.100 81.451  119.969 1.00 24.32 ?  157 MET C SD    1 
ATOM   12261 C  CE    . MET C 2 178 ? 113.674 81.669  120.825 1.00 23.64 ?  157 MET C CE    1 
ATOM   12262 N  N     . VAL C 2 179 ? 106.560 83.224  119.792 1.00 20.76 ?  158 VAL C N     1 
ATOM   12263 C  CA    . VAL C 2 179 ? 105.394 83.570  118.969 1.00 20.14 ?  158 VAL C CA    1 
ATOM   12264 C  C     . VAL C 2 179 ? 104.688 84.777  119.596 1.00 20.35 ?  158 VAL C C     1 
ATOM   12265 O  O     . VAL C 2 179 ? 104.327 85.733  118.905 1.00 19.82 ?  158 VAL C O     1 
ATOM   12266 C  CB    . VAL C 2 179 ? 104.392 82.391  118.846 1.00 20.07 ?  158 VAL C CB    1 
ATOM   12267 C  CG1   . VAL C 2 179 ? 103.083 82.860  118.205 1.00 20.07 ?  158 VAL C CG1   1 
ATOM   12268 C  CG2   . VAL C 2 179 ? 105.001 81.254  118.031 1.00 20.57 ?  158 VAL C CG2   1 
ATOM   12269 N  N     . ALA C 2 180 ? 104.504 84.714  120.911 1.00 19.89 ?  159 ALA C N     1 
ATOM   12270 C  CA    . ALA C 2 180 ? 103.897 85.808  121.670 1.00 20.50 ?  159 ALA C CA    1 
ATOM   12271 C  C     . ALA C 2 180 ? 104.692 87.110  121.474 1.00 20.67 ?  159 ALA C C     1 
ATOM   12272 O  O     . ALA C 2 180 ? 104.106 88.166  121.226 1.00 21.27 ?  159 ALA C O     1 
ATOM   12273 C  CB    . ALA C 2 180 ? 103.837 85.443  123.137 1.00 20.03 ?  159 ALA C CB    1 
ATOM   12274 N  N     . SER C 2 181 ? 106.017 87.019  121.573 1.00 20.78 ?  160 SER C N     1 
ATOM   12275 C  CA    . SER C 2 181 ? 106.906 88.167  121.356 1.00 21.26 ?  160 SER C CA    1 
ATOM   12276 C  C     . SER C 2 181 ? 106.807 88.724  119.929 1.00 21.19 ?  160 SER C C     1 
ATOM   12277 O  O     . SER C 2 181 ? 106.696 89.931  119.746 1.00 20.89 ?  160 SER C O     1 
ATOM   12278 C  CB    . SER C 2 181 ? 108.359 87.809  121.703 1.00 21.42 ?  160 SER C CB    1 
ATOM   12279 O  OG    . SER C 2 181 ? 109.210 88.940  121.581 1.00 23.69 ?  160 SER C OG    1 
ATOM   12280 N  N     . VAL C 2 182 ? 106.846 87.853  118.915 1.00 20.99 ?  161 VAL C N     1 
ATOM   12281 C  CA    . VAL C 2 182 ? 106.627 88.329  117.545 1.00 21.18 ?  161 VAL C CA    1 
ATOM   12282 C  C     . VAL C 2 182 ? 105.263 89.030  117.415 1.00 21.15 ?  161 VAL C C     1 
ATOM   12283 O  O     . VAL C 2 182 ? 105.167 90.103  116.797 1.00 21.18 ?  161 VAL C O     1 
ATOM   12284 C  CB    . VAL C 2 182 ? 106.782 87.197  116.479 1.00 21.11 ?  161 VAL C CB    1 
ATOM   12285 C  CG1   . VAL C 2 182 ? 106.346 87.690  115.101 1.00 21.75 ?  161 VAL C CG1   1 
ATOM   12286 C  CG2   . VAL C 2 182 ? 108.227 86.703  116.432 1.00 20.98 ?  161 VAL C CG2   1 
ATOM   12287 N  N     . TYR C 2 183 ? 104.210 88.448  118.004 1.00 21.10 ?  162 TYR C N     1 
ATOM   12288 C  CA    . TYR C 2 183 ? 102.885 89.085  117.960 1.00 21.21 ?  162 TYR C CA    1 
ATOM   12289 C  C     . TYR C 2 183 ? 102.854 90.446  118.655 1.00 21.38 ?  162 TYR C C     1 
ATOM   12290 O  O     . TYR C 2 183 ? 102.134 91.342  118.229 1.00 20.97 ?  162 TYR C O     1 
ATOM   12291 C  CB    . TYR C 2 183 ? 101.769 88.183  118.525 1.00 21.50 ?  162 TYR C CB    1 
ATOM   12292 C  CG    . TYR C 2 183 ? 101.422 87.010  117.647 1.00 22.20 ?  162 TYR C CG    1 
ATOM   12293 C  CD1   . TYR C 2 183 ? 101.736 87.014  116.289 1.00 23.80 ?  162 TYR C CD1   1 
ATOM   12294 C  CD2   . TYR C 2 183 ? 100.756 85.896  118.170 1.00 23.71 ?  162 TYR C CD2   1 
ATOM   12295 C  CE1   . TYR C 2 183 ? 101.415 85.925  115.470 1.00 25.52 ?  162 TYR C CE1   1 
ATOM   12296 C  CE2   . TYR C 2 183 ? 100.430 84.815  117.367 1.00 24.01 ?  162 TYR C CE2   1 
ATOM   12297 C  CZ    . TYR C 2 183 ? 100.768 84.828  116.024 1.00 25.47 ?  162 TYR C CZ    1 
ATOM   12298 O  OH    . TYR C 2 183 ? 100.460 83.748  115.224 1.00 25.37 ?  162 TYR C OH    1 
ATOM   12299 N  N     . LEU C 2 184 ? 103.619 90.584  119.727 1.00 22.12 ?  163 LEU C N     1 
ATOM   12300 C  CA    . LEU C 2 184 ? 103.770 91.892  120.395 1.00 23.80 ?  163 LEU C CA    1 
ATOM   12301 C  C     . LEU C 2 184 ? 104.536 92.869  119.492 1.00 24.21 ?  163 LEU C C     1 
ATOM   12302 O  O     . LEU C 2 184 ? 104.103 93.989  119.316 1.00 24.72 ?  163 LEU C O     1 
ATOM   12303 C  CB    . LEU C 2 184 ? 104.466 91.741  121.751 1.00 23.52 ?  163 LEU C CB    1 
ATOM   12304 C  CG    . LEU C 2 184 ? 104.645 92.963  122.675 1.00 24.91 ?  163 LEU C CG    1 
ATOM   12305 C  CD1   . LEU C 2 184 ? 104.561 92.527  124.116 1.00 24.81 ?  163 LEU C CD1   1 
ATOM   12306 C  CD2   . LEU C 2 184 ? 105.953 93.727  122.425 1.00 26.39 ?  163 LEU C CD2   1 
ATOM   12307 N  N     . GLU C 2 185 ? 105.658 92.425  118.909 1.00 25.17 ?  164 GLU C N     1 
ATOM   12308 C  CA    . GLU C 2 185 ? 106.527 93.302  118.109 1.00 25.30 ?  164 GLU C CA    1 
ATOM   12309 C  C     . GLU C 2 185 ? 105.877 93.780  116.800 1.00 25.07 ?  164 GLU C C     1 
ATOM   12310 O  O     . GLU C 2 185 ? 105.983 94.959  116.421 1.00 24.49 ?  164 GLU C O     1 
ATOM   12311 C  CB    . GLU C 2 185 ? 107.855 92.590  117.754 1.00 26.17 ?  164 GLU C CB    1 
ATOM   12312 C  CG    . GLU C 2 185 ? 108.771 92.276  118.957 1.00 27.05 ?  164 GLU C CG    1 
ATOM   12313 C  CD    . GLU C 2 185 ? 109.541 93.500  119.468 1.00 29.23 ?  164 GLU C CD    1 
ATOM   12314 O  OE1   . GLU C 2 185 ? 109.379 94.626  118.916 1.00 28.79 ?  164 GLU C OE1   1 
ATOM   12315 O  OE2   . GLU C 2 185 ? 110.350 93.341  120.411 1.00 28.65 -1 164 GLU C OE2   1 
ATOM   12316 N  N     . SER C 2 186 ? 105.230 92.845  116.116 1.00 24.23 ?  165 SER C N     1 
ATOM   12317 C  CA    . SER C 2 186 ? 104.868 93.001  114.712 1.00 24.71 ?  165 SER C CA    1 
ATOM   12318 C  C     . SER C 2 186 ? 103.368 93.143  114.477 1.00 24.51 ?  165 SER C C     1 
ATOM   12319 O  O     . SER C 2 186 ? 102.948 93.433  113.359 1.00 24.87 ?  165 SER C O     1 
ATOM   12320 C  CB    . SER C 2 186 ? 105.392 91.802  113.910 1.00 25.06 ?  165 SER C CB    1 
ATOM   12321 O  OG    . SER C 2 186 ? 106.796 91.670  114.031 1.00 26.29 ?  165 SER C OG    1 
ATOM   12322 N  N     . PHE C 2 187 ? 102.572 92.924  115.521 1.00 24.71 ?  166 PHE C N     1 
ATOM   12323 C  CA    . PHE C 2 187 ? 101.116 93.022  115.431 1.00 25.69 ?  166 PHE C CA    1 
ATOM   12324 C  C     . PHE C 2 187 ? 100.529 93.984  116.476 1.00 25.87 ?  166 PHE C C     1 
ATOM   12325 O  O     . PHE C 2 187 ? 99.913  94.983  116.099 1.00 26.03 ?  166 PHE C O     1 
ATOM   12326 C  CB    . PHE C 2 187 ? 100.457 91.632  115.529 1.00 25.54 ?  166 PHE C CB    1 
ATOM   12327 C  CG    . PHE C 2 187 ? 98.954  91.669  115.712 1.00 26.64 ?  166 PHE C CG    1 
ATOM   12328 C  CD1   . PHE C 2 187 ? 98.123  92.245  114.742 1.00 25.90 ?  166 PHE C CD1   1 
ATOM   12329 C  CD2   . PHE C 2 187 ? 98.366  91.113  116.852 1.00 27.45 ?  166 PHE C CD2   1 
ATOM   12330 C  CE1   . PHE C 2 187 ? 96.726  92.283  114.913 1.00 25.64 ?  166 PHE C CE1   1 
ATOM   12331 C  CE2   . PHE C 2 187 ? 96.963  91.141  117.035 1.00 26.52 ?  166 PHE C CE2   1 
ATOM   12332 C  CZ    . PHE C 2 187 ? 96.148  91.725  116.062 1.00 27.18 ?  166 PHE C CZ    1 
ATOM   12333 N  N     . LEU C 2 188 ? 100.735 93.685  117.761 1.00 26.13 ?  167 LEU C N     1 
ATOM   12334 C  CA    . LEU C 2 188 ? 100.084 94.419  118.878 1.00 27.13 ?  167 LEU C CA    1 
ATOM   12335 C  C     . LEU C 2 188 ? 100.445 95.910  119.010 1.00 27.22 ?  167 LEU C C     1 
ATOM   12336 O  O     . LEU C 2 188 ? 99.621  96.711  119.473 1.00 28.03 ?  167 LEU C O     1 
ATOM   12337 C  CB    . LEU C 2 188 ? 100.356 93.731  120.225 1.00 26.89 ?  167 LEU C CB    1 
ATOM   12338 C  CG    . LEU C 2 188 ? 99.813  92.334  120.560 1.00 28.64 ?  167 LEU C CG    1 
ATOM   12339 C  CD1   . LEU C 2 188 ? 100.286 91.904  121.947 1.00 28.34 ?  167 LEU C CD1   1 
ATOM   12340 C  CD2   . LEU C 2 188 ? 98.297  92.265  120.483 1.00 27.90 ?  167 LEU C CD2   1 
ATOM   12341 N  N     . PHE C 2 189 ? 101.672 96.272  118.653 1.00 26.79 ?  168 PHE C N     1 
ATOM   12342 C  CA    . PHE C 2 189 ? 102.092 97.671  118.718 1.00 26.90 ?  168 PHE C CA    1 
ATOM   12343 C  C     . PHE C 2 189 ? 101.310 98.535  117.722 1.00 26.52 ?  168 PHE C C     1 
ATOM   12344 O  O     . PHE C 2 189 ? 101.232 99.761  117.878 1.00 26.02 ?  168 PHE C O     1 
ATOM   12345 C  CB    . PHE C 2 189 ? 103.596 97.820  118.410 1.00 27.03 ?  168 PHE C CB    1 
ATOM   12346 C  CG    . PHE C 2 189 ? 104.518 97.645  119.614 1.00 28.09 ?  168 PHE C CG    1 
ATOM   12347 C  CD1   . PHE C 2 189 ? 104.367 98.420  120.766 1.00 28.69 ?  168 PHE C CD1   1 
ATOM   12348 C  CD2   . PHE C 2 189 ? 105.584 96.756  119.558 1.00 29.15 ?  168 PHE C CD2   1 
ATOM   12349 C  CE1   . PHE C 2 189 ? 105.228 98.274  121.864 1.00 28.50 ?  168 PHE C CE1   1 
ATOM   12350 C  CE2   . PHE C 2 189 ? 106.459 96.597  120.649 1.00 30.19 ?  168 PHE C CE2   1 
ATOM   12351 C  CZ    . PHE C 2 189 ? 106.273 97.365  121.812 1.00 29.81 ?  168 PHE C CZ    1 
ATOM   12352 N  N     . TYR C 2 190 ? 100.750 97.906  116.688 1.00 26.18 ?  169 TYR C N     1 
ATOM   12353 C  CA    . TYR C 2 190 ? 100.309 98.676  115.530 1.00 26.24 ?  169 TYR C CA    1 
ATOM   12354 C  C     . TYR C 2 190 ? 98.980  99.434  115.677 1.00 25.94 ?  169 TYR C C     1 
ATOM   12355 O  O     . TYR C 2 190 ? 98.758  100.440 115.001 1.00 25.71 ?  169 TYR C O     1 
ATOM   12356 C  CB    . TYR C 2 190 ? 100.438 97.847  114.251 1.00 27.13 ?  169 TYR C CB    1 
ATOM   12357 C  CG    . TYR C 2 190 ? 101.893 97.781  113.838 1.00 28.07 ?  169 TYR C CG    1 
ATOM   12358 C  CD1   . TYR C 2 190 ? 102.757 96.828  114.390 1.00 29.54 ?  169 TYR C CD1   1 
ATOM   12359 C  CD2   . TYR C 2 190 ? 102.426 98.717  112.950 1.00 29.31 ?  169 TYR C CD2   1 
ATOM   12360 C  CE1   . TYR C 2 190 ? 104.109 96.787  114.034 1.00 30.44 ?  169 TYR C CE1   1 
ATOM   12361 C  CE2   . TYR C 2 190 ? 103.781 98.683  112.585 1.00 30.64 ?  169 TYR C CE2   1 
ATOM   12362 C  CZ    . TYR C 2 190 ? 104.614 97.718  113.136 1.00 30.40 ?  169 TYR C CZ    1 
ATOM   12363 O  OH    . TYR C 2 190 ? 105.946 97.686  112.789 1.00 28.85 ?  169 TYR C OH    1 
ATOM   12364 N  N     . SER C 2 191 ? 98.133  98.986  116.600 1.00 25.17 ?  170 SER C N     1 
ATOM   12365 C  CA    . SER C 2 191 ? 96.918  99.722  116.937 1.00 25.10 ?  170 SER C CA    1 
ATOM   12366 C  C     . SER C 2 191 ? 97.314  101.064 117.566 1.00 25.16 ?  170 SER C C     1 
ATOM   12367 O  O     . SER C 2 191 ? 96.590  102.056 117.433 1.00 25.30 ?  170 SER C O     1 
ATOM   12368 C  CB    . SER C 2 191 ? 96.028  98.910  117.878 1.00 24.56 ?  170 SER C CB    1 
ATOM   12369 O  OG    . SER C 2 191 ? 96.659  98.697  119.126 1.00 24.98 ?  170 SER C OG    1 
ATOM   12370 N  N     . GLY C 2 192 ? 98.473  101.064 118.235 1.00 24.32 ?  171 GLY C N     1 
ATOM   12371 C  CA    . GLY C 2 192 ? 99.080  102.253 118.818 1.00 23.97 ?  171 GLY C CA    1 
ATOM   12372 C  C     . GLY C 2 192 ? 99.843  103.102 117.816 1.00 23.85 ?  171 GLY C C     1 
ATOM   12373 O  O     . GLY C 2 192 ? 99.608  104.309 117.744 1.00 23.99 ?  171 GLY C O     1 
ATOM   12374 N  N     . PHE C 2 193 ? 100.730 102.482 117.036 1.00 23.28 ?  172 PHE C N     1 
ATOM   12375 C  CA    . PHE C 2 193 ? 101.532 103.197 116.026 1.00 23.85 ?  172 PHE C CA    1 
ATOM   12376 C  C     . PHE C 2 193 ? 100.705 103.955 114.987 1.00 23.72 ?  172 PHE C C     1 
ATOM   12377 O  O     . PHE C 2 193 ? 101.176 104.949 114.438 1.00 23.92 ?  172 PHE C O     1 
ATOM   12378 C  CB    . PHE C 2 193 ? 102.471 102.252 115.263 1.00 23.47 ?  172 PHE C CB    1 
ATOM   12379 C  CG    . PHE C 2 193 ? 103.666 101.778 116.060 1.00 24.32 ?  172 PHE C CG    1 
ATOM   12380 C  CD1   . PHE C 2 193 ? 104.152 102.512 117.143 1.00 22.28 ?  172 PHE C CD1   1 
ATOM   12381 C  CD2   . PHE C 2 193 ? 104.321 100.599 115.699 1.00 23.82 ?  172 PHE C CD2   1 
ATOM   12382 C  CE1   . PHE C 2 193 ? 105.260 102.071 117.878 1.00 23.41 ?  172 PHE C CE1   1 
ATOM   12383 C  CE2   . PHE C 2 193 ? 105.435 100.141 116.424 1.00 24.70 ?  172 PHE C CE2   1 
ATOM   12384 C  CZ    . PHE C 2 193 ? 105.909 100.884 117.516 1.00 24.87 ?  172 PHE C CZ    1 
ATOM   12385 N  N     . TYR C 2 194 ? 99.496  103.469 114.699 1.00 23.31 ?  173 TYR C N     1 
ATOM   12386 C  CA    . TYR C 2 194 ? 98.655  104.060 113.655 1.00 23.26 ?  173 TYR C CA    1 
ATOM   12387 C  C     . TYR C 2 194 ? 98.539  105.579 113.808 1.00 23.04 ?  173 TYR C C     1 
ATOM   12388 O  O     . TYR C 2 194 ? 98.695  106.324 112.836 1.00 23.47 ?  173 TYR C O     1 
ATOM   12389 C  CB    . TYR C 2 194 ? 97.246  103.441 113.635 1.00 23.13 ?  173 TYR C CB    1 
ATOM   12390 C  CG    . TYR C 2 194 ? 96.379  103.956 112.494 1.00 24.10 ?  173 TYR C CG    1 
ATOM   12391 C  CD1   . TYR C 2 194 ? 96.306  103.262 111.285 1.00 25.72 ?  173 TYR C CD1   1 
ATOM   12392 C  CD2   . TYR C 2 194 ? 95.656  105.144 112.614 1.00 27.04 ?  173 TYR C CD2   1 
ATOM   12393 C  CE1   . TYR C 2 194 ? 95.514  103.729 110.227 1.00 28.94 ?  173 TYR C CE1   1 
ATOM   12394 C  CE2   . TYR C 2 194 ? 94.866  105.628 111.554 1.00 27.84 ?  173 TYR C CE2   1 
ATOM   12395 C  CZ    . TYR C 2 194 ? 94.806  104.911 110.369 1.00 29.97 ?  173 TYR C CZ    1 
ATOM   12396 O  OH    . TYR C 2 194 ? 94.044  105.374 109.311 1.00 34.34 ?  173 TYR C OH    1 
ATOM   12397 N  N     . TYR C 2 195 ? 98.259  106.025 115.023 1.00 22.51 ?  174 TYR C N     1 
ATOM   12398 C  CA    . TYR C 2 195 ? 97.853  107.409 115.243 1.00 22.60 ?  174 TYR C CA    1 
ATOM   12399 C  C     . TYR C 2 195 ? 99.009  108.418 115.109 1.00 22.64 ?  174 TYR C C     1 
ATOM   12400 O  O     . TYR C 2 195 ? 98.844  109.424 114.411 1.00 22.39 ?  174 TYR C O     1 
ATOM   12401 C  CB    . TYR C 2 195 ? 97.098  107.540 116.566 1.00 22.32 ?  174 TYR C CB    1 
ATOM   12402 C  CG    . TYR C 2 195 ? 96.045  108.630 116.593 1.00 23.39 ?  174 TYR C CG    1 
ATOM   12403 C  CD1   . TYR C 2 195 ? 95.324  108.981 115.440 1.00 22.84 ?  174 TYR C CD1   1 
ATOM   12404 C  CD2   . TYR C 2 195 ? 95.742  109.283 117.785 1.00 22.23 ?  174 TYR C CD2   1 
ATOM   12405 C  CE1   . TYR C 2 195 ? 94.346  109.982 115.480 1.00 24.05 ?  174 TYR C CE1   1 
ATOM   12406 C  CE2   . TYR C 2 195 ? 94.758  110.273 117.839 1.00 24.11 ?  174 TYR C CE2   1 
ATOM   12407 C  CZ    . TYR C 2 195 ? 94.067  110.613 116.689 1.00 23.92 ?  174 TYR C CZ    1 
ATOM   12408 O  OH    . TYR C 2 195 ? 93.122  111.601 116.754 1.00 25.00 ?  174 TYR C OH    1 
ATOM   12409 N  N     . PRO C 2 196 ? 100.182 108.147 115.754 1.00 22.25 ?  175 PRO C N     1 
ATOM   12410 C  CA    . PRO C 2 196 ? 101.344 109.009 115.484 1.00 22.45 ?  175 PRO C CA    1 
ATOM   12411 C  C     . PRO C 2 196 ? 101.723 109.050 114.004 1.00 22.59 ?  175 PRO C C     1 
ATOM   12412 O  O     . PRO C 2 196 ? 102.101 110.116 113.505 1.00 22.19 ?  175 PRO C O     1 
ATOM   12413 C  CB    . PRO C 2 196 ? 102.478 108.376 116.304 1.00 22.25 ?  175 PRO C CB    1 
ATOM   12414 C  CG    . PRO C 2 196 ? 101.807 107.558 117.357 1.00 22.22 ?  175 PRO C CG    1 
ATOM   12415 C  CD    . PRO C 2 196 ? 100.483 107.121 116.780 1.00 22.32 ?  175 PRO C CD    1 
ATOM   12416 N  N     . LEU C 2 197 ? 101.615 107.911 113.311 1.00 21.92 ?  176 LEU C N     1 
ATOM   12417 C  CA    . LEU C 2 197 ? 101.911 107.856 111.878 1.00 22.35 ?  176 LEU C CA    1 
ATOM   12418 C  C     . LEU C 2 197 ? 100.886 108.654 111.065 1.00 22.60 ?  176 LEU C C     1 
ATOM   12419 O  O     . LEU C 2 197 ? 101.233 109.328 110.091 1.00 22.41 ?  176 LEU C O     1 
ATOM   12420 C  CB    . LEU C 2 197 ? 101.950 106.416 111.370 1.00 22.69 ?  176 LEU C CB    1 
ATOM   12421 C  CG    . LEU C 2 197 ? 103.019 105.440 111.881 1.00 23.68 ?  176 LEU C CG    1 
ATOM   12422 C  CD1   . LEU C 2 197 ? 102.807 104.062 111.233 1.00 23.70 ?  176 LEU C CD1   1 
ATOM   12423 C  CD2   . LEU C 2 197 ? 104.423 105.961 111.591 1.00 23.09 ?  176 LEU C CD2   1 
ATOM   12424 N  N     . TYR C 2 198 ? 99.624  108.566 111.479 1.00 22.64 ?  177 TYR C N     1 
ATOM   12425 C  CA    . TYR C 2 198 ? 98.527  109.263 110.822 1.00 22.92 ?  177 TYR C CA    1 
ATOM   12426 C  C     . TYR C 2 198 ? 98.759  110.783 110.896 1.00 23.68 ?  177 TYR C C     1 
ATOM   12427 O  O     . TYR C 2 198 ? 98.584  111.498 109.906 1.00 23.81 ?  177 TYR C O     1 
ATOM   12428 C  CB    . TYR C 2 198 ? 97.221  108.844 111.490 1.00 22.73 ?  177 TYR C CB    1 
ATOM   12429 C  CG    . TYR C 2 198 ? 95.955  109.486 110.991 1.00 22.91 ?  177 TYR C CG    1 
ATOM   12430 C  CD1   . TYR C 2 198 ? 95.393  109.106 109.772 1.00 23.49 ?  177 TYR C CD1   1 
ATOM   12431 C  CD2   . TYR C 2 198 ? 95.281  110.427 111.771 1.00 21.97 ?  177 TYR C CD2   1 
ATOM   12432 C  CE1   . TYR C 2 198 ? 94.202  109.674 109.319 1.00 23.57 ?  177 TYR C CE1   1 
ATOM   12433 C  CE2   . TYR C 2 198 ? 94.078  111.004 111.328 1.00 22.54 ?  177 TYR C CE2   1 
ATOM   12434 C  CZ    . TYR C 2 198 ? 93.553  110.624 110.102 1.00 22.88 ?  177 TYR C CZ    1 
ATOM   12435 O  OH    . TYR C 2 198 ? 92.366  111.171 109.650 1.00 23.17 ?  177 TYR C OH    1 
ATOM   12436 N  N     . PHE C 2 199 ? 99.198  111.267 112.053 1.00 23.50 ?  178 PHE C N     1 
ATOM   12437 C  CA    . PHE C 2 199 ? 99.540  112.683 112.191 1.00 24.60 ?  178 PHE C CA    1 
ATOM   12438 C  C     . PHE C 2 199 ? 100.814 113.100 111.444 1.00 24.72 ?  178 PHE C C     1 
ATOM   12439 O  O     . PHE C 2 199 ? 100.829 114.116 110.751 1.00 24.19 ?  178 PHE C O     1 
ATOM   12440 C  CB    . PHE C 2 199 ? 99.616  113.080 113.668 1.00 24.35 ?  178 PHE C CB    1 
ATOM   12441 C  CG    . PHE C 2 199 ? 98.272  113.229 114.315 1.00 26.36 ?  178 PHE C CG    1 
ATOM   12442 C  CD1   . PHE C 2 199 ? 97.246  113.924 113.674 1.00 28.53 ?  178 PHE C CD1   1 
ATOM   12443 C  CD2   . PHE C 2 199 ? 98.028  112.694 115.572 1.00 28.23 ?  178 PHE C CD2   1 
ATOM   12444 C  CE1   . PHE C 2 199 ? 95.989  114.062 114.273 1.00 29.37 ?  178 PHE C CE1   1 
ATOM   12445 C  CE2   . PHE C 2 199 ? 96.770  112.840 116.183 1.00 28.69 ?  178 PHE C CE2   1 
ATOM   12446 C  CZ    . PHE C 2 199 ? 95.760  113.518 115.534 1.00 28.43 ?  178 PHE C CZ    1 
ATOM   12447 N  N     . TYR C 2 200 ? 101.872 112.305 111.588 1.00 25.36 ?  179 TYR C N     1 
ATOM   12448 C  CA    . TYR C 2 200 ? 103.144 112.539 110.893 1.00 26.02 ?  179 TYR C CA    1 
ATOM   12449 C  C     . TYR C 2 200 ? 102.898 112.729 109.396 1.00 26.57 ?  179 TYR C C     1 
ATOM   12450 O  O     . TYR C 2 200 ? 103.436 113.651 108.774 1.00 26.30 ?  179 TYR C O     1 
ATOM   12451 C  CB    . TYR C 2 200 ? 104.092 111.353 111.115 1.00 26.19 ?  179 TYR C CB    1 
ATOM   12452 C  CG    . TYR C 2 200 ? 105.507 111.574 110.629 1.00 27.82 ?  179 TYR C CG    1 
ATOM   12453 C  CD1   . TYR C 2 200 ? 105.939 111.033 109.414 1.00 30.77 ?  179 TYR C CD1   1 
ATOM   12454 C  CD2   . TYR C 2 200 ? 106.418 112.315 111.384 1.00 29.20 ?  179 TYR C CD2   1 
ATOM   12455 C  CE1   . TYR C 2 200 ? 107.239 111.230 108.962 1.00 31.82 ?  179 TYR C CE1   1 
ATOM   12456 C  CE2   . TYR C 2 200 ? 107.718 112.520 110.945 1.00 30.44 ?  179 TYR C CE2   1 
ATOM   12457 C  CZ    . TYR C 2 200 ? 108.122 111.973 109.731 1.00 32.74 ?  179 TYR C CZ    1 
ATOM   12458 O  OH    . TYR C 2 200 ? 109.401 112.172 109.274 1.00 34.58 ?  179 TYR C OH    1 
ATOM   12459 N  N     . GLY C 2 201 ? 102.057 111.861 108.837 1.00 26.71 ?  180 GLY C N     1 
ATOM   12460 C  CA    . GLY C 2 201 ? 101.722 111.897 107.420 1.00 27.38 ?  180 GLY C CA    1 
ATOM   12461 C  C     . GLY C 2 201 ? 100.970 113.140 106.972 1.00 27.62 ?  180 GLY C C     1 
ATOM   12462 O  O     . GLY C 2 201 ? 100.936 113.428 105.787 1.00 28.25 ?  180 GLY C O     1 
ATOM   12463 N  N     . GLN C 2 202 ? 100.376 113.868 107.917 1.00 27.60 ?  181 GLN C N     1 
ATOM   12464 C  CA    . GLN C 2 202 ? 99.671  115.130 107.630 1.00 28.24 ?  181 GLN C CA    1 
ATOM   12465 C  C     . GLN C 2 202 ? 100.516 116.340 107.997 1.00 28.30 ?  181 GLN C C     1 
ATOM   12466 O  O     . GLN C 2 202 ? 100.026 117.471 107.941 1.00 27.98 ?  181 GLN C O     1 
ATOM   12467 C  CB    . GLN C 2 202 ? 98.378  115.237 108.442 1.00 27.90 ?  181 GLN C CB    1 
ATOM   12468 C  CG    . GLN C 2 202 ? 97.348  114.185 108.180 1.00 29.54 ?  181 GLN C CG    1 
ATOM   12469 C  CD    . GLN C 2 202 ? 96.172  114.313 109.121 1.00 31.54 ?  181 GLN C CD    1 
ATOM   12470 O  OE1   . GLN C 2 202 ? 95.386  115.260 109.028 1.00 32.11 ?  181 GLN C OE1   1 
ATOM   12471 N  NE2   . GLN C 2 202 ? 96.048  113.367 110.043 1.00 31.29 ?  181 GLN C NE2   1 
ATOM   12472 N  N     . GLY C 2 203 ? 101.757 116.095 108.417 1.00 28.14 ?  182 GLY C N     1 
ATOM   12473 C  CA    . GLY C 2 203 ? 102.660 117.152 108.845 1.00 28.38 ?  182 GLY C CA    1 
ATOM   12474 C  C     . GLY C 2 203 ? 102.343 117.680 110.228 1.00 28.71 ?  182 GLY C C     1 
ATOM   12475 O  O     . GLY C 2 203 ? 102.583 118.849 110.513 1.00 28.80 ?  182 GLY C O     1 
ATOM   12476 N  N     . LYS C 2 204 ? 101.790 116.818 111.080 1.00 28.24 ?  183 LYS C N     1 
ATOM   12477 C  CA    . LYS C 2 204 ? 101.419 117.196 112.434 1.00 28.48 ?  183 LYS C CA    1 
ATOM   12478 C  C     . LYS C 2 204 ? 102.148 116.320 113.448 1.00 27.82 ?  183 LYS C C     1 
ATOM   12479 O  O     . LYS C 2 204 ? 102.356 115.121 113.213 1.00 26.73 ?  183 LYS C O     1 
ATOM   12480 C  CB    . LYS C 2 204 ? 99.907  117.088 112.637 1.00 29.13 ?  183 LYS C CB    1 
ATOM   12481 C  CG    . LYS C 2 204 ? 99.091  118.070 111.797 1.00 30.41 ?  183 LYS C CG    1 
ATOM   12482 C  CD    . LYS C 2 204 ? 97.668  117.568 111.604 1.00 33.74 ?  183 LYS C CD    1 
ATOM   12483 C  CE    . LYS C 2 204 ? 96.822  118.590 110.828 1.00 36.26 ?  183 LYS C CE    1 
ATOM   12484 N  NZ    . LYS C 2 204 ? 95.421  118.101 110.675 1.00 39.17 1  183 LYS C NZ    1 
ATOM   12485 N  N     . LEU C 2 205 ? 102.529 116.929 114.570 1.00 27.77 ?  184 LEU C N     1 
ATOM   12486 C  CA    . LEU C 2 205 ? 103.266 116.244 115.639 1.00 27.79 ?  184 LEU C CA    1 
ATOM   12487 C  C     . LEU C 2 205 ? 104.484 115.496 115.090 1.00 27.85 ?  184 LEU C C     1 
ATOM   12488 O  O     . LEU C 2 205 ? 104.700 114.306 115.361 1.00 27.07 ?  184 LEU C O     1 
ATOM   12489 C  CB    . LEU C 2 205 ? 102.334 115.304 116.431 1.00 27.76 ?  184 LEU C CB    1 
ATOM   12490 C  CG    . LEU C 2 205 ? 101.090 115.961 117.045 1.00 28.62 ?  184 LEU C CG    1 
ATOM   12491 C  CD1   . LEU C 2 205 ? 100.187 114.925 117.684 1.00 29.18 ?  184 LEU C CD1   1 
ATOM   12492 C  CD2   . LEU C 2 205 ? 101.473 117.025 118.063 1.00 28.43 ?  184 LEU C CD2   1 
ATOM   12493 N  N     . MET C 2 206 ? 105.297 116.208 114.325 1.00 28.15 ?  185 MET C N     1 
ATOM   12494 C  CA    . MET C 2 206 ? 106.343 115.549 113.576 1.00 28.80 ?  185 MET C CA    1 
ATOM   12495 C  C     . MET C 2 206 ? 107.572 115.165 114.390 1.00 28.77 ?  185 MET C C     1 
ATOM   12496 O  O     . MET C 2 206 ? 108.287 114.241 114.011 1.00 28.79 ?  185 MET C O     1 
ATOM   12497 C  CB    . MET C 2 206 ? 106.693 116.365 112.347 1.00 29.96 ?  185 MET C CB    1 
ATOM   12498 C  CG    . MET C 2 206 ? 105.534 116.381 111.344 1.00 31.23 ?  185 MET C CG    1 
ATOM   12499 S  SD    . MET C 2 206 ? 106.112 116.868 109.741 1.00 40.10 ?  185 MET C SD    1 
ATOM   12500 C  CE    . MET C 2 206 ? 107.022 115.426 109.223 1.00 35.10 ?  185 MET C CE    1 
ATOM   12501 N  N     . GLN C 2 207 ? 107.801 115.842 115.511 1.00 28.62 ?  186 GLN C N     1 
ATOM   12502 C  CA    . GLN C 2 207 ? 108.930 115.495 116.382 1.00 29.10 ?  186 GLN C CA    1 
ATOM   12503 C  C     . GLN C 2 207 ? 108.633 114.217 117.171 1.00 28.52 ?  186 GLN C C     1 
ATOM   12504 O  O     . GLN C 2 207 ? 109.458 113.306 117.194 1.00 28.28 ?  186 GLN C O     1 
ATOM   12505 C  CB    . GLN C 2 207 ? 109.306 116.650 117.316 1.00 29.21 ?  186 GLN C CB    1 
ATOM   12506 C  CG    . GLN C 2 207 ? 109.801 117.903 116.592 1.00 31.41 ?  186 GLN C CG    1 
ATOM   12507 C  CD    . GLN C 2 207 ? 111.100 117.670 115.847 1.00 34.70 ?  186 GLN C CD    1 
ATOM   12508 O  OE1   . GLN C 2 207 ? 111.096 117.321 114.670 1.00 37.69 ?  186 GLN C OE1   1 
ATOM   12509 N  NE2   . GLN C 2 207 ? 112.221 117.832 116.540 1.00 34.75 ?  186 GLN C NE2   1 
ATOM   12510 N  N     . SER C 2 208 ? 107.454 114.163 117.803 1.00 28.38 ?  187 SER C N     1 
ATOM   12511 C  CA    . SER C 2 208 ? 106.936 112.938 118.425 1.00 28.25 ?  187 SER C CA    1 
ATOM   12512 C  C     . SER C 2 208 ? 106.906 111.813 117.397 1.00 28.00 ?  187 SER C C     1 
ATOM   12513 O  O     . SER C 2 208 ? 107.267 110.676 117.705 1.00 27.90 ?  187 SER C O     1 
ATOM   12514 C  CB    . SER C 2 208 ? 105.512 113.147 118.942 1.00 27.88 ?  187 SER C CB    1 
ATOM   12515 O  OG    . SER C 2 208 ? 105.458 114.146 119.939 1.00 30.27 ?  187 SER C OG    1 
ATOM   12516 N  N     . GLY C 2 209 ? 106.460 112.147 116.182 1.00 27.31 ?  188 GLY C N     1 
ATOM   12517 C  CA    . GLY C 2 209 ? 106.390 111.198 115.074 1.00 27.86 ?  188 GLY C CA    1 
ATOM   12518 C  C     . GLY C 2 209 ? 107.741 110.637 114.672 1.00 27.96 ?  188 GLY C C     1 
ATOM   12519 O  O     . GLY C 2 209 ? 107.846 109.464 114.295 1.00 27.84 ?  188 GLY C O     1 
ATOM   12520 N  N     . GLU C 2 210 ? 108.776 111.475 114.749 1.00 28.21 ?  189 GLU C N     1 
ATOM   12521 C  CA    . GLU C 2 210 ? 110.143 111.045 114.473 1.00 29.15 ?  189 GLU C CA    1 
ATOM   12522 C  C     . GLU C 2 210 ? 110.602 109.988 115.497 1.00 28.02 ?  189 GLU C C     1 
ATOM   12523 O  O     . GLU C 2 210 ? 111.216 108.980 115.140 1.00 27.15 ?  189 GLU C O     1 
ATOM   12524 C  CB    . GLU C 2 210 ? 111.084 112.252 114.474 1.00 30.17 ?  189 GLU C CB    1 
ATOM   12525 C  CG    . GLU C 2 210 ? 111.987 112.344 113.254 1.00 35.68 ?  189 GLU C CG    1 
ATOM   12526 C  CD    . GLU C 2 210 ? 111.266 112.893 112.019 1.00 40.25 ?  189 GLU C CD    1 
ATOM   12527 O  OE1   . GLU C 2 210 ? 110.795 114.055 112.037 1.00 42.98 ?  189 GLU C OE1   1 
ATOM   12528 O  OE2   . GLU C 2 210 ? 111.181 112.161 111.014 1.00 43.59 -1 189 GLU C OE2   1 
ATOM   12529 N  N     . ILE C 2 211 ? 110.297 110.226 116.770 1.00 27.57 ?  190 ILE C N     1 
ATOM   12530 C  CA    . ILE C 2 211 ? 110.568 109.245 117.827 1.00 27.47 ?  190 ILE C CA    1 
ATOM   12531 C  C     . ILE C 2 211 ? 109.872 107.911 117.541 1.00 26.69 ?  190 ILE C C     1 
ATOM   12532 O  O     . ILE C 2 211 ? 110.496 106.842 117.564 1.00 26.56 ?  190 ILE C O     1 
ATOM   12533 C  CB    . ILE C 2 211 ? 110.173 109.802 119.228 1.00 27.84 ?  190 ILE C CB    1 
ATOM   12534 C  CG1   . ILE C 2 211 ? 111.159 110.904 119.645 1.00 28.56 ?  190 ILE C CG1   1 
ATOM   12535 C  CG2   . ILE C 2 211 ? 110.106 108.662 120.271 1.00 27.27 ?  190 ILE C CG2   1 
ATOM   12536 C  CD1   . ILE C 2 211 ? 110.904 111.491 121.029 1.00 30.09 ?  190 ILE C CD1   1 
ATOM   12537 N  N     . ILE C 2 212 ? 108.583 107.986 117.230 1.00 26.33 ?  191 ILE C N     1 
ATOM   12538 C  CA    . ILE C 2 212 ? 107.777 106.803 116.944 1.00 25.96 ?  191 ILE C CA    1 
ATOM   12539 C  C     . ILE C 2 212 ? 108.321 106.005 115.751 1.00 25.46 ?  191 ILE C C     1 
ATOM   12540 O  O     . ILE C 2 212 ? 108.347 104.778 115.799 1.00 24.84 ?  191 ILE C O     1 
ATOM   12541 C  CB    . ILE C 2 212 ? 106.274 107.173 116.754 1.00 26.00 ?  191 ILE C CB    1 
ATOM   12542 C  CG1   . ILE C 2 212 ? 105.682 107.714 118.066 1.00 27.16 ?  191 ILE C CG1   1 
ATOM   12543 C  CG2   . ILE C 2 212 ? 105.457 105.992 116.248 1.00 26.87 ?  191 ILE C CG2   1 
ATOM   12544 C  CD1   . ILE C 2 212 ? 105.652 106.721 119.214 1.00 29.84 ?  191 ILE C CD1   1 
ATOM   12545 N  N     . ASN C 2 213 ? 108.753 106.698 114.694 1.00 25.35 ?  192 ASN C N     1 
ATOM   12546 C  CA    . ASN C 2 213 ? 109.360 106.036 113.533 1.00 25.60 ?  192 ASN C CA    1 
ATOM   12547 C  C     . ASN C 2 213 ? 110.648 105.299 113.884 1.00 25.14 ?  192 ASN C C     1 
ATOM   12548 O  O     . ASN C 2 213 ? 110.929 104.216 113.346 1.00 25.61 ?  192 ASN C O     1 
ATOM   12549 C  CB    . ASN C 2 213 ? 109.626 107.030 112.394 1.00 26.55 ?  192 ASN C CB    1 
ATOM   12550 C  CG    . ASN C 2 213 ? 108.427 107.209 111.489 1.00 28.10 ?  192 ASN C CG    1 
ATOM   12551 O  OD1   . ASN C 2 213 ? 107.977 106.265 110.831 1.00 31.67 ?  192 ASN C OD1   1 
ATOM   12552 N  ND2   . ASN C 2 213 ? 107.908 108.423 111.440 1.00 30.36 ?  192 ASN C ND2   1 
ATOM   12553 N  N     . LEU C 2 214 ? 111.429 105.880 114.787 1.00 24.54 ?  193 LEU C N     1 
ATOM   12554 C  CA    . LEU C 2 214 ? 112.639 105.212 115.272 1.00 24.40 ?  193 LEU C CA    1 
ATOM   12555 C  C     . LEU C 2 214 ? 112.292 103.957 116.075 1.00 23.55 ?  193 LEU C C     1 
ATOM   12556 O  O     . LEU C 2 214 ? 112.905 102.904 115.879 1.00 23.09 ?  193 LEU C O     1 
ATOM   12557 C  CB    . LEU C 2 214 ? 113.519 106.176 116.064 1.00 24.00 ?  193 LEU C CB    1 
ATOM   12558 C  CG    . LEU C 2 214 ? 114.244 107.255 115.230 1.00 25.69 ?  193 LEU C CG    1 
ATOM   12559 C  CD1   . LEU C 2 214 ? 114.855 108.338 116.119 1.00 26.28 ?  193 LEU C CD1   1 
ATOM   12560 C  CD2   . LEU C 2 214 ? 115.331 106.650 114.338 1.00 26.05 ?  193 LEU C CD2   1 
ATOM   12561 N  N     . ILE C 2 215 ? 111.300 104.069 116.962 1.00 23.19 ?  194 ILE C N     1 
ATOM   12562 C  CA    . ILE C 2 215 ? 110.779 102.916 117.705 1.00 22.88 ?  194 ILE C CA    1 
ATOM   12563 C  C     . ILE C 2 215 ? 110.294 101.842 116.717 1.00 23.81 ?  194 ILE C C     1 
ATOM   12564 O  O     . ILE C 2 215 ? 110.649 100.670 116.848 1.00 23.83 ?  194 ILE C O     1 
ATOM   12565 C  CB    . ILE C 2 215 ? 109.641 103.316 118.686 1.00 22.92 ?  194 ILE C CB    1 
ATOM   12566 C  CG1   . ILE C 2 215 ? 110.153 104.314 119.727 1.00 21.11 ?  194 ILE C CG1   1 
ATOM   12567 C  CG2   . ILE C 2 215 ? 109.023 102.086 119.370 1.00 21.89 ?  194 ILE C CG2   1 
ATOM   12568 C  CD1   . ILE C 2 215 ? 109.101 104.780 120.712 1.00 22.26 ?  194 ILE C CD1   1 
ATOM   12569 N  N     . LEU C 2 216 ? 109.523 102.247 115.707 1.00 24.23 ?  195 LEU C N     1 
ATOM   12570 C  CA    . LEU C 2 216 ? 108.966 101.292 114.741 1.00 25.41 ?  195 LEU C CA    1 
ATOM   12571 C  C     . LEU C 2 216 ? 110.061 100.588 113.937 1.00 25.63 ?  195 LEU C C     1 
ATOM   12572 O  O     . LEU C 2 216 ? 109.994 99.369  113.715 1.00 25.46 ?  195 LEU C O     1 
ATOM   12573 C  CB    . LEU C 2 216 ? 107.955 101.984 113.807 1.00 26.03 ?  195 LEU C CB    1 
ATOM   12574 C  CG    . LEU C 2 216 ? 107.197 101.181 112.742 1.00 28.00 ?  195 LEU C CG    1 
ATOM   12575 C  CD1   . LEU C 2 216 ? 105.941 101.943 112.352 1.00 31.45 ?  195 LEU C CD1   1 
ATOM   12576 C  CD2   . LEU C 2 216 ? 108.056 100.889 111.506 1.00 29.83 ?  195 LEU C CD2   1 
ATOM   12577 N  N     . ARG C 2 217 ? 111.061 101.354 113.511 1.00 25.98 ?  196 ARG C N     1 
ATOM   12578 C  CA    . ARG C 2 217 ? 112.224 100.808 112.820 1.00 26.73 ?  196 ARG C CA    1 
ATOM   12579 C  C     . ARG C 2 217 ? 112.903 99.704  113.670 1.00 25.95 ?  196 ARG C C     1 
ATOM   12580 O  O     . ARG C 2 217 ? 113.249 98.647  113.132 1.00 25.75 ?  196 ARG C O     1 
ATOM   12581 C  CB    . ARG C 2 217 ? 113.209 101.930 112.486 1.00 27.29 ?  196 ARG C CB    1 
ATOM   12582 C  CG    . ARG C 2 217 ? 114.344 101.552 111.524 1.00 30.12 ?  196 ARG C CG    1 
ATOM   12583 C  CD    . ARG C 2 217 ? 115.576 102.378 111.842 1.00 35.40 ?  196 ARG C CD    1 
ATOM   12584 N  NE    . ARG C 2 217 ? 115.768 102.387 113.293 1.00 39.87 ?  196 ARG C NE    1 
ATOM   12585 C  CZ    . ARG C 2 217 ? 116.594 103.177 113.967 1.00 40.55 ?  196 ARG C CZ    1 
ATOM   12586 N  NH1   . ARG C 2 217 ? 117.363 104.066 113.338 1.00 40.77 1  196 ARG C NH1   1 
ATOM   12587 N  NH2   . ARG C 2 217 ? 116.640 103.070 115.289 1.00 41.10 ?  196 ARG C NH2   1 
ATOM   12588 N  N     . ASP C 2 218 ? 113.070 99.952  114.974 1.00 24.70 ?  197 ASP C N     1 
ATOM   12589 C  CA    . ASP C 2 218 ? 113.598 98.942  115.914 1.00 24.55 ?  197 ASP C CA    1 
ATOM   12590 C  C     . ASP C 2 218 ? 112.685 97.703  116.002 1.00 24.23 ?  197 ASP C C     1 
ATOM   12591 O  O     . ASP C 2 218 ? 113.162 96.573  115.859 1.00 23.69 ?  197 ASP C O     1 
ATOM   12592 C  CB    . ASP C 2 218 ? 113.812 99.507  117.334 1.00 24.50 ?  197 ASP C CB    1 
ATOM   12593 C  CG    . ASP C 2 218 ? 114.923 100.570 117.418 1.00 25.84 ?  197 ASP C CG    1 
ATOM   12594 O  OD1   . ASP C 2 218 ? 115.845 100.599 116.573 1.00 26.91 ?  197 ASP C OD1   1 
ATOM   12595 O  OD2   . ASP C 2 218 ? 114.879 101.377 118.367 1.00 25.72 -1 197 ASP C OD2   1 
ATOM   12596 N  N     . GLU C 2 219 ? 111.380 97.908  116.210 1.00 23.92 ?  198 GLU C N     1 
ATOM   12597 C  CA    . GLU C 2 219 ? 110.481 96.760  116.413 1.00 24.20 ?  198 GLU C CA    1 
ATOM   12598 C  C     . GLU C 2 219 ? 110.429 95.865  115.188 1.00 24.02 ?  198 GLU C C     1 
ATOM   12599 O  O     . GLU C 2 219 ? 110.318 94.653  115.331 1.00 24.24 ?  198 GLU C O     1 
ATOM   12600 C  CB    . GLU C 2 219 ? 109.056 97.160  116.808 1.00 24.05 ?  198 GLU C CB    1 
ATOM   12601 C  CG    . GLU C 2 219 ? 108.910 98.321  117.774 1.00 25.03 ?  198 GLU C CG    1 
ATOM   12602 C  CD    . GLU C 2 219 ? 109.334 98.054  119.232 1.00 26.31 ?  198 GLU C CD    1 
ATOM   12603 O  OE1   . GLU C 2 219 ? 110.169 97.151  119.531 1.00 27.65 ?  198 GLU C OE1   1 
ATOM   12604 O  OE2   . GLU C 2 219 ? 108.822 98.815  120.099 1.00 26.87 -1 198 GLU C OE2   1 
ATOM   12605 N  N     . ALA C 2 220 ? 110.507 96.457  113.995 1.00 24.00 ?  199 ALA C N     1 
ATOM   12606 C  CA    . ALA C 2 220 ? 110.514 95.679  112.761 1.00 24.72 ?  199 ALA C CA    1 
ATOM   12607 C  C     . ALA C 2 220 ? 111.668 94.664  112.727 1.00 24.80 ?  199 ALA C C     1 
ATOM   12608 O  O     . ALA C 2 220 ? 111.457 93.497  112.382 1.00 25.04 ?  199 ALA C O     1 
ATOM   12609 C  CB    . ALA C 2 220 ? 110.546 96.599  111.514 1.00 24.66 ?  199 ALA C CB    1 
ATOM   12610 N  N     . ILE C 2 221 ? 112.872 95.101  113.091 1.00 24.85 ?  200 ILE C N     1 
ATOM   12611 C  CA    . ILE C 2 221 ? 114.028 94.187  113.138 1.00 25.07 ?  200 ILE C CA    1 
ATOM   12612 C  C     . ILE C 2 221 ? 113.962 93.220  114.331 1.00 23.86 ?  200 ILE C C     1 
ATOM   12613 O  O     . ILE C 2 221 ? 114.406 92.075  114.216 1.00 23.72 ?  200 ILE C O     1 
ATOM   12614 C  CB    . ILE C 2 221 ? 115.419 94.912  113.057 1.00 25.71 ?  200 ILE C CB    1 
ATOM   12615 C  CG1   . ILE C 2 221 ? 115.761 95.636  114.363 1.00 27.10 ?  200 ILE C CG1   1 
ATOM   12616 C  CG2   . ILE C 2 221 ? 115.482 95.841  111.829 1.00 27.18 ?  200 ILE C CG2   1 
ATOM   12617 C  CD1   . ILE C 2 221 ? 117.182 96.206  114.437 1.00 29.63 ?  200 ILE C CD1   1 
ATOM   12618 N  N     . HIS C 2 222 ? 113.397 93.672  115.451 1.00 22.79 ?  201 HIS C N     1 
ATOM   12619 C  CA    . HIS C 2 222 ? 113.175 92.787  116.617 1.00 22.48 ?  201 HIS C CA    1 
ATOM   12620 C  C     . HIS C 2 222 ? 112.227 91.640  116.271 1.00 22.04 ?  201 HIS C C     1 
ATOM   12621 O  O     . HIS C 2 222 ? 112.472 90.504  116.658 1.00 22.06 ?  201 HIS C O     1 
ATOM   12622 C  CB    . HIS C 2 222 ? 112.560 93.535  117.801 1.00 21.77 ?  201 HIS C CB    1 
ATOM   12623 C  CG    . HIS C 2 222 ? 113.442 94.575  118.408 1.00 21.76 ?  201 HIS C CG    1 
ATOM   12624 N  ND1   . HIS C 2 222 ? 113.085 95.267  119.543 1.00 20.70 ?  201 HIS C ND1   1 
ATOM   12625 C  CD2   . HIS C 2 222 ? 114.661 95.041  118.050 1.00 22.07 ?  201 HIS C CD2   1 
ATOM   12626 C  CE1   . HIS C 2 222 ? 114.040 96.123  119.854 1.00 22.26 ?  201 HIS C CE1   1 
ATOM   12627 N  NE2   . HIS C 2 222 ? 115.003 96.012  118.960 1.00 22.52 ?  201 HIS C NE2   1 
ATOM   12628 N  N     . GLY C 2 223 ? 111.132 91.956  115.579 1.00 22.35 ?  202 GLY C N     1 
ATOM   12629 C  CA    . GLY C 2 223 ? 110.151 90.952  115.135 1.00 22.01 ?  202 GLY C CA    1 
ATOM   12630 C  C     . GLY C 2 223 ? 110.724 89.942  114.145 1.00 22.73 ?  202 GLY C C     1 
ATOM   12631 O  O     . GLY C 2 223 ? 110.424 88.738  114.223 1.00 21.99 ?  202 GLY C O     1 
ATOM   12632 N  N     . VAL C 2 224 ? 111.556 90.419  113.216 1.00 22.45 ?  203 VAL C N     1 
ATOM   12633 C  CA    . VAL C 2 224 ? 112.224 89.522  112.271 1.00 22.54 ?  203 VAL C CA    1 
ATOM   12634 C  C     . VAL C 2 224 ? 113.179 88.576  113.003 1.00 22.28 ?  203 VAL C C     1 
ATOM   12635 O  O     . VAL C 2 224 ? 113.122 87.364  112.810 1.00 22.44 ?  203 VAL C O     1 
ATOM   12636 C  CB    . VAL C 2 224 ? 112.986 90.292  111.139 1.00 23.00 ?  203 VAL C CB    1 
ATOM   12637 C  CG1   . VAL C 2 224 ? 113.845 89.323  110.307 1.00 23.10 ?  203 VAL C CG1   1 
ATOM   12638 C  CG2   . VAL C 2 224 ? 111.994 91.049  110.215 1.00 23.14 ?  203 VAL C CG2   1 
ATOM   12639 N  N     . TYR C 2 225 ? 114.025 89.134  113.866 1.00 22.41 ?  204 TYR C N     1 
ATOM   12640 C  CA    . TYR C 2 225 ? 115.014 88.342  114.597 1.00 22.03 ?  204 TYR C CA    1 
ATOM   12641 C  C     . TYR C 2 225 ? 114.380 87.252  115.459 1.00 21.66 ?  204 TYR C C     1 
ATOM   12642 O  O     . TYR C 2 225 ? 114.738 86.072  115.337 1.00 21.72 ?  204 TYR C O     1 
ATOM   12643 C  CB    . TYR C 2 225 ? 115.938 89.231  115.444 1.00 22.22 ?  204 TYR C CB    1 
ATOM   12644 C  CG    . TYR C 2 225 ? 117.106 88.463  116.032 1.00 21.92 ?  204 TYR C CG    1 
ATOM   12645 C  CD1   . TYR C 2 225 ? 118.119 87.966  115.212 1.00 22.36 ?  204 TYR C CD1   1 
ATOM   12646 C  CD2   . TYR C 2 225 ? 117.188 88.228  117.405 1.00 21.43 ?  204 TYR C CD2   1 
ATOM   12647 C  CE1   . TYR C 2 225 ? 119.186 87.244  115.745 1.00 23.82 ?  204 TYR C CE1   1 
ATOM   12648 C  CE2   . TYR C 2 225 ? 118.257 87.514  117.956 1.00 21.49 ?  204 TYR C CE2   1 
ATOM   12649 C  CZ    . TYR C 2 225 ? 119.246 87.029  117.121 1.00 23.58 ?  204 TYR C CZ    1 
ATOM   12650 O  OH    . TYR C 2 225 ? 120.293 86.330  117.658 1.00 25.42 ?  204 TYR C OH    1 
ATOM   12651 N  N     . VAL C 2 226 ? 113.436 87.638  116.321 1.00 20.95 ?  205 VAL C N     1 
ATOM   12652 C  CA    . VAL C 2 226 ? 112.730 86.659  117.158 1.00 20.49 ?  205 VAL C CA    1 
ATOM   12653 C  C     . VAL C 2 226 ? 111.975 85.637  116.289 1.00 20.84 ?  205 VAL C C     1 
ATOM   12654 O  O     . VAL C 2 226 ? 111.969 84.435  116.588 1.00 21.10 ?  205 VAL C O     1 
ATOM   12655 C  CB    . VAL C 2 226 ? 111.818 87.333  118.219 1.00 20.57 ?  205 VAL C CB    1 
ATOM   12656 C  CG1   . VAL C 2 226 ? 111.070 86.278  119.036 1.00 20.35 ?  205 VAL C CG1   1 
ATOM   12657 C  CG2   . VAL C 2 226 ? 112.666 88.213  119.150 1.00 19.60 ?  205 VAL C CG2   1 
ATOM   12658 N  N     . GLY C 2 227 ? 111.388 86.106  115.192 1.00 21.08 ?  206 GLY C N     1 
ATOM   12659 C  CA    . GLY C 2 227 ? 110.770 85.204  114.207 1.00 21.43 ?  206 GLY C CA    1 
ATOM   12660 C  C     . GLY C 2 227 ? 111.708 84.125  113.683 1.00 21.95 ?  206 GLY C C     1 
ATOM   12661 O  O     . GLY C 2 227 ? 111.323 82.948  113.572 1.00 21.84 ?  206 GLY C O     1 
ATOM   12662 N  N     . LEU C 2 228 ? 112.944 84.511  113.365 1.00 22.09 ?  207 LEU C N     1 
ATOM   12663 C  CA    . LEU C 2 228 ? 113.936 83.541  112.892 1.00 22.96 ?  207 LEU C CA    1 
ATOM   12664 C  C     . LEU C 2 228 ? 114.297 82.504  113.966 1.00 22.60 ?  207 LEU C C     1 
ATOM   12665 O  O     . LEU C 2 228 ? 114.452 81.317  113.662 1.00 22.04 ?  207 LEU C O     1 
ATOM   12666 C  CB    . LEU C 2 228 ? 115.187 84.238  112.339 1.00 23.39 ?  207 LEU C CB    1 
ATOM   12667 C  CG    . LEU C 2 228 ? 115.029 85.078  111.058 1.00 24.35 ?  207 LEU C CG    1 
ATOM   12668 C  CD1   . LEU C 2 228 ? 116.228 86.023  110.900 1.00 25.01 ?  207 LEU C CD1   1 
ATOM   12669 C  CD2   . LEU C 2 228 ? 114.868 84.213  109.813 1.00 25.11 ?  207 LEU C CD2   1 
ATOM   12670 N  N     . LEU C 2 229 ? 114.400 82.940  115.219 1.00 22.37 ?  208 LEU C N     1 
ATOM   12671 C  CA    . LEU C 2 229 ? 114.645 82.004  116.334 1.00 22.62 ?  208 LEU C CA    1 
ATOM   12672 C  C     . LEU C 2 229 ? 113.485 81.025  116.541 1.00 22.77 ?  208 LEU C C     1 
ATOM   12673 O  O     . LEU C 2 229 ? 113.703 79.825  116.780 1.00 22.57 ?  208 LEU C O     1 
ATOM   12674 C  CB    . LEU C 2 229 ? 114.972 82.754  117.629 1.00 22.44 ?  208 LEU C CB    1 
ATOM   12675 C  CG    . LEU C 2 229 ? 116.177 83.706  117.569 1.00 23.54 ?  208 LEU C CG    1 
ATOM   12676 C  CD1   . LEU C 2 229 ? 116.330 84.460  118.888 1.00 23.37 ?  208 LEU C CD1   1 
ATOM   12677 C  CD2   . LEU C 2 229 ? 117.474 82.959  117.211 1.00 23.91 ?  208 LEU C CD2   1 
ATOM   12678 N  N     . ALA C 2 230 ? 112.257 81.535  116.437 1.00 22.42 ?  209 ALA C N     1 
ATOM   12679 C  CA    . ALA C 2 230 ? 111.063 80.697  116.524 1.00 22.02 ?  209 ALA C CA    1 
ATOM   12680 C  C     . ALA C 2 230 ? 111.040 79.640  115.415 1.00 22.58 ?  209 ALA C C     1 
ATOM   12681 O  O     . ALA C 2 230 ? 110.769 78.475  115.676 1.00 22.14 ?  209 ALA C O     1 
ATOM   12682 C  CB    . ALA C 2 230 ? 109.814 81.546  116.467 1.00 22.04 ?  209 ALA C CB    1 
ATOM   12683 N  N     . GLN C 2 231 ? 111.345 80.056  114.187 1.00 22.96 ?  210 GLN C N     1 
ATOM   12684 C  CA    . GLN C 2 231 ? 111.414 79.120  113.050 1.00 24.30 ?  210 GLN C CA    1 
ATOM   12685 C  C     . GLN C 2 231 ? 112.444 78.022  113.242 1.00 25.11 ?  210 GLN C C     1 
ATOM   12686 O  O     . GLN C 2 231 ? 112.226 76.885  112.809 1.00 24.97 ?  210 GLN C O     1 
ATOM   12687 C  CB    . GLN C 2 231 ? 111.692 79.867  111.750 1.00 24.38 ?  210 GLN C CB    1 
ATOM   12688 C  CG    . GLN C 2 231 ? 110.519 80.756  111.306 1.00 25.12 ?  210 GLN C CG    1 
ATOM   12689 C  CD    . GLN C 2 231 ? 110.809 81.489  110.013 1.00 28.08 ?  210 GLN C CD    1 
ATOM   12690 O  OE1   . GLN C 2 231 ? 111.147 80.871  109.003 1.00 27.83 ?  210 GLN C OE1   1 
ATOM   12691 N  NE2   . GLN C 2 231 ? 110.697 82.819  110.040 1.00 26.38 ?  210 GLN C NE2   1 
ATOM   12692 N  N     . GLU C 2 232 ? 113.565 78.356  113.885 1.00 25.80 ?  211 GLU C N     1 
ATOM   12693 C  CA    . GLU C 2 232 ? 114.581 77.351  114.214 1.00 27.16 ?  211 GLU C CA    1 
ATOM   12694 C  C     . GLU C 2 232 ? 113.985 76.214  115.038 1.00 26.47 ?  211 GLU C C     1 
ATOM   12695 O  O     . GLU C 2 232 ? 114.242 75.035  114.768 1.00 26.10 ?  211 GLU C O     1 
ATOM   12696 C  CB    . GLU C 2 232 ? 115.718 77.967  115.019 1.00 27.59 ?  211 GLU C CB    1 
ATOM   12697 C  CG    . GLU C 2 232 ? 116.855 78.497  114.199 1.00 32.55 ?  211 GLU C CG    1 
ATOM   12698 C  CD    . GLU C 2 232 ? 118.192 78.365  114.919 1.00 36.72 ?  211 GLU C CD    1 
ATOM   12699 O  OE1   . GLU C 2 232 ? 118.214 77.945  116.100 1.00 38.32 ?  211 GLU C OE1   1 
ATOM   12700 O  OE2   . GLU C 2 232 ? 119.223 78.680  114.292 1.00 40.62 -1 211 GLU C OE2   1 
ATOM   12701 N  N     . ILE C 2 233 ? 113.204 76.577  116.055 1.00 25.55 ?  212 ILE C N     1 
ATOM   12702 C  CA    . ILE C 2 233 ? 112.598 75.587  116.946 1.00 25.32 ?  212 ILE C CA    1 
ATOM   12703 C  C     . ILE C 2 233 ? 111.509 74.794  116.235 1.00 25.48 ?  212 ILE C C     1 
ATOM   12704 O  O     . ILE C 2 233 ? 111.489 73.562  116.297 1.00 25.82 ?  212 ILE C O     1 
ATOM   12705 C  CB    . ILE C 2 233 ? 112.052 76.229  118.239 1.00 25.39 ?  212 ILE C CB    1 
ATOM   12706 C  CG1   . ILE C 2 233 ? 113.216 76.762  119.079 1.00 24.37 ?  212 ILE C CG1   1 
ATOM   12707 C  CG2   . ILE C 2 233 ? 111.211 75.219  119.028 1.00 24.86 ?  212 ILE C CG2   1 
ATOM   12708 C  CD1   . ILE C 2 233 ? 112.793 77.757  120.148 1.00 25.10 ?  212 ILE C CD1   1 
ATOM   12709 N  N     . TYR C 2 234 ? 110.624 75.503  115.540 1.00 25.27 ?  213 TYR C N     1 
ATOM   12710 C  CA    . TYR C 2 234 ? 109.578 74.885  114.722 1.00 25.77 ?  213 TYR C CA    1 
ATOM   12711 C  C     . TYR C 2 234 ? 110.147 73.857  113.727 1.00 26.44 ?  213 TYR C C     1 
ATOM   12712 O  O     . TYR C 2 234 ? 109.587 72.773  113.549 1.00 26.29 ?  213 TYR C O     1 
ATOM   12713 C  CB    . TYR C 2 234 ? 108.803 75.985  113.980 1.00 25.67 ?  213 TYR C CB    1 
ATOM   12714 C  CG    . TYR C 2 234 ? 107.713 75.534  113.029 1.00 25.65 ?  213 TYR C CG    1 
ATOM   12715 C  CD1   . TYR C 2 234 ? 106.391 75.412  113.464 1.00 25.02 ?  213 TYR C CD1   1 
ATOM   12716 C  CD2   . TYR C 2 234 ? 107.994 75.284  111.676 1.00 26.59 ?  213 TYR C CD2   1 
ATOM   12717 C  CE1   . TYR C 2 234 ? 105.381 75.025  112.590 1.00 26.52 ?  213 TYR C CE1   1 
ATOM   12718 C  CE2   . TYR C 2 234 ? 106.990 74.889  110.791 1.00 27.00 ?  213 TYR C CE2   1 
ATOM   12719 C  CZ    . TYR C 2 234 ? 105.689 74.760  111.260 1.00 27.79 ?  213 TYR C CZ    1 
ATOM   12720 O  OH    . TYR C 2 234 ? 104.696 74.390  110.398 1.00 29.00 ?  213 TYR C OH    1 
ATOM   12721 N  N     . ASN C 2 235 ? 111.259 74.199  113.079 1.00 26.96 ?  214 ASN C N     1 
ATOM   12722 C  CA    . ASN C 2 235 ? 111.834 73.319  112.063 1.00 28.05 ?  214 ASN C CA    1 
ATOM   12723 C  C     . ASN C 2 235 ? 112.428 72.021  112.602 1.00 28.24 ?  214 ASN C C     1 
ATOM   12724 O  O     . ASN C 2 235 ? 112.673 71.096  111.835 1.00 28.63 ?  214 ASN C O     1 
ATOM   12725 C  CB    . ASN C 2 235 ? 112.835 74.070  111.171 1.00 28.38 ?  214 ASN C CB    1 
ATOM   12726 C  CG    . ASN C 2 235 ? 112.160 75.121  110.297 1.00 31.14 ?  214 ASN C CG    1 
ATOM   12727 O  OD1   . ASN C 2 235 ? 111.009 74.959  109.879 1.00 34.16 ?  214 ASN C OD1   1 
ATOM   12728 N  ND2   . ASN C 2 235 ? 112.873 76.207  110.022 1.00 32.42 ?  214 ASN C ND2   1 
ATOM   12729 N  N     . LYS C 2 236 ? 112.635 71.949  113.916 1.00 27.91 ?  215 LYS C N     1 
ATOM   12730 C  CA    . LYS C 2 236 ? 113.118 70.732  114.572 1.00 28.49 ?  215 LYS C CA    1 
ATOM   12731 C  C     . LYS C 2 236 ? 112.018 69.694  114.819 1.00 28.50 ?  215 LYS C C     1 
ATOM   12732 O  O     . LYS C 2 236 ? 112.306 68.538  115.138 1.00 28.98 ?  215 LYS C O     1 
ATOM   12733 C  CB    . LYS C 2 236 ? 113.799 71.069  115.903 1.00 28.10 ?  215 LYS C CB    1 
ATOM   12734 C  CG    . LYS C 2 236 ? 115.062 71.907  115.768 1.00 29.25 ?  215 LYS C CG    1 
ATOM   12735 C  CD    . LYS C 2 236 ? 115.694 72.184  117.122 1.00 30.19 ?  215 LYS C CD    1 
ATOM   12736 C  CE    . LYS C 2 236 ? 116.746 73.260  116.991 1.00 32.63 ?  215 LYS C CE    1 
ATOM   12737 N  NZ    . LYS C 2 236 ? 117.379 73.563  118.295 1.00 35.39 1  215 LYS C NZ    1 
ATOM   12738 N  N     . GLN C 2 237 ? 110.761 70.093  114.655 1.00 28.25 ?  216 GLN C N     1 
ATOM   12739 C  CA    . GLN C 2 237 ? 109.645 69.241  115.068 1.00 28.34 ?  216 GLN C CA    1 
ATOM   12740 C  C     . GLN C 2 237 ? 109.200 68.230  113.998 1.00 28.92 ?  216 GLN C C     1 
ATOM   12741 O  O     . GLN C 2 237 ? 109.482 68.402  112.811 1.00 28.53 ?  216 GLN C O     1 
ATOM   12742 C  CB    . GLN C 2 237 ? 108.469 70.111  115.534 1.00 27.68 ?  216 GLN C CB    1 
ATOM   12743 C  CG    . GLN C 2 237 ? 108.850 71.194  116.573 1.00 26.67 ?  216 GLN C CG    1 
ATOM   12744 C  CD    . GLN C 2 237 ? 109.639 70.657  117.763 1.00 25.32 ?  216 GLN C CD    1 
ATOM   12745 O  OE1   . GLN C 2 237 ? 109.308 69.612  118.328 1.00 25.49 ?  216 GLN C OE1   1 
ATOM   12746 N  NE2   . GLN C 2 237 ? 110.689 71.377  118.152 1.00 23.63 ?  216 GLN C NE2   1 
ATOM   12747 N  N     . THR C 2 238 ? 108.500 67.181  114.431 1.00 29.53 ?  217 THR C N     1 
ATOM   12748 C  CA    . THR C 2 238 ? 107.800 66.283  113.507 1.00 30.73 ?  217 THR C CA    1 
ATOM   12749 C  C     . THR C 2 238 ? 106.688 67.062  112.795 1.00 31.13 ?  217 THR C C     1 
ATOM   12750 O  O     . THR C 2 238 ? 106.292 68.153  113.246 1.00 30.17 ?  217 THR C O     1 
ATOM   12751 C  CB    . THR C 2 238 ? 107.133 65.104  114.238 1.00 30.79 ?  217 THR C CB    1 
ATOM   12752 O  OG1   . THR C 2 238 ? 106.049 65.597  115.038 1.00 31.16 ?  217 THR C OG1   1 
ATOM   12753 C  CG2   . THR C 2 238 ? 108.132 64.353  115.126 1.00 31.22 ?  217 THR C CG2   1 
ATOM   12754 N  N     . GLU C 2 239 ? 106.166 66.494  111.706 1.00 31.67 ?  218 GLU C N     1 
ATOM   12755 C  CA    . GLU C 2 239 ? 105.057 67.124  110.989 1.00 32.25 ?  218 GLU C CA    1 
ATOM   12756 C  C     . GLU C 2 239 ? 103.810 67.266  111.869 1.00 31.86 ?  218 GLU C C     1 
ATOM   12757 O  O     . GLU C 2 239 ? 103.112 68.283  111.813 1.00 31.09 ?  218 GLU C O     1 
ATOM   12758 C  CB    . GLU C 2 239 ? 104.748 66.377  109.679 1.00 33.29 ?  218 GLU C CB    1 
ATOM   12759 C  CG    . GLU C 2 239 ? 105.859 66.513  108.621 1.00 35.65 ?  218 GLU C CG    1 
ATOM   12760 C  CD    . GLU C 2 239 ? 106.139 67.970  108.231 1.00 39.17 ?  218 GLU C CD    1 
ATOM   12761 O  OE1   . GLU C 2 239 ? 105.167 68.729  107.984 1.00 41.08 ?  218 GLU C OE1   1 
ATOM   12762 O  OE2   . GLU C 2 239 ? 107.331 68.361  108.178 1.00 39.64 -1 218 GLU C OE2   1 
ATOM   12763 N  N     . GLU C 2 240 ? 103.566 66.257  112.706 1.00 31.72 ?  219 GLU C N     1 
ATOM   12764 C  CA    . GLU C 2 240 ? 102.448 66.261  113.640 1.00 31.76 ?  219 GLU C CA    1 
ATOM   12765 C  C     . GLU C 2 240 ? 102.580 67.397  114.665 1.00 30.21 ?  219 GLU C C     1 
ATOM   12766 O  O     . GLU C 2 240 ? 101.612 68.122  114.936 1.00 29.63 ?  219 GLU C O     1 
ATOM   12767 C  CB    . GLU C 2 240 ? 102.351 64.899  114.331 1.00 32.58 ?  219 GLU C CB    1 
ATOM   12768 C  CG    . GLU C 2 240 ? 101.091 64.687  115.155 1.00 36.93 ?  219 GLU C CG    1 
ATOM   12769 C  CD    . GLU C 2 240 ? 100.857 63.219  115.493 1.00 42.06 ?  219 GLU C CD    1 
ATOM   12770 O  OE1   . GLU C 2 240 ? 100.935 62.858  116.689 1.00 44.09 ?  219 GLU C OE1   1 
ATOM   12771 O  OE2   . GLU C 2 240 ? 100.603 62.422  114.560 1.00 44.45 -1 219 GLU C OE2   1 
ATOM   12772 N  N     . LYS C 2 241 ? 103.784 67.551  115.216 1.00 28.91 ?  220 LYS C N     1 
ATOM   12773 C  CA    . LYS C 2 241 ? 104.072 68.609  116.175 1.00 28.14 ?  220 LYS C CA    1 
ATOM   12774 C  C     . LYS C 2 241 ? 103.957 70.000  115.549 1.00 27.03 ?  220 LYS C C     1 
ATOM   12775 O  O     . LYS C 2 241 ? 103.413 70.919  116.171 1.00 26.72 ?  220 LYS C O     1 
ATOM   12776 C  CB    . LYS C 2 241 ? 105.454 68.419  116.806 1.00 27.83 ?  220 LYS C CB    1 
ATOM   12777 C  CG    . LYS C 2 241 ? 105.772 69.435  117.911 1.00 29.68 ?  220 LYS C CG    1 
ATOM   12778 C  CD    . LYS C 2 241 ? 105.511 68.875  119.302 1.00 33.58 ?  220 LYS C CD    1 
ATOM   12779 C  CE    . LYS C 2 241 ? 104.065 68.987  119.697 1.00 33.71 ?  220 LYS C CE    1 
ATOM   12780 N  NZ    . LYS C 2 241 ? 103.773 68.292  120.994 1.00 34.69 1  220 LYS C NZ    1 
ATOM   12781 N  N     . LYS C 2 242 ? 104.477 70.142  114.328 1.00 26.38 ?  221 LYS C N     1 
ATOM   12782 C  CA    . LYS C 2 242 ? 104.361 71.375  113.545 1.00 25.87 ?  221 LYS C CA    1 
ATOM   12783 C  C     . LYS C 2 242 ? 102.915 71.794  113.353 1.00 25.72 ?  221 LYS C C     1 
ATOM   12784 O  O     . LYS C 2 242 ? 102.582 72.977  113.508 1.00 24.52 ?  221 LYS C O     1 
ATOM   12785 C  CB    . LYS C 2 242 ? 105.024 71.229  112.174 1.00 25.83 ?  221 LYS C CB    1 
ATOM   12786 C  CG    . LYS C 2 242 ? 106.535 71.284  112.186 1.00 26.76 ?  221 LYS C CG    1 
ATOM   12787 C  CD    . LYS C 2 242 ? 107.064 71.264  110.756 1.00 28.40 ?  221 LYS C CD    1 
ATOM   12788 C  CE    . LYS C 2 242 ? 108.556 71.087  110.717 1.00 29.84 ?  221 LYS C CE    1 
ATOM   12789 N  NZ    . LYS C 2 242 ? 109.017 70.848  109.329 1.00 30.96 1  221 LYS C NZ    1 
ATOM   12790 N  N     . ALA C 2 243 ? 102.068 70.820  113.005 1.00 25.97 ?  222 ALA C N     1 
ATOM   12791 C  CA    . ALA C 2 243 ? 100.631 71.061  112.851 1.00 25.79 ?  222 ALA C CA    1 
ATOM   12792 C  C     . ALA C 2 243 ? 100.010 71.620  114.132 1.00 25.24 ?  222 ALA C C     1 
ATOM   12793 O  O     . ALA C 2 243 ? 99.187  72.545  114.074 1.00 25.37 ?  222 ALA C O     1 
ATOM   12794 C  CB    . ALA C 2 243 ? 99.913  69.790  112.394 1.00 26.17 ?  222 ALA C CB    1 
ATOM   12795 N  N     . GLU C 2 244 ? 100.419 71.091  115.284 1.00 25.02 ?  223 GLU C N     1 
ATOM   12796 C  CA    . GLU C 2 244 ? 99.955  71.616  116.577 1.00 25.08 ?  223 GLU C CA    1 
ATOM   12797 C  C     . GLU C 2 244 ? 100.476 73.038  116.857 1.00 24.70 ?  223 GLU C C     1 
ATOM   12798 O  O     . GLU C 2 244 ? 99.747  73.885  117.395 1.00 24.20 ?  223 GLU C O     1 
ATOM   12799 C  CB    . GLU C 2 244 ? 100.332 70.675  117.726 1.00 25.35 ?  223 GLU C CB    1 
ATOM   12800 C  CG    . GLU C 2 244 ? 99.815  71.153  119.095 1.00 26.67 ?  223 GLU C CG    1 
ATOM   12801 C  CD    . GLU C 2 244 ? 100.419 70.392  120.261 1.00 28.29 ?  223 GLU C CD    1 
ATOM   12802 O  OE1   . GLU C 2 244 ? 100.870 69.246  120.074 1.00 29.51 ?  223 GLU C OE1   1 
ATOM   12803 O  OE2   . GLU C 2 244 ? 100.445 70.949  121.374 1.00 29.09 -1 223 GLU C OE2   1 
ATOM   12804 N  N     . LEU C 2 245 ? 101.731 73.290  116.502 1.00 24.27 ?  224 LEU C N     1 
ATOM   12805 C  CA    . LEU C 2 245 ? 102.325 74.613  116.707 1.00 24.54 ?  224 LEU C CA    1 
ATOM   12806 C  C     . LEU C 2 245 ? 101.659 75.701  115.852 1.00 24.42 ?  224 LEU C C     1 
ATOM   12807 O  O     . LEU C 2 245 ? 101.474 76.829  116.316 1.00 24.10 ?  224 LEU C O     1 
ATOM   12808 C  CB    . LEU C 2 245 ? 103.850 74.571  116.500 1.00 23.86 ?  224 LEU C CB    1 
ATOM   12809 C  CG    . LEU C 2 245 ? 104.638 73.761  117.539 1.00 24.78 ?  224 LEU C CG    1 
ATOM   12810 C  CD1   . LEU C 2 245 ? 106.144 73.839  117.267 1.00 25.54 ?  224 LEU C CD1   1 
ATOM   12811 C  CD2   . LEU C 2 245 ? 104.334 74.204  118.977 1.00 25.29 ?  224 LEU C CD2   1 
ATOM   12812 N  N     . ARG C 2 246 ? 101.290 75.353  114.620 1.00 25.26 ?  225 ARG C N     1 
ATOM   12813 C  CA    . ARG C 2 246 ? 100.522 76.256  113.751 1.00 25.97 ?  225 ARG C CA    1 
ATOM   12814 C  C     . ARG C 2 246 ? 99.159  76.544  114.365 1.00 25.85 ?  225 ARG C C     1 
ATOM   12815 O  O     . ARG C 2 246 ? 98.707  77.691  114.358 1.00 25.01 ?  225 ARG C O     1 
ATOM   12816 C  CB    . ARG C 2 246 ? 100.366 75.687  112.324 1.00 26.65 ?  225 ARG C CB    1 
ATOM   12817 C  CG    . ARG C 2 246 ? 101.678 75.594  111.549 1.00 28.90 ?  225 ARG C CG    1 
ATOM   12818 C  CD    . ARG C 2 246 ? 101.480 75.402  110.026 1.00 31.26 ?  225 ARG C CD    1 
ATOM   12819 N  NE    . ARG C 2 246 ? 100.729 74.189  109.694 1.00 34.01 ?  225 ARG C NE    1 
ATOM   12820 C  CZ    . ARG C 2 246 ? 101.227 72.952  109.714 1.00 35.64 ?  225 ARG C CZ    1 
ATOM   12821 N  NH1   . ARG C 2 246 ? 102.490 72.733  110.056 1.00 36.11 1  225 ARG C NH1   1 
ATOM   12822 N  NH2   . ARG C 2 246 ? 100.450 71.925  109.390 1.00 37.05 ?  225 ARG C NH2   1 
ATOM   12823 N  N     . GLU C 2 247 ? 98.513  75.507  114.904 1.00 26.01 ?  226 GLU C N     1 
ATOM   12824 C  CA    . GLU C 2 247 ? 97.243  75.675  115.620 1.00 26.48 ?  226 GLU C CA    1 
ATOM   12825 C  C     . GLU C 2 247 ? 97.402  76.638  116.796 1.00 25.72 ?  226 GLU C C     1 
ATOM   12826 O  O     . GLU C 2 247 ? 96.587  77.555  116.970 1.00 25.16 ?  226 GLU C O     1 
ATOM   12827 C  CB    . GLU C 2 247 ? 96.699  74.338  116.132 1.00 27.18 ?  226 GLU C CB    1 
ATOM   12828 C  CG    . GLU C 2 247 ? 95.220  74.399  116.494 1.00 30.38 ?  226 GLU C CG    1 
ATOM   12829 C  CD    . GLU C 2 247 ? 94.837  73.564  117.702 1.00 35.77 ?  226 GLU C CD    1 
ATOM   12830 O  OE1   . GLU C 2 247 ? 95.485  72.534  117.983 1.00 38.02 ?  226 GLU C OE1   1 
ATOM   12831 O  OE2   . GLU C 2 247 ? 93.860  73.947  118.382 1.00 40.39 -1 226 GLU C OE2   1 
ATOM   12832 N  N     . PHE C 2 248 ? 98.451  76.428  117.594 1.00 24.71 ?  227 PHE C N     1 
ATOM   12833 C  CA    . PHE C 2 248 ? 98.743  77.321  118.714 1.00 23.71 ?  227 PHE C CA    1 
ATOM   12834 C  C     . PHE C 2 248 ? 98.885  78.764  118.224 1.00 23.14 ?  227 PHE C C     1 
ATOM   12835 O  O     . PHE C 2 248 ? 98.273  79.673  118.789 1.00 22.40 ?  227 PHE C O     1 
ATOM   12836 C  CB    . PHE C 2 248 ? 100.009 76.903  119.482 1.00 23.85 ?  227 PHE C CB    1 
ATOM   12837 C  CG    . PHE C 2 248 ? 100.525 77.978  120.405 1.00 23.64 ?  227 PHE C CG    1 
ATOM   12838 C  CD1   . PHE C 2 248 ? 99.968  78.142  121.676 1.00 23.07 ?  227 PHE C CD1   1 
ATOM   12839 C  CD2   . PHE C 2 248 ? 101.518 78.874  119.974 1.00 23.04 ?  227 PHE C CD2   1 
ATOM   12840 C  CE1   . PHE C 2 248 ? 100.417 79.151  122.528 1.00 22.73 ?  227 PHE C CE1   1 
ATOM   12841 C  CE2   . PHE C 2 248 ? 101.973 79.893  120.812 1.00 23.31 ?  227 PHE C CE2   1 
ATOM   12842 C  CZ    . PHE C 2 248 ? 101.424 80.034  122.098 1.00 21.51 ?  227 PHE C CZ    1 
ATOM   12843 N  N     . ALA C 2 249 ? 99.684  78.957  117.174 1.00 22.95 ?  228 ALA C N     1 
ATOM   12844 C  CA    . ALA C 2 249 ? 100.005 80.300  116.672 1.00 22.96 ?  228 ALA C CA    1 
ATOM   12845 C  C     . ALA C 2 249 ? 98.767  81.014  116.138 1.00 23.31 ?  228 ALA C C     1 
ATOM   12846 O  O     . ALA C 2 249 ? 98.557  82.199  116.406 1.00 22.63 ?  228 ALA C O     1 
ATOM   12847 C  CB    . ALA C 2 249 ? 101.088 80.228  115.597 1.00 22.40 ?  228 ALA C CB    1 
ATOM   12848 N  N     . ILE C 2 250 ? 97.954  80.281  115.384 1.00 23.66 ?  229 ILE C N     1 
ATOM   12849 C  CA    . ILE C 2 250 ? 96.733  80.832  114.796 1.00 25.00 ?  229 ILE C CA    1 
ATOM   12850 C  C     . ILE C 2 250 ? 95.647  81.082  115.852 1.00 24.64 ?  229 ILE C C     1 
ATOM   12851 O  O     . ILE C 2 250 ? 95.009  82.142  115.845 1.00 24.26 ?  229 ILE C O     1 
ATOM   12852 C  CB    . ILE C 2 250 ? 96.237  79.970  113.593 1.00 25.43 ?  229 ILE C CB    1 
ATOM   12853 C  CG1   . ILE C 2 250 ? 97.197  80.160  112.409 1.00 27.27 ?  229 ILE C CG1   1 
ATOM   12854 C  CG2   . ILE C 2 250 ? 94.814  80.404  113.147 1.00 27.62 ?  229 ILE C CG2   1 
ATOM   12855 C  CD1   . ILE C 2 250 ? 97.427  78.908  111.551 1.00 31.32 ?  229 ILE C CD1   1 
ATOM   12856 N  N     . ASP C 2 251 ? 95.459  80.136  116.773 1.00 24.78 ?  230 ASP C N     1 
ATOM   12857 C  CA    . ASP C 2 251 ? 94.532  80.347  117.901 1.00 25.20 ?  230 ASP C CA    1 
ATOM   12858 C  C     . ASP C 2 251 ? 94.925  81.560  118.745 1.00 24.08 ?  230 ASP C C     1 
ATOM   12859 O  O     . ASP C 2 251 ? 94.064  82.351  119.161 1.00 23.34 ?  230 ASP C O     1 
ATOM   12860 C  CB    . ASP C 2 251 ? 94.479  79.125  118.827 1.00 25.73 ?  230 ASP C CB    1 
ATOM   12861 C  CG    . ASP C 2 251 ? 93.681  77.979  118.250 1.00 28.78 ?  230 ASP C CG    1 
ATOM   12862 O  OD1   . ASP C 2 251 ? 93.063  78.136  117.172 1.00 29.99 ?  230 ASP C OD1   1 
ATOM   12863 O  OD2   . ASP C 2 251 ? 93.680  76.907  118.891 1.00 33.31 -1 230 ASP C OD2   1 
ATOM   12864 N  N     . LEU C 2 252 ? 96.222  81.693  119.010 1.00 22.98 ?  231 LEU C N     1 
ATOM   12865 C  CA    . LEU C 2 252 ? 96.708  82.821  119.806 1.00 21.63 ?  231 LEU C CA    1 
ATOM   12866 C  C     . LEU C 2 252 ? 96.495  84.131  119.057 1.00 21.66 ?  231 LEU C C     1 
ATOM   12867 O  O     . LEU C 2 252 ? 96.075  85.134  119.636 1.00 19.41 ?  231 LEU C O     1 
ATOM   12868 C  CB    . LEU C 2 252 ? 98.188  82.658  120.151 1.00 21.89 ?  231 LEU C CB    1 
ATOM   12869 C  CG    . LEU C 2 252 ? 98.866  83.813  120.912 1.00 21.33 ?  231 LEU C CG    1 
ATOM   12870 C  CD1   . LEU C 2 252 ? 98.164  84.106  122.255 1.00 20.89 ?  231 LEU C CD1   1 
ATOM   12871 C  CD2   . LEU C 2 252 ? 100.347 83.481  121.114 1.00 20.31 ?  231 LEU C CD2   1 
ATOM   12872 N  N     . LEU C 2 253 ? 96.798  84.116  117.761 1.00 22.28 ?  232 LEU C N     1 
ATOM   12873 C  CA    . LEU C 2 253 ? 96.632  85.319  116.952 1.00 23.05 ?  232 LEU C CA    1 
ATOM   12874 C  C     . LEU C 2 253 ? 95.176  85.773  116.949 1.00 23.36 ?  232 LEU C C     1 
ATOM   12875 O  O     . LEU C 2 253 ? 94.894  86.956  117.203 1.00 22.96 ?  232 LEU C O     1 
ATOM   12876 C  CB    . LEU C 2 253 ? 97.146  85.104  115.527 1.00 23.53 ?  232 LEU C CB    1 
ATOM   12877 C  CG    . LEU C 2 253 ? 97.009  86.337  114.625 1.00 25.63 ?  232 LEU C CG    1 
ATOM   12878 C  CD1   . LEU C 2 253 ? 97.872  87.498  115.120 1.00 25.88 ?  232 LEU C CD1   1 
ATOM   12879 C  CD2   . LEU C 2 253 ? 97.369  85.965  113.195 1.00 27.67 ?  232 LEU C CD2   1 
ATOM   12880 N  N     . ASN C 2 254 ? 94.260  84.836  116.681 1.00 23.55 ?  233 ASN C N     1 
ATOM   12881 C  CA    . ASN C 2 254 ? 92.817  85.134  116.708 1.00 24.61 ?  233 ASN C CA    1 
ATOM   12882 C  C     . ASN C 2 254 ? 92.325  85.667  118.056 1.00 23.57 ?  233 ASN C C     1 
ATOM   12883 O  O     . ASN C 2 254 ? 91.536  86.608  118.110 1.00 23.52 ?  233 ASN C O     1 
ATOM   12884 C  CB    . ASN C 2 254 ? 91.992  83.918  116.281 1.00 24.99 ?  233 ASN C CB    1 
ATOM   12885 C  CG    . ASN C 2 254 ? 91.852  83.807  114.768 1.00 28.92 ?  233 ASN C CG    1 
ATOM   12886 O  OD1   . ASN C 2 254 ? 91.363  84.721  114.102 1.00 33.75 ?  233 ASN C OD1   1 
ATOM   12887 N  ND2   . ASN C 2 254 ? 92.277  82.682  114.224 1.00 30.99 ?  233 ASN C ND2   1 
ATOM   12888 N  N     . GLN C 2 255 ? 92.796  85.066  119.144 1.00 23.22 ?  234 GLN C N     1 
ATOM   12889 C  CA    . GLN C 2 255 ? 92.421  85.529  120.473 1.00 22.54 ?  234 GLN C CA    1 
ATOM   12890 C  C     . GLN C 2 255 ? 92.921  86.965  120.737 1.00 22.00 ?  234 GLN C C     1 
ATOM   12891 O  O     . GLN C 2 255 ? 92.176  87.815  121.255 1.00 21.73 ?  234 GLN C O     1 
ATOM   12892 C  CB    . GLN C 2 255 ? 92.937  84.565  121.540 1.00 22.85 ?  234 GLN C CB    1 
ATOM   12893 C  CG    . GLN C 2 255 ? 92.335  84.807  122.909 1.00 23.87 ?  234 GLN C CG    1 
ATOM   12894 C  CD    . GLN C 2 255 ? 92.877  83.864  123.977 1.00 24.95 ?  234 GLN C CD    1 
ATOM   12895 O  OE1   . GLN C 2 255 ? 93.590  82.900  123.675 1.00 24.21 ?  234 GLN C OE1   1 
ATOM   12896 N  NE2   . GLN C 2 255 ? 92.559  84.158  125.239 1.00 25.97 ?  234 GLN C NE2   1 
ATOM   12897 N  N     . LEU C 2 256 ? 94.173  87.228  120.383 1.00 21.27 ?  235 LEU C N     1 
ATOM   12898 C  CA    . LEU C 2 256 ? 94.740  88.566  120.517 1.00 21.37 ?  235 LEU C CA    1 
ATOM   12899 C  C     . LEU C 2 256 ? 94.027  89.557  119.591 1.00 21.21 ?  235 LEU C C     1 
ATOM   12900 O  O     . LEU C 2 256 ? 93.764  90.697  119.969 1.00 20.75 ?  235 LEU C O     1 
ATOM   12901 C  CB    . LEU C 2 256 ? 96.240  88.537  120.195 1.00 20.93 ?  235 LEU C CB    1 
ATOM   12902 C  CG    . LEU C 2 256 ? 97.197  87.880  121.193 1.00 21.74 ?  235 LEU C CG    1 
ATOM   12903 C  CD1   . LEU C 2 256 ? 98.619  87.851  120.612 1.00 20.15 ?  235 LEU C CD1   1 
ATOM   12904 C  CD2   . LEU C 2 256 ? 97.185  88.581  122.551 1.00 20.90 ?  235 LEU C CD2   1 
ATOM   12905 N  N     . TYR C 2 257 ? 93.741  89.105  118.375 1.00 21.68 ?  236 TYR C N     1 
ATOM   12906 C  CA    . TYR C 2 257 ? 93.064  89.921  117.367 1.00 22.40 ?  236 TYR C CA    1 
ATOM   12907 C  C     . TYR C 2 257 ? 91.685  90.394  117.857 1.00 23.31 ?  236 TYR C C     1 
ATOM   12908 O  O     . TYR C 2 257 ? 91.383  91.603  117.809 1.00 22.99 ?  236 TYR C O     1 
ATOM   12909 C  CB    . TYR C 2 257 ? 92.955  89.147  116.049 1.00 22.81 ?  236 TYR C CB    1 
ATOM   12910 C  CG    . TYR C 2 257 ? 92.147  89.834  114.966 1.00 23.76 ?  236 TYR C CG    1 
ATOM   12911 C  CD1   . TYR C 2 257 ? 92.599  91.015  114.371 1.00 24.05 ?  236 TYR C CD1   1 
ATOM   12912 C  CD2   . TYR C 2 257 ? 90.925  89.309  114.548 1.00 24.04 ?  236 TYR C CD2   1 
ATOM   12913 C  CE1   . TYR C 2 257 ? 91.855  91.655  113.386 1.00 24.40 ?  236 TYR C CE1   1 
ATOM   12914 C  CE2   . TYR C 2 257 ? 90.176  89.943  113.559 1.00 26.30 ?  236 TYR C CE2   1 
ATOM   12915 C  CZ    . TYR C 2 257 ? 90.654  91.106  112.984 1.00 25.80 ?  236 TYR C CZ    1 
ATOM   12916 O  OH    . TYR C 2 257 ? 89.921  91.720  112.008 1.00 28.42 ?  236 TYR C OH    1 
ATOM   12917 N  N     . GLU C 2 258 ? 90.877  89.458  118.367 1.00 22.99 ?  237 GLU C N     1 
ATOM   12918 C  CA    . GLU C 2 258 ? 89.531  89.781  118.854 1.00 24.46 ?  237 GLU C CA    1 
ATOM   12919 C  C     . GLU C 2 258 ? 89.567  90.796  119.984 1.00 23.86 ?  237 GLU C C     1 
ATOM   12920 O  O     . GLU C 2 258 ? 88.754  91.720  120.020 1.00 24.01 ?  237 GLU C O     1 
ATOM   12921 C  CB    . GLU C 2 258 ? 88.756  88.517  119.264 1.00 25.21 ?  237 GLU C CB    1 
ATOM   12922 C  CG    . GLU C 2 258 ? 88.373  87.610  118.072 1.00 30.12 ?  237 GLU C CG    1 
ATOM   12923 C  CD    . GLU C 2 258 ? 87.369  88.264  117.118 1.00 35.29 ?  237 GLU C CD    1 
ATOM   12924 O  OE1   . GLU C 2 258 ? 86.556  89.106  117.565 1.00 37.71 ?  237 GLU C OE1   1 
ATOM   12925 O  OE2   . GLU C 2 258 ? 87.388  87.929  115.910 1.00 39.07 -1 237 GLU C OE2   1 
ATOM   12926 N  N     . ASN C 2 259 ? 90.531  90.642  120.891 1.00 23.25 ?  238 ASN C N     1 
ATOM   12927 C  CA    . ASN C 2 259 ? 90.741  91.618  121.958 1.00 23.10 ?  238 ASN C CA    1 
ATOM   12928 C  C     . ASN C 2 259 ? 91.194  92.981  121.401 1.00 22.68 ?  238 ASN C C     1 
ATOM   12929 O  O     . ASN C 2 259 ? 90.734  94.034  121.851 1.00 22.73 ?  238 ASN C O     1 
ATOM   12930 C  CB    . ASN C 2 259 ? 91.745  91.070  122.975 1.00 23.22 ?  238 ASN C CB    1 
ATOM   12931 C  CG    . ASN C 2 259 ? 91.979  92.019  124.132 1.00 24.46 ?  238 ASN C CG    1 
ATOM   12932 O  OD1   . ASN C 2 259 ? 91.102  92.222  124.977 1.00 26.28 ?  238 ASN C OD1   1 
ATOM   12933 N  ND2   . ASN C 2 259 ? 93.168  92.608  124.177 1.00 24.93 ?  238 ASN C ND2   1 
ATOM   12934 N  N     . GLU C 2 260 ? 92.075  92.957  120.403 1.00 22.64 ?  239 GLU C N     1 
ATOM   12935 C  CA    . GLU C 2 260 ? 92.596  94.193  119.816 1.00 23.18 ?  239 GLU C CA    1 
ATOM   12936 C  C     . GLU C 2 260 ? 91.498  94.990  119.090 1.00 23.40 ?  239 GLU C C     1 
ATOM   12937 O  O     . GLU C 2 260 ? 91.509  96.231  119.100 1.00 23.57 ?  239 GLU C O     1 
ATOM   12938 C  CB    . GLU C 2 260 ? 93.778  93.904  118.880 1.00 23.19 ?  239 GLU C CB    1 
ATOM   12939 C  CG    . GLU C 2 260 ? 94.781  95.075  118.751 1.00 24.33 ?  239 GLU C CG    1 
ATOM   12940 C  CD    . GLU C 2 260 ? 95.511  95.407  120.065 1.00 27.99 ?  239 GLU C CD    1 
ATOM   12941 O  OE1   . GLU C 2 260 ? 95.378  94.664  121.062 1.00 27.36 ?  239 GLU C OE1   1 
ATOM   12942 O  OE2   . GLU C 2 260 ? 96.224  96.434  120.105 1.00 28.98 -1 239 GLU C OE2   1 
ATOM   12943 N  N     . LEU C 2 261 ? 90.553  94.277  118.476 1.00 23.35 ?  240 LEU C N     1 
ATOM   12944 C  CA    . LEU C 2 261 ? 89.382  94.919  117.859 1.00 23.74 ?  240 LEU C CA    1 
ATOM   12945 C  C     . LEU C 2 261 ? 88.594  95.769  118.859 1.00 23.80 ?  240 LEU C C     1 
ATOM   12946 O  O     . LEU C 2 261 ? 88.257  96.931  118.581 1.00 23.33 ?  240 LEU C O     1 
ATOM   12947 C  CB    . LEU C 2 261 ? 88.455  93.880  117.221 1.00 24.09 ?  240 LEU C CB    1 
ATOM   12948 C  CG    . LEU C 2 261 ? 88.962  93.166  115.969 1.00 24.07 ?  240 LEU C CG    1 
ATOM   12949 C  CD1   . LEU C 2 261 ? 87.921  92.163  115.490 1.00 24.77 ?  240 LEU C CD1   1 
ATOM   12950 C  CD2   . LEU C 2 261 ? 89.311  94.175  114.856 1.00 24.38 ?  240 LEU C CD2   1 
ATOM   12951 N  N     . GLU C 2 262 ? 88.298  95.183  120.013 1.00 23.41 ?  241 GLU C N     1 
ATOM   12952 C  CA    . GLU C 2 262 ? 87.582  95.888  121.075 1.00 24.02 ?  241 GLU C CA    1 
ATOM   12953 C  C     . GLU C 2 262 ? 88.384  97.081  121.617 1.00 22.91 ?  241 GLU C C     1 
ATOM   12954 O  O     . GLU C 2 262 ? 87.823  98.143  121.855 1.00 22.94 ?  241 GLU C O     1 
ATOM   12955 C  CB    . GLU C 2 262 ? 87.239  94.915  122.205 1.00 24.92 ?  241 GLU C CB    1 
ATOM   12956 C  CG    . GLU C 2 262 ? 86.250  93.828  121.817 1.00 27.82 ?  241 GLU C CG    1 
ATOM   12957 C  CD    . GLU C 2 262 ? 85.919  92.909  122.979 1.00 33.08 ?  241 GLU C CD    1 
ATOM   12958 O  OE1   . GLU C 2 262 ? 86.705  91.978  123.266 1.00 36.94 ?  241 GLU C OE1   1 
ATOM   12959 O  OE2   . GLU C 2 262 ? 84.862  93.112  123.604 1.00 37.48 -1 241 GLU C OE2   1 
ATOM   12960 N  N     . TYR C 2 263 ? 89.689  96.886  121.817 1.00 21.84 ?  242 TYR C N     1 
ATOM   12961 C  CA    . TYR C 2 263 ? 90.610  97.948  122.219 1.00 21.66 ?  242 TYR C CA    1 
ATOM   12962 C  C     . TYR C 2 263 ? 90.616  99.079  121.197 1.00 21.28 ?  242 TYR C C     1 
ATOM   12963 O  O     . TYR C 2 263 ? 90.562  100.261 121.564 1.00 21.14 ?  242 TYR C O     1 
ATOM   12964 C  CB    . TYR C 2 263 ? 92.033  97.382  122.343 1.00 21.44 ?  242 TYR C CB    1 
ATOM   12965 C  CG    . TYR C 2 263 ? 93.111  98.364  122.780 1.00 21.89 ?  242 TYR C CG    1 
ATOM   12966 C  CD1   . TYR C 2 263 ? 93.145  98.861  124.084 1.00 22.52 ?  242 TYR C CD1   1 
ATOM   12967 C  CD2   . TYR C 2 263 ? 94.118  98.765  121.898 1.00 22.58 ?  242 TYR C CD2   1 
ATOM   12968 C  CE1   . TYR C 2 263 ? 94.146  99.742  124.494 1.00 22.67 ?  242 TYR C CE1   1 
ATOM   12969 C  CE2   . TYR C 2 263 ? 95.130  99.644  122.300 1.00 24.03 ?  242 TYR C CE2   1 
ATOM   12970 C  CZ    . TYR C 2 263 ? 95.137  100.119 123.607 1.00 23.75 ?  242 TYR C CZ    1 
ATOM   12971 O  OH    . TYR C 2 263 ? 96.122  100.993 124.023 1.00 26.82 ?  242 TYR C OH    1 
ATOM   12972 N  N     . THR C 2 264 ? 90.687  98.710  119.921 1.00 20.66 ?  243 THR C N     1 
ATOM   12973 C  CA    . THR C 2 264 ? 90.727  99.691  118.827 1.00 20.99 ?  243 THR C CA    1 
ATOM   12974 C  C     . THR C 2 264 ? 89.444  100.529 118.796 1.00 21.22 ?  243 THR C C     1 
ATOM   12975 O  O     . THR C 2 264 ? 89.505  101.765 118.705 1.00 20.95 ?  243 THR C O     1 
ATOM   12976 C  CB    . THR C 2 264 ? 90.970  98.999  117.458 1.00 20.58 ?  243 THR C CB    1 
ATOM   12977 O  OG1   . THR C 2 264 ? 92.274  98.411  117.457 1.00 20.84 ?  243 THR C OG1   1 
ATOM   12978 C  CG2   . THR C 2 264 ? 90.879  99.997  116.301 1.00 20.90 ?  243 THR C CG2   1 
ATOM   12979 N  N     . GLU C 2 265 ? 88.293  99.864  118.902 1.00 21.62 ?  244 GLU C N     1 
ATOM   12980 C  CA    . GLU C 2 265 ? 87.013  100.575 118.917 1.00 23.46 ?  244 GLU C CA    1 
ATOM   12981 C  C     . GLU C 2 265 ? 86.914  101.508 120.107 1.00 23.33 ?  244 GLU C C     1 
ATOM   12982 O  O     . GLU C 2 265 ? 86.472  102.651 119.985 1.00 22.86 ?  244 GLU C O     1 
ATOM   12983 C  CB    . GLU C 2 265 ? 85.830  99.606  118.913 1.00 24.31 ?  244 GLU C CB    1 
ATOM   12984 C  CG    . GLU C 2 265 ? 85.629  98.897  117.577 1.00 27.63 ?  244 GLU C CG    1 
ATOM   12985 C  CD    . GLU C 2 265 ? 84.438  97.945  117.593 1.00 33.27 ?  244 GLU C CD    1 
ATOM   12986 O  OE1   . GLU C 2 265 ? 83.466  98.202  118.340 1.00 35.56 ?  244 GLU C OE1   1 
ATOM   12987 O  OE2   . GLU C 2 265 ? 84.470  96.939  116.847 1.00 35.96 -1 244 GLU C OE2   1 
ATOM   12988 N  N     . ASP C 2 266 ? 87.339  101.014 121.261 1.00 23.36 ?  245 ASP C N     1 
ATOM   12989 C  CA    . ASP C 2 266 ? 87.321  101.804 122.481 1.00 24.18 ?  245 ASP C CA    1 
ATOM   12990 C  C     . ASP C 2 266 ? 88.131  103.108 122.346 1.00 23.96 ?  245 ASP C C     1 
ATOM   12991 O  O     . ASP C 2 266 ? 87.704  104.161 122.813 1.00 24.19 ?  245 ASP C O     1 
ATOM   12992 C  CB    . ASP C 2 266 ? 87.859  100.960 123.634 1.00 25.14 ?  245 ASP C CB    1 
ATOM   12993 C  CG    . ASP C 2 266 ? 87.645  101.610 124.966 1.00 27.35 ?  245 ASP C CG    1 
ATOM   12994 O  OD1   . ASP C 2 266 ? 86.482  101.932 125.290 1.00 28.45 ?  245 ASP C OD1   1 
ATOM   12995 O  OD2   . ASP C 2 266 ? 88.648  101.799 125.688 1.00 31.99 -1 245 ASP C OD2   1 
ATOM   12996 N  N     . LEU C 2 267 ? 89.284  103.035 121.692 1.00 23.34 ?  246 LEU C N     1 
ATOM   12997 C  CA    . LEU C 2 267 ? 90.147  104.211 121.535 1.00 23.53 ?  246 LEU C CA    1 
ATOM   12998 C  C     . LEU C 2 267 ? 89.785  105.114 120.366 1.00 22.94 ?  246 LEU C C     1 
ATOM   12999 O  O     . LEU C 2 267 ? 89.825  106.339 120.490 1.00 23.14 ?  246 LEU C O     1 
ATOM   13000 C  CB    . LEU C 2 267 ? 91.604  103.780 121.389 1.00 23.37 ?  246 LEU C CB    1 
ATOM   13001 C  CG    . LEU C 2 267 ? 92.303  103.235 122.636 1.00 26.17 ?  246 LEU C CG    1 
ATOM   13002 C  CD1   . LEU C 2 267 ? 93.731  102.893 122.272 1.00 27.31 ?  246 LEU C CD1   1 
ATOM   13003 C  CD2   . LEU C 2 267 ? 92.280  104.261 123.764 1.00 28.08 ?  246 LEU C CD2   1 
ATOM   13004 N  N     . TYR C 2 268 ? 89.458  104.507 119.228 1.00 22.46 ?  247 TYR C N     1 
ATOM   13005 C  CA    . TYR C 2 268 ? 89.329  105.258 117.982 1.00 22.00 ?  247 TYR C CA    1 
ATOM   13006 C  C     . TYR C 2 268 ? 87.939  105.710 117.567 1.00 22.26 ?  247 TYR C C     1 
ATOM   13007 O  O     . TYR C 2 268 ? 87.833  106.572 116.693 1.00 22.17 ?  247 TYR C O     1 
ATOM   13008 C  CB    . TYR C 2 268 ? 89.985  104.493 116.825 1.00 21.73 ?  247 TYR C CB    1 
ATOM   13009 C  CG    . TYR C 2 268 ? 91.492  104.466 116.900 1.00 21.49 ?  247 TYR C CG    1 
ATOM   13010 C  CD1   . TYR C 2 268 ? 92.165  103.339 117.384 1.00 19.45 ?  247 TYR C CD1   1 
ATOM   13011 C  CD2   . TYR C 2 268 ? 92.247  105.575 116.502 1.00 22.71 ?  247 TYR C CD2   1 
ATOM   13012 C  CE1   . TYR C 2 268 ? 93.561  103.316 117.463 1.00 20.30 ?  247 TYR C CE1   1 
ATOM   13013 C  CE2   . TYR C 2 268 ? 93.651  105.565 116.571 1.00 21.69 ?  247 TYR C CE2   1 
ATOM   13014 C  CZ    . TYR C 2 268 ? 94.292  104.428 117.039 1.00 21.40 ?  247 TYR C CZ    1 
ATOM   13015 O  OH    . TYR C 2 268 ? 95.662  104.415 117.100 1.00 22.11 ?  247 TYR C OH    1 
ATOM   13016 N  N     . ASP C 2 269 ? 86.879  105.135 118.144 1.00 22.40 ?  248 ASP C N     1 
ATOM   13017 C  CA    . ASP C 2 269 ? 85.517  105.572 117.788 1.00 22.75 ?  248 ASP C CA    1 
ATOM   13018 C  C     . ASP C 2 269 ? 85.328  107.076 117.991 1.00 22.55 ?  248 ASP C C     1 
ATOM   13019 O  O     . ASP C 2 269 ? 84.672  107.734 117.174 1.00 22.22 ?  248 ASP C O     1 
ATOM   13020 C  CB    . ASP C 2 269 ? 84.426  104.785 118.540 1.00 23.03 ?  248 ASP C CB    1 
ATOM   13021 C  CG    . ASP C 2 269 ? 84.134  103.432 117.913 1.00 25.02 ?  248 ASP C CG    1 
ATOM   13022 O  OD1   . ASP C 2 269 ? 84.607  103.151 116.791 1.00 26.85 ?  248 ASP C OD1   1 
ATOM   13023 O  OD2   . ASP C 2 269 ? 83.414  102.636 118.549 1.00 28.74 -1 248 ASP C OD2   1 
ATOM   13024 N  N     . GLN C 2 270 ? 85.913  107.619 119.062 1.00 22.21 ?  249 GLN C N     1 
ATOM   13025 C  CA    . GLN C 2 270 ? 85.774  109.064 119.354 1.00 22.39 ?  249 GLN C CA    1 
ATOM   13026 C  C     . GLN C 2 270 ? 86.506  109.987 118.369 1.00 21.65 ?  249 GLN C C     1 
ATOM   13027 O  O     . GLN C 2 270 ? 86.272  111.196 118.371 1.00 21.70 ?  249 GLN C O     1 
ATOM   13028 C  CB    . GLN C 2 270 ? 86.167  109.397 120.802 1.00 22.53 ?  249 GLN C CB    1 
ATOM   13029 C  CG    . GLN C 2 270 ? 87.637  109.096 121.191 1.00 22.73 ?  249 GLN C CG    1 
ATOM   13030 C  CD    . GLN C 2 270 ? 87.921  109.459 122.634 1.00 25.39 ?  249 GLN C CD    1 
ATOM   13031 O  OE1   . GLN C 2 270 ? 86.997  109.646 123.428 1.00 27.88 ?  249 GLN C OE1   1 
ATOM   13032 N  NE2   . GLN C 2 270 ? 89.199  109.573 122.985 1.00 24.88 ?  249 GLN C NE2   1 
ATOM   13033 N  N     . VAL C 2 271 ? 87.385  109.418 117.542 1.00 20.91 ?  250 VAL C N     1 
ATOM   13034 C  CA    . VAL C 2 271 ? 88.098  110.192 116.499 1.00 20.62 ?  250 VAL C CA    1 
ATOM   13035 C  C     . VAL C 2 271 ? 87.740  109.714 115.079 1.00 20.53 ?  250 VAL C C     1 
ATOM   13036 O  O     . VAL C 2 271 ? 88.266  110.231 114.081 1.00 20.05 ?  250 VAL C O     1 
ATOM   13037 C  CB    . VAL C 2 271 ? 89.656  110.244 116.725 1.00 20.32 ?  250 VAL C CB    1 
ATOM   13038 C  CG1   . VAL C 2 271 ? 89.994  110.988 118.012 1.00 20.35 ?  250 VAL C CG1   1 
ATOM   13039 C  CG2   . VAL C 2 271 ? 90.287  108.843 116.748 1.00 19.32 ?  250 VAL C CG2   1 
ATOM   13040 N  N     . GLY C 2 272 ? 86.834  108.737 115.007 1.00 20.29 ?  251 GLY C N     1 
ATOM   13041 C  CA    . GLY C 2 272 ? 86.244  108.296 113.740 1.00 20.51 ?  251 GLY C CA    1 
ATOM   13042 C  C     . GLY C 2 272 ? 87.104  107.381 112.881 1.00 20.99 ?  251 GLY C C     1 
ATOM   13043 O  O     . GLY C 2 272 ? 86.881  107.278 111.664 1.00 20.22 ?  251 GLY C O     1 
ATOM   13044 N  N     . LEU C 2 273 ? 88.083  106.715 113.500 1.00 20.76 ?  252 LEU C N     1 
ATOM   13045 C  CA    . LEU C 2 273 ? 89.104  106.003 112.725 1.00 21.38 ?  252 LEU C CA    1 
ATOM   13046 C  C     . LEU C 2 273 ? 89.164  104.490 112.917 1.00 21.86 ?  252 LEU C C     1 
ATOM   13047 O  O     . LEU C 2 273 ? 90.056  103.838 112.377 1.00 22.45 ?  252 LEU C O     1 
ATOM   13048 C  CB    . LEU C 2 273 ? 90.493  106.625 112.956 1.00 21.44 ?  252 LEU C CB    1 
ATOM   13049 C  CG    . LEU C 2 273 ? 90.699  108.106 112.631 1.00 22.02 ?  252 LEU C CG    1 
ATOM   13050 C  CD1   . LEU C 2 273 ? 92.119  108.517 113.008 1.00 22.86 ?  252 LEU C CD1   1 
ATOM   13051 C  CD2   . LEU C 2 273 ? 90.413  108.399 111.142 1.00 23.88 ?  252 LEU C CD2   1 
ATOM   13052 N  N     . SER C 2 274 ? 88.214  103.924 113.658 1.00 22.19 ?  253 SER C N     1 
ATOM   13053 C  CA    . SER C 2 274 ? 88.319  102.530 114.084 1.00 22.47 ?  253 SER C CA    1 
ATOM   13054 C  C     . SER C 2 274 ? 88.453  101.548 112.920 1.00 22.94 ?  253 SER C C     1 
ATOM   13055 O  O     . SER C 2 274 ? 89.296  100.657 112.953 1.00 22.07 ?  253 SER C O     1 
ATOM   13056 C  CB    . SER C 2 274 ? 87.130  102.148 114.970 1.00 22.91 ?  253 SER C CB    1 
ATOM   13057 O  OG    . SER C 2 274 ? 87.211  102.840 116.200 1.00 24.25 ?  253 SER C OG    1 
ATOM   13058 N  N     . HIS C 2 275 ? 87.645  101.740 111.880 1.00 24.59 ?  254 HIS C N     1 
ATOM   13059 C  CA    . HIS C 2 275 ? 87.663  100.848 110.715 1.00 25.66 ?  254 HIS C CA    1 
ATOM   13060 C  C     . HIS C 2 275 ? 89.013  100.889 109.980 1.00 26.01 ?  254 HIS C C     1 
ATOM   13061 O  O     . HIS C 2 275 ? 89.532  99.850  109.536 1.00 26.23 ?  254 HIS C O     1 
ATOM   13062 C  CB    . HIS C 2 275 ? 86.516  101.201 109.759 1.00 26.89 ?  254 HIS C CB    1 
ATOM   13063 C  CG    . HIS C 2 275 ? 86.399  100.274 108.589 1.00 29.10 ?  254 HIS C CG    1 
ATOM   13064 N  ND1   . HIS C 2 275 ? 86.291  98.906  108.730 1.00 32.70 ?  254 HIS C ND1   1 
ATOM   13065 C  CD2   . HIS C 2 275 ? 86.370  100.517 107.258 1.00 31.68 ?  254 HIS C CD2   1 
ATOM   13066 C  CE1   . HIS C 2 275 ? 86.205  98.347  107.536 1.00 33.55 ?  254 HIS C CE1   1 
ATOM   13067 N  NE2   . HIS C 2 275 ? 86.235  99.303  106.627 1.00 33.71 ?  254 HIS C NE2   1 
ATOM   13068 N  N     . ASP C 2 276 ? 89.569  102.089 109.858 1.00 25.93 ?  255 ASP C N     1 
ATOM   13069 C  CA    . ASP C 2 276 ? 90.873  102.291 109.235 1.00 26.65 ?  255 ASP C CA    1 
ATOM   13070 C  C     . ASP C 2 276 ? 91.996  101.596 110.007 1.00 25.61 ?  255 ASP C C     1 
ATOM   13071 O  O     . ASP C 2 276 ? 92.839  100.919 109.403 1.00 25.34 ?  255 ASP C O     1 
ATOM   13072 C  CB    . ASP C 2 276 ? 91.175  103.784 109.092 1.00 27.44 ?  255 ASP C CB    1 
ATOM   13073 C  CG    . ASP C 2 276 ? 91.209  104.230 107.647 1.00 32.09 ?  255 ASP C CG    1 
ATOM   13074 O  OD1   . ASP C 2 276 ? 91.821  103.512 106.818 1.00 36.67 ?  255 ASP C OD1   1 
ATOM   13075 O  OD2   . ASP C 2 276 ? 90.617  105.288 107.331 1.00 36.30 -1 255 ASP C OD2   1 
ATOM   13076 N  N     . VAL C 2 277 ? 91.997  101.770 111.333 1.00 24.17 ?  256 VAL C N     1 
ATOM   13077 C  CA    . VAL C 2 277 ? 92.990  101.129 112.205 1.00 23.71 ?  256 VAL C CA    1 
ATOM   13078 C  C     . VAL C 2 277 ? 92.887  99.603  112.119 1.00 23.48 ?  256 VAL C C     1 
ATOM   13079 O  O     . VAL C 2 277 ? 93.905  98.912  112.071 1.00 23.08 ?  256 VAL C O     1 
ATOM   13080 C  CB    . VAL C 2 277 ? 92.856  101.574 113.688 1.00 23.27 ?  256 VAL C CB    1 
ATOM   13081 C  CG1   . VAL C 2 277 ? 93.909  100.887 114.563 1.00 24.02 ?  256 VAL C CG1   1 
ATOM   13082 C  CG2   . VAL C 2 277 ? 92.973  103.087 113.818 1.00 23.35 ?  256 VAL C CG2   1 
ATOM   13083 N  N     . LYS C 2 278 ? 91.661  99.087  112.099 1.00 23.36 ?  257 LYS C N     1 
ATOM   13084 C  CA    . LYS C 2 278 ? 91.432  97.648  111.966 1.00 24.12 ?  257 LYS C CA    1 
ATOM   13085 C  C     . LYS C 2 278 ? 92.079  97.060  110.715 1.00 24.30 ?  257 LYS C C     1 
ATOM   13086 O  O     . LYS C 2 278 ? 92.665  95.969  110.761 1.00 24.37 ?  257 LYS C O     1 
ATOM   13087 C  CB    . LYS C 2 278 ? 89.939  97.323  111.992 1.00 24.22 ?  257 LYS C CB    1 
ATOM   13088 C  CG    . LYS C 2 278 ? 89.306  97.435  113.369 1.00 24.96 ?  257 LYS C CG    1 
ATOM   13089 C  CD    . LYS C 2 278 ? 87.801  97.237  113.255 1.00 26.34 ?  257 LYS C CD    1 
ATOM   13090 C  CE    . LYS C 2 278 ? 87.121  97.381  114.589 1.00 27.16 ?  257 LYS C CE    1 
ATOM   13091 N  NZ    . LYS C 2 278 ? 85.654  97.167  114.409 1.00 29.60 1  257 LYS C NZ    1 
ATOM   13092 N  N     . LYS C 2 279 ? 91.980  97.780  109.598 1.00 24.55 ?  258 LYS C N     1 
ATOM   13093 C  CA    . LYS C 2 279 ? 92.641  97.353  108.368 1.00 24.85 ?  258 LYS C CA    1 
ATOM   13094 C  C     . LYS C 2 279 ? 94.155  97.309  108.564 1.00 24.57 ?  258 LYS C C     1 
ATOM   13095 O  O     . LYS C 2 279 ? 94.814  96.381  108.096 1.00 24.07 ?  258 LYS C O     1 
ATOM   13096 C  CB    . LYS C 2 279 ? 92.289  98.288  107.211 1.00 25.30 ?  258 LYS C CB    1 
ATOM   13097 C  CG    . LYS C 2 279 ? 90.816  98.328  106.877 1.00 26.63 ?  258 LYS C CG    1 
ATOM   13098 C  CD    . LYS C 2 279 ? 90.582  99.292  105.720 1.00 29.30 ?  258 LYS C CD    1 
ATOM   13099 C  CE    . LYS C 2 279 ? 89.156  99.237  105.261 1.00 31.79 ?  258 LYS C CE    1 
ATOM   13100 N  NZ    . LYS C 2 279 ? 88.874  100.407 104.393 1.00 33.80 1  258 LYS C NZ    1 
ATOM   13101 N  N     . PHE C 2 280 ? 94.686  98.299  109.283 1.00 24.29 ?  259 PHE C N     1 
ATOM   13102 C  CA    . PHE C 2 280 ? 96.127  98.405  109.548 1.00 24.90 ?  259 PHE C CA    1 
ATOM   13103 C  C     . PHE C 2 280 ? 96.648  97.244  110.416 1.00 24.86 ?  259 PHE C C     1 
ATOM   13104 O  O     . PHE C 2 280 ? 97.709  96.676  110.135 1.00 24.68 ?  259 PHE C O     1 
ATOM   13105 C  CB    . PHE C 2 280 ? 96.428  99.769  110.185 1.00 24.70 ?  259 PHE C CB    1 
ATOM   13106 C  CG    . PHE C 2 280 ? 97.897  100.109 110.293 1.00 25.70 ?  259 PHE C CG    1 
ATOM   13107 C  CD1   . PHE C 2 280 ? 98.708  100.165 109.160 1.00 26.86 ?  259 PHE C CD1   1 
ATOM   13108 C  CD2   . PHE C 2 280 ? 98.459  100.419 111.538 1.00 26.19 ?  259 PHE C CD2   1 
ATOM   13109 C  CE1   . PHE C 2 280 ? 100.065 100.505 109.259 1.00 26.66 ?  259 PHE C CE1   1 
ATOM   13110 C  CE2   . PHE C 2 280 ? 99.810  100.766 111.647 1.00 26.52 ?  259 PHE C CE2   1 
ATOM   13111 C  CZ    . PHE C 2 280 ? 100.616 100.803 110.502 1.00 26.23 ?  259 PHE C CZ    1 
ATOM   13112 N  N     . ILE C 2 281 ? 95.898  96.889  111.460 1.00 25.53 ?  260 ILE C N     1 
ATOM   13113 C  CA    . ILE C 2 281 ? 96.318  95.799  112.343 1.00 26.21 ?  260 ILE C CA    1 
ATOM   13114 C  C     . ILE C 2 281 ? 96.260  94.434  111.642 1.00 26.47 ?  260 ILE C C     1 
ATOM   13115 O  O     . ILE C 2 281 ? 97.098  93.576  111.901 1.00 26.52 ?  260 ILE C O     1 
ATOM   13116 C  CB    . ILE C 2 281 ? 95.595  95.801  113.734 1.00 26.27 ?  260 ILE C CB    1 
ATOM   13117 C  CG1   . ILE C 2 281 ? 94.178  95.229  113.647 1.00 27.37 ?  260 ILE C CG1   1 
ATOM   13118 C  CG2   . ILE C 2 281 ? 95.627  97.214  114.359 1.00 26.92 ?  260 ILE C CG2   1 
ATOM   13119 C  CD1   . ILE C 2 281 ? 93.451  95.141  114.989 1.00 29.51 ?  260 ILE C CD1   1 
ATOM   13120 N  N     . ARG C 2 282 ? 95.303  94.257  110.729 1.00 26.57 ?  261 ARG C N     1 
ATOM   13121 C  CA    . ARG C 2 282 ? 95.229  93.029  109.931 1.00 26.84 ?  261 ARG C CA    1 
ATOM   13122 C  C     . ARG C 2 282 ? 96.432  92.914  108.996 1.00 27.34 ?  261 ARG C C     1 
ATOM   13123 O  O     . ARG C 2 282 ? 97.033  91.850  108.881 1.00 27.54 ?  261 ARG C O     1 
ATOM   13124 C  CB    . ARG C 2 282 ? 93.917  92.941  109.149 1.00 26.98 ?  261 ARG C CB    1 
ATOM   13125 C  CG    . ARG C 2 282 ? 92.725  92.496  109.974 1.00 26.53 ?  261 ARG C CG    1 
ATOM   13126 C  CD    . ARG C 2 282 ? 91.513  92.149  109.086 1.00 27.77 ?  261 ARG C CD    1 
ATOM   13127 N  NE    . ARG C 2 282 ? 90.916  93.324  108.458 1.00 28.67 ?  261 ARG C NE    1 
ATOM   13128 C  CZ    . ARG C 2 282 ? 90.000  94.108  109.033 1.00 29.68 ?  261 ARG C CZ    1 
ATOM   13129 N  NH1   . ARG C 2 282 ? 89.559  93.852  110.264 1.00 28.31 1  261 ARG C NH1   1 
ATOM   13130 N  NH2   . ARG C 2 282 ? 89.517  95.147  108.372 1.00 29.15 ?  261 ARG C NH2   1 
ATOM   13131 N  N     . TYR C 2 283 ? 96.775  94.025  108.346 1.00 27.78 ?  262 TYR C N     1 
ATOM   13132 C  CA    . TYR C 2 283 ? 97.978  94.133  107.523 1.00 28.18 ?  262 TYR C CA    1 
ATOM   13133 C  C     . TYR C 2 283 ? 99.229  93.688  108.303 1.00 27.08 ?  262 TYR C C     1 
ATOM   13134 O  O     . TYR C 2 283 ? 100.023 92.857  107.833 1.00 26.51 ?  262 TYR C O     1 
ATOM   13135 C  CB    . TYR C 2 283 ? 98.136  95.583  107.046 1.00 29.11 ?  262 TYR C CB    1 
ATOM   13136 C  CG    . TYR C 2 283 ? 99.335  95.835  106.165 1.00 32.56 ?  262 TYR C CG    1 
ATOM   13137 C  CD1   . TYR C 2 283 ? 99.338  95.428  104.830 1.00 36.59 ?  262 TYR C CD1   1 
ATOM   13138 C  CD2   . TYR C 2 283 ? 100.464 96.496  106.659 1.00 36.34 ?  262 TYR C CD2   1 
ATOM   13139 C  CE1   . TYR C 2 283 ? 100.441 95.662  104.003 1.00 39.47 ?  262 TYR C CE1   1 
ATOM   13140 C  CE2   . TYR C 2 283 ? 101.577 96.741  105.834 1.00 39.23 ?  262 TYR C CE2   1 
ATOM   13141 C  CZ    . TYR C 2 283 ? 101.553 96.317  104.509 1.00 40.48 ?  262 TYR C CZ    1 
ATOM   13142 O  OH    . TYR C 2 283 ? 102.634 96.542  103.686 1.00 44.00 ?  262 TYR C OH    1 
ATOM   13143 N  N     . ASN C 2 284 ? 99.381  94.222  109.506 1.00 26.08 ?  263 ASN C N     1 
ATOM   13144 C  CA    . ASN C 2 284 ? 100.527 93.886  110.337 1.00 25.73 ?  263 ASN C CA    1 
ATOM   13145 C  C     . ASN C 2 284 ? 100.488 92.486  110.954 1.00 25.24 ?  263 ASN C C     1 
ATOM   13146 O  O     . ASN C 2 284 ? 101.544 91.863  111.131 1.00 25.56 ?  263 ASN C O     1 
ATOM   13147 C  CB    . ASN C 2 284 ? 100.774 94.985  111.371 1.00 25.69 ?  263 ASN C CB    1 
ATOM   13148 C  CG    . ASN C 2 284 ? 101.389 96.218  110.749 1.00 26.39 ?  263 ASN C CG    1 
ATOM   13149 O  OD1   . ASN C 2 284 ? 102.582 96.238  110.432 1.00 26.91 ?  263 ASN C OD1   1 
ATOM   13150 N  ND2   . ASN C 2 284 ? 100.582 97.252  110.560 1.00 27.56 ?  263 ASN C ND2   1 
ATOM   13151 N  N     . ALA C 2 285 ? 99.290  91.975  111.249 1.00 24.51 ?  264 ALA C N     1 
ATOM   13152 C  CA    . ALA C 2 285 ? 99.139  90.557  111.626 1.00 24.19 ?  264 ALA C CA    1 
ATOM   13153 C  C     . ALA C 2 285 ? 99.750  89.610  110.573 1.00 24.63 ?  264 ALA C C     1 
ATOM   13154 O  O     . ALA C 2 285 ? 100.433 88.648  110.919 1.00 24.01 ?  264 ALA C O     1 
ATOM   13155 C  CB    . ALA C 2 285 ? 97.683  90.203  111.862 1.00 23.63 ?  264 ALA C CB    1 
ATOM   13156 N  N     . ASN C 2 286 ? 99.500  89.893  109.295 1.00 24.66 ?  265 ASN C N     1 
ATOM   13157 C  CA    . ASN C 2 286 ? 100.105 89.129  108.204 1.00 25.24 ?  265 ASN C CA    1 
ATOM   13158 C  C     . ASN C 2 286 ? 101.629 89.177  108.183 1.00 25.09 ?  265 ASN C C     1 
ATOM   13159 O  O     . ASN C 2 286 ? 102.273 88.169  107.848 1.00 24.14 ?  265 ASN C O     1 
ATOM   13160 C  CB    . ASN C 2 286 ? 99.549  89.571  106.838 1.00 25.62 ?  265 ASN C CB    1 
ATOM   13161 C  CG    . ASN C 2 286 ? 98.133  89.072  106.597 1.00 26.46 ?  265 ASN C CG    1 
ATOM   13162 O  OD1   . ASN C 2 286 ? 97.627  88.217  107.329 1.00 27.14 ?  265 ASN C OD1   1 
ATOM   13163 N  ND2   . ASN C 2 286 ? 97.477  89.620  105.572 1.00 27.89 ?  265 ASN C ND2   1 
ATOM   13164 N  N     . LYS C 2 287 ? 102.187 90.342  108.522 1.00 24.99 ?  266 LYS C N     1 
ATOM   13165 C  CA    . LYS C 2 287 ? 103.635 90.529  108.635 1.00 25.91 ?  266 LYS C CA    1 
ATOM   13166 C  C     . LYS C 2 287 ? 104.202 89.724  109.800 1.00 25.23 ?  266 LYS C C     1 
ATOM   13167 O  O     . LYS C 2 287 ? 105.286 89.146  109.687 1.00 25.34 ?  266 LYS C O     1 
ATOM   13168 C  CB    . LYS C 2 287 ? 103.997 92.000  108.838 1.00 25.96 ?  266 LYS C CB    1 
ATOM   13169 C  CG    . LYS C 2 287 ? 103.888 92.886  107.607 1.00 29.60 ?  266 LYS C CG    1 
ATOM   13170 C  CD    . LYS C 2 287 ? 104.533 94.243  107.918 1.00 34.20 ?  266 LYS C CD    1 
ATOM   13171 C  CE    . LYS C 2 287 ? 104.560 95.158  106.719 1.00 37.67 ?  266 LYS C CE    1 
ATOM   13172 N  NZ    . LYS C 2 287 ? 105.325 96.407  107.044 1.00 39.48 1  266 LYS C NZ    1 
ATOM   13173 N  N     . ALA C 2 288 ? 103.480 89.700  110.917 1.00 24.87 ?  267 ALA C N     1 
ATOM   13174 C  CA    . ALA C 2 288 ? 103.867 88.862  112.067 1.00 24.23 ?  267 ALA C CA    1 
ATOM   13175 C  C     . ALA C 2 288 ? 103.881 87.373  111.695 1.00 24.24 ?  267 ALA C C     1 
ATOM   13176 O  O     . ALA C 2 288 ? 104.838 86.660  112.002 1.00 23.96 ?  267 ALA C O     1 
ATOM   13177 C  CB    . ALA C 2 288 ? 102.943 89.108  113.245 1.00 24.23 ?  267 ALA C CB    1 
ATOM   13178 N  N     . LEU C 2 289 ? 102.824 86.907  111.030 1.00 24.63 ?  268 LEU C N     1 
ATOM   13179 C  CA    . LEU C 2 289 ? 102.780 85.521  110.556 1.00 25.14 ?  268 LEU C CA    1 
ATOM   13180 C  C     . LEU C 2 289 ? 103.954 85.231  109.635 1.00 25.58 ?  268 LEU C C     1 
ATOM   13181 O  O     . LEU C 2 289 ? 104.605 84.201  109.766 1.00 25.42 ?  268 LEU C O     1 
ATOM   13182 C  CB    . LEU C 2 289 ? 101.452 85.198  109.853 1.00 25.28 ?  268 LEU C CB    1 
ATOM   13183 C  CG    . LEU C 2 289 ? 100.242 85.043  110.779 1.00 25.93 ?  268 LEU C CG    1 
ATOM   13184 C  CD1   . LEU C 2 289 ? 98.947  85.180  110.002 1.00 26.50 ?  268 LEU C CD1   1 
ATOM   13185 C  CD2   . LEU C 2 289 ? 100.279 83.730  111.583 1.00 25.20 ?  268 LEU C CD2   1 
ATOM   13186 N  N     . MET C 2 290 ? 104.238 86.154  108.715 1.00 26.32 ?  269 MET C N     1 
ATOM   13187 C  CA    . MET C 2 290 ? 105.361 85.962  107.802 1.00 27.41 ?  269 MET C CA    1 
ATOM   13188 C  C     . MET C 2 290 ? 106.707 85.900  108.519 1.00 26.66 ?  269 MET C C     1 
ATOM   13189 O  O     . MET C 2 290 ? 107.566 85.096  108.148 1.00 26.69 ?  269 MET C O     1 
ATOM   13190 C  CB    . MET C 2 290 ? 105.351 87.002  106.686 1.00 28.28 ?  269 MET C CB    1 
ATOM   13191 C  CG    . MET C 2 290 ? 104.562 86.513  105.473 1.00 32.91 ?  269 MET C CG    1 
ATOM   13192 S  SD    . MET C 2 290 ? 104.231 87.811  104.278 1.00 42.49 ?  269 MET C SD    1 
ATOM   13193 C  CE    . MET C 2 290 ? 102.483 88.097  104.555 1.00 38.74 ?  269 MET C CE    1 
ATOM   13194 N  N     . ASN C 2 291 ? 106.873 86.717  109.561 1.00 25.48 ?  270 ASN C N     1 
ATOM   13195 C  CA    . ASN C 2 291 ? 108.078 86.679  110.406 1.00 25.39 ?  270 ASN C CA    1 
ATOM   13196 C  C     . ASN C 2 291 ? 108.275 85.309  111.075 1.00 25.18 ?  270 ASN C C     1 
ATOM   13197 O  O     . ASN C 2 291 ? 109.407 84.909  111.384 1.00 24.73 ?  270 ASN C O     1 
ATOM   13198 C  CB    . ASN C 2 291 ? 108.035 87.791  111.463 1.00 24.83 ?  270 ASN C CB    1 
ATOM   13199 C  CG    . ASN C 2 291 ? 108.324 89.178  110.879 1.00 25.58 ?  270 ASN C CG    1 
ATOM   13200 O  OD1   . ASN C 2 291 ? 108.790 89.309  109.751 1.00 25.58 ?  270 ASN C OD1   1 
ATOM   13201 N  ND2   . ASN C 2 291 ? 108.046 90.213  111.656 1.00 24.32 ?  270 ASN C ND2   1 
ATOM   13202 N  N     . LEU C 2 292 ? 107.159 84.598  111.261 1.00 25.09 ?  271 LEU C N     1 
ATOM   13203 C  CA    . LEU C 2 292 ? 107.133 83.238  111.816 1.00 25.46 ?  271 LEU C CA    1 
ATOM   13204 C  C     . LEU C 2 292 ? 107.196 82.122  110.760 1.00 26.18 ?  271 LEU C C     1 
ATOM   13205 O  O     . LEU C 2 292 ? 107.155 80.923  111.094 1.00 26.06 ?  271 LEU C O     1 
ATOM   13206 C  CB    . LEU C 2 292 ? 105.897 83.069  112.708 1.00 25.19 ?  271 LEU C CB    1 
ATOM   13207 C  CG    . LEU C 2 292 ? 105.876 83.932  113.981 1.00 25.03 ?  271 LEU C CG    1 
ATOM   13208 C  CD1   . LEU C 2 292 ? 104.503 83.912  114.613 1.00 24.50 ?  271 LEU C CD1   1 
ATOM   13209 C  CD2   . LEU C 2 292 ? 106.946 83.449  114.974 1.00 25.64 ?  271 LEU C CD2   1 
ATOM   13210 N  N     . GLY C 2 293 ? 107.300 82.511  109.490 1.00 26.71 ?  272 GLY C N     1 
ATOM   13211 C  CA    . GLY C 2 293 ? 107.351 81.552  108.380 1.00 28.06 ?  272 GLY C CA    1 
ATOM   13212 C  C     . GLY C 2 293 ? 106.009 80.961  107.977 1.00 29.34 ?  272 GLY C C     1 
ATOM   13213 O  O     . GLY C 2 293 ? 105.954 79.885  107.364 1.00 29.73 ?  272 GLY C O     1 
ATOM   13214 N  N     . PHE C 2 294 ? 104.927 81.658  108.318 1.00 29.88 ?  273 PHE C N     1 
ATOM   13215 C  CA    . PHE C 2 294 ? 103.573 81.209  108.004 1.00 31.24 ?  273 PHE C CA    1 
ATOM   13216 C  C     . PHE C 2 294 ? 102.942 82.074  106.904 1.00 32.42 ?  273 PHE C C     1 
ATOM   13217 O  O     . PHE C 2 294 ? 103.354 83.222  106.684 1.00 32.30 ?  273 PHE C O     1 
ATOM   13218 C  CB    . PHE C 2 294 ? 102.690 81.211  109.258 1.00 30.82 ?  273 PHE C CB    1 
ATOM   13219 C  CG    . PHE C 2 294 ? 103.179 80.298  110.363 1.00 30.93 ?  273 PHE C CG    1 
ATOM   13220 C  CD1   . PHE C 2 294 ? 103.543 78.978  110.100 1.00 30.85 ?  273 PHE C CD1   1 
ATOM   13221 C  CD2   . PHE C 2 294 ? 103.262 80.759  111.669 1.00 30.30 ?  273 PHE C CD2   1 
ATOM   13222 C  CE1   . PHE C 2 294 ? 103.998 78.144  111.119 1.00 30.75 ?  273 PHE C CE1   1 
ATOM   13223 C  CE2   . PHE C 2 294 ? 103.702 79.929  112.702 1.00 30.41 ?  273 PHE C CE2   1 
ATOM   13224 C  CZ    . PHE C 2 294 ? 104.066 78.617  112.428 1.00 30.88 ?  273 PHE C CZ    1 
ATOM   13225 N  N     . ASP C 2 295 ? 101.957 81.507  106.211 1.00 33.81 ?  274 ASP C N     1 
ATOM   13226 C  CA    . ASP C 2 295 ? 101.205 82.220  105.174 1.00 35.32 ?  274 ASP C CA    1 
ATOM   13227 C  C     . ASP C 2 295 ? 100.320 83.327  105.775 1.00 35.36 ?  274 ASP C C     1 
ATOM   13228 O  O     . ASP C 2 295 ? 99.838  83.185  106.896 1.00 34.78 ?  274 ASP C O     1 
ATOM   13229 C  CB    . ASP C 2 295 ? 100.316 81.240  104.397 1.00 35.95 ?  274 ASP C CB    1 
ATOM   13230 C  CG    . ASP C 2 295 ? 101.114 80.190  103.628 1.00 37.98 ?  274 ASP C CG    1 
ATOM   13231 O  OD1   . ASP C 2 295 ? 102.274 80.453  103.242 1.00 39.83 ?  274 ASP C OD1   1 
ATOM   13232 O  OD2   . ASP C 2 295 ? 100.565 79.090  103.405 1.00 40.03 -1 274 ASP C OD2   1 
ATOM   13233 N  N     . PRO C 2 296 ? 100.098 84.425  105.027 1.00 36.33 ?  275 PRO C N     1 
ATOM   13234 C  CA    . PRO C 2 296 ? 99.156  85.472  105.481 1.00 36.92 ?  275 PRO C CA    1 
ATOM   13235 C  C     . PRO C 2 296 ? 97.749  84.922  105.766 1.00 37.68 ?  275 PRO C C     1 
ATOM   13236 O  O     . PRO C 2 296 ? 97.288  84.014  105.069 1.00 38.07 ?  275 PRO C O     1 
ATOM   13237 C  CB    . PRO C 2 296 ? 99.122  86.460  104.304 1.00 36.82 ?  275 PRO C CB    1 
ATOM   13238 C  CG    . PRO C 2 296 ? 99.782  85.733  103.141 1.00 37.42 ?  275 PRO C CG    1 
ATOM   13239 C  CD    . PRO C 2 296 ? 100.762 84.795  103.764 1.00 36.41 ?  275 PRO C CD    1 
ATOM   13240 N  N     . TYR C 2 297 ? 97.083  85.472  106.782 1.00 38.10 ?  276 TYR C N     1 
ATOM   13241 C  CA    . TYR C 2 297 ? 95.787  84.963  107.254 1.00 38.96 ?  276 TYR C CA    1 
ATOM   13242 C  C     . TYR C 2 297 ? 94.614  85.875  106.874 1.00 39.71 ?  276 TYR C C     1 
ATOM   13243 O  O     . TYR C 2 297 ? 93.481  85.408  106.714 1.00 40.18 ?  276 TYR C O     1 
ATOM   13244 C  CB    . TYR C 2 297 ? 95.840  84.787  108.775 1.00 38.94 ?  276 TYR C CB    1 
ATOM   13245 C  CG    . TYR C 2 297 ? 94.633  84.170  109.449 1.00 39.64 ?  276 TYR C CG    1 
ATOM   13246 C  CD1   . TYR C 2 297 ? 94.454  82.785  109.484 1.00 40.43 ?  276 TYR C CD1   1 
ATOM   13247 C  CD2   . TYR C 2 297 ? 93.701  84.966  110.107 1.00 41.04 ?  276 TYR C CD2   1 
ATOM   13248 C  CE1   . TYR C 2 297 ? 93.352  82.214  110.123 1.00 41.69 ?  276 TYR C CE1   1 
ATOM   13249 C  CE2   . TYR C 2 297 ? 92.594  84.409  110.748 1.00 41.60 ?  276 TYR C CE2   1 
ATOM   13250 C  CZ    . TYR C 2 297 ? 92.428  83.034  110.757 1.00 41.92 ?  276 TYR C CZ    1 
ATOM   13251 O  OH    . TYR C 2 297 ? 91.339  82.489  111.400 1.00 42.52 ?  276 TYR C OH    1 
ATOM   13252 N  N     . PHE C 2 298 ? 94.880  87.170  106.744 1.00 39.85 ?  277 PHE C N     1 
ATOM   13253 C  CA    . PHE C 2 298 ? 93.836  88.128  106.401 1.00 40.77 ?  277 PHE C CA    1 
ATOM   13254 C  C     . PHE C 2 298 ? 93.976  88.578  104.956 1.00 41.95 ?  277 PHE C C     1 
ATOM   13255 O  O     . PHE C 2 298 ? 95.086  88.633  104.428 1.00 41.91 ?  277 PHE C O     1 
ATOM   13256 C  CB    . PHE C 2 298 ? 93.891  89.338  107.340 1.00 39.94 ?  277 PHE C CB    1 
ATOM   13257 C  CG    . PHE C 2 298 ? 93.623  89.006  108.782 1.00 39.09 ?  277 PHE C CG    1 
ATOM   13258 C  CD1   . PHE C 2 298 ? 94.657  88.999  109.710 1.00 37.84 ?  277 PHE C CD1   1 
ATOM   13259 C  CD2   . PHE C 2 298 ? 92.332  88.716  109.217 1.00 38.97 ?  277 PHE C CD2   1 
ATOM   13260 C  CE1   . PHE C 2 298 ? 94.418  88.699  111.049 1.00 37.46 ?  277 PHE C CE1   1 
ATOM   13261 C  CE2   . PHE C 2 298 ? 92.080  88.414  110.550 1.00 38.20 ?  277 PHE C CE2   1 
ATOM   13262 C  CZ    . PHE C 2 298 ? 93.126  88.407  111.471 1.00 37.91 ?  277 PHE C CZ    1 
ATOM   13263 N  N     . GLU C 2 299 ? 92.855  88.897  104.307 1.00 43.74 ?  278 GLU C N     1 
ATOM   13264 C  CA    . GLU C 2 299 ? 92.904  89.387  102.926 1.00 45.61 ?  278 GLU C CA    1 
ATOM   13265 C  C     . GLU C 2 299 ? 93.448  90.816  102.880 1.00 46.04 ?  278 GLU C C     1 
ATOM   13266 O  O     . GLU C 2 299 ? 93.269  91.588  103.822 1.00 45.88 ?  278 GLU C O     1 
ATOM   13267 C  CB    . GLU C 2 299 ? 91.533  89.316  102.246 1.00 46.43 ?  278 GLU C CB    1 
ATOM   13268 C  CG    . GLU C 2 299 ? 91.617  89.085  100.727 1.00 48.82 ?  278 GLU C CG    1 
ATOM   13269 C  CD    . GLU C 2 299 ? 90.359  89.498  99.978  1.00 51.86 ?  278 GLU C CD    1 
ATOM   13270 O  OE1   . GLU C 2 299 ? 90.343  89.361  98.734  1.00 53.35 ?  278 GLU C OE1   1 
ATOM   13271 O  OE2   . GLU C 2 299 ? 89.389  89.964  100.621 1.00 53.10 -1 278 GLU C OE2   1 
ATOM   13272 N  N     . GLU C 2 300 ? 94.125  91.149  101.783 1.00 47.16 ?  279 GLU C N     1 
ATOM   13273 C  CA    . GLU C 2 300 ? 94.693  92.486  101.576 1.00 47.75 ?  279 GLU C CA    1 
ATOM   13274 C  C     . GLU C 2 300 ? 93.615  93.573  101.453 1.00 47.71 ?  279 GLU C C     1 
ATOM   13275 O  O     . GLU C 2 300 ? 92.561  93.349  100.847 1.00 47.77 ?  279 GLU C O     1 
ATOM   13276 C  CB    . GLU C 2 300 ? 95.621  92.488  100.349 1.00 48.42 ?  279 GLU C CB    1 
ATOM   13277 C  CG    . GLU C 2 300 ? 95.007  91.891  99.077  1.00 50.63 ?  279 GLU C CG    1 
ATOM   13278 C  CD    . GLU C 2 300 ? 96.055  91.398  98.078  1.00 53.06 ?  279 GLU C CD    1 
ATOM   13279 O  OE1   . GLU C 2 300 ? 96.952  92.189  97.700  1.00 54.35 ?  279 GLU C OE1   1 
ATOM   13280 O  OE2   . GLU C 2 300 ? 95.969  90.220  97.661  1.00 53.32 -1 279 GLU C OE2   1 
ATOM   13281 N  N     . GLU C 2 301 ? 93.886  94.733  102.052 1.00 47.40 ?  280 GLU C N     1 
ATOM   13282 C  CA    . GLU C 2 301 ? 92.990  95.896  102.009 1.00 47.46 ?  280 GLU C CA    1 
ATOM   13283 C  C     . GLU C 2 301 ? 93.791  97.186  101.797 1.00 47.31 ?  280 GLU C C     1 
ATOM   13284 O  O     . GLU C 2 301 ? 94.984  97.237  102.111 1.00 47.21 ?  280 GLU C O     1 
ATOM   13285 C  CB    . GLU C 2 301 ? 92.183  96.012  103.310 1.00 47.19 ?  280 GLU C CB    1 
ATOM   13286 C  CG    . GLU C 2 301 ? 91.267  94.831  103.636 1.00 47.14 ?  280 GLU C CG    1 
ATOM   13287 C  CD    . GLU C 2 301 ? 90.910  94.764  105.118 1.00 47.21 ?  280 GLU C CD    1 
ATOM   13288 O  OE1   . GLU C 2 301 ? 89.755  95.086  105.466 1.00 46.97 ?  280 GLU C OE1   1 
ATOM   13289 O  OE2   . GLU C 2 301 ? 91.789  94.401  105.938 1.00 46.13 -1 280 GLU C OE2   1 
ATOM   13290 N  N     . ASP C 2 302 ? 93.137  98.222  101.272 1.00 47.15 ?  281 ASP C N     1 
ATOM   13291 C  CA    . ASP C 2 302 ? 93.783  99.525  101.083 1.00 47.04 ?  281 ASP C CA    1 
ATOM   13292 C  C     . ASP C 2 302 ? 93.934  100.255 102.421 1.00 46.05 ?  281 ASP C C     1 
ATOM   13293 O  O     . ASP C 2 302 ? 92.939  100.553 103.091 1.00 46.10 ?  281 ASP C O     1 
ATOM   13294 C  CB    . ASP C 2 302 ? 92.997  100.403 100.092 1.00 47.66 ?  281 ASP C CB    1 
ATOM   13295 C  CG    . ASP C 2 302 ? 93.135  99.942  98.638  1.00 49.53 ?  281 ASP C CG    1 
ATOM   13296 O  OD1   . ASP C 2 302 ? 94.216  99.445  98.251  1.00 50.58 ?  281 ASP C OD1   1 
ATOM   13297 O  OD2   . ASP C 2 302 ? 92.156  100.106 97.870  1.00 51.14 -1 281 ASP C OD2   1 
ATOM   13298 N  N     . ILE C 2 303 ? 95.180  100.524 102.806 1.00 44.96 ?  282 ILE C N     1 
ATOM   13299 C  CA    . ILE C 2 303 ? 95.490  101.281 104.024 1.00 43.99 ?  282 ILE C CA    1 
ATOM   13300 C  C     . ILE C 2 303 ? 95.446  102.782 103.724 1.00 43.53 ?  282 ILE C C     1 
ATOM   13301 O  O     . ILE C 2 303 ? 95.785  103.200 102.615 1.00 43.52 ?  282 ILE C O     1 
ATOM   13302 C  CB    . ILE C 2 303 ? 96.888  100.893 104.591 1.00 43.84 ?  282 ILE C CB    1 
ATOM   13303 C  CG1   . ILE C 2 303 ? 96.997  99.373  104.820 1.00 43.91 ?  282 ILE C CG1   1 
ATOM   13304 C  CG2   . ILE C 2 303 ? 97.225  101.691 105.863 1.00 43.55 ?  282 ILE C CG2   1 
ATOM   13305 C  CD1   . ILE C 2 303 ? 95.965  98.779  105.782 1.00 42.76 ?  282 ILE C CD1   1 
ATOM   13306 N  N     . ASN C 2 304 ? 95.019  103.581 104.703 1.00 42.51 ?  283 ASN C N     1 
ATOM   13307 C  CA    . ASN C 2 304 ? 94.987  105.037 104.559 1.00 41.93 ?  283 ASN C CA    1 
ATOM   13308 C  C     . ASN C 2 304 ? 96.336  105.555 104.036 1.00 41.78 ?  283 ASN C C     1 
ATOM   13309 O  O     . ASN C 2 304 ? 97.373  105.323 104.673 1.00 41.13 ?  283 ASN C O     1 
ATOM   13310 C  CB    . ASN C 2 304 ? 94.637  105.697 105.902 1.00 41.83 ?  283 ASN C CB    1 
ATOM   13311 C  CG    . ASN C 2 304 ? 94.108  107.123 105.749 1.00 41.27 ?  283 ASN C CG    1 
ATOM   13312 O  OD1   . ASN C 2 304 ? 94.652  107.932 105.001 1.00 41.28 ?  283 ASN C OD1   1 
ATOM   13313 N  ND2   . ASN C 2 304 ? 93.043  107.431 106.474 1.00 40.67 ?  283 ASN C ND2   1 
ATOM   13314 N  N     . PRO C 2 305 ? 96.331  106.239 102.866 1.00 41.74 ?  284 PRO C N     1 
ATOM   13315 C  CA    . PRO C 2 305 ? 97.594  106.698 102.265 1.00 41.82 ?  284 PRO C CA    1 
ATOM   13316 C  C     . PRO C 2 305 ? 98.344  107.710 103.139 1.00 41.56 ?  284 PRO C C     1 
ATOM   13317 O  O     . PRO C 2 305 ? 99.560  107.857 103.003 1.00 41.46 ?  284 PRO C O     1 
ATOM   13318 C  CB    . PRO C 2 305 ? 97.156  107.330 100.930 1.00 42.14 ?  284 PRO C CB    1 
ATOM   13319 C  CG    . PRO C 2 305 ? 95.714  107.638 101.093 1.00 42.59 ?  284 PRO C CG    1 
ATOM   13320 C  CD    . PRO C 2 305 ? 95.167  106.586 102.027 1.00 42.05 ?  284 PRO C CD    1 
ATOM   13321 N  N     . ILE C 2 306 ? 97.621  108.380 104.034 1.00 41.19 ?  285 ILE C N     1 
ATOM   13322 C  CA    . ILE C 2 306 ? 98.223  109.287 105.012 1.00 41.47 ?  285 ILE C CA    1 
ATOM   13323 C  C     . ILE C 2 306 ? 99.207  108.524 105.909 1.00 41.71 ?  285 ILE C C     1 
ATOM   13324 O  O     . ILE C 2 306 ? 100.329 108.976 106.135 1.00 41.38 ?  285 ILE C O     1 
ATOM   13325 C  CB    . ILE C 2 306 ? 97.143  109.973 105.890 1.00 41.22 ?  285 ILE C CB    1 
ATOM   13326 C  CG1   . ILE C 2 306 ? 96.210  110.836 105.029 1.00 41.27 ?  285 ILE C CG1   1 
ATOM   13327 C  CG2   . ILE C 2 306 ? 97.786  110.796 107.004 1.00 40.37 ?  285 ILE C CG2   1 
ATOM   13328 C  CD1   . ILE C 2 306 ? 94.921  111.235 105.733 1.00 41.85 ?  285 ILE C CD1   1 
ATOM   13329 N  N     . VAL C 2 307 ? 98.768  107.369 106.407 1.00 42.33 ?  286 VAL C N     1 
ATOM   13330 C  CA    . VAL C 2 307 ? 99.595  106.502 107.253 1.00 43.36 ?  286 VAL C CA    1 
ATOM   13331 C  C     . VAL C 2 307 ? 100.819 105.961 106.502 1.00 44.51 ?  286 VAL C C     1 
ATOM   13332 O  O     . VAL C 2 307 ? 101.888 105.810 107.090 1.00 44.57 ?  286 VAL C O     1 
ATOM   13333 C  CB    . VAL C 2 307 ? 98.750  105.366 107.879 1.00 42.97 ?  286 VAL C CB    1 
ATOM   13334 C  CG1   . VAL C 2 307 ? 99.637  104.257 108.470 1.00 42.86 ?  286 VAL C CG1   1 
ATOM   13335 C  CG2   . VAL C 2 307 ? 97.836  105.947 108.941 1.00 41.93 ?  286 VAL C CG2   1 
ATOM   13336 N  N     . LEU C 2 308 ? 100.650 105.699 105.206 1.00 46.21 ?  287 LEU C N     1 
ATOM   13337 C  CA    . LEU C 2 308 ? 101.739 105.255 104.324 1.00 47.66 ?  287 LEU C CA    1 
ATOM   13338 C  C     . LEU C 2 308 ? 102.775 106.352 104.085 1.00 48.82 ?  287 LEU C C     1 
ATOM   13339 O  O     . LEU C 2 308 ? 103.975 106.067 103.969 1.00 49.02 ?  287 LEU C O     1 
ATOM   13340 C  CB    . LEU C 2 308 ? 101.179 104.738 102.992 1.00 47.95 ?  287 LEU C CB    1 
ATOM   13341 C  CG    . LEU C 2 308 ? 100.835 103.244 102.868 1.00 48.23 ?  287 LEU C CG    1 
ATOM   13342 C  CD1   . LEU C 2 308 ? 100.492 102.571 104.205 1.00 48.10 ?  287 LEU C CD1   1 
ATOM   13343 C  CD2   . LEU C 2 308 ? 99.727  103.016 101.843 1.00 48.81 ?  287 LEU C CD2   1 
ATOM   13344 N  N     . ASN C 2 309 ? 102.306 107.599 104.011 1.00 49.80 ?  288 ASN C N     1 
ATOM   13345 C  CA    . ASN C 2 309 ? 103.188 108.763 104.015 1.00 51.09 ?  288 ASN C CA    1 
ATOM   13346 C  C     . ASN C 2 309 ? 103.845 108.998 105.379 1.00 51.08 ?  288 ASN C C     1 
ATOM   13347 O  O     . ASN C 2 309 ? 104.914 109.601 105.459 1.00 51.41 ?  288 ASN C O     1 
ATOM   13348 C  CB    . ASN C 2 309 ? 102.450 110.017 103.542 1.00 51.37 ?  288 ASN C CB    1 
ATOM   13349 C  CG    . ASN C 2 309 ? 102.352 110.098 102.031 1.00 53.22 ?  288 ASN C CG    1 
ATOM   13350 O  OD1   . ASN C 2 309 ? 102.009 109.118 101.361 1.00 54.39 ?  288 ASN C OD1   1 
ATOM   13351 N  ND2   . ASN C 2 309 ? 102.657 111.270 101.483 1.00 54.70 ?  288 ASN C ND2   1 
ATOM   13352 N  N     . GLY C 2 310 ? 103.199 108.519 106.442 1.00 51.25 ?  289 GLY C N     1 
ATOM   13353 C  CA    . GLY C 2 310 ? 103.770 108.542 107.790 1.00 51.35 ?  289 GLY C CA    1 
ATOM   13354 C  C     . GLY C 2 310 ? 104.997 107.651 107.940 1.00 51.86 ?  289 GLY C C     1 
ATOM   13355 O  O     . GLY C 2 310 ? 105.806 107.848 108.854 1.00 51.49 ?  289 GLY C O     1 
ATOM   13356 N  N     . LEU C 2 311 ? 105.134 106.671 107.046 1.00 52.45 ?  290 LEU C N     1 
ATOM   13357 C  CA    . LEU C 2 311 ? 106.293 105.776 107.029 1.00 52.99 ?  290 LEU C CA    1 
ATOM   13358 C  C     . LEU C 2 311 ? 107.440 106.362 106.200 1.00 53.65 ?  290 LEU C C     1 
ATOM   13359 O  O     . LEU C 2 311 ? 107.365 106.444 104.968 1.00 54.22 ?  290 LEU C O     1 
ATOM   13360 C  CB    . LEU C 2 311 ? 105.904 104.394 106.494 1.00 53.08 ?  290 LEU C CB    1 
ATOM   13361 C  CG    . LEU C 2 311 ? 105.056 103.466 107.369 1.00 53.33 ?  290 LEU C CG    1 
ATOM   13362 C  CD1   . LEU C 2 311 ? 104.474 102.337 106.531 1.00 53.79 ?  290 LEU C CD1   1 
ATOM   13363 C  CD2   . LEU C 2 311 ? 105.865 102.907 108.542 1.00 53.22 ?  290 LEU C CD2   1 
ATOM   13364 N  N     . LYS C 2 330 ? 141.449 111.069 117.648 1.00 58.93 ?  309 LYS C N     1 
ATOM   13365 C  CA    . LYS C 2 330 ? 142.907 111.088 117.614 1.00 61.98 ?  309 LYS C CA    1 
ATOM   13366 C  C     . LYS C 2 330 ? 143.437 110.532 116.296 1.00 61.97 ?  309 LYS C C     1 
ATOM   13367 O  O     . LYS C 2 330 ? 142.862 109.608 115.722 1.00 59.24 ?  309 LYS C O     1 
ATOM   13368 C  CB    . LYS C 2 330 ? 143.482 110.291 118.786 1.00 60.82 ?  309 LYS C CB    1 
ATOM   13369 C  CG    . LYS C 2 330 ? 143.121 110.845 120.154 1.00 60.80 ?  309 LYS C CG    1 
ATOM   13370 C  CD    . LYS C 2 330 ? 143.898 112.117 120.456 1.00 60.28 ?  309 LYS C CD    1 
ATOM   13371 C  CE    . LYS C 2 330 ? 144.777 111.952 121.685 1.00 62.15 ?  309 LYS C CE    1 
ATOM   13372 N  NZ    . LYS C 2 330 ? 144.166 111.042 122.692 1.00 62.59 1  309 LYS C NZ    1 
ATOM   13373 N  N     . ALA C 2 331 ? 144.539 111.105 115.824 1.00 55.97 ?  310 ALA C N     1 
ATOM   13374 C  CA    . ALA C 2 331 ? 145.193 110.675 114.600 1.00 53.20 ?  310 ALA C CA    1 
ATOM   13375 C  C     . ALA C 2 331 ? 146.606 110.197 114.905 1.00 52.13 ?  310 ALA C C     1 
ATOM   13376 O  O     . ALA C 2 331 ? 147.224 110.624 115.885 1.00 53.07 ?  310 ALA C O     1 
ATOM   13377 C  CB    . ALA C 2 331 ? 145.235 111.807 113.568 1.00 51.98 ?  310 ALA C CB    1 
ATOM   13378 N  N     . THR C 2 332 ? 147.105 109.298 114.059 1.00 45.82 ?  311 THR C N     1 
ATOM   13379 C  CA    . THR C 2 332 ? 148.456 108.777 114.224 1.00 46.85 ?  311 THR C CA    1 
ATOM   13380 C  C     . THR C 2 332 ? 149.477 109.906 114.157 1.00 43.12 ?  311 THR C C     1 
ATOM   13381 O  O     . THR C 2 332 ? 149.354 110.833 113.352 1.00 48.26 ?  311 THR C O     1 
ATOM   13382 C  CB    . THR C 2 332 ? 148.749 107.722 113.156 1.00 45.72 ?  311 THR C CB    1 
ATOM   13383 O  OG1   . THR C 2 332 ? 149.990 107.067 113.448 1.00 46.36 ?  311 THR C OG1   1 
ATOM   13384 C  CG2   . THR C 2 332 ? 148.799 108.351 111.775 1.00 44.89 ?  311 THR C CG2   1 
ATOM   13385 N  N     . VAL C 2 333 ? 150.484 109.827 115.022 1.00 42.01 ?  312 VAL C N     1 
ATOM   13386 C  CA    . VAL C 2 333 ? 151.437 110.909 115.240 1.00 38.55 ?  312 VAL C CA    1 
ATOM   13387 C  C     . VAL C 2 333 ? 152.826 110.409 114.869 1.00 41.18 ?  312 VAL C C     1 
ATOM   13388 O  O     . VAL C 2 333 ? 153.292 109.392 115.400 1.00 46.85 ?  312 VAL C O     1 
ATOM   13389 C  CB    . VAL C 2 333 ? 151.404 111.407 116.691 1.00 37.39 ?  312 VAL C CB    1 
ATOM   13390 C  CG1   . VAL C 2 333 ? 152.621 112.268 116.988 1.00 40.81 ?  312 VAL C CG1   1 
ATOM   13391 C  CG2   . VAL C 2 333 ? 150.117 112.165 116.969 1.00 39.47 ?  312 VAL C CG2   1 
ATOM   13392 N  N     . GLU C 2 334 ? 153.493 111.120 113.957 1.00 34.01 ?  313 GLU C N     1 
ATOM   13393 C  CA    . GLU C 2 334 ? 154.907 110.892 113.713 1.00 34.45 ?  313 GLU C CA    1 
ATOM   13394 C  C     . GLU C 2 334 ? 155.709 112.140 114.068 1.00 37.55 ?  313 GLU C C     1 
ATOM   13395 O  O     . GLU C 2 334 ? 155.233 113.264 113.880 1.00 40.51 ?  313 GLU C O     1 
ATOM   13396 C  CB    . GLU C 2 334 ? 155.199 110.528 112.252 1.00 34.27 ?  313 GLU C CB    1 
ATOM   13397 C  CG    . GLU C 2 334 ? 154.386 109.385 111.685 1.00 38.73 ?  313 GLU C CG    1 
ATOM   13398 C  CD    . GLU C 2 334 ? 154.810 109.034 110.271 1.00 42.14 ?  313 GLU C CD    1 
ATOM   13399 O  OE1   . GLU C 2 334 ? 155.917 108.482 110.104 1.00 40.76 ?  313 GLU C OE1   1 
ATOM   13400 O  OE2   . GLU C 2 334 ? 154.048 109.323 109.327 1.00 39.96 -1 313 GLU C OE2   1 
ATOM   13401 N  N     . PRO C 2 335 ? 156.923 111.980 114.586 1.00 33.56 ?  314 PRO C N     1 
ATOM   13402 C  CA    . PRO C 2 335 ? 157.777 113.144 114.836 1.00 34.05 ?  314 PRO C CA    1 
ATOM   13403 C  C     . PRO C 2 335 ? 158.256 113.759 113.529 1.00 35.93 ?  314 PRO C C     1 
ATOM   13404 O  O     . PRO C 2 335 ? 158.302 113.116 112.478 1.00 36.72 ?  314 PRO C O     1 
ATOM   13405 C  CB    . PRO C 2 335 ? 158.946 112.574 115.649 1.00 36.78 ?  314 PRO C CB    1 
ATOM   13406 C  CG    . PRO C 2 335 ? 158.499 111.203 116.086 1.00 33.20 ?  314 PRO C CG    1 
ATOM   13407 C  CD    . PRO C 2 335 ? 157.553 110.730 115.035 1.00 33.09 ?  314 PRO C CD    1 
ATOM   13408 N  N     . LEU C 2 336 ? 158.616 115.035 113.608 1.00 31.29 ?  315 LEU C N     1 
ATOM   13409 C  CA    . LEU C 2 336 ? 159.102 115.773 112.451 1.00 25.88 ?  315 LEU C CA    1 
ATOM   13410 C  C     . LEU C 2 336 ? 160.592 115.531 112.262 1.00 28.32 ?  315 LEU C C     1 
ATOM   13411 O  O     . LEU C 2 336 ? 161.387 115.752 113.182 1.00 26.34 ?  315 LEU C O     1 
ATOM   13412 C  CB    . LEU C 2 336 ? 158.828 117.269 112.608 1.00 25.22 ?  315 LEU C CB    1 
ATOM   13413 C  CG    . LEU C 2 336 ? 157.451 117.743 112.147 1.00 26.15 ?  315 LEU C CG    1 
ATOM   13414 C  CD1   . LEU C 2 336 ? 157.296 119.234 112.379 1.00 26.32 ?  315 LEU C CD1   1 
ATOM   13415 C  CD2   . LEU C 2 336 ? 157.259 117.404 110.680 1.00 21.64 ?  315 LEU C CD2   1 
ATOM   13416 N  N     . LYS C 2 337 ? 160.964 115.076 111.071 1.00 24.69 ?  316 LYS C N     1 
ATOM   13417 C  CA    . LYS C 2 337 ? 162.361 114.902 110.713 1.00 25.14 ?  316 LYS C CA    1 
ATOM   13418 C  C     . LYS C 2 337 ? 162.938 116.218 110.204 1.00 19.78 ?  316 LYS C C     1 
ATOM   13419 O  O     . LYS C 2 337 ? 162.214 117.122 109.785 1.00 30.21 ?  316 LYS C O     1 
ATOM   13420 C  CB    . LYS C 2 337 ? 162.517 113.815 109.649 1.00 29.25 ?  316 LYS C CB    1 
ATOM   13421 C  CG    . LYS C 2 337 ? 161.558 112.647 109.802 1.00 28.02 ?  316 LYS C CG    1 
ATOM   13422 C  CD    . LYS C 2 337 ? 162.265 111.415 110.340 1.00 27.52 ?  316 LYS C CD    1 
ATOM   13423 C  CE    . LYS C 2 337 ? 161.356 110.615 111.258 1.00 32.76 ?  316 LYS C CE    1 
ATOM   13424 N  NZ    . LYS C 2 337 ? 162.109 109.589 112.032 1.00 30.53 1  316 LYS C NZ    1 
ATOM   13425 N  N     . ASP C 2 338 ? 164.267 116.316 110.249 1.00 29.74 ?  317 ASP C N     1 
ATOM   13426 C  CA    . ASP C 2 338 ? 164.938 117.504 109.739 1.00 26.29 ?  317 ASP C CA    1 
ATOM   13427 C  C     . ASP C 2 338 ? 164.775 117.657 108.233 1.00 29.71 ?  317 ASP C C     1 
ATOM   13428 O  O     . ASP C 2 338 ? 164.959 118.761 107.712 1.00 21.95 ?  317 ASP C O     1 
ATOM   13429 C  CB    . ASP C 2 338 ? 166.423 117.469 110.103 1.00 25.78 ?  317 ASP C CB    1 
ATOM   13430 C  CG    . ASP C 2 338 ? 166.659 117.025 111.531 1.00 35.15 ?  317 ASP C CG    1 
ATOM   13431 O  OD1   . ASP C 2 338 ? 166.215 115.914 111.891 1.00 32.75 ?  317 ASP C OD1   1 
ATOM   13432 O  OD2   . ASP C 2 338 ? 167.289 117.786 112.296 1.00 36.30 -1 317 ASP C OD2   1 
ATOM   13433 N  N     . ASP C 2 339 ? 164.433 116.581 107.526 1.00 26.99 ?  318 ASP C N     1 
ATOM   13434 C  CA    . ASP C 2 339 ? 164.226 116.633 106.087 1.00 24.15 ?  318 ASP C CA    1 
ATOM   13435 C  C     . ASP C 2 339 ? 162.831 117.105 105.700 1.00 20.41 ?  318 ASP C C     1 
ATOM   13436 O  O     . ASP C 2 339 ? 162.599 117.401 104.524 1.00 28.59 ?  318 ASP C O     1 
ATOM   13437 C  CB    . ASP C 2 339 ? 164.487 115.256 105.466 1.00 23.02 ?  318 ASP C CB    1 
ATOM   13438 C  CG    . ASP C 2 339 ? 165.606 114.507 106.163 1.00 32.33 ?  318 ASP C CG    1 
ATOM   13439 O  OD1   . ASP C 2 339 ? 165.313 113.528 106.881 1.00 34.56 ?  318 ASP C OD1   1 
ATOM   13440 O  OD2   . ASP C 2 339 ? 166.779 114.898 105.992 1.00 32.78 -1 318 ASP C OD2   1 
ATOM   13441 N  N     . ASP C 2 340 ? 161.903 117.182 106.652 1.00 18.60 ?  319 ASP C N     1 
ATOM   13442 C  CA    . ASP C 2 340 ? 160.565 117.692 106.390 1.00 13.68 ?  319 ASP C CA    1 
ATOM   13443 C  C     . ASP C 2 340 ? 160.508 119.212 106.387 1.00 14.05 ?  319 ASP C C     1 
ATOM   13444 O  O     . ASP C 2 340 ? 159.461 119.780 106.059 1.00 30.27 ?  319 ASP C O     1 
ATOM   13445 C  CB    . ASP C 2 340 ? 159.577 117.143 107.424 1.00 12.38 ?  319 ASP C CB    1 
ATOM   13446 C  CG    . ASP C 2 340 ? 159.726 115.653 107.638 1.00 24.62 ?  319 ASP C CG    1 
ATOM   13447 O  OD1   . ASP C 2 340 ? 159.889 114.920 106.641 1.00 25.90 ?  319 ASP C OD1   1 
ATOM   13448 O  OD2   . ASP C 2 340 ? 159.672 115.212 108.805 1.00 30.97 -1 319 ASP C OD2   1 
ATOM   13449 N  N     . PHE C 2 341 ? 161.600 119.879 106.749 1.00 14.34 ?  320 PHE C N     1 
ATOM   13450 C  CA    . PHE C 2 341 ? 161.675 121.331 106.766 1.00 3.83  ?  320 PHE C CA    1 
ATOM   13451 C  C     . PHE C 2 341 ? 162.334 121.895 105.515 1.00 6.43  ?  320 PHE C C     1 
ATOM   13452 O  O     . PHE C 2 341 ? 162.541 123.109 105.429 1.00 11.38 ?  320 PHE C O     1 
ATOM   13453 C  CB    . PHE C 2 341 ? 162.430 121.801 108.008 1.00 8.01  ?  320 PHE C CB    1 
ATOM   13454 C  CG    . PHE C 2 341 ? 161.651 121.658 109.283 1.00 9.69  ?  320 PHE C CG    1 
ATOM   13455 C  CD1   . PHE C 2 341 ? 160.838 122.684 109.730 1.00 6.44  ?  320 PHE C CD1   1 
ATOM   13456 C  CD2   . PHE C 2 341 ? 161.731 120.498 110.033 1.00 7.94  ?  320 PHE C CD2   1 
ATOM   13457 C  CE1   . PHE C 2 341 ? 160.121 122.557 110.902 1.00 10.55 ?  320 PHE C CE1   1 
ATOM   13458 C  CE2   . PHE C 2 341 ? 161.014 120.365 111.205 1.00 8.92  ?  320 PHE C CE2   1 
ATOM   13459 C  CZ    . PHE C 2 341 ? 160.207 121.396 111.640 1.00 6.02  ?  320 PHE C CZ    1 
ATOM   13460 N  N     . TYR C 2 342 ? 162.668 121.044 104.548 1.00 6.07  ?  321 TYR C N     1 
ATOM   13461 C  CA    . TYR C 2 342 ? 163.345 121.463 103.331 1.00 12.59 ?  321 TYR C CA    1 
ATOM   13462 C  C     . TYR C 2 342 ? 162.631 120.871 102.127 1.00 16.10 ?  321 TYR C C     1 
ATOM   13463 O  O     . TYR C 2 342 ? 162.183 119.721 102.163 1.00 16.79 ?  321 TYR C O     1 
ATOM   13464 C  CB    . TYR C 2 342 ? 164.815 121.030 103.337 1.00 6.93  ?  321 TYR C CB    1 
ATOM   13465 C  CG    . TYR C 2 342 ? 165.619 121.646 104.456 1.00 3.43  ?  321 TYR C CG    1 
ATOM   13466 C  CD1   . TYR C 2 342 ? 165.700 121.030 105.698 1.00 8.24  ?  321 TYR C CD1   1 
ATOM   13467 C  CD2   . TYR C 2 342 ? 166.290 122.846 104.276 1.00 11.16 ?  321 TYR C CD2   1 
ATOM   13468 C  CE1   . TYR C 2 342 ? 166.431 121.590 106.726 1.00 12.34 ?  321 TYR C CE1   1 
ATOM   13469 C  CE2   . TYR C 2 342 ? 167.023 123.415 105.298 1.00 13.11 ?  321 TYR C CE2   1 
ATOM   13470 C  CZ    . TYR C 2 342 ? 167.091 122.782 106.521 1.00 17.37 ?  321 TYR C CZ    1 
ATOM   13471 O  OH    . TYR C 2 342 ? 167.820 123.347 107.540 1.00 21.45 ?  321 TYR C OH    1 
ATOM   13472 N  N     . PHE C 2 343 ? 162.524 121.662 101.065 1.00 12.77 ?  322 PHE C N     1 
ATOM   13473 C  CA    . PHE C 2 343 ? 161.813 121.240 99.865  1.00 15.81 ?  322 PHE C CA    1 
ATOM   13474 C  C     . PHE C 2 343 ? 162.575 121.659 98.614  1.00 24.63 ?  322 PHE C C     1 
ATOM   13475 O  O     . PHE C 2 343 ? 163.443 122.529 98.662  1.00 24.06 ?  322 PHE C O     1 
ATOM   13476 C  CB    . PHE C 2 343 ? 160.387 121.813 99.827  1.00 11.49 ?  322 PHE C CB    1 
ATOM   13477 C  CG    . PHE C 2 343 ? 159.713 121.890 101.174 1.00 8.46  ?  322 PHE C CG    1 
ATOM   13478 C  CD1   . PHE C 2 343 ? 160.009 122.908 102.069 1.00 8.80  ?  322 PHE C CD1   1 
ATOM   13479 C  CD2   . PHE C 2 343 ? 158.797 120.924 101.551 1.00 13.46 ?  322 PHE C CD2   1 
ATOM   13480 C  CE1   . PHE C 2 343 ? 159.395 122.962 103.302 1.00 5.58  ?  322 PHE C CE1   1 
ATOM   13481 C  CE2   . PHE C 2 343 ? 158.182 120.976 102.783 1.00 8.14  ?  322 PHE C CE2   1 
ATOM   13482 C  CZ    . PHE C 2 343 ? 158.481 121.995 103.659 1.00 2.41  ?  322 PHE C CZ    1 
ATOM   13483 N  N     . ASP D 2 37  ? 115.851 108.123 144.903 1.00 32.44 ?  16  ASP D N     1 
ATOM   13484 C  CA    . ASP D 2 37  ? 116.603 109.381 144.899 1.00 32.83 ?  16  ASP D CA    1 
ATOM   13485 C  C     . ASP D 2 37  ? 117.723 109.433 143.862 1.00 31.65 ?  16  ASP D C     1 
ATOM   13486 O  O     . ASP D 2 37  ? 118.350 110.482 143.691 1.00 32.65 ?  16  ASP D O     1 
ATOM   13487 C  CB    . ASP D 2 37  ? 117.235 109.640 146.275 1.00 33.73 ?  16  ASP D CB    1 
ATOM   13488 C  CG    . ASP D 2 37  ? 116.208 109.866 147.374 1.00 36.81 ?  16  ASP D CG    1 
ATOM   13489 O  OD1   . ASP D 2 37  ? 116.589 109.724 148.561 1.00 39.69 ?  16  ASP D OD1   1 
ATOM   13490 O  OD2   . ASP D 2 37  ? 115.033 110.174 147.068 1.00 39.67 -1 16  ASP D OD2   1 
ATOM   13491 N  N     . PHE D 2 38  ? 117.988 108.323 143.176 1.00 29.55 ?  17  PHE D N     1 
ATOM   13492 C  CA    . PHE D 2 38  ? 119.244 108.209 142.434 1.00 27.75 ?  17  PHE D CA    1 
ATOM   13493 C  C     . PHE D 2 38  ? 119.191 107.556 141.043 1.00 26.21 ?  17  PHE D C     1 
ATOM   13494 O  O     . PHE D 2 38  ? 120.107 107.742 140.249 1.00 25.93 ?  17  PHE D O     1 
ATOM   13495 C  CB    . PHE D 2 38  ? 120.300 107.507 143.318 1.00 27.37 ?  17  PHE D CB    1 
ATOM   13496 C  CG    . PHE D 2 38  ? 119.899 106.122 143.752 1.00 27.32 ?  17  PHE D CG    1 
ATOM   13497 C  CD1   . PHE D 2 38  ? 120.124 105.027 142.923 1.00 27.01 ?  17  PHE D CD1   1 
ATOM   13498 C  CD2   . PHE D 2 38  ? 119.296 105.910 144.985 1.00 28.02 ?  17  PHE D CD2   1 
ATOM   13499 C  CE1   . PHE D 2 38  ? 119.749 103.744 143.316 1.00 27.66 ?  17  PHE D CE1   1 
ATOM   13500 C  CE2   . PHE D 2 38  ? 118.914 104.634 145.381 1.00 27.68 ?  17  PHE D CE2   1 
ATOM   13501 C  CZ    . PHE D 2 38  ? 119.143 103.547 144.542 1.00 27.47 ?  17  PHE D CZ    1 
ATOM   13502 N  N     . THR D 2 39  ? 118.139 106.798 140.750 1.00 24.88 ?  18  THR D N     1 
ATOM   13503 C  CA    . THR D 2 39  ? 118.094 105.993 139.519 1.00 23.81 ?  18  THR D CA    1 
ATOM   13504 C  C     . THR D 2 39  ? 118.109 106.818 138.219 1.00 23.56 ?  18  THR D C     1 
ATOM   13505 O  O     . THR D 2 39  ? 118.805 106.474 137.263 1.00 23.02 ?  18  THR D O     1 
ATOM   13506 C  CB    . THR D 2 39  ? 116.943 104.959 139.553 1.00 23.40 ?  18  THR D CB    1 
ATOM   13507 O  OG1   . THR D 2 39  ? 117.335 103.852 140.374 1.00 23.77 ?  18  THR D OG1   1 
ATOM   13508 C  CG2   . THR D 2 39  ? 116.625 104.426 138.165 1.00 22.31 ?  18  THR D CG2   1 
ATOM   13509 N  N     . GLN D 2 40  ? 117.363 107.915 138.180 1.00 23.78 ?  19  GLN D N     1 
ATOM   13510 C  CA    . GLN D 2 40  ? 117.377 108.752 136.977 1.00 23.88 ?  19  GLN D CA    1 
ATOM   13511 C  C     . GLN D 2 40  ? 118.744 109.397 136.736 1.00 24.09 ?  19  GLN D C     1 
ATOM   13512 O  O     . GLN D 2 40  ? 119.221 109.441 135.610 1.00 23.15 ?  19  GLN D O     1 
ATOM   13513 C  CB    . GLN D 2 40  ? 116.253 109.789 137.003 1.00 24.53 ?  19  GLN D CB    1 
ATOM   13514 C  CG    . GLN D 2 40  ? 114.880 109.146 136.887 1.00 24.06 ?  19  GLN D CG    1 
ATOM   13515 C  CD    . GLN D 2 40  ? 113.799 110.112 136.460 1.00 25.83 ?  19  GLN D CD    1 
ATOM   13516 O  OE1   . GLN D 2 40  ? 114.086 111.222 136.018 1.00 25.90 ?  19  GLN D OE1   1 
ATOM   13517 N  NE2   . GLN D 2 40  ? 112.542 109.682 136.568 1.00 23.56 ?  19  GLN D NE2   1 
ATOM   13518 N  N     . MET D 2 41  ? 119.391 109.853 137.802 1.00 24.07 ?  20  MET D N     1 
ATOM   13519 C  CA    . MET D 2 41  ? 120.760 110.359 137.693 1.00 25.53 ?  20  MET D CA    1 
ATOM   13520 C  C     . MET D 2 41  ? 121.739 109.303 137.139 1.00 24.24 ?  20  MET D C     1 
ATOM   13521 O  O     . MET D 2 41  ? 122.563 109.610 136.273 1.00 23.16 ?  20  MET D O     1 
ATOM   13522 C  CB    . MET D 2 41  ? 121.233 110.887 139.052 1.00 26.79 ?  20  MET D CB    1 
ATOM   13523 C  CG    . MET D 2 41  ? 122.654 111.414 139.072 1.00 32.62 ?  20  MET D CG    1 
ATOM   13524 S  SD    . MET D 2 41  ? 123.190 111.685 140.778 1.00 44.01 ?  20  MET D SD    1 
ATOM   13525 C  CE    . MET D 2 41  ? 124.972 111.546 140.608 1.00 41.93 ?  20  MET D CE    1 
ATOM   13526 N  N     . PHE D 2 42  ? 121.640 108.064 137.625 1.00 23.31 ?  21  PHE D N     1 
ATOM   13527 C  CA    . PHE D 2 42  ? 122.513 107.000 137.126 1.00 23.44 ?  21  PHE D CA    1 
ATOM   13528 C  C     . PHE D 2 42  ? 122.163 106.592 135.710 1.00 23.55 ?  21  PHE D C     1 
ATOM   13529 O  O     . PHE D 2 42  ? 123.046 106.246 134.932 1.00 23.74 ?  21  PHE D O     1 
ATOM   13530 C  CB    . PHE D 2 42  ? 122.520 105.790 138.062 1.00 22.97 ?  21  PHE D CB    1 
ATOM   13531 C  CG    . PHE D 2 42  ? 123.510 105.920 139.167 1.00 23.86 ?  21  PHE D CG    1 
ATOM   13532 C  CD1   . PHE D 2 42  ? 124.780 105.363 139.048 1.00 24.55 ?  21  PHE D CD1   1 
ATOM   13533 C  CD2   . PHE D 2 42  ? 123.196 106.634 140.307 1.00 24.06 ?  21  PHE D CD2   1 
ATOM   13534 C  CE1   . PHE D 2 42  ? 125.717 105.502 140.075 1.00 25.78 ?  21  PHE D CE1   1 
ATOM   13535 C  CE2   . PHE D 2 42  ? 124.127 106.779 141.339 1.00 25.25 ?  21  PHE D CE2   1 
ATOM   13536 C  CZ    . PHE D 2 42  ? 125.383 106.220 141.222 1.00 25.79 ?  21  PHE D CZ    1 
ATOM   13537 N  N     . TYR D 2 43  ? 120.875 106.653 135.379 1.00 24.08 ?  22  TYR D N     1 
ATOM   13538 C  CA    . TYR D 2 43  ? 120.432 106.432 134.012 1.00 24.74 ?  22  TYR D CA    1 
ATOM   13539 C  C     . TYR D 2 43  ? 121.187 107.375 133.074 1.00 25.72 ?  22  TYR D C     1 
ATOM   13540 O  O     . TYR D 2 43  ? 121.760 106.941 132.070 1.00 25.56 ?  22  TYR D O     1 
ATOM   13541 C  CB    . TYR D 2 43  ? 118.914 106.630 133.862 1.00 24.90 ?  22  TYR D CB    1 
ATOM   13542 C  CG    . TYR D 2 43  ? 118.477 106.568 132.405 1.00 24.38 ?  22  TYR D CG    1 
ATOM   13543 C  CD1   . TYR D 2 43  ? 118.122 105.359 131.819 1.00 23.96 ?  22  TYR D CD1   1 
ATOM   13544 C  CD2   . TYR D 2 43  ? 118.478 107.714 131.606 1.00 24.73 ?  22  TYR D CD2   1 
ATOM   13545 C  CE1   . TYR D 2 43  ? 117.756 105.292 130.473 1.00 23.42 ?  22  TYR D CE1   1 
ATOM   13546 C  CE2   . TYR D 2 43  ? 118.101 107.665 130.262 1.00 26.65 ?  22  TYR D CE2   1 
ATOM   13547 C  CZ    . TYR D 2 43  ? 117.745 106.448 129.706 1.00 25.68 ?  22  TYR D CZ    1 
ATOM   13548 O  OH    . TYR D 2 43  ? 117.376 106.394 128.382 1.00 26.57 ?  22  TYR D OH    1 
ATOM   13549 N  N     . ASN D 2 44  ? 121.172 108.662 133.413 1.00 26.77 ?  23  ASN D N     1 
ATOM   13550 C  CA    . ASN D 2 44  ? 121.826 109.690 132.612 1.00 28.57 ?  23  ASN D CA    1 
ATOM   13551 C  C     . ASN D 2 44  ? 123.310 109.430 132.435 1.00 28.70 ?  23  ASN D C     1 
ATOM   13552 O  O     . ASN D 2 44  ? 123.805 109.412 131.305 1.00 28.99 ?  23  ASN D O     1 
ATOM   13553 C  CB    . ASN D 2 44  ? 121.566 111.078 133.204 1.00 29.62 ?  23  ASN D CB    1 
ATOM   13554 C  CG    . ASN D 2 44  ? 120.115 111.511 133.043 1.00 32.44 ?  23  ASN D CG    1 
ATOM   13555 O  OD1   . ASN D 2 44  ? 119.395 111.007 132.171 1.00 34.30 ?  23  ASN D OD1   1 
ATOM   13556 N  ND2   . ASN D 2 44  ? 119.674 112.445 133.883 1.00 35.17 ?  23  ASN D ND2   1 
ATOM   13557 N  N     . GLN D 2 45  ? 124.003 109.185 133.545 1.00 28.97 ?  24  GLN D N     1 
ATOM   13558 C  CA    . GLN D 2 45  ? 125.438 108.933 133.509 1.00 29.99 ?  24  GLN D CA    1 
ATOM   13559 C  C     . GLN D 2 45  ? 125.791 107.670 132.710 1.00 29.69 ?  24  GLN D C     1 
ATOM   13560 O  O     . GLN D 2 45  ? 126.768 107.661 131.962 1.00 30.01 ?  24  GLN D O     1 
ATOM   13561 C  CB    . GLN D 2 45  ? 126.022 108.872 134.926 1.00 30.27 ?  24  GLN D CB    1 
ATOM   13562 C  CG    . GLN D 2 45  ? 127.567 108.843 134.963 1.00 32.29 ?  24  GLN D CG    1 
ATOM   13563 C  CD    . GLN D 2 45  ? 128.207 110.098 134.385 1.00 35.95 ?  24  GLN D CD    1 
ATOM   13564 O  OE1   . GLN D 2 45  ? 127.621 111.185 134.415 1.00 36.72 ?  24  GLN D OE1   1 
ATOM   13565 N  NE2   . GLN D 2 45  ? 129.418 109.954 133.857 1.00 37.05 ?  24  GLN D NE2   1 
ATOM   13566 N  N     . ASN D 2 46  ? 124.981 106.621 132.850 1.00 28.93 ?  25  ASN D N     1 
ATOM   13567 C  CA    . ASN D 2 46  ? 125.187 105.394 132.098 1.00 28.70 ?  25  ASN D CA    1 
ATOM   13568 C  C     . ASN D 2 46  ? 125.058 105.571 130.591 1.00 29.05 ?  25  ASN D C     1 
ATOM   13569 O  O     . ASN D 2 46  ? 125.957 105.176 129.843 1.00 28.51 ?  25  ASN D O     1 
ATOM   13570 C  CB    . ASN D 2 46  ? 124.254 104.278 132.586 1.00 28.36 ?  25  ASN D CB    1 
ATOM   13571 C  CG    . ASN D 2 46  ? 124.845 103.494 133.738 1.00 28.45 ?  25  ASN D CG    1 
ATOM   13572 O  OD1   . ASN D 2 46  ? 125.430 102.434 133.528 1.00 28.03 ?  25  ASN D OD1   1 
ATOM   13573 N  ND2   . ASN D 2 46  ? 124.724 104.023 134.954 1.00 26.53 ?  25  ASN D ND2   1 
ATOM   13574 N  N     . VAL D 2 47  ? 123.959 106.182 130.150 1.00 29.66 ?  26  VAL D N     1 
ATOM   13575 C  CA    . VAL D 2 47  ? 123.692 106.295 128.715 1.00 31.15 ?  26  VAL D CA    1 
ATOM   13576 C  C     . VAL D 2 47  ? 124.636 107.286 128.042 1.00 32.39 ?  26  VAL D C     1 
ATOM   13577 O  O     . VAL D 2 47  ? 124.976 107.124 126.871 1.00 32.80 ?  26  VAL D O     1 
ATOM   13578 C  CB    . VAL D 2 47  ? 122.195 106.600 128.373 1.00 31.08 ?  26  VAL D CB    1 
ATOM   13579 C  CG1   . VAL D 2 47  ? 121.276 105.550 128.987 1.00 31.09 ?  26  VAL D CG1   1 
ATOM   13580 C  CG2   . VAL D 2 47  ? 121.785 108.017 128.798 1.00 30.81 ?  26  VAL D CG2   1 
ATOM   13581 N  N     . LYS D 2 48  ? 125.089 108.294 128.778 1.00 33.28 ?  27  LYS D N     1 
ATOM   13582 C  CA    . LYS D 2 48  ? 126.028 109.233 128.186 1.00 34.87 ?  27  LYS D CA    1 
ATOM   13583 C  C     . LYS D 2 48  ? 127.465 108.681 128.084 1.00 34.91 ?  27  LYS D C     1 
ATOM   13584 O  O     . LYS D 2 48  ? 128.304 109.258 127.397 1.00 34.92 ?  27  LYS D O     1 
ATOM   13585 C  CB    . LYS D 2 48  ? 125.955 110.608 128.867 1.00 35.45 ?  27  LYS D CB    1 
ATOM   13586 C  CG    . LYS D 2 48  ? 126.792 110.789 130.112 1.00 37.41 ?  27  LYS D CG    1 
ATOM   13587 C  CD    . LYS D 2 48  ? 126.922 112.286 130.437 1.00 40.91 ?  27  LYS D CD    1 
ATOM   13588 C  CE    . LYS D 2 48  ? 128.064 112.540 131.424 1.00 42.46 ?  27  LYS D CE    1 
ATOM   13589 N  NZ    . LYS D 2 48  ? 128.326 113.993 131.649 1.00 45.13 1  27  LYS D NZ    1 
ATOM   13590 N  N     . GLN D 2 49  ? 127.723 107.555 128.754 1.00 34.66 ?  28  GLN D N     1 
ATOM   13591 C  CA    . GLN D 2 49  ? 129.006 106.861 128.688 1.00 34.64 ?  28  GLN D CA    1 
ATOM   13592 C  C     . GLN D 2 49  ? 129.007 105.774 127.615 1.00 34.20 ?  28  GLN D C     1 
ATOM   13593 O  O     . GLN D 2 49  ? 129.958 104.994 127.534 1.00 34.53 ?  28  GLN D O     1 
ATOM   13594 C  CB    . GLN D 2 49  ? 129.357 106.226 130.049 1.00 34.89 ?  28  GLN D CB    1 
ATOM   13595 C  CG    . GLN D 2 49  ? 130.091 107.147 131.021 1.00 36.47 ?  28  GLN D CG    1 
ATOM   13596 C  CD    . GLN D 2 49  ? 130.249 106.554 132.423 1.00 38.37 ?  28  GLN D CD    1 
ATOM   13597 O  OE1   . GLN D 2 49  ? 130.264 107.288 133.411 1.00 40.68 ?  28  GLN D OE1   1 
ATOM   13598 N  NE2   . GLN D 2 49  ? 130.364 105.228 132.515 1.00 38.57 ?  28  GLN D NE2   1 
ATOM   13599 N  N     . PHE D 2 50  ? 127.953 105.708 126.801 1.00 33.42 ?  29  PHE D N     1 
ATOM   13600 C  CA    . PHE D 2 50  ? 127.840 104.644 125.804 1.00 32.57 ?  29  PHE D CA    1 
ATOM   13601 C  C     . PHE D 2 50  ? 128.990 104.729 124.800 1.00 32.60 ?  29  PHE D C     1 
ATOM   13602 O  O     . PHE D 2 50  ? 129.377 105.820 124.371 1.00 32.39 ?  29  PHE D O     1 
ATOM   13603 C  CB    . PHE D 2 50  ? 126.478 104.668 125.091 1.00 32.77 ?  29  PHE D CB    1 
ATOM   13604 C  CG    . PHE D 2 50  ? 126.300 103.561 124.071 1.00 32.24 ?  29  PHE D CG    1 
ATOM   13605 C  CD1   . PHE D 2 50  ? 126.049 102.253 124.474 1.00 31.50 ?  29  PHE D CD1   1 
ATOM   13606 C  CD2   . PHE D 2 50  ? 126.387 103.831 122.710 1.00 33.60 ?  29  PHE D CD2   1 
ATOM   13607 C  CE1   . PHE D 2 50  ? 125.888 101.236 123.546 1.00 33.02 ?  29  PHE D CE1   1 
ATOM   13608 C  CE2   . PHE D 2 50  ? 126.230 102.816 121.764 1.00 33.78 ?  29  PHE D CE2   1 
ATOM   13609 C  CZ    . PHE D 2 50  ? 125.974 101.519 122.181 1.00 33.13 ?  29  PHE D CZ    1 
ATOM   13610 N  N     . TRP D 2 51  ? 129.533 103.572 124.446 1.00 31.95 ?  30  TRP D N     1 
ATOM   13611 C  CA    . TRP D 2 51  ? 130.648 103.480 123.504 1.00 32.03 ?  30  TRP D CA    1 
ATOM   13612 C  C     . TRP D 2 51  ? 130.618 102.121 122.818 1.00 33.03 ?  30  TRP D C     1 
ATOM   13613 O  O     . TRP D 2 51  ? 129.888 101.220 123.237 1.00 32.54 ?  30  TRP D O     1 
ATOM   13614 C  CB    . TRP D 2 51  ? 131.994 103.718 124.207 1.00 31.19 ?  30  TRP D CB    1 
ATOM   13615 C  CG    . TRP D 2 51  ? 132.309 102.711 125.294 1.00 28.11 ?  30  TRP D CG    1 
ATOM   13616 C  CD1   . TRP D 2 51  ? 131.813 102.698 126.561 1.00 26.51 ?  30  TRP D CD1   1 
ATOM   13617 C  CD2   . TRP D 2 51  ? 133.183 101.575 125.194 1.00 25.93 ?  30  TRP D CD2   1 
ATOM   13618 N  NE1   . TRP D 2 51  ? 132.328 101.628 127.264 1.00 24.52 ?  30  TRP D NE1   1 
ATOM   13619 C  CE2   . TRP D 2 51  ? 133.167 100.922 126.448 1.00 24.42 ?  30  TRP D CE2   1 
ATOM   13620 C  CE3   . TRP D 2 51  ? 133.983 101.050 124.168 1.00 25.37 ?  30  TRP D CE3   1 
ATOM   13621 C  CZ2   . TRP D 2 51  ? 133.925 99.771  126.707 1.00 24.00 ?  30  TRP D CZ2   1 
ATOM   13622 C  CZ3   . TRP D 2 51  ? 134.730 99.900  124.424 1.00 24.99 ?  30  TRP D CZ3   1 
ATOM   13623 C  CH2   . TRP D 2 51  ? 134.694 99.274  125.684 1.00 23.72 ?  30  TRP D CH2   1 
ATOM   13624 N  N     . LEU D 2 52  ? 131.404 101.991 121.754 1.00 34.81 ?  31  LEU D N     1 
ATOM   13625 C  CA    . LEU D 2 52  ? 131.478 100.767 120.970 1.00 36.58 ?  31  LEU D CA    1 
ATOM   13626 C  C     . LEU D 2 52  ? 132.937 100.401 120.712 1.00 37.80 ?  31  LEU D C     1 
ATOM   13627 O  O     . LEU D 2 52  ? 133.776 101.286 120.577 1.00 37.92 ?  31  LEU D O     1 
ATOM   13628 C  CB    . LEU D 2 52  ? 130.718 100.930 119.644 1.00 36.95 ?  31  LEU D CB    1 
ATOM   13629 C  CG    . LEU D 2 52  ? 129.194 100.771 119.637 1.00 38.15 ?  31  LEU D CG    1 
ATOM   13630 C  CD1   . LEU D 2 52  ? 128.688 100.620 118.207 1.00 39.50 ?  31  LEU D CD1   1 
ATOM   13631 C  CD2   . LEU D 2 52  ? 128.739 99.576  120.468 1.00 37.94 ?  31  LEU D CD2   1 
ATOM   13632 N  N     . PRO D 2 53  ? 133.246 99.091  120.636 1.00 39.26 ?  32  PRO D N     1 
ATOM   13633 C  CA    . PRO D 2 53  ? 134.623 98.613  120.409 1.00 40.41 ?  32  PRO D CA    1 
ATOM   13634 C  C     . PRO D 2 53  ? 135.285 99.212  119.160 1.00 41.91 ?  32  PRO D C     1 
ATOM   13635 O  O     . PRO D 2 53  ? 136.445 99.633  119.215 1.00 42.52 ?  32  PRO D O     1 
ATOM   13636 C  CB    . PRO D 2 53  ? 134.443 97.103  120.221 1.00 40.42 ?  32  PRO D CB    1 
ATOM   13637 C  CG    . PRO D 2 53  ? 133.149 96.783  120.854 1.00 40.01 ?  32  PRO D CG    1 
ATOM   13638 C  CD    . PRO D 2 53  ? 132.280 97.979  120.688 1.00 39.30 ?  32  PRO D CD    1 
ATOM   13639 N  N     . GLU D 2 54  ? 134.539 99.263  118.060 1.00 43.27 ?  33  GLU D N     1 
ATOM   13640 C  CA    . GLU D 2 54  ? 135.022 99.766  116.763 1.00 45.17 ?  33  GLU D CA    1 
ATOM   13641 C  C     . GLU D 2 54  ? 135.649 101.170 116.794 1.00 45.57 ?  33  GLU D C     1 
ATOM   13642 O  O     . GLU D 2 54  ? 136.421 101.527 115.899 1.00 46.08 ?  33  GLU D O     1 
ATOM   13643 C  CB    . GLU D 2 54  ? 133.882 99.737  115.735 1.00 45.55 ?  33  GLU D CB    1 
ATOM   13644 C  CG    . GLU D 2 54  ? 133.633 98.372  115.087 1.00 48.19 ?  33  GLU D CG    1 
ATOM   13645 C  CD    . GLU D 2 54  ? 133.182 97.301  116.071 1.00 50.61 ?  33  GLU D CD    1 
ATOM   13646 O  OE1   . GLU D 2 54  ? 132.262 97.571  116.879 1.00 51.10 ?  33  GLU D OE1   1 
ATOM   13647 O  OE2   . GLU D 2 54  ? 133.757 96.187  116.033 1.00 52.64 -1 33  GLU D OE2   1 
ATOM   13648 N  N     . GLU D 2 55  ? 135.314 101.954 117.818 1.00 45.74 ?  34  GLU D N     1 
ATOM   13649 C  CA    . GLU D 2 55  ? 135.790 103.337 117.940 1.00 46.28 ?  34  GLU D CA    1 
ATOM   13650 C  C     . GLU D 2 55  ? 137.304 103.441 118.159 1.00 46.49 ?  34  GLU D C     1 
ATOM   13651 O  O     . GLU D 2 55  ? 137.931 104.422 117.747 1.00 46.73 ?  34  GLU D O     1 
ATOM   13652 C  CB    . GLU D 2 55  ? 135.044 104.075 119.057 1.00 46.17 ?  34  GLU D CB    1 
ATOM   13653 C  CG    . GLU D 2 55  ? 133.539 104.240 118.828 1.00 47.10 ?  34  GLU D CG    1 
ATOM   13654 C  CD    . GLU D 2 55  ? 132.865 105.032 119.947 1.00 48.43 ?  34  GLU D CD    1 
ATOM   13655 O  OE1   . GLU D 2 55  ? 133.198 106.225 120.123 1.00 49.62 ?  34  GLU D OE1   1 
ATOM   13656 O  OE2   . GLU D 2 55  ? 132.000 104.465 120.648 1.00 47.11 -1 34  GLU D OE2   1 
ATOM   13657 N  N     . ILE D 2 56  ? 137.883 102.433 118.811 1.00 46.23 ?  35  ILE D N     1 
ATOM   13658 C  CA    . ILE D 2 56  ? 139.323 102.393 119.055 1.00 46.25 ?  35  ILE D CA    1 
ATOM   13659 C  C     . ILE D 2 56  ? 139.978 101.420 118.075 1.00 46.30 ?  35  ILE D C     1 
ATOM   13660 O  O     . ILE D 2 56  ? 139.644 100.232 118.054 1.00 46.36 ?  35  ILE D O     1 
ATOM   13661 C  CB    . ILE D 2 56  ? 139.659 101.963 120.526 1.00 45.84 ?  35  ILE D CB    1 
ATOM   13662 C  CG1   . ILE D 2 56  ? 138.729 102.633 121.558 1.00 46.15 ?  35  ILE D CG1   1 
ATOM   13663 C  CG2   . ILE D 2 56  ? 141.152 102.184 120.845 1.00 45.72 ?  35  ILE D CG2   1 
ATOM   13664 C  CD1   . ILE D 2 56  ? 138.809 104.153 121.641 1.00 47.27 ?  35  ILE D CD1   1 
ATOM   13665 N  N     . ALA D 2 57  ? 140.897 101.926 117.258 1.00 46.51 ?  36  ALA D N     1 
ATOM   13666 C  CA    . ALA D 2 57  ? 141.687 101.075 116.364 1.00 46.56 ?  36  ALA D CA    1 
ATOM   13667 C  C     . ALA D 2 57  ? 142.771 100.361 117.176 1.00 46.08 ?  36  ALA D C     1 
ATOM   13668 O  O     . ALA D 2 57  ? 143.546 101.012 117.876 1.00 45.70 ?  36  ALA D O     1 
ATOM   13669 C  CB    . ALA D 2 57  ? 142.308 101.903 115.242 1.00 47.10 ?  36  ALA D CB    1 
ATOM   13670 N  N     . LEU D 2 58  ? 142.829 99.035  117.069 1.00 45.66 ?  37  LEU D N     1 
ATOM   13671 C  CA    . LEU D 2 58  ? 143.724 98.235  117.918 1.00 45.27 ?  37  LEU D CA    1 
ATOM   13672 C  C     . LEU D 2 58  ? 145.084 97.871  117.326 1.00 45.25 ?  37  LEU D C     1 
ATOM   13673 O  O     . LEU D 2 58  ? 146.022 97.561  118.068 1.00 44.82 ?  37  LEU D O     1 
ATOM   13674 C  CB    . LEU D 2 58  ? 143.018 96.963  118.388 1.00 45.05 ?  37  LEU D CB    1 
ATOM   13675 C  CG    . LEU D 2 58  ? 142.041 97.165  119.543 1.00 45.41 ?  37  LEU D CG    1 
ATOM   13676 C  CD1   . LEU D 2 58  ? 141.356 95.853  119.873 1.00 45.40 ?  37  LEU D CD1   1 
ATOM   13677 C  CD2   . LEU D 2 58  ? 142.755 97.728  120.770 1.00 44.70 ?  37  LEU D CD2   1 
ATOM   13678 N  N     . ASN D 2 59  ? 145.199 97.922  116.002 1.00 45.33 ?  38  ASN D N     1 
ATOM   13679 C  CA    . ASN D 2 59  ? 146.375 97.374  115.318 1.00 45.22 ?  38  ASN D CA    1 
ATOM   13680 C  C     . ASN D 2 59  ? 147.724 97.983  115.724 1.00 44.39 ?  38  ASN D C     1 
ATOM   13681 O  O     . ASN D 2 59  ? 148.742 97.281  115.734 1.00 44.33 ?  38  ASN D O     1 
ATOM   13682 C  CB    . ASN D 2 59  ? 146.186 97.434  113.804 1.00 46.22 ?  38  ASN D CB    1 
ATOM   13683 C  CG    . ASN D 2 59  ? 146.806 96.243  113.094 1.00 47.90 ?  38  ASN D CG    1 
ATOM   13684 O  OD1   . ASN D 2 59  ? 147.719 96.396  112.284 1.00 49.28 ?  38  ASN D OD1   1 
ATOM   13685 N  ND2   . ASN D 2 59  ? 146.307 95.043  113.397 1.00 49.18 ?  38  ASN D ND2   1 
ATOM   13686 N  N     . GLY D 2 60  ? 147.722 99.269  116.077 1.00 43.45 ?  39  GLY D N     1 
ATOM   13687 C  CA    . GLY D 2 60  ? 148.934 99.978  116.502 1.00 42.42 ?  39  GLY D CA    1 
ATOM   13688 C  C     . GLY D 2 60  ? 149.559 99.508  117.814 1.00 41.55 ?  39  GLY D C     1 
ATOM   13689 O  O     . GLY D 2 60  ? 150.655 99.946  118.179 1.00 41.29 ?  39  GLY D O     1 
ATOM   13690 N  N     . ASP D 2 61  ? 148.866 98.625  118.530 1.00 40.35 ?  40  ASP D N     1 
ATOM   13691 C  CA    . ASP D 2 61  ? 149.421 98.016  119.745 1.00 39.53 ?  40  ASP D CA    1 
ATOM   13692 C  C     . ASP D 2 61  ? 150.534 97.017  119.459 1.00 39.38 ?  40  ASP D C     1 
ATOM   13693 O  O     . ASP D 2 61  ? 151.374 96.755  120.316 1.00 38.90 ?  40  ASP D O     1 
ATOM   13694 C  CB    . ASP D 2 61  ? 148.326 97.326  120.544 1.00 38.93 ?  40  ASP D CB    1 
ATOM   13695 C  CG    . ASP D 2 61  ? 147.603 98.267  121.465 1.00 38.21 ?  40  ASP D CG    1 
ATOM   13696 O  OD1   . ASP D 2 61  ? 147.955 99.467  121.514 1.00 38.79 ?  40  ASP D OD1   1 
ATOM   13697 O  OD2   . ASP D 2 61  ? 146.681 97.800  122.153 1.00 38.02 -1 40  ASP D OD2   1 
ATOM   13698 N  N     . LEU D 2 62  ? 150.529 96.464  118.250 1.00 39.82 ?  41  LEU D N     1 
ATOM   13699 C  CA    . LEU D 2 62  ? 151.524 95.479  117.842 1.00 40.22 ?  41  LEU D CA    1 
ATOM   13700 C  C     . LEU D 2 62  ? 152.933 96.072  117.823 1.00 40.40 ?  41  LEU D C     1 
ATOM   13701 O  O     . LEU D 2 62  ? 153.918 95.336  117.891 1.00 40.91 ?  41  LEU D O     1 
ATOM   13702 C  CB    . LEU D 2 62  ? 151.152 94.888  116.479 1.00 40.52 ?  41  LEU D CB    1 
ATOM   13703 C  CG    . LEU D 2 62  ? 149.864 94.057  116.434 1.00 41.03 ?  41  LEU D CG    1 
ATOM   13704 C  CD1   . LEU D 2 62  ? 149.561 93.614  115.009 1.00 42.53 ?  41  LEU D CD1   1 
ATOM   13705 C  CD2   . LEU D 2 62  ? 149.937 92.852  117.381 1.00 41.89 ?  41  LEU D CD2   1 
ATOM   13706 N  N     . LEU D 2 63  ? 153.007 97.404  117.756 1.00 40.20 ?  42  LEU D N     1 
ATOM   13707 C  CA    . LEU D 2 63  ? 154.266 98.149  117.750 1.00 39.85 ?  42  LEU D CA    1 
ATOM   13708 C  C     . LEU D 2 63  ? 154.927 98.243  119.139 1.00 38.90 ?  42  LEU D C     1 
ATOM   13709 O  O     . LEU D 2 63  ? 156.110 98.585  119.250 1.00 39.48 ?  42  LEU D O     1 
ATOM   13710 C  CB    . LEU D 2 63  ? 154.027 99.550  117.165 1.00 40.50 ?  42  LEU D CB    1 
ATOM   13711 C  CG    . LEU D 2 63  ? 155.096 100.288 116.344 1.00 41.98 ?  42  LEU D CG    1 
ATOM   13712 C  CD1   . LEU D 2 63  ? 155.581 99.473  115.149 1.00 43.07 ?  42  LEU D CD1   1 
ATOM   13713 C  CD2   . LEU D 2 63  ? 154.534 101.611 115.854 1.00 43.17 ?  42  LEU D CD2   1 
ATOM   13714 N  N     . THR D 2 64  ? 154.174 97.957  120.198 1.00 37.28 ?  43  THR D N     1 
ATOM   13715 C  CA    . THR D 2 64  ? 154.773 97.864  121.539 1.00 35.53 ?  43  THR D CA    1 
ATOM   13716 C  C     . THR D 2 64  ? 154.720 96.445  122.092 1.00 34.57 ?  43  THR D C     1 
ATOM   13717 O  O     . THR D 2 64  ? 155.581 96.048  122.882 1.00 34.23 ?  43  THR D O     1 
ATOM   13718 C  CB    . THR D 2 64  ? 154.169 98.858  122.556 1.00 35.18 ?  43  THR D CB    1 
ATOM   13719 O  OG1   . THR D 2 64  ? 152.740 98.805  122.515 1.00 34.59 ?  43  THR D OG1   1 
ATOM   13720 C  CG2   . THR D 2 64  ? 154.625 100.258 122.256 1.00 35.48 ?  43  THR D CG2   1 
ATOM   13721 N  N     . TRP D 2 65  ? 153.710 95.689  121.661 1.00 33.62 ?  44  TRP D N     1 
ATOM   13722 C  CA    . TRP D 2 65  ? 153.527 94.286  122.067 1.00 32.87 ?  44  TRP D CA    1 
ATOM   13723 C  C     . TRP D 2 65  ? 154.753 93.428  121.726 1.00 33.46 ?  44  TRP D C     1 
ATOM   13724 O  O     . TRP D 2 65  ? 155.203 92.624  122.544 1.00 32.58 ?  44  TRP D O     1 
ATOM   13725 C  CB    . TRP D 2 65  ? 152.267 93.711  121.402 1.00 32.09 ?  44  TRP D CB    1 
ATOM   13726 C  CG    . TRP D 2 65  ? 152.006 92.258  121.688 1.00 30.42 ?  44  TRP D CG    1 
ATOM   13727 C  CD1   . TRP D 2 65  ? 152.179 91.213  120.824 1.00 29.35 ?  44  TRP D CD1   1 
ATOM   13728 C  CD2   . TRP D 2 65  ? 151.518 91.690  122.913 1.00 28.04 ?  44  TRP D CD2   1 
ATOM   13729 N  NE1   . TRP D 2 65  ? 151.830 90.030  121.434 1.00 28.44 ?  44  TRP D NE1   1 
ATOM   13730 C  CE2   . TRP D 2 65  ? 151.425 90.294  122.717 1.00 28.14 ?  44  TRP D CE2   1 
ATOM   13731 C  CE3   . TRP D 2 65  ? 151.160 92.223  124.159 1.00 27.11 ?  44  TRP D CE3   1 
ATOM   13732 C  CZ2   . TRP D 2 65  ? 150.980 89.419  123.717 1.00 27.21 ?  44  TRP D CZ2   1 
ATOM   13733 C  CZ3   . TRP D 2 65  ? 150.707 91.352  125.155 1.00 27.45 ?  44  TRP D CZ3   1 
ATOM   13734 C  CH2   . TRP D 2 65  ? 150.618 89.965  124.921 1.00 27.25 ?  44  TRP D CH2   1 
ATOM   13735 N  N     . LYS D 2 66  ? 155.278 93.620  120.517 1.00 34.52 ?  45  LYS D N     1 
ATOM   13736 C  CA    . LYS D 2 66  ? 156.457 92.904  120.037 1.00 36.41 ?  45  LYS D CA    1 
ATOM   13737 C  C     . LYS D 2 66  ? 157.710 93.135  120.880 1.00 36.26 ?  45  LYS D C     1 
ATOM   13738 O  O     . LYS D 2 66  ? 158.635 92.325  120.839 1.00 36.52 ?  45  LYS D O     1 
ATOM   13739 C  CB    . LYS D 2 66  ? 156.740 93.256  118.570 1.00 36.98 ?  45  LYS D CB    1 
ATOM   13740 C  CG    . LYS D 2 66  ? 156.289 92.188  117.577 1.00 40.03 ?  45  LYS D CG    1 
ATOM   13741 C  CD    . LYS D 2 66  ? 154.763 92.094  117.465 1.00 43.70 ?  45  LYS D CD    1 
ATOM   13742 C  CE    . LYS D 2 66  ? 154.343 91.055  116.421 1.00 45.57 ?  45  LYS D CE    1 
ATOM   13743 N  NZ    . LYS D 2 66  ? 154.818 91.390  115.046 1.00 46.59 1  45  LYS D NZ    1 
ATOM   13744 N  N     . TYR D 2 67  ? 157.728 94.222  121.646 1.00 36.26 ?  46  TYR D N     1 
ATOM   13745 C  CA    . TYR D 2 67  ? 158.894 94.546  122.474 1.00 36.90 ?  46  TYR D CA    1 
ATOM   13746 C  C     . TYR D 2 67  ? 158.810 94.072  123.926 1.00 36.28 ?  46  TYR D C     1 
ATOM   13747 O  O     . TYR D 2 67  ? 159.749 94.274  124.690 1.00 36.44 ?  46  TYR D O     1 
ATOM   13748 C  CB    . TYR D 2 67  ? 159.223 96.042  122.412 1.00 37.15 ?  46  TYR D CB    1 
ATOM   13749 C  CG    . TYR D 2 67  ? 159.471 96.550  121.011 1.00 39.40 ?  46  TYR D CG    1 
ATOM   13750 C  CD1   . TYR D 2 67  ? 160.249 95.817  120.109 1.00 41.26 ?  46  TYR D CD1   1 
ATOM   13751 C  CD2   . TYR D 2 67  ? 158.953 97.771  120.593 1.00 41.06 ?  46  TYR D CD2   1 
ATOM   13752 C  CE1   . TYR D 2 67  ? 160.480 96.279  118.814 1.00 43.03 ?  46  TYR D CE1   1 
ATOM   13753 C  CE2   . TYR D 2 67  ? 159.184 98.247  119.300 1.00 43.05 ?  46  TYR D CE2   1 
ATOM   13754 C  CZ    . TYR D 2 67  ? 159.948 97.500  118.417 1.00 43.80 ?  46  TYR D CZ    1 
ATOM   13755 O  OH    . TYR D 2 67  ? 160.171 97.971  117.136 1.00 45.18 ?  46  TYR D OH    1 
ATOM   13756 N  N     . LEU D 2 68  ? 157.695 93.454  124.311 1.00 35.71 ?  47  LEU D N     1 
ATOM   13757 C  CA    . LEU D 2 68  ? 157.571 92.904  125.662 1.00 34.92 ?  47  LEU D CA    1 
ATOM   13758 C  C     . LEU D 2 68  ? 158.232 91.525  125.750 1.00 34.32 ?  47  LEU D C     1 
ATOM   13759 O  O     . LEU D 2 68  ? 158.240 90.768  124.776 1.00 34.50 ?  47  LEU D O     1 
ATOM   13760 C  CB    . LEU D 2 68  ? 156.102 92.821  126.103 1.00 35.00 ?  47  LEU D CB    1 
ATOM   13761 C  CG    . LEU D 2 68  ? 155.205 94.067  125.998 1.00 35.82 ?  47  LEU D CG    1 
ATOM   13762 C  CD1   . LEU D 2 68  ? 153.804 93.744  126.494 1.00 35.95 ?  47  LEU D CD1   1 
ATOM   13763 C  CD2   . LEU D 2 68  ? 155.771 95.273  126.748 1.00 35.97 ?  47  LEU D CD2   1 
ATOM   13764 N  N     . GLY D 2 69  ? 158.783 91.211  126.921 1.00 33.50 ?  48  GLY D N     1 
ATOM   13765 C  CA    . GLY D 2 69  ? 159.300 89.876  127.210 1.00 32.41 ?  48  GLY D CA    1 
ATOM   13766 C  C     . GLY D 2 69  ? 158.202 88.824  127.277 1.00 32.15 ?  48  GLY D C     1 
ATOM   13767 O  O     . GLY D 2 69  ? 157.010 89.151  127.340 1.00 30.98 ?  48  GLY D O     1 
ATOM   13768 N  N     . LYS D 2 70  ? 158.610 87.557  127.272 1.00 32.14 ?  49  LYS D N     1 
ATOM   13769 C  CA    . LYS D 2 70  ? 157.673 86.439  127.342 1.00 32.25 ?  49  LYS D CA    1 
ATOM   13770 C  C     . LYS D 2 70  ? 156.826 86.463  128.613 1.00 31.24 ?  49  LYS D C     1 
ATOM   13771 O  O     . LYS D 2 70  ? 155.624 86.218  128.542 1.00 31.34 ?  49  LYS D O     1 
ATOM   13772 C  CB    . LYS D 2 70  ? 158.406 85.101  127.220 1.00 33.07 ?  49  LYS D CB    1 
ATOM   13773 C  CG    . LYS D 2 70  ? 159.129 84.912  125.896 1.00 35.74 ?  49  LYS D CG    1 
ATOM   13774 C  CD    . LYS D 2 70  ? 160.058 83.704  125.968 1.00 39.67 ?  49  LYS D CD    1 
ATOM   13775 C  CE    . LYS D 2 70  ? 161.026 83.678  124.795 1.00 40.96 ?  49  LYS D CE    1 
ATOM   13776 N  NZ    . LYS D 2 70  ? 162.098 82.684  125.043 1.00 42.55 1  49  LYS D NZ    1 
ATOM   13777 N  N     . ASN D 2 71  ? 157.445 86.767  129.759 1.00 29.92 ?  50  ASN D N     1 
ATOM   13778 C  CA    . ASN D 2 71  ? 156.719 86.837  131.032 1.00 29.37 ?  50  ASN D CA    1 
ATOM   13779 C  C     . ASN D 2 71  ? 155.674 87.948  131.031 1.00 28.35 ?  50  ASN D C     1 
ATOM   13780 O  O     . ASN D 2 71  ? 154.567 87.757  131.549 1.00 27.64 ?  50  ASN D O     1 
ATOM   13781 C  CB    . ASN D 2 71  ? 157.661 87.004  132.240 1.00 29.38 ?  50  ASN D CB    1 
ATOM   13782 C  CG    . ASN D 2 71  ? 158.383 85.712  132.619 1.00 31.22 ?  50  ASN D CG    1 
ATOM   13783 O  OD1   . ASN D 2 71  ? 157.866 84.608  132.435 1.00 33.03 ?  50  ASN D OD1   1 
ATOM   13784 N  ND2   . ASN D 2 71  ? 159.585 85.851  133.167 1.00 31.97 ?  50  ASN D ND2   1 
ATOM   13785 N  N     . GLU D 2 72  ? 156.025 89.093  130.441 1.00 27.72 ?  51  GLU D N     1 
ATOM   13786 C  CA    . GLU D 2 72  ? 155.086 90.220  130.325 1.00 27.70 ?  51  GLU D CA    1 
ATOM   13787 C  C     . GLU D 2 72  ? 153.892 89.867  129.432 1.00 27.62 ?  51  GLU D C     1 
ATOM   13788 O  O     . GLU D 2 72  ? 152.745 90.190  129.756 1.00 27.56 ?  51  GLU D O     1 
ATOM   13789 C  CB    . GLU D 2 72  ? 155.780 91.473  129.782 1.00 27.55 ?  51  GLU D CB    1 
ATOM   13790 C  CG    . GLU D 2 72  ? 156.948 91.988  130.632 1.00 28.77 ?  51  GLU D CG    1 
ATOM   13791 C  CD    . GLU D 2 72  ? 157.496 93.298  130.094 1.00 31.18 ?  51  GLU D CD    1 
ATOM   13792 O  OE1   . GLU D 2 72  ? 158.154 93.279  129.032 1.00 33.17 ?  51  GLU D OE1   1 
ATOM   13793 O  OE2   . GLU D 2 72  ? 157.261 94.345  130.728 1.00 31.66 -1 51  GLU D OE2   1 
ATOM   13794 N  N     . GLN D 2 73  ? 154.173 89.206  128.313 1.00 27.32 ?  52  GLN D N     1 
ATOM   13795 C  CA    . GLN D 2 73  ? 153.131 88.801  127.375 1.00 27.33 ?  52  GLN D CA    1 
ATOM   13796 C  C     . GLN D 2 73  ? 152.235 87.733  128.009 1.00 26.85 ?  52  GLN D C     1 
ATOM   13797 O  O     . GLN D 2 73  ? 151.009 87.783  127.873 1.00 26.24 ?  52  GLN D O     1 
ATOM   13798 C  CB    . GLN D 2 73  ? 153.740 88.301  126.071 1.00 27.65 ?  52  GLN D CB    1 
ATOM   13799 C  CG    . GLN D 2 73  ? 154.331 89.403  125.170 1.00 29.66 ?  52  GLN D CG    1 
ATOM   13800 C  CD    . GLN D 2 73  ? 154.755 88.888  123.795 1.00 32.60 ?  52  GLN D CD    1 
ATOM   13801 O  OE1   . GLN D 2 73  ? 154.974 87.694  123.606 1.00 34.76 ?  52  GLN D OE1   1 
ATOM   13802 N  NE2   . GLN D 2 73  ? 154.888 89.793  122.838 1.00 33.42 ?  52  GLN D NE2   1 
ATOM   13803 N  N     . ASP D 2 74  ? 152.859 86.801  128.726 1.00 26.26 ?  53  ASP D N     1 
ATOM   13804 C  CA    . ASP D 2 74  ? 152.159 85.728  129.440 1.00 26.50 ?  53  ASP D CA    1 
ATOM   13805 C  C     . ASP D 2 74  ? 151.242 86.287  130.520 1.00 25.81 ?  53  ASP D C     1 
ATOM   13806 O  O     . ASP D 2 74  ? 150.080 85.901  130.606 1.00 26.12 ?  53  ASP D O     1 
ATOM   13807 C  CB    . ASP D 2 74  ? 153.180 84.770  130.070 1.00 26.84 ?  53  ASP D CB    1 
ATOM   13808 C  CG    . ASP D 2 74  ? 152.541 83.538  130.709 1.00 29.50 ?  53  ASP D CG    1 
ATOM   13809 O  OD1   . ASP D 2 74  ? 151.924 82.722  129.990 1.00 32.08 ?  53  ASP D OD1   1 
ATOM   13810 O  OD2   . ASP D 2 74  ? 152.698 83.359  131.934 1.00 33.52 -1 53  ASP D OD2   1 
ATOM   13811 N  N     . THR D 2 75  ? 151.761 87.197  131.342 1.00 25.10 ?  54  THR D N     1 
ATOM   13812 C  CA    . THR D 2 75  ? 150.953 87.799  132.407 1.00 24.11 ?  54  THR D CA    1 
ATOM   13813 C  C     . THR D 2 75  ? 149.766 88.561  131.812 1.00 23.82 ?  54  THR D C     1 
ATOM   13814 O  O     . THR D 2 75  ? 148.630 88.390  132.255 1.00 23.81 ?  54  THR D O     1 
ATOM   13815 C  CB    . THR D 2 75  ? 151.797 88.705  133.325 1.00 23.80 ?  54  THR D CB    1 
ATOM   13816 O  OG1   . THR D 2 75  ? 152.791 87.908  133.982 1.00 24.62 ?  54  THR D OG1   1 
ATOM   13817 C  CG2   . THR D 2 75  ? 150.915 89.387  134.386 1.00 23.25 ?  54  THR D CG2   1 
ATOM   13818 N  N     . TYR D 2 76  ? 150.039 89.402  130.825 1.00 24.06 ?  55  TYR D N     1 
ATOM   13819 C  CA    . TYR D 2 76  ? 148.991 90.153  130.140 1.00 24.76 ?  55  TYR D CA    1 
ATOM   13820 C  C     . TYR D 2 76  ? 147.872 89.252  129.598 1.00 24.85 ?  55  TYR D C     1 
ATOM   13821 O  O     . TYR D 2 76  ? 146.691 89.522  129.833 1.00 24.83 ?  55  TYR D O     1 
ATOM   13822 C  CB    . TYR D 2 76  ? 149.575 90.999  129.009 1.00 24.78 ?  55  TYR D CB    1 
ATOM   13823 C  CG    . TYR D 2 76  ? 148.671 92.143  128.597 1.00 26.19 ?  55  TYR D CG    1 
ATOM   13824 C  CD1   . TYR D 2 76  ? 148.795 93.394  129.204 1.00 27.81 ?  55  TYR D CD1   1 
ATOM   13825 C  CD2   . TYR D 2 76  ? 147.686 91.978  127.619 1.00 28.03 ?  55  TYR D CD2   1 
ATOM   13826 C  CE1   . TYR D 2 76  ? 147.977 94.456  128.842 1.00 29.32 ?  55  TYR D CE1   1 
ATOM   13827 C  CE2   . TYR D 2 76  ? 146.851 93.042  127.248 1.00 29.01 ?  55  TYR D CE2   1 
ATOM   13828 C  CZ    . TYR D 2 76  ? 147.009 94.276  127.870 1.00 30.76 ?  55  TYR D CZ    1 
ATOM   13829 O  OH    . TYR D 2 76  ? 146.215 95.346  127.528 1.00 34.50 ?  55  TYR D OH    1 
ATOM   13830 N  N     . MET D 2 77  ? 148.248 88.197  128.877 1.00 25.76 ?  56  MET D N     1 
ATOM   13831 C  CA    . MET D 2 77  ? 147.277 87.237  128.343 1.00 26.81 ?  56  MET D CA    1 
ATOM   13832 C  C     . MET D 2 77  ? 146.415 86.623  129.450 1.00 26.23 ?  56  MET D C     1 
ATOM   13833 O  O     . MET D 2 77  ? 145.191 86.546  129.326 1.00 25.00 ?  56  MET D O     1 
ATOM   13834 C  CB    . MET D 2 77  ? 147.981 86.128  127.562 1.00 28.11 ?  56  MET D CB    1 
ATOM   13835 C  CG    . MET D 2 77  ? 148.616 86.566  126.237 1.00 32.52 ?  56  MET D CG    1 
ATOM   13836 S  SD    . MET D 2 77  ? 147.426 86.910  124.930 1.00 42.68 ?  56  MET D SD    1 
ATOM   13837 C  CE    . MET D 2 77  ? 147.001 88.626  125.232 1.00 38.97 ?  56  MET D CE    1 
ATOM   13838 N  N     . LYS D 2 78  ? 147.071 86.183  130.525 1.00 26.01 ?  57  LYS D N     1 
ATOM   13839 C  CA    . LYS D 2 78  ? 146.383 85.529  131.642 1.00 26.07 ?  57  LYS D CA    1 
ATOM   13840 C  C     . LYS D 2 78  ? 145.438 86.478  132.377 1.00 25.69 ?  57  LYS D C     1 
ATOM   13841 O  O     . LYS D 2 78  ? 144.331 86.088  132.766 1.00 25.58 ?  57  LYS D O     1 
ATOM   13842 C  CB    . LYS D 2 78  ? 147.389 84.908  132.621 1.00 26.08 ?  57  LYS D CB    1 
ATOM   13843 C  CG    . LYS D 2 78  ? 148.131 83.689  132.053 1.00 27.64 ?  57  LYS D CG    1 
ATOM   13844 C  CD    . LYS D 2 78  ? 149.236 83.220  132.993 1.00 29.47 ?  57  LYS D CD    1 
ATOM   13845 C  CE    . LYS D 2 78  ? 149.814 81.895  132.520 1.00 31.69 ?  57  LYS D CE    1 
ATOM   13846 N  NZ    . LYS D 2 78  ? 150.881 81.392  133.426 1.00 33.36 1  57  LYS D NZ    1 
ATOM   13847 N  N     . VAL D 2 79  ? 145.883 87.718  132.565 1.00 25.32 ?  58  VAL D N     1 
ATOM   13848 C  CA    . VAL D 2 79  ? 145.075 88.752  133.222 1.00 25.47 ?  58  VAL D CA    1 
ATOM   13849 C  C     . VAL D 2 79  ? 143.849 89.049  132.364 1.00 25.09 ?  58  VAL D C     1 
ATOM   13850 O  O     . VAL D 2 79  ? 142.719 89.090  132.858 1.00 24.46 ?  58  VAL D O     1 
ATOM   13851 C  CB    . VAL D 2 79  ? 145.920 90.037  133.445 1.00 25.83 ?  58  VAL D CB    1 
ATOM   13852 C  CG1   . VAL D 2 79  ? 145.053 91.275  133.487 1.00 27.35 ?  58  VAL D CG1   1 
ATOM   13853 C  CG2   . VAL D 2 79  ? 146.771 89.893  134.707 1.00 26.42 ?  58  VAL D CG2   1 
ATOM   13854 N  N     . LEU D 2 80  ? 144.088 89.203  131.063 1.00 25.27 ?  59  LEU D N     1 
ATOM   13855 C  CA    . LEU D 2 80  ? 143.039 89.530  130.123 1.00 25.55 ?  59  LEU D CA    1 
ATOM   13856 C  C     . LEU D 2 80  ? 141.969 88.439  130.120 1.00 24.94 ?  59  LEU D C     1 
ATOM   13857 O  O     . LEU D 2 80  ? 140.778 88.744  130.137 1.00 24.82 ?  59  LEU D O     1 
ATOM   13858 C  CB    . LEU D 2 80  ? 143.626 89.704  128.721 1.00 25.80 ?  59  LEU D CB    1 
ATOM   13859 C  CG    . LEU D 2 80  ? 143.450 91.000  127.922 1.00 28.76 ?  59  LEU D CG    1 
ATOM   13860 C  CD1   . LEU D 2 80  ? 143.412 90.644  126.436 1.00 30.25 ?  59  LEU D CD1   1 
ATOM   13861 C  CD2   . LEU D 2 80  ? 142.225 91.815  128.301 1.00 27.79 ?  59  LEU D CD2   1 
ATOM   13862 N  N     . ALA D 2 81  ? 142.402 87.178  130.104 1.00 24.86 ?  60  ALA D N     1 
ATOM   13863 C  CA    . ALA D 2 81  ? 141.479 86.035  130.109 1.00 24.60 ?  60  ALA D CA    1 
ATOM   13864 C  C     . ALA D 2 81  ? 140.692 85.983  131.415 1.00 23.80 ?  60  ALA D C     1 
ATOM   13865 O  O     . ALA D 2 81  ? 139.507 85.666  131.422 1.00 24.07 ?  60  ALA D O     1 
ATOM   13866 C  CB    . ALA D 2 81  ? 142.239 84.728  129.890 1.00 24.48 ?  60  ALA D CB    1 
ATOM   13867 N  N     . GLY D 2 82  ? 141.358 86.304  132.517 1.00 23.54 ?  61  GLY D N     1 
ATOM   13868 C  CA    . GLY D 2 82  ? 140.706 86.395  133.818 1.00 22.53 ?  61  GLY D CA    1 
ATOM   13869 C  C     . GLY D 2 82  ? 139.575 87.402  133.805 1.00 22.23 ?  61  GLY D C     1 
ATOM   13870 O  O     . GLY D 2 82  ? 138.460 87.100  134.229 1.00 21.27 ?  61  GLY D O     1 
ATOM   13871 N  N     . LEU D 2 83  ? 139.860 88.606  133.311 1.00 22.36 ?  62  LEU D N     1 
ATOM   13872 C  CA    . LEU D 2 83  ? 138.838 89.655  133.212 1.00 22.42 ?  62  LEU D CA    1 
ATOM   13873 C  C     . LEU D 2 83  ? 137.695 89.228  132.301 1.00 22.91 ?  62  LEU D C     1 
ATOM   13874 O  O     . LEU D 2 83  ? 136.519 89.433  132.632 1.00 22.99 ?  62  LEU D O     1 
ATOM   13875 C  CB    . LEU D 2 83  ? 139.439 90.970  132.702 1.00 22.19 ?  62  LEU D CB    1 
ATOM   13876 C  CG    . LEU D 2 83  ? 140.463 91.664  133.615 1.00 22.17 ?  62  LEU D CG    1 
ATOM   13877 C  CD1   . LEU D 2 83  ? 141.214 92.746  132.827 1.00 21.55 ?  62  LEU D CD1   1 
ATOM   13878 C  CD2   . LEU D 2 83  ? 139.759 92.257  134.822 1.00 22.42 ?  62  LEU D CD2   1 
ATOM   13879 N  N     . THR D 2 84  ? 138.041 88.617  131.173 1.00 23.39 ?  63  THR D N     1 
ATOM   13880 C  CA    . THR D 2 84  ? 137.043 88.189  130.196 1.00 24.42 ?  63  THR D CA    1 
ATOM   13881 C  C     . THR D 2 84  ? 136.069 87.182  130.813 1.00 24.55 ?  63  THR D C     1 
ATOM   13882 O  O     . THR D 2 84  ? 134.850 87.338  130.709 1.00 23.68 ?  63  THR D O     1 
ATOM   13883 C  CB    . THR D 2 84  ? 137.698 87.574  128.933 1.00 24.70 ?  63  THR D CB    1 
ATOM   13884 O  OG1   . THR D 2 84  ? 138.561 88.543  128.324 1.00 25.57 ?  63  THR D OG1   1 
ATOM   13885 C  CG2   . THR D 2 84  ? 136.633 87.173  127.926 1.00 25.36 ?  63  THR D CG2   1 
ATOM   13886 N  N     . LEU D 2 85  ? 136.631 86.162  131.453 1.00 25.38 ?  64  LEU D N     1 
ATOM   13887 C  CA    . LEU D 2 85  ? 135.842 85.106  132.075 1.00 26.44 ?  64  LEU D CA    1 
ATOM   13888 C  C     . LEU D 2 85  ? 134.924 85.640  133.178 1.00 25.96 ?  64  LEU D C     1 
ATOM   13889 O  O     . LEU D 2 85  ? 133.730 85.312  133.192 1.00 25.83 ?  64  LEU D O     1 
ATOM   13890 C  CB    . LEU D 2 85  ? 136.740 83.952  132.547 1.00 26.65 ?  64  LEU D CB    1 
ATOM   13891 C  CG    . LEU D 2 85  ? 137.217 83.061  131.384 1.00 29.62 ?  64  LEU D CG    1 
ATOM   13892 C  CD1   . LEU D 2 85  ? 138.491 82.310  131.725 1.00 31.57 ?  64  LEU D CD1   1 
ATOM   13893 C  CD2   . LEU D 2 85  ? 136.129 82.071  130.930 1.00 30.96 ?  64  LEU D CD2   1 
ATOM   13894 N  N     . LEU D 2 86  ? 135.451 86.493  134.060 1.00 25.63 ?  65  LEU D N     1 
ATOM   13895 C  CA    . LEU D 2 86  ? 134.612 87.092  135.102 1.00 25.59 ?  65  LEU D CA    1 
ATOM   13896 C  C     . LEU D 2 86  ? 133.512 87.997  134.550 1.00 25.60 ?  65  LEU D C     1 
ATOM   13897 O  O     . LEU D 2 86  ? 132.394 88.017  135.072 1.00 25.47 ?  65  LEU D O     1 
ATOM   13898 C  CB    . LEU D 2 86  ? 135.446 87.840  136.159 1.00 25.76 ?  65  LEU D CB    1 
ATOM   13899 C  CG    . LEU D 2 86  ? 136.317 86.970  137.075 1.00 26.71 ?  65  LEU D CG    1 
ATOM   13900 C  CD1   . LEU D 2 86  ? 137.330 87.807  137.850 1.00 28.01 ?  65  LEU D CD1   1 
ATOM   13901 C  CD2   . LEU D 2 86  ? 135.473 86.163  138.035 1.00 28.01 ?  65  LEU D CD2   1 
ATOM   13902 N  N     . ASP D 2 87  ? 133.825 88.752  133.504 1.00 25.49 ?  66  ASP D N     1 
ATOM   13903 C  CA    . ASP D 2 87  ? 132.861 89.690  132.953 1.00 25.83 ?  66  ASP D CA    1 
ATOM   13904 C  C     . ASP D 2 87  ? 131.704 88.980  132.236 1.00 26.20 ?  66  ASP D C     1 
ATOM   13905 O  O     . ASP D 2 87  ? 130.582 89.474  132.222 1.00 25.99 ?  66  ASP D O     1 
ATOM   13906 C  CB    . ASP D 2 87  ? 133.548 90.687  132.029 1.00 25.50 ?  66  ASP D CB    1 
ATOM   13907 C  CG    . ASP D 2 87  ? 132.877 92.030  132.045 1.00 25.76 ?  66  ASP D CG    1 
ATOM   13908 O  OD1   . ASP D 2 87  ? 132.264 92.373  133.085 1.00 26.91 ?  66  ASP D OD1   1 
ATOM   13909 O  OD2   . ASP D 2 87  ? 132.956 92.751  131.031 1.00 23.11 -1 66  ASP D OD2   1 
ATOM   13910 N  N     . THR D 2 88  ? 131.990 87.810  131.669 1.00 27.12 ?  67  THR D N     1 
ATOM   13911 C  CA    . THR D 2 88  ? 130.976 86.970  131.046 1.00 28.40 ?  67  THR D CA    1 
ATOM   13912 C  C     . THR D 2 88  ? 129.956 86.486  132.064 1.00 28.28 ?  67  THR D C     1 
ATOM   13913 O  O     . THR D 2 88  ? 128.759 86.480  131.785 1.00 28.10 ?  67  THR D O     1 
ATOM   13914 C  CB    . THR D 2 88  ? 131.608 85.767  130.320 1.00 29.04 ?  67  THR D CB    1 
ATOM   13915 O  OG1   . THR D 2 88  ? 132.504 86.250  129.317 1.00 31.00 ?  67  THR D OG1   1 
ATOM   13916 C  CG2   . THR D 2 88  ? 130.532 84.919  129.644 1.00 30.16 ?  67  THR D CG2   1 
ATOM   13917 N  N     . GLU D 2 89  ? 130.424 86.083  133.244 1.00 28.28 ?  68  GLU D N     1 
ATOM   13918 C  CA    . GLU D 2 89  ? 129.508 85.701  134.313 1.00 29.16 ?  68  GLU D CA    1 
ATOM   13919 C  C     . GLU D 2 89  ? 128.601 86.878  134.667 1.00 28.65 ?  68  GLU D C     1 
ATOM   13920 O  O     . GLU D 2 89  ? 127.408 86.700  134.870 1.00 28.44 ?  68  GLU D O     1 
ATOM   13921 C  CB    . GLU D 2 89  ? 130.258 85.219  135.562 1.00 29.32 ?  68  GLU D CB    1 
ATOM   13922 C  CG    . GLU D 2 89  ? 131.150 83.989  135.339 1.00 31.95 ?  68  GLU D CG    1 
ATOM   13923 C  CD    . GLU D 2 89  ? 130.381 82.729  134.953 1.00 35.19 ?  68  GLU D CD    1 
ATOM   13924 O  OE1   . GLU D 2 89  ? 129.144 82.667  135.138 1.00 35.47 ?  68  GLU D OE1   1 
ATOM   13925 O  OE2   . GLU D 2 89  ? 131.030 81.788  134.451 1.00 38.06 -1 68  GLU D OE2   1 
ATOM   13926 N  N     . GLN D 2 90  ? 129.170 88.079  134.721 1.00 28.45 ?  69  GLN D N     1 
ATOM   13927 C  CA    . GLN D 2 90  ? 128.394 89.268  135.074 1.00 28.47 ?  69  GLN D CA    1 
ATOM   13928 C  C     . GLN D 2 90  ? 127.333 89.596  134.014 1.00 28.97 ?  69  GLN D C     1 
ATOM   13929 O  O     . GLN D 2 90  ? 126.217 89.986  134.354 1.00 28.84 ?  69  GLN D O     1 
ATOM   13930 C  CB    . GLN D 2 90  ? 129.317 90.462  135.339 1.00 28.21 ?  69  GLN D CB    1 
ATOM   13931 C  CG    . GLN D 2 90  ? 128.666 91.610  136.108 1.00 27.75 ?  69  GLN D CG    1 
ATOM   13932 C  CD    . GLN D 2 90  ? 128.403 91.304  137.578 1.00 28.91 ?  69  GLN D CD    1 
ATOM   13933 O  OE1   . GLN D 2 90  ? 128.321 90.139  137.992 1.00 27.62 ?  69  GLN D OE1   1 
ATOM   13934 N  NE2   . GLN D 2 90  ? 128.246 92.362  138.375 1.00 28.23 ?  69  GLN D NE2   1 
ATOM   13935 N  N     . GLY D 2 91  ? 127.678 89.411  132.740 1.00 29.62 ?  70  GLY D N     1 
ATOM   13936 C  CA    . GLY D 2 91  ? 126.737 89.634  131.640 1.00 30.43 ?  70  GLY D CA    1 
ATOM   13937 C  C     . GLY D 2 91  ? 125.642 88.582  131.507 1.00 31.11 ?  70  GLY D C     1 
ATOM   13938 O  O     . GLY D 2 91  ? 124.481 88.905  131.233 1.00 30.77 ?  70  GLY D O     1 
ATOM   13939 N  N     . ASN D 2 92  ? 126.004 87.321  131.689 1.00 31.69 ?  71  ASN D N     1 
ATOM   13940 C  CA    . ASN D 2 92  ? 125.030 86.246  131.548 1.00 32.72 ?  71  ASN D CA    1 
ATOM   13941 C  C     . ASN D 2 92  ? 124.161 85.995  132.772 1.00 32.60 ?  71  ASN D C     1 
ATOM   13942 O  O     . ASN D 2 92  ? 123.017 85.555  132.629 1.00 33.12 ?  71  ASN D O     1 
ATOM   13943 C  CB    . ASN D 2 92  ? 125.714 84.958  131.110 1.00 33.68 ?  71  ASN D CB    1 
ATOM   13944 C  CG    . ASN D 2 92  ? 126.174 85.013  129.668 1.00 35.15 ?  71  ASN D CG    1 
ATOM   13945 O  OD1   . ASN D 2 92  ? 127.122 84.333  129.295 1.00 40.21 ?  71  ASN D OD1   1 
ATOM   13946 N  ND2   . ASN D 2 92  ? 125.510 85.835  128.852 1.00 36.91 ?  71  ASN D ND2   1 
ATOM   13947 N  N     . THR D 2 93  ? 124.693 86.293  133.958 1.00 31.76 ?  72  THR D N     1 
ATOM   13948 C  CA    . THR D 2 93  ? 124.009 85.975  135.206 1.00 31.47 ?  72  THR D CA    1 
ATOM   13949 C  C     . THR D 2 93  ? 123.875 87.161  136.158 1.00 30.62 ?  72  THR D C     1 
ATOM   13950 O  O     . THR D 2 93  ? 122.763 87.532  136.524 1.00 30.71 ?  72  THR D O     1 
ATOM   13951 C  CB    . THR D 2 93  ? 124.700 84.819  135.922 1.00 31.60 ?  72  THR D CB    1 
ATOM   13952 O  OG1   . THR D 2 93  ? 124.774 83.698  135.031 1.00 33.14 ?  72  THR D OG1   1 
ATOM   13953 C  CG2   . THR D 2 93  ? 123.932 84.423  137.173 1.00 31.89 ?  72  THR D CG2   1 
ATOM   13954 N  N     . GLY D 2 94  ? 125.005 87.748  136.548 1.00 29.61 ?  73  GLY D N     1 
ATOM   13955 C  CA    . GLY D 2 94  ? 125.035 88.791  137.574 1.00 28.47 ?  73  GLY D CA    1 
ATOM   13956 C  C     . GLY D 2 94  ? 124.079 89.950  137.370 1.00 27.90 ?  73  GLY D C     1 
ATOM   13957 O  O     . GLY D 2 94  ? 123.264 90.265  138.248 1.00 28.27 ?  73  GLY D O     1 
ATOM   13958 N  N     . MET D 2 95  ? 124.181 90.615  136.228 1.00 26.67 ?  74  MET D N     1 
ATOM   13959 C  CA    . MET D 2 95  ? 123.292 91.751  135.994 1.00 26.00 ?  74  MET D CA    1 
ATOM   13960 C  C     . MET D 2 95  ? 121.867 91.305  135.690 1.00 25.25 ?  74  MET D C     1 
ATOM   13961 O  O     . MET D 2 95  ? 120.933 91.896  136.217 1.00 24.97 ?  74  MET D O     1 
ATOM   13962 C  CB    . MET D 2 95  ? 123.818 92.704  134.913 1.00 26.00 ?  74  MET D CB    1 
ATOM   13963 C  CG    . MET D 2 95  ? 124.894 93.645  135.399 1.00 26.40 ?  74  MET D CG    1 
ATOM   13964 S  SD    . MET D 2 95  ? 124.359 94.755  136.726 1.00 28.10 ?  74  MET D SD    1 
ATOM   13965 C  CE    . MET D 2 95  ? 125.931 95.515  137.112 1.00 28.95 ?  74  MET D CE    1 
ATOM   13966 N  N     . PRO D 2 96  ? 121.691 90.278  134.837 1.00 24.98 ?  75  PRO D N     1 
ATOM   13967 C  CA    . PRO D 2 96  ? 120.289 89.911  134.564 1.00 24.59 ?  75  PRO D CA    1 
ATOM   13968 C  C     . PRO D 2 96  ? 119.537 89.361  135.774 1.00 23.90 ?  75  PRO D C     1 
ATOM   13969 O  O     . PRO D 2 96  ? 118.333 89.570  135.868 1.00 23.45 ?  75  PRO D O     1 
ATOM   13970 C  CB    . PRO D 2 96  ? 120.401 88.830  133.481 1.00 24.80 ?  75  PRO D CB    1 
ATOM   13971 C  CG    . PRO D 2 96  ? 121.723 89.111  132.803 1.00 25.75 ?  75  PRO D CG    1 
ATOM   13972 C  CD    . PRO D 2 96  ? 122.625 89.617  133.900 1.00 25.07 ?  75  PRO D CD    1 
ATOM   13973 N  N     . ILE D 2 97  ? 120.227 88.660  136.678 1.00 23.36 ?  76  ILE D N     1 
ATOM   13974 C  CA    . ILE D 2 97  ? 119.549 88.088  137.837 1.00 23.48 ?  76  ILE D CA    1 
ATOM   13975 C  C     . ILE D 2 97  ? 119.126 89.179  138.806 1.00 23.30 ?  76  ILE D C     1 
ATOM   13976 O  O     . ILE D 2 97  ? 118.052 89.096  139.399 1.00 23.45 ?  76  ILE D O     1 
ATOM   13977 C  CB    . ILE D 2 97  ? 120.384 86.981  138.542 1.00 23.96 ?  76  ILE D CB    1 
ATOM   13978 C  CG1   . ILE D 2 97  ? 119.473 86.011  139.286 1.00 24.71 ?  76  ILE D CG1   1 
ATOM   13979 C  CG2   . ILE D 2 97  ? 121.463 87.569  139.483 1.00 24.02 ?  76  ILE D CG2   1 
ATOM   13980 C  CD1   . ILE D 2 97  ? 120.024 84.564  139.289 1.00 29.17 ?  76  ILE D CD1   1 
ATOM   13981 N  N     . VAL D 2 98  ? 119.962 90.206  138.956 1.00 22.71 ?  77  VAL D N     1 
ATOM   13982 C  CA    . VAL D 2 98  ? 119.625 91.345  139.826 1.00 22.78 ?  77  VAL D CA    1 
ATOM   13983 C  C     . VAL D 2 98  ? 118.471 92.150  139.225 1.00 22.89 ?  77  VAL D C     1 
ATOM   13984 O  O     . VAL D 2 98  ? 117.540 92.537  139.931 1.00 23.72 ?  77  VAL D O     1 
ATOM   13985 C  CB    . VAL D 2 98  ? 120.870 92.224  140.128 1.00 22.49 ?  77  VAL D CB    1 
ATOM   13986 C  CG1   . VAL D 2 98  ? 120.483 93.533  140.840 1.00 21.91 ?  77  VAL D CG1   1 
ATOM   13987 C  CG2   . VAL D 2 98  ? 121.852 91.442  140.985 1.00 23.02 ?  77  VAL D CG2   1 
ATOM   13988 N  N     . ALA D 2 99  ? 118.513 92.370  137.911 1.00 23.19 ?  78  ALA D N     1 
ATOM   13989 C  CA    . ALA D 2 99  ? 117.419 93.065  137.217 1.00 23.05 ?  78  ALA D CA    1 
ATOM   13990 C  C     . ALA D 2 99  ? 116.092 92.324  137.406 1.00 23.52 ?  78  ALA D C     1 
ATOM   13991 O  O     . ALA D 2 99  ? 115.033 92.940  137.567 1.00 23.68 ?  78  ALA D O     1 
ATOM   13992 C  CB    . ALA D 2 99  ? 117.746 93.227  135.742 1.00 22.81 ?  78  ALA D CB    1 
ATOM   13993 N  N     . GLU D 2 100 ? 116.150 90.996  137.396 1.00 23.68 ?  79  GLU D N     1 
ATOM   13994 C  CA    . GLU D 2 100 ? 114.956 90.178  137.593 1.00 24.14 ?  79  GLU D CA    1 
ATOM   13995 C  C     . GLU D 2 100 ? 114.298 90.349  138.972 1.00 23.66 ?  79  GLU D C     1 
ATOM   13996 O  O     . GLU D 2 100 ? 113.070 90.428  139.076 1.00 22.94 ?  79  GLU D O     1 
ATOM   13997 C  CB    . GLU D 2 100 ? 115.298 88.707  137.350 1.00 24.47 ?  79  GLU D CB    1 
ATOM   13998 C  CG    . GLU D 2 100 ? 114.088 87.794  137.296 1.00 27.90 ?  79  GLU D CG    1 
ATOM   13999 C  CD    . GLU D 2 100 ? 114.468 86.326  137.232 1.00 32.30 ?  79  GLU D CD    1 
ATOM   14000 O  OE1   . GLU D 2 100 ? 115.577 86.007  136.745 1.00 32.88 ?  79  GLU D OE1   1 
ATOM   14001 O  OE2   . GLU D 2 100 ? 113.653 85.493  137.678 1.00 34.74 -1 79  GLU D OE2   1 
ATOM   14002 N  N     . HIS D 2 101 ? 115.109 90.397  140.028 1.00 23.62 ?  80  HIS D N     1 
ATOM   14003 C  CA    . HIS D 2 101 ? 114.578 90.451  141.403 1.00 23.99 ?  80  HIS D CA    1 
ATOM   14004 C  C     . HIS D 2 101 ? 114.338 91.850  141.985 1.00 24.35 ?  80  HIS D C     1 
ATOM   14005 O  O     . HIS D 2 101 ? 113.607 91.990  142.967 1.00 24.21 ?  80  HIS D O     1 
ATOM   14006 C  CB    . HIS D 2 101 ? 115.448 89.607  142.345 1.00 24.13 ?  80  HIS D CB    1 
ATOM   14007 C  CG    . HIS D 2 101 ? 115.409 88.140  142.034 1.00 24.76 ?  80  HIS D CG    1 
ATOM   14008 N  ND1   . HIS D 2 101 ? 114.535 87.270  142.654 1.00 25.68 ?  80  HIS D ND1   1 
ATOM   14009 C  CD2   . HIS D 2 101 ? 116.117 87.396  141.152 1.00 25.75 ?  80  HIS D CD2   1 
ATOM   14010 C  CE1   . HIS D 2 101 ? 114.713 86.052  142.169 1.00 26.21 ?  80  HIS D CE1   1 
ATOM   14011 N  NE2   . HIS D 2 101 ? 115.667 86.101  141.258 1.00 25.35 ?  80  HIS D NE2   1 
ATOM   14012 N  N     . VAL D 2 102 ? 114.953 92.878  141.401 1.00 24.50 ?  81  VAL D N     1 
ATOM   14013 C  CA    . VAL D 2 102 ? 114.742 94.254  141.849 1.00 25.50 ?  81  VAL D CA    1 
ATOM   14014 C  C     . VAL D 2 102 ? 113.379 94.768  141.359 1.00 26.14 ?  81  VAL D C     1 
ATOM   14015 O  O     . VAL D 2 102 ? 113.032 94.576  140.197 1.00 26.96 ?  81  VAL D O     1 
ATOM   14016 C  CB    . VAL D 2 102 ? 115.884 95.189  141.355 1.00 25.30 ?  81  VAL D CB    1 
ATOM   14017 C  CG1   . VAL D 2 102 ? 115.534 96.642  141.575 1.00 27.08 ?  81  VAL D CG1   1 
ATOM   14018 C  CG2   . VAL D 2 102 ? 117.181 94.866  142.080 1.00 25.41 ?  81  VAL D CG2   1 
ATOM   14019 N  N     . ASP D 2 103 ? 112.615 95.396  142.250 1.00 26.45 ?  82  ASP D N     1 
ATOM   14020 C  CA    . ASP D 2 103 ? 111.346 96.026  141.879 1.00 27.15 ?  82  ASP D CA    1 
ATOM   14021 C  C     . ASP D 2 103 ? 111.567 97.474  141.467 1.00 26.39 ?  82  ASP D C     1 
ATOM   14022 O  O     . ASP D 2 103 ? 112.382 98.188  142.066 1.00 26.40 ?  82  ASP D O     1 
ATOM   14023 C  CB    . ASP D 2 103 ? 110.341 95.975  143.034 1.00 27.72 ?  82  ASP D CB    1 
ATOM   14024 C  CG    . ASP D 2 103 ? 109.960 94.554  143.435 1.00 31.46 ?  82  ASP D CG    1 
ATOM   14025 O  OD1   . ASP D 2 103 ? 109.926 93.641  142.566 1.00 34.26 ?  82  ASP D OD1   1 
ATOM   14026 O  OD2   . ASP D 2 103 ? 109.681 94.348  144.638 1.00 35.52 -1 82  ASP D OD2   1 
ATOM   14027 N  N     . GLY D 2 104 ? 110.822 97.907  140.454 1.00 25.52 ?  83  GLY D N     1 
ATOM   14028 C  CA    . GLY D 2 104 ? 110.894 99.287  139.976 1.00 24.31 ?  83  GLY D CA    1 
ATOM   14029 C  C     . GLY D 2 104 ? 111.234 99.290  138.490 1.00 23.27 ?  83  GLY D C     1 
ATOM   14030 O  O     . GLY D 2 104 ? 112.241 98.719  138.075 1.00 22.38 ?  83  GLY D O     1 
ATOM   14031 N  N     . HIS D 2 105 ? 110.382 99.921  137.687 1.00 22.46 ?  84  HIS D N     1 
ATOM   14032 C  CA    . HIS D 2 105 ? 110.605 99.976  136.240 1.00 22.17 ?  84  HIS D CA    1 
ATOM   14033 C  C     . HIS D 2 105 ? 111.888 100.692 135.854 1.00 21.13 ?  84  HIS D C     1 
ATOM   14034 O  O     . HIS D 2 105 ? 112.583 100.262 134.935 1.00 20.91 ?  84  HIS D O     1 
ATOM   14035 C  CB    . HIS D 2 105 ? 109.405 100.619 135.531 1.00 22.07 ?  84  HIS D CB    1 
ATOM   14036 C  CG    . HIS D 2 105 ? 108.125 99.882  135.762 1.00 23.85 ?  84  HIS D CG    1 
ATOM   14037 N  ND1   . HIS D 2 105 ? 108.007 98.525  135.548 1.00 24.86 ?  84  HIS D ND1   1 
ATOM   14038 C  CD2   . HIS D 2 105 ? 106.923 100.298 136.223 1.00 25.19 ?  84  HIS D CD2   1 
ATOM   14039 C  CE1   . HIS D 2 105 ? 106.779 98.141  135.846 1.00 24.94 ?  84  HIS D CE1   1 
ATOM   14040 N  NE2   . HIS D 2 105 ? 106.105 99.197  136.264 1.00 26.41 ?  84  HIS D NE2   1 
ATOM   14041 N  N     . GLN D 2 106 ? 112.200 101.778 136.547 1.00 20.66 ?  85  GLN D N     1 
ATOM   14042 C  CA    . GLN D 2 106 ? 113.349 102.593 136.161 1.00 20.70 ?  85  GLN D CA    1 
ATOM   14043 C  C     . GLN D 2 106 ? 114.648 101.880 136.534 1.00 20.46 ?  85  GLN D C     1 
ATOM   14044 O  O     . GLN D 2 106 ? 115.614 101.916 135.772 1.00 20.72 ?  85  GLN D O     1 
ATOM   14045 C  CB    . GLN D 2 106 ? 113.241 104.018 136.728 1.00 20.60 ?  85  GLN D CB    1 
ATOM   14046 C  CG    . GLN D 2 106 ? 111.994 104.781 136.203 1.00 20.74 ?  85  GLN D CG    1 
ATOM   14047 C  CD    . GLN D 2 106 ? 111.740 106.127 136.892 1.00 22.11 ?  85  GLN D CD    1 
ATOM   14048 O  OE1   . GLN D 2 106 ? 112.662 106.785 137.361 1.00 22.88 ?  85  GLN D OE1   1 
ATOM   14049 N  NE2   . GLN D 2 106 ? 110.476 106.541 136.938 1.00 21.64 ?  85  GLN D NE2   1 
ATOM   14050 N  N     . ARG D 2 107 ? 114.646 101.193 137.679 1.00 20.17 ?  86  ARG D N     1 
ATOM   14051 C  CA    . ARG D 2 107 ? 115.800 100.400 138.105 1.00 20.29 ?  86  ARG D CA    1 
ATOM   14052 C  C     . ARG D 2 107 ? 116.043 99.244  137.148 1.00 20.07 ?  86  ARG D C     1 
ATOM   14053 O  O     . ARG D 2 107 ? 117.181 98.963  136.797 1.00 19.53 ?  86  ARG D O     1 
ATOM   14054 C  CB    . ARG D 2 107 ? 115.595 99.844  139.512 1.00 20.88 ?  86  ARG D CB    1 
ATOM   14055 C  CG    . ARG D 2 107 ? 115.371 100.911 140.534 1.00 22.56 ?  86  ARG D CG    1 
ATOM   14056 C  CD    . ARG D 2 107 ? 114.851 100.319 141.819 1.00 27.21 ?  86  ARG D CD    1 
ATOM   14057 N  NE    . ARG D 2 107 ? 115.149 101.276 142.868 1.00 31.70 ?  86  ARG D NE    1 
ATOM   14058 C  CZ    . ARG D 2 107 ? 115.218 100.998 144.153 1.00 32.23 ?  86  ARG D CZ    1 
ATOM   14059 N  NH1   . ARG D 2 107 ? 114.994 99.761  144.595 1.00 34.27 1  86  ARG D NH1   1 
ATOM   14060 N  NH2   . ARG D 2 107 ? 115.520 101.975 144.988 1.00 33.79 ?  86  ARG D NH2   1 
ATOM   14061 N  N     . LYS D 2 108 ? 114.968 98.567  136.741 1.00 19.61 ?  87  LYS D N     1 
ATOM   14062 C  CA    . LYS D 2 108 ? 115.098 97.478  135.773 1.00 19.92 ?  87  LYS D CA    1 
ATOM   14063 C  C     . LYS D 2 108 ? 115.695 97.966  134.449 1.00 20.08 ?  87  LYS D C     1 
ATOM   14064 O  O     . LYS D 2 108 ? 116.449 97.236  133.797 1.00 20.38 ?  87  LYS D O     1 
ATOM   14065 C  CB    . LYS D 2 108 ? 113.766 96.762  135.536 1.00 19.54 ?  87  LYS D CB    1 
ATOM   14066 C  CG    . LYS D 2 108 ? 113.247 95.997  136.739 1.00 20.55 ?  87  LYS D CG    1 
ATOM   14067 C  CD    . LYS D 2 108 ? 111.930 95.286  136.422 1.00 21.09 ?  87  LYS D CD    1 
ATOM   14068 C  CE    . LYS D 2 108 ? 111.414 94.477  137.607 1.00 22.98 ?  87  LYS D CE    1 
ATOM   14069 N  NZ    . LYS D 2 108 ? 112.259 93.242  137.830 1.00 22.30 1  87  LYS D NZ    1 
ATOM   14070 N  N     . ALA D 2 109 ? 115.352 99.190  134.050 1.00 19.72 ?  88  ALA D N     1 
ATOM   14071 C  CA    . ALA D 2 109 ? 115.870 99.750  132.807 1.00 19.83 ?  88  ALA D CA    1 
ATOM   14072 C  C     . ALA D 2 109 ? 117.369 100.035 132.906 1.00 19.84 ?  88  ALA D C     1 
ATOM   14073 O  O     . ALA D 2 109 ? 118.135 99.687  132.001 1.00 19.96 ?  88  ALA D O     1 
ATOM   14074 C  CB    . ALA D 2 109 ? 115.086 101.010 132.404 1.00 19.65 ?  88  ALA D CB    1 
ATOM   14075 N  N     . VAL D 2 110 ? 117.790 100.642 134.013 1.00 19.33 ?  89  VAL D N     1 
ATOM   14076 C  CA    . VAL D 2 110 ? 119.214 100.928 134.238 1.00 19.22 ?  89  VAL D CA    1 
ATOM   14077 C  C     . VAL D 2 110 ? 119.992 99.600  134.282 1.00 19.45 ?  89  VAL D C     1 
ATOM   14078 O  O     . VAL D 2 110 ? 120.978 99.416  133.554 1.00 18.97 ?  89  VAL D O     1 
ATOM   14079 C  CB    . VAL D 2 110 ? 119.419 101.808 135.504 1.00 19.01 ?  89  VAL D CB    1 
ATOM   14080 C  CG1   . VAL D 2 110 ? 120.924 101.961 135.869 1.00 19.90 ?  89  VAL D CG1   1 
ATOM   14081 C  CG2   . VAL D 2 110 ? 118.813 103.174 135.271 1.00 19.69 ?  89  VAL D CG2   1 
ATOM   14082 N  N     . LEU D 2 111 ? 119.499 98.652  135.080 1.00 19.27 ?  90  LEU D N     1 
ATOM   14083 C  CA    . LEU D 2 111 ? 120.125 97.330  135.151 1.00 19.96 ?  90  LEU D CA    1 
ATOM   14084 C  C     . LEU D 2 111 ? 120.210 96.621  133.793 1.00 20.30 ?  90  LEU D C     1 
ATOM   14085 O  O     . LEU D 2 111 ? 121.239 96.019  133.475 1.00 19.88 ?  90  LEU D O     1 
ATOM   14086 C  CB    . LEU D 2 111 ? 119.460 96.453  136.220 1.00 19.87 ?  90  LEU D CB    1 
ATOM   14087 C  CG    . LEU D 2 111 ? 119.689 96.962  137.645 1.00 20.24 ?  90  LEU D CG    1 
ATOM   14088 C  CD1   . LEU D 2 111 ? 118.752 96.307  138.672 1.00 21.85 ?  90  LEU D CD1   1 
ATOM   14089 C  CD2   . LEU D 2 111 ? 121.165 96.812  138.058 1.00 20.29 ?  90  LEU D CD2   1 
ATOM   14090 N  N     . ASN D 2 112 ? 119.147 96.713  132.989 1.00 20.92 ?  91  ASN D N     1 
ATOM   14091 C  CA    . ASN D 2 112 ? 119.180 96.205  131.598 1.00 20.70 ?  91  ASN D CA    1 
ATOM   14092 C  C     . ASN D 2 112 ? 120.260 96.856  130.752 1.00 20.57 ?  91  ASN D C     1 
ATOM   14093 O  O     . ASN D 2 112 ? 120.886 96.199  129.904 1.00 20.45 ?  91  ASN D O     1 
ATOM   14094 C  CB    . ASN D 2 112 ? 117.853 96.457  130.880 1.00 21.16 ?  91  ASN D CB    1 
ATOM   14095 C  CG    . ASN D 2 112 ? 116.916 95.267  130.925 1.00 21.98 ?  91  ASN D CG    1 
ATOM   14096 O  OD1   . ASN D 2 112 ? 117.190 94.251  131.572 1.00 25.37 ?  91  ASN D OD1   1 
ATOM   14097 N  ND2   . ASN D 2 112 ? 115.787 95.398  130.253 1.00 21.12 ?  91  ASN D ND2   1 
ATOM   14098 N  N     . PHE D 2 113 ? 120.414 98.167  130.919 1.00 19.70 ?  92  PHE D N     1 
ATOM   14099 C  CA    . PHE D 2 113 ? 121.440 98.889  130.199 1.00 20.02 ?  92  PHE D CA    1 
ATOM   14100 C  C     . PHE D 2 113 ? 122.838 98.385  130.588 1.00 19.97 ?  92  PHE D C     1 
ATOM   14101 O  O     . PHE D 2 113 ? 123.688 98.155  129.721 1.00 19.22 ?  92  PHE D O     1 
ATOM   14102 C  CB    . PHE D 2 113 ? 121.325 100.411 130.393 1.00 20.09 ?  92  PHE D CB    1 
ATOM   14103 C  CG    . PHE D 2 113 ? 122.259 101.177 129.524 1.00 20.54 ?  92  PHE D CG    1 
ATOM   14104 C  CD1   . PHE D 2 113 ? 121.872 101.570 128.242 1.00 20.14 ?  92  PHE D CD1   1 
ATOM   14105 C  CD2   . PHE D 2 113 ? 123.557 101.451 129.958 1.00 20.77 ?  92  PHE D CD2   1 
ATOM   14106 C  CE1   . PHE D 2 113 ? 122.759 102.254 127.415 1.00 20.54 ?  92  PHE D CE1   1 
ATOM   14107 C  CE2   . PHE D 2 113 ? 124.453 102.129 129.133 1.00 21.23 ?  92  PHE D CE2   1 
ATOM   14108 C  CZ    . PHE D 2 113 ? 124.046 102.527 127.853 1.00 20.92 ?  92  PHE D CZ    1 
ATOM   14109 N  N     . MET D 2 114 ? 123.060 98.207  131.887 1.00 19.67 ?  93  MET D N     1 
ATOM   14110 C  CA    . MET D 2 114 ? 124.325 97.668  132.371 1.00 20.55 ?  93  MET D CA    1 
ATOM   14111 C  C     . MET D 2 114 ? 124.592 96.256  131.848 1.00 20.82 ?  93  MET D C     1 
ATOM   14112 O  O     . MET D 2 114 ? 125.713 95.975  131.446 1.00 20.43 ?  93  MET D O     1 
ATOM   14113 C  CB    . MET D 2 114 ? 124.387 97.702  133.893 1.00 20.24 ?  93  MET D CB    1 
ATOM   14114 C  CG    . MET D 2 114 ? 124.196 99.109  134.422 1.00 22.05 ?  93  MET D CG    1 
ATOM   14115 S  SD    . MET D 2 114 ? 124.059 99.219  136.191 1.00 25.85 ?  93  MET D SD    1 
ATOM   14116 C  CE    . MET D 2 114 ? 124.569 100.930 136.421 1.00 27.57 ?  93  MET D CE    1 
ATOM   14117 N  N     . ALA D 2 115 ? 123.570 95.388  131.853 1.00 21.19 ?  94  ALA D N     1 
ATOM   14118 C  CA    . ALA D 2 115 ? 123.704 94.027  131.297 1.00 21.53 ?  94  ALA D CA    1 
ATOM   14119 C  C     . ALA D 2 115 ? 124.067 94.081  129.814 1.00 21.75 ?  94  ALA D C     1 
ATOM   14120 O  O     . ALA D 2 115 ? 124.942 93.340  129.365 1.00 22.18 ?  94  ALA D O     1 
ATOM   14121 C  CB    . ALA D 2 115 ? 122.429 93.205  131.515 1.00 21.32 ?  94  ALA D CB    1 
ATOM   14122 N  N     . MET D 2 116 ? 123.417 94.978  129.068 1.00 21.47 ?  95  MET D N     1 
ATOM   14123 C  CA    . MET D 2 116 ? 123.743 95.199  127.662 1.00 21.83 ?  95  MET D CA    1 
ATOM   14124 C  C     . MET D 2 116 ? 125.232 95.544  127.467 1.00 22.15 ?  95  MET D C     1 
ATOM   14125 O  O     . MET D 2 116 ? 125.888 94.979  126.594 1.00 22.09 ?  95  MET D O     1 
ATOM   14126 C  CB    . MET D 2 116 ? 122.841 96.292  127.064 1.00 21.72 ?  95  MET D CB    1 
ATOM   14127 C  CG    . MET D 2 116 ? 123.165 96.680  125.612 1.00 22.57 ?  95  MET D CG    1 
ATOM   14128 S  SD    . MET D 2 116 ? 124.580 97.796  125.427 1.00 22.75 ?  95  MET D SD    1 
ATOM   14129 C  CE    . MET D 2 116 ? 123.964 99.294  126.193 1.00 22.96 ?  95  MET D CE    1 
ATOM   14130 N  N     . MET D 2 117 ? 125.751 96.467  128.279 1.00 22.04 ?  96  MET D N     1 
ATOM   14131 C  CA    . MET D 2 117 ? 127.163 96.876  128.184 1.00 22.45 ?  96  MET D CA    1 
ATOM   14132 C  C     . MET D 2 117 ? 128.116 95.689  128.404 1.00 22.39 ?  96  MET D C     1 
ATOM   14133 O  O     . MET D 2 117 ? 129.124 95.559  127.707 1.00 21.88 ?  96  MET D O     1 
ATOM   14134 C  CB    . MET D 2 117 ? 127.478 98.027  129.162 1.00 22.00 ?  96  MET D CB    1 
ATOM   14135 C  CG    . MET D 2 117 ? 126.859 99.387  128.747 1.00 23.25 ?  96  MET D CG    1 
ATOM   14136 S  SD    . MET D 2 117 ? 127.385 99.962  127.115 1.00 24.28 ?  96  MET D SD    1 
ATOM   14137 C  CE    . MET D 2 117 ? 129.076 100.454 127.432 1.00 24.59 ?  96  MET D CE    1 
ATOM   14138 N  N     . GLU D 2 118 ? 127.780 94.816  129.353 1.00 22.66 ?  97  GLU D N     1 
ATOM   14139 C  CA    . GLU D 2 118 ? 128.587 93.615  129.605 1.00 23.52 ?  97  GLU D CA    1 
ATOM   14140 C  C     . GLU D 2 118 ? 128.650 92.718  128.381 1.00 24.25 ?  97  GLU D C     1 
ATOM   14141 O  O     . GLU D 2 118 ? 129.740 92.330  127.955 1.00 25.05 ?  97  GLU D O     1 
ATOM   14142 C  CB    . GLU D 2 118 ? 128.071 92.798  130.812 1.00 23.11 ?  97  GLU D CB    1 
ATOM   14143 C  CG    . GLU D 2 118 ? 127.693 93.597  132.065 1.00 23.08 ?  97  GLU D CG    1 
ATOM   14144 C  CD    . GLU D 2 118 ? 128.871 94.227  132.790 1.00 24.08 ?  97  GLU D CD    1 
ATOM   14145 O  OE1   . GLU D 2 118 ? 129.959 94.327  132.202 1.00 26.39 ?  97  GLU D OE1   1 
ATOM   14146 O  OE2   . GLU D 2 118 ? 128.702 94.652  133.952 1.00 27.52 -1 97  GLU D OE2   1 
ATOM   14147 N  N     . ASN D 2 119 ? 127.485 92.415  127.813 1.00 25.47 ?  98  ASN D N     1 
ATOM   14148 C  CA    . ASN D 2 119 ? 127.342 91.404  126.746 1.00 26.32 ?  98  ASN D CA    1 
ATOM   14149 C  C     . ASN D 2 119 ? 127.632 91.904  125.334 1.00 26.22 ?  98  ASN D C     1 
ATOM   14150 O  O     . ASN D 2 119 ? 128.208 91.170  124.504 1.00 26.54 ?  98  ASN D O     1 
ATOM   14151 C  CB    . ASN D 2 119 ? 125.933 90.785  126.781 1.00 26.72 ?  98  ASN D CB    1 
ATOM   14152 C  CG    . ASN D 2 119 ? 125.681 89.981  128.057 1.00 29.12 ?  98  ASN D CG    1 
ATOM   14153 O  OD1   . ASN D 2 119 ? 126.453 89.081  128.403 1.00 32.07 ?  98  ASN D OD1   1 
ATOM   14154 N  ND2   . ASN D 2 119 ? 124.616 90.326  128.773 1.00 29.12 ?  98  ASN D ND2   1 
ATOM   14155 N  N     . ALA D 2 120 ? 127.210 93.134  125.061 1.00 25.46 ?  99  ALA D N     1 
ATOM   14156 C  CA    . ALA D 2 120 ? 127.303 93.704  123.718 1.00 25.77 ?  99  ALA D CA    1 
ATOM   14157 C  C     . ALA D 2 120 ? 128.561 94.538  123.499 1.00 25.51 ?  99  ALA D C     1 
ATOM   14158 O  O     . ALA D 2 120 ? 129.032 94.658  122.364 1.00 26.64 ?  99  ALA D O     1 
ATOM   14159 C  CB    . ALA D 2 120 ? 126.052 94.539  123.397 1.00 25.75 ?  99  ALA D CB    1 
ATOM   14160 N  N     . VAL D 2 121 ? 129.099 95.120  124.565 1.00 24.40 ?  100 VAL D N     1 
ATOM   14161 C  CA    . VAL D 2 121 ? 130.208 96.056  124.417 1.00 24.15 ?  100 VAL D CA    1 
ATOM   14162 C  C     . VAL D 2 121 ? 131.501 95.505  125.025 1.00 23.94 ?  100 VAL D C     1 
ATOM   14163 O  O     . VAL D 2 121 ? 132.499 95.332  124.319 1.00 23.75 ?  100 VAL D O     1 
ATOM   14164 C  CB    . VAL D 2 121 ? 129.857 97.464  124.989 1.00 23.68 ?  100 VAL D CB    1 
ATOM   14165 C  CG1   . VAL D 2 121 ? 131.018 98.436  124.786 1.00 23.76 ?  100 VAL D CG1   1 
ATOM   14166 C  CG2   . VAL D 2 121 ? 128.596 98.007  124.310 1.00 23.99 ?  100 VAL D CG2   1 
ATOM   14167 N  N     . HIS D 2 122 ? 131.474 95.228  126.327 1.00 23.68 ?  101 HIS D N     1 
ATOM   14168 C  CA    . HIS D 2 122 ? 132.653 94.717  127.028 1.00 24.02 ?  101 HIS D CA    1 
ATOM   14169 C  C     . HIS D 2 122 ? 133.149 93.393  126.469 1.00 24.39 ?  101 HIS D C     1 
ATOM   14170 O  O     . HIS D 2 122 ? 134.344 93.244  126.228 1.00 24.71 ?  101 HIS D O     1 
ATOM   14171 C  CB    . HIS D 2 122 ? 132.414 94.597  128.539 1.00 23.20 ?  101 HIS D CB    1 
ATOM   14172 C  CG    . HIS D 2 122 ? 132.163 95.907  129.218 1.00 22.82 ?  101 HIS D CG    1 
ATOM   14173 N  ND1   . HIS D 2 122 ? 131.866 96.001  130.560 1.00 20.48 ?  101 HIS D ND1   1 
ATOM   14174 C  CD2   . HIS D 2 122 ? 132.138 97.175  128.738 1.00 21.03 ?  101 HIS D CD2   1 
ATOM   14175 C  CE1   . HIS D 2 122 ? 131.684 97.269  130.881 1.00 19.88 ?  101 HIS D CE1   1 
ATOM   14176 N  NE2   . HIS D 2 122 ? 131.845 98.003  129.793 1.00 21.62 ?  101 HIS D NE2   1 
ATOM   14177 N  N     . ALA D 2 123 ? 132.241 92.441  126.254 1.00 25.30 ?  102 ALA D N     1 
ATOM   14178 C  CA    . ALA D 2 123 ? 132.647 91.106  125.790 1.00 25.77 ?  102 ALA D CA    1 
ATOM   14179 C  C     . ALA D 2 123 ? 133.288 91.144  124.399 1.00 26.37 ?  102 ALA D C     1 
ATOM   14180 O  O     . ALA D 2 123 ? 134.271 90.440  124.136 1.00 25.87 ?  102 ALA D O     1 
ATOM   14181 C  CB    . ALA D 2 123 ? 131.462 90.131  125.819 1.00 26.43 ?  102 ALA D CB    1 
ATOM   14182 N  N     . LYS D 2 124 ? 132.727 91.971  123.516 1.00 26.51 ?  103 LYS D N     1 
ATOM   14183 C  CA    . LYS D 2 124 ? 133.268 92.149  122.176 1.00 27.22 ?  103 LYS D CA    1 
ATOM   14184 C  C     . LYS D 2 124 ? 134.633 92.850  122.234 1.00 26.63 ?  103 LYS D C     1 
ATOM   14185 O  O     . LYS D 2 124 ? 135.527 92.529  121.450 1.00 26.07 ?  103 LYS D O     1 
ATOM   14186 C  CB    . LYS D 2 124 ? 132.277 92.929  121.289 1.00 27.51 ?  103 LYS D CB    1 
ATOM   14187 C  CG    . LYS D 2 124 ? 132.776 93.259  119.866 1.00 30.58 ?  103 LYS D CG    1 
ATOM   14188 C  CD    . LYS D 2 124 ? 132.937 92.014  119.006 1.00 35.72 ?  103 LYS D CD    1 
ATOM   14189 C  CE    . LYS D 2 124 ? 133.462 92.339  117.606 1.00 37.33 ?  103 LYS D CE    1 
ATOM   14190 N  NZ    . LYS D 2 124 ? 132.464 93.135  116.843 1.00 40.73 1  103 LYS D NZ    1 
ATOM   14191 N  N     . SER D 2 125 ? 134.781 93.785  123.177 1.00 26.02 ?  104 SER D N     1 
ATOM   14192 C  CA    . SER D 2 125 ? 136.022 94.543  123.354 1.00 26.16 ?  104 SER D CA    1 
ATOM   14193 C  C     . SER D 2 125 ? 137.185 93.657  123.799 1.00 26.18 ?  104 SER D C     1 
ATOM   14194 O  O     . SER D 2 125 ? 138.301 93.788  123.282 1.00 26.06 ?  104 SER D O     1 
ATOM   14195 C  CB    . SER D 2 125 ? 135.830 95.690  124.349 1.00 26.10 ?  104 SER D CB    1 
ATOM   14196 O  OG    . SER D 2 125 ? 134.921 96.643  123.829 1.00 26.58 ?  104 SER D OG    1 
ATOM   14197 N  N     . TYR D 2 126 ? 136.918 92.765  124.751 1.00 25.68 ?  105 TYR D N     1 
ATOM   14198 C  CA    . TYR D 2 126 ? 137.926 91.809  125.226 1.00 26.12 ?  105 TYR D CA    1 
ATOM   14199 C  C     . TYR D 2 126 ? 138.337 90.854  124.101 1.00 26.38 ?  105 TYR D C     1 
ATOM   14200 O  O     . TYR D 2 126 ? 139.524 90.581  123.906 1.00 26.83 ?  105 TYR D O     1 
ATOM   14201 C  CB    . TYR D 2 126 ? 137.412 91.003  126.434 1.00 25.35 ?  105 TYR D CB    1 
ATOM   14202 C  CG    . TYR D 2 126 ? 137.449 91.736  127.762 1.00 25.46 ?  105 TYR D CG    1 
ATOM   14203 C  CD1   . TYR D 2 126 ? 138.638 92.288  128.240 1.00 25.41 ?  105 TYR D CD1   1 
ATOM   14204 C  CD2   . TYR D 2 126 ? 136.301 91.849  128.561 1.00 24.77 ?  105 TYR D CD2   1 
ATOM   14205 C  CE1   . TYR D 2 126 ? 138.686 92.960  129.459 1.00 25.89 ?  105 TYR D CE1   1 
ATOM   14206 C  CE2   . TYR D 2 126 ? 136.340 92.524  129.791 1.00 23.11 ?  105 TYR D CE2   1 
ATOM   14207 C  CZ    . TYR D 2 126 ? 137.539 93.062  130.237 1.00 25.38 ?  105 TYR D CZ    1 
ATOM   14208 O  OH    . TYR D 2 126 ? 137.615 93.730  131.440 1.00 23.31 ?  105 TYR D OH    1 
ATOM   14209 N  N     . SER D 2 127 ? 137.352 90.367  123.354 1.00 27.16 ?  106 SER D N     1 
ATOM   14210 C  CA    . SER D 2 127 ? 137.605 89.483  122.211 1.00 27.83 ?  106 SER D CA    1 
ATOM   14211 C  C     . SER D 2 127 ? 138.495 90.171  121.166 1.00 28.21 ?  106 SER D C     1 
ATOM   14212 O  O     . SER D 2 127 ? 139.478 89.579  120.701 1.00 28.30 ?  106 SER D O     1 
ATOM   14213 C  CB    . SER D 2 127 ? 136.279 89.010  121.593 1.00 28.37 ?  106 SER D CB    1 
ATOM   14214 O  OG    . SER D 2 127 ? 136.498 88.239  120.413 1.00 29.33 ?  106 SER D OG    1 
ATOM   14215 N  N     . ASN D 2 128 ? 138.148 91.413  120.816 1.00 28.27 ?  107 ASN D N     1 
ATOM   14216 C  CA    . ASN D 2 128 ? 138.938 92.249  119.898 1.00 28.79 ?  107 ASN D CA    1 
ATOM   14217 C  C     . ASN D 2 128 ? 140.393 92.426  120.321 1.00 28.53 ?  107 ASN D C     1 
ATOM   14218 O  O     . ASN D 2 128 ? 141.298 92.316  119.487 1.00 28.03 ?  107 ASN D O     1 
ATOM   14219 C  CB    . ASN D 2 128 ? 138.299 93.636  119.701 1.00 29.05 ?  107 ASN D CB    1 
ATOM   14220 C  CG    . ASN D 2 128 ? 136.996 93.583  118.897 1.00 30.48 ?  107 ASN D CG    1 
ATOM   14221 O  OD1   . ASN D 2 128 ? 136.653 92.558  118.313 1.00 32.19 ?  107 ASN D OD1   1 
ATOM   14222 N  ND2   . ASN D 2 128 ? 136.262 94.691  118.886 1.00 31.59 ?  107 ASN D ND2   1 
ATOM   14223 N  N     . ILE D 2 129 ? 140.617 92.726  121.603 1.00 28.21 ?  108 ILE D N     1 
ATOM   14224 C  CA    . ILE D 2 129 ? 141.986 92.839  122.124 1.00 28.76 ?  108 ILE D CA    1 
ATOM   14225 C  C     . ILE D 2 129 ? 142.757 91.523  121.929 1.00 29.83 ?  108 ILE D C     1 
ATOM   14226 O  O     . ILE D 2 129 ? 143.889 91.523  121.425 1.00 29.99 ?  108 ILE D O     1 
ATOM   14227 C  CB    . ILE D 2 129 ? 142.028 93.298  123.618 1.00 28.28 ?  108 ILE D CB    1 
ATOM   14228 C  CG1   . ILE D 2 129 ? 141.441 94.708  123.774 1.00 27.94 ?  108 ILE D CG1   1 
ATOM   14229 C  CG2   . ILE D 2 129 ? 143.469 93.276  124.148 1.00 27.52 ?  108 ILE D CG2   1 
ATOM   14230 C  CD1   . ILE D 2 129 ? 141.106 95.090  125.211 1.00 27.98 ?  108 ILE D CD1   1 
ATOM   14231 N  N     . PHE D 2 130 ? 142.145 90.408  122.320 1.00 30.86 ?  109 PHE D N     1 
ATOM   14232 C  CA    . PHE D 2 130 ? 142.762 89.095  122.153 1.00 32.76 ?  109 PHE D CA    1 
ATOM   14233 C  C     . PHE D 2 130 ? 143.137 88.782  120.701 1.00 34.37 ?  109 PHE D C     1 
ATOM   14234 O  O     . PHE D 2 130 ? 144.280 88.433  120.420 1.00 34.61 ?  109 PHE D O     1 
ATOM   14235 C  CB    . PHE D 2 130 ? 141.858 87.994  122.700 1.00 32.81 ?  109 PHE D CB    1 
ATOM   14236 C  CG    . PHE D 2 130 ? 142.182 87.584  124.108 1.00 33.84 ?  109 PHE D CG    1 
ATOM   14237 C  CD1   . PHE D 2 130 ? 143.371 86.919  124.396 1.00 34.61 ?  109 PHE D CD1   1 
ATOM   14238 C  CD2   . PHE D 2 130 ? 141.284 87.832  125.139 1.00 35.74 ?  109 PHE D CD2   1 
ATOM   14239 C  CE1   . PHE D 2 130 ? 143.675 86.524  125.699 1.00 36.99 ?  109 PHE D CE1   1 
ATOM   14240 C  CE2   . PHE D 2 130 ? 141.574 87.441  126.452 1.00 36.96 ?  109 PHE D CE2   1 
ATOM   14241 C  CZ    . PHE D 2 130 ? 142.771 86.786  126.734 1.00 36.91 ?  109 PHE D CZ    1 
ATOM   14242 N  N     . MET D 2 131 ? 142.169 88.926  119.794 1.00 35.90 ?  110 MET D N     1 
ATOM   14243 C  CA    . MET D 2 131 ? 142.359 88.625  118.374 1.00 37.94 ?  110 MET D CA    1 
ATOM   14244 C  C     . MET D 2 131 ? 143.451 89.477  117.741 1.00 38.05 ?  110 MET D C     1 
ATOM   14245 O  O     . MET D 2 131 ? 144.091 89.047  116.788 1.00 38.20 ?  110 MET D O     1 
ATOM   14246 C  CB    . MET D 2 131 ? 141.047 88.789  117.589 1.00 38.63 ?  110 MET D CB    1 
ATOM   14247 C  CG    . MET D 2 131 ? 139.964 87.750  117.925 1.00 42.34 ?  110 MET D CG    1 
ATOM   14248 S  SD    . MET D 2 131 ? 138.413 87.941  116.985 1.00 50.15 ?  110 MET D SD    1 
ATOM   14249 C  CE    . MET D 2 131 ? 137.721 89.458  117.657 1.00 48.14 ?  110 MET D CE    1 
ATOM   14250 N  N     . THR D 2 132 ? 143.657 90.680  118.275 1.00 38.12 ?  111 THR D N     1 
ATOM   14251 C  CA    . THR D 2 132 ? 144.707 91.571  117.780 1.00 38.79 ?  111 THR D CA    1 
ATOM   14252 C  C     . THR D 2 132 ? 146.113 91.109  118.207 1.00 38.81 ?  111 THR D C     1 
ATOM   14253 O  O     . THR D 2 132 ? 147.046 91.137  117.398 1.00 39.26 ?  111 THR D O     1 
ATOM   14254 C  CB    . THR D 2 132 ? 144.460 93.027  118.223 1.00 38.78 ?  111 THR D CB    1 
ATOM   14255 O  OG1   . THR D 2 132 ? 143.170 93.449  117.766 1.00 39.32 ?  111 THR D OG1   1 
ATOM   14256 C  CG2   . THR D 2 132 ? 145.509 93.966  117.635 1.00 39.75 ?  111 THR D CG2   1 
ATOM   14257 N  N     . LEU D 2 133 ? 146.245 90.676  119.461 1.00 38.34 ?  112 LEU D N     1 
ATOM   14258 C  CA    . LEU D 2 133 ? 147.546 90.377  120.067 1.00 38.36 ?  112 LEU D CA    1 
ATOM   14259 C  C     . LEU D 2 133 ? 148.021 88.931  119.917 1.00 38.94 ?  112 LEU D C     1 
ATOM   14260 O  O     . LEU D 2 133 ? 149.223 88.679  119.851 1.00 39.14 ?  112 LEU D O     1 
ATOM   14261 C  CB    . LEU D 2 133 ? 147.544 90.752  121.559 1.00 37.62 ?  112 LEU D CB    1 
ATOM   14262 C  CG    . LEU D 2 133 ? 147.160 92.181  121.953 1.00 36.50 ?  112 LEU D CG    1 
ATOM   14263 C  CD1   . LEU D 2 133 ? 146.976 92.285  123.470 1.00 35.80 ?  112 LEU D CD1   1 
ATOM   14264 C  CD2   . LEU D 2 133 ? 148.164 93.206  121.454 1.00 35.32 ?  112 LEU D CD2   1 
ATOM   14265 N  N     . ALA D 2 134 ? 147.097 87.980  119.879 1.00 39.41 ?  113 ALA D N     1 
ATOM   14266 C  CA    . ALA D 2 134 ? 147.497 86.570  119.805 1.00 40.33 ?  113 ALA D CA    1 
ATOM   14267 C  C     . ALA D 2 134 ? 146.857 85.837  118.630 1.00 41.05 ?  113 ALA D C     1 
ATOM   14268 O  O     . ALA D 2 134 ? 145.756 86.188  118.220 1.00 40.81 ?  113 ALA D O     1 
ATOM   14269 C  CB    . ALA D 2 134 ? 147.176 85.866  121.110 1.00 40.15 ?  113 ALA D CB    1 
ATOM   14270 N  N     . PRO D 2 135 ? 147.552 84.821  118.074 1.00 42.21 ?  114 PRO D N     1 
ATOM   14271 C  CA    . PRO D 2 135 ? 146.894 83.973  117.072 1.00 43.27 ?  114 PRO D CA    1 
ATOM   14272 C  C     . PRO D 2 135 ? 145.852 83.052  117.724 1.00 43.89 ?  114 PRO D C     1 
ATOM   14273 O  O     . PRO D 2 135 ? 145.911 82.812  118.933 1.00 43.31 ?  114 PRO D O     1 
ATOM   14274 C  CB    . PRO D 2 135 ? 148.047 83.155  116.486 1.00 43.69 ?  114 PRO D CB    1 
ATOM   14275 C  CG    . PRO D 2 135 ? 149.059 83.107  117.566 1.00 43.01 ?  114 PRO D CG    1 
ATOM   14276 C  CD    . PRO D 2 135 ? 148.949 84.408  118.311 1.00 42.16 ?  114 PRO D CD    1 
ATOM   14277 N  N     . THR D 2 136 ? 144.921 82.541  116.918 1.00 45.26 ?  115 THR D N     1 
ATOM   14278 C  CA    . THR D 2 136 ? 143.783 81.746  117.407 1.00 46.11 ?  115 THR D CA    1 
ATOM   14279 C  C     . THR D 2 136 ? 144.190 80.624  118.367 1.00 46.35 ?  115 THR D C     1 
ATOM   14280 O  O     . THR D 2 136 ? 143.576 80.463  119.427 1.00 46.25 ?  115 THR D O     1 
ATOM   14281 C  CB    . THR D 2 136 ? 142.927 81.184  116.239 1.00 46.59 ?  115 THR D CB    1 
ATOM   14282 O  OG1   . THR D 2 136 ? 142.544 82.258  115.373 1.00 47.80 ?  115 THR D OG1   1 
ATOM   14283 C  CG2   . THR D 2 136 ? 141.653 80.514  116.751 1.00 46.94 ?  115 THR D CG2   1 
ATOM   14284 N  N     . GLU D 2 137 ? 145.230 79.872  118.008 1.00 46.92 ?  116 GLU D N     1 
ATOM   14285 C  CA    . GLU D 2 137 ? 145.687 78.750  118.828 1.00 47.37 ?  116 GLU D CA    1 
ATOM   14286 C  C     . GLU D 2 137 ? 146.174 79.180  120.215 1.00 46.64 ?  116 GLU D C     1 
ATOM   14287 O  O     . GLU D 2 137 ? 145.920 78.483  121.199 1.00 46.89 ?  116 GLU D O     1 
ATOM   14288 C  CB    . GLU D 2 137 ? 146.763 77.929  118.102 1.00 48.04 ?  116 GLU D CB    1 
ATOM   14289 C  CG    . GLU D 2 137 ? 147.211 76.654  118.841 1.00 49.86 ?  116 GLU D CG    1 
ATOM   14290 C  CD    . GLU D 2 137 ? 146.155 75.538  118.867 1.00 52.40 ?  116 GLU D CD    1 
ATOM   14291 O  OE1   . GLU D 2 137 ? 145.004 75.788  119.290 1.00 52.97 ?  116 GLU D OE1   1 
ATOM   14292 O  OE2   . GLU D 2 137 ? 146.490 74.393  118.483 1.00 54.12 -1 116 GLU D OE2   1 
ATOM   14293 N  N     . THR D 2 138 ? 146.861 80.319  120.283 1.00 46.09 ?  117 THR D N     1 
ATOM   14294 C  CA    . THR D 2 138 ? 147.338 80.880  121.556 1.00 45.30 ?  117 THR D CA    1 
ATOM   14295 C  C     . THR D 2 138 ? 146.179 81.328  122.457 1.00 44.63 ?  117 THR D C     1 
ATOM   14296 O  O     . THR D 2 138 ? 146.215 81.119  123.673 1.00 44.51 ?  117 THR D O     1 
ATOM   14297 C  CB    . THR D 2 138 ? 148.314 82.059  121.325 1.00 45.20 ?  117 THR D CB    1 
ATOM   14298 O  OG1   . THR D 2 138 ? 149.407 81.619  120.512 1.00 45.69 ?  117 THR D OG1   1 
ATOM   14299 C  CG2   . THR D 2 138 ? 148.867 82.594  122.645 1.00 44.67 ?  117 THR D CG2   1 
ATOM   14300 N  N     . ILE D 2 139 ? 145.155 81.935  121.856 1.00 44.24 ?  118 ILE D N     1 
ATOM   14301 C  CA    . ILE D 2 139 ? 143.963 82.355  122.597 1.00 43.65 ?  118 ILE D CA    1 
ATOM   14302 C  C     . ILE D 2 139 ? 143.267 81.145  123.238 1.00 43.87 ?  118 ILE D C     1 
ATOM   14303 O  O     . ILE D 2 139 ? 142.966 81.156  124.434 1.00 43.36 ?  118 ILE D O     1 
ATOM   14304 C  CB    . ILE D 2 139 ? 142.994 83.172  121.703 1.00 43.68 ?  118 ILE D CB    1 
ATOM   14305 C  CG1   . ILE D 2 139 ? 143.636 84.515  121.321 1.00 43.30 ?  118 ILE D CG1   1 
ATOM   14306 C  CG2   . ILE D 2 139 ? 141.642 83.396  122.406 1.00 43.11 ?  118 ILE D CG2   1 
ATOM   14307 C  CD1   . ILE D 2 139 ? 142.981 85.232  120.147 1.00 43.41 ?  118 ILE D CD1   1 
ATOM   14308 N  N     . ASN D 2 140 ? 143.048 80.098  122.443 1.00 44.52 ?  119 ASN D N     1 
ATOM   14309 C  CA    . ASN D 2 140 ? 142.423 78.864  122.931 1.00 45.00 ?  119 ASN D CA    1 
ATOM   14310 C  C     . ASN D 2 140 ? 143.187 78.221  124.107 1.00 44.99 ?  119 ASN D C     1 
ATOM   14311 O  O     . ASN D 2 140 ? 142.571 77.748  125.071 1.00 44.61 ?  119 ASN D O     1 
ATOM   14312 C  CB    . ASN D 2 140 ? 142.225 77.860  121.782 1.00 45.74 ?  119 ASN D CB    1 
ATOM   14313 C  CG    . ASN D 2 140 ? 141.306 78.390  120.675 1.00 46.40 ?  119 ASN D CG    1 
ATOM   14314 O  OD1   . ASN D 2 140 ? 140.582 79.376  120.854 1.00 46.85 ?  119 ASN D OD1   1 
ATOM   14315 N  ND2   . ASN D 2 140 ? 141.329 77.721  119.524 1.00 48.16 ?  119 ASN D ND2   1 
ATOM   14316 N  N     . GLU D 2 141 ? 144.520 78.234  124.037 1.00 45.09 ?  120 GLU D N     1 
ATOM   14317 C  CA    . GLU D 2 141 ? 145.362 77.665  125.094 1.00 45.27 ?  120 GLU D CA    1 
ATOM   14318 C  C     . GLU D 2 141 ? 145.343 78.475  126.398 1.00 44.75 ?  120 GLU D C     1 
ATOM   14319 O  O     . GLU D 2 141 ? 145.279 77.901  127.491 1.00 44.37 ?  120 GLU D O     1 
ATOM   14320 C  CB    . GLU D 2 141 ? 146.800 77.479  124.609 1.00 45.75 ?  120 GLU D CB    1 
ATOM   14321 C  CG    . GLU D 2 141 ? 146.963 76.394  123.543 1.00 48.17 ?  120 GLU D CG    1 
ATOM   14322 C  CD    . GLU D 2 141 ? 148.403 76.185  123.120 1.00 50.15 ?  120 GLU D CD    1 
ATOM   14323 O  OE1   . GLU D 2 141 ? 149.275 76.026  124.000 1.00 50.90 ?  120 GLU D OE1   1 
ATOM   14324 O  OE2   . GLU D 2 141 ? 148.663 76.174  121.899 1.00 52.25 -1 120 GLU D OE2   1 
ATOM   14325 N  N     . VAL D 2 142 ? 145.417 79.800  126.276 1.00 44.31 ?  121 VAL D N     1 
ATOM   14326 C  CA    . VAL D 2 142 ? 145.341 80.695  127.433 1.00 43.91 ?  121 VAL D CA    1 
ATOM   14327 C  C     . VAL D 2 142 ? 144.006 80.519  128.164 1.00 43.71 ?  121 VAL D C     1 
ATOM   14328 O  O     . VAL D 2 142 ? 143.971 80.451  129.392 1.00 43.44 ?  121 VAL D O     1 
ATOM   14329 C  CB    . VAL D 2 142 ? 145.553 82.182  127.035 1.00 43.65 ?  121 VAL D CB    1 
ATOM   14330 C  CG1   . VAL D 2 142 ? 145.340 83.104  128.235 1.00 43.40 ?  121 VAL D CG1   1 
ATOM   14331 C  CG2   . VAL D 2 142 ? 146.955 82.386  126.468 1.00 43.96 ?  121 VAL D CG2   1 
ATOM   14332 N  N     . PHE D 2 143 ? 142.917 80.431  127.405 1.00 44.03 ?  122 PHE D N     1 
ATOM   14333 C  CA    . PHE D 2 143 ? 141.601 80.231  128.002 1.00 44.42 ?  122 PHE D CA    1 
ATOM   14334 C  C     . PHE D 2 143 ? 141.441 78.855  128.637 1.00 45.38 ?  122 PHE D C     1 
ATOM   14335 O  O     . PHE D 2 143 ? 140.796 78.730  129.675 1.00 45.50 ?  122 PHE D O     1 
ATOM   14336 C  CB    . PHE D 2 143 ? 140.476 80.543  127.012 1.00 44.27 ?  122 PHE D CB    1 
ATOM   14337 C  CG    . PHE D 2 143 ? 140.092 81.991  127.002 1.00 43.28 ?  122 PHE D CG    1 
ATOM   14338 C  CD1   . PHE D 2 143 ? 139.223 82.499  127.966 1.00 42.17 ?  122 PHE D CD1   1 
ATOM   14339 C  CD2   . PHE D 2 143 ? 140.623 82.858  126.056 1.00 42.76 ?  122 PHE D CD2   1 
ATOM   14340 C  CE1   . PHE D 2 143 ? 138.874 83.844  127.978 1.00 42.16 ?  122 PHE D CE1   1 
ATOM   14341 C  CE2   . PHE D 2 143 ? 140.282 84.206  126.058 1.00 42.77 ?  122 PHE D CE2   1 
ATOM   14342 C  CZ    . PHE D 2 143 ? 139.404 84.702  127.022 1.00 42.28 ?  122 PHE D CZ    1 
ATOM   14343 N  N     . GLU D 2 144 ? 142.046 77.837  128.029 1.00 46.18 ?  123 GLU D N     1 
ATOM   14344 C  CA    . GLU D 2 144 ? 142.118 76.509  128.638 1.00 47.19 ?  123 GLU D CA    1 
ATOM   14345 C  C     . GLU D 2 144 ? 142.848 76.555  129.989 1.00 46.99 ?  123 GLU D C     1 
ATOM   14346 O  O     . GLU D 2 144 ? 142.373 75.963  130.964 1.00 46.94 ?  123 GLU D O     1 
ATOM   14347 C  CB    . GLU D 2 144 ? 142.801 75.519  127.685 1.00 47.80 ?  123 GLU D CB    1 
ATOM   14348 C  CG    . GLU D 2 144 ? 142.808 74.058  128.146 1.00 49.54 ?  123 GLU D CG    1 
ATOM   14349 C  CD    . GLU D 2 144 ? 143.604 73.140  127.213 1.00 52.37 ?  123 GLU D CD    1 
ATOM   14350 O  OE1   . GLU D 2 144 ? 144.735 73.505  126.814 1.00 52.92 ?  123 GLU D OE1   1 
ATOM   14351 O  OE2   . GLU D 2 144 ? 143.101 72.046  126.882 1.00 53.55 -1 123 GLU D OE2   1 
ATOM   14352 N  N     . TRP D 2 145 ? 143.985 77.259  130.036 1.00 47.02 ?  124 TRP D N     1 
ATOM   14353 C  CA    . TRP D 2 145 ? 144.797 77.401  131.258 1.00 46.93 ?  124 TRP D CA    1 
ATOM   14354 C  C     . TRP D 2 145 ? 144.044 78.156  132.343 1.00 46.55 ?  124 TRP D C     1 
ATOM   14355 O  O     . TRP D 2 145 ? 143.941 77.686  133.473 1.00 46.42 ?  124 TRP D O     1 
ATOM   14356 C  CB    . TRP D 2 145 ? 146.122 78.124  130.964 1.00 47.07 ?  124 TRP D CB    1 
ATOM   14357 C  CG    . TRP D 2 145 ? 147.124 78.142  132.122 1.00 47.82 ?  124 TRP D CG    1 
ATOM   14358 C  CD1   . TRP D 2 145 ? 148.134 77.243  132.346 1.00 48.78 ?  124 TRP D CD1   1 
ATOM   14359 C  CD2   . TRP D 2 145 ? 147.219 79.115  133.183 1.00 47.80 ?  124 TRP D CD2   1 
ATOM   14360 N  NE1   . TRP D 2 145 ? 148.842 77.587  133.476 1.00 49.06 ?  124 TRP D NE1   1 
ATOM   14361 C  CE2   . TRP D 2 145 ? 148.302 78.728  134.011 1.00 48.24 ?  124 TRP D CE2   1 
ATOM   14362 C  CE3   . TRP D 2 145 ? 146.493 80.267  133.517 1.00 47.65 ?  124 TRP D CE3   1 
ATOM   14363 C  CZ2   . TRP D 2 145 ? 148.674 79.455  135.154 1.00 47.74 ?  124 TRP D CZ2   1 
ATOM   14364 C  CZ3   . TRP D 2 145 ? 146.864 80.990  134.653 1.00 46.92 ?  124 TRP D CZ3   1 
ATOM   14365 C  CH2   . TRP D 2 145 ? 147.948 80.578  135.456 1.00 47.88 ?  124 TRP D CH2   1 
ATOM   14366 N  N     . VAL D 2 146 ? 143.521 79.328  131.995 1.00 46.09 ?  125 VAL D N     1 
ATOM   14367 C  CA    . VAL D 2 146 ? 142.838 80.178  132.964 1.00 45.36 ?  125 VAL D CA    1 
ATOM   14368 C  C     . VAL D 2 146 ? 141.532 79.516  133.435 1.00 45.28 ?  125 VAL D C     1 
ATOM   14369 O  O     . VAL D 2 146 ? 141.140 79.663  134.598 1.00 45.29 ?  125 VAL D O     1 
ATOM   14370 C  CB    . VAL D 2 146 ? 142.677 81.635  132.422 1.00 45.33 ?  125 VAL D CB    1 
ATOM   14371 C  CG1   . VAL D 2 146 ? 141.843 82.485  133.345 1.00 44.97 ?  125 VAL D CG1   1 
ATOM   14372 C  CG2   . VAL D 2 146 ? 144.053 82.284  132.256 1.00 44.52 ?  125 VAL D CG2   1 
ATOM   14373 N  N     . LYS D 2 147 ? 140.897 78.749  132.549 1.00 44.98 ?  126 LYS D N     1 
ATOM   14374 C  CA    . LYS D 2 147 ? 139.697 77.978  132.903 1.00 44.65 ?  126 LYS D CA    1 
ATOM   14375 C  C     . LYS D 2 147 ? 139.971 76.895  133.959 1.00 44.06 ?  126 LYS D C     1 
ATOM   14376 O  O     . LYS D 2 147 ? 139.086 76.546  134.742 1.00 44.65 ?  126 LYS D O     1 
ATOM   14377 C  CB    . LYS D 2 147 ? 139.068 77.334  131.664 1.00 45.31 ?  126 LYS D CB    1 
ATOM   14378 C  CG    . LYS D 2 147 ? 137.556 77.492  131.598 1.00 46.54 ?  126 LYS D CG    1 
ATOM   14379 C  CD    . LYS D 2 147 ? 136.846 76.214  131.147 1.00 49.06 ?  126 LYS D CD    1 
ATOM   14380 C  CE    . LYS D 2 147 ? 136.537 75.299  132.340 1.00 50.46 ?  126 LYS D CE    1 
ATOM   14381 N  NZ    . LYS D 2 147 ? 135.363 74.408  132.095 1.00 51.33 1  126 LYS D NZ    1 
ATOM   14382 N  N     . GLN D 2 148 ? 141.193 76.369  133.973 1.00 42.58 ?  127 GLN D N     1 
ATOM   14383 C  CA    . GLN D 2 148 ? 141.593 75.343  134.936 1.00 41.39 ?  127 GLN D CA    1 
ATOM   14384 C  C     . GLN D 2 148 ? 142.263 75.933  136.184 1.00 39.56 ?  127 GLN D C     1 
ATOM   14385 O  O     . GLN D 2 148 ? 142.396 75.248  137.197 1.00 39.77 ?  127 GLN D O     1 
ATOM   14386 C  CB    . GLN D 2 148 ? 142.493 74.302  134.242 1.00 42.11 ?  127 GLN D CB    1 
ATOM   14387 C  CG    . GLN D 2 148 ? 143.607 73.694  135.090 1.00 44.08 ?  127 GLN D CG    1 
ATOM   14388 C  CD    . GLN D 2 148 ? 144.968 74.361  134.877 1.00 46.12 ?  127 GLN D CD    1 
ATOM   14389 O  OE1   . GLN D 2 148 ? 145.075 75.590  134.777 1.00 46.47 ?  127 GLN D OE1   1 
ATOM   14390 N  NE2   . GLN D 2 148 ? 146.019 73.543  134.823 1.00 45.69 ?  127 GLN D NE2   1 
ATOM   14391 N  N     . ASN D 2 149 ? 142.670 77.202  136.104 1.00 36.99 ?  128 ASN D N     1 
ATOM   14392 C  CA    . ASN D 2 149 ? 143.381 77.871  137.193 1.00 34.54 ?  128 ASN D CA    1 
ATOM   14393 C  C     . ASN D 2 149 ? 142.599 77.932  138.508 1.00 33.13 ?  128 ASN D C     1 
ATOM   14394 O  O     . ASN D 2 149 ? 141.472 78.418  138.552 1.00 32.62 ?  128 ASN D O     1 
ATOM   14395 C  CB    . ASN D 2 149 ? 143.805 79.281  136.777 1.00 34.24 ?  128 ASN D CB    1 
ATOM   14396 C  CG    . ASN D 2 149 ? 144.647 79.963  137.837 1.00 33.83 ?  128 ASN D CG    1 
ATOM   14397 O  OD1   . ASN D 2 149 ? 144.148 80.785  138.608 1.00 32.21 ?  128 ASN D OD1   1 
ATOM   14398 N  ND2   . ASN D 2 149 ? 145.925 79.598  137.902 1.00 33.26 ?  128 ASN D ND2   1 
ATOM   14399 N  N     . LYS D 2 150 ? 143.232 77.462  139.580 1.00 31.49 ?  129 LYS D N     1 
ATOM   14400 C  CA    . LYS D 2 150 ? 142.595 77.327  140.888 1.00 30.68 ?  129 LYS D CA    1 
ATOM   14401 C  C     . LYS D 2 150 ? 142.086 78.657  141.494 1.00 28.95 ?  129 LYS D C     1 
ATOM   14402 O  O     . LYS D 2 150 ? 140.991 78.704  142.066 1.00 27.90 ?  129 LYS D O     1 
ATOM   14403 C  CB    . LYS D 2 150 ? 143.570 76.605  141.831 1.00 31.17 ?  129 LYS D CB    1 
ATOM   14404 C  CG    . LYS D 2 150 ? 143.276 76.661  143.316 1.00 33.66 ?  129 LYS D CG    1 
ATOM   14405 C  CD    . LYS D 2 150 ? 144.377 75.910  144.081 1.00 38.08 ?  129 LYS D CD    1 
ATOM   14406 C  CE    . LYS D 2 150 ? 144.531 76.416  145.520 1.00 40.20 ?  129 LYS D CE    1 
ATOM   14407 N  NZ    . LYS D 2 150 ? 143.698 75.649  146.486 1.00 42.60 1  129 LYS D NZ    1 
ATOM   14408 N  N     . TYR D 2 151 ? 142.876 79.722  141.371 1.00 27.36 ?  130 TYR D N     1 
ATOM   14409 C  CA    . TYR D 2 151 ? 142.536 81.005  142.014 1.00 26.56 ?  130 TYR D CA    1 
ATOM   14410 C  C     . TYR D 2 151 ? 141.470 81.771  141.245 1.00 25.66 ?  130 TYR D C     1 
ATOM   14411 O  O     . TYR D 2 151 ? 140.602 82.396  141.862 1.00 25.61 ?  130 TYR D O     1 
ATOM   14412 C  CB    . TYR D 2 151 ? 143.791 81.864  142.266 1.00 26.32 ?  130 TYR D CB    1 
ATOM   14413 C  CG    . TYR D 2 151 ? 144.922 81.049  142.862 1.00 27.20 ?  130 TYR D CG    1 
ATOM   14414 C  CD1   . TYR D 2 151 ? 144.843 80.575  144.172 1.00 27.31 ?  130 TYR D CD1   1 
ATOM   14415 C  CD2   . TYR D 2 151 ? 146.040 80.705  142.102 1.00 27.22 ?  130 TYR D CD2   1 
ATOM   14416 C  CE1   . TYR D 2 151 ? 145.860 79.797  144.720 1.00 29.65 ?  130 TYR D CE1   1 
ATOM   14417 C  CE2   . TYR D 2 151 ? 147.071 79.921  142.645 1.00 28.75 ?  130 TYR D CE2   1 
ATOM   14418 C  CZ    . TYR D 2 151 ? 146.964 79.482  143.968 1.00 29.17 ?  130 TYR D CZ    1 
ATOM   14419 O  OH    . TYR D 2 151 ? 147.951 78.713  144.542 1.00 30.61 ?  130 TYR D OH    1 
ATOM   14420 N  N     . LEU D 2 152 ? 141.537 81.719  139.913 1.00 24.87 ?  131 LEU D N     1 
ATOM   14421 C  CA    . LEU D 2 152 ? 140.485 82.297  139.083 1.00 24.37 ?  131 LEU D CA    1 
ATOM   14422 C  C     . LEU D 2 152 ? 139.159 81.563  139.319 1.00 24.18 ?  131 LEU D C     1 
ATOM   14423 O  O     . LEU D 2 152 ? 138.142 82.201  139.589 1.00 23.16 ?  131 LEU D O     1 
ATOM   14424 C  CB    . LEU D 2 152 ? 140.839 82.302  137.592 1.00 24.45 ?  131 LEU D CB    1 
ATOM   14425 C  CG    . LEU D 2 152 ? 139.655 82.983  136.882 1.00 26.33 ?  131 LEU D CG    1 
ATOM   14426 C  CD1   . LEU D 2 152 ? 139.673 84.499  137.118 1.00 25.00 ?  131 LEU D CD1   1 
ATOM   14427 C  CD2   . LEU D 2 152 ? 139.538 82.646  135.424 1.00 29.15 ?  131 LEU D CD2   1 
ATOM   14428 N  N     . GLN D 2 153 ? 139.185 80.231  139.247 1.00 24.07 ?  132 GLN D N     1 
ATOM   14429 C  CA    . GLN D 2 153 ? 137.974 79.429  139.523 1.00 24.99 ?  132 GLN D CA    1 
ATOM   14430 C  C     . GLN D 2 153 ? 137.387 79.664  140.912 1.00 24.24 ?  132 GLN D C     1 
ATOM   14431 O  O     . GLN D 2 153 ? 136.161 79.815  141.063 1.00 23.75 ?  132 GLN D O     1 
ATOM   14432 C  CB    . GLN D 2 153 ? 138.214 77.930  139.274 1.00 25.84 ?  132 GLN D CB    1 
ATOM   14433 C  CG    . GLN D 2 153 ? 138.362 77.566  137.773 1.00 28.48 ?  132 GLN D CG    1 
ATOM   14434 C  CD    . GLN D 2 153 ? 137.121 77.900  136.929 1.00 30.95 ?  132 GLN D CD    1 
ATOM   14435 O  OE1   . GLN D 2 153 ? 135.993 77.772  137.391 1.00 31.78 ?  132 GLN D OE1   1 
ATOM   14436 N  NE2   . GLN D 2 153 ? 137.337 78.317  135.680 1.00 32.81 ?  132 GLN D NE2   1 
ATOM   14437 N  N     . LYS D 2 154 ? 138.239 79.709  141.933 1.00 24.00 ?  133 LYS D N     1 
ATOM   14438 C  CA    . LYS D 2 154 ? 137.718 79.914  143.284 1.00 24.43 ?  133 LYS D CA    1 
ATOM   14439 C  C     . LYS D 2 154 ? 136.840 81.172  143.359 1.00 23.40 ?  133 LYS D C     1 
ATOM   14440 O  O     . LYS D 2 154 ? 135.690 81.106  143.799 1.00 22.68 ?  133 LYS D O     1 
ATOM   14441 C  CB    . LYS D 2 154 ? 138.822 79.987  144.344 1.00 24.64 ?  133 LYS D CB    1 
ATOM   14442 C  CG    . LYS D 2 154 ? 138.224 80.164  145.752 1.00 28.01 ?  133 LYS D CG    1 
ATOM   14443 C  CD    . LYS D 2 154 ? 139.233 80.070  146.872 1.00 32.56 ?  133 LYS D CD    1 
ATOM   14444 C  CE    . LYS D 2 154 ? 139.746 78.660  147.035 1.00 34.45 ?  133 LYS D CE    1 
ATOM   14445 N  NZ    . LYS D 2 154 ? 140.751 78.592  148.142 1.00 36.11 1  133 LYS D NZ    1 
ATOM   14446 N  N     . LYS D 2 155 ? 137.379 82.311  142.926 1.00 23.07 ?  134 LYS D N     1 
ATOM   14447 C  CA    . LYS D 2 155 ? 136.600 83.547  142.969 1.00 22.70 ?  134 LYS D CA    1 
ATOM   14448 C  C     . LYS D 2 155 ? 135.413 83.525  142.008 1.00 21.96 ?  134 LYS D C     1 
ATOM   14449 O  O     . LYS D 2 155 ? 134.324 83.944  142.387 1.00 22.25 ?  134 LYS D O     1 
ATOM   14450 C  CB    . LYS D 2 155 ? 137.474 84.802  142.791 1.00 22.70 ?  134 LYS D CB    1 
ATOM   14451 C  CG    . LYS D 2 155 ? 138.160 84.968  141.450 1.00 23.62 ?  134 LYS D CG    1 
ATOM   14452 C  CD    . LYS D 2 155 ? 138.911 86.298  141.433 1.00 25.32 ?  134 LYS D CD    1 
ATOM   14453 C  CE    . LYS D 2 155 ? 140.194 86.179  140.615 1.00 27.09 ?  134 LYS D CE    1 
ATOM   14454 N  NZ    . LYS D 2 155 ? 140.890 87.497  140.538 1.00 26.65 1  134 LYS D NZ    1 
ATOM   14455 N  N     . ALA D 2 156 ? 135.591 83.017  140.788 1.00 21.76 ?  135 ALA D N     1 
ATOM   14456 C  CA    . ALA D 2 156 ? 134.469 82.985  139.833 1.00 21.83 ?  135 ALA D CA    1 
ATOM   14457 C  C     . ALA D 2 156 ? 133.282 82.187  140.400 1.00 22.30 ?  135 ALA D C     1 
ATOM   14458 O  O     . ALA D 2 156 ? 132.137 82.647  140.357 1.00 21.92 ?  135 ALA D O     1 
ATOM   14459 C  CB    . ALA D 2 156 ? 134.905 82.415  138.472 1.00 22.30 ?  135 ALA D CB    1 
ATOM   14460 N  N     . GLN D 2 157 ? 133.562 81.008  140.957 1.00 22.15 ?  136 GLN D N     1 
ATOM   14461 C  CA    . GLN D 2 157 ? 132.494 80.155  141.490 1.00 22.38 ?  136 GLN D CA    1 
ATOM   14462 C  C     . GLN D 2 157 ? 131.879 80.676  142.796 1.00 21.59 ?  136 GLN D C     1 
ATOM   14463 O  O     . GLN D 2 157 ? 130.693 80.462  143.048 1.00 21.44 ?  136 GLN D O     1 
ATOM   14464 C  CB    . GLN D 2 157 ? 132.953 78.695  141.644 1.00 22.94 ?  136 GLN D CB    1 
ATOM   14465 C  CG    . GLN D 2 157 ? 133.448 78.029  140.350 1.00 25.31 ?  136 GLN D CG    1 
ATOM   14466 C  CD    . GLN D 2 157 ? 132.541 78.274  139.140 1.00 28.02 ?  136 GLN D CD    1 
ATOM   14467 O  OE1   . GLN D 2 157 ? 131.311 78.273  139.245 1.00 27.14 ?  136 GLN D OE1   1 
ATOM   14468 N  NE2   . GLN D 2 157 ? 133.160 78.475  137.979 1.00 29.47 ?  136 GLN D NE2   1 
ATOM   14469 N  N     . MET D 2 158 ? 132.672 81.346  143.624 1.00 21.52 ?  137 MET D N     1 
ATOM   14470 C  CA    . MET D 2 158 ? 132.133 81.984  144.838 1.00 22.20 ?  137 MET D CA    1 
ATOM   14471 C  C     . MET D 2 158 ? 131.064 83.032  144.505 1.00 21.84 ?  137 MET D C     1 
ATOM   14472 O  O     . MET D 2 158 ? 130.006 83.075  145.138 1.00 21.91 ?  137 MET D O     1 
ATOM   14473 C  CB    . MET D 2 158 ? 133.242 82.626  145.671 1.00 22.52 ?  137 MET D CB    1 
ATOM   14474 C  CG    . MET D 2 158 ? 134.065 81.620  146.489 1.00 25.81 ?  137 MET D CG    1 
ATOM   14475 S  SD    . MET D 2 158 ? 135.384 82.392  147.466 1.00 31.19 ?  137 MET D SD    1 
ATOM   14476 C  CE    . MET D 2 158 ? 134.374 83.377  148.540 1.00 23.91 ?  137 MET D CE    1 
ATOM   14477 N  N     . ILE D 2 159 ? 131.354 83.864  143.507 1.00 21.41 ?  138 ILE D N     1 
ATOM   14478 C  CA    . ILE D 2 159 ? 130.442 84.921  143.078 1.00 21.51 ?  138 ILE D CA    1 
ATOM   14479 C  C     . ILE D 2 159 ? 129.172 84.315  142.460 1.00 21.77 ?  138 ILE D C     1 
ATOM   14480 O  O     . ILE D 2 159 ? 128.050 84.690  142.836 1.00 21.44 ?  138 ILE D O     1 
ATOM   14481 C  CB    . ILE D 2 159 ? 131.173 85.921  142.101 1.00 21.49 ?  138 ILE D CB    1 
ATOM   14482 C  CG1   . ILE D 2 159 ? 132.345 86.627  142.801 1.00 21.16 ?  138 ILE D CG1   1 
ATOM   14483 C  CG2   . ILE D 2 159 ? 130.205 86.943  141.493 1.00 22.34 ?  138 ILE D CG2   1 
ATOM   14484 C  CD1   . ILE D 2 159 ? 131.952 87.509  144.005 1.00 23.85 ?  138 ILE D CD1   1 
ATOM   14485 N  N     . VAL D 2 160 ? 129.364 83.374  141.528 1.00 21.96 ?  139 VAL D N     1 
ATOM   14486 C  CA    . VAL D 2 160 ? 128.270 82.697  140.815 1.00 22.59 ?  139 VAL D CA    1 
ATOM   14487 C  C     . VAL D 2 160 ? 127.368 81.935  141.796 1.00 22.36 ?  139 VAL D C     1 
ATOM   14488 O  O     . VAL D 2 160 ? 126.144 81.910  141.628 1.00 21.64 ?  139 VAL D O     1 
ATOM   14489 C  CB    . VAL D 2 160 ? 128.821 81.748  139.698 1.00 23.08 ?  139 VAL D CB    1 
ATOM   14490 C  CG1   . VAL D 2 160 ? 127.758 80.751  139.198 1.00 24.33 ?  139 VAL D CG1   1 
ATOM   14491 C  CG2   . VAL D 2 160 ? 129.374 82.565  138.519 1.00 22.87 ?  139 VAL D CG2   1 
ATOM   14492 N  N     . GLY D 2 161 ? 127.979 81.328  142.817 1.00 22.21 ?  140 GLY D N     1 
ATOM   14493 C  CA    . GLY D 2 161 ? 127.233 80.633  143.863 1.00 22.50 ?  140 GLY D CA    1 
ATOM   14494 C  C     . GLY D 2 161 ? 126.216 81.537  144.553 1.00 22.88 ?  140 GLY D C     1 
ATOM   14495 O  O     . GLY D 2 161 ? 125.069 81.130  144.785 1.00 23.54 ?  140 GLY D O     1 
ATOM   14496 N  N     . LEU D 2 162 ? 126.623 82.766  144.869 1.00 22.25 ?  141 LEU D N     1 
ATOM   14497 C  CA    . LEU D 2 162 ? 125.713 83.726  145.500 1.00 22.48 ?  141 LEU D CA    1 
ATOM   14498 C  C     . LEU D 2 162 ? 124.596 84.201  144.566 1.00 22.27 ?  141 LEU D C     1 
ATOM   14499 O  O     . LEU D 2 162 ? 123.473 84.422  145.022 1.00 22.31 ?  141 LEU D O     1 
ATOM   14500 C  CB    . LEU D 2 162 ? 126.473 84.905  146.139 1.00 22.07 ?  141 LEU D CB    1 
ATOM   14501 C  CG    . LEU D 2 162 ? 127.198 84.546  147.454 1.00 22.81 ?  141 LEU D CG    1 
ATOM   14502 C  CD1   . LEU D 2 162 ? 128.320 85.528  147.781 1.00 21.65 ?  141 LEU D CD1   1 
ATOM   14503 C  CD2   . LEU D 2 162 ? 126.237 84.371  148.635 1.00 23.35 ?  141 LEU D CD2   1 
ATOM   14504 N  N     . TYR D 2 163 ? 124.893 84.359  143.275 1.00 22.63 ?  142 TYR D N     1 
ATOM   14505 C  CA    . TYR D 2 163 ? 123.845 84.678  142.284 1.00 23.30 ?  142 TYR D CA    1 
ATOM   14506 C  C     . TYR D 2 163 ? 122.825 83.554  142.154 1.00 23.40 ?  142 TYR D C     1 
ATOM   14507 O  O     . TYR D 2 163 ? 121.637 83.809  142.030 1.00 23.75 ?  142 TYR D O     1 
ATOM   14508 C  CB    . TYR D 2 163 ? 124.423 84.919  140.897 1.00 23.22 ?  142 TYR D CB    1 
ATOM   14509 C  CG    . TYR D 2 163 ? 125.381 86.072  140.769 1.00 24.01 ?  142 TYR D CG    1 
ATOM   14510 C  CD1   . TYR D 2 163 ? 125.367 87.124  141.676 1.00 24.47 ?  142 TYR D CD1   1 
ATOM   14511 C  CD2   . TYR D 2 163 ? 126.298 86.108  139.723 1.00 24.62 ?  142 TYR D CD2   1 
ATOM   14512 C  CE1   . TYR D 2 163 ? 126.246 88.181  141.552 1.00 26.33 ?  142 TYR D CE1   1 
ATOM   14513 C  CE2   . TYR D 2 163 ? 127.177 87.170  139.581 1.00 26.07 ?  142 TYR D CE2   1 
ATOM   14514 C  CZ    . TYR D 2 163 ? 127.138 88.206  140.505 1.00 26.65 ?  142 TYR D CZ    1 
ATOM   14515 O  OH    . TYR D 2 163 ? 128.008 89.265  140.391 1.00 31.13 ?  142 TYR D OH    1 
ATOM   14516 N  N     . LYS D 2 164 ? 123.295 82.314  142.170 1.00 23.70 ?  143 LYS D N     1 
ATOM   14517 C  CA    . LYS D 2 164 ? 122.401 81.150  142.073 1.00 24.47 ?  143 LYS D CA    1 
ATOM   14518 C  C     . LYS D 2 164 ? 121.531 80.933  143.323 1.00 24.55 ?  143 LYS D C     1 
ATOM   14519 O  O     . LYS D 2 164 ? 120.526 80.222  143.271 1.00 24.49 ?  143 LYS D O     1 
ATOM   14520 C  CB    . LYS D 2 164 ? 123.216 79.889  141.778 1.00 24.98 ?  143 LYS D CB    1 
ATOM   14521 C  CG    . LYS D 2 164 ? 123.720 79.774  140.331 1.00 27.10 ?  143 LYS D CG    1 
ATOM   14522 C  CD    . LYS D 2 164 ? 124.407 78.432  140.130 1.00 30.75 ?  143 LYS D CD    1 
ATOM   14523 C  CE    . LYS D 2 164 ? 124.844 78.202  138.684 1.00 32.81 ?  143 LYS D CE    1 
ATOM   14524 N  NZ    . LYS D 2 164 ? 125.621 76.907  138.525 1.00 33.68 1  143 LYS D NZ    1 
ATOM   14525 N  N     . ALA D 2 165 ? 121.927 81.535  144.441 1.00 24.18 ?  144 ALA D N     1 
ATOM   14526 C  CA    . ALA D 2 165 ? 121.221 81.348  145.712 1.00 25.04 ?  144 ALA D CA    1 
ATOM   14527 C  C     . ALA D 2 165 ? 120.117 82.379  145.987 1.00 25.00 ?  144 ALA D C     1 
ATOM   14528 O  O     . ALA D 2 165 ? 119.435 82.293  147.019 1.00 25.50 ?  144 ALA D O     1 
ATOM   14529 C  CB    . ALA D 2 165 ? 122.219 81.309  146.882 1.00 25.02 ?  144 ALA D CB    1 
ATOM   14530 N  N     . ILE D 2 166 ? 119.938 83.348  145.086 1.00 24.60 ?  145 ILE D N     1 
ATOM   14531 C  CA    . ILE D 2 166 ? 118.858 84.325  145.232 1.00 24.40 ?  145 ILE D CA    1 
ATOM   14532 C  C     . ILE D 2 166 ? 117.507 83.600  145.159 1.00 25.75 ?  145 ILE D C     1 
ATOM   14533 O  O     . ILE D 2 166 ? 117.283 82.768  144.274 1.00 25.84 ?  145 ILE D O     1 
ATOM   14534 C  CB    . ILE D 2 166 ? 118.890 85.441  144.150 1.00 24.15 ?  145 ILE D CB    1 
ATOM   14535 C  CG1   . ILE D 2 166 ? 120.277 86.076  144.053 1.00 23.15 ?  145 ILE D CG1   1 
ATOM   14536 C  CG2   . ILE D 2 166 ? 117.839 86.508  144.455 1.00 22.72 ?  145 ILE D CG2   1 
ATOM   14537 C  CD1   . ILE D 2 166 ? 120.444 87.004  142.868 1.00 21.70 ?  145 ILE D CD1   1 
ATOM   14538 N  N     . GLN D 2 167 ? 116.632 83.897  146.112 1.00 26.52 ?  146 GLN D N     1 
ATOM   14539 C  CA    . GLN D 2 167 ? 115.292 83.326  146.124 1.00 28.77 ?  146 GLN D CA    1 
ATOM   14540 C  C     . GLN D 2 167 ? 114.248 84.405  145.867 1.00 29.20 ?  146 GLN D C     1 
ATOM   14541 O  O     . GLN D 2 167 ? 114.374 85.536  146.358 1.00 28.89 ?  146 GLN D O     1 
ATOM   14542 C  CB    . GLN D 2 167 ? 115.021 82.640  147.460 1.00 29.04 ?  146 GLN D CB    1 
ATOM   14543 C  CG    . GLN D 2 167 ? 115.908 81.435  147.706 1.00 31.87 ?  146 GLN D CG    1 
ATOM   14544 C  CD    . GLN D 2 167 ? 116.440 81.403  149.114 1.00 35.35 ?  146 GLN D CD    1 
ATOM   14545 O  OE1   . GLN D 2 167 ? 115.689 81.196  150.070 1.00 36.91 ?  146 GLN D OE1   1 
ATOM   14546 N  NE2   . GLN D 2 167 ? 117.748 81.607  149.255 1.00 36.19 ?  146 GLN D NE2   1 
ATOM   14547 N  N     . LYS D 2 168 ? 113.220 84.049  145.100 1.00 30.29 ?  147 LYS D N     1 
ATOM   14548 C  CA    . LYS D 2 168 ? 112.115 84.966  144.827 1.00 31.24 ?  147 LYS D CA    1 
ATOM   14549 C  C     . LYS D 2 168 ? 111.556 85.564  146.118 1.00 31.73 ?  147 LYS D C     1 
ATOM   14550 O  O     . LYS D 2 168 ? 111.373 84.848  147.102 1.00 31.46 ?  147 LYS D O     1 
ATOM   14551 C  CB    . LYS D 2 168 ? 111.013 84.261  144.040 1.00 31.92 ?  147 LYS D CB    1 
ATOM   14552 C  CG    . LYS D 2 168 ? 109.867 85.179  143.644 1.00 33.23 ?  147 LYS D CG    1 
ATOM   14553 C  CD    . LYS D 2 168 ? 108.918 84.504  142.667 1.00 36.06 ?  147 LYS D CD    1 
ATOM   14554 C  CE    . LYS D 2 168 ? 107.742 85.399  142.336 1.00 35.46 ?  147 LYS D CE    1 
ATOM   14555 N  NZ    . LYS D 2 168 ? 108.137 86.556  141.489 1.00 38.24 1  147 LYS D NZ    1 
ATOM   14556 N  N     . ASP D 2 169 ? 111.313 86.877  146.106 1.00 32.28 ?  148 ASP D N     1 
ATOM   14557 C  CA    . ASP D 2 169 ? 110.770 87.612  147.261 1.00 33.45 ?  148 ASP D CA    1 
ATOM   14558 C  C     . ASP D 2 169 ? 111.574 87.499  148.556 1.00 33.30 ?  148 ASP D C     1 
ATOM   14559 O  O     . ASP D 2 169 ? 111.025 87.667  149.647 1.00 34.32 ?  148 ASP D O     1 
ATOM   14560 C  CB    . ASP D 2 169 ? 109.320 87.190  147.549 1.00 34.63 ?  148 ASP D CB    1 
ATOM   14561 C  CG    . ASP D 2 169 ? 108.334 87.718  146.530 1.00 36.09 ?  148 ASP D CG    1 
ATOM   14562 O  OD1   . ASP D 2 169 ? 108.684 88.607  145.724 1.00 37.80 ?  148 ASP D OD1   1 
ATOM   14563 O  OD2   . ASP D 2 169 ? 107.185 87.231  146.548 1.00 40.47 -1 148 ASP D OD2   1 
ATOM   14564 N  N     . ASP D 2 170 ? 112.858 87.193  148.455 1.00 32.58 ?  149 ASP D N     1 
ATOM   14565 C  CA    . ASP D 2 170 ? 113.710 87.189  149.642 1.00 32.01 ?  149 ASP D CA    1 
ATOM   14566 C  C     . ASP D 2 170 ? 114.812 88.226  149.461 1.00 30.59 ?  149 ASP D C     1 
ATOM   14567 O  O     . ASP D 2 170 ? 115.776 88.004  148.728 1.00 29.11 ?  149 ASP D O     1 
ATOM   14568 C  CB    . ASP D 2 170 ? 114.275 85.793  149.919 1.00 32.93 ?  149 ASP D CB    1 
ATOM   14569 C  CG    . ASP D 2 170 ? 115.355 85.790  150.992 1.00 35.05 ?  149 ASP D CG    1 
ATOM   14570 O  OD1   . ASP D 2 170 ? 115.345 86.646  151.904 1.00 39.25 ?  149 ASP D OD1   1 
ATOM   14571 O  OD2   . ASP D 2 170 ? 116.221 84.907  150.933 1.00 39.22 -1 149 ASP D OD2   1 
ATOM   14572 N  N     . GLU D 2 171 ? 114.640 89.360  150.134 1.00 29.34 ?  150 GLU D N     1 
ATOM   14573 C  CA    . GLU D 2 171 ? 115.549 90.494  149.994 1.00 28.51 ?  150 GLU D CA    1 
ATOM   14574 C  C     . GLU D 2 171 ? 116.920 90.262  150.643 1.00 27.27 ?  150 GLU D C     1 
ATOM   14575 O  O     . GLU D 2 171 ? 117.890 90.900  150.265 1.00 26.62 ?  150 GLU D O     1 
ATOM   14576 C  CB    . GLU D 2 171 ? 114.893 91.780  150.516 1.00 29.09 ?  150 GLU D CB    1 
ATOM   14577 C  CG    . GLU D 2 171 ? 114.686 91.844  152.028 1.00 30.68 ?  150 GLU D CG    1 
ATOM   14578 C  CD    . GLU D 2 171 ? 113.873 93.057  152.452 1.00 33.92 ?  150 GLU D CD    1 
ATOM   14579 O  OE1   . GLU D 2 171 ? 113.507 93.872  151.569 1.00 36.31 ?  150 GLU D OE1   1 
ATOM   14580 O  OE2   . GLU D 2 171 ? 113.600 93.210  153.662 1.00 34.02 -1 150 GLU D OE2   1 
ATOM   14581 N  N     . ILE D 2 172 ? 117.000 89.336  151.597 1.00 26.19 ?  151 ILE D N     1 
ATOM   14582 C  CA    . ILE D 2 172 ? 118.277 88.998  152.228 1.00 25.49 ?  151 ILE D CA    1 
ATOM   14583 C  C     . ILE D 2 172 ? 119.208 88.312  151.223 1.00 24.61 ?  151 ILE D C     1 
ATOM   14584 O  O     . ILE D 2 172 ? 120.377 88.692  151.088 1.00 24.09 ?  151 ILE D O     1 
ATOM   14585 C  CB    . ILE D 2 172 ? 118.088 88.138  153.509 1.00 25.98 ?  151 ILE D CB    1 
ATOM   14586 C  CG1   . ILE D 2 172 ? 117.321 88.917  154.578 1.00 26.86 ?  151 ILE D CG1   1 
ATOM   14587 C  CG2   . ILE D 2 172 ? 119.438 87.621  154.075 1.00 26.50 ?  151 ILE D CG2   1 
ATOM   14588 C  CD1   . ILE D 2 172 ? 118.006 90.196  155.038 1.00 27.81 ?  151 ILE D CD1   1 
ATOM   14589 N  N     . SER D 2 173 ? 118.676 87.324  150.508 1.00 23.71 ?  152 SER D N     1 
ATOM   14590 C  CA    . SER D 2 173 ? 119.446 86.612  149.490 1.00 23.38 ?  152 SER D CA    1 
ATOM   14591 C  C     . SER D 2 173 ? 119.804 87.542  148.317 1.00 22.41 ?  152 SER D C     1 
ATOM   14592 O  O     . SER D 2 173 ? 120.877 87.423  147.718 1.00 21.43 ?  152 SER D O     1 
ATOM   14593 C  CB    . SER D 2 173 ? 118.702 85.359  149.011 1.00 23.90 ?  152 SER D CB    1 
ATOM   14594 O  OG    . SER D 2 173 ? 117.547 85.655  148.227 1.00 23.74 ?  152 SER D OG    1 
ATOM   14595 N  N     . LEU D 2 174 ? 118.911 88.478  148.009 1.00 21.63 ?  153 LEU D N     1 
ATOM   14596 C  CA    . LEU D 2 174 ? 119.197 89.470  146.968 1.00 20.75 ?  153 LEU D CA    1 
ATOM   14597 C  C     . LEU D 2 174 ? 120.353 90.366  147.408 1.00 20.96 ?  153 LEU D C     1 
ATOM   14598 O  O     . LEU D 2 174 ? 121.264 90.636  146.626 1.00 20.41 ?  153 LEU D O     1 
ATOM   14599 C  CB    . LEU D 2 174 ? 117.948 90.312  146.637 1.00 20.62 ?  153 LEU D CB    1 
ATOM   14600 C  CG    . LEU D 2 174 ? 118.125 91.424  145.581 1.00 19.55 ?  153 LEU D CG    1 
ATOM   14601 C  CD1   . LEU D 2 174 ? 118.728 90.861  144.288 1.00 20.44 ?  153 LEU D CD1   1 
ATOM   14602 C  CD2   . LEU D 2 174 ? 116.779 92.113  145.312 1.00 20.99 ?  153 LEU D CD2   1 
ATOM   14603 N  N     . PHE D 2 175 ? 120.315 90.819  148.661 1.00 21.07 ?  154 PHE D N     1 
ATOM   14604 C  CA    . PHE D 2 175 ? 121.374 91.669  149.199 1.00 21.32 ?  154 PHE D CA    1 
ATOM   14605 C  C     . PHE D 2 175 ? 122.741 90.979  149.123 1.00 21.08 ?  154 PHE D C     1 
ATOM   14606 O  O     . PHE D 2 175 ? 123.732 91.587  148.715 1.00 20.85 ?  154 PHE D O     1 
ATOM   14607 C  CB    . PHE D 2 175 ? 121.063 92.063  150.648 1.00 21.20 ?  154 PHE D CB    1 
ATOM   14608 C  CG    . PHE D 2 175 ? 122.215 92.704  151.363 1.00 22.46 ?  154 PHE D CG    1 
ATOM   14609 C  CD1   . PHE D 2 175 ? 122.376 94.089  151.341 1.00 21.21 ?  154 PHE D CD1   1 
ATOM   14610 C  CD2   . PHE D 2 175 ? 123.139 91.930  152.070 1.00 22.53 ?  154 PHE D CD2   1 
ATOM   14611 C  CE1   . PHE D 2 175 ? 123.426 94.690  152.005 1.00 22.11 ?  154 PHE D CE1   1 
ATOM   14612 C  CE2   . PHE D 2 175 ? 124.212 92.527  152.727 1.00 23.26 ?  154 PHE D CE2   1 
ATOM   14613 C  CZ    . PHE D 2 175 ? 124.354 93.910  152.702 1.00 22.08 ?  154 PHE D CZ    1 
ATOM   14614 N  N     . LYS D 2 176 ? 122.786 89.714  149.528 1.00 21.14 ?  155 LYS D N     1 
ATOM   14615 C  CA    . LYS D 2 176 ? 124.026 88.933  149.484 1.00 20.93 ?  155 LYS D CA    1 
ATOM   14616 C  C     . LYS D 2 176 ? 124.605 88.846  148.074 1.00 20.61 ?  155 LYS D C     1 
ATOM   14617 O  O     . LYS D 2 176 ? 125.817 88.985  147.878 1.00 20.62 ?  155 LYS D O     1 
ATOM   14618 C  CB    . LYS D 2 176 ? 123.782 87.543  150.052 1.00 21.27 ?  155 LYS D CB    1 
ATOM   14619 C  CG    . LYS D 2 176 ? 123.622 87.566  151.547 1.00 22.04 ?  155 LYS D CG    1 
ATOM   14620 C  CD    . LYS D 2 176 ? 123.273 86.203  152.121 1.00 25.24 ?  155 LYS D CD    1 
ATOM   14621 C  CE    . LYS D 2 176 ? 123.195 86.305  153.623 1.00 25.83 ?  155 LYS D CE    1 
ATOM   14622 N  NZ    . LYS D 2 176 ? 122.874 85.004  154.279 1.00 26.64 1  155 LYS D NZ    1 
ATOM   14623 N  N     . ALA D 2 177 ? 123.729 88.645  147.096 1.00 20.02 ?  156 ALA D N     1 
ATOM   14624 C  CA    . ALA D 2 177 ? 124.133 88.647  145.692 1.00 19.86 ?  156 ALA D CA    1 
ATOM   14625 C  C     . ALA D 2 177 ? 124.626 90.028  145.234 1.00 19.61 ?  156 ALA D C     1 
ATOM   14626 O  O     . ALA D 2 177 ? 125.542 90.133  144.416 1.00 19.69 ?  156 ALA D O     1 
ATOM   14627 C  CB    . ALA D 2 177 ? 122.988 88.196  144.846 1.00 19.99 ?  156 ALA D CB    1 
ATOM   14628 N  N     . MET D 2 178 ? 124.009 91.086  145.755 1.00 19.75 ?  157 MET D N     1 
ATOM   14629 C  CA    . MET D 2 178 ? 124.409 92.461  145.390 1.00 18.89 ?  157 MET D CA    1 
ATOM   14630 C  C     . MET D 2 178 ? 125.794 92.768  145.938 1.00 18.62 ?  157 MET D C     1 
ATOM   14631 O  O     . MET D 2 178 ? 126.609 93.408  145.263 1.00 18.10 ?  157 MET D O     1 
ATOM   14632 C  CB    . MET D 2 178 ? 123.397 93.480  145.906 1.00 18.82 ?  157 MET D CB    1 
ATOM   14633 C  CG    . MET D 2 178 ? 122.105 93.502  145.106 1.00 20.20 ?  157 MET D CG    1 
ATOM   14634 S  SD    . MET D 2 178 ? 120.920 94.616  145.872 1.00 23.78 ?  157 MET D SD    1 
ATOM   14635 C  CE    . MET D 2 178 ? 119.648 94.631  144.612 1.00 22.62 ?  157 MET D CE    1 
ATOM   14636 N  N     . VAL D 2 179 ? 126.057 92.283  147.153 1.00 18.34 ?  158 VAL D N     1 
ATOM   14637 C  CA    . VAL D 2 179 ? 127.374 92.393  147.761 1.00 18.75 ?  158 VAL D CA    1 
ATOM   14638 C  C     . VAL D 2 179 ? 128.417 91.698  146.893 1.00 18.86 ?  158 VAL D C     1 
ATOM   14639 O  O     . VAL D 2 179 ? 129.487 92.274  146.628 1.00 18.79 ?  158 VAL D O     1 
ATOM   14640 C  CB    . VAL D 2 179 ? 127.419 91.816  149.201 1.00 19.02 ?  158 VAL D CB    1 
ATOM   14641 C  CG1   . VAL D 2 179 ? 128.870 91.753  149.701 1.00 19.10 ?  158 VAL D CG1   1 
ATOM   14642 C  CG2   . VAL D 2 179 ? 126.547 92.653  150.150 1.00 18.94 ?  158 VAL D CG2   1 
ATOM   14643 N  N     . ALA D 2 180 ? 128.106 90.467  146.469 1.00 18.96 ?  159 ALA D N     1 
ATOM   14644 C  CA    . ALA D 2 180 ? 128.963 89.723  145.544 1.00 19.05 ?  159 ALA D CA    1 
ATOM   14645 C  C     . ALA D 2 180 ? 129.200 90.513  144.255 1.00 18.67 ?  159 ALA D C     1 
ATOM   14646 O  O     . ALA D 2 180 ? 130.341 90.621  143.788 1.00 17.72 ?  159 ALA D O     1 
ATOM   14647 C  CB    . ALA D 2 180 ? 128.362 88.340  145.231 1.00 19.43 ?  159 ALA D CB    1 
ATOM   14648 N  N     . SER D 2 181 ? 128.126 91.090  143.708 1.00 18.49 ?  160 SER D N     1 
ATOM   14649 C  CA    . SER D 2 181 ? 128.231 91.885  142.483 1.00 18.51 ?  160 SER D CA    1 
ATOM   14650 C  C     . SER D 2 181 ? 129.119 93.117  142.659 1.00 18.23 ?  160 SER D C     1 
ATOM   14651 O  O     . SER D 2 181 ? 129.980 93.386  141.832 1.00 18.18 ?  160 SER D O     1 
ATOM   14652 C  CB    . SER D 2 181 ? 126.850 92.311  141.977 1.00 18.51 ?  160 SER D CB    1 
ATOM   14653 O  OG    . SER D 2 181 ? 126.986 92.925  140.710 1.00 19.42 ?  160 SER D OG    1 
ATOM   14654 N  N     . VAL D 2 182 ? 128.910 93.857  143.746 1.00 18.43 ?  161 VAL D N     1 
ATOM   14655 C  CA    . VAL D 2 182 ? 129.761 95.013  144.046 1.00 18.09 ?  161 VAL D CA    1 
ATOM   14656 C  C     . VAL D 2 182 ? 131.225 94.592  144.220 1.00 18.41 ?  161 VAL D C     1 
ATOM   14657 O  O     . VAL D 2 182 ? 132.129 95.258  143.712 1.00 18.52 ?  161 VAL D O     1 
ATOM   14658 C  CB    . VAL D 2 182 ? 129.257 95.796  145.265 1.00 17.71 ?  161 VAL D CB    1 
ATOM   14659 C  CG1   . VAL D 2 182 ? 130.282 96.875  145.691 1.00 16.02 ?  161 VAL D CG1   1 
ATOM   14660 C  CG2   . VAL D 2 182 ? 127.907 96.445  144.930 1.00 17.78 ?  161 VAL D CG2   1 
ATOM   14661 N  N     . TYR D 2 183 ? 131.452 93.466  144.898 1.00 19.06 ?  162 TYR D N     1 
ATOM   14662 C  CA    . TYR D 2 183 ? 132.816 92.973  145.060 1.00 19.73 ?  162 TYR D CA    1 
ATOM   14663 C  C     . TYR D 2 183 ? 133.454 92.641  143.719 1.00 19.90 ?  162 TYR D C     1 
ATOM   14664 O  O     . TYR D 2 183 ? 134.640 92.868  143.540 1.00 20.73 ?  162 TYR D O     1 
ATOM   14665 C  CB    . TYR D 2 183 ? 132.907 91.777  146.026 1.00 19.84 ?  162 TYR D CB    1 
ATOM   14666 C  CG    . TYR D 2 183 ? 132.723 92.136  147.486 1.00 20.24 ?  162 TYR D CG    1 
ATOM   14667 C  CD1   . TYR D 2 183 ? 132.753 93.461  147.912 1.00 21.51 ?  162 TYR D CD1   1 
ATOM   14668 C  CD2   . TYR D 2 183 ? 132.539 91.139  148.453 1.00 20.45 ?  162 TYR D CD2   1 
ATOM   14669 C  CE1   . TYR D 2 183 ? 132.588 93.791  149.263 1.00 21.68 ?  162 TYR D CE1   1 
ATOM   14670 C  CE2   . TYR D 2 183 ? 132.396 91.458  149.809 1.00 19.97 ?  162 TYR D CE2   1 
ATOM   14671 C  CZ    . TYR D 2 183 ? 132.417 92.785  150.203 1.00 21.83 ?  162 TYR D CZ    1 
ATOM   14672 O  OH    . TYR D 2 183 ? 132.266 93.114  151.536 1.00 21.96 ?  162 TYR D OH    1 
ATOM   14673 N  N     . LEU D 2 184 ? 132.679 92.130  142.772 1.00 20.22 ?  163 LEU D N     1 
ATOM   14674 C  CA    . LEU D 2 184 ? 133.234 91.845  141.452 1.00 20.89 ?  163 LEU D CA    1 
ATOM   14675 C  C     . LEU D 2 184 ? 133.540 93.156  140.711 1.00 20.72 ?  163 LEU D C     1 
ATOM   14676 O  O     . LEU D 2 184 ? 134.669 93.373  140.282 1.00 21.07 ?  163 LEU D O     1 
ATOM   14677 C  CB    . LEU D 2 184 ? 132.320 90.902  140.644 1.00 21.16 ?  163 LEU D CB    1 
ATOM   14678 C  CG    . LEU D 2 184 ? 132.718 90.520  139.203 1.00 22.77 ?  163 LEU D CG    1 
ATOM   14679 C  CD1   . LEU D 2 184 ? 134.164 89.986  139.101 1.00 22.44 ?  163 LEU D CD1   1 
ATOM   14680 C  CD2   . LEU D 2 184 ? 131.745 89.514  138.610 1.00 24.75 ?  163 LEU D CD2   1 
ATOM   14681 N  N     . GLU D 2 185 ? 132.542 94.032  140.608 1.00 20.65 ?  164 GLU D N     1 
ATOM   14682 C  CA    . GLU D 2 185 ? 132.666 95.303  139.879 1.00 20.69 ?  164 GLU D CA    1 
ATOM   14683 C  C     . GLU D 2 185 ? 133.736 96.247  140.427 1.00 20.64 ?  164 GLU D C     1 
ATOM   14684 O  O     . GLU D 2 185 ? 134.446 96.911  139.657 1.00 20.25 ?  164 GLU D O     1 
ATOM   14685 C  CB    . GLU D 2 185 ? 131.324 96.049  139.878 1.00 21.03 ?  164 GLU D CB    1 
ATOM   14686 C  CG    . GLU D 2 185 ? 130.156 95.280  139.255 1.00 22.19 ?  164 GLU D CG    1 
ATOM   14687 C  CD    . GLU D 2 185 ? 130.086 95.385  137.733 1.00 24.19 ?  164 GLU D CD    1 
ATOM   14688 O  OE1   . GLU D 2 185 ? 130.982 95.970  137.098 1.00 27.97 ?  164 GLU D OE1   1 
ATOM   14689 O  OE2   . GLU D 2 185 ? 129.111 94.899  137.159 1.00 25.47 -1 164 GLU D OE2   1 
ATOM   14690 N  N     . SER D 2 186 ? 133.826 96.328  141.750 1.00 20.42 ?  165 SER D N     1 
ATOM   14691 C  CA    . SER D 2 186 ? 134.623 97.365  142.405 1.00 20.70 ?  165 SER D CA    1 
ATOM   14692 C  C     . SER D 2 186 ? 135.900 96.849  143.068 1.00 20.88 ?  165 SER D C     1 
ATOM   14693 O  O     . SER D 2 186 ? 136.648 97.630  143.655 1.00 21.21 ?  165 SER D O     1 
ATOM   14694 C  CB    . SER D 2 186 ? 133.777 98.121  143.444 1.00 21.25 ?  165 SER D CB    1 
ATOM   14695 O  OG    . SER D 2 186 ? 132.560 98.602  142.888 1.00 20.97 ?  165 SER D OG    1 
ATOM   14696 N  N     . PHE D 2 187 ? 136.165 95.545  142.977 1.00 20.94 ?  166 PHE D N     1 
ATOM   14697 C  CA    . PHE D 2 187 ? 137.266 94.973  143.737 1.00 21.19 ?  166 PHE D CA    1 
ATOM   14698 C  C     . PHE D 2 187 ? 137.985 93.860  142.976 1.00 21.22 ?  166 PHE D C     1 
ATOM   14699 O  O     . PHE D 2 187 ? 139.169 94.016  142.657 1.00 21.10 ?  166 PHE D O     1 
ATOM   14700 C  CB    . PHE D 2 187 ? 136.779 94.575  145.158 1.00 21.63 ?  166 PHE D CB    1 
ATOM   14701 C  CG    . PHE D 2 187 ? 137.639 93.565  145.871 1.00 24.05 ?  166 PHE D CG    1 
ATOM   14702 C  CD1   . PHE D 2 187 ? 138.986 93.817  146.133 1.00 25.52 ?  166 PHE D CD1   1 
ATOM   14703 C  CD2   . PHE D 2 187 ? 137.084 92.373  146.329 1.00 27.03 ?  166 PHE D CD2   1 
ATOM   14704 C  CE1   . PHE D 2 187 ? 139.763 92.888  146.813 1.00 26.73 ?  166 PHE D CE1   1 
ATOM   14705 C  CE2   . PHE D 2 187 ? 137.869 91.428  147.006 1.00 27.36 ?  166 PHE D CE2   1 
ATOM   14706 C  CZ    . PHE D 2 187 ? 139.204 91.691  147.242 1.00 27.87 ?  166 PHE D CZ    1 
ATOM   14707 N  N     . LEU D 2 188 ? 137.276 92.786  142.641 1.00 20.78 ?  167 LEU D N     1 
ATOM   14708 C  CA    . LEU D 2 188 ? 137.905 91.605  142.014 1.00 21.78 ?  167 LEU D CA    1 
ATOM   14709 C  C     . LEU D 2 188 ? 138.526 91.855  140.634 1.00 21.91 ?  167 LEU D C     1 
ATOM   14710 O  O     . LEU D 2 188 ? 139.524 91.223  140.288 1.00 22.87 ?  167 LEU D O     1 
ATOM   14711 C  CB    . LEU D 2 188 ? 136.920 90.440  141.927 1.00 22.32 ?  167 LEU D CB    1 
ATOM   14712 C  CG    . LEU D 2 188 ? 136.418 89.757  143.198 1.00 23.33 ?  167 LEU D CG    1 
ATOM   14713 C  CD1   . LEU D 2 188 ? 135.441 88.662  142.807 1.00 22.43 ?  167 LEU D CD1   1 
ATOM   14714 C  CD2   . LEU D 2 188 ? 137.556 89.187  144.055 1.00 25.71 ?  167 LEU D CD2   1 
ATOM   14715 N  N     . PHE D 2 189 ? 137.930 92.752  139.845 1.00 21.56 ?  168 PHE D N     1 
ATOM   14716 C  CA    . PHE D 2 189 ? 138.480 93.122  138.538 1.00 21.86 ?  168 PHE D CA    1 
ATOM   14717 C  C     . PHE D 2 189 ? 139.861 93.804  138.643 1.00 21.87 ?  168 PHE D C     1 
ATOM   14718 O  O     . PHE D 2 189 ? 140.641 93.794  137.687 1.00 21.79 ?  168 PHE D O     1 
ATOM   14719 C  CB    . PHE D 2 189 ? 137.538 94.087  137.794 1.00 21.79 ?  168 PHE D CB    1 
ATOM   14720 C  CG    . PHE D 2 189 ? 136.361 93.422  137.119 1.00 21.88 ?  168 PHE D CG    1 
ATOM   14721 C  CD1   . PHE D 2 189 ? 136.490 92.189  136.477 1.00 21.44 ?  168 PHE D CD1   1 
ATOM   14722 C  CD2   . PHE D 2 189 ? 135.121 94.062  137.099 1.00 22.82 ?  168 PHE D CD2   1 
ATOM   14723 C  CE1   . PHE D 2 189 ? 135.392 91.588  135.848 1.00 22.35 ?  168 PHE D CE1   1 
ATOM   14724 C  CE2   . PHE D 2 189 ? 134.017 93.479  136.475 1.00 22.08 ?  168 PHE D CE2   1 
ATOM   14725 C  CZ    . PHE D 2 189 ? 134.148 92.232  135.857 1.00 22.60 ?  168 PHE D CZ    1 
ATOM   14726 N  N     . TYR D 2 190 ? 140.151 94.414  139.787 1.00 21.91 ?  169 TYR D N     1 
ATOM   14727 C  CA    . TYR D 2 190 ? 141.293 95.338  139.860 1.00 22.52 ?  169 TYR D CA    1 
ATOM   14728 C  C     . TYR D 2 190 ? 142.677 94.690  139.938 1.00 22.75 ?  169 TYR D C     1 
ATOM   14729 O  O     . TYR D 2 190 ? 143.646 95.303  139.511 1.00 21.93 ?  169 TYR D O     1 
ATOM   14730 C  CB    . TYR D 2 190 ? 141.080 96.416  140.927 1.00 22.67 ?  169 TYR D CB    1 
ATOM   14731 C  CG    . TYR D 2 190 ? 140.097 97.461  140.441 1.00 24.77 ?  169 TYR D CG    1 
ATOM   14732 C  CD1   . TYR D 2 190 ? 138.725 97.195  140.399 1.00 25.65 ?  169 TYR D CD1   1 
ATOM   14733 C  CD2   . TYR D 2 190 ? 140.543 98.696  139.977 1.00 25.94 ?  169 TYR D CD2   1 
ATOM   14734 C  CE1   . TYR D 2 190 ? 137.821 98.149  139.919 1.00 26.62 ?  169 TYR D CE1   1 
ATOM   14735 C  CE2   . TYR D 2 190 ? 139.650 99.659  139.513 1.00 26.91 ?  169 TYR D CE2   1 
ATOM   14736 C  CZ    . TYR D 2 190 ? 138.297 99.380  139.482 1.00 27.39 ?  169 TYR D CZ    1 
ATOM   14737 O  OH    . TYR D 2 190 ? 137.429 100.347 139.011 1.00 27.50 ?  169 TYR D OH    1 
ATOM   14738 N  N     . SER D 2 191 ? 142.763 93.455  140.442 1.00 22.74 ?  170 SER D N     1 
ATOM   14739 C  CA    . SER D 2 191 ? 144.016 92.696  140.337 1.00 23.43 ?  170 SER D CA    1 
ATOM   14740 C  C     . SER D 2 191 ? 144.355 92.489  138.861 1.00 23.08 ?  170 SER D C     1 
ATOM   14741 O  O     . SER D 2 191 ? 145.514 92.399  138.492 1.00 23.67 ?  170 SER D O     1 
ATOM   14742 C  CB    . SER D 2 191 ? 143.937 91.346  141.067 1.00 23.39 ?  170 SER D CB    1 
ATOM   14743 O  OG    . SER D 2 191 ? 142.928 90.512  140.513 1.00 24.10 ?  170 SER D OG    1 
ATOM   14744 N  N     . GLY D 2 192 ? 143.328 92.457  138.022 1.00 22.82 ?  171 GLY D N     1 
ATOM   14745 C  CA    . GLY D 2 192 ? 143.490 92.329  136.579 1.00 22.08 ?  171 GLY D CA    1 
ATOM   14746 C  C     . GLY D 2 192 ? 143.736 93.653  135.875 1.00 22.12 ?  171 GLY D C     1 
ATOM   14747 O  O     . GLY D 2 192 ? 144.679 93.770  135.090 1.00 22.86 ?  171 GLY D O     1 
ATOM   14748 N  N     . PHE D 2 193 ? 142.897 94.651  136.153 1.00 21.48 ?  172 PHE D N     1 
ATOM   14749 C  CA    . PHE D 2 193 ? 143.038 95.989  135.549 1.00 21.06 ?  172 PHE D CA    1 
ATOM   14750 C  C     . PHE D 2 193 ? 144.426 96.588  135.773 1.00 21.13 ?  172 PHE D C     1 
ATOM   14751 O  O     . PHE D 2 193 ? 144.897 97.378  134.953 1.00 21.18 ?  172 PHE D O     1 
ATOM   14752 C  CB    . PHE D 2 193 ? 142.000 96.959  136.111 1.00 21.33 ?  172 PHE D CB    1 
ATOM   14753 C  CG    . PHE D 2 193 ? 140.586 96.710  135.643 1.00 20.93 ?  172 PHE D CG    1 
ATOM   14754 C  CD1   . PHE D 2 193 ? 140.318 96.154  134.392 1.00 20.88 ?  172 PHE D CD1   1 
ATOM   14755 C  CD2   . PHE D 2 193 ? 139.518 97.086  136.446 1.00 19.83 ?  172 PHE D CD2   1 
ATOM   14756 C  CE1   . PHE D 2 193 ? 138.998 95.950  133.972 1.00 22.31 ?  172 PHE D CE1   1 
ATOM   14757 C  CE2   . PHE D 2 193 ? 138.195 96.898  136.029 1.00 20.67 ?  172 PHE D CE2   1 
ATOM   14758 C  CZ    . PHE D 2 193 ? 137.937 96.329  134.790 1.00 21.00 ?  172 PHE D CZ    1 
ATOM   14759 N  N     . TYR D 2 194 ? 145.079 96.201  136.871 1.00 20.48 ?  173 TYR D N     1 
ATOM   14760 C  CA    . TYR D 2 194 ? 146.388 96.745  137.226 1.00 20.76 ?  173 TYR D CA    1 
ATOM   14761 C  C     . TYR D 2 194 ? 147.356 96.739  136.037 1.00 20.53 ?  173 TYR D C     1 
ATOM   14762 O  O     . TYR D 2 194 ? 147.982 97.753  135.713 1.00 19.89 ?  173 TYR D O     1 
ATOM   14763 C  CB    . TYR D 2 194 ? 147.006 95.983  138.425 1.00 20.94 ?  173 TYR D CB    1 
ATOM   14764 C  CG    . TYR D 2 194 ? 148.252 96.662  138.965 1.00 21.56 ?  173 TYR D CG    1 
ATOM   14765 C  CD1   . TYR D 2 194 ? 148.191 97.476  140.099 1.00 22.23 ?  173 TYR D CD1   1 
ATOM   14766 C  CD2   . TYR D 2 194 ? 149.490 96.510  138.329 1.00 22.00 ?  173 TYR D CD2   1 
ATOM   14767 C  CE1   . TYR D 2 194 ? 149.328 98.121  140.584 1.00 21.58 ?  173 TYR D CE1   1 
ATOM   14768 C  CE2   . TYR D 2 194 ? 150.624 97.140  138.808 1.00 20.52 ?  173 TYR D CE2   1 
ATOM   14769 C  CZ    . TYR D 2 194 ? 150.538 97.944  139.932 1.00 21.66 ?  173 TYR D CZ    1 
ATOM   14770 O  OH    . TYR D 2 194 ? 151.660 98.590  140.391 1.00 21.37 ?  173 TYR D OH    1 
ATOM   14771 N  N     . TYR D 2 195 ? 147.453 95.602  135.369 1.00 20.77 ?  174 TYR D N     1 
ATOM   14772 C  CA    . TYR D 2 195 ? 148.492 95.430  134.370 1.00 21.12 ?  174 TYR D CA    1 
ATOM   14773 C  C     . TYR D 2 195 ? 148.287 96.305  133.120 1.00 21.49 ?  174 TYR D C     1 
ATOM   14774 O  O     . TYR D 2 195 ? 149.214 97.025  132.735 1.00 21.60 ?  174 TYR D O     1 
ATOM   14775 C  CB    . TYR D 2 195 ? 148.688 93.944  134.054 1.00 21.23 ?  174 TYR D CB    1 
ATOM   14776 C  CG    . TYR D 2 195 ? 150.091 93.559  133.639 1.00 21.77 ?  174 TYR D CG    1 
ATOM   14777 C  CD1   . TYR D 2 195 ? 151.213 94.140  134.238 1.00 23.28 ?  174 TYR D CD1   1 
ATOM   14778 C  CD2   . TYR D 2 195 ? 150.295 92.591  132.658 1.00 22.87 ?  174 TYR D CD2   1 
ATOM   14779 C  CE1   . TYR D 2 195 ? 152.509 93.769  133.848 1.00 23.81 ?  174 TYR D CE1   1 
ATOM   14780 C  CE2   . TYR D 2 195 ? 151.579 92.212  132.274 1.00 24.09 ?  174 TYR D CE2   1 
ATOM   14781 C  CZ    . TYR D 2 195 ? 152.675 92.806  132.865 1.00 23.51 ?  174 TYR D CZ    1 
ATOM   14782 O  OH    . TYR D 2 195 ? 153.946 92.432  132.472 1.00 25.36 ?  174 TYR D OH    1 
ATOM   14783 N  N     . PRO D 2 196 ? 147.084 96.264  132.492 1.00 21.86 ?  175 PRO D N     1 
ATOM   14784 C  CA    . PRO D 2 196 ? 146.823 97.183  131.373 1.00 22.03 ?  175 PRO D CA    1 
ATOM   14785 C  C     . PRO D 2 196 ? 147.009 98.651  131.752 1.00 22.18 ?  175 PRO D C     1 
ATOM   14786 O  O     . PRO D 2 196 ? 147.526 99.421  130.938 1.00 23.00 ?  175 PRO D O     1 
ATOM   14787 C  CB    . PRO D 2 196 ? 145.352 96.924  131.020 1.00 21.50 ?  175 PRO D CB    1 
ATOM   14788 C  CG    . PRO D 2 196 ? 145.051 95.606  131.535 1.00 22.47 ?  175 PRO D CG    1 
ATOM   14789 C  CD    . PRO D 2 196 ? 146.022 95.250  132.622 1.00 20.91 ?  175 PRO D CD    1 
ATOM   14790 N  N     . LEU D 2 197 ? 146.608 99.033  132.966 1.00 21.70 ?  176 LEU D N     1 
ATOM   14791 C  CA    . LEU D 2 197 ? 146.821 100.406 133.447 1.00 22.40 ?  176 LEU D CA    1 
ATOM   14792 C  C     . LEU D 2 197 ? 148.303 100.739 133.631 1.00 22.58 ?  176 LEU D C     1 
ATOM   14793 O  O     . LEU D 2 197 ? 148.732 101.867 133.354 1.00 22.15 ?  176 LEU D O     1 
ATOM   14794 C  CB    . LEU D 2 197 ? 146.092 100.645 134.764 1.00 22.15 ?  176 LEU D CB    1 
ATOM   14795 C  CG    . LEU D 2 197 ? 144.561 100.733 134.770 1.00 23.08 ?  176 LEU D CG    1 
ATOM   14796 C  CD1   . LEU D 2 197 ? 144.081 100.608 136.206 1.00 21.62 ?  176 LEU D CD1   1 
ATOM   14797 C  CD2   . LEU D 2 197 ? 144.074 102.049 134.130 1.00 21.94 ?  176 LEU D CD2   1 
ATOM   14798 N  N     . TYR D 2 198 ? 149.064 99.750  134.105 1.00 22.76 ?  177 TYR D N     1 
ATOM   14799 C  CA    . TYR D 2 198 ? 150.517 99.852  134.259 1.00 23.23 ?  177 TYR D CA    1 
ATOM   14800 C  C     . TYR D 2 198 ? 151.197 100.102 132.913 1.00 23.91 ?  177 TYR D C     1 
ATOM   14801 O  O     . TYR D 2 198 ? 152.046 100.999 132.799 1.00 24.20 ?  177 TYR D O     1 
ATOM   14802 C  CB    . TYR D 2 198 ? 151.066 98.590  134.945 1.00 23.19 ?  177 TYR D CB    1 
ATOM   14803 C  CG    . TYR D 2 198 ? 152.560 98.576  135.207 1.00 23.52 ?  177 TYR D CG    1 
ATOM   14804 C  CD1   . TYR D 2 198 ? 153.134 99.451  136.119 1.00 24.85 ?  177 TYR D CD1   1 
ATOM   14805 C  CD2   . TYR D 2 198 ? 153.393 97.649  134.568 1.00 25.30 ?  177 TYR D CD2   1 
ATOM   14806 C  CE1   . TYR D 2 198 ? 154.507 99.429  136.379 1.00 26.05 ?  177 TYR D CE1   1 
ATOM   14807 C  CE2   . TYR D 2 198 ? 154.774 97.615  134.825 1.00 26.38 ?  177 TYR D CE2   1 
ATOM   14808 C  CZ    . TYR D 2 198 ? 155.314 98.509  135.730 1.00 26.68 ?  177 TYR D CZ    1 
ATOM   14809 O  OH    . TYR D 2 198 ? 156.664 98.495  136.003 1.00 30.01 ?  177 TYR D OH    1 
ATOM   14810 N  N     . PHE D 2 199 ? 150.828 99.332  131.889 1.00 24.84 ?  178 PHE D N     1 
ATOM   14811 C  CA    . PHE D 2 199 ? 151.340 99.599  130.541 1.00 25.81 ?  178 PHE D CA    1 
ATOM   14812 C  C     . PHE D 2 199 ? 150.878 100.938 129.981 1.00 26.23 ?  178 PHE D C     1 
ATOM   14813 O  O     . PHE D 2 199 ? 151.677 101.691 129.424 1.00 26.58 ?  178 PHE D O     1 
ATOM   14814 C  CB    . PHE D 2 199 ? 150.989 98.472  129.578 1.00 26.08 ?  178 PHE D CB    1 
ATOM   14815 C  CG    . PHE D 2 199 ? 151.827 97.243  129.764 1.00 28.71 ?  178 PHE D CG    1 
ATOM   14816 C  CD1   . PHE D 2 199 ? 153.206 97.341  129.902 1.00 32.03 ?  178 PHE D CD1   1 
ATOM   14817 C  CD2   . PHE D 2 199 ? 151.246 95.987  129.807 1.00 31.77 ?  178 PHE D CD2   1 
ATOM   14818 C  CE1   . PHE D 2 199 ? 154.000 96.198  130.089 1.00 32.29 ?  178 PHE D CE1   1 
ATOM   14819 C  CE2   . PHE D 2 199 ? 152.032 94.843  129.983 1.00 32.72 ?  178 PHE D CE2   1 
ATOM   14820 C  CZ    . PHE D 2 199 ? 153.410 94.957  130.123 1.00 31.91 ?  178 PHE D CZ    1 
ATOM   14821 N  N     . TYR D 2 200 ? 149.586 101.214 130.139 1.00 26.46 ?  179 TYR D N     1 
ATOM   14822 C  CA    . TYR D 2 200 ? 148.943 102.446 129.657 1.00 27.43 ?  179 TYR D CA    1 
ATOM   14823 C  C     . TYR D 2 200 ? 149.629 103.680 130.235 1.00 27.68 ?  179 TYR D C     1 
ATOM   14824 O  O     . TYR D 2 200 ? 149.827 104.670 129.533 1.00 28.71 ?  179 TYR D O     1 
ATOM   14825 C  CB    . TYR D 2 200 ? 147.478 102.417 130.081 1.00 27.27 ?  179 TYR D CB    1 
ATOM   14826 C  CG    . TYR D 2 200 ? 146.528 103.359 129.383 1.00 28.90 ?  179 TYR D CG    1 
ATOM   14827 C  CD1   . TYR D 2 200 ? 146.509 103.476 128.000 1.00 29.00 ?  179 TYR D CD1   1 
ATOM   14828 C  CD2   . TYR D 2 200 ? 145.591 104.086 130.123 1.00 30.14 ?  179 TYR D CD2   1 
ATOM   14829 C  CE1   . TYR D 2 200 ? 145.606 104.326 127.364 1.00 31.26 ?  179 TYR D CE1   1 
ATOM   14830 C  CE2   . TYR D 2 200 ? 144.681 104.925 129.503 1.00 31.86 ?  179 TYR D CE2   1 
ATOM   14831 C  CZ    . TYR D 2 200 ? 144.696 105.046 128.124 1.00 32.51 ?  179 TYR D CZ    1 
ATOM   14832 O  OH    . TYR D 2 200 ? 143.795 105.882 127.509 1.00 33.77 ?  179 TYR D OH    1 
ATOM   14833 N  N     . GLY D 2 201 ? 149.993 103.612 131.514 1.00 27.68 ?  180 GLY D N     1 
ATOM   14834 C  CA    . GLY D 2 201 ? 150.712 104.694 132.177 1.00 28.02 ?  180 GLY D CA    1 
ATOM   14835 C  C     . GLY D 2 201 ? 152.158 104.882 131.725 1.00 28.60 ?  180 GLY D C     1 
ATOM   14836 O  O     . GLY D 2 201 ? 152.760 105.905 132.023 1.00 28.44 ?  180 GLY D O     1 
ATOM   14837 N  N     . GLN D 2 202 ? 152.707 103.884 131.025 1.00 29.34 ?  181 GLN D N     1 
ATOM   14838 C  CA    . GLN D 2 202 ? 154.082 103.902 130.497 1.00 30.39 ?  181 GLN D CA    1 
ATOM   14839 C  C     . GLN D 2 202 ? 154.156 104.203 129.000 1.00 30.55 ?  181 GLN D C     1 
ATOM   14840 O  O     . GLN D 2 202 ? 155.253 104.261 128.436 1.00 31.23 ?  181 GLN D O     1 
ATOM   14841 C  CB    . GLN D 2 202 ? 154.729 102.524 130.647 1.00 30.31 ?  181 GLN D CB    1 
ATOM   14842 C  CG    . GLN D 2 202 ? 155.033 102.040 132.014 1.00 32.40 ?  181 GLN D CG    1 
ATOM   14843 C  CD    . GLN D 2 202 ? 155.657 100.661 131.955 1.00 33.85 ?  181 GLN D CD    1 
ATOM   14844 O  OE1   . GLN D 2 202 ? 155.016 99.660  132.263 1.00 33.94 ?  181 GLN D OE1   1 
ATOM   14845 N  NE2   . GLN D 2 202 ? 156.901 100.600 131.512 1.00 34.92 ?  181 GLN D NE2   1 
ATOM   14846 N  N     . GLY D 2 203 ? 153.009 104.319 128.341 1.00 30.57 ?  182 GLY D N     1 
ATOM   14847 C  CA    . GLY D 2 203 ? 152.981 104.537 126.893 1.00 30.83 ?  182 GLY D CA    1 
ATOM   14848 C  C     . GLY D 2 203 ? 152.978 103.258 126.069 1.00 30.80 ?  182 GLY D C     1 
ATOM   14849 O  O     . GLY D 2 203 ? 153.158 103.301 124.849 1.00 30.86 ?  182 GLY D O     1 
ATOM   14850 N  N     . LYS D 2 204 ? 152.767 102.120 126.732 1.00 30.14 ?  183 LYS D N     1 
ATOM   14851 C  CA    . LYS D 2 204 ? 152.705 100.823 126.052 1.00 30.35 ?  183 LYS D CA    1 
ATOM   14852 C  C     . LYS D 2 204 ? 151.270 100.318 125.920 1.00 29.52 ?  183 LYS D C     1 
ATOM   14853 O  O     . LYS D 2 204 ? 150.445 100.564 126.797 1.00 28.60 ?  183 LYS D O     1 
ATOM   14854 C  CB    . LYS D 2 204 ? 153.561 99.793  126.787 1.00 30.76 ?  183 LYS D CB    1 
ATOM   14855 C  CG    . LYS D 2 204 ? 155.059 100.109 126.757 1.00 32.95 ?  183 LYS D CG    1 
ATOM   14856 C  CD    . LYS D 2 204 ? 155.794 99.221  127.732 1.00 36.37 ?  183 LYS D CD    1 
ATOM   14857 C  CE    . LYS D 2 204 ? 157.287 99.492  127.741 1.00 38.47 ?  183 LYS D CE    1 
ATOM   14858 N  NZ    . LYS D 2 204 ? 157.889 98.761  128.896 1.00 40.21 1  183 LYS D NZ    1 
ATOM   14859 N  N     . LEU D 2 205 ? 150.988 99.605  124.827 1.00 29.47 ?  184 LEU D N     1 
ATOM   14860 C  CA    . LEU D 2 205 ? 149.651 99.056  124.547 1.00 29.06 ?  184 LEU D CA    1 
ATOM   14861 C  C     . LEU D 2 205 ? 148.537 100.079 124.854 1.00 28.96 ?  184 LEU D C     1 
ATOM   14862 O  O     . LEU D 2 205 ? 147.602 99.812  125.619 1.00 27.68 ?  184 LEU D O     1 
ATOM   14863 C  CB    . LEU D 2 205 ? 149.427 97.737  125.302 1.00 28.63 ?  184 LEU D CB    1 
ATOM   14864 C  CG    . LEU D 2 205 ? 150.431 96.596  125.072 1.00 29.00 ?  184 LEU D CG    1 
ATOM   14865 C  CD1   . LEU D 2 205 ? 150.088 95.400  125.965 1.00 28.90 ?  184 LEU D CD1   1 
ATOM   14866 C  CD2   . LEU D 2 205 ? 150.466 96.168  123.611 1.00 28.67 ?  184 LEU D CD2   1 
ATOM   14867 N  N     . MET D 2 206 ? 148.671 101.246 124.231 1.00 29.02 ?  185 MET D N     1 
ATOM   14868 C  CA    . MET D 2 206 ? 147.792 102.386 124.442 1.00 29.72 ?  185 MET D CA    1 
ATOM   14869 C  C     . MET D 2 206 ? 146.365 102.220 123.930 1.00 29.54 ?  185 MET D C     1 
ATOM   14870 O  O     . MET D 2 206 ? 145.439 102.770 124.522 1.00 29.47 ?  185 MET D O     1 
ATOM   14871 C  CB    . MET D 2 206 ? 148.418 103.642 123.823 1.00 30.69 ?  185 MET D CB    1 
ATOM   14872 C  CG    . MET D 2 206 ? 149.786 103.969 124.402 1.00 32.03 ?  185 MET D CG    1 
ATOM   14873 S  SD    . MET D 2 206 ? 149.703 104.214 126.185 1.00 36.63 ?  185 MET D SD    1 
ATOM   14874 C  CE    . MET D 2 206 ? 149.228 105.932 126.257 1.00 33.80 ?  185 MET D CE    1 
ATOM   14875 N  N     . GLN D 2 207 ? 146.192 101.491 122.829 1.00 29.56 ?  186 GLN D N     1 
ATOM   14876 C  CA    . GLN D 2 207 ? 144.865 101.290 122.237 1.00 29.17 ?  186 GLN D CA    1 
ATOM   14877 C  C     . GLN D 2 207 ? 144.030 100.347 123.098 1.00 28.26 ?  186 GLN D C     1 
ATOM   14878 O  O     . GLN D 2 207 ? 142.878 100.645 123.402 1.00 27.98 ?  186 GLN D O     1 
ATOM   14879 C  CB    . GLN D 2 207 ? 144.965 100.760 120.797 1.00 29.80 ?  186 GLN D CB    1 
ATOM   14880 C  CG    . GLN D 2 207 ? 145.831 101.605 119.865 1.00 31.75 ?  186 GLN D CG    1 
ATOM   14881 C  CD    . GLN D 2 207 ? 145.438 103.068 119.887 1.00 34.93 ?  186 GLN D CD    1 
ATOM   14882 O  OE1   . GLN D 2 207 ? 144.379 103.455 119.375 1.00 36.91 ?  186 GLN D OE1   1 
ATOM   14883 N  NE2   . GLN D 2 207 ? 146.285 103.892 120.494 1.00 36.09 ?  186 GLN D NE2   1 
ATOM   14884 N  N     . SER D 2 208 ? 144.610 99.215  123.490 0.50 27.75 ?  187 SER D N     1 
ATOM   14885 C  CA    . SER D 2 208 ? 143.914 98.275  124.360 0.50 27.12 ?  187 SER D CA    1 
ATOM   14886 C  C     . SER D 2 208 ? 143.759 98.850  125.765 0.50 26.72 ?  187 SER D C     1 
ATOM   14887 O  O     . SER D 2 208 ? 142.772 98.564  126.440 0.50 26.30 ?  187 SER D O     1 
ATOM   14888 C  CB    . SER D 2 208 ? 144.630 96.924  124.403 0.50 26.88 ?  187 SER D CB    1 
ATOM   14889 O  OG    . SER D 2 208 ? 145.996 97.093  124.713 0.50 26.59 ?  187 SER D OG    1 
ATOM   14890 N  N     . GLY D 2 209 ? 144.731 99.658  126.190 1.00 26.64 ?  188 GLY D N     1 
ATOM   14891 C  CA    . GLY D 2 209 ? 144.659 100.361 127.487 1.00 26.43 ?  188 GLY D CA    1 
ATOM   14892 C  C     . GLY D 2 209 ? 143.532 101.385 127.535 1.00 26.66 ?  188 GLY D C     1 
ATOM   14893 O  O     . GLY D 2 209 ? 142.892 101.574 128.569 1.00 26.57 ?  188 GLY D O     1 
ATOM   14894 N  N     . GLU D 2 210 ? 143.290 102.056 126.412 1.00 27.42 ?  189 GLU D N     1 
ATOM   14895 C  CA    . GLU D 2 210 ? 142.163 102.981 126.303 1.00 27.73 ?  189 GLU D CA    1 
ATOM   14896 C  C     . GLU D 2 210 ? 140.841 102.209 126.432 1.00 27.04 ?  189 GLU D C     1 
ATOM   14897 O  O     . GLU D 2 210 ? 139.946 102.615 127.174 1.00 26.57 ?  189 GLU D O     1 
ATOM   14898 C  CB    . GLU D 2 210 ? 142.222 103.779 124.989 1.00 28.28 ?  189 GLU D CB    1 
ATOM   14899 C  CG    . GLU D 2 210 ? 141.115 104.839 124.867 1.00 30.71 ?  189 GLU D CG    1 
ATOM   14900 C  CD    . GLU D 2 210 ? 141.303 105.814 123.707 1.00 35.43 ?  189 GLU D CD    1 
ATOM   14901 O  OE1   . GLU D 2 210 ? 142.209 105.613 122.860 1.00 36.89 ?  189 GLU D OE1   1 
ATOM   14902 O  OE2   . GLU D 2 210 ? 140.535 106.802 123.652 1.00 37.04 -1 189 GLU D OE2   1 
ATOM   14903 N  N     . ILE D 2 211 ? 140.734 101.094 125.716 1.00 26.80 ?  190 ILE D N     1 
ATOM   14904 C  CA    . ILE D 2 211 ? 139.572 100.218 125.836 1.00 26.92 ?  190 ILE D CA    1 
ATOM   14905 C  C     . ILE D 2 211 ? 139.365 99.771  127.277 1.00 26.45 ?  190 ILE D C     1 
ATOM   14906 O  O     . ILE D 2 211 ? 138.251 99.855  127.789 1.00 26.65 ?  190 ILE D O     1 
ATOM   14907 C  CB    . ILE D 2 211 ? 139.655 99.002  124.878 1.00 27.00 ?  190 ILE D CB    1 
ATOM   14908 C  CG1   . ILE D 2 211 ? 139.479 99.477  123.430 1.00 28.77 ?  190 ILE D CG1   1 
ATOM   14909 C  CG2   . ILE D 2 211 ? 138.583 97.956  125.229 1.00 26.82 ?  190 ILE D CG2   1 
ATOM   14910 C  CD1   . ILE D 2 211 ? 139.692 98.403  122.371 1.00 30.88 ?  190 ILE D CD1   1 
ATOM   14911 N  N     . ILE D 2 212 ? 140.436 99.326  127.941 1.00 26.49 ?  191 ILE D N     1 
ATOM   14912 C  CA    . ILE D 2 212 ? 140.320 98.834  129.314 1.00 25.73 ?  191 ILE D CA    1 
ATOM   14913 C  C     . ILE D 2 212 ? 139.854 99.947  130.254 1.00 25.48 ?  191 ILE D C     1 
ATOM   14914 O  O     . ILE D 2 212 ? 139.034 99.716  131.147 1.00 24.95 ?  191 ILE D O     1 
ATOM   14915 C  CB    . ILE D 2 212 ? 141.639 98.180  129.824 1.00 26.44 ?  191 ILE D CB    1 
ATOM   14916 C  CG1   . ILE D 2 212 ? 141.962 96.909  129.028 1.00 26.71 ?  191 ILE D CG1   1 
ATOM   14917 C  CG2   . ILE D 2 212 ? 141.565 97.880  131.338 1.00 26.01 ?  191 ILE D CG2   1 
ATOM   14918 C  CD1   . ILE D 2 212 ? 140.945 95.787  129.131 1.00 30.50 ?  191 ILE D CD1   1 
ATOM   14919 N  N     . ASN D 2 213 ? 140.361 101.156 130.029 1.00 24.79 ?  192 ASN D N     1 
ATOM   14920 C  CA    . ASN D 2 213 ? 139.966 102.306 130.830 1.00 24.80 ?  192 ASN D CA    1 
ATOM   14921 C  C     . ASN D 2 213 ? 138.464 102.635 130.693 1.00 24.44 ?  192 ASN D C     1 
ATOM   14922 O  O     . ASN D 2 213 ? 137.822 103.064 131.659 1.00 23.25 ?  192 ASN D O     1 
ATOM   14923 C  CB    . ASN D 2 213 ? 140.834 103.516 130.479 1.00 25.68 ?  192 ASN D CB    1 
ATOM   14924 C  CG    . ASN D 2 213 ? 141.171 104.364 131.690 1.00 27.89 ?  192 ASN D CG    1 
ATOM   14925 O  OD1   . ASN D 2 213 ? 141.276 103.867 132.808 1.00 31.05 ?  192 ASN D OD1   1 
ATOM   14926 N  ND2   . ASN D 2 213 ? 141.349 105.659 131.467 1.00 31.70 ?  192 ASN D ND2   1 
ATOM   14927 N  N     . LEU D 2 214 ? 137.910 102.417 129.500 1.00 23.60 ?  193 LEU D N     1 
ATOM   14928 C  CA    . LEU D 2 214 ? 136.484 102.653 129.269 1.00 23.84 ?  193 LEU D CA    1 
ATOM   14929 C  C     . LEU D 2 214 ? 135.658 101.586 129.964 1.00 23.48 ?  193 LEU D C     1 
ATOM   14930 O  O     . LEU D 2 214 ? 134.627 101.891 130.571 1.00 24.12 ?  193 LEU D O     1 
ATOM   14931 C  CB    . LEU D 2 214 ? 136.173 102.674 127.773 1.00 23.71 ?  193 LEU D CB    1 
ATOM   14932 C  CG    . LEU D 2 214 ? 136.641 103.926 127.018 1.00 25.29 ?  193 LEU D CG    1 
ATOM   14933 C  CD1   . LEU D 2 214 ? 136.407 103.763 125.516 1.00 25.41 ?  193 LEU D CD1   1 
ATOM   14934 C  CD2   . LEU D 2 214 ? 135.950 105.180 127.528 1.00 25.80 ?  193 LEU D CD2   1 
ATOM   14935 N  N     . ILE D 2 215 ? 136.125 100.340 129.879 1.00 22.89 ?  194 ILE D N     1 
ATOM   14936 C  CA    . ILE D 2 215 ? 135.483 99.222  130.554 1.00 22.25 ?  194 ILE D CA    1 
ATOM   14937 C  C     . ILE D 2 215 ? 135.484 99.478  132.057 1.00 22.55 ?  194 ILE D C     1 
ATOM   14938 O  O     . ILE D 2 215 ? 134.440 99.389  132.719 1.00 22.53 ?  194 ILE D O     1 
ATOM   14939 C  CB    . ILE D 2 215 ? 136.192 97.886  130.254 1.00 22.37 ?  194 ILE D CB    1 
ATOM   14940 C  CG1   . ILE D 2 215 ? 136.027 97.515  128.774 1.00 21.89 ?  194 ILE D CG1   1 
ATOM   14941 C  CG2   . ILE D 2 215 ? 135.670 96.774  131.186 1.00 20.25 ?  194 ILE D CG2   1 
ATOM   14942 C  CD1   . ILE D 2 215 ? 136.711 96.204  128.368 1.00 20.48 ?  194 ILE D CD1   1 
ATOM   14943 N  N     . LEU D 2 216 ? 136.656 99.814  132.589 1.00 22.35 ?  195 LEU D N     1 
ATOM   14944 C  CA    . LEU D 2 216 ? 136.816 100.039 134.023 1.00 22.51 ?  195 LEU D CA    1 
ATOM   14945 C  C     . LEU D 2 216 ? 135.880 101.155 134.497 1.00 22.30 ?  195 LEU D C     1 
ATOM   14946 O  O     . LEU D 2 216 ? 135.267 101.037 135.566 1.00 21.62 ?  195 LEU D O     1 
ATOM   14947 C  CB    . LEU D 2 216 ? 138.282 100.382 134.330 1.00 23.06 ?  195 LEU D CB    1 
ATOM   14948 C  CG    . LEU D 2 216 ? 138.786 100.797 135.721 1.00 23.98 ?  195 LEU D CG    1 
ATOM   14949 C  CD1   . LEU D 2 216 ? 140.287 100.670 135.732 1.00 24.44 ?  195 LEU D CD1   1 
ATOM   14950 C  CD2   . LEU D 2 216 ? 138.386 102.236 136.083 1.00 25.00 ?  195 LEU D CD2   1 
ATOM   14951 N  N     . ARG D 2 217 ? 135.783 102.228 133.705 1.00 21.64 ?  196 ARG D N     1 
ATOM   14952 C  CA    . ARG D 2 217 ? 134.885 103.346 134.019 1.00 22.49 ?  196 ARG D CA    1 
ATOM   14953 C  C     . ARG D 2 217 ? 133.408 102.888 134.097 1.00 21.56 ?  196 ARG D C     1 
ATOM   14954 O  O     . ARG D 2 217 ? 132.673 103.343 134.964 1.00 21.32 ?  196 ARG D O     1 
ATOM   14955 C  CB    . ARG D 2 217 ? 135.065 104.523 133.040 1.00 23.07 ?  196 ARG D CB    1 
ATOM   14956 C  CG    . ARG D 2 217 ? 134.274 105.791 133.428 1.00 25.64 ?  196 ARG D CG    1 
ATOM   14957 C  CD    . ARG D 2 217 ? 134.289 106.872 132.332 1.00 32.11 ?  196 ARG D CD    1 
ATOM   14958 N  NE    . ARG D 2 217 ? 133.727 106.390 131.063 1.00 35.06 ?  196 ARG D NE    1 
ATOM   14959 C  CZ    . ARG D 2 217 ? 133.421 107.163 130.026 1.00 37.65 ?  196 ARG D CZ    1 
ATOM   14960 N  NH1   . ARG D 2 217 ? 133.593 108.479 130.094 1.00 40.20 1  196 ARG D NH1   1 
ATOM   14961 N  NH2   . ARG D 2 217 ? 132.927 106.621 128.916 1.00 38.20 ?  196 ARG D NH2   1 
ATOM   14962 N  N     . ASP D 2 218 ? 132.986 101.993 133.202 1.00 21.34 ?  197 ASP D N     1 
ATOM   14963 C  CA    . ASP D 2 218 ? 131.659 101.367 133.305 1.00 21.09 ?  197 ASP D CA    1 
ATOM   14964 C  C     . ASP D 2 218 ? 131.522 100.516 134.584 1.00 20.65 ?  197 ASP D C     1 
ATOM   14965 O  O     . ASP D 2 218 ? 130.521 100.630 135.296 1.00 20.16 ?  197 ASP D O     1 
ATOM   14966 C  CB    . ASP D 2 218 ? 131.347 100.501 132.075 1.00 21.58 ?  197 ASP D CB    1 
ATOM   14967 C  CG    . ASP D 2 218 ? 131.188 101.315 130.791 1.00 22.60 ?  197 ASP D CG    1 
ATOM   14968 O  OD1   . ASP D 2 218 ? 130.877 102.528 130.856 1.00 24.72 ?  197 ASP D OD1   1 
ATOM   14969 O  OD2   . ASP D 2 218 ? 131.390 100.728 129.703 1.00 22.64 -1 197 ASP D OD2   1 
ATOM   14970 N  N     . GLU D 2 219 ? 132.507 99.667  134.882 1.00 20.59 ?  198 GLU D N     1 
ATOM   14971 C  CA    . GLU D 2 219 ? 132.403 98.798  136.075 1.00 20.66 ?  198 GLU D CA    1 
ATOM   14972 C  C     . GLU D 2 219 ? 132.328 99.616  137.368 1.00 20.45 ?  198 GLU D C     1 
ATOM   14973 O  O     . GLU D 2 219 ? 131.615 99.240  138.304 1.00 20.59 ?  198 GLU D O     1 
ATOM   14974 C  CB    . GLU D 2 219 ? 133.544 97.771  136.160 1.00 20.55 ?  198 GLU D CB    1 
ATOM   14975 C  CG    . GLU D 2 219 ? 133.943 97.071  134.823 1.00 21.99 ?  198 GLU D CG    1 
ATOM   14976 C  CD    . GLU D 2 219 ? 132.832 96.255  134.150 1.00 24.00 ?  198 GLU D CD    1 
ATOM   14977 O  OE1   . GLU D 2 219 ? 131.627 96.508  134.362 1.00 25.06 ?  198 GLU D OE1   1 
ATOM   14978 O  OE2   . GLU D 2 219 ? 133.169 95.355  133.363 1.00 24.49 -1 198 GLU D OE2   1 
ATOM   14979 N  N     . ALA D 2 220 ? 133.046 100.735 137.407 1.00 20.47 ?  199 ALA D N     1 
ATOM   14980 C  CA    . ALA D 2 220 ? 132.995 101.654 138.564 1.00 21.10 ?  199 ALA D CA    1 
ATOM   14981 C  C     . ALA D 2 220 ? 131.576 102.138 138.850 1.00 21.34 ?  199 ALA D C     1 
ATOM   14982 O  O     . ALA D 2 220 ? 131.088 101.982 139.967 1.00 21.19 ?  199 ALA D O     1 
ATOM   14983 C  CB    . ALA D 2 220 ? 133.951 102.835 138.381 1.00 21.09 ?  199 ALA D CB    1 
ATOM   14984 N  N     . ILE D 2 221 ? 130.909 102.695 137.836 1.00 21.31 ?  200 ILE D N     1 
ATOM   14985 C  CA    . ILE D 2 221 ? 129.517 103.107 137.998 1.00 21.80 ?  200 ILE D CA    1 
ATOM   14986 C  C     . ILE D 2 221 ? 128.552 101.932 138.266 1.00 20.90 ?  200 ILE D C     1 
ATOM   14987 O  O     . ILE D 2 221 ? 127.613 102.078 139.048 1.00 20.54 ?  200 ILE D O     1 
ATOM   14988 C  CB    . ILE D 2 221 ? 129.021 104.044 136.859 1.00 22.75 ?  200 ILE D CB    1 
ATOM   14989 C  CG1   . ILE D 2 221 ? 127.746 104.755 137.297 1.00 24.63 ?  200 ILE D CG1   1 
ATOM   14990 C  CG2   . ILE D 2 221 ? 128.759 103.275 135.565 1.00 23.38 ?  200 ILE D CG2   1 
ATOM   14991 C  CD1   . ILE D 2 221 ? 127.463 106.022 136.544 1.00 26.91 ?  200 ILE D CD1   1 
ATOM   14992 N  N     . HIS D 2 222 ? 128.801 100.766 137.660 1.00 20.31 ?  201 HIS D N     1 
ATOM   14993 C  CA    . HIS D 2 222 ? 127.993 99.581  137.964 1.00 20.25 ?  201 HIS D CA    1 
ATOM   14994 C  C     . HIS D 2 222 ? 128.079 99.249  139.452 1.00 20.51 ?  201 HIS D C     1 
ATOM   14995 O  O     . HIS D 2 222 ? 127.054 99.062  140.118 1.00 20.99 ?  201 HIS D O     1 
ATOM   14996 C  CB    . HIS D 2 222 ? 128.415 98.362  137.136 1.00 19.79 ?  201 HIS D CB    1 
ATOM   14997 C  CG    . HIS D 2 222 ? 128.258 98.527  135.656 1.00 19.25 ?  201 HIS D CG    1 
ATOM   14998 N  ND1   . HIS D 2 222 ? 128.735 97.594  134.760 1.00 18.35 ?  201 HIS D ND1   1 
ATOM   14999 C  CD2   . HIS D 2 222 ? 127.695 99.512  134.911 1.00 17.64 ?  201 HIS D CD2   1 
ATOM   15000 C  CE1   . HIS D 2 222 ? 128.462 97.985  133.528 1.00 18.28 ?  201 HIS D CE1   1 
ATOM   15001 N  NE2   . HIS D 2 222 ? 127.839 99.150  133.591 1.00 20.01 ?  201 HIS D NE2   1 
ATOM   15002 N  N     . GLY D 2 223 ? 129.306 99.200  139.974 1.00 20.33 ?  202 GLY D N     1 
ATOM   15003 C  CA    . GLY D 2 223 ? 129.546 98.938  141.399 1.00 19.94 ?  202 GLY D CA    1 
ATOM   15004 C  C     . GLY D 2 223 ? 128.872 99.941  142.328 1.00 19.80 ?  202 GLY D C     1 
ATOM   15005 O  O     . GLY D 2 223 ? 128.253 99.549  143.316 1.00 19.96 ?  202 GLY D O     1 
ATOM   15006 N  N     . VAL D 2 224 ? 128.961 101.232 142.001 1.00 19.49 ?  203 VAL D N     1 
ATOM   15007 C  CA    . VAL D 2 224 ? 128.311 102.276 142.811 1.00 18.88 ?  203 VAL D CA    1 
ATOM   15008 C  C     . VAL D 2 224 ? 126.784 102.122 142.821 1.00 18.55 ?  203 VAL D C     1 
ATOM   15009 O  O     . VAL D 2 224 ? 126.141 102.212 143.880 1.00 17.65 ?  203 VAL D O     1 
ATOM   15010 C  CB    . VAL D 2 224 ? 128.717 103.725 142.354 1.00 19.22 ?  203 VAL D CB    1 
ATOM   15011 C  CG1   . VAL D 2 224 ? 127.996 104.792 143.203 1.00 18.51 ?  203 VAL D CG1   1 
ATOM   15012 C  CG2   . VAL D 2 224 ? 130.244 103.920 142.444 1.00 19.69 ?  203 VAL D CG2   1 
ATOM   15013 N  N     . TYR D 2 225 ? 126.213 101.862 141.647 1.00 18.17 ?  204 TYR D N     1 
ATOM   15014 C  CA    . TYR D 2 225 ? 124.762 101.724 141.498 1.00 18.76 ?  204 TYR D CA    1 
ATOM   15015 C  C     . TYR D 2 225 ? 124.219 100.503 142.259 1.00 18.93 ?  204 TYR D C     1 
ATOM   15016 O  O     . TYR D 2 225 ? 123.288 100.620 143.067 1.00 18.77 ?  204 TYR D O     1 
ATOM   15017 C  CB    . TYR D 2 225 ? 124.358 101.661 140.011 1.00 18.96 ?  204 TYR D CB    1 
ATOM   15018 C  CG    . TYR D 2 225 ? 122.844 101.655 139.835 1.00 20.06 ?  204 TYR D CG    1 
ATOM   15019 C  CD1   . TYR D 2 225 ? 122.082 102.779 140.182 1.00 21.79 ?  204 TYR D CD1   1 
ATOM   15020 C  CD2   . TYR D 2 225 ? 122.174 100.525 139.357 1.00 19.51 ?  204 TYR D CD2   1 
ATOM   15021 C  CE1   . TYR D 2 225 ? 120.692 102.778 140.053 1.00 20.38 ?  204 TYR D CE1   1 
ATOM   15022 C  CE2   . TYR D 2 225 ? 120.768 100.518 139.217 1.00 19.38 ?  204 TYR D CE2   1 
ATOM   15023 C  CZ    . TYR D 2 225 ? 120.044 101.652 139.574 1.00 20.84 ?  204 TYR D CZ    1 
ATOM   15024 O  OH    . TYR D 2 225 ? 118.672 101.677 139.466 1.00 20.77 ?  204 TYR D OH    1 
ATOM   15025 N  N     . VAL D 2 226 ? 124.805 99.334  142.009 1.00 18.76 ?  205 VAL D N     1 
ATOM   15026 C  CA    . VAL D 2 226 ? 124.383 98.125  142.712 1.00 18.85 ?  205 VAL D CA    1 
ATOM   15027 C  C     . VAL D 2 226 ? 124.583 98.301  144.217 1.00 19.19 ?  205 VAL D C     1 
ATOM   15028 O  O     . VAL D 2 226 ? 123.761 97.833  145.006 1.00 19.87 ?  205 VAL D O     1 
ATOM   15029 C  CB    . VAL D 2 226 ? 125.098 96.875  142.186 1.00 19.28 ?  205 VAL D CB    1 
ATOM   15030 C  CG1   . VAL D 2 226 ? 124.682 95.615  142.993 1.00 18.22 ?  205 VAL D CG1   1 
ATOM   15031 C  CG2   . VAL D 2 226 ? 124.775 96.705  140.692 1.00 18.40 ?  205 VAL D CG2   1 
ATOM   15032 N  N     . GLY D 2 227 ? 125.654 98.999  144.599 1.00 18.53 ?  206 GLY D N     1 
ATOM   15033 C  CA    . GLY D 2 227 ? 125.899 99.349  146.011 1.00 18.74 ?  206 GLY D CA    1 
ATOM   15034 C  C     . GLY D 2 227 ? 124.767 100.123 146.665 1.00 19.17 ?  206 GLY D C     1 
ATOM   15035 O  O     . GLY D 2 227 ? 124.414 99.871  147.826 1.00 18.66 ?  206 GLY D O     1 
ATOM   15036 N  N     . LEU D 2 228 ? 124.205 101.082 145.931 1.00 19.00 ?  207 LEU D N     1 
ATOM   15037 C  CA    . LEU D 2 228 ? 123.079 101.864 146.444 1.00 19.73 ?  207 LEU D CA    1 
ATOM   15038 C  C     . LEU D 2 228 ? 121.827 100.990 146.601 1.00 19.76 ?  207 LEU D C     1 
ATOM   15039 O  O     . LEU D 2 228 ? 121.105 101.116 147.590 1.00 20.07 ?  207 LEU D O     1 
ATOM   15040 C  CB    . LEU D 2 228 ? 122.813 103.083 145.559 1.00 19.36 ?  207 LEU D CB    1 
ATOM   15041 C  CG    . LEU D 2 228 ? 123.888 104.180 145.608 1.00 20.50 ?  207 LEU D CG    1 
ATOM   15042 C  CD1   . LEU D 2 228 ? 123.662 105.200 144.507 1.00 19.87 ?  207 LEU D CD1   1 
ATOM   15043 C  CD2   . LEU D 2 228 ? 123.930 104.878 146.998 1.00 22.38 ?  207 LEU D CD2   1 
ATOM   15044 N  N     . LEU D 2 229 ? 121.598 100.080 145.655 1.00 19.27 ?  208 LEU D N     1 
ATOM   15045 C  CA    . LEU D 2 229 ? 120.489 99.114  145.770 1.00 19.47 ?  208 LEU D CA    1 
ATOM   15046 C  C     . LEU D 2 229 ? 120.644 98.172  146.970 1.00 19.67 ?  208 LEU D C     1 
ATOM   15047 O  O     . LEU D 2 229 ? 119.652 97.811  147.616 1.00 19.82 ?  208 LEU D O     1 
ATOM   15048 C  CB    . LEU D 2 229 ? 120.327 98.294  144.473 1.00 19.51 ?  208 LEU D CB    1 
ATOM   15049 C  CG    . LEU D 2 229 ? 120.004 99.016  143.155 1.00 19.48 ?  208 LEU D CG    1 
ATOM   15050 C  CD1   . LEU D 2 229 ? 120.045 98.023  141.980 1.00 20.14 ?  208 LEU D CD1   1 
ATOM   15051 C  CD2   . LEU D 2 229 ? 118.658 99.774  143.192 1.00 19.95 ?  208 LEU D CD2   1 
ATOM   15052 N  N     . ALA D 2 230 ? 121.880 97.766  147.264 1.00 19.43 ?  209 ALA D N     1 
ATOM   15053 C  CA    . ALA D 2 230 ? 122.166 96.945  148.448 1.00 20.29 ?  209 ALA D CA    1 
ATOM   15054 C  C     . ALA D 2 230 ? 121.933 97.711  149.752 1.00 21.17 ?  209 ALA D C     1 
ATOM   15055 O  O     . ALA D 2 230 ? 121.351 97.174  150.689 1.00 21.73 ?  209 ALA D O     1 
ATOM   15056 C  CB    . ALA D 2 230 ? 123.591 96.400  148.393 1.00 19.99 ?  209 ALA D CB    1 
ATOM   15057 N  N     . GLN D 2 231 ? 122.382 98.964  149.808 1.00 22.26 ?  210 GLN D N     1 
ATOM   15058 C  CA    . GLN D 2 231 ? 122.162 99.818  150.991 1.00 23.33 ?  210 GLN D CA    1 
ATOM   15059 C  C     . GLN D 2 231 ? 120.672 100.034 151.275 1.00 23.85 ?  210 GLN D C     1 
ATOM   15060 O  O     . GLN D 2 231 ? 120.260 100.077 152.431 1.00 24.91 ?  210 GLN D O     1 
ATOM   15061 C  CB    . GLN D 2 231 ? 122.849 101.178 150.832 1.00 23.49 ?  210 GLN D CB    1 
ATOM   15062 C  CG    . GLN D 2 231 ? 124.380 101.139 150.791 1.00 23.05 ?  210 GLN D CG    1 
ATOM   15063 C  CD    . GLN D 2 231 ? 124.980 102.531 150.603 1.00 24.65 ?  210 GLN D CD    1 
ATOM   15064 O  OE1   . GLN D 2 231 ? 124.639 103.459 151.336 1.00 25.85 ?  210 GLN D OE1   1 
ATOM   15065 N  NE2   . GLN D 2 231 ? 125.862 102.683 149.614 1.00 22.30 ?  210 GLN D NE2   1 
ATOM   15066 N  N     . GLU D 2 232 ? 119.875 100.186 150.221 1.00 24.36 ?  211 GLU D N     1 
ATOM   15067 C  CA    . GLU D 2 232 ? 118.423 100.271 150.358 1.00 24.83 ?  211 GLU D CA    1 
ATOM   15068 C  C     . GLU D 2 232 ? 117.846 99.061  151.100 1.00 24.34 ?  211 GLU D C     1 
ATOM   15069 O  O     . GLU D 2 232 ? 117.021 99.225  152.001 1.00 24.20 ?  211 GLU D O     1 
ATOM   15070 C  CB    . GLU D 2 232 ? 117.761 100.408 148.992 1.00 25.15 ?  211 GLU D CB    1 
ATOM   15071 C  CG    . GLU D 2 232 ? 116.298 100.763 149.053 1.00 28.55 ?  211 GLU D CG    1 
ATOM   15072 C  CD    . GLU D 2 232 ? 115.711 100.908 147.676 1.00 33.83 ?  211 GLU D CD    1 
ATOM   15073 O  OE1   . GLU D 2 232 ? 115.710 102.044 147.160 1.00 35.09 ?  211 GLU D OE1   1 
ATOM   15074 O  OE2   . GLU D 2 232 ? 115.294 99.882  147.094 1.00 35.51 -1 211 GLU D OE2   1 
ATOM   15075 N  N     . ILE D 2 233 ? 118.280 97.856  150.731 1.00 23.39 ?  212 ILE D N     1 
ATOM   15076 C  CA    . ILE D 2 233 ? 117.847 96.636  151.434 1.00 23.42 ?  212 ILE D CA    1 
ATOM   15077 C  C     . ILE D 2 233 ? 118.375 96.615  152.869 1.00 23.74 ?  212 ILE D C     1 
ATOM   15078 O  O     . ILE D 2 233 ? 117.621 96.384  153.813 1.00 24.61 ?  212 ILE D O     1 
ATOM   15079 C  CB    . ILE D 2 233 ? 118.249 95.342  150.676 1.00 22.81 ?  212 ILE D CB    1 
ATOM   15080 C  CG1   . ILE D 2 233 ? 117.499 95.249  149.339 1.00 22.94 ?  212 ILE D CG1   1 
ATOM   15081 C  CG2   . ILE D 2 233 ? 117.953 94.096  151.522 1.00 22.45 ?  212 ILE D CG2   1 
ATOM   15082 C  CD1   . ILE D 2 233 ? 118.078 94.201  148.364 1.00 22.21 ?  212 ILE D CD1   1 
ATOM   15083 N  N     . TYR D 2 234 ? 119.669 96.878  153.028 1.00 24.19 ?  213 TYR D N     1 
ATOM   15084 C  CA    . TYR D 2 234 ? 120.320 96.906  154.330 1.00 24.59 ?  213 TYR D CA    1 
ATOM   15085 C  C     . TYR D 2 234 ? 119.586 97.825  155.312 1.00 25.15 ?  213 TYR D C     1 
ATOM   15086 O  O     . TYR D 2 234 ? 119.396 97.462  156.476 1.00 24.94 ?  213 TYR D O     1 
ATOM   15087 C  CB    . TYR D 2 234 ? 121.773 97.363  154.170 1.00 24.41 ?  213 TYR D CB    1 
ATOM   15088 C  CG    . TYR D 2 234 ? 122.566 97.453  155.457 1.00 25.93 ?  213 TYR D CG    1 
ATOM   15089 C  CD1   . TYR D 2 234 ? 123.206 96.335  155.979 1.00 24.70 ?  213 TYR D CD1   1 
ATOM   15090 C  CD2   . TYR D 2 234 ? 122.682 98.667  156.148 1.00 26.11 ?  213 TYR D CD2   1 
ATOM   15091 C  CE1   . TYR D 2 234 ? 123.942 96.412  157.157 1.00 27.90 ?  213 TYR D CE1   1 
ATOM   15092 C  CE2   . TYR D 2 234 ? 123.420 98.753  157.321 1.00 27.70 ?  213 TYR D CE2   1 
ATOM   15093 C  CZ    . TYR D 2 234 ? 124.048 97.625  157.818 1.00 27.89 ?  213 TYR D CZ    1 
ATOM   15094 O  OH    . TYR D 2 234 ? 124.777 97.704  158.982 1.00 32.34 ?  213 TYR D OH    1 
ATOM   15095 N  N     . ASN D 2 235 ? 119.186 99.005  154.834 1.00 25.43 ?  214 ASN D N     1 
ATOM   15096 C  CA    . ASN D 2 235 ? 118.525 100.015 155.676 1.00 26.77 ?  214 ASN D CA    1 
ATOM   15097 C  C     . ASN D 2 235 ? 117.098 99.652  156.084 1.00 27.06 ?  214 ASN D C     1 
ATOM   15098 O  O     . ASN D 2 235 ? 116.518 100.288 156.959 1.00 27.42 ?  214 ASN D O     1 
ATOM   15099 C  CB    . ASN D 2 235 ? 118.510 101.384 154.991 1.00 26.80 ?  214 ASN D CB    1 
ATOM   15100 C  CG    . ASN D 2 235 ? 119.890 101.941 154.769 1.00 28.19 ?  214 ASN D CG    1 
ATOM   15101 O  OD1   . ASN D 2 235 ? 120.799 101.735 155.570 1.00 29.35 ?  214 ASN D OD1   1 
ATOM   15102 N  ND2   . ASN D 2 235 ? 120.053 102.667 153.675 1.00 30.84 ?  214 ASN D ND2   1 
ATOM   15103 N  N     . LYS D 2 236 ? 116.538 98.636  155.445 1.00 26.87 ?  215 LYS D N     1 
ATOM   15104 C  CA    . LYS D 2 236 ? 115.203 98.165  155.792 1.00 27.86 ?  215 LYS D CA    1 
ATOM   15105 C  C     . LYS D 2 236 ? 115.250 97.106  156.903 1.00 28.07 ?  215 LYS D C     1 
ATOM   15106 O  O     . LYS D 2 236 ? 114.210 96.632  157.357 1.00 28.22 ?  215 LYS D O     1 
ATOM   15107 C  CB    . LYS D 2 236 ? 114.492 97.613  154.555 1.00 27.52 ?  215 LYS D CB    1 
ATOM   15108 C  CG    . LYS D 2 236 ? 114.216 98.644  153.488 1.00 29.60 ?  215 LYS D CG    1 
ATOM   15109 C  CD    . LYS D 2 236 ? 113.031 98.253  152.620 1.00 34.24 ?  215 LYS D CD    1 
ATOM   15110 C  CE    . LYS D 2 236 ? 113.433 97.628  151.298 1.00 36.75 ?  215 LYS D CE    1 
ATOM   15111 N  NZ    . LYS D 2 236 ? 114.109 96.327  151.489 1.00 40.41 1  215 LYS D NZ    1 
ATOM   15112 N  N     . GLN D 2 237 ? 116.455 96.750  157.340 1.00 28.33 ?  216 GLN D N     1 
ATOM   15113 C  CA    . GLN D 2 237 ? 116.634 95.653  158.294 1.00 29.60 ?  216 GLN D CA    1 
ATOM   15114 C  C     . GLN D 2 237 ? 116.726 96.137  159.737 1.00 30.69 ?  216 GLN D C     1 
ATOM   15115 O  O     . GLN D 2 237 ? 117.046 97.303  159.991 1.00 30.85 ?  216 GLN D O     1 
ATOM   15116 C  CB    . GLN D 2 237 ? 117.887 94.820  157.953 1.00 29.08 ?  216 GLN D CB    1 
ATOM   15117 C  CG    . GLN D 2 237 ? 117.970 94.304  156.512 1.00 27.78 ?  216 GLN D CG    1 
ATOM   15118 C  CD    . GLN D 2 237 ? 116.701 93.608  156.046 1.00 28.38 ?  216 GLN D CD    1 
ATOM   15119 O  OE1   . GLN D 2 237 ? 116.187 92.715  156.717 1.00 29.30 ?  216 GLN D OE1   1 
ATOM   15120 N  NE2   . GLN D 2 237 ? 116.199 94.008  154.883 1.00 26.88 ?  216 GLN D NE2   1 
ATOM   15121 N  N     . THR D 2 238 ? 116.457 95.227  160.672 1.00 32.02 ?  217 THR D N     1 
ATOM   15122 C  CA    . THR D 2 238 ? 116.664 95.485  162.100 1.00 33.47 ?  217 THR D CA    1 
ATOM   15123 C  C     . THR D 2 238 ? 118.152 95.661  162.419 1.00 34.29 ?  217 THR D C     1 
ATOM   15124 O  O     . THR D 2 238 ? 119.024 95.387  161.577 1.00 33.78 ?  217 THR D O     1 
ATOM   15125 C  CB    . THR D 2 238 ? 116.094 94.333  162.974 1.00 34.00 ?  217 THR D CB    1 
ATOM   15126 O  OG1   . THR D 2 238 ? 116.838 93.129  162.734 1.00 34.33 ?  217 THR D OG1   1 
ATOM   15127 C  CG2   . THR D 2 238 ? 114.608 94.087  162.662 1.00 33.53 ?  217 THR D CG2   1 
ATOM   15128 N  N     . GLU D 2 239 ? 118.450 96.103  163.637 1.00 35.45 ?  218 GLU D N     1 
ATOM   15129 C  CA    . GLU D 2 239 ? 119.838 96.286  164.049 1.00 36.37 ?  218 GLU D CA    1 
ATOM   15130 C  C     . GLU D 2 239 ? 120.603 94.967  164.134 1.00 36.29 ?  218 GLU D C     1 
ATOM   15131 O  O     . GLU D 2 239 ? 121.770 94.902  163.736 1.00 36.18 ?  218 GLU D O     1 
ATOM   15132 C  CB    . GLU D 2 239 ? 119.930 97.074  165.359 1.00 37.27 ?  218 GLU D CB    1 
ATOM   15133 C  CG    . GLU D 2 239 ? 119.529 98.553  165.214 1.00 39.45 ?  218 GLU D CG    1 
ATOM   15134 C  CD    . GLU D 2 239 ? 120.336 99.298  164.153 1.00 41.22 ?  218 GLU D CD    1 
ATOM   15135 O  OE1   . GLU D 2 239 ? 121.580 99.165  164.129 1.00 42.62 ?  218 GLU D OE1   1 
ATOM   15136 O  OE2   . GLU D 2 239 ? 119.725 100.021 163.337 1.00 41.24 -1 218 GLU D OE2   1 
ATOM   15137 N  N     . GLU D 2 240 ? 119.946 93.921  164.630 1.00 36.66 ?  219 GLU D N     1 
ATOM   15138 C  CA    . GLU D 2 240 ? 120.570 92.599  164.714 1.00 37.01 ?  219 GLU D CA    1 
ATOM   15139 C  C     . GLU D 2 240 ? 120.827 92.026  163.320 1.00 35.85 ?  219 GLU D C     1 
ATOM   15140 O  O     . GLU D 2 240 ? 121.889 91.447  163.074 1.00 35.62 ?  219 GLU D O     1 
ATOM   15141 C  CB    . GLU D 2 240 ? 119.724 91.622  165.545 1.00 37.98 ?  219 GLU D CB    1 
ATOM   15142 C  CG    . GLU D 2 240 ? 120.399 90.256  165.741 1.00 40.87 ?  219 GLU D CG    1 
ATOM   15143 C  CD    . GLU D 2 240 ? 119.577 89.257  166.553 1.00 44.58 ?  219 GLU D CD    1 
ATOM   15144 O  OE1   . GLU D 2 240 ? 120.198 88.359  167.172 1.00 45.86 ?  219 GLU D OE1   1 
ATOM   15145 O  OE2   . GLU D 2 240 ? 118.326 89.359  166.573 1.00 45.75 -1 219 GLU D OE2   1 
ATOM   15146 N  N     . LYS D 2 241 ? 119.852 92.190  162.426 1.00 34.54 ?  220 LYS D N     1 
ATOM   15147 C  CA    . LYS D 2 241 ? 119.973 91.722  161.043 1.00 33.65 ?  220 LYS D CA    1 
ATOM   15148 C  C     . LYS D 2 241 ? 121.066 92.495  160.294 1.00 32.67 ?  220 LYS D C     1 
ATOM   15149 O  O     . LYS D 2 241 ? 121.801 91.905  159.508 1.00 32.05 ?  220 LYS D O     1 
ATOM   15150 C  CB    . LYS D 2 241 ? 118.629 91.813  160.312 1.00 33.30 ?  220 LYS D CB    1 
ATOM   15151 C  CG    . LYS D 2 241 ? 118.600 91.200  158.899 1.00 34.50 ?  220 LYS D CG    1 
ATOM   15152 C  CD    . LYS D 2 241 ? 118.923 89.701  158.887 1.00 36.30 ?  220 LYS D CD    1 
ATOM   15153 C  CE    . LYS D 2 241 ? 117.797 88.873  159.496 1.00 38.44 ?  220 LYS D CE    1 
ATOM   15154 N  NZ    . LYS D 2 241 ? 118.298 87.560  159.984 1.00 39.28 1  220 LYS D NZ    1 
ATOM   15155 N  N     . LYS D 2 242 ? 121.163 93.804  160.549 1.00 31.90 ?  221 LYS D N     1 
ATOM   15156 C  CA    . LYS D 2 242 ? 122.229 94.631  159.982 1.00 31.28 ?  221 LYS D CA    1 
ATOM   15157 C  C     . LYS D 2 242 ? 123.610 94.121  160.390 1.00 31.32 ?  221 LYS D C     1 
ATOM   15158 O  O     . LYS D 2 242 ? 124.470 93.937  159.537 1.00 30.72 ?  221 LYS D O     1 
ATOM   15159 C  CB    . LYS D 2 242 ? 122.078 96.103  160.393 1.00 31.38 ?  221 LYS D CB    1 
ATOM   15160 C  CG    . LYS D 2 242 ? 121.085 96.901  159.554 1.00 30.64 ?  221 LYS D CG    1 
ATOM   15161 C  CD    . LYS D 2 242 ? 121.023 98.348  160.040 1.00 32.51 ?  221 LYS D CD    1 
ATOM   15162 C  CE    . LYS D 2 242 ? 120.065 99.165  159.201 1.00 32.66 ?  221 LYS D CE    1 
ATOM   15163 N  NZ    . LYS D 2 242 ? 119.823 100.490 159.815 1.00 35.31 1  221 LYS D NZ    1 
ATOM   15164 N  N     . ALA D 2 243 ? 123.813 93.901  161.693 1.00 31.62 ?  222 ALA D N     1 
ATOM   15165 C  CA    . ALA D 2 243 ? 125.079 93.370  162.211 1.00 31.66 ?  222 ALA D CA    1 
ATOM   15166 C  C     . ALA D 2 243 ? 125.448 92.031  161.561 1.00 31.52 ?  222 ALA D C     1 
ATOM   15167 O  O     . ALA D 2 243 ? 126.623 91.752  161.304 1.00 31.41 ?  222 ALA D O     1 
ATOM   15168 C  CB    . ALA D 2 243 ? 125.020 93.240  163.737 1.00 31.89 ?  222 ALA D CB    1 
ATOM   15169 N  N     . GLU D 2 244 ? 124.426 91.227  161.283 1.00 31.35 ?  223 GLU D N     1 
ATOM   15170 C  CA    . GLU D 2 244 ? 124.567 89.927  160.648 1.00 31.54 ?  223 GLU D CA    1 
ATOM   15171 C  C     . GLU D 2 244 ? 124.963 90.057  159.159 1.00 30.63 ?  223 GLU D C     1 
ATOM   15172 O  O     . GLU D 2 244 ? 125.795 89.294  158.649 1.00 29.47 ?  223 GLU D O     1 
ATOM   15173 C  CB    . GLU D 2 244 ? 123.243 89.196  160.800 1.00 32.45 ?  223 GLU D CB    1 
ATOM   15174 C  CG    . GLU D 2 244 ? 123.239 87.729  160.496 1.00 35.31 ?  223 GLU D CG    1 
ATOM   15175 C  CD    . GLU D 2 244 ? 121.965 87.076  160.993 1.00 38.36 ?  223 GLU D CD    1 
ATOM   15176 O  OE1   . GLU D 2 244 ? 121.781 86.987  162.225 1.00 41.93 ?  223 GLU D OE1   1 
ATOM   15177 O  OE2   . GLU D 2 244 ? 121.139 86.659  160.157 1.00 39.37 -1 223 GLU D OE2   1 
ATOM   15178 N  N     . LEU D 2 245 ? 124.363 91.030  158.481 1.00 29.62 ?  224 LEU D N     1 
ATOM   15179 C  CA    . LEU D 2 245 ? 124.714 91.344  157.098 1.00 29.44 ?  224 LEU D CA    1 
ATOM   15180 C  C     . LEU D 2 245 ? 126.112 91.953  156.973 1.00 28.99 ?  224 LEU D C     1 
ATOM   15181 O  O     . LEU D 2 245 ? 126.808 91.688  155.997 1.00 28.63 ?  224 LEU D O     1 
ATOM   15182 C  CB    . LEU D 2 245 ? 123.662 92.263  156.468 1.00 29.06 ?  224 LEU D CB    1 
ATOM   15183 C  CG    . LEU D 2 245 ? 122.274 91.656  156.238 1.00 29.27 ?  224 LEU D CG    1 
ATOM   15184 C  CD1   . LEU D 2 245 ? 121.376 92.687  155.560 1.00 30.76 ?  224 LEU D CD1   1 
ATOM   15185 C  CD2   . LEU D 2 245 ? 122.338 90.385  155.398 1.00 28.11 ?  224 LEU D CD2   1 
ATOM   15186 N  N     . ARG D 2 246 ? 126.514 92.760  157.957 1.00 29.31 ?  225 ARG D N     1 
ATOM   15187 C  CA    . ARG D 2 246 ? 127.879 93.296  158.006 1.00 29.86 ?  225 ARG D CA    1 
ATOM   15188 C  C     . ARG D 2 246 ? 128.900 92.177  158.163 1.00 29.23 ?  225 ARG D C     1 
ATOM   15189 O  O     . ARG D 2 246 ? 129.922 92.172  157.490 1.00 28.95 ?  225 ARG D O     1 
ATOM   15190 C  CB    . ARG D 2 246 ? 128.067 94.292  159.155 1.00 30.56 ?  225 ARG D CB    1 
ATOM   15191 C  CG    . ARG D 2 246 ? 127.476 95.661  158.908 1.00 33.71 ?  225 ARG D CG    1 
ATOM   15192 C  CD    . ARG D 2 246 ? 128.128 96.748  159.785 1.00 37.42 ?  225 ARG D CD    1 
ATOM   15193 N  NE    . ARG D 2 246 ? 128.073 96.453  161.222 1.00 39.17 ?  225 ARG D NE    1 
ATOM   15194 C  CZ    . ARG D 2 246 ? 127.005 96.617  162.004 1.00 40.68 ?  225 ARG D CZ    1 
ATOM   15195 N  NH1   . ARG D 2 246 ? 125.855 97.068  161.509 1.00 40.28 1  225 ARG D NH1   1 
ATOM   15196 N  NH2   . ARG D 2 246 ? 127.086 96.314  163.295 1.00 41.65 ?  225 ARG D NH2   1 
ATOM   15197 N  N     . GLU D 2 247 ? 128.621 91.246  159.066 1.00 28.89 ?  226 GLU D N     1 
ATOM   15198 C  CA    . GLU D 2 247 ? 129.492 90.092  159.267 1.00 29.27 ?  226 GLU D CA    1 
ATOM   15199 C  C     . GLU D 2 247 ? 129.604 89.268  157.984 1.00 27.84 ?  226 GLU D C     1 
ATOM   15200 O  O     . GLU D 2 247 ? 130.706 88.849  157.623 1.00 27.37 ?  226 GLU D O     1 
ATOM   15201 C  CB    . GLU D 2 247 ? 129.014 89.226  160.446 1.00 30.21 ?  226 GLU D CB    1 
ATOM   15202 C  CG    . GLU D 2 247 ? 129.807 87.921  160.655 1.00 34.46 ?  226 GLU D CG    1 
ATOM   15203 C  CD    . GLU D 2 247 ? 131.293 88.157  160.909 1.00 40.77 ?  226 GLU D CD    1 
ATOM   15204 O  OE1   . GLU D 2 247 ? 131.627 88.792  161.937 1.00 44.03 ?  226 GLU D OE1   1 
ATOM   15205 O  OE2   . GLU D 2 247 ? 132.131 87.713  160.084 1.00 42.98 -1 226 GLU D OE2   1 
ATOM   15206 N  N     . PHE D 2 248 ? 128.476 89.055  157.300 1.00 26.73 ?  227 PHE D N     1 
ATOM   15207 C  CA    . PHE D 2 248 ? 128.474 88.377  155.998 1.00 26.15 ?  227 PHE D CA    1 
ATOM   15208 C  C     . PHE D 2 248 ? 129.412 89.065  155.002 1.00 25.33 ?  227 PHE D C     1 
ATOM   15209 O  O     . PHE D 2 248 ? 130.227 88.404  154.365 1.00 24.70 ?  227 PHE D O     1 
ATOM   15210 C  CB    . PHE D 2 248 ? 127.070 88.274  155.371 1.00 26.02 ?  227 PHE D CB    1 
ATOM   15211 C  CG    . PHE D 2 248 ? 127.095 87.927  153.883 1.00 25.61 ?  227 PHE D CG    1 
ATOM   15212 C  CD1   . PHE D 2 248 ? 127.160 86.602  153.463 1.00 26.51 ?  227 PHE D CD1   1 
ATOM   15213 C  CD2   . PHE D 2 248 ? 127.093 88.934  152.913 1.00 26.21 ?  227 PHE D CD2   1 
ATOM   15214 C  CE1   . PHE D 2 248 ? 127.209 86.275  152.107 1.00 26.16 ?  227 PHE D CE1   1 
ATOM   15215 C  CE2   . PHE D 2 248 ? 127.145 88.621  151.548 1.00 26.07 ?  227 PHE D CE2   1 
ATOM   15216 C  CZ    . PHE D 2 248 ? 127.206 87.283  151.148 1.00 25.82 ?  227 PHE D CZ    1 
ATOM   15217 N  N     . ALA D 2 249 ? 129.269 90.385  154.869 1.00 24.83 ?  228 ALA D N     1 
ATOM   15218 C  CA    . ALA D 2 249 ? 130.039 91.174  153.897 1.00 24.08 ?  228 ALA D CA    1 
ATOM   15219 C  C     . ALA D 2 249 ? 131.546 91.132  154.189 1.00 23.93 ?  228 ALA D C     1 
ATOM   15220 O  O     . ALA D 2 249 ? 132.358 90.974  153.275 1.00 22.51 ?  228 ALA D O     1 
ATOM   15221 C  CB    . ALA D 2 249 ? 129.542 92.624  153.887 1.00 24.18 ?  228 ALA D CB    1 
ATOM   15222 N  N     . ILE D 2 250 ? 131.908 91.282  155.464 1.00 24.20 ?  229 ILE D N     1 
ATOM   15223 C  CA    . ILE D 2 250 ? 133.313 91.264  155.873 1.00 24.86 ?  229 ILE D CA    1 
ATOM   15224 C  C     . ILE D 2 250 ? 133.915 89.864  155.706 1.00 24.68 ?  229 ILE D C     1 
ATOM   15225 O  O     . ILE D 2 250 ? 135.037 89.725  155.234 1.00 24.30 ?  229 ILE D O     1 
ATOM   15226 C  CB    . ILE D 2 250 ? 133.511 91.807  157.332 1.00 25.44 ?  229 ILE D CB    1 
ATOM   15227 C  CG1   . ILE D 2 250 ? 132.993 93.251  157.479 1.00 26.49 ?  229 ILE D CG1   1 
ATOM   15228 C  CG2   . ILE D 2 250 ? 134.977 91.713  157.777 1.00 27.13 ?  229 ILE D CG2   1 
ATOM   15229 C  CD1   . ILE D 2 250 ? 133.549 94.262  156.473 1.00 28.58 ?  229 ILE D CD1   1 
ATOM   15230 N  N     . ASP D 2 251 ? 133.161 88.834  156.090 1.00 24.90 ?  230 ASP D N     1 
ATOM   15231 C  CA    . ASP D 2 251 ? 133.594 87.450  155.932 1.00 25.04 ?  230 ASP D CA    1 
ATOM   15232 C  C     . ASP D 2 251 ? 133.831 87.115  154.448 1.00 24.25 ?  230 ASP D C     1 
ATOM   15233 O  O     . ASP D 2 251 ? 134.859 86.533  154.093 1.00 23.60 ?  230 ASP D O     1 
ATOM   15234 C  CB    . ASP D 2 251 ? 132.555 86.506  156.547 1.00 26.23 ?  230 ASP D CB    1 
ATOM   15235 C  CG    . ASP D 2 251 ? 132.868 85.045  156.309 1.00 28.91 ?  230 ASP D CG    1 
ATOM   15236 O  OD1   . ASP D 2 251 ? 133.861 84.533  156.868 1.00 32.03 ?  230 ASP D OD1   1 
ATOM   15237 O  OD2   . ASP D 2 251 ? 132.097 84.397  155.575 1.00 33.16 -1 230 ASP D OD2   1 
ATOM   15238 N  N     . LEU D 2 252 ? 132.875 87.479  153.597 1.00 23.43 ?  231 LEU D N     1 
ATOM   15239 C  CA    . LEU D 2 252 ? 133.022 87.294  152.156 1.00 22.79 ?  231 LEU D CA    1 
ATOM   15240 C  C     . LEU D 2 252 ? 134.246 88.047  151.623 1.00 22.71 ?  231 LEU D C     1 
ATOM   15241 O  O     . LEU D 2 252 ? 135.031 87.495  150.843 1.00 21.58 ?  231 LEU D O     1 
ATOM   15242 C  CB    . LEU D 2 252 ? 131.763 87.747  151.409 1.00 22.48 ?  231 LEU D CB    1 
ATOM   15243 C  CG    . LEU D 2 252 ? 131.806 87.592  149.877 1.00 21.05 ?  231 LEU D CG    1 
ATOM   15244 C  CD1   . LEU D 2 252 ? 132.066 86.130  149.453 1.00 22.94 ?  231 LEU D CD1   1 
ATOM   15245 C  CD2   . LEU D 2 252 ? 130.517 88.095  149.242 1.00 19.31 ?  231 LEU D CD2   1 
ATOM   15246 N  N     . LEU D 2 253 ? 134.397 89.304  152.043 1.00 22.90 ?  232 LEU D N     1 
ATOM   15247 C  CA    . LEU D 2 253 ? 135.547 90.109  151.607 1.00 23.78 ?  232 LEU D CA    1 
ATOM   15248 C  C     . LEU D 2 253 ? 136.869 89.424  151.973 1.00 23.75 ?  232 LEU D C     1 
ATOM   15249 O  O     . LEU D 2 253 ? 137.780 89.345  151.148 1.00 23.26 ?  232 LEU D O     1 
ATOM   15250 C  CB    . LEU D 2 253 ? 135.513 91.511  152.220 1.00 24.03 ?  232 LEU D CB    1 
ATOM   15251 C  CG    . LEU D 2 253 ? 136.795 92.336  152.004 1.00 26.46 ?  232 LEU D CG    1 
ATOM   15252 C  CD1   . LEU D 2 253 ? 136.894 92.774  150.562 1.00 26.52 ?  232 LEU D CD1   1 
ATOM   15253 C  CD2   . LEU D 2 253 ? 136.852 93.553  152.931 1.00 27.50 ?  232 LEU D CD2   1 
ATOM   15254 N  N     . ASN D 2 254 ? 136.965 88.959  153.220 1.00 24.63 ?  233 ASN D N     1 
ATOM   15255 C  CA    . ASN D 2 254 ? 138.140 88.223  153.693 1.00 25.49 ?  233 ASN D CA    1 
ATOM   15256 C  C     . ASN D 2 254 ? 138.480 86.988  152.846 1.00 24.94 ?  233 ASN D C     1 
ATOM   15257 O  O     . ASN D 2 254 ? 139.649 86.774  152.516 1.00 24.64 ?  233 ASN D O     1 
ATOM   15258 C  CB    . ASN D 2 254 ? 137.972 87.808  155.152 1.00 26.98 ?  233 ASN D CB    1 
ATOM   15259 C  CG    . ASN D 2 254 ? 138.400 88.891  156.117 1.00 29.94 ?  233 ASN D CG    1 
ATOM   15260 O  OD1   . ASN D 2 254 ? 139.409 89.576  155.904 1.00 34.55 ?  233 ASN D OD1   1 
ATOM   15261 N  ND2   . ASN D 2 254 ? 137.645 89.046  157.196 1.00 33.81 ?  233 ASN D ND2   1 
ATOM   15262 N  N     . GLN D 2 255 ? 137.469 86.185  152.513 1.00 24.08 ?  234 GLN D N     1 
ATOM   15263 C  CA    . GLN D 2 255 ? 137.687 84.986  151.699 1.00 24.35 ?  234 GLN D CA    1 
ATOM   15264 C  C     . GLN D 2 255 ? 138.224 85.373  150.333 1.00 23.26 ?  234 GLN D C     1 
ATOM   15265 O  O     . GLN D 2 255 ? 139.210 84.791  149.869 1.00 23.12 ?  234 GLN D O     1 
ATOM   15266 C  CB    . GLN D 2 255 ? 136.402 84.172  151.506 1.00 24.84 ?  234 GLN D CB    1 
ATOM   15267 C  CG    . GLN D 2 255 ? 135.907 83.417  152.720 1.00 27.45 ?  234 GLN D CG    1 
ATOM   15268 C  CD    . GLN D 2 255 ? 136.945 82.474  153.301 1.00 32.02 ?  234 GLN D CD    1 
ATOM   15269 O  OE1   . GLN D 2 255 ? 137.352 82.633  154.450 1.00 35.80 ?  234 GLN D OE1   1 
ATOM   15270 N  NE2   . GLN D 2 255 ? 137.376 81.486  152.514 1.00 32.12 ?  234 GLN D NE2   1 
ATOM   15271 N  N     . LEU D 2 256 ? 137.575 86.355  149.704 1.00 21.77 ?  235 LEU D N     1 
ATOM   15272 C  CA    . LEU D 2 256 ? 137.977 86.818  148.374 1.00 21.68 ?  235 LEU D CA    1 
ATOM   15273 C  C     . LEU D 2 256 ? 139.360 87.458  148.412 1.00 21.49 ?  235 LEU D C     1 
ATOM   15274 O  O     . LEU D 2 256 ? 140.172 87.234  147.521 1.00 20.89 ?  235 LEU D O     1 
ATOM   15275 C  CB    . LEU D 2 256 ? 136.956 87.811  147.784 1.00 20.49 ?  235 LEU D CB    1 
ATOM   15276 C  CG    . LEU D 2 256 ? 135.578 87.246  147.414 1.00 21.52 ?  235 LEU D CG    1 
ATOM   15277 C  CD1   . LEU D 2 256 ? 134.581 88.361  147.052 1.00 20.71 ?  235 LEU D CD1   1 
ATOM   15278 C  CD2   . LEU D 2 256 ? 135.667 86.240  146.275 1.00 20.74 ?  235 LEU D CD2   1 
ATOM   15279 N  N     . TYR D 2 257 ? 139.618 88.250  149.453 1.00 21.42 ?  236 TYR D N     1 
ATOM   15280 C  CA    . TYR D 2 257 ? 140.910 88.923  149.583 1.00 22.02 ?  236 TYR D CA    1 
ATOM   15281 C  C     . TYR D 2 257 ? 142.072 87.940  149.717 1.00 22.61 ?  236 TYR D C     1 
ATOM   15282 O  O     . TYR D 2 257 ? 143.113 88.115  149.082 1.00 22.19 ?  236 TYR D O     1 
ATOM   15283 C  CB    . TYR D 2 257 ? 140.899 89.914  150.742 1.00 22.06 ?  236 TYR D CB    1 
ATOM   15284 C  CG    . TYR D 2 257 ? 142.249 90.529  151.036 1.00 23.44 ?  236 TYR D CG    1 
ATOM   15285 C  CD1   . TYR D 2 257 ? 142.860 91.397  150.123 1.00 24.01 ?  236 TYR D CD1   1 
ATOM   15286 C  CD2   . TYR D 2 257 ? 142.910 90.251  152.230 1.00 25.22 ?  236 TYR D CD2   1 
ATOM   15287 C  CE1   . TYR D 2 257 ? 144.102 91.966  150.397 1.00 25.14 ?  236 TYR D CE1   1 
ATOM   15288 C  CE2   . TYR D 2 257 ? 144.155 90.806  152.510 1.00 26.71 ?  236 TYR D CE2   1 
ATOM   15289 C  CZ    . TYR D 2 257 ? 144.740 91.663  151.594 1.00 25.35 ?  236 TYR D CZ    1 
ATOM   15290 O  OH    . TYR D 2 257 ? 145.961 92.212  151.888 1.00 26.77 ?  236 TYR D OH    1 
ATOM   15291 N  N     . GLU D 2 258 ? 141.896 86.901  150.530 1.00 23.09 ?  237 GLU D N     1 
ATOM   15292 C  CA    . GLU D 2 258 ? 142.975 85.929  150.719 1.00 23.98 ?  237 GLU D CA    1 
ATOM   15293 C  C     . GLU D 2 258 ? 143.273 85.161  149.431 1.00 23.13 ?  237 GLU D C     1 
ATOM   15294 O  O     . GLU D 2 258 ? 144.431 84.899  149.119 1.00 23.02 ?  237 GLU D O     1 
ATOM   15295 C  CB    . GLU D 2 258 ? 142.688 84.988  151.899 1.00 25.20 ?  237 GLU D CB    1 
ATOM   15296 C  CG    . GLU D 2 258 ? 142.670 85.701  153.262 1.00 28.82 ?  237 GLU D CG    1 
ATOM   15297 C  CD    . GLU D 2 258 ? 144.047 86.178  153.744 1.00 34.48 ?  237 GLU D CD    1 
ATOM   15298 O  OE1   . GLU D 2 258 ? 145.083 85.557  153.388 1.00 37.75 ?  237 GLU D OE1   1 
ATOM   15299 O  OE2   . GLU D 2 258 ? 144.096 87.179  154.500 1.00 37.16 -1 237 GLU D OE2   1 
ATOM   15300 N  N     . ASN D 2 259 ? 142.231 84.837  148.676 1.00 22.12 ?  238 ASN D N     1 
ATOM   15301 C  CA    . ASN D 2 259 ? 142.398 84.247  147.347 1.00 22.35 ?  238 ASN D CA    1 
ATOM   15302 C  C     . ASN D 2 259 ? 143.031 85.218  146.315 1.00 22.11 ?  238 ASN D C     1 
ATOM   15303 O  O     . ASN D 2 259 ? 143.823 84.791  145.472 1.00 22.24 ?  238 ASN D O     1 
ATOM   15304 C  CB    . ASN D 2 259 ? 141.063 83.692  146.836 1.00 21.69 ?  238 ASN D CB    1 
ATOM   15305 C  CG    . ASN D 2 259 ? 141.190 83.023  145.479 1.00 23.38 ?  238 ASN D CG    1 
ATOM   15306 O  OD1   . ASN D 2 259 ? 141.749 81.922  145.359 1.00 23.95 ?  238 ASN D OD1   1 
ATOM   15307 N  ND2   . ASN D 2 259 ? 140.685 83.687  144.449 1.00 21.14 ?  238 ASN D ND2   1 
ATOM   15308 N  N     . GLU D 2 260 ? 142.684 86.508  146.391 1.00 21.95 ?  239 GLU D N     1 
ATOM   15309 C  CA    . GLU D 2 260 ? 143.301 87.544  145.536 1.00 22.50 ?  239 GLU D CA    1 
ATOM   15310 C  C     . GLU D 2 260 ? 144.810 87.648  145.750 1.00 22.03 ?  239 GLU D C     1 
ATOM   15311 O  O     . GLU D 2 260 ? 145.558 87.887  144.806 1.00 22.03 ?  239 GLU D O     1 
ATOM   15312 C  CB    . GLU D 2 260 ? 142.699 88.938  145.789 1.00 22.90 ?  239 GLU D CB    1 
ATOM   15313 C  CG    . GLU D 2 260 ? 141.393 89.261  145.045 1.00 25.84 ?  239 GLU D CG    1 
ATOM   15314 C  CD    . GLU D 2 260 ? 141.429 88.927  143.557 1.00 28.59 ?  239 GLU D CD    1 
ATOM   15315 O  OE1   . GLU D 2 260 ? 141.253 87.740  143.212 1.00 28.18 ?  239 GLU D OE1   1 
ATOM   15316 O  OE2   . GLU D 2 260 ? 141.591 89.856  142.731 1.00 30.32 -1 239 GLU D OE2   1 
ATOM   15317 N  N     . LEU D 2 261 ? 145.248 87.506  146.996 1.00 21.50 ?  240 LEU D N     1 
ATOM   15318 C  CA    . LEU D 2 261 ? 146.674 87.559  147.299 1.00 22.03 ?  240 LEU D CA    1 
ATOM   15319 C  C     . LEU D 2 261 ? 147.393 86.416  146.605 1.00 21.52 ?  240 LEU D C     1 
ATOM   15320 O  O     . LEU D 2 261 ? 148.452 86.623  146.011 1.00 21.44 ?  240 LEU D O     1 
ATOM   15321 C  CB    . LEU D 2 261 ? 146.937 87.517  148.802 1.00 21.57 ?  240 LEU D CB    1 
ATOM   15322 C  CG    . LEU D 2 261 ? 146.367 88.646  149.662 1.00 23.22 ?  240 LEU D CG    1 
ATOM   15323 C  CD1   . LEU D 2 261 ? 146.717 88.386  151.115 1.00 23.06 ?  240 LEU D CD1   1 
ATOM   15324 C  CD2   . LEU D 2 261 ? 146.895 90.008  149.212 1.00 23.52 ?  240 LEU D CD2   1 
ATOM   15325 N  N     . GLU D 2 262 ? 146.801 85.223  146.663 1.00 21.69 ?  241 GLU D N     1 
ATOM   15326 C  CA    . GLU D 2 262 ? 147.366 84.049  145.976 1.00 22.31 ?  241 GLU D CA    1 
ATOM   15327 C  C     . GLU D 2 262 ? 147.311 84.200  144.455 1.00 21.69 ?  241 GLU D C     1 
ATOM   15328 O  O     . GLU D 2 262 ? 148.275 83.881  143.754 1.00 21.75 ?  241 GLU D O     1 
ATOM   15329 C  CB    . GLU D 2 262 ? 146.640 82.765  146.390 1.00 22.46 ?  241 GLU D CB    1 
ATOM   15330 C  CG    . GLU D 2 262 ? 146.721 82.403  147.875 1.00 25.63 ?  241 GLU D CG    1 
ATOM   15331 C  CD    . GLU D 2 262 ? 146.052 81.064  148.153 1.00 29.83 ?  241 GLU D CD    1 
ATOM   15332 O  OE1   . GLU D 2 262 ? 144.807 81.019  148.238 1.00 33.22 ?  241 GLU D OE1   1 
ATOM   15333 O  OE2   . GLU D 2 262 ? 146.764 80.049  148.257 1.00 33.36 -1 241 GLU D OE2   1 
ATOM   15334 N  N     . TYR D 2 263 ? 146.171 84.667  143.947 1.00 21.42 ?  242 TYR D N     1 
ATOM   15335 C  CA    . TYR D 2 263 ? 145.993 84.948  142.518 1.00 21.04 ?  242 TYR D CA    1 
ATOM   15336 C  C     . TYR D 2 263 ? 147.074 85.925  142.035 1.00 21.15 ?  242 TYR D C     1 
ATOM   15337 O  O     . TYR D 2 263 ? 147.649 85.755  140.959 1.00 20.32 ?  242 TYR D O     1 
ATOM   15338 C  CB    . TYR D 2 263 ? 144.596 85.548  142.286 1.00 20.95 ?  242 TYR D CB    1 
ATOM   15339 C  CG    . TYR D 2 263 ? 144.296 85.987  140.864 1.00 21.86 ?  242 TYR D CG    1 
ATOM   15340 C  CD1   . TYR D 2 263 ? 143.915 85.059  139.895 1.00 23.53 ?  242 TYR D CD1   1 
ATOM   15341 C  CD2   . TYR D 2 263 ? 144.392 87.331  140.489 1.00 21.20 ?  242 TYR D CD2   1 
ATOM   15342 C  CE1   . TYR D 2 263 ? 143.636 85.455  138.595 1.00 23.34 ?  242 TYR D CE1   1 
ATOM   15343 C  CE2   . TYR D 2 263 ? 144.115 87.735  139.187 1.00 23.11 ?  242 TYR D CE2   1 
ATOM   15344 C  CZ    . TYR D 2 263 ? 143.744 86.790  138.246 1.00 23.27 ?  242 TYR D CZ    1 
ATOM   15345 O  OH    . TYR D 2 263 ? 143.467 87.185  136.955 1.00 27.07 ?  242 TYR D OH    1 
ATOM   15346 N  N     . THR D 2 264 ? 147.317 86.951  142.847 1.00 21.12 ?  243 THR D N     1 
ATOM   15347 C  CA    . THR D 2 264 ? 148.266 88.015  142.534 1.00 21.98 ?  243 THR D CA    1 
ATOM   15348 C  C     . THR D 2 264 ? 149.693 87.480  142.431 1.00 22.32 ?  243 THR D C     1 
ATOM   15349 O  O     . THR D 2 264 ? 150.370 87.720  141.434 1.00 21.78 ?  243 THR D O     1 
ATOM   15350 C  CB    . THR D 2 264 ? 148.166 89.166  143.560 1.00 21.68 ?  243 THR D CB    1 
ATOM   15351 O  OG1   . THR D 2 264 ? 146.883 89.787  143.434 1.00 23.29 ?  243 THR D OG1   1 
ATOM   15352 C  CG2   . THR D 2 264 ? 149.268 90.223  143.359 1.00 23.16 ?  243 THR D CG2   1 
ATOM   15353 N  N     . GLU D 2 265 ? 150.135 86.737  143.445 1.00 22.48 ?  244 GLU D N     1 
ATOM   15354 C  CA    . GLU D 2 265 ? 151.482 86.162  143.411 1.00 23.73 ?  244 GLU D CA    1 
ATOM   15355 C  C     . GLU D 2 265 ? 151.656 85.220  142.229 1.00 23.85 ?  244 GLU D C     1 
ATOM   15356 O  O     . GLU D 2 265 ? 152.691 85.242  141.577 1.00 24.40 ?  244 GLU D O     1 
ATOM   15357 C  CB    . GLU D 2 265 ? 151.806 85.444  144.712 1.00 23.19 ?  244 GLU D CB    1 
ATOM   15358 C  CG    . GLU D 2 265 ? 152.064 86.409  145.838 1.00 25.08 ?  244 GLU D CG    1 
ATOM   15359 C  CD    . GLU D 2 265 ? 152.217 85.727  147.182 1.00 27.30 ?  244 GLU D CD    1 
ATOM   15360 O  OE1   . GLU D 2 265 ? 152.328 84.486  147.227 1.00 27.77 ?  244 GLU D OE1   1 
ATOM   15361 O  OE2   . GLU D 2 265 ? 152.227 86.446  148.198 1.00 28.63 -1 244 GLU D OE2   1 
ATOM   15362 N  N     . ASP D 2 266 ? 150.620 84.430  141.945 1.00 24.13 ?  245 ASP D N     1 
ATOM   15363 C  CA    . ASP D 2 266 ? 150.628 83.464  140.842 1.00 25.22 ?  245 ASP D CA    1 
ATOM   15364 C  C     . ASP D 2 266 ? 150.885 84.128  139.471 1.00 24.84 ?  245 ASP D C     1 
ATOM   15365 O  O     . ASP D 2 266 ? 151.574 83.555  138.621 1.00 25.64 ?  245 ASP D O     1 
ATOM   15366 C  CB    . ASP D 2 266 ? 149.302 82.687  140.840 1.00 25.79 ?  245 ASP D CB    1 
ATOM   15367 C  CG    . ASP D 2 266 ? 149.268 81.562  139.814 1.00 27.71 ?  245 ASP D CG    1 
ATOM   15368 O  OD1   . ASP D 2 266 ? 150.156 80.697  139.852 1.00 31.57 ?  245 ASP D OD1   1 
ATOM   15369 O  OD2   . ASP D 2 266 ? 148.337 81.527  138.981 1.00 30.29 -1 245 ASP D OD2   1 
ATOM   15370 N  N     . LEU D 2 267 ? 150.354 85.331  139.274 1.00 24.07 ?  246 LEU D N     1 
ATOM   15371 C  CA    . LEU D 2 267 ? 150.466 86.037  137.996 1.00 23.98 ?  246 LEU D CA    1 
ATOM   15372 C  C     . LEU D 2 267 ? 151.604 87.056  137.927 1.00 22.83 ?  246 LEU D C     1 
ATOM   15373 O  O     . LEU D 2 267 ? 152.256 87.186  136.883 1.00 23.00 ?  246 LEU D O     1 
ATOM   15374 C  CB    . LEU D 2 267 ? 149.146 86.752  137.653 1.00 23.82 ?  246 LEU D CB    1 
ATOM   15375 C  CG    . LEU D 2 267 ? 147.952 85.857  137.295 1.00 26.05 ?  246 LEU D CG    1 
ATOM   15376 C  CD1   . LEU D 2 267 ? 146.825 86.678  136.733 1.00 26.74 ?  246 LEU D CD1   1 
ATOM   15377 C  CD2   . LEU D 2 267 ? 148.338 84.773  136.307 1.00 28.00 ?  246 LEU D CD2   1 
ATOM   15378 N  N     . TYR D 2 268 ? 151.830 87.771  139.030 1.00 21.68 ?  247 TYR D N     1 
ATOM   15379 C  CA    . TYR D 2 268 ? 152.702 88.949  139.023 1.00 20.95 ?  247 TYR D CA    1 
ATOM   15380 C  C     . TYR D 2 268 ? 154.119 88.771  139.583 1.00 21.43 ?  247 TYR D C     1 
ATOM   15381 O  O     . TYR D 2 268 ? 154.972 89.622  139.336 1.00 20.73 ?  247 TYR D O     1 
ATOM   15382 C  CB    . TYR D 2 268 ? 152.027 90.127  139.734 1.00 20.27 ?  247 TYR D CB    1 
ATOM   15383 C  CG    . TYR D 2 268 ? 150.858 90.735  138.980 1.00 19.54 ?  247 TYR D CG    1 
ATOM   15384 C  CD1   . TYR D 2 268 ? 149.547 90.439  139.337 1.00 18.52 ?  247 TYR D CD1   1 
ATOM   15385 C  CD2   . TYR D 2 268 ? 151.072 91.607  137.902 1.00 20.62 ?  247 TYR D CD2   1 
ATOM   15386 C  CE1   . TYR D 2 268 ? 148.448 91.013  138.645 1.00 18.33 ?  247 TYR D CE1   1 
ATOM   15387 C  CE2   . TYR D 2 268 ? 149.987 92.185  137.202 1.00 20.79 ?  247 TYR D CE2   1 
ATOM   15388 C  CZ    . TYR D 2 268 ? 148.688 91.887  137.589 1.00 20.23 ?  247 TYR D CZ    1 
ATOM   15389 O  OH    . TYR D 2 268 ? 147.638 92.456  136.897 1.00 20.50 ?  247 TYR D OH    1 
ATOM   15390 N  N     . ASP D 2 269 ? 154.376 87.701  140.344 1.00 21.65 ?  248 ASP D N     1 
ATOM   15391 C  CA    . ASP D 2 269 ? 155.752 87.449  140.787 1.00 22.30 ?  248 ASP D CA    1 
ATOM   15392 C  C     . ASP D 2 269 ? 156.753 87.366  139.609 1.00 22.54 ?  248 ASP D C     1 
ATOM   15393 O  O     . ASP D 2 269 ? 157.878 87.860  139.719 1.00 22.49 ?  248 ASP D O     1 
ATOM   15394 C  CB    . ASP D 2 269 ? 155.851 86.200  141.665 1.00 22.83 ?  248 ASP D CB    1 
ATOM   15395 C  CG    . ASP D 2 269 ? 155.453 86.466  143.114 1.00 23.55 ?  248 ASP D CG    1 
ATOM   15396 O  OD1   . ASP D 2 269 ? 155.249 87.640  143.482 1.00 24.95 ?  248 ASP D OD1   1 
ATOM   15397 O  OD2   . ASP D 2 269 ? 155.344 85.490  143.891 1.00 24.47 -1 248 ASP D OD2   1 
ATOM   15398 N  N     . GLN D 2 270 ? 156.339 86.757  138.496 1.00 22.79 ?  249 GLN D N     1 
ATOM   15399 C  CA    . GLN D 2 270 ? 157.224 86.590  137.336 1.00 23.41 ?  249 GLN D CA    1 
ATOM   15400 C  C     . GLN D 2 270 ? 157.598 87.908  136.651 1.00 22.83 ?  249 GLN D C     1 
ATOM   15401 O  O     . GLN D 2 270 ? 158.543 87.947  135.865 1.00 23.75 ?  249 GLN D O     1 
ATOM   15402 C  CB    . GLN D 2 270 ? 156.641 85.607  136.315 1.00 24.02 ?  249 GLN D CB    1 
ATOM   15403 C  CG    . GLN D 2 270 ? 155.401 86.116  135.559 1.00 25.40 ?  249 GLN D CG    1 
ATOM   15404 C  CD    . GLN D 2 270 ? 154.685 85.011  134.802 1.00 29.23 ?  249 GLN D CD    1 
ATOM   15405 O  OE1   . GLN D 2 270 ? 154.690 83.853  135.222 1.00 31.31 ?  249 GLN D OE1   1 
ATOM   15406 N  NE2   . GLN D 2 270 ? 154.051 85.365  133.686 1.00 30.04 ?  249 GLN D NE2   1 
ATOM   15407 N  N     . VAL D 2 271 ? 156.849 88.974  136.934 1.00 21.93 ?  250 VAL D N     1 
ATOM   15408 C  CA    . VAL D 2 271 ? 157.183 90.307  136.421 1.00 21.29 ?  250 VAL D CA    1 
ATOM   15409 C  C     . VAL D 2 271 ? 157.487 91.308  137.551 1.00 21.16 ?  250 VAL D C     1 
ATOM   15410 O  O     . VAL D 2 271 ? 157.573 92.517  137.313 1.00 21.54 ?  250 VAL D O     1 
ATOM   15411 C  CB    . VAL D 2 271 ? 156.078 90.841  135.453 1.00 21.62 ?  250 VAL D CB    1 
ATOM   15412 C  CG1   . VAL D 2 271 ? 155.993 89.964  134.205 1.00 21.36 ?  250 VAL D CG1   1 
ATOM   15413 C  CG2   . VAL D 2 271 ? 154.710 90.926  136.155 1.00 21.17 ?  250 VAL D CG2   1 
ATOM   15414 N  N     . GLY D 2 272 ? 157.625 90.798  138.781 1.00 20.92 ?  251 GLY D N     1 
ATOM   15415 C  CA    . GLY D 2 272 ? 158.096 91.583  139.940 1.00 20.61 ?  251 GLY D CA    1 
ATOM   15416 C  C     . GLY D 2 272 ? 157.182 92.675  140.490 1.00 20.77 ?  251 GLY D C     1 
ATOM   15417 O  O     . GLY D 2 272 ? 157.657 93.637  141.113 1.00 20.28 ?  251 GLY D O     1 
ATOM   15418 N  N     . LEU D 2 273 ? 155.875 92.525  140.290 1.00 19.85 ?  252 LEU D N     1 
ATOM   15419 C  CA    . LEU D 2 273 ? 154.948 93.611  140.612 1.00 20.09 ?  252 LEU D CA    1 
ATOM   15420 C  C     . LEU D 2 273 ? 154.004 93.371  141.794 1.00 19.88 ?  252 LEU D C     1 
ATOM   15421 O  O     . LEU D 2 273 ? 153.268 94.277  142.171 1.00 20.04 ?  252 LEU D O     1 
ATOM   15422 C  CB    . LEU D 2 273 ? 154.105 93.947  139.370 1.00 19.97 ?  252 LEU D CB    1 
ATOM   15423 C  CG    . LEU D 2 273 ? 154.860 94.382  138.122 1.00 20.26 ?  252 LEU D CG    1 
ATOM   15424 C  CD1   . LEU D 2 273 ? 153.842 94.764  137.070 1.00 18.98 ?  252 LEU D CD1   1 
ATOM   15425 C  CD2   . LEU D 2 273 ? 155.831 95.561  138.408 1.00 21.03 ?  252 LEU D CD2   1 
ATOM   15426 N  N     . SER D 2 274 ? 154.044 92.169  142.371 0.50 19.54 ?  253 SER D N     1 
ATOM   15427 C  CA    . SER D 2 274 ? 153.017 91.721  143.326 0.50 19.34 ?  253 SER D CA    1 
ATOM   15428 C  C     . SER D 2 274 ? 152.791 92.649  144.525 0.50 20.05 ?  253 SER D C     1 
ATOM   15429 O  O     . SER D 2 274 ? 151.647 92.880  144.916 0.50 20.31 ?  253 SER D O     1 
ATOM   15430 C  CB    . SER D 2 274 ? 153.291 90.287  143.799 0.50 18.97 ?  253 SER D CB    1 
ATOM   15431 O  OG    . SER D 2 274 ? 153.388 89.393  142.706 0.50 15.35 ?  253 SER D OG    1 
ATOM   15432 N  N     . HIS D 2 275 ? 153.873 93.164  145.108 1.00 20.77 ?  254 HIS D N     1 
ATOM   15433 C  CA    . HIS D 2 275 ? 153.774 94.111  146.237 1.00 21.18 ?  254 HIS D CA    1 
ATOM   15434 C  C     . HIS D 2 275 ? 152.854 95.303  145.918 1.00 21.50 ?  254 HIS D C     1 
ATOM   15435 O  O     . HIS D 2 275 ? 151.942 95.625  146.697 1.00 19.88 ?  254 HIS D O     1 
ATOM   15436 C  CB    . HIS D 2 275 ? 155.159 94.609  146.683 1.00 21.60 ?  254 HIS D CB    1 
ATOM   15437 C  CG    . HIS D 2 275 ? 155.100 95.669  147.741 1.00 22.43 ?  254 HIS D CG    1 
ATOM   15438 N  ND1   . HIS D 2 275 ? 155.070 95.379  149.091 1.00 22.77 ?  254 HIS D ND1   1 
ATOM   15439 C  CD2   . HIS D 2 275 ? 155.048 97.021  147.644 1.00 22.50 ?  254 HIS D CD2   1 
ATOM   15440 C  CE1   . HIS D 2 275 ? 155.008 96.508  149.777 1.00 24.05 ?  254 HIS D CE1   1 
ATOM   15441 N  NE2   . HIS D 2 275 ? 154.986 97.518  148.923 1.00 23.22 ?  254 HIS D NE2   1 
ATOM   15442 N  N     . ASP D 2 276 ? 153.091 95.935  144.768 1.00 22.34 ?  255 ASP D N     1 
ATOM   15443 C  CA    . ASP D 2 276 ? 152.299 97.090  144.353 1.00 23.19 ?  255 ASP D CA    1 
ATOM   15444 C  C     . ASP D 2 276 ? 150.876 96.713  143.965 1.00 22.17 ?  255 ASP D C     1 
ATOM   15445 O  O     . ASP D 2 276 ? 149.958 97.487  144.201 1.00 21.87 ?  255 ASP D O     1 
ATOM   15446 C  CB    . ASP D 2 276 ? 152.965 97.845  143.192 1.00 24.33 ?  255 ASP D CB    1 
ATOM   15447 C  CG    . ASP D 2 276 ? 153.967 98.904  143.661 1.00 27.58 ?  255 ASP D CG    1 
ATOM   15448 O  OD1   . ASP D 2 276 ? 153.856 99.402  144.803 1.00 31.10 ?  255 ASP D OD1   1 
ATOM   15449 O  OD2   . ASP D 2 276 ? 154.877 99.236  142.868 1.00 29.88 -1 255 ASP D OD2   1 
ATOM   15450 N  N     . VAL D 2 277 ? 150.700 95.550  143.339 1.00 21.21 ?  256 VAL D N     1 
ATOM   15451 C  CA    . VAL D 2 277 ? 149.356 95.073  142.999 1.00 20.51 ?  256 VAL D CA    1 
ATOM   15452 C  C     . VAL D 2 277 ? 148.510 94.853  144.258 1.00 20.32 ?  256 VAL D C     1 
ATOM   15453 O  O     . VAL D 2 277 ? 147.332 95.199  144.279 1.00 19.81 ?  256 VAL D O     1 
ATOM   15454 C  CB    . VAL D 2 277 ? 149.383 93.780  142.133 1.00 20.30 ?  256 VAL D CB    1 
ATOM   15455 C  CG1   . VAL D 2 277 ? 147.971 93.284  141.869 1.00 21.16 ?  256 VAL D CG1   1 
ATOM   15456 C  CG2   . VAL D 2 277 ? 150.093 94.039  140.817 1.00 19.06 ?  256 VAL D CG2   1 
ATOM   15457 N  N     . LYS D 2 278 ? 149.129 94.300  145.301 1.00 19.84 ?  257 LYS D N     1 
ATOM   15458 C  CA    . LYS D 2 278 ? 148.453 94.087  146.581 1.00 20.27 ?  257 LYS D CA    1 
ATOM   15459 C  C     . LYS D 2 278 ? 147.933 95.392  147.197 1.00 20.16 ?  257 LYS D C     1 
ATOM   15460 O  O     . LYS D 2 278 ? 146.815 95.418  147.706 1.00 19.88 ?  257 LYS D O     1 
ATOM   15461 C  CB    . LYS D 2 278 ? 149.346 93.322  147.562 1.00 20.20 ?  257 LYS D CB    1 
ATOM   15462 C  CG    . LYS D 2 278 ? 149.493 91.845  147.212 1.00 21.60 ?  257 LYS D CG    1 
ATOM   15463 C  CD    . LYS D 2 278 ? 150.591 91.175  148.029 1.00 21.53 ?  257 LYS D CD    1 
ATOM   15464 C  CE    . LYS D 2 278 ? 150.813 89.767  147.532 1.00 24.52 ?  257 LYS D CE    1 
ATOM   15465 N  NZ    . LYS D 2 278 ? 151.865 89.076  148.348 1.00 26.32 1  257 LYS D NZ    1 
ATOM   15466 N  N     . LYS D 2 279 ? 148.727 96.466  147.123 1.00 19.67 ?  258 LYS D N     1 
ATOM   15467 C  CA    . LYS D 2 279 ? 148.268 97.786  147.583 1.00 20.10 ?  258 LYS D CA    1 
ATOM   15468 C  C     . LYS D 2 279 ? 147.025 98.241  146.808 1.00 19.12 ?  258 LYS D C     1 
ATOM   15469 O  O     . LYS D 2 279 ? 146.094 98.791  147.399 1.00 18.59 ?  258 LYS D O     1 
ATOM   15470 C  CB    . LYS D 2 279 ? 149.377 98.850  147.478 1.00 20.54 ?  258 LYS D CB    1 
ATOM   15471 C  CG    . LYS D 2 279 ? 150.621 98.569  148.318 1.00 22.84 ?  258 LYS D CG    1 
ATOM   15472 C  CD    . LYS D 2 279 ? 151.417 99.855  148.641 1.00 24.16 ?  258 LYS D CD    1 
ATOM   15473 C  CE    . LYS D 2 279 ? 152.037 100.492 147.401 1.00 25.61 ?  258 LYS D CE    1 
ATOM   15474 N  NZ    . LYS D 2 279 ? 152.820 101.747 147.728 1.00 24.70 1  258 LYS D NZ    1 
ATOM   15475 N  N     . PHE D 2 280 ? 147.020 97.983  145.497 1.00 19.04 ?  259 PHE D N     1 
ATOM   15476 C  CA    . PHE D 2 280 ? 145.911 98.352  144.598 1.00 19.31 ?  259 PHE D CA    1 
ATOM   15477 C  C     . PHE D 2 280 ? 144.627 97.562  144.876 1.00 19.25 ?  259 PHE D C     1 
ATOM   15478 O  O     . PHE D 2 280 ? 143.519 98.111  144.813 1.00 19.71 ?  259 PHE D O     1 
ATOM   15479 C  CB    . PHE D 2 280 ? 146.335 98.150  143.143 1.00 19.04 ?  259 PHE D CB    1 
ATOM   15480 C  CG    . PHE D 2 280 ? 145.454 98.848  142.124 1.00 20.15 ?  259 PHE D CG    1 
ATOM   15481 C  CD1   . PHE D 2 280 ? 145.227 100.215 142.191 1.00 21.63 ?  259 PHE D CD1   1 
ATOM   15482 C  CD2   . PHE D 2 280 ? 144.898 98.125  141.066 1.00 19.95 ?  259 PHE D CD2   1 
ATOM   15483 C  CE1   . PHE D 2 280 ? 144.438 100.863 141.215 1.00 22.56 ?  259 PHE D CE1   1 
ATOM   15484 C  CE2   . PHE D 2 280 ? 144.118 98.749  140.094 1.00 20.29 ?  259 PHE D CE2   1 
ATOM   15485 C  CZ    . PHE D 2 280 ? 143.884 100.123 140.170 1.00 21.30 ?  259 PHE D CZ    1 
ATOM   15486 N  N     . ILE D 2 281 ? 144.772 96.273  145.166 1.00 19.36 ?  260 ILE D N     1 
ATOM   15487 C  CA    . ILE D 2 281 ? 143.646 95.447  145.612 1.00 19.45 ?  260 ILE D CA    1 
ATOM   15488 C  C     . ILE D 2 281 ? 142.980 96.000  146.891 1.00 19.61 ?  260 ILE D C     1 
ATOM   15489 O  O     . ILE D 2 281 ? 141.754 96.117  146.941 1.00 19.72 ?  260 ILE D O     1 
ATOM   15490 C  CB    . ILE D 2 281 ? 144.106 93.978  145.804 1.00 19.49 ?  260 ILE D CB    1 
ATOM   15491 C  CG1   . ILE D 2 281 ? 144.500 93.382  144.449 1.00 20.10 ?  260 ILE D CG1   1 
ATOM   15492 C  CG2   . ILE D 2 281 ? 143.050 93.119  146.533 1.00 20.53 ?  260 ILE D CG2   1 
ATOM   15493 C  CD1   . ILE D 2 281 ? 145.278 92.070  144.593 1.00 21.17 ?  260 ILE D CD1   1 
ATOM   15494 N  N     . ARG D 2 282 ? 143.781 96.344  147.901 1.00 19.75 ?  261 ARG D N     1 
ATOM   15495 C  CA    . ARG D 2 282 ? 143.243 96.831  149.186 1.00 20.34 ?  261 ARG D CA    1 
ATOM   15496 C  C     . ARG D 2 282 ? 142.542 98.177  149.036 1.00 21.18 ?  261 ARG D C     1 
ATOM   15497 O  O     . ARG D 2 282 ? 141.481 98.417  149.630 1.00 21.68 ?  261 ARG D O     1 
ATOM   15498 C  CB    . ARG D 2 282 ? 144.339 96.911  150.257 1.00 20.20 ?  261 ARG D CB    1 
ATOM   15499 C  CG    . ARG D 2 282 ? 144.821 95.557  150.746 1.00 20.57 ?  261 ARG D CG    1 
ATOM   15500 C  CD    . ARG D 2 282 ? 145.785 95.701  151.926 1.00 23.15 ?  261 ARG D CD    1 
ATOM   15501 N  NE    . ARG D 2 282 ? 147.113 96.185  151.542 1.00 23.46 ?  261 ARG D NE    1 
ATOM   15502 C  CZ    . ARG D 2 282 ? 148.126 95.404  151.169 1.00 22.84 ?  261 ARG D CZ    1 
ATOM   15503 N  NH1   . ARG D 2 282 ? 147.971 94.089  151.088 1.00 23.37 1  261 ARG D NH1   1 
ATOM   15504 N  NH2   . ARG D 2 282 ? 149.297 95.945  150.865 1.00 22.27 ?  261 ARG D NH2   1 
ATOM   15505 N  N     . TYR D 2 283 ? 143.157 99.055  148.251 1.00 21.46 ?  262 TYR D N     1 
ATOM   15506 C  CA    . TYR D 2 283 ? 142.588 100.363 147.936 1.00 22.97 ?  262 TYR D CA    1 
ATOM   15507 C  C     . TYR D 2 283 ? 141.210 100.201 147.256 1.00 22.12 ?  262 TYR D C     1 
ATOM   15508 O  O     . TYR D 2 283 ? 140.253 100.901 147.595 1.00 22.00 ?  262 TYR D O     1 
ATOM   15509 C  CB    . TYR D 2 283 ? 143.591 101.135 147.071 1.00 23.37 ?  262 TYR D CB    1 
ATOM   15510 C  CG    . TYR D 2 283 ? 143.069 102.358 146.354 1.00 27.31 ?  262 TYR D CG    1 
ATOM   15511 C  CD1   . TYR D 2 283 ? 143.060 103.605 146.979 1.00 30.79 ?  262 TYR D CD1   1 
ATOM   15512 C  CD2   . TYR D 2 283 ? 142.628 102.276 145.034 1.00 30.31 ?  262 TYR D CD2   1 
ATOM   15513 C  CE1   . TYR D 2 283 ? 142.583 104.745 146.312 1.00 33.18 ?  262 TYR D CE1   1 
ATOM   15514 C  CE2   . TYR D 2 283 ? 142.161 103.405 144.354 1.00 33.20 ?  262 TYR D CE2   1 
ATOM   15515 C  CZ    . TYR D 2 283 ? 142.149 104.636 145.000 1.00 34.74 ?  262 TYR D CZ    1 
ATOM   15516 O  OH    . TYR D 2 283 ? 141.694 105.751 144.323 1.00 37.63 ?  262 TYR D OH    1 
ATOM   15517 N  N     . ASN D 2 284 ? 141.098 99.245  146.338 1.00 21.63 ?  263 ASN D N     1 
ATOM   15518 C  CA    . ASN D 2 284 ? 139.829 99.010  145.655 1.00 21.41 ?  263 ASN D CA    1 
ATOM   15519 C  C     . ASN D 2 284 ? 138.809 98.244  146.502 1.00 20.86 ?  263 ASN D C     1 
ATOM   15520 O  O     . ASN D 2 284 ? 137.611 98.460  146.362 1.00 20.92 ?  263 ASN D O     1 
ATOM   15521 C  CB    . ASN D 2 284 ? 140.045 98.376  144.280 1.00 21.15 ?  263 ASN D CB    1 
ATOM   15522 C  CG    . ASN D 2 284 ? 140.568 99.381  143.263 1.00 22.59 ?  263 ASN D CG    1 
ATOM   15523 O  OD1   . ASN D 2 284 ? 139.834 100.267 142.816 1.00 22.35 ?  263 ASN D OD1   1 
ATOM   15524 N  ND2   . ASN D 2 284 ? 141.844 99.260  142.904 1.00 22.93 ?  263 ASN D ND2   1 
ATOM   15525 N  N     . ALA D 2 285 ? 139.287 97.363  147.382 1.00 20.92 ?  264 ALA D N     1 
ATOM   15526 C  CA    . ALA D 2 285 ? 138.427 96.738  148.402 1.00 20.77 ?  264 ALA D CA    1 
ATOM   15527 C  C     . ALA D 2 285 ? 137.729 97.787  149.274 1.00 21.13 ?  264 ALA D C     1 
ATOM   15528 O  O     . ALA D 2 285 ? 136.528 97.674  149.550 1.00 19.92 ?  264 ALA D O     1 
ATOM   15529 C  CB    . ALA D 2 285 ? 139.231 95.758  149.270 1.00 20.68 ?  264 ALA D CB    1 
ATOM   15530 N  N     . ASN D 2 286 ? 138.485 98.806  149.696 1.00 21.38 ?  265 ASN D N     1 
ATOM   15531 C  CA    . ASN D 2 286 ? 137.937 99.927  150.464 1.00 21.94 ?  265 ASN D CA    1 
ATOM   15532 C  C     . ASN D 2 286 ? 136.863 100.705 149.682 1.00 22.13 ?  265 ASN D C     1 
ATOM   15533 O  O     . ASN D 2 286 ? 135.859 101.115 150.252 1.00 21.95 ?  265 ASN D O     1 
ATOM   15534 C  CB    . ASN D 2 286 ? 139.047 100.885 150.903 1.00 22.22 ?  265 ASN D CB    1 
ATOM   15535 C  CG    . ASN D 2 286 ? 139.827 100.391 152.118 1.00 22.80 ?  265 ASN D CG    1 
ATOM   15536 O  OD1   . ASN D 2 286 ? 139.427 99.452  152.815 1.00 22.57 ?  265 ASN D OD1   1 
ATOM   15537 N  ND2   . ASN D 2 286 ? 140.961 101.035 152.370 1.00 23.91 ?  265 ASN D ND2   1 
ATOM   15538 N  N     . LYS D 2 287 ? 137.074 100.898 148.382 1.00 22.51 ?  266 LYS D N     1 
ATOM   15539 C  CA    . LYS D 2 287 ? 136.063 101.557 147.543 1.00 22.91 ?  266 LYS D CA    1 
ATOM   15540 C  C     . LYS D 2 287 ? 134.776 100.727 147.467 1.00 22.33 ?  266 LYS D C     1 
ATOM   15541 O  O     . LYS D 2 287 ? 133.684 101.275 147.557 1.00 22.24 ?  266 LYS D O     1 
ATOM   15542 C  CB    . LYS D 2 287 ? 136.603 101.844 146.135 1.00 23.65 ?  266 LYS D CB    1 
ATOM   15543 C  CG    . LYS D 2 287 ? 137.588 103.012 146.077 1.00 26.50 ?  266 LYS D CG    1 
ATOM   15544 C  CD    . LYS D 2 287 ? 138.072 103.246 144.634 1.00 31.30 ?  266 LYS D CD    1 
ATOM   15545 C  CE    . LYS D 2 287 ? 138.619 104.655 144.483 1.00 35.08 ?  266 LYS D CE    1 
ATOM   15546 N  NZ    . LYS D 2 287 ? 139.079 104.975 143.098 1.00 37.66 1  266 LYS D NZ    1 
ATOM   15547 N  N     . ALA D 2 288 ? 134.923 99.409  147.318 1.00 21.41 ?  267 ALA D N     1 
ATOM   15548 C  CA    . ALA D 2 288 ? 133.797 98.475  147.278 1.00 21.53 ?  267 ALA D CA    1 
ATOM   15549 C  C     . ALA D 2 288 ? 132.981 98.514  148.582 1.00 21.77 ?  267 ALA D C     1 
ATOM   15550 O  O     . ALA D 2 288 ? 131.739 98.555  148.563 1.00 21.59 ?  267 ALA D O     1 
ATOM   15551 C  CB    . ALA D 2 288 ? 134.294 97.052  146.984 1.00 21.33 ?  267 ALA D CB    1 
ATOM   15552 N  N     . LEU D 2 289 ? 133.681 98.525  149.709 1.00 21.71 ?  268 LEU D N     1 
ATOM   15553 C  CA    . LEU D 2 289 ? 133.022 98.670  151.001 1.00 22.36 ?  268 LEU D CA    1 
ATOM   15554 C  C     . LEU D 2 289 ? 132.285 100.000 151.095 1.00 23.01 ?  268 LEU D C     1 
ATOM   15555 O  O     . LEU D 2 289 ? 131.128 100.044 151.518 1.00 23.14 ?  268 LEU D O     1 
ATOM   15556 C  CB    . LEU D 2 289 ? 134.021 98.500  152.151 1.00 22.61 ?  268 LEU D CB    1 
ATOM   15557 C  CG    . LEU D 2 289 ? 134.558 97.067  152.356 1.00 21.22 ?  268 LEU D CG    1 
ATOM   15558 C  CD1   . LEU D 2 289 ? 135.756 97.065  153.294 1.00 20.77 ?  268 LEU D CD1   1 
ATOM   15559 C  CD2   . LEU D 2 289 ? 133.463 96.107  152.874 1.00 21.40 ?  268 LEU D CD2   1 
ATOM   15560 N  N     . MET D 2 290 ? 132.931 101.084 150.677 1.00 23.87 ?  269 MET D N     1 
ATOM   15561 C  CA    . MET D 2 290 ? 132.255 102.378 150.712 1.00 25.26 ?  269 MET D CA    1 
ATOM   15562 C  C     . MET D 2 290 ? 131.008 102.400 149.811 1.00 24.37 ?  269 MET D C     1 
ATOM   15563 O  O     . MET D 2 290 ? 129.994 102.969 150.201 1.00 23.97 ?  269 MET D O     1 
ATOM   15564 C  CB    . MET D 2 290 ? 133.229 103.523 150.454 1.00 25.94 ?  269 MET D CB    1 
ATOM   15565 C  CG    . MET D 2 290 ? 134.044 103.852 151.720 1.00 31.08 ?  269 MET D CG    1 
ATOM   15566 S  SD    . MET D 2 290 ? 135.253 105.180 151.510 1.00 41.28 ?  269 MET D SD    1 
ATOM   15567 C  CE    . MET D 2 290 ? 134.222 106.500 150.821 1.00 38.56 ?  269 MET D CE    1 
ATOM   15568 N  N     . ASN D 2 291 ? 131.068 101.739 148.651 1.00 23.66 ?  270 ASN D N     1 
ATOM   15569 C  CA    . ASN D 2 291 ? 129.869 101.556 147.799 1.00 23.17 ?  270 ASN D CA    1 
ATOM   15570 C  C     . ASN D 2 291 ? 128.691 100.878 148.504 1.00 23.22 ?  270 ASN D C     1 
ATOM   15571 O  O     . ASN D 2 291 ? 127.533 101.138 148.177 1.00 22.68 ?  270 ASN D O     1 
ATOM   15572 C  CB    . ASN D 2 291 ? 130.199 100.780 146.514 1.00 22.41 ?  270 ASN D CB    1 
ATOM   15573 C  CG    . ASN D 2 291 ? 131.056 101.575 145.556 1.00 21.93 ?  270 ASN D CG    1 
ATOM   15574 O  OD1   . ASN D 2 291 ? 131.217 102.791 145.707 1.00 20.94 ?  270 ASN D OD1   1 
ATOM   15575 N  ND2   . ASN D 2 291 ? 131.615 100.894 144.559 1.00 19.20 ?  270 ASN D ND2   1 
ATOM   15576 N  N     . LEU D 2 292 ? 129.006 100.011 149.465 1.00 23.53 ?  271 LEU D N     1 
ATOM   15577 C  CA    . LEU D 2 292 ? 128.001 99.295  150.253 1.00 24.21 ?  271 LEU D CA    1 
ATOM   15578 C  C     . LEU D 2 292 ? 127.666 100.024 151.559 1.00 25.14 ?  271 LEU D C     1 
ATOM   15579 O  O     . LEU D 2 292 ? 126.975 99.477  152.434 1.00 25.14 ?  271 LEU D O     1 
ATOM   15580 C  CB    . LEU D 2 292 ? 128.468 97.851  150.535 1.00 23.71 ?  271 LEU D CB    1 
ATOM   15581 C  CG    . LEU D 2 292 ? 128.648 96.915  149.331 1.00 23.37 ?  271 LEU D CG    1 
ATOM   15582 C  CD1   . LEU D 2 292 ? 129.481 95.688  149.711 1.00 23.28 ?  271 LEU D CD1   1 
ATOM   15583 C  CD2   . LEU D 2 292 ? 127.294 96.492  148.729 1.00 23.06 ?  271 LEU D CD2   1 
ATOM   15584 N  N     . GLY D 2 293 ? 128.150 101.261 151.679 1.00 25.82 ?  272 GLY D N     1 
ATOM   15585 C  CA    . GLY D 2 293 ? 127.907 102.085 152.858 1.00 27.13 ?  272 GLY D CA    1 
ATOM   15586 C  C     . GLY D 2 293 ? 128.649 101.638 154.101 1.00 27.99 ?  272 GLY D C     1 
ATOM   15587 O  O     . GLY D 2 293 ? 128.274 102.013 155.208 1.00 27.97 ?  272 GLY D O     1 
ATOM   15588 N  N     . PHE D 2 294 ? 129.701 100.834 153.921 1.00 28.02 ?  273 PHE D N     1 
ATOM   15589 C  CA    . PHE D 2 294 ? 130.514 100.337 155.038 1.00 28.75 ?  273 PHE D CA    1 
ATOM   15590 C  C     . PHE D 2 294 ? 131.836 101.100 155.184 1.00 29.00 ?  273 PHE D C     1 
ATOM   15591 O  O     . PHE D 2 294 ? 132.298 101.737 154.239 1.00 28.74 ?  273 PHE D O     1 
ATOM   15592 C  CB    . PHE D 2 294 ? 130.808 98.838  154.864 1.00 28.32 ?  273 PHE D CB    1 
ATOM   15593 C  CG    . PHE D 2 294 ? 129.585 97.964  154.924 1.00 28.66 ?  273 PHE D CG    1 
ATOM   15594 C  CD1   . PHE D 2 294 ? 128.585 98.198  155.868 1.00 30.23 ?  273 PHE D CD1   1 
ATOM   15595 C  CD2   . PHE D 2 294 ? 129.442 96.897  154.047 1.00 26.94 ?  273 PHE D CD2   1 
ATOM   15596 C  CE1   . PHE D 2 294 ? 127.448 97.384  155.924 1.00 31.04 ?  273 PHE D CE1   1 
ATOM   15597 C  CE2   . PHE D 2 294 ? 128.323 96.077  154.094 1.00 27.39 ?  273 PHE D CE2   1 
ATOM   15598 C  CZ    . PHE D 2 294 ? 127.323 96.312  155.030 1.00 29.80 ?  273 PHE D CZ    1 
ATOM   15599 N  N     . ASP D 2 295 ? 132.434 101.030 156.371 1.00 29.60 ?  274 ASP D N     1 
ATOM   15600 C  CA    . ASP D 2 295 ? 133.729 101.655 156.631 1.00 30.40 ?  274 ASP D CA    1 
ATOM   15601 C  C     . ASP D 2 295 ? 134.869 100.929 155.892 1.00 29.58 ?  274 ASP D C     1 
ATOM   15602 O  O     . ASP D 2 295 ? 134.775 99.728  155.634 1.00 28.68 ?  274 ASP D O     1 
ATOM   15603 C  CB    . ASP D 2 295 ? 134.027 101.682 158.136 1.00 31.44 ?  274 ASP D CB    1 
ATOM   15604 C  CG    . ASP D 2 295 ? 133.063 102.566 158.920 1.00 34.27 ?  274 ASP D CG    1 
ATOM   15605 O  OD1   . ASP D 2 295 ? 132.530 103.552 158.356 1.00 36.43 ?  274 ASP D OD1   1 
ATOM   15606 O  OD2   . ASP D 2 295 ? 132.847 102.266 160.114 1.00 38.03 -1 274 ASP D OD2   1 
ATOM   15607 N  N     . PRO D 2 296 ? 135.953 101.656 155.561 1.00 29.59 ?  275 PRO D N     1 
ATOM   15608 C  CA    . PRO D 2 296 ? 137.096 100.977 154.943 1.00 29.09 ?  275 PRO D CA    1 
ATOM   15609 C  C     . PRO D 2 296 ? 137.683 99.929  155.889 1.00 29.26 ?  275 PRO D C     1 
ATOM   15610 O  O     . PRO D 2 296 ? 137.683 100.118 157.106 1.00 29.36 ?  275 PRO D O     1 
ATOM   15611 C  CB    . PRO D 2 296 ? 138.105 102.109 154.704 1.00 29.49 ?  275 PRO D CB    1 
ATOM   15612 C  CG    . PRO D 2 296 ? 137.667 103.235 155.600 1.00 30.28 ?  275 PRO D CG    1 
ATOM   15613 C  CD    . PRO D 2 296 ? 136.182 103.105 155.724 1.00 29.63 ?  275 PRO D CD    1 
ATOM   15614 N  N     . TYR D 2 297 ? 138.156 98.826  155.329 1.00 28.97 ?  276 TYR D N     1 
ATOM   15615 C  CA    . TYR D 2 297 ? 138.699 97.731  156.124 1.00 29.63 ?  276 TYR D CA    1 
ATOM   15616 C  C     . TYR D 2 297 ? 140.222 97.859  156.290 1.00 29.55 ?  276 TYR D C     1 
ATOM   15617 O  O     . TYR D 2 297 ? 140.786 97.498  157.331 1.00 30.12 ?  276 TYR D O     1 
ATOM   15618 C  CB    . TYR D 2 297 ? 138.357 96.410  155.436 1.00 29.49 ?  276 TYR D CB    1 
ATOM   15619 C  CG    . TYR D 2 297 ? 138.563 95.175  156.272 1.00 31.19 ?  276 TYR D CG    1 
ATOM   15620 C  CD1   . TYR D 2 297 ? 137.830 94.976  157.446 1.00 31.93 ?  276 TYR D CD1   1 
ATOM   15621 C  CD2   . TYR D 2 297 ? 139.470 94.189  155.880 1.00 31.98 ?  276 TYR D CD2   1 
ATOM   15622 C  CE1   . TYR D 2 297 ? 138.006 93.836  158.219 1.00 33.86 ?  276 TYR D CE1   1 
ATOM   15623 C  CE2   . TYR D 2 297 ? 139.651 93.036  156.646 1.00 33.88 ?  276 TYR D CE2   1 
ATOM   15624 C  CZ    . TYR D 2 297 ? 138.909 92.871  157.811 1.00 34.42 ?  276 TYR D CZ    1 
ATOM   15625 O  OH    . TYR D 2 297 ? 139.076 91.749  158.582 1.00 37.63 ?  276 TYR D OH    1 
ATOM   15626 N  N     . PHE D 2 298 ? 140.867 98.373  155.248 1.00 29.10 ?  277 PHE D N     1 
ATOM   15627 C  CA    . PHE D 2 298 ? 142.322 98.443  155.160 1.00 28.97 ?  277 PHE D CA    1 
ATOM   15628 C  C     . PHE D 2 298 ? 142.815 99.879  155.376 1.00 29.77 ?  277 PHE D C     1 
ATOM   15629 O  O     . PHE D 2 298 ? 142.126 100.839 155.020 1.00 29.07 ?  277 PHE D O     1 
ATOM   15630 C  CB    . PHE D 2 298 ? 142.788 97.945  153.787 1.00 27.99 ?  277 PHE D CB    1 
ATOM   15631 C  CG    . PHE D 2 298 ? 142.422 96.509  153.495 1.00 27.61 ?  277 PHE D CG    1 
ATOM   15632 C  CD1   . PHE D 2 298 ? 141.429 96.203  152.574 1.00 25.91 ?  277 PHE D CD1   1 
ATOM   15633 C  CD2   . PHE D 2 298 ? 143.090 95.462  154.133 1.00 27.32 ?  277 PHE D CD2   1 
ATOM   15634 C  CE1   . PHE D 2 298 ? 141.099 94.887  152.300 1.00 26.65 ?  277 PHE D CE1   1 
ATOM   15635 C  CE2   . PHE D 2 298 ? 142.772 94.142  153.868 1.00 25.38 ?  277 PHE D CE2   1 
ATOM   15636 C  CZ    . PHE D 2 298 ? 141.773 93.847  152.959 1.00 26.20 ?  277 PHE D CZ    1 
ATOM   15637 N  N     . GLU D 2 299 ? 144.003 100.011 155.965 1.00 31.10 ?  278 GLU D N     1 
ATOM   15638 C  CA    . GLU D 2 299 ? 144.660 101.312 156.116 1.00 32.86 ?  278 GLU D CA    1 
ATOM   15639 C  C     . GLU D 2 299 ? 144.930 101.923 154.734 1.00 33.04 ?  278 GLU D C     1 
ATOM   15640 O  O     . GLU D 2 299 ? 145.125 101.199 153.753 1.00 32.23 ?  278 GLU D O     1 
ATOM   15641 C  CB    . GLU D 2 299 ? 145.967 101.174 156.915 1.00 33.45 ?  278 GLU D CB    1 
ATOM   15642 C  CG    . GLU D 2 299 ? 147.012 100.274 156.237 1.00 36.27 ?  278 GLU D CG    1 
ATOM   15643 C  CD    . GLU D 2 299 ? 148.361 100.231 156.938 1.00 40.47 ?  278 GLU D CD    1 
ATOM   15644 O  OE1   . GLU D 2 299 ? 148.408 100.185 158.189 1.00 41.72 ?  278 GLU D OE1   1 
ATOM   15645 O  OE2   . GLU D 2 299 ? 149.382 100.212 156.216 1.00 42.65 -1 278 GLU D OE2   1 
ATOM   15646 N  N     . GLU D 2 300 ? 144.930 103.253 154.675 1.00 34.09 ?  279 GLU D N     1 
ATOM   15647 C  CA    . GLU D 2 300 ? 145.196 103.988 153.446 1.00 35.06 ?  279 GLU D CA    1 
ATOM   15648 C  C     . GLU D 2 300 ? 146.646 103.781 153.007 1.00 34.97 ?  279 GLU D C     1 
ATOM   15649 O  O     . GLU D 2 300 ? 147.567 103.839 153.823 1.00 34.96 ?  279 GLU D O     1 
ATOM   15650 C  CB    . GLU D 2 300 ? 144.892 105.483 153.646 1.00 35.81 ?  279 GLU D CB    1 
ATOM   15651 C  CG    . GLU D 2 300 ? 144.955 106.317 152.365 1.00 38.58 ?  279 GLU D CG    1 
ATOM   15652 C  CD    . GLU D 2 300 ? 144.113 107.589 152.434 1.00 43.09 ?  279 GLU D CD    1 
ATOM   15653 O  OE1   . GLU D 2 300 ? 143.234 107.766 151.560 1.00 44.69 ?  279 GLU D OE1   1 
ATOM   15654 O  OE2   . GLU D 2 300 ? 144.321 108.406 153.362 1.00 44.94 -1 279 GLU D OE2   1 
ATOM   15655 N  N     . GLU D 2 301 ? 146.827 103.513 151.717 1.00 34.73 ?  280 GLU D N     1 
ATOM   15656 C  CA    . GLU D 2 301 ? 148.147 103.326 151.129 1.00 35.16 ?  280 GLU D CA    1 
ATOM   15657 C  C     . GLU D 2 301 ? 148.239 104.144 149.852 1.00 35.23 ?  280 GLU D C     1 
ATOM   15658 O  O     . GLU D 2 301 ? 147.224 104.401 149.196 1.00 34.92 ?  280 GLU D O     1 
ATOM   15659 C  CB    . GLU D 2 301 ? 148.385 101.845 150.802 1.00 35.10 ?  280 GLU D CB    1 
ATOM   15660 C  CG    . GLU D 2 301 ? 148.809 100.984 151.990 1.00 36.62 ?  280 GLU D CG    1 
ATOM   15661 C  CD    . GLU D 2 301 ? 148.770 99.487  151.683 1.00 37.59 ?  280 GLU D CD    1 
ATOM   15662 O  OE1   . GLU D 2 301 ? 147.698 98.976  151.295 1.00 38.10 ?  280 GLU D OE1   1 
ATOM   15663 O  OE2   . GLU D 2 301 ? 149.804 98.814  151.854 1.00 38.93 -1 280 GLU D OE2   1 
ATOM   15664 N  N     . ASP D 2 302 ? 149.450 104.554 149.495 1.00 35.60 ?  281 ASP D N     1 
ATOM   15665 C  CA    . ASP D 2 302 ? 149.658 105.240 148.226 1.00 35.96 ?  281 ASP D CA    1 
ATOM   15666 C  C     . ASP D 2 302 ? 149.714 104.197 147.117 1.00 35.01 ?  281 ASP D C     1 
ATOM   15667 O  O     . ASP D 2 302 ? 150.072 103.046 147.365 1.00 35.52 ?  281 ASP D O     1 
ATOM   15668 C  CB    . ASP D 2 302 ? 150.919 106.121 148.265 1.00 36.82 ?  281 ASP D CB    1 
ATOM   15669 C  CG    . ASP D 2 302 ? 152.220 105.321 148.462 1.00 39.01 ?  281 ASP D CG    1 
ATOM   15670 O  OD1   . ASP D 2 302 ? 152.193 104.168 148.960 1.00 40.83 ?  281 ASP D OD1   1 
ATOM   15671 O  OD2   . ASP D 2 302 ? 153.288 105.875 148.131 1.00 41.13 -1 281 ASP D OD2   1 
ATOM   15672 N  N     . ILE D 2 303 ? 149.324 104.579 145.908 1.00 33.94 ?  282 ILE D N     1 
ATOM   15673 C  CA    . ILE D 2 303 ? 149.327 103.646 144.784 1.00 33.00 ?  282 ILE D CA    1 
ATOM   15674 C  C     . ILE D 2 303 ? 150.475 103.924 143.805 1.00 31.59 ?  282 ILE D C     1 
ATOM   15675 O  O     . ILE D 2 303 ? 150.936 105.061 143.686 1.00 31.14 ?  282 ILE D O     1 
ATOM   15676 C  CB    . ILE D 2 303 ? 147.932 103.593 144.083 1.00 33.44 ?  282 ILE D CB    1 
ATOM   15677 C  CG1   . ILE D 2 303 ? 148.051 103.271 142.588 1.00 34.29 ?  282 ILE D CG1   1 
ATOM   15678 C  CG2   . ILE D 2 303 ? 147.166 104.886 144.311 1.00 35.47 ?  282 ILE D CG2   1 
ATOM   15679 C  CD1   . ILE D 2 303 ? 146.753 103.404 141.817 1.00 36.30 ?  282 ILE D CD1   1 
ATOM   15680 N  N     . ASN D 2 304 ? 150.946 102.873 143.132 1.00 29.53 ?  283 ASN D N     1 
ATOM   15681 C  CA    . ASN D 2 304 ? 151.974 103.006 142.104 1.00 28.49 ?  283 ASN D CA    1 
ATOM   15682 C  C     . ASN D 2 304 ? 151.669 104.176 141.144 1.00 27.87 ?  283 ASN D C     1 
ATOM   15683 O  O     . ASN D 2 304 ? 150.590 104.225 140.556 1.00 27.02 ?  283 ASN D O     1 
ATOM   15684 C  CB    . ASN D 2 304 ? 152.107 101.695 141.326 1.00 28.20 ?  283 ASN D CB    1 
ATOM   15685 C  CG    . ASN D 2 304 ? 153.218 101.739 140.311 1.00 28.17 ?  283 ASN D CG    1 
ATOM   15686 O  OD1   . ASN D 2 304 ? 153.024 102.199 139.191 1.00 29.01 ?  283 ASN D OD1   1 
ATOM   15687 N  ND2   . ASN D 2 304 ? 154.391 101.260 140.694 1.00 27.24 ?  283 ASN D ND2   1 
ATOM   15688 N  N     . PRO D 2 305 ? 152.614 105.127 140.998 1.00 28.00 ?  284 PRO D N     1 
ATOM   15689 C  CA    . PRO D 2 305 ? 152.353 106.332 140.196 1.00 27.58 ?  284 PRO D CA    1 
ATOM   15690 C  C     . PRO D 2 305 ? 152.162 106.074 138.700 1.00 27.01 ?  284 PRO D C     1 
ATOM   15691 O  O     . PRO D 2 305 ? 151.510 106.865 138.026 1.00 26.66 ?  284 PRO D O     1 
ATOM   15692 C  CB    . PRO D 2 305 ? 153.596 107.201 140.434 1.00 28.21 ?  284 PRO D CB    1 
ATOM   15693 C  CG    . PRO D 2 305 ? 154.636 106.285 140.909 1.00 28.80 ?  284 PRO D CG    1 
ATOM   15694 C  CD    . PRO D 2 305 ? 153.913 105.212 141.693 1.00 28.11 ?  284 PRO D CD    1 
ATOM   15695 N  N     . ILE D 2 306 ? 152.720 104.980 138.190 1.00 26.52 ?  285 ILE D N     1 
ATOM   15696 C  CA    . ILE D 2 306 ? 152.540 104.626 136.787 1.00 26.50 ?  285 ILE D CA    1 
ATOM   15697 C  C     . ILE D 2 306 ? 151.089 104.190 136.539 1.00 26.43 ?  285 ILE D C     1 
ATOM   15698 O  O     . ILE D 2 306 ? 150.430 104.661 135.601 1.00 26.00 ?  285 ILE D O     1 
ATOM   15699 C  CB    . ILE D 2 306 ? 153.562 103.557 136.326 1.00 26.88 ?  285 ILE D CB    1 
ATOM   15700 C  CG1   . ILE D 2 306 ? 154.993 104.098 136.494 1.00 26.98 ?  285 ILE D CG1   1 
ATOM   15701 C  CG2   . ILE D 2 306 ? 153.273 103.146 134.882 1.00 24.94 ?  285 ILE D CG2   1 
ATOM   15702 C  CD1   . ILE D 2 306 ? 156.087 103.093 136.260 1.00 26.65 ?  285 ILE D CD1   1 
ATOM   15703 N  N     . VAL D 2 307 ? 150.591 103.317 137.408 1.00 26.36 ?  286 VAL D N     1 
ATOM   15704 C  CA    . VAL D 2 307 ? 149.184 102.939 137.396 1.00 26.71 ?  286 VAL D CA    1 
ATOM   15705 C  C     . VAL D 2 307 ? 148.271 104.151 137.613 1.00 27.68 ?  286 VAL D C     1 
ATOM   15706 O  O     . VAL D 2 307 ? 147.263 104.282 136.918 1.00 27.92 ?  286 VAL D O     1 
ATOM   15707 C  CB    . VAL D 2 307 ? 148.891 101.789 138.398 1.00 26.37 ?  286 VAL D CB    1 
ATOM   15708 C  CG1   . VAL D 2 307 ? 147.380 101.561 138.571 1.00 25.48 ?  286 VAL D CG1   1 
ATOM   15709 C  CG2   . VAL D 2 307 ? 149.537 100.536 137.901 1.00 25.55 ?  286 VAL D CG2   1 
ATOM   15710 N  N     . LEU D 2 308 ? 148.632 105.051 138.532 1.00 28.80 ?  287 LEU D N     1 
ATOM   15711 C  CA    . LEU D 2 308 ? 147.869 106.299 138.700 1.00 30.07 ?  287 LEU D CA    1 
ATOM   15712 C  C     . LEU D 2 308 ? 147.809 107.129 137.414 1.00 30.38 ?  287 LEU D C     1 
ATOM   15713 O  O     . LEU D 2 308 ? 146.758 107.676 137.063 1.00 30.71 ?  287 LEU D O     1 
ATOM   15714 C  CB    . LEU D 2 308 ? 148.420 107.148 139.849 1.00 30.86 ?  287 LEU D CB    1 
ATOM   15715 C  CG    . LEU D 2 308 ? 147.913 106.786 141.249 1.00 32.62 ?  287 LEU D CG    1 
ATOM   15716 C  CD1   . LEU D 2 308 ? 148.677 107.548 142.309 1.00 33.97 ?  287 LEU D CD1   1 
ATOM   15717 C  CD2   . LEU D 2 308 ? 146.399 107.034 141.384 1.00 34.73 ?  287 LEU D CD2   1 
ATOM   15718 N  N     . ASN D 2 309 ? 148.930 107.214 136.707 1.00 30.81 ?  288 ASN D N     1 
ATOM   15719 C  CA    . ASN D 2 309 ? 148.967 107.939 135.441 1.00 31.25 ?  288 ASN D CA    1 
ATOM   15720 C  C     . ASN D 2 309 ? 148.072 107.284 134.388 1.00 31.83 ?  288 ASN D C     1 
ATOM   15721 O  O     . ASN D 2 309 ? 147.469 107.973 133.560 1.00 31.73 ?  288 ASN D O     1 
ATOM   15722 C  CB    . ASN D 2 309 ? 150.402 108.100 134.926 1.00 31.21 ?  288 ASN D CB    1 
ATOM   15723 C  CG    . ASN D 2 309 ? 150.481 109.021 133.719 1.00 31.41 ?  288 ASN D CG    1 
ATOM   15724 O  OD1   . ASN D 2 309 ? 149.856 110.087 133.697 1.00 31.88 ?  288 ASN D OD1   1 
ATOM   15725 N  ND2   . ASN D 2 309 ? 151.241 108.613 132.707 1.00 29.12 ?  288 ASN D ND2   1 
ATOM   15726 N  N     . GLY D 2 310 ? 147.987 105.954 134.433 1.00 32.04 ?  289 GLY D N     1 
ATOM   15727 C  CA    . GLY D 2 310 ? 147.057 105.205 133.596 1.00 33.04 ?  289 GLY D CA    1 
ATOM   15728 C  C     . GLY D 2 310 ? 145.610 105.511 133.960 1.00 33.85 ?  289 GLY D C     1 
ATOM   15729 O  O     . GLY D 2 310 ? 144.792 105.781 133.080 1.00 34.05 ?  289 GLY D O     1 
ATOM   15730 N  N     . LEU D 2 311 ? 145.301 105.471 135.255 1.00 34.33 ?  290 LEU D N     1 
ATOM   15731 C  CA    . LEU D 2 311 ? 143.947 105.721 135.759 1.00 35.77 ?  290 LEU D CA    1 
ATOM   15732 C  C     . LEU D 2 311 ? 143.435 107.123 135.444 1.00 37.01 ?  290 LEU D C     1 
ATOM   15733 O  O     . LEU D 2 311 ? 142.266 107.298 135.097 1.00 37.18 ?  290 LEU D O     1 
ATOM   15734 C  CB    . LEU D 2 311 ? 143.889 105.510 137.277 1.00 35.50 ?  290 LEU D CB    1 
ATOM   15735 C  CG    . LEU D 2 311 ? 143.551 104.152 137.884 1.00 35.45 ?  290 LEU D CG    1 
ATOM   15736 C  CD1   . LEU D 2 311 ? 143.758 104.215 139.406 1.00 35.28 ?  290 LEU D CD1   1 
ATOM   15737 C  CD2   . LEU D 2 311 ? 142.123 103.708 137.558 1.00 34.16 ?  290 LEU D CD2   1 
ATOM   15738 N  N     . LYS D 2 330 ? 119.049 118.024 150.416 1.00 42.55 ?  309 LYS D N     1 
ATOM   15739 C  CA    . LYS D 2 330 ? 117.652 117.812 150.056 1.00 44.90 ?  309 LYS D CA    1 
ATOM   15740 C  C     . LYS D 2 330 ? 116.768 117.652 151.287 1.00 43.76 ?  309 LYS D C     1 
ATOM   15741 O  O     . LYS D 2 330 ? 116.582 116.545 151.790 1.00 44.28 ?  309 LYS D O     1 
ATOM   15742 C  CB    . LYS D 2 330 ? 117.513 116.582 149.154 1.00 40.63 ?  309 LYS D CB    1 
ATOM   15743 C  CG    . LYS D 2 330 ? 116.165 116.474 148.456 1.00 43.98 ?  309 LYS D CG    1 
ATOM   15744 C  CD    . LYS D 2 330 ? 115.917 117.650 147.525 1.00 43.19 ?  309 LYS D CD    1 
ATOM   15745 C  CE    . LYS D 2 330 ? 115.963 117.218 146.069 1.00 45.38 ?  309 LYS D CE    1 
ATOM   15746 N  NZ    . LYS D 2 330 ? 116.021 118.384 145.145 1.00 43.90 1  309 LYS D NZ    1 
ATOM   15747 N  N     . ALA D 2 331 ? 116.226 118.767 151.770 1.00 41.98 ?  310 ALA D N     1 
ATOM   15748 C  CA    . ALA D 2 331 ? 115.277 118.724 152.868 1.00 42.36 ?  310 ALA D CA    1 
ATOM   15749 C  C     . ALA D 2 331 ? 113.940 118.164 152.389 1.00 42.70 ?  310 ALA D C     1 
ATOM   15750 O  O     . ALA D 2 331 ? 113.613 118.199 151.200 1.00 44.14 ?  310 ALA D O     1 
ATOM   15751 C  CB    . ALA D 2 331 ? 115.081 120.113 153.473 1.00 39.32 ?  310 ALA D CB    1 
ATOM   15752 N  N     . THR D 2 332 ? 113.168 117.640 153.335 1.00 33.29 ?  311 THR D N     1 
ATOM   15753 C  CA    . THR D 2 332 ? 111.890 117.006 153.023 1.00 32.46 ?  311 THR D CA    1 
ATOM   15754 C  C     . THR D 2 332 ? 110.929 118.063 152.498 1.00 32.78 ?  311 THR D C     1 
ATOM   15755 O  O     . THR D 2 332 ? 110.642 119.053 153.175 1.00 35.85 ?  311 THR D O     1 
ATOM   15756 C  CB    . THR D 2 332 ? 111.323 116.309 154.256 1.00 36.71 ?  311 THR D CB    1 
ATOM   15757 O  OG1   . THR D 2 332 ? 111.961 115.037 154.421 1.00 39.19 ?  311 THR D OG1   1 
ATOM   15758 C  CG2   . THR D 2 332 ? 109.824 116.090 154.102 1.00 34.82 ?  311 THR D CG2   1 
ATOM   15759 N  N     . VAL D 2 333 ? 110.439 117.866 151.277 1.00 30.31 ?  312 VAL D N     1 
ATOM   15760 C  CA    . VAL D 2 333 ? 109.487 118.792 150.675 1.00 24.24 ?  312 VAL D CA    1 
ATOM   15761 C  C     . VAL D 2 333 ? 108.109 118.536 151.267 1.00 30.13 ?  312 VAL D C     1 
ATOM   15762 O  O     . VAL D 2 333 ? 107.537 117.454 151.094 1.00 35.56 ?  312 VAL D O     1 
ATOM   15763 C  CB    . VAL D 2 333 ? 109.465 118.657 149.142 1.00 29.05 ?  312 VAL D CB    1 
ATOM   15764 C  CG1   . VAL D 2 333 ? 108.575 119.727 148.531 1.00 31.60 ?  312 VAL D CG1   1 
ATOM   15765 C  CG2   . VAL D 2 333 ? 110.876 118.743 148.584 1.00 29.59 ?  312 VAL D CG2   1 
ATOM   15766 N  N     . GLU D 2 334 ? 107.568 119.527 151.970 1.00 28.79 ?  313 GLU D N     1 
ATOM   15767 C  CA    . GLU D 2 334 ? 106.249 119.423 152.578 1.00 29.66 ?  313 GLU D CA    1 
ATOM   15768 C  C     . GLU D 2 334 ? 105.389 120.575 152.077 1.00 31.26 ?  313 GLU D C     1 
ATOM   15769 O  O     . GLU D 2 334 ? 105.774 121.745 152.242 1.00 34.83 ?  313 GLU D O     1 
ATOM   15770 C  CB    . GLU D 2 334 ? 106.347 119.442 154.105 1.00 29.26 ?  313 GLU D CB    1 
ATOM   15771 C  CG    . GLU D 2 334 ? 105.025 119.665 154.815 1.00 33.58 ?  313 GLU D CG    1 
ATOM   15772 C  CD    . GLU D 2 334 ? 105.140 119.498 156.318 1.00 35.28 ?  313 GLU D CD    1 
ATOM   15773 O  OE1   . GLU D 2 334 ? 106.218 119.803 156.869 1.00 33.47 ?  313 GLU D OE1   1 
ATOM   15774 O  OE2   . GLU D 2 334 ? 104.153 119.061 156.947 1.00 31.19 -1 313 GLU D OE2   1 
ATOM   15775 N  N     . PRO D 2 335 ? 104.241 120.306 151.457 1.00 31.21 ?  314 PRO D N     1 
ATOM   15776 C  CA    . PRO D 2 335 ? 103.446 121.388 150.867 1.00 33.35 ?  314 PRO D CA    1 
ATOM   15777 C  C     . PRO D 2 335 ? 102.917 122.346 151.925 1.00 33.18 ?  314 PRO D C     1 
ATOM   15778 O  O     . PRO D 2 335 ? 102.670 121.965 153.071 1.00 33.38 ?  314 PRO D O     1 
ATOM   15779 C  CB    . PRO D 2 335 ? 102.305 120.644 150.164 1.00 30.11 ?  314 PRO D CB    1 
ATOM   15780 C  CG    . PRO D 2 335 ? 102.242 119.314 150.848 1.00 31.03 ?  314 PRO D CG    1 
ATOM   15781 C  CD    . PRO D 2 335 ? 103.659 118.983 151.184 1.00 33.22 ?  314 PRO D CD    1 
ATOM   15782 N  N     . LEU D 2 336 ? 102.750 123.605 151.529 1.00 30.38 ?  315 LEU D N     1 
ATOM   15783 C  CA    . LEU D 2 336 ? 102.128 124.591 152.397 1.00 26.61 ?  315 LEU D CA    1 
ATOM   15784 C  C     . LEU D 2 336 ? 100.650 124.266 152.572 1.00 27.64 ?  315 LEU D C     1 
ATOM   15785 O  O     . LEU D 2 336 ? 99.913  124.078 151.602 1.00 34.77 ?  315 LEU D O     1 
ATOM   15786 C  CB    . LEU D 2 336 ? 102.300 125.996 151.820 1.00 22.39 ?  315 LEU D CB    1 
ATOM   15787 C  CG    . LEU D 2 336 ? 103.626 126.691 152.136 1.00 25.97 ?  315 LEU D CG    1 
ATOM   15788 C  CD1   . LEU D 2 336 ? 103.722 128.023 151.412 1.00 19.59 ?  315 LEU D CD1   1 
ATOM   15789 C  CD2   . LEU D 2 336 ? 103.799 126.878 153.636 1.00 27.01 ?  315 LEU D CD2   1 
ATOM   15790 N  N     . LYS D 2 337 ? 100.221 124.204 153.832 1.00 28.30 ?  316 LYS D N     1 
ATOM   15791 C  CA    . LYS D 2 337 ? 98.893  123.711 154.182 1.00 36.46 ?  316 LYS D CA    1 
ATOM   15792 C  C     . LYS D 2 337 ? 97.886  124.826 154.424 1.00 36.32 ?  316 LYS D C     1 
ATOM   15793 O  O     . LYS D 2 337 ? 96.800  124.552 154.948 1.00 40.02 ?  316 LYS D O     1 
ATOM   15794 C  CB    . LYS D 2 337 ? 98.970  122.819 155.424 1.00 33.57 ?  316 LYS D CB    1 
ATOM   15795 C  CG    . LYS D 2 337 ? 100.119 121.831 155.412 1.00 36.47 ?  316 LYS D CG    1 
ATOM   15796 C  CD    . LYS D 2 337 ? 99.657  120.451 155.842 1.00 38.79 ?  316 LYS D CD    1 
ATOM   15797 C  CE    . LYS D 2 337 ? 100.839 119.545 156.129 1.00 37.56 ?  316 LYS D CE    1 
ATOM   15798 N  NZ    . LYS D 2 337 ? 101.738 119.439 154.950 1.00 36.72 1  316 LYS D NZ    1 
ATOM   15799 N  N     . ASP D 2 338 ? 98.225  126.071 154.076 1.00 24.38 ?  317 ASP D N     1 
ATOM   15800 C  CA    . ASP D 2 338 ? 97.433  127.251 154.418 1.00 29.04 ?  317 ASP D CA    1 
ATOM   15801 C  C     . ASP D 2 338 ? 97.405  127.430 155.933 1.00 28.87 ?  317 ASP D C     1 
ATOM   15802 O  O     . ASP D 2 338 ? 97.787  126.521 156.677 1.00 33.66 ?  317 ASP D O     1 
ATOM   15803 C  CB    . ASP D 2 338 ? 96.016  127.162 153.840 1.00 31.69 ?  317 ASP D CB    1 
ATOM   15804 C  CG    . ASP D 2 338 ? 95.283  128.488 153.886 1.00 32.42 ?  317 ASP D CG    1 
ATOM   15805 O  OD1   . ASP D 2 338 ? 95.955  129.535 153.984 1.00 34.34 ?  317 ASP D OD1   1 
ATOM   15806 O  OD2   . ASP D 2 338 ? 94.036  128.484 153.821 1.00 28.35 -1 317 ASP D OD2   1 
ATOM   15807 N  N     . ASP D 2 339 ? 97.003  128.617 156.392 1.00 22.82 ?  318 ASP D N     1 
ATOM   15808 C  CA    . ASP D 2 339 ? 97.085  129.012 157.797 1.00 24.73 ?  318 ASP D CA    1 
ATOM   15809 C  C     . ASP D 2 339 ? 98.544  129.128 158.226 1.00 24.49 ?  318 ASP D C     1 
ATOM   15810 O  O     . ASP D 2 339 ? 98.837  129.473 159.375 1.00 31.22 ?  318 ASP D O     1 
ATOM   15811 C  CB    . ASP D 2 339 ? 96.321  128.039 158.702 1.00 23.30 ?  318 ASP D CB    1 
ATOM   15812 C  CG    . ASP D 2 339 ? 94.956  127.682 158.149 1.00 31.35 ?  318 ASP D CG    1 
ATOM   15813 O  OD1   . ASP D 2 339 ? 94.108  128.591 158.019 1.00 29.84 ?  318 ASP D OD1   1 
ATOM   15814 O  OD2   . ASP D 2 339 ? 94.729  126.493 157.840 1.00 30.37 -1 318 ASP D OD2   1 
ATOM   15815 N  N     . ASP D 2 340 ? 99.463  128.838 157.307 1.00 24.54 ?  319 ASP D N     1 
ATOM   15816 C  CA    . ASP D 2 340 ? 100.867 129.190 157.440 1.00 16.40 ?  319 ASP D CA    1 
ATOM   15817 C  C     . ASP D 2 340 ? 101.129 130.611 156.973 1.00 13.50 ?  319 ASP D C     1 
ATOM   15818 O  O     . ASP D 2 340 ? 102.238 131.123 157.152 1.00 33.12 ?  319 ASP D O     1 
ATOM   15819 C  CB    . ASP D 2 340 ? 101.735 128.213 156.645 1.00 15.31 ?  319 ASP D CB    1 
ATOM   15820 C  CG    . ASP D 2 340 ? 101.732 126.817 157.234 1.00 20.12 ?  319 ASP D CG    1 
ATOM   15821 O  OD1   . ASP D 2 340 ? 101.589 126.690 158.468 1.00 32.00 ?  319 ASP D OD1   1 
ATOM   15822 O  OD2   . ASP D 2 340 ? 101.873 125.847 156.461 1.00 22.25 -1 319 ASP D OD2   1 
ATOM   15823 N  N     . PHE D 2 341 ? 100.123 131.251 156.374 1.00 10.33 ?  320 PHE D N     1 
ATOM   15824 C  CA    . PHE D 2 341 ? 100.201 132.636 155.936 1.00 15.27 ?  320 PHE D CA    1 
ATOM   15825 C  C     . PHE D 2 341 ? 99.585  133.580 156.959 1.00 19.34 ?  320 PHE D C     1 
ATOM   15826 O  O     . PHE D 2 341 ? 99.557  134.794 156.728 1.00 16.81 ?  320 PHE D O     1 
ATOM   15827 C  CB    . PHE D 2 341 ? 99.493  132.807 154.588 1.00 19.36 ?  320 PHE D CB    1 
ATOM   15828 C  CG    . PHE D 2 341 ? 100.135 132.049 153.464 1.00 13.21 ?  320 PHE D CG    1 
ATOM   15829 C  CD1   . PHE D 2 341 ? 101.113 132.636 152.681 1.00 12.45 ?  320 PHE D CD1   1 
ATOM   15830 C  CD2   . PHE D 2 341 ? 99.759  130.745 153.191 1.00 11.41 ?  320 PHE D CD2   1 
ATOM   15831 C  CE1   . PHE D 2 341 ? 101.700 131.938 151.645 1.00 11.53 ?  320 PHE D CE1   1 
ATOM   15832 C  CE2   . PHE D 2 341 ? 100.345 130.044 152.158 1.00 15.13 ?  320 PHE D CE2   1 
ATOM   15833 C  CZ    . PHE D 2 341 ? 101.316 130.641 151.385 1.00 8.25  ?  320 PHE D CZ    1 
ATOM   15834 N  N     . TYR D 2 342 ? 99.088  133.054 158.075 1.00 12.30 ?  321 TYR D N     1 
ATOM   15835 C  CA    . TYR D 2 342 ? 98.400  133.839 159.086 1.00 16.33 ?  321 TYR D CA    1 
ATOM   15836 C  C     . TYR D 2 342 ? 99.070  133.611 160.430 1.00 22.82 ?  321 TYR D C     1 
ATOM   15837 O  O     . TYR D 2 342 ? 99.502  132.495 160.737 1.00 19.28 ?  321 TYR D O     1 
ATOM   15838 C  CB    . TYR D 2 342 ? 96.917  133.462 159.161 1.00 12.46 ?  321 TYR D CB    1 
ATOM   15839 C  CG    . TYR D 2 342 ? 96.176  133.672 157.861 1.00 15.87 ?  321 TYR D CG    1 
ATOM   15840 C  CD1   . TYR D 2 342 ? 95.664  134.917 157.523 1.00 18.56 ?  321 TYR D CD1   1 
ATOM   15841 C  CD2   . TYR D 2 342 ? 95.995  132.625 156.968 1.00 15.63 ?  321 TYR D CD2   1 
ATOM   15842 C  CE1   . TYR D 2 342 ? 94.990  135.112 156.333 1.00 14.14 ?  321 TYR D CE1   1 
ATOM   15843 C  CE2   . TYR D 2 342 ? 95.323  132.810 155.776 1.00 15.01 ?  321 TYR D CE2   1 
ATOM   15844 C  CZ    . TYR D 2 342 ? 94.822  134.055 155.464 1.00 17.53 ?  321 TYR D CZ    1 
ATOM   15845 O  OH    . TYR D 2 342 ? 94.150  134.245 154.279 1.00 21.36 ?  321 TYR D OH    1 
ATOM   15846 N  N     . PHE D 2 343 ? 99.162  134.672 161.224 1.00 12.45 ?  322 PHE D N     1 
ATOM   15847 C  CA    . PHE D 2 343 ? 99.884  134.616 162.487 1.00 16.01 ?  322 PHE D CA    1 
ATOM   15848 C  C     . PHE D 2 343 ? 99.136  135.370 163.581 1.00 27.60 ?  322 PHE D C     1 
ATOM   15849 O  O     . PHE D 2 343 ? 98.360  136.283 163.303 1.00 22.19 ?  322 PHE D O     1 
ATOM   15850 C  CB    . PHE D 2 343 ? 101.294 135.187 162.314 1.00 18.28 ?  322 PHE D CB    1 
ATOM   15851 C  CG    . PHE D 2 343 ? 102.020 134.650 161.113 1.00 19.26 ?  322 PHE D CG    1 
ATOM   15852 C  CD1   . PHE D 2 343 ? 102.742 133.472 161.190 1.00 20.02 ?  322 PHE D CD1   1 
ATOM   15853 C  CD2   . PHE D 2 343 ? 101.965 135.316 159.899 1.00 13.80 ?  322 PHE D CD2   1 
ATOM   15854 C  CE1   . PHE D 2 343 ? 103.401 132.974 160.084 1.00 12.20 ?  322 PHE D CE1   1 
ATOM   15855 C  CE2   . PHE D 2 343 ? 102.620 134.823 158.792 1.00 9.90  ?  322 PHE D CE2   1 
ATOM   15856 C  CZ    . PHE D 2 343 ? 103.339 133.650 158.884 1.00 11.36 ?  322 PHE D CZ    1 
HETATM 15857 P  PG    . ATP E 3 .   ? 107.014 131.989 81.121  1.00 68.91 ?  801 ATP A PG    1 
HETATM 15858 O  O1G   . ATP E 3 .   ? 105.809 132.311 80.303  1.00 61.99 ?  801 ATP A O1G   1 
HETATM 15859 O  O2G   . ATP E 3 .   ? 108.229 132.868 80.798  1.00 61.48 -1 801 ATP A O2G   1 
HETATM 15860 O  O3G   . ATP E 3 .   ? 106.760 132.024 82.632  1.00 57.91 ?  801 ATP A O3G   1 
HETATM 15861 P  PB    . ATP E 3 .   ? 108.665 129.727 80.052  1.00 68.42 ?  801 ATP A PB    1 
HETATM 15862 O  O1B   . ATP E 3 .   ? 108.538 129.879 78.588  1.00 59.48 -1 801 ATP A O1B   1 
HETATM 15863 O  O2B   . ATP E 3 .   ? 109.996 130.183 80.650  1.00 59.06 ?  801 ATP A O2B   1 
HETATM 15864 O  O3B   . ATP E 3 .   ? 107.510 130.496 80.831  1.00 62.04 ?  801 ATP A O3B   1 
HETATM 15865 P  PA    . ATP E 3 .   ? 108.547 127.394 81.869  1.00 63.87 ?  801 ATP A PA    1 
HETATM 15866 O  O1A   . ATP E 3 .   ? 109.697 126.467 81.835  1.00 60.02 -1 801 ATP A O1A   1 
HETATM 15867 O  O2A   . ATP E 3 .   ? 107.193 126.728 82.110  1.00 58.33 ?  801 ATP A O2A   1 
HETATM 15868 O  O3A   . ATP E 3 .   ? 108.427 128.223 80.516  1.00 62.45 ?  801 ATP A O3A   1 
HETATM 15869 O  "O5'" . ATP E 3 .   ? 108.748 128.517 82.959  1.00 59.78 ?  801 ATP A "O5'" 1 
HETATM 15870 C  "C5'" . ATP E 3 .   ? 107.676 128.904 83.843  1.00 58.13 ?  801 ATP A "C5'" 1 
HETATM 15871 C  "C4'" . ATP E 3 .   ? 108.205 129.901 84.842  1.00 59.51 ?  801 ATP A "C4'" 1 
HETATM 15872 O  "O4'" . ATP E 3 .   ? 108.682 129.203 86.015  1.00 62.13 ?  801 ATP A "O4'" 1 
HETATM 15873 C  "C3'" . ATP E 3 .   ? 109.384 130.741 84.361  1.00 57.82 ?  801 ATP A "C3'" 1 
HETATM 15874 O  "O3'" . ATP E 3 .   ? 108.938 131.930 83.719  1.00 58.51 ?  801 ATP A "O3'" 1 
HETATM 15875 C  "C2'" . ATP E 3 .   ? 110.119 131.051 85.665  1.00 58.31 ?  801 ATP A "C2'" 1 
HETATM 15876 O  "O2'" . ATP E 3 .   ? 109.525 132.140 86.359  1.00 58.66 ?  801 ATP A "O2'" 1 
HETATM 15877 C  "C1'" . ATP E 3 .   ? 109.921 129.744 86.438  1.00 58.50 ?  801 ATP A "C1'" 1 
HETATM 15878 N  N9    . ATP E 3 .   ? 110.962 128.750 86.203  1.00 58.48 ?  801 ATP A N9    1 
HETATM 15879 C  C8    . ATP E 3 .   ? 110.819 127.524 85.609  1.00 58.26 ?  801 ATP A C8    1 
HETATM 15880 N  N7    . ATP E 3 .   ? 111.930 126.834 85.529  1.00 56.05 ?  801 ATP A N7    1 
HETATM 15881 C  C5    . ATP E 3 .   ? 112.875 127.665 86.114  1.00 58.55 ?  801 ATP A C5    1 
HETATM 15882 C  C6    . ATP E 3 .   ? 114.256 127.520 86.344  1.00 56.46 ?  801 ATP A C6    1 
HETATM 15883 N  N6    . ATP E 3 .   ? 114.960 126.439 85.996  1.00 55.74 ?  801 ATP A N6    1 
HETATM 15884 N  N1    . ATP E 3 .   ? 114.901 128.539 86.953  1.00 57.23 ?  801 ATP A N1    1 
HETATM 15885 C  C2    . ATP E 3 .   ? 114.206 129.626 87.299  1.00 55.67 ?  801 ATP A C2    1 
HETATM 15886 N  N3    . ATP E 3 .   ? 112.905 129.873 87.136  1.00 57.17 ?  801 ATP A N3    1 
HETATM 15887 C  C4    . ATP E 3 .   ? 112.292 128.850 86.534  1.00 59.07 ?  801 ATP A C4    1 
HETATM 15888 P  PB    . GDP F 4 .   ? 104.524 145.767 82.220  1.00 70.96 ?  802 GDP A PB    1 
HETATM 15889 O  O1B   . GDP F 4 .   ? 105.701 144.976 81.702  1.00 59.03 ?  802 GDP A O1B   1 
HETATM 15890 O  O2B   . GDP F 4 .   ? 104.020 146.685 81.133  1.00 60.98 -1 802 GDP A O2B   1 
HETATM 15891 O  O3B   . GDP F 4 .   ? 103.422 144.822 82.636  1.00 60.51 ?  802 GDP A O3B   1 
HETATM 15892 O  O3A   . GDP F 4 .   ? 105.009 146.651 83.473  1.00 58.04 ?  802 GDP A O3A   1 
HETATM 15893 P  PA    . GDP F 4 .   ? 105.446 145.968 84.862  1.00 62.53 ?  802 GDP A PA    1 
HETATM 15894 O  O1A   . GDP F 4 .   ? 105.046 146.835 86.031  1.00 60.36 -1 802 GDP A O1A   1 
HETATM 15895 O  O2A   . GDP F 4 .   ? 104.857 144.586 85.008  1.00 57.51 ?  802 GDP A O2A   1 
HETATM 15896 O  "O5'" . GDP F 4 .   ? 107.050 145.897 84.741  1.00 58.41 ?  802 GDP A "O5'" 1 
HETATM 15897 C  "C5'" . GDP F 4 .   ? 107.846 145.888 85.920  1.00 58.74 ?  802 GDP A "C5'" 1 
HETATM 15898 C  "C4'" . GDP F 4 .   ? 108.929 144.826 85.825  1.00 56.36 ?  802 GDP A "C4'" 1 
HETATM 15899 O  "O4'" . GDP F 4 .   ? 109.206 144.360 87.147  1.00 56.52 ?  802 GDP A "O4'" 1 
HETATM 15900 C  "C3'" . GDP F 4 .   ? 108.465 143.642 84.996  1.00 58.64 ?  802 GDP A "C3'" 1 
HETATM 15901 O  "O3'" . GDP F 4 .   ? 109.355 143.439 83.894  1.00 59.90 ?  802 GDP A "O3'" 1 
HETATM 15902 C  "C2'" . GDP F 4 .   ? 108.502 142.438 85.913  1.00 57.17 ?  802 GDP A "C2'" 1 
HETATM 15903 O  "O2'" . GDP F 4 .   ? 109.311 141.407 85.341  1.00 58.14 ?  802 GDP A "O2'" 1 
HETATM 15904 C  "C1'" . GDP F 4 .   ? 109.126 142.934 87.209  1.00 54.02 ?  802 GDP A "C1'" 1 
HETATM 15905 N  N9    . GDP F 4 .   ? 108.364 142.506 88.413  1.00 54.87 ?  802 GDP A N9    1 
HETATM 15906 C  C8    . GDP F 4 .   ? 108.932 142.108 89.564  1.00 56.62 ?  802 GDP A C8    1 
HETATM 15907 N  N7    . GDP F 4 .   ? 108.001 141.781 90.493  1.00 56.41 ?  802 GDP A N7    1 
HETATM 15908 C  C5    . GDP F 4 .   ? 106.794 141.984 89.938  1.00 56.75 ?  802 GDP A C5    1 
HETATM 15909 C  C6    . GDP F 4 .   ? 105.387 141.838 90.378  1.00 57.45 ?  802 GDP A C6    1 
HETATM 15910 O  O6    . GDP F 4 .   ? 105.113 141.434 91.528  1.00 57.90 ?  802 GDP A O6    1 
HETATM 15911 N  N1    . GDP F 4 .   ? 104.421 142.148 89.507  1.00 57.76 ?  802 GDP A N1    1 
HETATM 15912 C  C2    . GDP F 4 .   ? 104.690 142.585 88.264  1.00 56.48 ?  802 GDP A C2    1 
HETATM 15913 N  N2    . GDP F 4 .   ? 103.655 142.879 87.443  1.00 57.02 ?  802 GDP A N2    1 
HETATM 15914 N  N3    . GDP F 4 .   ? 105.955 142.744 87.796  1.00 58.50 ?  802 GDP A N3    1 
HETATM 15915 C  C4    . GDP F 4 .   ? 107.034 142.465 88.569  1.00 57.68 ?  802 GDP A C4    1 
HETATM 15916 P  PA    . TTP G 5 .   ? 145.018 146.464 133.578 1.00 19.24 ?  803 TTP A PA    1 
HETATM 15917 O  O1A   . TTP G 5 .   ? 143.563 146.407 133.967 1.00 19.64 -1 803 TTP A O1A   1 
HETATM 15918 O  O2A   . TTP G 5 .   ? 145.300 147.646 132.687 1.00 31.54 ?  803 TTP A O2A   1 
HETATM 15919 O  O3A   . TTP G 5 .   ? 145.974 146.490 134.869 1.00 30.64 ?  803 TTP A O3A   1 
HETATM 15920 P  PB    . TTP G 5 .   ? 146.205 147.823 135.735 1.00 31.57 ?  803 TTP A PB    1 
HETATM 15921 O  O1B   . TTP G 5 .   ? 146.091 149.072 134.897 1.00 27.79 -1 803 TTP A O1B   1 
HETATM 15922 O  O2B   . TTP G 5 .   ? 145.238 147.872 136.890 1.00 31.36 ?  803 TTP A O2B   1 
HETATM 15923 O  O3B   . TTP G 5 .   ? 147.707 147.614 136.267 1.00 27.98 ?  803 TTP A O3B   1 
HETATM 15924 P  PG    . TTP G 5 .   ? 148.939 147.500 135.239 1.00 26.76 ?  803 TTP A PG    1 
HETATM 15925 O  O1G   . TTP G 5 .   ? 148.664 148.318 134.001 1.00 32.07 ?  803 TTP A O1G   1 
HETATM 15926 O  O2G   . TTP G 5 .   ? 150.203 147.989 135.900 1.00 34.92 -1 803 TTP A O2G   1 
HETATM 15927 O  O3G   . TTP G 5 .   ? 149.120 146.054 134.854 1.00 18.37 ?  803 TTP A O3G   1 
HETATM 15928 O  "O5'" . TTP G 5 .   ? 145.477 145.101 132.868 1.00 23.88 ?  803 TTP A "O5'" 1 
HETATM 15929 C  "C5'" . TTP G 5 .   ? 145.924 144.019 133.675 1.00 21.43 ?  803 TTP A "C5'" 1 
HETATM 15930 C  "C4'" . TTP G 5 .   ? 145.908 142.741 132.856 1.00 24.35 ?  803 TTP A "C4'" 1 
HETATM 15931 O  "O4'" . TTP G 5 .   ? 145.644 141.654 133.741 1.00 31.28 ?  803 TTP A "O4'" 1 
HETATM 15932 C  "C3'" . TTP G 5 .   ? 144.801 142.788 131.821 1.00 26.08 ?  803 TTP A "C3'" 1 
HETATM 15933 O  "O3'" . TTP G 5 .   ? 145.341 142.623 130.507 1.00 24.00 ?  803 TTP A "O3'" 1 
HETATM 15934 C  "C2'" . TTP G 5 .   ? 143.879 141.632 132.140 1.00 25.88 ?  803 TTP A "C2'" 1 
HETATM 15935 C  "C1'" . TTP G 5 .   ? 144.490 140.918 133.335 1.00 25.26 ?  803 TTP A "C1'" 1 
HETATM 15936 N  N1    . TTP G 5 .   ? 143.531 140.890 134.438 1.00 25.70 ?  803 TTP A N1    1 
HETATM 15937 C  C2    . TTP G 5 .   ? 143.116 139.654 134.978 1.00 25.54 ?  803 TTP A C2    1 
HETATM 15938 O  O2    . TTP G 5 .   ? 143.573 138.593 134.503 1.00 22.46 ?  803 TTP A O2    1 
HETATM 15939 N  N3    . TTP G 5 .   ? 142.241 139.596 135.989 1.00 24.38 ?  803 TTP A N3    1 
HETATM 15940 C  C4    . TTP G 5 .   ? 141.736 140.714 136.516 1.00 29.17 ?  803 TTP A C4    1 
HETATM 15941 O  O4    . TTP G 5 .   ? 140.921 140.658 137.460 1.00 37.02 ?  803 TTP A O4    1 
HETATM 15942 C  C5    . TTP G 5 .   ? 142.157 142.025 135.968 1.00 28.26 ?  803 TTP A C5    1 
HETATM 15943 C  C5M   . TTP G 5 .   ? 141.612 143.307 136.536 1.00 26.39 ?  803 TTP A C5M   1 
HETATM 15944 C  C6    . TTP G 5 .   ? 143.064 142.045 134.922 1.00 27.03 ?  803 TTP A C6    1 
HETATM 15945 MG MG    . MG  H 6 .   ? 147.077 148.626 132.262 1.00 18.30 ?  804 MG  A MG    1 
HETATM 15946 P  PA    . TTP I 5 .   ? 118.902 145.925 122.721 1.00 24.11 ?  801 TTP B PA    1 
HETATM 15947 O  O1A   . TTP I 5 .   ? 120.366 146.265 122.837 1.00 30.19 -1 801 TTP B O1A   1 
HETATM 15948 O  O2A   . TTP I 5 .   ? 118.047 147.000 123.343 1.00 22.18 ?  801 TTP B O2A   1 
HETATM 15949 O  O3A   . TTP I 5 .   ? 118.502 145.643 121.191 1.00 32.55 ?  801 TTP B O3A   1 
HETATM 15950 P  PB    . TTP I 5 .   ? 117.773 146.757 120.291 1.00 29.61 ?  801 TTP B PB    1 
HETATM 15951 O  O1B   . TTP I 5 .   ? 117.802 148.127 120.920 1.00 32.07 -1 801 TTP B O1B   1 
HETATM 15952 O  O2B   . TTP I 5 .   ? 118.406 146.798 118.923 1.00 29.33 ?  801 TTP B O2B   1 
HETATM 15953 O  O3B   . TTP I 5 .   ? 116.278 146.166 120.223 1.00 19.28 ?  801 TTP B O3B   1 
HETATM 15954 P  PG    . TTP I 5 .   ? 115.034 146.983 120.836 1.00 31.34 ?  801 TTP B PG    1 
HETATM 15955 O  O1G   . TTP I 5 .   ? 114.727 148.176 119.966 1.00 34.07 ?  801 TTP B O1G   1 
HETATM 15956 O  O2G   . TTP I 5 .   ? 113.826 146.081 120.896 1.00 23.32 -1 801 TTP B O2G   1 
HETATM 15957 O  O3G   . TTP I 5 .   ? 115.375 147.450 122.229 1.00 34.53 ?  801 TTP B O3G   1 
HETATM 15958 O  "O5'" . TTP I 5 .   ? 118.581 144.509 123.408 1.00 24.93 ?  801 TTP B "O5'" 1 
HETATM 15959 C  "C5'" . TTP I 5 .   ? 117.572 144.450 124.409 1.00 24.44 ?  801 TTP B "C5'" 1 
HETATM 15960 C  "C4'" . TTP I 5 .   ? 117.522 143.060 125.021 1.00 24.00 ?  801 TTP B "C4'" 1 
HETATM 15961 O  "O4'" . TTP I 5 .   ? 117.723 142.068 124.016 1.00 28.53 ?  801 TTP B "O4'" 1 
HETATM 15962 C  "C3'" . TTP I 5 .   ? 118.623 142.859 126.044 1.00 27.23 ?  801 TTP B "C3'" 1 
HETATM 15963 O  "O3'" . TTP I 5 .   ? 118.123 143.043 127.370 1.00 27.74 ?  801 TTP B "O3'" 1 
HETATM 15964 C  "C2'" . TTP I 5 .   ? 119.083 141.429 125.848 1.00 27.40 ?  801 TTP B "C2'" 1 
HETATM 15965 C  "C1'" . TTP I 5 .   ? 118.410 140.946 124.573 1.00 29.90 ?  801 TTP B "C1'" 1 
HETATM 15966 N  N1    . TTP I 5 .   ? 119.421 140.442 123.644 1.00 28.87 ?  801 TTP B N1    1 
HETATM 15967 C  C2    . TTP I 5 .   ? 119.765 139.074 123.679 1.00 27.67 ?  801 TTP B C2    1 
HETATM 15968 O  O2    . TTP I 5 .   ? 119.191 138.323 124.495 1.00 29.22 ?  801 TTP B O2    1 
HETATM 15969 N  N3    . TTP I 5 .   ? 120.685 138.562 122.852 1.00 25.56 ?  801 TTP B N3    1 
HETATM 15970 C  C4    . TTP I 5 .   ? 121.310 139.342 121.970 1.00 29.58 ?  801 TTP B C4    1 
HETATM 15971 O  O4    . TTP I 5 .   ? 122.168 138.864 121.201 1.00 38.14 ?  801 TTP B O4    1 
HETATM 15972 C  C5    . TTP I 5 .   ? 120.972 140.785 121.916 1.00 24.40 ?  801 TTP B C5    1 
HETATM 15973 C  C5M   . TTP I 5 .   ? 121.655 141.698 120.934 1.00 26.91 ?  801 TTP B C5M   1 
HETATM 15974 C  C6    . TTP I 5 .   ? 120.013 141.280 122.788 1.00 27.32 ?  801 TTP B C6    1 
HETATM 15975 MG MG    . MG  J 6 .   ? 116.901 148.675 123.188 1.00 37.62 ?  802 MG  B MG    1 
HETATM 15976 P  PG    . ATP K 3 .   ? 153.638 145.007 179.038 1.00 70.08 ?  803 ATP B PG    1 
HETATM 15977 O  O1G   . ATP K 3 .   ? 153.649 145.336 177.584 1.00 62.41 ?  803 ATP B O1G   1 
HETATM 15978 O  O2G   . ATP K 3 .   ? 153.610 146.242 179.944 1.00 61.28 -1 803 ATP B O2G   1 
HETATM 15979 O  O3G   . ATP K 3 .   ? 152.505 144.060 179.447 1.00 60.15 ?  803 ATP B O3G   1 
HETATM 15980 P  PB    . ATP K 3 .   ? 155.451 142.813 179.988 1.00 67.84 ?  803 ATP B PB    1 
HETATM 15981 O  O1B   . ATP K 3 .   ? 156.744 142.405 179.405 1.00 59.55 -1 803 ATP B O1B   1 
HETATM 15982 O  O2B   . ATP K 3 .   ? 155.396 142.864 181.515 1.00 61.48 ?  803 ATP B O2B   1 
HETATM 15983 O  O3B   . ATP K 3 .   ? 154.979 144.236 179.452 1.00 62.14 ?  803 ATP B O3B   1 
HETATM 15984 P  PA    . ATP K 3 .   ? 153.909 141.026 178.202 1.00 67.77 ?  803 ATP B PA    1 
HETATM 15985 O  O1A   . ATP K 3 .   ? 152.507 141.236 177.790 1.00 60.17 -1 803 ATP B O1A   1 
HETATM 15986 O  O2A   . ATP K 3 .   ? 154.293 139.574 178.485 1.00 60.55 ?  803 ATP B O2A   1 
HETATM 15987 O  O3A   . ATP K 3 .   ? 154.265 141.867 179.505 1.00 61.79 ?  803 ATP B O3A   1 
HETATM 15988 O  "O5'" . ATP K 3 .   ? 154.911 141.603 177.127 1.00 60.51 ?  803 ATP B "O5'" 1 
HETATM 15989 C  "C5'" . ATP K 3 .   ? 155.064 140.979 175.834 1.00 57.17 ?  803 ATP B "C5'" 1 
HETATM 15990 C  "C4'" . ATP K 3 .   ? 154.649 141.958 174.765 1.00 59.72 ?  803 ATP B "C4'" 1 
HETATM 15991 O  "O4'" . ATP K 3 .   ? 153.982 141.249 173.697 1.00 60.83 ?  803 ATP B "O4'" 1 
HETATM 15992 C  "C3'" . ATP K 3 .   ? 153.670 143.038 175.216 1.00 58.64 ?  803 ATP B "C3'" 1 
HETATM 15993 O  "O3'" . ATP K 3 .   ? 154.362 144.188 175.688 1.00 58.59 ?  803 ATP B "O3'" 1 
HETATM 15994 C  "C2'" . ATP K 3 .   ? 152.891 143.335 173.934 1.00 58.56 ?  803 ATP B "C2'" 1 
HETATM 15995 O  "O2'" . ATP K 3 .   ? 153.592 144.236 173.085 1.00 59.99 ?  803 ATP B "O2'" 1 
HETATM 15996 C  "C1'" . ATP K 3 .   ? 152.814 141.946 173.299 1.00 57.94 ?  803 ATP B "C1'" 1 
HETATM 15997 N  N9    . ATP K 3 .   ? 151.652 141.166 173.711 1.00 59.22 ?  803 ATP B N9    1 
HETATM 15998 C  C8    . ATP K 3 .   ? 151.628 140.100 174.571 1.00 57.41 ?  803 ATP B C8    1 
HETATM 15999 N  N7    . ATP K 3 .   ? 150.437 139.588 174.758 1.00 58.19 ?  803 ATP B N7    1 
HETATM 16000 C  C5    . ATP K 3 .   ? 149.615 140.374 173.965 1.00 58.18 ?  803 ATP B C5    1 
HETATM 16001 C  C6    . ATP K 3 .   ? 148.229 140.352 173.717 1.00 55.35 ?  803 ATP B C6    1 
HETATM 16002 N  N6    . ATP K 3 .   ? 147.388 139.473 174.270 1.00 55.86 ?  803 ATP B N6    1 
HETATM 16003 N  N1    . ATP K 3 .   ? 147.727 141.278 172.871 1.00 57.37 ?  803 ATP B N1    1 
HETATM 16004 C  C2    . ATP K 3 .   ? 148.561 142.162 172.316 1.00 55.85 ?  803 ATP B C2    1 
HETATM 16005 N  N3    . ATP K 3 .   ? 149.880 142.278 172.472 1.00 57.67 ?  803 ATP B N3    1 
HETATM 16006 C  C4    . ATP K 3 .   ? 150.350 141.351 173.313 1.00 59.74 ?  803 ATP B C4    1 
HETATM 16007 P  PB    . GDP L 4 .   ? 160.566 158.044 171.393 1.00 69.13 ?  804 GDP B PB    1 
HETATM 16008 O  O1B   . GDP L 4 .   ? 161.299 156.752 171.656 1.00 61.24 ?  804 GDP B O1B   1 
HETATM 16009 O  O2B   . GDP L 4 .   ? 160.586 158.895 172.640 1.00 59.98 -1 804 GDP B O2B   1 
HETATM 16010 O  O3B   . GDP L 4 .   ? 161.235 158.784 170.260 1.00 59.87 ?  804 GDP B O3B   1 
HETATM 16011 O  O3A   . GDP L 4 .   ? 159.037 157.726 171.007 1.00 58.19 ?  804 GDP B O3A   1 
HETATM 16012 P  PA    . GDP L 4 .   ? 158.638 156.997 169.629 1.00 64.69 ?  804 GDP B PA    1 
HETATM 16013 O  O1A   . GDP L 4 .   ? 158.845 157.901 168.438 1.00 59.39 -1 804 GDP B O1A   1 
HETATM 16014 O  O2A   . GDP L 4 .   ? 159.413 155.713 169.456 1.00 58.30 ?  804 GDP B O2A   1 
HETATM 16015 O  "O5'" . GDP L 4 .   ? 157.075 156.700 169.861 1.00 61.40 ?  804 GDP B "O5'" 1 
HETATM 16016 C  "C5'" . GDP L 4 .   ? 156.126 156.849 168.810 1.00 57.46 ?  804 GDP B "C5'" 1 
HETATM 16017 C  "C4'" . GDP L 4 .   ? 154.917 155.984 169.126 1.00 55.92 ?  804 GDP B "C4'" 1 
HETATM 16018 O  "O4'" . GDP L 4 .   ? 154.666 155.151 167.994 1.00 58.58 ?  804 GDP B "O4'" 1 
HETATM 16019 C  "C3'" . GDP L 4 .   ? 155.202 155.085 170.318 1.00 59.02 ?  804 GDP B "C3'" 1 
HETATM 16020 O  "O3'" . GDP L 4 .   ? 154.143 155.177 171.276 1.00 58.82 ?  804 GDP B "O3'" 1 
HETATM 16021 C  "C2'" . GDP L 4 .   ? 155.277 153.677 169.769 1.00 56.94 ?  804 GDP B "C2'" 1 
HETATM 16022 O  "O2'" . GDP L 4 .   ? 154.511 152.783 170.580 1.00 59.26 ?  804 GDP B "O2'" 1 
HETATM 16023 C  "C1'" . GDP L 4 .   ? 154.688 153.773 168.371 1.00 55.87 ?  804 GDP B "C1'" 1 
HETATM 16024 N  N9    . GDP L 4 .   ? 155.439 152.977 167.365 1.00 56.16 ?  804 GDP B N9    1 
HETATM 16025 C  C8    . GDP L 4 .   ? 154.866 152.313 166.346 1.00 57.86 ?  804 GDP B C8    1 
HETATM 16026 N  N7    . GDP L 4 .   ? 155.790 151.683 165.585 1.00 59.36 ?  804 GDP B N7    1 
HETATM 16027 C  C5    . GDP L 4 .   ? 156.997 151.955 166.109 1.00 59.05 ?  804 GDP B C5    1 
HETATM 16028 C  C6    . GDP L 4 .   ? 158.400 151.603 165.788 1.00 58.07 ?  804 GDP B C6    1 
HETATM 16029 O  O6    . GDP L 4 .   ? 158.670 150.879 164.806 1.00 59.08 ?  804 GDP B O6    1 
HETATM 16030 N  N1    . GDP L 4 .   ? 159.366 152.085 166.578 1.00 57.10 ?  804 GDP B N1    1 
HETATM 16031 C  C2    . GDP L 4 .   ? 159.101 152.866 167.640 1.00 57.92 ?  804 GDP B C2    1 
HETATM 16032 N  N2    . GDP L 4 .   ? 160.133 153.314 168.394 1.00 58.60 ?  804 GDP B N2    1 
HETATM 16033 N  N3    . GDP L 4 .   ? 157.842 153.227 167.991 1.00 60.62 ?  804 GDP B N3    1 
HETATM 16034 C  C4    . GDP L 4 .   ? 156.765 152.812 167.282 1.00 59.26 ?  804 GDP B C4    1 
HETATM 16035 MN MN    . MN  M 7 .   ? 110.819 95.249  120.357 0.85 25.05 ?  401 MN  C MN    1 
HETATM 16036 MN MN    . MN  N 7 .   ? 109.983 98.580  121.827 0.85 26.37 ?  402 MN  C MN    1 
HETATM 16037 MN MN    . MN  O 7 .   ? 129.901 95.604  135.097 1.00 22.51 ?  401 MN  D MN    1 
HETATM 16038 MN MN    . MN  P 7 .   ? 131.936 94.395  131.983 1.00 24.72 ?  402 MN  D MN    1 
# 
