data_9BZO
# 
_entry.id   9BZO 
# 
_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   9BZO         pdb_00009bzo 10.2210/pdb9bzo/pdb 
WWPDB D_1000284455 ?            ?                   
EMDB  EMD-45072    ?            ?                   
# 
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                        9BZO 
_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 50 model for combined refinement of Bacillus subtilis ribonucleotide reductase complex' 
_pdbx_database_related.db_id          EMD-45072 
_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 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GDP ? ? GDP ? ? '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                   9BZO 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BZO 
_struct.title                        'Class 50 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        9BZO 
_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 9BZO A 1  ? 700 ? P50620 1 ? 700 ? 1 700 
2 1 9BZO B 1  ? 700 ? P50620 1 ? 700 ? 1 700 
3 2 9BZO C 22 ? 350 ? P50621 1 ? 329 ? 1 329 
4 2 9BZO 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 9BZO MET C 1  ? UNP P50621 ? ? 'initiating methionine' -20 1  
3 9BZO GLY C 2  ? UNP P50621 ? ? 'expression tag'        -19 2  
3 9BZO SER C 3  ? UNP P50621 ? ? 'expression tag'        -18 3  
3 9BZO SER C 4  ? UNP P50621 ? ? 'expression tag'        -17 4  
3 9BZO HIS C 5  ? UNP P50621 ? ? 'expression tag'        -16 5  
3 9BZO HIS C 6  ? UNP P50621 ? ? 'expression tag'        -15 6  
3 9BZO HIS C 7  ? UNP P50621 ? ? 'expression tag'        -14 7  
3 9BZO HIS C 8  ? UNP P50621 ? ? 'expression tag'        -13 8  
3 9BZO HIS C 9  ? UNP P50621 ? ? 'expression tag'        -12 9  
3 9BZO HIS C 10 ? UNP P50621 ? ? 'expression tag'        -11 10 
3 9BZO SER C 11 ? UNP P50621 ? ? 'expression tag'        -10 11 
3 9BZO SER C 12 ? UNP P50621 ? ? 'expression tag'        -9  12 
3 9BZO GLY C 13 ? UNP P50621 ? ? 'expression tag'        -8  13 
3 9BZO LEU C 14 ? UNP P50621 ? ? 'expression tag'        -7  14 
3 9BZO VAL C 15 ? UNP P50621 ? ? 'expression tag'        -6  15 
3 9BZO PRO C 16 ? UNP P50621 ? ? 'expression tag'        -5  16 
3 9BZO ARG C 17 ? UNP P50621 ? ? 'expression tag'        -4  17 
3 9BZO GLY C 18 ? UNP P50621 ? ? 'expression tag'        -3  18 
3 9BZO SER C 19 ? UNP P50621 ? ? 'expression tag'        -2  19 
3 9BZO HIS C 20 ? UNP P50621 ? ? 'expression tag'        -1  20 
3 9BZO MET C 21 ? UNP P50621 ? ? 'expression tag'        0   21 
4 9BZO MET D 1  ? UNP P50621 ? ? 'initiating methionine' -20 22 
4 9BZO GLY D 2  ? UNP P50621 ? ? 'expression tag'        -19 23 
4 9BZO SER D 3  ? UNP P50621 ? ? 'expression tag'        -18 24 
4 9BZO SER D 4  ? UNP P50621 ? ? 'expression tag'        -17 25 
4 9BZO HIS D 5  ? UNP P50621 ? ? 'expression tag'        -16 26 
4 9BZO HIS D 6  ? UNP P50621 ? ? 'expression tag'        -15 27 
4 9BZO HIS D 7  ? UNP P50621 ? ? 'expression tag'        -14 28 
4 9BZO HIS D 8  ? UNP P50621 ? ? 'expression tag'        -13 29 
4 9BZO HIS D 9  ? UNP P50621 ? ? 'expression tag'        -12 30 
4 9BZO HIS D 10 ? UNP P50621 ? ? 'expression tag'        -11 31 
4 9BZO SER D 11 ? UNP P50621 ? ? 'expression tag'        -10 32 
4 9BZO SER D 12 ? UNP P50621 ? ? 'expression tag'        -9  33 
4 9BZO GLY D 13 ? UNP P50621 ? ? 'expression tag'        -8  34 
4 9BZO LEU D 14 ? UNP P50621 ? ? 'expression tag'        -7  35 
4 9BZO VAL D 15 ? UNP P50621 ? ? 'expression tag'        -6  36 
4 9BZO PRO D 16 ? UNP P50621 ? ? 'expression tag'        -5  37 
4 9BZO ARG D 17 ? UNP P50621 ? ? 'expression tag'        -4  38 
4 9BZO GLY D 18 ? UNP P50621 ? ? 'expression tag'        -3  39 
4 9BZO SER D 19 ? UNP P50621 ? ? 'expression tag'        -2  40 
4 9BZO HIS D 20 ? UNP P50621 ? ? 'expression tag'        -1  41 
4 9BZO 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 ? ? ? ? ? ? ? 2.375 ? ? 
metalc4  metalc ? ? I TTP .   O2A ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc5  metalc ? ? I TTP .   O1B ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.502 ? ? 
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 ? ? ? ? ? ? ? 2.030 ? ? 
metalc8  metalc ? ? C GLU 118 OE2 ? ? ? 1_555 M MN . MN ? ? C GLU 97  C MN 401 1_555 ? ? ? ? ? ? ? 1.961 ? ? 
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 ? ? ? ? ? ? ? 2.176 ? ? 
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 ? ? ? ? ? ? ? 2.172 ? ? 
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 ? ? ? ? ? ? ? 2.409 ? ? 
metalc17 metalc ? ? D ASP 87  OD1 ? ? ? 1_555 P MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc18 metalc ? ? D ASP 87  OD2 ? ? ? 1_555 P MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.157 ? ? 
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 ? ? ? ? ? ? ? 1.991 ? ? 
metalc21 metalc ? ? D HIS 122 ND1 ? ? ? 1_555 P MN . MN ? ? D HIS 101 D MN 402 1_555 ? ? ? ? ? ? ? 2.146 ? ? 
metalc22 metalc ? ? D GLU 185 OE1 ? ? ? 1_555 O MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.303 ? ? 
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_555 137.8 ? 
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 64.8  ? 
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_555 103.9 ? 
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 93.4  ? 
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_555 122.1 ? 
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_555 153.4 ? 
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 99.7  ? 
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 0.45 
2 TYR 355 B . ? TYR 355 B PRO 356 B ? PRO 356 B 1 0.72 
# 
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                   9BZO 
_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 ? ? -69.51  2.77    
2  1 ASP A 398 ? ? 39.35   35.71   
3  1 SER A 593 ? ? 56.68   -153.85 
4  1 ASP B 215 ? ? 74.82   -2.77   
5  1 SER B 593 ? ? 60.60   -154.22 
6  1 THR C 72  ? ? -128.06 -59.10  
7  1 ASP C 148 ? ? 58.10   15.70   
8  1 PHE C 166 ? ? -125.68 -60.78  
9  1 THR D 72  ? ? -128.18 -58.46  
10 1 PHE D 166 ? ? -144.16 -61.15  
11 1 ASP D 317 ? ? 64.30   164.43  
12 1 ASP D 318 ? ? 66.25   -1.34   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BZO 
_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                    9BZO 
_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                  4.48 
_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                        9BZO 
_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              9BZO 
_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                9BZO 
_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              9BZO 
_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           9BZO 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'Class 50 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                    9BZO 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
MN 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . VAL A 1 6   ? 104.397 117.095 97.834  1.00 61.20 ?  6   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 6   ? 105.601 117.549 97.152  1.00 61.32 ?  6   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 6   ? 105.238 118.459 95.977  1.00 62.07 ?  6   VAL A C     1 
ATOM   4     O  O     . VAL A 1 6   ? 104.410 118.104 95.138  1.00 60.69 ?  6   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 6   ? 106.464 116.348 96.695  1.00 61.34 ?  6   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 6   ? 105.651 115.379 95.846  1.00 61.29 ?  6   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 6   ? 107.693 116.827 95.941  1.00 59.53 ?  6   VAL A CG2   1 
ATOM   8     N  N     . PRO A 1 7   ? 105.839 119.645 95.933  1.00 58.51 ?  7   PRO A N     1 
ATOM   9     C  CA    . PRO A 1 7   ? 105.542 120.582 94.844  1.00 54.85 ?  7   PRO A CA    1 
ATOM   10    C  C     . PRO A 1 7   ? 106.122 120.107 93.520  1.00 54.57 ?  7   PRO A C     1 
ATOM   11    O  O     . PRO A 1 7   ? 107.071 119.324 93.466  1.00 55.81 ?  7   PRO A O     1 
ATOM   12    C  CB    . PRO A 1 7   ? 106.191 121.897 95.292  1.00 53.42 ?  7   PRO A CB    1 
ATOM   13    C  CG    . PRO A 1 7   ? 106.859 121.634 96.590  1.00 53.02 ?  7   PRO A CG    1 
ATOM   14    C  CD    . PRO A 1 7   ? 106.783 120.186 96.923  1.00 55.87 ?  7   PRO A CD    1 
ATOM   15    N  N     . LYS A 1 8   ? 105.527 120.614 92.436  1.00 54.03 ?  8   LYS A N     1 
ATOM   16    C  CA    . LYS A 1 8   ? 105.890 120.154 91.098  1.00 53.45 ?  8   LYS A CA    1 
ATOM   17    C  C     . LYS A 1 8   ? 107.347 120.461 90.772  1.00 55.16 ?  8   LYS A C     1 
ATOM   18    O  O     . LYS A 1 8   ? 108.048 119.626 90.184  1.00 57.31 ?  8   LYS A O     1 
ATOM   19    C  CB    . LYS A 1 8   ? 104.964 120.789 90.060  1.00 55.50 ?  8   LYS A CB    1 
ATOM   20    C  CG    . LYS A 1 8   ? 105.349 120.499 88.620  1.00 55.15 ?  8   LYS A CG    1 
ATOM   21    C  CD    . LYS A 1 8   ? 104.595 121.401 87.656  1.00 55.42 ?  8   LYS A CD    1 
ATOM   22    C  CE    . LYS A 1 8   ? 105.082 121.213 86.229  1.00 55.63 ?  8   LYS A CE    1 
ATOM   23    N  NZ    . LYS A 1 8   ? 104.576 122.281 85.323  1.00 56.86 1  8   LYS A NZ    1 
ATOM   24    N  N     . TRP A 1 9   ? 107.821 121.655 91.136  1.00 54.44 ?  9   TRP A N     1 
ATOM   25    C  CA    . TRP A 1 9   ? 109.206 122.006 90.843  1.00 52.69 ?  9   TRP A CA    1 
ATOM   26    C  C     . TRP A 1 9   ? 110.176 121.110 91.601  1.00 51.63 ?  9   TRP A C     1 
ATOM   27    O  O     . TRP A 1 9   ? 111.249 120.781 91.086  1.00 53.76 ?  9   TRP A O     1 
ATOM   28    C  CB    . TRP A 1 9   ? 109.470 123.476 91.170  1.00 52.54 ?  9   TRP A CB    1 
ATOM   29    C  CG    . TRP A 1 9   ? 109.223 123.855 92.598  1.00 49.94 ?  9   TRP A CG    1 
ATOM   30    C  CD1   . TRP A 1 9   ? 110.107 123.765 93.631  1.00 49.74 ?  9   TRP A CD1   1 
ATOM   31    C  CD2   . TRP A 1 9   ? 108.021 124.408 93.147  1.00 51.38 ?  9   TRP A CD2   1 
ATOM   32    N  NE1   . TRP A 1 9   ? 109.529 124.215 94.793  1.00 49.45 ?  9   TRP A NE1   1 
ATOM   33    C  CE2   . TRP A 1 9   ? 108.249 124.617 94.522  1.00 51.17 ?  9   TRP A CE2   1 
ATOM   34    C  CE3   . TRP A 1 9   ? 106.774 124.740 92.612  1.00 49.58 ?  9   TRP A CE3   1 
ATOM   35    C  CZ2   . TRP A 1 9   ? 107.276 125.144 95.367  1.00 49.84 ?  9   TRP A CZ2   1 
ATOM   36    C  CZ3   . TRP A 1 9   ? 105.810 125.262 93.453  1.00 51.27 ?  9   TRP A CZ3   1 
ATOM   37    C  CH2   . TRP A 1 9   ? 106.065 125.456 94.816  1.00 51.47 ?  9   TRP A CH2   1 
ATOM   38    N  N     . ILE A 1 10  ? 109.809 120.686 92.811  1.00 54.01 ?  10  ILE A N     1 
ATOM   39    C  CA    . ILE A 1 10  ? 110.678 119.795 93.572  1.00 53.77 ?  10  ILE A CA    1 
ATOM   40    C  C     . ILE A 1 10  ? 110.733 118.416 92.922  1.00 53.66 ?  10  ILE A C     1 
ATOM   41    O  O     . ILE A 1 10  ? 111.792 117.780 92.882  1.00 56.41 ?  10  ILE A O     1 
ATOM   42    C  CB    . ILE A 1 10  ? 110.218 119.728 95.038  1.00 54.66 ?  10  ILE A CB    1 
ATOM   43    C  CG1   . ILE A 1 10  ? 110.510 121.060 95.732  1.00 54.34 ?  10  ILE A CG1   1 
ATOM   44    C  CG2   . ILE A 1 10  ? 110.915 118.592 95.769  1.00 54.60 ?  10  ILE A CG2   1 
ATOM   45    C  CD1   . ILE A 1 10  ? 110.387 121.016 97.234  1.00 55.93 ?  10  ILE A CD1   1 
ATOM   46    N  N     . GLN A 1 11  ? 109.605 117.932 92.396  1.00 57.00 ?  11  GLN A N     1 
ATOM   47    C  CA    . GLN A 1 11  ? 109.636 116.676 91.649  1.00 57.95 ?  11  GLN A CA    1 
ATOM   48    C  C     . GLN A 1 11  ? 110.499 116.800 90.400  1.00 57.73 ?  11  GLN A C     1 
ATOM   49    O  O     . GLN A 1 11  ? 111.290 115.901 90.090  1.00 59.00 ?  11  GLN A O     1 
ATOM   50    C  CB    . GLN A 1 11  ? 108.220 116.235 91.275  1.00 57.52 ?  11  GLN A CB    1 
ATOM   51    C  CG    . GLN A 1 11  ? 107.188 116.407 92.372  1.00 58.92 ?  11  GLN A CG    1 
ATOM   52    C  CD    . GLN A 1 11  ? 105.791 116.627 91.826  1.00 60.78 ?  11  GLN A CD    1 
ATOM   53    O  OE1   . GLN A 1 11  ? 105.564 116.549 90.620  1.00 58.86 ?  11  GLN A OE1   1 
ATOM   54    N  NE2   . GLN A 1 11  ? 104.846 116.903 92.717  1.00 58.93 ?  11  GLN A NE2   1 
ATOM   55    N  N     . LEU A 1 12  ? 110.366 117.912 89.673  1.00 53.91 ?  12  LEU A N     1 
ATOM   56    C  CA    . LEU A 1 12  ? 111.181 118.110 88.479  1.00 52.66 ?  12  LEU A CA    1 
ATOM   57    C  C     . LEU A 1 12  ? 112.662 118.211 88.820  1.00 54.69 ?  12  LEU A C     1 
ATOM   58    O  O     . LEU A 1 12  ? 113.513 117.813 88.019  1.00 56.24 ?  12  LEU A O     1 
ATOM   59    C  CB    . LEU A 1 12  ? 110.718 119.358 87.728  1.00 52.80 ?  12  LEU A CB    1 
ATOM   60    C  CG    . LEU A 1 12  ? 109.561 119.164 86.746  1.00 53.51 ?  12  LEU A CG    1 
ATOM   61    C  CD1   . LEU A 1 12  ? 109.009 120.505 86.291  1.00 55.35 ?  12  LEU A CD1   1 
ATOM   62    C  CD2   . LEU A 1 12  ? 110.006 118.333 85.554  1.00 52.97 ?  12  LEU A CD2   1 
ATOM   63    N  N     . ASN A 1 13  ? 112.988 118.744 89.999  1.00 53.32 ?  13  ASN A N     1 
ATOM   64    C  CA    . ASN A 1 13  ? 114.379 118.819 90.428  1.00 51.61 ?  13  ASN A CA    1 
ATOM   65    C  C     . ASN A 1 13  ? 114.912 117.453 90.847  1.00 53.33 ?  13  ASN A C     1 
ATOM   66    O  O     . ASN A 1 13  ? 116.046 117.097 90.507  1.00 57.21 ?  13  ASN A O     1 
ATOM   67    C  CB    . ASN A 1 13  ? 114.520 119.824 91.572  1.00 52.13 ?  13  ASN A CB    1 
ATOM   68    C  CG    . ASN A 1 13  ? 115.951 119.969 92.046  1.00 51.95 ?  13  ASN A CG    1 
ATOM   69    O  OD1   . ASN A 1 13  ? 116.355 119.356 93.033  1.00 52.22 ?  13  ASN A OD1   1 
ATOM   70    N  ND2   . ASN A 1 13  ? 116.726 120.785 91.342  1.00 53.37 ?  13  ASN A ND2   1 
ATOM   71    N  N     . ASN A 1 14  ? 114.115 116.679 91.586  1.00 56.37 ?  14  ASN A N     1 
ATOM   72    C  CA    . ASN A 1 14  ? 114.529 115.335 91.976  1.00 55.27 ?  14  ASN A CA    1 
ATOM   73    C  C     . ASN A 1 14  ? 114.572 114.376 90.797  1.00 55.96 ?  14  ASN A C     1 
ATOM   74    O  O     . ASN A 1 14  ? 115.195 113.314 90.900  1.00 59.84 ?  14  ASN A O     1 
ATOM   75    C  CB    . ASN A 1 14  ? 113.602 114.790 93.064  1.00 55.43 ?  14  ASN A CB    1 
ATOM   76    C  CG    . ASN A 1 14  ? 113.667 115.600 94.343  1.00 58.93 ?  14  ASN A CG    1 
ATOM   77    O  OD1   . ASN A 1 14  ? 113.875 116.811 94.317  1.00 59.21 ?  14  ASN A OD1   1 
ATOM   78    N  ND2   . ASN A 1 14  ? 113.485 114.931 95.475  1.00 59.70 ?  14  ASN A ND2   1 
ATOM   79    N  N     . GLU A 1 15  ? 113.931 114.722 89.680  1.00 57.11 ?  15  GLU A N     1 
ATOM   80    C  CA    . GLU A 1 15  ? 114.034 113.899 88.483  1.00 58.53 ?  15  GLU A CA    1 
ATOM   81    C  C     . GLU A 1 15  ? 115.419 113.948 87.849  1.00 58.60 ?  15  GLU A C     1 
ATOM   82    O  O     . GLU A 1 15  ? 115.677 113.181 86.915  1.00 61.66 ?  15  GLU A O     1 
ATOM   83    C  CB    . GLU A 1 15  ? 112.976 114.320 87.460  1.00 58.15 ?  15  GLU A CB    1 
ATOM   84    C  CG    . GLU A 1 15  ? 111.589 113.764 87.749  1.00 58.81 ?  15  GLU A CG    1 
ATOM   85    C  CD    . GLU A 1 15  ? 110.523 114.333 86.833  1.00 61.24 ?  15  GLU A CD    1 
ATOM   86    O  OE1   . GLU A 1 15  ? 110.855 114.699 85.688  1.00 60.87 ?  15  GLU A OE1   1 
ATOM   87    O  OE2   . GLU A 1 15  ? 109.352 114.416 87.260  1.00 59.03 -1 15  GLU A OE2   1 
ATOM   88    N  N     . ILE A 1 16  ? 116.303 114.833 88.317  1.00 58.15 ?  16  ILE A N     1 
ATOM   89    C  CA    . ILE A 1 16  ? 117.667 114.883 87.791  1.00 58.69 ?  16  ILE A CA    1 
ATOM   90    C  C     . ILE A 1 16  ? 118.391 113.571 88.066  1.00 57.58 ?  16  ILE A C     1 
ATOM   91    O  O     . ILE A 1 16  ? 119.040 113.000 87.182  1.00 58.61 ?  16  ILE A O     1 
ATOM   92    C  CB    . ILE A 1 16  ? 118.432 116.074 88.395  1.00 57.30 ?  16  ILE A CB    1 
ATOM   93    C  CG1   . ILE A 1 16  ? 117.931 117.395 87.814  1.00 56.73 ?  16  ILE A CG1   1 
ATOM   94    C  CG2   . ILE A 1 16  ? 119.929 115.927 88.161  1.00 57.89 ?  16  ILE A CG2   1 
ATOM   95    C  CD1   . ILE A 1 16  ? 118.195 118.571 88.714  1.00 56.64 ?  16  ILE A CD1   1 
ATOM   96    N  N     . MET A 1 17  ? 118.289 113.074 89.302  1.00 57.91 ?  17  MET A N     1 
ATOM   97    C  CA    . MET A 1 17  ? 119.009 111.861 89.676  1.00 60.77 ?  17  MET A CA    1 
ATOM   98    C  C     . MET A 1 17  ? 118.492 110.642 88.927  1.00 60.83 ?  17  MET A C     1 
ATOM   99    O  O     . MET A 1 17  ? 119.239 109.678 88.727  1.00 61.69 ?  17  MET A O     1 
ATOM   100   C  CB    . MET A 1 17  ? 118.908 111.635 91.183  1.00 60.42 ?  17  MET A CB    1 
ATOM   101   C  CG    . MET A 1 17  ? 119.435 112.784 92.024  1.00 59.88 ?  17  MET A CG    1 
ATOM   102   S  SD    . MET A 1 17  ? 120.703 113.785 91.224  1.00 62.45 ?  17  MET A SD    1 
ATOM   103   C  CE    . MET A 1 17  ? 122.119 112.698 91.358  1.00 58.33 ?  17  MET A CE    1 
ATOM   104   N  N     . ILE A 1 18  ? 117.227 110.659 88.514  1.00 63.10 ?  18  ILE A N     1 
ATOM   105   C  CA    . ILE A 1 18  ? 116.667 109.557 87.735  1.00 63.93 ?  18  ILE A CA    1 
ATOM   106   C  C     . ILE A 1 18  ? 117.396 109.529 86.396  1.00 64.49 ?  18  ILE A C     1 
ATOM   107   O  O     . ILE A 1 18  ? 117.329 110.486 85.620  1.00 66.32 ?  18  ILE A O     1 
ATOM   108   C  CB    . ILE A 1 18  ? 115.149 109.697 87.549  1.00 63.43 ?  18  ILE A CB    1 
ATOM   109   C  CG1   . ILE A 1 18  ? 114.362 109.201 88.776  1.00 64.00 ?  18  ILE A CG1   1 
ATOM   110   C  CG2   . ILE A 1 18  ? 114.686 108.929 86.318  1.00 63.67 ?  18  ILE A CG2   1 
ATOM   111   C  CD1   . ILE A 1 18  ? 114.893 109.609 90.137  1.00 63.77 ?  18  ILE A CD1   1 
ATOM   112   N  N     . GLN A 1 19  ? 118.109 108.438 86.129  1.00 67.59 ?  19  GLN A N     1 
ATOM   113   C  CA    . GLN A 1 19  ? 118.984 108.372 84.970  1.00 69.12 ?  19  GLN A CA    1 
ATOM   114   C  C     . GLN A 1 19  ? 118.231 107.841 83.756  1.00 70.12 ?  19  GLN A C     1 
ATOM   115   O  O     . GLN A 1 19  ? 117.590 106.788 83.821  1.00 70.79 ?  19  GLN A O     1 
ATOM   116   C  CB    . GLN A 1 19  ? 120.194 107.488 85.271  1.00 70.18 ?  19  GLN A CB    1 
ATOM   117   C  CG    . GLN A 1 19  ? 121.227 108.147 86.171  1.00 68.31 ?  19  GLN A CG    1 
ATOM   118   C  CD    . GLN A 1 19  ? 122.596 107.506 86.060  1.00 70.65 ?  19  GLN A CD    1 
ATOM   119   O  OE1   . GLN A 1 19  ? 122.846 106.706 85.159  1.00 71.53 ?  19  GLN A OE1   1 
ATOM   120   N  NE2   . GLN A 1 19  ? 123.490 107.856 86.975  1.00 69.08 ?  19  GLN A NE2   1 
ATOM   121   N  N     . LYS A 1 20  ? 118.311 108.577 82.652  1.00 72.27 ?  20  LYS A N     1 
ATOM   122   C  CA    . LYS A 1 20  ? 117.747 108.161 81.377  1.00 73.91 ?  20  LYS A CA    1 
ATOM   123   C  C     . LYS A 1 20  ? 118.888 107.909 80.402  1.00 76.01 ?  20  LYS A C     1 
ATOM   124   O  O     . LYS A 1 20  ? 119.730 108.787 80.187  1.00 75.81 ?  20  LYS A O     1 
ATOM   125   C  CB    . LYS A 1 20  ? 116.789 109.221 80.828  1.00 71.70 ?  20  LYS A CB    1 
ATOM   126   C  CG    . LYS A 1 20  ? 116.569 109.158 79.325  1.00 73.05 ?  20  LYS A CG    1 
ATOM   127   C  CD    . LYS A 1 20  ? 117.260 110.311 78.612  1.00 74.70 ?  20  LYS A CD    1 
ATOM   128   C  CE    . LYS A 1 20  ? 117.558 109.964 77.162  1.00 74.77 ?  20  LYS A CE    1 
ATOM   129   N  NZ    . LYS A 1 20  ? 117.746 111.185 76.328  1.00 74.65 1  20  LYS A NZ    1 
ATOM   130   N  N     . ASP A 1 21  ? 118.913 106.707 79.823  1.00 77.71 ?  21  ASP A N     1 
ATOM   131   C  CA    . ASP A 1 21  ? 119.994 106.277 78.934  1.00 78.08 ?  21  ASP A CA    1 
ATOM   132   C  C     . ASP A 1 21  ? 121.350 106.370 79.633  1.00 78.21 ?  21  ASP A C     1 
ATOM   133   O  O     . ASP A 1 21  ? 122.365 106.714 79.023  1.00 77.84 ?  21  ASP A O     1 
ATOM   134   C  CB    . ASP A 1 21  ? 119.994 107.079 77.630  1.00 78.03 ?  21  ASP A CB    1 
ATOM   135   C  CG    . ASP A 1 21  ? 120.733 106.372 76.510  1.00 79.20 ?  21  ASP A CG    1 
ATOM   136   O  OD1   . ASP A 1 21  ? 120.558 105.144 76.366  1.00 77.85 ?  21  ASP A OD1   1 
ATOM   137   O  OD2   . ASP A 1 21  ? 121.489 107.044 75.777  1.00 77.64 -1 21  ASP A OD2   1 
ATOM   138   N  N     . GLY A 1 22  ? 121.366 106.063 80.928  1.00 74.06 ?  22  GLY A N     1 
ATOM   139   C  CA    . GLY A 1 22  ? 122.597 106.109 81.691  1.00 72.25 ?  22  GLY A CA    1 
ATOM   140   C  C     . GLY A 1 22  ? 123.158 107.494 81.913  1.00 73.50 ?  22  GLY A C     1 
ATOM   141   O  O     . GLY A 1 22  ? 124.350 107.628 82.198  1.00 74.68 ?  22  GLY A O     1 
ATOM   142   N  N     . LYS A 1 23  ? 122.334 108.532 81.792  1.00 69.34 ?  23  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 23  ? 122.779 109.905 81.965  1.00 67.22 ?  23  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 23  ? 121.815 110.653 82.874  1.00 68.95 ?  23  LYS A C     1 
ATOM   145   O  O     . LYS A 1 23  ? 120.606 110.404 82.866  1.00 70.38 ?  23  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 23  ? 122.892 110.637 80.621  1.00 68.25 ?  23  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 23  ? 123.956 110.078 79.694  1.00 68.58 ?  23  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 23  ? 123.871 110.714 78.317  1.00 68.77 ?  23  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 23  ? 124.779 110.008 77.327  1.00 71.00 ?  23  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 23  ? 124.557 110.480 75.934  1.00 69.00 1  23  LYS A NZ    1 
ATOM   151   N  N     . PHE A 1 24  ? 122.365 111.574 83.659  1.00 62.03 ?  24  PHE A N     1 
ATOM   152   C  CA    . PHE A 1 24  ? 121.542 112.410 84.520  1.00 59.31 ?  24  PHE A CA    1 
ATOM   153   C  C     . PHE A 1 24  ? 120.733 113.392 83.683  1.00 59.62 ?  24  PHE A C     1 
ATOM   154   O  O     . PHE A 1 24  ? 121.227 113.951 82.702  1.00 59.64 ?  24  PHE A O     1 
ATOM   155   C  CB    . PHE A 1 24  ? 122.416 113.167 85.519  1.00 57.58 ?  24  PHE A CB    1 
ATOM   156   C  CG    . PHE A 1 24  ? 123.102 112.281 86.516  1.00 59.16 ?  24  PHE A CG    1 
ATOM   157   C  CD1   . PHE A 1 24  ? 122.416 111.782 87.608  1.00 60.30 ?  24  PHE A CD1   1 
ATOM   158   C  CD2   . PHE A 1 24  ? 124.438 111.950 86.362  1.00 60.20 ?  24  PHE A CD2   1 
ATOM   159   C  CE1   . PHE A 1 24  ? 123.049 110.966 88.524  1.00 61.28 ?  24  PHE A CE1   1 
ATOM   160   C  CE2   . PHE A 1 24  ? 125.075 111.136 87.277  1.00 58.77 ?  24  PHE A CE2   1 
ATOM   161   C  CZ    . PHE A 1 24  ? 124.379 110.645 88.360  1.00 59.24 ?  24  PHE A CZ    1 
ATOM   162   N  N     . GLN A 1 25  ? 119.476 113.599 84.077  1.00 59.49 ?  25  GLN A N     1 
ATOM   163   C  CA    . GLN A 1 25  ? 118.590 114.529 83.378  1.00 61.28 ?  25  GLN A CA    1 
ATOM   164   C  C     . GLN A 1 25  ? 118.840 115.935 83.918  1.00 60.68 ?  25  GLN A C     1 
ATOM   165   O  O     . GLN A 1 25  ? 118.058 116.495 84.690  1.00 62.38 ?  25  GLN A O     1 
ATOM   166   C  CB    . GLN A 1 25  ? 117.134 114.111 83.538  1.00 61.69 ?  25  GLN A CB    1 
ATOM   167   C  CG    . GLN A 1 25  ? 116.786 112.804 82.849  1.00 60.60 ?  25  GLN A CG    1 
ATOM   168   C  CD    . GLN A 1 25  ? 115.406 112.303 83.217  1.00 61.28 ?  25  GLN A CD    1 
ATOM   169   O  OE1   . GLN A 1 25  ? 114.412 112.674 82.593  1.00 60.75 ?  25  GLN A OE1   1 
ATOM   170   N  NE2   . GLN A 1 25  ? 115.338 111.454 84.235  1.00 60.63 ?  25  GLN A NE2   1 
ATOM   171   N  N     . PHE A 1 26  ? 119.971 116.507 83.502  1.00 56.32 ?  26  PHE A N     1 
ATOM   172   C  CA    . PHE A 1 26  ? 120.328 117.854 83.936  1.00 54.81 ?  26  PHE A CA    1 
ATOM   173   C  C     . PHE A 1 26  ? 119.344 118.888 83.402  1.00 56.40 ?  26  PHE A C     1 
ATOM   174   O  O     . PHE A 1 26  ? 118.957 119.815 84.124  1.00 56.54 ?  26  PHE A O     1 
ATOM   175   C  CB    . PHE A 1 26  ? 121.750 118.187 83.488  1.00 51.71 ?  26  PHE A CB    1 
ATOM   176   C  CG    . PHE A 1 26  ? 122.806 117.350 84.151  1.00 54.69 ?  26  PHE A CG    1 
ATOM   177   C  CD1   . PHE A 1 26  ? 122.860 117.245 85.529  1.00 52.92 ?  26  PHE A CD1   1 
ATOM   178   C  CD2   . PHE A 1 26  ? 123.743 116.668 83.394  1.00 52.64 ?  26  PHE A CD2   1 
ATOM   179   C  CE1   . PHE A 1 26  ? 123.830 116.476 86.142  1.00 52.85 ?  26  PHE A CE1   1 
ATOM   180   C  CE2   . PHE A 1 26  ? 124.713 115.896 84.000  1.00 50.88 ?  26  PHE A CE2   1 
ATOM   181   C  CZ    . PHE A 1 26  ? 124.759 115.801 85.376  1.00 52.70 ?  26  PHE A CZ    1 
ATOM   182   N  N     . ASP A 1 27  ? 118.925 118.739 82.141  1.00 58.64 ?  27  ASP A N     1 
ATOM   183   C  CA    . ASP A 1 27  ? 118.019 119.709 81.533  1.00 58.79 ?  27  ASP A CA    1 
ATOM   184   C  C     . ASP A 1 27  ? 116.706 119.815 82.297  1.00 59.03 ?  27  ASP A C     1 
ATOM   185   O  O     . ASP A 1 27  ? 116.073 120.879 82.297  1.00 59.44 ?  27  ASP A O     1 
ATOM   186   C  CB    . ASP A 1 27  ? 117.761 119.336 80.071  1.00 59.79 ?  27  ASP A CB    1 
ATOM   187   C  CG    . ASP A 1 27  ? 117.189 117.938 79.913  1.00 62.16 ?  27  ASP A CG    1 
ATOM   188   O  OD1   . ASP A 1 27  ? 116.039 117.703 80.340  1.00 62.25 ?  27  ASP A OD1   1 
ATOM   189   O  OD2   . ASP A 1 27  ? 117.894 117.069 79.358  1.00 62.20 -1 27  ASP A OD2   1 
ATOM   190   N  N     . LYS A 1 28  ? 116.290 118.733 82.963  1.00 56.53 ?  28  LYS A N     1 
ATOM   191   C  CA    . LYS A 1 28  ? 115.069 118.777 83.760  1.00 58.97 ?  28  LYS A CA    1 
ATOM   192   C  C     . LYS A 1 28  ? 115.128 119.878 84.807  1.00 59.60 ?  28  LYS A C     1 
ATOM   193   O  O     . LYS A 1 28  ? 114.100 120.492 85.118  1.00 59.48 ?  28  LYS A O     1 
ATOM   194   C  CB    . LYS A 1 28  ? 114.827 117.423 84.426  1.00 58.52 ?  28  LYS A CB    1 
ATOM   195   C  CG    . LYS A 1 28  ? 114.195 116.388 83.513  1.00 60.37 ?  28  LYS A CG    1 
ATOM   196   C  CD    . LYS A 1 28  ? 112.689 116.339 83.696  1.00 59.68 ?  28  LYS A CD    1 
ATOM   197   C  CE    . LYS A 1 28  ? 111.997 115.848 82.438  1.00 58.32 ?  28  LYS A CE    1 
ATOM   198   N  NZ    . LYS A 1 28  ? 112.299 116.715 81.266  1.00 59.76 1  28  LYS A NZ    1 
ATOM   199   N  N     . ASP A 1 29  ? 116.322 120.157 85.340  1.00 57.46 ?  29  ASP A N     1 
ATOM   200   C  CA    . ASP A 1 29  ? 116.472 121.249 86.297  1.00 54.95 ?  29  ASP A CA    1 
ATOM   201   C  C     . ASP A 1 29  ? 115.916 122.546 85.735  1.00 53.98 ?  29  ASP A C     1 
ATOM   202   O  O     . ASP A 1 29  ? 115.183 123.264 86.425  1.00 56.72 ?  29  ASP A O     1 
ATOM   203   C  CB    . ASP A 1 29  ? 117.942 121.422 86.677  1.00 55.38 ?  29  ASP A CB    1 
ATOM   204   C  CG    . ASP A 1 29  ? 118.120 121.981 88.074  1.00 56.18 ?  29  ASP A CG    1 
ATOM   205   O  OD1   . ASP A 1 29  ? 117.222 121.776 88.918  1.00 55.71 ?  29  ASP A OD1   1 
ATOM   206   O  OD2   . ASP A 1 29  ? 119.160 122.622 88.331  1.00 55.40 -1 29  ASP A OD2   1 
ATOM   207   N  N     . LYS A 1 30  ? 116.225 122.845 84.470  1.00 54.92 ?  30  LYS A N     1 
ATOM   208   C  CA    . LYS A 1 30  ? 115.687 124.045 83.838  1.00 56.30 ?  30  LYS A CA    1 
ATOM   209   C  C     . LYS A 1 30  ? 114.167 124.063 83.924  1.00 55.88 ?  30  LYS A C     1 
ATOM   210   O  O     . LYS A 1 30  ? 113.568 125.063 84.337  1.00 58.29 ?  30  LYS A O     1 
ATOM   211   C  CB    . LYS A 1 30  ? 116.147 124.122 82.382  1.00 57.24 ?  30  LYS A CB    1 
ATOM   212   C  CG    . LYS A 1 30  ? 117.654 124.223 82.210  1.00 59.30 ?  30  LYS A CG    1 
ATOM   213   C  CD    . LYS A 1 30  ? 118.041 124.273 80.740  1.00 59.58 ?  30  LYS A CD    1 
ATOM   214   C  CE    . LYS A 1 30  ? 119.539 124.088 80.559  1.00 58.77 ?  30  LYS A CE    1 
ATOM   215   N  NZ    . LYS A 1 30  ? 119.878 123.515 79.226  1.00 58.18 1  30  LYS A NZ    1 
ATOM   216   N  N     . GLU A 1 31  ? 113.531 122.937 83.584  1.00 57.35 ?  31  GLU A N     1 
ATOM   217   C  CA    . GLU A 1 31  ? 112.079 122.856 83.688  1.00 56.70 ?  31  GLU A CA    1 
ATOM   218   C  C     . GLU A 1 31  ? 111.621 123.169 85.104  1.00 56.29 ?  31  GLU A C     1 
ATOM   219   O  O     . GLU A 1 31  ? 110.659 123.922 85.301  1.00 58.26 ?  31  GLU A O     1 
ATOM   220   C  CB    . GLU A 1 31  ? 111.595 121.468 83.258  1.00 56.01 ?  31  GLU A CB    1 
ATOM   221   C  CG    . GLU A 1 31  ? 112.310 120.855 82.046  1.00 58.50 ?  31  GLU A CG    1 
ATOM   222   C  CD    . GLU A 1 31  ? 112.107 121.622 80.740  1.00 61.13 ?  31  GLU A CD    1 
ATOM   223   O  OE1   . GLU A 1 31  ? 112.333 122.850 80.696  1.00 60.18 ?  31  GLU A OE1   1 
ATOM   224   O  OE2   . GLU A 1 31  ? 111.715 120.980 79.744  1.00 59.93 -1 31  GLU A OE2   1 
ATOM   225   N  N     . ALA A 1 32  ? 112.333 122.635 86.101  1.00 50.08 ?  32  ALA A N     1 
ATOM   226   C  CA    . ALA A 1 32  ? 111.997 122.919 87.491  1.00 48.71 ?  32  ALA A CA    1 
ATOM   227   C  C     . ALA A 1 32  ? 111.932 124.418 87.734  1.00 52.68 ?  32  ALA A C     1 
ATOM   228   O  O     . ALA A 1 32  ? 110.968 124.921 88.327  1.00 55.36 ?  32  ALA A O     1 
ATOM   229   C  CB    . ALA A 1 32  ? 113.016 122.260 88.423  1.00 47.76 ?  32  ALA A CB    1 
ATOM   230   N  N     . VAL A 1 33  ? 112.926 125.158 87.230  1.00 50.76 ?  33  VAL A N     1 
ATOM   231   C  CA    . VAL A 1 33  ? 112.933 126.607 87.413  1.00 49.52 ?  33  VAL A CA    1 
ATOM   232   C  C     . VAL A 1 33  ? 111.636 127.197 86.888  1.00 50.65 ?  33  VAL A C     1 
ATOM   233   O  O     . VAL A 1 33  ? 110.955 127.963 87.582  1.00 52.98 ?  33  VAL A O     1 
ATOM   234   C  CB    . VAL A 1 33  ? 114.150 127.241 86.717  1.00 50.41 ?  33  VAL A CB    1 
ATOM   235   C  CG1   . VAL A 1 33  ? 114.456 128.604 87.324  1.00 48.62 ?  33  VAL A CG1   1 
ATOM   236   C  CG2   . VAL A 1 33  ? 115.347 126.331 86.796  1.00 50.88 ?  33  VAL A CG2   1 
ATOM   237   N  N     . HIS A 1 34  ? 111.249 126.800 85.673  1.00 47.66 ?  34  HIS A N     1 
ATOM   238   C  CA    . HIS A 1 34  ? 110.000 127.283 85.100  1.00 47.52 ?  34  HIS A CA    1 
ATOM   239   C  C     . HIS A 1 34  ? 108.842 127.002 86.043  1.00 50.23 ?  34  HIS A C     1 
ATOM   240   O  O     . HIS A 1 34  ? 108.068 127.905 86.384  1.00 54.05 ?  34  HIS A O     1 
ATOM   241   C  CB    . HIS A 1 34  ? 109.770 126.632 83.738  1.00 50.92 ?  34  HIS A CB    1 
ATOM   242   C  CG    . HIS A 1 34  ? 109.032 127.501 82.769  1.00 50.54 ?  34  HIS A CG    1 
ATOM   243   N  ND1   . HIS A 1 34  ? 107.784 128.020 83.036  1.00 53.04 ?  34  HIS A ND1   1 
ATOM   244   C  CD2   . HIS A 1 34  ? 109.369 127.947 81.536  1.00 51.78 ?  34  HIS A CD2   1 
ATOM   245   C  CE1   . HIS A 1 34  ? 107.383 128.745 82.007  1.00 54.94 ?  34  HIS A CE1   1 
ATOM   246   N  NE2   . HIS A 1 34  ? 108.326 128.718 81.085  1.00 54.28 ?  34  HIS A NE2   1 
ATOM   247   N  N     . SER A 1 35  ? 108.753 125.762 86.534  1.00 48.83 ?  35  SER A N     1 
ATOM   248   C  CA    . SER A 1 35  ? 107.704 125.427 87.487  1.00 49.75 ?  35  SER A CA    1 
ATOM   249   C  C     . SER A 1 35  ? 107.811 126.304 88.724  1.00 50.04 ?  35  SER A C     1 
ATOM   250   O  O     . SER A 1 35  ? 106.818 126.891 89.172  1.00 52.60 ?  35  SER A O     1 
ATOM   251   C  CB    . SER A 1 35  ? 107.787 123.946 87.859  1.00 50.64 ?  35  SER A CB    1 
ATOM   252   O  OG    . SER A 1 35  ? 106.892 123.633 88.911  1.00 52.65 ?  35  SER A OG    1 
ATOM   253   N  N     . TYR A 1 36  ? 109.031 126.459 89.249  1.00 47.40 ?  36  TYR A N     1 
ATOM   254   C  CA    . TYR A 1 36  ? 109.220 127.261 90.453  1.00 48.30 ?  36  TYR A CA    1 
ATOM   255   C  C     . TYR A 1 36  ? 108.764 128.694 90.237  1.00 46.43 ?  36  TYR A C     1 
ATOM   256   O  O     . TYR A 1 36  ? 108.412 129.385 91.198  1.00 46.71 ?  36  TYR A O     1 
ATOM   257   C  CB    . TYR A 1 36  ? 110.685 127.224 90.886  1.00 46.66 ?  36  TYR A CB    1 
ATOM   258   C  CG    . TYR A 1 36  ? 110.953 127.913 92.203  1.00 45.89 ?  36  TYR A CG    1 
ATOM   259   C  CD1   . TYR A 1 36  ? 110.324 127.497 93.369  1.00 46.40 ?  36  TYR A CD1   1 
ATOM   260   C  CD2   . TYR A 1 36  ? 111.841 128.977 92.284  1.00 45.04 ?  36  TYR A CD2   1 
ATOM   261   C  CE1   . TYR A 1 36  ? 110.569 128.122 94.576  1.00 44.74 ?  36  TYR A CE1   1 
ATOM   262   C  CE2   . TYR A 1 36  ? 112.092 129.607 93.486  1.00 44.92 ?  36  TYR A CE2   1 
ATOM   263   C  CZ    . TYR A 1 36  ? 111.455 129.176 94.628  1.00 45.50 ?  36  TYR A CZ    1 
ATOM   264   O  OH    . TYR A 1 36  ? 111.704 129.804 95.827  1.00 47.43 ?  36  TYR A OH    1 
ATOM   265   N  N     . PHE A 1 37  ? 108.744 129.151 88.987  1.00 48.48 ?  37  PHE A N     1 
ATOM   266   C  CA    . PHE A 1 37  ? 108.230 130.476 88.680  1.00 49.98 ?  37  PHE A CA    1 
ATOM   267   C  C     . PHE A 1 37  ? 106.780 130.458 88.226  1.00 52.80 ?  37  PHE A C     1 
ATOM   268   O  O     . PHE A 1 37  ? 106.067 131.442 88.439  1.00 56.29 ?  37  PHE A O     1 
ATOM   269   C  CB    . PHE A 1 37  ? 109.096 131.146 87.609  1.00 51.07 ?  37  PHE A CB    1 
ATOM   270   C  CG    . PHE A 1 37  ? 110.359 131.747 88.151  1.00 51.02 ?  37  PHE A CG    1 
ATOM   271   C  CD1   . PHE A 1 37  ? 110.371 133.043 88.638  1.00 50.72 ?  37  PHE A CD1   1 
ATOM   272   C  CD2   . PHE A 1 37  ? 111.528 131.011 88.191  1.00 50.97 ?  37  PHE A CD2   1 
ATOM   273   C  CE1   . PHE A 1 37  ? 111.530 133.594 89.144  1.00 50.45 ?  37  PHE A CE1   1 
ATOM   274   C  CE2   . PHE A 1 37  ? 112.689 131.557 88.695  1.00 50.90 ?  37  PHE A CE2   1 
ATOM   275   C  CZ    . PHE A 1 37  ? 112.689 132.849 89.175  1.00 49.87 ?  37  PHE A CZ    1 
ATOM   276   N  N     . VAL A 1 38  ? 106.322 129.361 87.621  1.00 54.56 ?  38  VAL A N     1 
ATOM   277   C  CA    . VAL A 1 38  ? 104.941 129.319 87.153  1.00 53.41 ?  38  VAL A CA    1 
ATOM   278   C  C     . VAL A 1 38  ? 103.994 129.008 88.304  1.00 53.94 ?  38  VAL A C     1 
ATOM   279   O  O     . VAL A 1 38  ? 102.870 129.521 88.352  1.00 55.77 ?  38  VAL A O     1 
ATOM   280   C  CB    . VAL A 1 38  ? 104.805 128.309 85.998  1.00 53.67 ?  38  VAL A CB    1 
ATOM   281   C  CG1   . VAL A 1 38  ? 103.405 127.716 85.945  1.00 56.03 ?  38  VAL A CG1   1 
ATOM   282   C  CG2   . VAL A 1 38  ? 105.137 128.982 84.681  1.00 52.77 ?  38  VAL A CG2   1 
ATOM   283   N  N     . ASP A 1 39  ? 104.433 128.194 89.262  1.00 52.80 ?  39  ASP A N     1 
ATOM   284   C  CA    . ASP A 1 39  ? 103.578 127.742 90.350  1.00 53.63 ?  39  ASP A CA    1 
ATOM   285   C  C     . ASP A 1 39  ? 103.728 128.564 91.622  1.00 57.33 ?  39  ASP A C     1 
ATOM   286   O  O     . ASP A 1 39  ? 102.732 128.806 92.312  1.00 58.77 ?  39  ASP A O     1 
ATOM   287   C  CB    . ASP A 1 39  ? 103.864 126.271 90.663  1.00 55.81 ?  39  ASP A CB    1 
ATOM   288   C  CG    . ASP A 1 39  ? 103.895 125.406 89.419  1.00 57.71 ?  39  ASP A CG    1 
ATOM   289   O  OD1   . ASP A 1 39  ? 103.107 125.673 88.489  1.00 56.94 ?  39  ASP A OD1   1 
ATOM   290   O  OD2   . ASP A 1 39  ? 104.709 124.461 89.372  1.00 58.02 -1 39  ASP A OD2   1 
ATOM   291   N  N     . TYR A 1 40  ? 104.941 129.003 91.961  1.00 55.98 ?  40  TYR A N     1 
ATOM   292   C  CA    . TYR A 1 40  ? 105.193 129.618 93.258  1.00 53.64 ?  40  TYR A CA    1 
ATOM   293   C  C     . TYR A 1 40  ? 105.579 131.088 93.165  1.00 58.23 ?  40  TYR A C     1 
ATOM   294   O  O     . TYR A 1 40  ? 104.922 131.934 93.777  1.00 60.63 ?  40  TYR A O     1 
ATOM   295   C  CB    . TYR A 1 40  ? 106.284 128.835 94.000  1.00 53.89 ?  40  TYR A CB    1 
ATOM   296   C  CG    . TYR A 1 40  ? 106.405 129.198 95.463  1.00 54.81 ?  40  TYR A CG    1 
ATOM   297   C  CD1   . TYR A 1 40  ? 107.239 130.227 95.877  1.00 53.49 ?  40  TYR A CD1   1 
ATOM   298   C  CD2   . TYR A 1 40  ? 105.679 128.514 96.428  1.00 55.81 ?  40  TYR A CD2   1 
ATOM   299   C  CE1   . TYR A 1 40  ? 107.350 130.564 97.211  1.00 55.23 ?  40  TYR A CE1   1 
ATOM   300   C  CE2   . TYR A 1 40  ? 105.784 128.844 97.765  1.00 57.31 ?  40  TYR A CE2   1 
ATOM   301   C  CZ    . TYR A 1 40  ? 106.620 129.869 98.151  1.00 58.22 ?  40  TYR A CZ    1 
ATOM   302   O  OH    . TYR A 1 40  ? 106.726 130.200 99.481  1.00 57.01 ?  40  TYR A OH    1 
ATOM   303   N  N     . ILE A 1 41  ? 106.635 131.422 92.420  1.00 55.03 ?  41  ILE A N     1 
ATOM   304   C  CA    . ILE A 1 41  ? 107.214 132.760 92.518  1.00 51.74 ?  41  ILE A CA    1 
ATOM   305   C  C     . ILE A 1 41  ? 106.235 133.812 92.012  1.00 50.75 ?  41  ILE A C     1 
ATOM   306   O  O     . ILE A 1 41  ? 105.991 134.825 92.679  1.00 53.01 ?  41  ILE A O     1 
ATOM   307   C  CB    . ILE A 1 41  ? 108.555 132.828 91.768  1.00 49.42 ?  41  ILE A CB    1 
ATOM   308   C  CG1   . ILE A 1 41  ? 109.614 131.999 92.495  1.00 48.58 ?  41  ILE A CG1   1 
ATOM   309   C  CG2   . ILE A 1 41  ? 109.022 134.267 91.653  1.00 48.07 ?  41  ILE A CG2   1 
ATOM   310   C  CD1   . ILE A 1 41  ? 109.760 132.343 93.958  1.00 46.20 ?  41  ILE A CD1   1 
ATOM   311   N  N     . ASN A 1 42  ? 105.648 133.588 90.834  1.00 51.13 ?  42  ASN A N     1 
ATOM   312   C  CA    . ASN A 1 42  ? 104.719 134.570 90.285  1.00 51.45 ?  42  ASN A CA    1 
ATOM   313   C  C     . ASN A 1 42  ? 103.447 134.675 91.117  1.00 55.41 ?  42  ASN A C     1 
ATOM   314   O  O     . ASN A 1 42  ? 102.877 135.765 91.239  1.00 56.50 ?  42  ASN A O     1 
ATOM   315   C  CB    . ASN A 1 42  ? 104.383 134.225 88.834  1.00 52.87 ?  42  ASN A CB    1 
ATOM   316   C  CG    . ASN A 1 42  ? 105.588 134.321 87.921  1.00 53.98 ?  42  ASN A CG    1 
ATOM   317   O  OD1   . ASN A 1 42  ? 106.621 134.876 88.293  1.00 57.56 ?  42  ASN A OD1   1 
ATOM   318   N  ND2   . ASN A 1 42  ? 105.462 133.780 86.715  1.00 54.07 ?  42  ASN A ND2   1 
ATOM   319   N  N     . GLN A 1 43  ? 102.987 133.561 91.692  1.00 57.91 ?  43  GLN A N     1 
ATOM   320   C  CA    . GLN A 1 43  ? 101.781 133.593 92.512  1.00 55.47 ?  43  GLN A CA    1 
ATOM   321   C  C     . GLN A 1 43  ? 101.991 134.405 93.786  1.00 55.81 ?  43  GLN A C     1 
ATOM   322   O  O     . GLN A 1 43  ? 101.094 135.140 94.214  1.00 56.47 ?  43  GLN A O     1 
ATOM   323   C  CB    . GLN A 1 43  ? 101.342 132.170 92.851  1.00 55.39 ?  43  GLN A CB    1 
ATOM   324   C  CG    . GLN A 1 43  ? 100.360 131.566 91.859  1.00 57.56 ?  43  GLN A CG    1 
ATOM   325   C  CD    . GLN A 1 43  ? 100.963 131.365 90.482  1.00 58.38 ?  43  GLN A CD    1 
ATOM   326   O  OE1   . GLN A 1 43  ? 102.183 131.334 90.324  1.00 57.94 ?  43  GLN A OE1   1 
ATOM   327   N  NE2   . GLN A 1 43  ? 100.107 131.228 89.476  1.00 56.72 ?  43  GLN A NE2   1 
ATOM   328   N  N     . ASN A 1 44  ? 103.165 134.286 94.403  1.00 54.90 ?  44  ASN A N     1 
ATOM   329   C  CA    . ASN A 1 44  ? 103.454 134.945 95.669  1.00 55.01 ?  44  ASN A CA    1 
ATOM   330   C  C     . ASN A 1 44  ? 104.257 136.230 95.507  1.00 54.27 ?  44  ASN A C     1 
ATOM   331   O  O     . ASN A 1 44  ? 104.785 136.745 96.497  1.00 54.47 ?  44  ASN A O     1 
ATOM   332   C  CB    . ASN A 1 44  ? 104.187 133.983 96.609  1.00 53.41 ?  44  ASN A CB    1 
ATOM   333   C  CG    . ASN A 1 44  ? 103.403 132.709 96.865  1.00 55.83 ?  44  ASN A CG    1 
ATOM   334   O  OD1   . ASN A 1 44  ? 102.875 132.499 97.955  1.00 56.75 ?  44  ASN A OD1   1 
ATOM   335   N  ND2   . ASN A 1 44  ? 103.327 131.851 95.855  1.00 56.44 ?  44  ASN A ND2   1 
ATOM   336   N  N     . THR A 1 45  ? 104.362 136.758 94.292  1.00 54.15 ?  45  THR A N     1 
ATOM   337   C  CA    . THR A 1 45  ? 105.057 138.015 94.044  1.00 55.09 ?  45  THR A CA    1 
ATOM   338   C  C     . THR A 1 45  ? 104.047 139.152 94.004  1.00 55.66 ?  45  THR A C     1 
ATOM   339   O  O     . THR A 1 45  ? 103.082 139.106 93.233  1.00 56.05 ?  45  THR A O     1 
ATOM   340   C  CB    . THR A 1 45  ? 105.844 137.962 92.732  1.00 55.01 ?  45  THR A CB    1 
ATOM   341   O  OG1   . THR A 1 45  ? 107.072 137.251 92.938  1.00 57.88 ?  45  THR A OG1   1 
ATOM   342   C  CG2   . THR A 1 45  ? 106.162 139.366 92.236  1.00 53.39 ?  45  THR A CG2   1 
ATOM   343   N  N     . VAL A 1 46  ? 104.268 140.168 94.837  1.00 55.46 ?  46  VAL A N     1 
ATOM   344   C  CA    . VAL A 1 46  ? 103.372 141.318 94.876  1.00 55.19 ?  46  VAL A CA    1 
ATOM   345   C  C     . VAL A 1 46  ? 103.610 142.168 93.636  1.00 55.73 ?  46  VAL A C     1 
ATOM   346   O  O     . VAL A 1 46  ? 104.743 142.571 93.350  1.00 58.54 ?  46  VAL A O     1 
ATOM   347   C  CB    . VAL A 1 46  ? 103.582 142.134 96.158  1.00 55.20 ?  46  VAL A CB    1 
ATOM   348   C  CG1   . VAL A 1 46  ? 102.754 143.406 96.116  1.00 54.96 ?  46  VAL A CG1   1 
ATOM   349   C  CG2   . VAL A 1 46  ? 103.225 141.308 97.375  1.00 54.62 ?  46  VAL A CG2   1 
ATOM   350   N  N     . PHE A 1 47  ? 102.543 142.446 92.896  1.00 59.11 ?  47  PHE A N     1 
ATOM   351   C  CA    . PHE A 1 47  ? 102.618 143.252 91.689  1.00 59.69 ?  47  PHE A CA    1 
ATOM   352   C  C     . PHE A 1 47  ? 101.890 144.573 91.893  1.00 61.94 ?  47  PHE A C     1 
ATOM   353   O  O     . PHE A 1 47  ? 100.886 144.648 92.606  1.00 63.68 ?  47  PHE A O     1 
ATOM   354   C  CB    . PHE A 1 47  ? 102.025 142.512 90.488  1.00 60.14 ?  47  PHE A CB    1 
ATOM   355   C  CG    . PHE A 1 47  ? 102.545 142.997 89.165  1.00 62.75 ?  47  PHE A CG    1 
ATOM   356   C  CD1   . PHE A 1 47  ? 103.794 142.611 88.713  1.00 61.43 ?  47  PHE A CD1   1 
ATOM   357   C  CD2   . PHE A 1 47  ? 101.784 143.844 88.375  1.00 62.25 ?  47  PHE A CD2   1 
ATOM   358   C  CE1   . PHE A 1 47  ? 104.278 143.057 87.498  1.00 61.54 ?  47  PHE A CE1   1 
ATOM   359   C  CE2   . PHE A 1 47  ? 102.262 144.294 87.158  1.00 61.58 ?  47  PHE A CE2   1 
ATOM   360   C  CZ    . PHE A 1 47  ? 103.509 143.900 86.720  1.00 61.77 ?  47  PHE A CZ    1 
ATOM   361   N  N     . PHE A 1 48  ? 102.412 145.615 91.255  1.00 57.51 ?  48  PHE A N     1 
ATOM   362   C  CA    . PHE A 1 48  ? 101.869 146.958 91.349  1.00 57.86 ?  48  PHE A CA    1 
ATOM   363   C  C     . PHE A 1 48  ? 101.519 147.466 89.956  1.00 58.93 ?  48  PHE A C     1 
ATOM   364   O  O     . PHE A 1 48  ? 102.043 146.987 88.948  1.00 61.11 ?  48  PHE A O     1 
ATOM   365   C  CB    . PHE A 1 48  ? 102.860 147.913 92.026  1.00 57.18 ?  48  PHE A CB    1 
ATOM   366   C  CG    . PHE A 1 48  ? 103.212 147.528 93.436  1.00 56.27 ?  48  PHE A CG    1 
ATOM   367   C  CD1   . PHE A 1 48  ? 104.206 146.597 93.688  1.00 56.87 ?  48  PHE A CD1   1 
ATOM   368   C  CD2   . PHE A 1 48  ? 102.558 148.106 94.509  1.00 58.06 ?  48  PHE A CD2   1 
ATOM   369   C  CE1   . PHE A 1 48  ? 104.536 146.248 94.983  1.00 57.84 ?  48  PHE A CE1   1 
ATOM   370   C  CE2   . PHE A 1 48  ? 102.882 147.758 95.807  1.00 58.40 ?  48  PHE A CE2   1 
ATOM   371   C  CZ    . PHE A 1 48  ? 103.872 146.828 96.044  1.00 57.22 ?  48  PHE A CZ    1 
ATOM   372   N  N     . HIS A 1 49  ? 100.611 148.444 89.914  1.00 63.64 ?  49  HIS A N     1 
ATOM   373   C  CA    . HIS A 1 49  ? 100.184 148.998 88.633  1.00 66.40 ?  49  HIS A CA    1 
ATOM   374   C  C     . HIS A 1 49  ? 101.339 149.665 87.897  1.00 67.18 ?  49  HIS A C     1 
ATOM   375   O  O     . HIS A 1 49  ? 101.391 149.631 86.662  1.00 67.16 ?  49  HIS A O     1 
ATOM   376   C  CB    . HIS A 1 49  ? 99.041  149.991 88.846  1.00 67.54 ?  49  HIS A CB    1 
ATOM   377   C  CG    . HIS A 1 49  ? 98.460  150.525 87.573  1.00 69.46 ?  49  HIS A CG    1 
ATOM   378   N  ND1   . HIS A 1 49  ? 97.994  149.706 86.568  1.00 68.49 ?  49  HIS A ND1   1 
ATOM   379   C  CD2   . HIS A 1 49  ? 98.268  151.795 87.145  1.00 67.80 ?  49  HIS A CD2   1 
ATOM   380   C  CE1   . HIS A 1 49  ? 97.540  150.448 85.574  1.00 68.74 ?  49  HIS A CE1   1 
ATOM   381   N  NE2   . HIS A 1 49  ? 97.695  151.720 85.898  1.00 69.21 ?  49  HIS A NE2   1 
ATOM   382   N  N     . ASN A 1 50  ? 102.268 150.270 88.631  1.00 64.74 ?  50  ASN A N     1 
ATOM   383   C  CA    . ASN A 1 50  ? 103.446 150.883 88.037  1.00 63.49 ?  50  ASN A CA    1 
ATOM   384   C  C     . ASN A 1 50  ? 104.560 150.906 89.075  1.00 62.85 ?  50  ASN A C     1 
ATOM   385   O  O     . ASN A 1 50  ? 104.334 150.670 90.264  1.00 61.77 ?  50  ASN A O     1 
ATOM   386   C  CB    . ASN A 1 50  ? 103.139 152.289 87.499  1.00 62.57 ?  50  ASN A CB    1 
ATOM   387   C  CG    . ASN A 1 50  ? 102.853 153.295 88.600  1.00 64.44 ?  50  ASN A CG    1 
ATOM   388   O  OD1   . ASN A 1 50  ? 102.582 152.930 89.743  1.00 64.51 ?  50  ASN A OD1   1 
ATOM   389   N  ND2   . ASN A 1 50  ? 102.913 154.575 88.254  1.00 63.77 ?  50  ASN A ND2   1 
ATOM   390   N  N     . LEU A 1 51  ? 105.778 151.185 88.605  1.00 57.68 ?  51  LEU A N     1 
ATOM   391   C  CA    . LEU A 1 51  ? 106.930 151.193 89.499  1.00 56.20 ?  51  LEU A CA    1 
ATOM   392   C  C     . LEU A 1 51  ? 106.835 152.304 90.536  1.00 57.94 ?  51  LEU A C     1 
ATOM   393   O  O     . LEU A 1 51  ? 107.389 152.173 91.633  1.00 59.15 ?  51  LEU A O     1 
ATOM   394   C  CB    . LEU A 1 51  ? 108.219 151.331 88.693  1.00 55.60 ?  51  LEU A CB    1 
ATOM   395   C  CG    . LEU A 1 51  ? 109.541 151.283 89.460  1.00 55.06 ?  51  LEU A CG    1 
ATOM   396   C  CD1   . LEU A 1 51  ? 109.745 149.919 90.099  1.00 54.14 ?  51  LEU A CD1   1 
ATOM   397   C  CD2   . LEU A 1 51  ? 110.695 151.628 88.538  1.00 54.35 ?  51  LEU A CD2   1 
ATOM   398   N  N     . LYS A 1 52  ? 106.151 153.403 90.210  1.00 57.99 ?  52  LYS A N     1 
ATOM   399   C  CA    . LYS A 1 52  ? 105.983 154.483 91.176  1.00 57.65 ?  52  LYS A CA    1 
ATOM   400   C  C     . LYS A 1 52  ? 105.220 153.998 92.403  1.00 58.88 ?  52  LYS A C     1 
ATOM   401   O  O     . LYS A 1 52  ? 105.604 154.285 93.542  1.00 59.30 ?  52  LYS A O     1 
ATOM   402   C  CB    . LYS A 1 52  ? 105.265 155.662 90.518  1.00 57.85 ?  52  LYS A CB    1 
ATOM   403   C  CG    . LYS A 1 52  ? 105.791 157.030 90.928  1.00 58.85 ?  52  LYS A CG    1 
ATOM   404   C  CD    . LYS A 1 52  ? 105.378 157.394 92.341  1.00 59.24 ?  52  LYS A CD    1 
ATOM   405   C  CE    . LYS A 1 52  ? 105.784 158.816 92.683  1.00 59.48 ?  52  LYS A CE    1 
ATOM   406   N  NZ    . LYS A 1 52  ? 105.922 159.013 94.153  1.00 59.50 1  52  LYS A NZ    1 
ATOM   407   N  N     . GLU A 1 53  ? 104.139 153.246 92.183  1.00 60.58 ?  53  GLU A N     1 
ATOM   408   C  CA    . GLU A 1 53  ? 103.373 152.700 93.298  1.00 60.45 ?  53  GLU A CA    1 
ATOM   409   C  C     . GLU A 1 53  ? 104.205 151.715 94.109  1.00 60.19 ?  53  GLU A C     1 
ATOM   410   O  O     . GLU A 1 53  ? 104.137 151.703 95.342  1.00 60.00 ?  53  GLU A O     1 
ATOM   411   C  CB    . GLU A 1 53  ? 102.102 152.027 92.782  1.00 61.07 ?  53  GLU A CB    1 
ATOM   412   C  CG    . GLU A 1 53  ? 101.143 151.580 93.872  1.00 62.36 ?  53  GLU A CG    1 
ATOM   413   C  CD    . GLU A 1 53  ? 100.030 150.699 93.340  1.00 63.76 ?  53  GLU A CD    1 
ATOM   414   O  OE1   . GLU A 1 53  ? 99.789  149.623 93.927  1.00 62.97 ?  53  GLU A OE1   1 
ATOM   415   O  OE2   . GLU A 1 53  ? 99.396  151.080 92.333  1.00 62.77 -1 53  GLU A OE2   1 
ATOM   416   N  N     . LYS A 1 54  ? 104.993 150.878 93.431  1.00 58.66 ?  54  LYS A N     1 
ATOM   417   C  CA    . LYS A 1 54  ? 105.839 149.918 94.134  1.00 54.61 ?  54  LYS A CA    1 
ATOM   418   C  C     . LYS A 1 54  ? 106.857 150.626 95.018  1.00 52.64 ?  54  LYS A C     1 
ATOM   419   O  O     . LYS A 1 54  ? 107.044 150.265 96.186  1.00 55.36 ?  54  LYS A O     1 
ATOM   420   C  CB    . LYS A 1 54  ? 106.546 149.012 93.127  1.00 54.10 ?  54  LYS A CB    1 
ATOM   421   C  CG    . LYS A 1 54  ? 107.642 148.156 93.732  1.00 57.14 ?  54  LYS A CG    1 
ATOM   422   C  CD    . LYS A 1 54  ? 107.985 146.985 92.833  1.00 55.57 ?  54  LYS A CD    1 
ATOM   423   C  CE    . LYS A 1 54  ? 109.041 146.098 93.462  1.00 55.37 ?  54  LYS A CE    1 
ATOM   424   N  NZ    . LYS A 1 54  ? 109.052 144.740 92.854  1.00 55.79 1  54  LYS A NZ    1 
ATOM   425   N  N     . LEU A 1 55  ? 107.524 151.645 94.472  1.00 53.92 ?  55  LEU A N     1 
ATOM   426   C  CA    . LEU A 1 55  ? 108.520 152.377 95.245  1.00 55.07 ?  55  LEU A CA    1 
ATOM   427   C  C     . LEU A 1 55  ? 107.878 153.125 96.404  1.00 57.40 ?  55  LEU A C     1 
ATOM   428   O  O     . LEU A 1 55  ? 108.435 153.163 97.506  1.00 58.63 ?  55  LEU A O     1 
ATOM   429   C  CB    . LEU A 1 55  ? 109.284 153.338 94.337  1.00 55.64 ?  55  LEU A CB    1 
ATOM   430   C  CG    . LEU A 1 55  ? 110.166 152.691 93.268  1.00 56.12 ?  55  LEU A CG    1 
ATOM   431   C  CD1   . LEU A 1 55  ? 110.709 153.745 92.319  1.00 56.83 ?  55  LEU A CD1   1 
ATOM   432   C  CD2   . LEU A 1 55  ? 111.298 151.895 93.899  1.00 53.50 ?  55  LEU A CD2   1 
ATOM   433   N  N     . ASP A 1 56  ? 106.703 153.721 96.179  1.00 60.10 ?  56  ASP A N     1 
ATOM   434   C  CA    . ASP A 1 56  ? 106.008 154.408 97.262  1.00 59.38 ?  56  ASP A CA    1 
ATOM   435   C  C     . ASP A 1 56  ? 105.618 153.437 98.369  1.00 57.92 ?  56  ASP A C     1 
ATOM   436   O  O     . ASP A 1 56  ? 105.779 153.743 99.555  1.00 57.64 ?  56  ASP A O     1 
ATOM   437   C  CB    . ASP A 1 56  ? 104.773 155.127 96.721  1.00 60.22 ?  56  ASP A CB    1 
ATOM   438   C  CG    . ASP A 1 56  ? 105.121 156.391 95.966  1.00 62.26 ?  56  ASP A CG    1 
ATOM   439   O  OD1   . ASP A 1 56  ? 104.224 156.954 95.304  1.00 62.19 ?  56  ASP A OD1   1 
ATOM   440   O  OD2   . ASP A 1 56  ? 106.292 156.822 96.034  1.00 61.30 -1 56  ASP A OD2   1 
ATOM   441   N  N     . TYR A 1 57  ? 105.107 152.260 98.002  1.00 52.63 ?  57  TYR A N     1 
ATOM   442   C  CA    . TYR A 1 57  ? 104.725 151.275 99.007  1.00 54.65 ?  57  TYR A CA    1 
ATOM   443   C  C     . TYR A 1 57  ? 105.936 150.778 99.784  1.00 56.13 ?  57  TYR A C     1 
ATOM   444   O  O     . TYR A 1 57  ? 105.865 150.601 101.006 1.00 57.38 ?  57  TYR A O     1 
ATOM   445   C  CB    . TYR A 1 57  ? 103.996 150.106 98.345  1.00 53.46 ?  57  TYR A CB    1 
ATOM   446   C  CG    . TYR A 1 57  ? 103.675 148.973 99.294  1.00 55.24 ?  57  TYR A CG    1 
ATOM   447   C  CD1   . TYR A 1 57  ? 102.555 149.025 100.113 1.00 54.93 ?  57  TYR A CD1   1 
ATOM   448   C  CD2   . TYR A 1 57  ? 104.492 147.852 99.369  1.00 55.44 ?  57  TYR A CD2   1 
ATOM   449   C  CE1   . TYR A 1 57  ? 102.260 147.992 100.982 1.00 55.25 ?  57  TYR A CE1   1 
ATOM   450   C  CE2   . TYR A 1 57  ? 104.204 146.817 100.235 1.00 55.86 ?  57  TYR A CE2   1 
ATOM   451   C  CZ    . TYR A 1 57  ? 103.087 146.891 101.038 1.00 55.58 ?  57  TYR A CZ    1 
ATOM   452   O  OH    . TYR A 1 57  ? 102.797 145.859 101.900 1.00 56.63 ?  57  TYR A OH    1 
ATOM   453   N  N     . LEU A 1 58  ? 107.053 150.540 99.095  1.00 51.42 ?  58  LEU A N     1 
ATOM   454   C  CA    . LEU A 1 58  ? 108.236 150.024 99.776  1.00 50.27 ?  58  LEU A CA    1 
ATOM   455   C  C     . LEU A 1 58  ? 108.862 151.079 100.682 1.00 51.95 ?  58  LEU A C     1 
ATOM   456   O  O     . LEU A 1 58  ? 109.338 150.759 101.777 1.00 52.72 ?  58  LEU A O     1 
ATOM   457   C  CB    . LEU A 1 58  ? 109.246 149.511 98.752  1.00 49.61 ?  58  LEU A CB    1 
ATOM   458   C  CG    . LEU A 1 58  ? 108.807 148.243 98.012  1.00 50.58 ?  58  LEU A CG    1 
ATOM   459   C  CD1   . LEU A 1 58  ? 109.670 147.992 96.789  1.00 51.28 ?  58  LEU A CD1   1 
ATOM   460   C  CD2   . LEU A 1 58  ? 108.829 147.041 98.940  1.00 51.20 ?  58  LEU A CD2   1 
ATOM   461   N  N     . VAL A 1 59  ? 108.868 152.341 100.250 1.00 53.73 ?  59  VAL A N     1 
ATOM   462   C  CA    . VAL A 1 59  ? 109.435 153.403 101.075 1.00 54.61 ?  59  VAL A CA    1 
ATOM   463   C  C     . VAL A 1 59  ? 108.541 153.683 102.279 1.00 57.60 ?  59  VAL A C     1 
ATOM   464   O  O     . VAL A 1 59  ? 109.020 153.810 103.412 1.00 56.54 ?  59  VAL A O     1 
ATOM   465   C  CB    . VAL A 1 59  ? 109.657 154.669 100.231 1.00 54.59 ?  59  VAL A CB    1 
ATOM   466   C  CG1   . VAL A 1 59  ? 109.793 155.886 101.124 1.00 53.14 ?  59  VAL A CG1   1 
ATOM   467   C  CG2   . VAL A 1 59  ? 110.888 154.508 99.355  1.00 54.08 ?  59  VAL A CG2   1 
ATOM   468   N  N     . GLU A 1 60  ? 107.228 153.776 102.052 1.00 60.48 ?  60  GLU A N     1 
ATOM   469   C  CA    . GLU A 1 60  ? 106.307 154.131 103.126 1.00 58.01 ?  60  GLU A CA    1 
ATOM   470   C  C     . GLU A 1 60  ? 106.244 153.044 104.192 1.00 57.85 ?  60  GLU A C     1 
ATOM   471   O  O     . GLU A 1 60  ? 106.161 153.345 105.388 1.00 58.08 ?  60  GLU A O     1 
ATOM   472   C  CB    . GLU A 1 60  ? 104.917 154.407 102.552 1.00 58.23 ?  60  GLU A CB    1 
ATOM   473   C  CG    . GLU A 1 60  ? 104.797 155.748 101.845 1.00 59.63 ?  60  GLU A CG    1 
ATOM   474   C  CD    . GLU A 1 60  ? 103.644 155.789 100.860 1.00 61.74 ?  60  GLU A CD    1 
ATOM   475   O  OE1   . GLU A 1 60  ? 102.833 154.839 100.851 1.00 59.38 ?  60  GLU A OE1   1 
ATOM   476   O  OE2   . GLU A 1 60  ? 103.551 156.770 100.093 1.00 61.31 -1 60  GLU A OE2   1 
ATOM   477   N  N     . ASN A 1 61  ? 106.281 151.777 103.783 1.00 53.71 ?  61  ASN A N     1 
ATOM   478   C  CA    . ASN A 1 61  ? 106.216 150.658 104.714 1.00 52.50 ?  61  ASN A CA    1 
ATOM   479   C  C     . ASN A 1 61  ? 107.571 150.310 105.320 1.00 54.36 ?  61  ASN A C     1 
ATOM   480   O  O     . ASN A 1 61  ? 107.735 149.200 105.841 1.00 54.46 ?  61  ASN A O     1 
ATOM   481   C  CB    . ASN A 1 61  ? 105.620 149.431 104.022 1.00 53.45 ?  61  ASN A CB    1 
ATOM   482   C  CG    . ASN A 1 61  ? 104.118 149.530 103.857 1.00 56.30 ?  61  ASN A CG    1 
ATOM   483   O  OD1   . ASN A 1 61  ? 103.588 150.586 103.514 1.00 54.48 ?  61  ASN A OD1   1 
ATOM   484   N  ND2   . ASN A 1 61  ? 103.422 148.425 104.101 1.00 55.68 ?  61  ASN A ND2   1 
ATOM   485   N  N     . GLN A 1 62  ? 108.533 151.233 105.257 1.00 53.25 ?  62  GLN A N     1 
ATOM   486   C  CA    . GLN A 1 62  ? 109.850 151.076 105.878 1.00 52.66 ?  62  GLN A CA    1 
ATOM   487   C  C     . GLN A 1 62  ? 110.607 149.869 105.331 1.00 52.40 ?  62  GLN A C     1 
ATOM   488   O  O     . GLN A 1 62  ? 111.373 149.224 106.052 1.00 53.31 ?  62  GLN A O     1 
ATOM   489   C  CB    . GLN A 1 62  ? 109.741 150.990 107.404 1.00 51.98 ?  62  GLN A CB    1 
ATOM   490   C  CG    . GLN A 1 62  ? 108.773 151.991 108.019 1.00 51.77 ?  62  GLN A CG    1 
ATOM   491   C  CD    . GLN A 1 62  ? 109.147 153.428 107.716 1.00 54.59 ?  62  GLN A CD    1 
ATOM   492   O  OE1   . GLN A 1 62  ? 110.136 153.946 108.232 1.00 54.15 ?  62  GLN A OE1   1 
ATOM   493   N  NE2   . GLN A 1 62  ? 108.354 154.080 106.874 1.00 54.94 ?  62  GLN A NE2   1 
ATOM   494   N  N     . TYR A 1 63  ? 110.401 149.548 104.054 1.00 50.12 ?  63  TYR A N     1 
ATOM   495   C  CA    . TYR A 1 63  ? 111.201 148.523 103.394 1.00 46.66 ?  63  TYR A CA    1 
ATOM   496   C  C     . TYR A 1 63  ? 112.495 149.102 102.834 1.00 48.34 ?  63  TYR A C     1 
ATOM   497   O  O     . TYR A 1 63  ? 113.567 148.516 103.005 1.00 49.61 ?  63  TYR A O     1 
ATOM   498   C  CB    . TYR A 1 63  ? 110.401 147.853 102.273 1.00 47.01 ?  63  TYR A CB    1 
ATOM   499   C  CG    . TYR A 1 63  ? 109.269 146.976 102.752 1.00 49.24 ?  63  TYR A CG    1 
ATOM   500   C  CD1   . TYR A 1 63  ? 109.515 145.866 103.547 1.00 48.39 ?  63  TYR A CD1   1 
ATOM   501   C  CD2   . TYR A 1 63  ? 107.956 147.253 102.400 1.00 50.04 ?  63  TYR A CD2   1 
ATOM   502   C  CE1   . TYR A 1 63  ? 108.484 145.061 103.983 1.00 48.45 ?  63  TYR A CE1   1 
ATOM   503   C  CE2   . TYR A 1 63  ? 106.919 146.452 102.830 1.00 50.57 ?  63  TYR A CE2   1 
ATOM   504   C  CZ    . TYR A 1 63  ? 107.188 145.360 103.622 1.00 50.75 ?  63  TYR A CZ    1 
ATOM   505   O  OH    . TYR A 1 63  ? 106.152 144.563 104.051 1.00 53.58 ?  63  TYR A OH    1 
ATOM   506   N  N     . TYR A 1 64  ? 112.406 150.247 102.166 1.00 47.25 ?  64  TYR A N     1 
ATOM   507   C  CA    . TYR A 1 64  ? 113.546 150.906 101.549 1.00 43.93 ?  64  TYR A CA    1 
ATOM   508   C  C     . TYR A 1 64  ? 113.945 152.142 102.343 1.00 46.86 ?  64  TYR A C     1 
ATOM   509   O  O     . TYR A 1 64  ? 113.263 152.562 103.280 1.00 49.91 ?  64  TYR A O     1 
ATOM   510   C  CB    . TYR A 1 64  ? 113.234 151.301 100.102 1.00 45.49 ?  64  TYR A CB    1 
ATOM   511   C  CG    . TYR A 1 64  ? 113.246 150.153 99.127  1.00 45.64 ?  64  TYR A CG    1 
ATOM   512   C  CD1   . TYR A 1 64  ? 113.655 148.885 99.519  1.00 42.74 ?  64  TYR A CD1   1 
ATOM   513   C  CD2   . TYR A 1 64  ? 112.852 150.337 97.812  1.00 47.43 ?  64  TYR A CD2   1 
ATOM   514   C  CE1   . TYR A 1 64  ? 113.666 147.834 98.627  1.00 40.32 ?  64  TYR A CE1   1 
ATOM   515   C  CE2   . TYR A 1 64  ? 112.861 149.297 96.914  1.00 46.63 ?  64  TYR A CE2   1 
ATOM   516   C  CZ    . TYR A 1 64  ? 113.266 148.047 97.326  1.00 44.90 ?  64  TYR A CZ    1 
ATOM   517   O  OH    . TYR A 1 64  ? 113.274 147.009 96.426  1.00 44.35 ?  64  TYR A OH    1 
ATOM   518   N  N     . GLU A 1 65  ? 115.072 152.724 101.946 1.00 52.27 ?  65  GLU A N     1 
ATOM   519   C  CA    . GLU A 1 65  ? 115.514 154.003 102.478 1.00 50.80 ?  65  GLU A CA    1 
ATOM   520   C  C     . GLU A 1 65  ? 115.139 155.121 101.514 1.00 53.51 ?  65  GLU A C     1 
ATOM   521   O  O     . GLU A 1 65  ? 115.214 154.957 100.293 1.00 54.80 ?  65  GLU A O     1 
ATOM   522   C  CB    . GLU A 1 65  ? 117.025 154.002 102.715 1.00 50.17 ?  65  GLU A CB    1 
ATOM   523   C  CG    . GLU A 1 65  ? 117.460 153.314 103.998 1.00 51.49 ?  65  GLU A CG    1 
ATOM   524   C  CD    . GLU A 1 65  ? 118.875 152.779 103.921 1.00 52.41 ?  65  GLU A CD    1 
ATOM   525   O  OE1   . GLU A 1 65  ? 119.652 153.267 103.074 1.00 53.30 ?  65  GLU A OE1   1 
ATOM   526   O  OE2   . GLU A 1 65  ? 119.217 151.878 104.715 1.00 52.68 -1 65  GLU A OE2   1 
ATOM   527   N  N     . GLU A 1 66  ? 114.724 156.258 102.074 1.00 54.86 ?  66  GLU A N     1 
ATOM   528   C  CA    . GLU A 1 66  ? 114.359 157.405 101.252 1.00 54.45 ?  66  GLU A CA    1 
ATOM   529   C  C     . GLU A 1 66  ? 115.579 158.115 100.680 1.00 56.09 ?  66  GLU A C     1 
ATOM   530   O  O     . GLU A 1 66  ? 115.497 158.697 99.593  1.00 56.40 ?  66  GLU A O     1 
ATOM   531   C  CB    . GLU A 1 66  ? 113.527 158.396 102.071 1.00 55.78 ?  66  GLU A CB    1 
ATOM   532   C  CG    . GLU A 1 66  ? 112.052 158.570 101.664 1.00 57.32 ?  66  GLU A CG    1 
ATOM   533   C  CD    . GLU A 1 66  ? 111.814 159.034 100.224 1.00 58.41 ?  66  GLU A CD    1 
ATOM   534   O  OE1   . GLU A 1 66  ? 112.736 159.008 99.383  1.00 58.37 ?  66  GLU A OE1   1 
ATOM   535   O  OE2   . GLU A 1 66  ? 110.668 159.438 99.932  1.00 55.35 -1 66  GLU A OE2   1 
ATOM   536   N  N     . GLU A 1 67  ? 116.707 158.080 101.392 1.00 54.76 ?  67  GLU A N     1 
ATOM   537   C  CA    . GLU A 1 67  ? 117.850 158.911 101.023 1.00 55.13 ?  67  GLU A CA    1 
ATOM   538   C  C     . GLU A 1 67  ? 118.425 158.509 99.670  1.00 55.53 ?  67  GLU A C     1 
ATOM   539   O  O     . GLU A 1 67  ? 118.671 159.365 98.811  1.00 55.42 ?  67  GLU A O     1 
ATOM   540   C  CB    . GLU A 1 67  ? 118.923 158.830 102.110 1.00 56.55 ?  67  GLU A CB    1 
ATOM   541   C  CG    . GLU A 1 67  ? 118.400 159.071 103.516 1.00 57.39 ?  67  GLU A CG    1 
ATOM   542   C  CD    . GLU A 1 67  ? 118.138 157.783 104.270 1.00 60.75 ?  67  GLU A CD    1 
ATOM   543   O  OE1   . GLU A 1 67  ? 119.111 157.168 104.755 1.00 59.46 ?  67  GLU A OE1   1 
ATOM   544   O  OE2   . GLU A 1 67  ? 116.959 157.386 104.379 1.00 57.42 -1 67  GLU A OE2   1 
ATOM   545   N  N     . PHE A 1 68  ? 118.644 157.209 99.456  1.00 48.39 ?  68  PHE A N     1 
ATOM   546   C  CA    . PHE A 1 68  ? 119.299 156.782 98.224  1.00 44.87 ?  68  PHE A CA    1 
ATOM   547   C  C     . PHE A 1 68  ? 118.366 156.882 97.024  1.00 44.22 ?  68  PHE A C     1 
ATOM   548   O  O     . PHE A 1 68  ? 118.830 157.109 95.901  1.00 47.66 ?  68  PHE A O     1 
ATOM   549   C  CB    . PHE A 1 68  ? 119.845 155.360 98.381  1.00 46.19 ?  68  PHE A CB    1 
ATOM   550   C  CG    . PHE A 1 68  ? 118.868 154.279 98.017  1.00 44.21 ?  68  PHE A CG    1 
ATOM   551   C  CD1   . PHE A 1 68  ? 117.893 153.876 98.913  1.00 44.39 ?  68  PHE A CD1   1 
ATOM   552   C  CD2   . PHE A 1 68  ? 118.946 153.642 96.790  1.00 39.83 ?  68  PHE A CD2   1 
ATOM   553   C  CE1   . PHE A 1 68  ? 117.001 152.876 98.583  1.00 42.62 ?  68  PHE A CE1   1 
ATOM   554   C  CE2   . PHE A 1 68  ? 118.057 152.641 96.455  1.00 43.07 ?  68  PHE A CE2   1 
ATOM   555   C  CZ    . PHE A 1 68  ? 117.085 152.256 97.354  1.00 45.52 ?  68  PHE A CZ    1 
ATOM   556   N  N     . LEU A 1 69  ? 117.058 156.721 97.233  1.00 46.25 ?  69  LEU A N     1 
ATOM   557   C  CA    . LEU A 1 69  ? 116.115 156.888 96.133  1.00 46.48 ?  69  LEU A CA    1 
ATOM   558   C  C     . LEU A 1 69  ? 115.869 158.355 95.808  1.00 48.21 ?  69  LEU A C     1 
ATOM   559   O  O     . LEU A 1 69  ? 115.547 158.684 94.660  1.00 45.42 ?  69  LEU A O     1 
ATOM   560   C  CB    . LEU A 1 69  ? 114.792 156.194 96.460  1.00 45.84 ?  69  LEU A CB    1 
ATOM   561   C  CG    . LEU A 1 69  ? 114.784 154.673 96.297  1.00 43.33 ?  69  LEU A CG    1 
ATOM   562   C  CD1   . LEU A 1 69  ? 113.450 154.086 96.727  1.00 43.30 ?  69  LEU A CD1   1 
ATOM   563   C  CD2   . LEU A 1 69  ? 115.110 154.280 94.865  1.00 42.58 ?  69  LEU A CD2   1 
ATOM   564   N  N     . SER A 1 70  ? 116.018 159.245 96.792  1.00 50.75 ?  70  SER A N     1 
ATOM   565   C  CA    . SER A 1 70  ? 115.781 160.664 96.560  1.00 49.04 ?  70  SER A CA    1 
ATOM   566   C  C     . SER A 1 70  ? 116.861 161.305 95.699  1.00 49.55 ?  70  SER A C     1 
ATOM   567   O  O     . SER A 1 70  ? 116.641 162.398 95.166  1.00 51.31 ?  70  SER A O     1 
ATOM   568   C  CB    . SER A 1 70  ? 115.677 161.402 97.896  1.00 50.83 ?  70  SER A CB    1 
ATOM   569   O  OG    . SER A 1 70  ? 116.949 161.538 98.503  1.00 52.71 ?  70  SER A OG    1 
ATOM   570   N  N     . LEU A 1 71  ? 118.018 160.658 95.550  1.00 44.06 ?  71  LEU A N     1 
ATOM   571   C  CA    . LEU A 1 71  ? 119.087 161.208 94.727  1.00 43.61 ?  71  LEU A CA    1 
ATOM   572   C  C     . LEU A 1 71  ? 118.781 161.139 93.238  1.00 44.26 ?  71  LEU A C     1 
ATOM   573   O  O     . LEU A 1 71  ? 119.473 161.795 92.451  1.00 44.16 ?  71  LEU A O     1 
ATOM   574   C  CB    . LEU A 1 71  ? 120.401 160.479 95.013  1.00 45.70 ?  71  LEU A CB    1 
ATOM   575   C  CG    . LEU A 1 71  ? 120.814 160.374 96.480  1.00 47.64 ?  71  LEU A CG    1 
ATOM   576   C  CD1   . LEU A 1 71  ? 121.728 159.179 96.692  1.00 47.24 ?  71  LEU A CD1   1 
ATOM   577   C  CD2   . LEU A 1 71  ? 121.488 161.657 96.934  1.00 45.83 ?  71  LEU A CD2   1 
ATOM   578   N  N     . TYR A 1 72  ? 117.775 160.371 92.834  1.00 44.00 ?  72  TYR A N     1 
ATOM   579   C  CA    . TYR A 1 72  ? 117.395 160.238 91.437  1.00 44.48 ?  72  TYR A CA    1 
ATOM   580   C  C     . TYR A 1 72  ? 115.979 160.751 91.235  1.00 46.44 ?  72  TYR A C     1 
ATOM   581   O  O     . TYR A 1 72  ? 115.134 160.666 92.131  1.00 47.83 ?  72  TYR A O     1 
ATOM   582   C  CB    . TYR A 1 72  ? 117.461 158.778 90.961  1.00 43.94 ?  72  TYR A CB    1 
ATOM   583   C  CG    . TYR A 1 72  ? 118.718 158.029 91.336  1.00 41.73 ?  72  TYR A CG    1 
ATOM   584   C  CD1   . TYR A 1 72  ? 118.864 157.467 92.597  1.00 42.19 ?  72  TYR A CD1   1 
ATOM   585   C  CD2   . TYR A 1 72  ? 119.746 157.861 90.421  1.00 40.29 ?  72  TYR A CD2   1 
ATOM   586   C  CE1   . TYR A 1 72  ? 120.005 156.777 92.942  1.00 41.19 ?  72  TYR A CE1   1 
ATOM   587   C  CE2   . TYR A 1 72  ? 120.891 157.169 90.756  1.00 40.28 ?  72  TYR A CE2   1 
ATOM   588   C  CZ    . TYR A 1 72  ? 121.015 156.630 92.018  1.00 40.85 ?  72  TYR A CZ    1 
ATOM   589   O  OH    . TYR A 1 72  ? 122.153 155.942 92.360  1.00 43.51 ?  72  TYR A OH    1 
ATOM   590   N  N     . SER A 1 73  ? 115.727 161.290 90.047  1.00 51.19 ?  73  SER A N     1 
ATOM   591   C  CA    . SER A 1 73  ? 114.355 161.504 89.625  1.00 50.58 ?  73  SER A CA    1 
ATOM   592   C  C     . SER A 1 73  ? 113.698 160.156 89.344  1.00 52.96 ?  73  SER A C     1 
ATOM   593   O  O     . SER A 1 73  ? 114.370 159.151 89.092  1.00 52.97 ?  73  SER A O     1 
ATOM   594   C  CB    . SER A 1 73  ? 114.303 162.396 88.386  1.00 50.80 ?  73  SER A CB    1 
ATOM   595   O  OG    . SER A 1 73  ? 114.636 161.667 87.218  1.00 50.85 ?  73  SER A OG    1 
ATOM   596   N  N     . PHE A 1 74  ? 112.366 160.133 89.403  1.00 55.14 ?  74  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 74  ? 111.660 158.878 89.171  1.00 53.82 ?  74  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 74  ? 111.899 158.351 87.762  1.00 55.08 ?  74  PHE A C     1 
ATOM   599   O  O     . PHE A 1 74  ? 111.886 157.135 87.546  1.00 56.91 ?  74  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 74  ? 110.163 159.043 89.424  1.00 54.87 ?  74  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 74  ? 109.343 157.880 88.944  1.00 56.02 ?  74  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 74  ? 109.398 156.665 89.607  1.00 54.35 ?  74  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 74  ? 108.530 157.993 87.829  1.00 56.03 ?  74  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 74  ? 108.657 155.588 89.169  1.00 56.64 ?  74  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 74  ? 107.784 156.917 87.387  1.00 56.94 ?  74  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 74  ? 107.848 155.714 88.059  1.00 57.05 ?  74  PHE A CZ    1 
ATOM   607   N  N     . GLU A 1 75  ? 112.117 159.245 86.793  1.00 54.57 ?  75  GLU A N     1 
ATOM   608   C  CA    . GLU A 1 75  ? 112.410 158.800 85.434  1.00 55.54 ?  75  GLU A CA    1 
ATOM   609   C  C     . GLU A 1 75  ? 113.717 158.016 85.383  1.00 57.99 ?  75  GLU A C     1 
ATOM   610   O  O     . GLU A 1 75  ? 113.808 156.990 84.703  1.00 58.35 ?  75  GLU A O     1 
ATOM   611   C  CB    . GLU A 1 75  ? 112.459 160.000 84.482  1.00 54.90 ?  75  GLU A CB    1 
ATOM   612   C  CG    . GLU A 1 75  ? 111.212 160.933 84.418  1.00 55.52 ?  75  GLU A CG    1 
ATOM   613   C  CD    . GLU A 1 75  ? 109.837 160.241 84.370  1.00 58.83 ?  75  GLU A CD    1 
ATOM   614   O  OE1   . GLU A 1 75  ? 109.721 159.010 84.518  1.00 59.31 ?  75  GLU A OE1   1 
ATOM   615   O  OE2   . GLU A 1 75  ? 108.834 160.966 84.183  1.00 57.49 -1 75  GLU A OE2   1 
ATOM   616   N  N     . ASP A 1 76  ? 114.736 158.480 86.109  1.00 52.85 ?  76  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 76  ? 116.012 157.772 86.136  1.00 49.88 ?  76  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 76  ? 115.883 156.408 86.809  1.00 49.23 ?  76  ASP A C     1 
ATOM   619   O  O     . ASP A 1 76  ? 116.462 155.422 86.339  1.00 53.95 ?  76  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 76  ? 117.064 158.626 86.840  1.00 52.85 ?  76  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 76  ? 117.449 159.851 86.034  1.00 55.11 ?  76  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 76  ? 116.835 160.082 84.971  1.00 54.60 ?  76  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 76  ? 118.372 160.577 86.457  1.00 53.49 -1 76  ASP A OD2   1 
ATOM   624   N  N     . ILE A 1 77  ? 115.129 156.332 87.909  1.00 44.02 ?  77  ILE A N     1 
ATOM   625   C  CA    . ILE A 1 77  ? 114.918 155.049 88.580  1.00 45.79 ?  77  ILE A CA    1 
ATOM   626   C  C     . ILE A 1 77  ? 114.164 154.089 87.670  1.00 44.53 ?  77  ILE A C     1 
ATOM   627   O  O     . ILE A 1 77  ? 114.487 152.896 87.590  1.00 47.23 ?  77  ILE A O     1 
ATOM   628   C  CB    . ILE A 1 77  ? 114.180 155.261 89.916  1.00 46.81 ?  77  ILE A CB    1 
ATOM   629   C  CG1   . ILE A 1 77  ? 115.014 156.140 90.846  1.00 46.87 ?  77  ILE A CG1   1 
ATOM   630   C  CG2   . ILE A 1 77  ? 113.881 153.927 90.578  1.00 44.75 ?  77  ILE A CG2   1 
ATOM   631   C  CD1   . ILE A 1 77  ? 114.280 156.584 92.087  1.00 45.19 ?  77  ILE A CD1   1 
ATOM   632   N  N     . LYS A 1 78  ? 113.141 154.592 86.975  1.00 48.26 ?  78  LYS A N     1 
ATOM   633   C  CA    . LYS A 1 78  ? 112.397 153.757 86.039  1.00 49.51 ?  78  LYS A CA    1 
ATOM   634   C  C     . LYS A 1 78  ? 113.288 153.282 84.900  1.00 49.50 ?  78  LYS A C     1 
ATOM   635   O  O     . LYS A 1 78  ? 113.176 152.135 84.455  1.00 51.38 ?  78  LYS A O     1 
ATOM   636   C  CB    . LYS A 1 78  ? 111.191 154.526 85.499  1.00 51.36 ?  78  LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 78  ? 110.267 153.707 84.616  1.00 50.07 ?  78  LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 78  ? 109.038 154.507 84.225  1.00 51.85 ?  78  LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 78  ? 108.296 153.848 83.079  1.00 53.23 ?  78  LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 78  ? 107.377 154.806 82.408  1.00 50.53 1  78  LYS A NZ    1 
ATOM   641   N  N     . GLU A 1 79  ? 114.180 154.148 84.412  1.00 50.11 ?  79  GLU A N     1 
ATOM   642   C  CA    . GLU A 1 79  ? 115.109 153.743 83.362  1.00 50.50 ?  79  GLU A CA    1 
ATOM   643   C  C     . GLU A 1 79  ? 116.069 152.668 83.855  1.00 48.79 ?  79  GLU A C     1 
ATOM   644   O  O     . GLU A 1 79  ? 116.392 151.731 83.117  1.00 48.81 ?  79  GLU A O     1 
ATOM   645   C  CB    . GLU A 1 79  ? 115.880 154.957 82.840  1.00 50.57 ?  79  GLU A CB    1 
ATOM   646   C  CG    . GLU A 1 79  ? 115.483 155.475 81.440  1.00 51.59 ?  79  GLU A CG    1 
ATOM   647   C  CD    . GLU A 1 79  ? 115.621 154.458 80.298  1.00 55.08 ?  79  GLU A CD    1 
ATOM   648   O  OE1   . GLU A 1 79  ? 115.740 154.910 79.139  1.00 55.04 ?  79  GLU A OE1   1 
ATOM   649   O  OE2   . GLU A 1 79  ? 115.620 153.231 80.524  1.00 54.19 -1 79  GLU A OE2   1 
ATOM   650   N  N     . VAL A 1 80  ? 116.539 152.786 85.097  1.00 44.57 ?  80  VAL A N     1 
ATOM   651   C  CA    . VAL A 1 80  ? 117.419 151.763 85.656  1.00 41.51 ?  80  VAL A CA    1 
ATOM   652   C  C     . VAL A 1 80  ? 116.684 150.431 85.781  1.00 45.35 ?  80  VAL A C     1 
ATOM   653   O  O     . VAL A 1 80  ? 117.224 149.369 85.438  1.00 46.84 ?  80  VAL A O     1 
ATOM   654   C  CB    . VAL A 1 80  ? 117.983 152.236 87.006  1.00 40.87 ?  80  VAL A CB    1 
ATOM   655   C  CG1   . VAL A 1 80  ? 118.699 151.102 87.713  1.00 41.66 ?  80  VAL A CG1   1 
ATOM   656   C  CG2   . VAL A 1 80  ? 118.925 153.408 86.796  1.00 40.91 ?  80  VAL A CG2   1 
ATOM   657   N  N     . PHE A 1 81  ? 115.441 150.463 86.268  1.00 41.17 ?  81  PHE A N     1 
ATOM   658   C  CA    . PHE A 1 81  ? 114.655 149.236 86.372  1.00 39.00 ?  81  PHE A CA    1 
ATOM   659   C  C     . PHE A 1 81  ? 114.388 148.631 84.998  1.00 43.72 ?  81  PHE A C     1 
ATOM   660   O  O     . PHE A 1 81  ? 114.419 147.405 84.832  1.00 47.44 ?  81  PHE A O     1 
ATOM   661   C  CB    . PHE A 1 81  ? 113.339 149.515 87.099  1.00 40.74 ?  81  PHE A CB    1 
ATOM   662   C  CG    . PHE A 1 81  ? 113.420 149.354 88.591  1.00 39.06 ?  81  PHE A CG    1 
ATOM   663   C  CD1   . PHE A 1 81  ? 113.906 150.379 89.386  1.00 40.39 ?  81  PHE A CD1   1 
ATOM   664   C  CD2   . PHE A 1 81  ? 113.010 148.181 89.197  1.00 38.70 ?  81  PHE A CD2   1 
ATOM   665   C  CE1   . PHE A 1 81  ? 113.980 150.235 90.758  1.00 41.25 ?  81  PHE A CE1   1 
ATOM   666   C  CE2   . PHE A 1 81  ? 113.082 148.032 90.570  1.00 39.22 ?  81  PHE A CE2   1 
ATOM   667   C  CZ    . PHE A 1 81  ? 113.568 149.061 91.350  1.00 39.43 ?  81  PHE A CZ    1 
ATOM   668   N  N     . LYS A 1 82  ? 114.116 149.475 84.002  1.00 45.50 ?  82  LYS A N     1 
ATOM   669   C  CA    . LYS A 1 82  ? 113.897 148.988 82.645  1.00 44.86 ?  82  LYS A CA    1 
ATOM   670   C  C     . LYS A 1 82  ? 115.163 148.362 82.076  1.00 44.10 ?  82  LYS A C     1 
ATOM   671   O  O     . LYS A 1 82  ? 115.096 147.353 81.369  1.00 46.58 ?  82  LYS A O     1 
ATOM   672   C  CB    . LYS A 1 82  ? 113.411 150.128 81.752  1.00 46.41 ?  82  LYS A CB    1 
ATOM   673   C  CG    . LYS A 1 82  ? 111.929 150.427 81.883  1.00 47.69 ?  82  LYS A CG    1 
ATOM   674   C  CD    . LYS A 1 82  ? 111.457 151.362 80.783  1.00 49.23 ?  82  LYS A CD    1 
ATOM   675   C  CE    . LYS A 1 82  ? 110.027 151.055 80.380  1.00 48.47 ?  82  LYS A CE    1 
ATOM   676   N  NZ    . LYS A 1 82  ? 109.712 149.607 80.532  1.00 48.61 1  82  LYS A NZ    1 
ATOM   677   N  N     . THR A 1 83  ? 116.323 148.954 82.362  1.00 41.81 ?  83  THR A N     1 
ATOM   678   C  CA    . THR A 1 83  ? 117.584 148.356 81.936  1.00 42.61 ?  83  THR A CA    1 
ATOM   679   C  C     . THR A 1 83  ? 117.792 147.000 82.595  1.00 44.80 ?  83  THR A C     1 
ATOM   680   O  O     . THR A 1 83  ? 118.281 146.058 81.959  1.00 47.02 ?  83  THR A O     1 
ATOM   681   C  CB    . THR A 1 83  ? 118.748 149.294 82.258  1.00 42.16 ?  83  THR A CB    1 
ATOM   682   O  OG1   . THR A 1 83  ? 118.502 150.580 81.675  1.00 47.88 ?  83  THR A OG1   1 
ATOM   683   C  CG2   . THR A 1 83  ? 120.050 148.741 81.703  1.00 43.17 ?  83  THR A CG2   1 
ATOM   684   N  N     . ALA A 1 84  ? 117.431 146.883 83.875  1.00 38.43 ?  84  ALA A N     1 
ATOM   685   C  CA    . ALA A 1 84  ? 117.539 145.595 84.555  1.00 35.86 ?  84  ALA A CA    1 
ATOM   686   C  C     . ALA A 1 84  ? 116.620 144.554 83.931  1.00 39.07 ?  84  ALA A C     1 
ATOM   687   O  O     . ALA A 1 84  ? 117.017 143.400 83.736  1.00 42.31 ?  84  ALA A O     1 
ATOM   688   C  CB    . ALA A 1 84  ? 117.231 145.758 86.041  1.00 36.56 ?  84  ALA A CB    1 
ATOM   689   N  N     . TYR A 1 85  ? 115.385 144.940 83.612  1.00 44.03 ?  85  TYR A N     1 
ATOM   690   C  CA    . TYR A 1 85  ? 114.415 143.997 83.070  1.00 39.83 ?  85  TYR A CA    1 
ATOM   691   C  C     . TYR A 1 85  ? 114.600 143.722 81.583  1.00 40.48 ?  85  TYR A C     1 
ATOM   692   O  O     . TYR A 1 85  ? 114.045 142.738 81.082  1.00 41.84 ?  85  TYR A O     1 
ATOM   693   C  CB    . TYR A 1 85  ? 112.993 144.505 83.320  1.00 41.64 ?  85  TYR A CB    1 
ATOM   694   C  CG    . TYR A 1 85  ? 112.460 144.186 84.697  1.00 41.09 ?  85  TYR A CG    1 
ATOM   695   C  CD1   . TYR A 1 85  ? 111.786 142.998 84.942  1.00 39.31 ?  85  TYR A CD1   1 
ATOM   696   C  CD2   . TYR A 1 85  ? 112.630 145.070 85.754  1.00 42.16 ?  85  TYR A CD2   1 
ATOM   697   C  CE1   . TYR A 1 85  ? 111.296 142.699 86.196  1.00 41.12 ?  85  TYR A CE1   1 
ATOM   698   C  CE2   . TYR A 1 85  ? 112.142 144.780 87.013  1.00 42.11 ?  85  TYR A CE2   1 
ATOM   699   C  CZ    . TYR A 1 85  ? 111.476 143.594 87.228  1.00 43.05 ?  85  TYR A CZ    1 
ATOM   700   O  OH    . TYR A 1 85  ? 110.989 143.299 88.478  1.00 43.05 ?  85  TYR A OH    1 
ATOM   701   N  N     . ALA A 1 86  ? 115.359 144.555 80.867  1.00 40.35 ?  86  ALA A N     1 
ATOM   702   C  CA    . ALA A 1 86  ? 115.569 144.335 79.442  1.00 40.94 ?  86  ALA A CA    1 
ATOM   703   C  C     . ALA A 1 86  ? 116.440 143.120 79.164  1.00 45.40 ?  86  ALA A C     1 
ATOM   704   O  O     . ALA A 1 86  ? 116.367 142.559 78.066  1.00 45.64 ?  86  ALA A O     1 
ATOM   705   C  CB    . ALA A 1 86  ? 116.193 145.576 78.805  1.00 39.65 ?  86  ALA A CB    1 
ATOM   706   N  N     . LYS A 1 87  ? 117.262 142.705 80.129  1.00 43.91 ?  87  LYS A N     1 
ATOM   707   C  CA    . LYS A 1 87  ? 118.080 141.513 79.941  1.00 41.44 ?  87  LYS A CA    1 
ATOM   708   C  C     . LYS A 1 87  ? 117.223 140.258 79.834  1.00 42.51 ?  87  LYS A C     1 
ATOM   709   O  O     . LYS A 1 87  ? 117.625 139.289 79.179  1.00 44.65 ?  87  LYS A O     1 
ATOM   710   C  CB    . LYS A 1 87  ? 119.085 141.387 81.089  1.00 41.57 ?  87  LYS A CB    1 
ATOM   711   C  CG    . LYS A 1 87  ? 119.830 140.063 81.143  1.00 43.60 ?  87  LYS A CG    1 
ATOM   712   C  CD    . LYS A 1 87  ? 121.309 140.245 80.864  1.00 40.15 ?  87  LYS A CD    1 
ATOM   713   C  CE    . LYS A 1 87  ? 122.044 138.917 80.902  1.00 40.86 ?  87  LYS A CE    1 
ATOM   714   N  NZ    . LYS A 1 87  ? 122.979 138.769 79.753  1.00 42.63 1  87  LYS A NZ    1 
ATOM   715   N  N     . LYS A 1 88  ? 116.032 140.273 80.437  1.00 43.17 ?  88  LYS A N     1 
ATOM   716   C  CA    . LYS A 1 88  ? 115.174 139.091 80.528  1.00 41.87 ?  88  LYS A CA    1 
ATOM   717   C  C     . LYS A 1 88  ? 115.929 137.937 81.181  1.00 40.24 ?  88  LYS A C     1 
ATOM   718   O  O     . LYS A 1 88  ? 115.923 136.802 80.699  1.00 43.96 ?  88  LYS A O     1 
ATOM   719   C  CB    . LYS A 1 88  ? 114.627 138.691 79.155  1.00 43.41 ?  88  LYS A CB    1 
ATOM   720   C  CG    . LYS A 1 88  ? 113.304 139.348 78.793  1.00 44.06 ?  88  LYS A CG    1 
ATOM   721   C  CD    . LYS A 1 88  ? 113.510 140.525 77.852  1.00 44.79 ?  88  LYS A CD    1 
ATOM   722   C  CE    . LYS A 1 88  ? 112.534 141.652 78.151  1.00 45.47 ?  88  LYS A CE    1 
ATOM   723   N  NZ    . LYS A 1 88  ? 112.831 142.873 77.351  1.00 43.81 1  88  LYS A NZ    1 
ATOM   724   N  N     . PHE A 1 89  ? 116.599 138.247 82.289  1.00 39.10 ?  89  PHE A N     1 
ATOM   725   C  CA    . PHE A 1 89  ? 117.418 137.260 82.977  1.00 33.63 ?  89  PHE A CA    1 
ATOM   726   C  C     . PHE A 1 89  ? 116.568 136.094 83.458  1.00 40.27 ?  89  PHE A C     1 
ATOM   727   O  O     . PHE A 1 89  ? 115.481 136.279 84.013  1.00 42.10 ?  89  PHE A O     1 
ATOM   728   C  CB    . PHE A 1 89  ? 118.143 137.903 84.161  1.00 34.46 ?  89  PHE A CB    1 
ATOM   729   C  CG    . PHE A 1 89  ? 118.902 136.924 85.008  1.00 34.23 ?  89  PHE A CG    1 
ATOM   730   C  CD1   . PHE A 1 89  ? 120.172 136.515 84.643  1.00 34.64 ?  89  PHE A CD1   1 
ATOM   731   C  CD2   . PHE A 1 89  ? 118.346 136.408 86.166  1.00 35.69 ?  89  PHE A CD2   1 
ATOM   732   C  CE1   . PHE A 1 89  ? 120.871 135.611 85.416  1.00 37.08 ?  89  PHE A CE1   1 
ATOM   733   C  CE2   . PHE A 1 89  ? 119.041 135.502 86.940  1.00 32.64 ?  89  PHE A CE2   1 
ATOM   734   C  CZ    . PHE A 1 89  ? 120.305 135.105 86.568  1.00 35.02 ?  89  PHE A CZ    1 
ATOM   735   N  N     . ARG A 1 90  ? 117.075 134.884 83.242  1.00 41.70 ?  90  ARG A N     1 
ATOM   736   C  CA    . ARG A 1 90  ? 116.425 133.665 83.697  1.00 40.07 ?  90  ARG A CA    1 
ATOM   737   C  C     . ARG A 1 90  ? 117.418 132.856 84.513  1.00 39.11 ?  90  ARG A C     1 
ATOM   738   O  O     . ARG A 1 90  ? 118.556 132.647 84.080  1.00 40.65 ?  90  ARG A O     1 
ATOM   739   C  CB    . ARG A 1 90  ? 115.906 132.835 82.516  1.00 39.99 ?  90  ARG A CB    1 
ATOM   740   C  CG    . ARG A 1 90  ? 114.983 133.591 81.580  1.00 41.43 ?  90  ARG A CG    1 
ATOM   741   C  CD    . ARG A 1 90  ? 113.639 133.871 82.231  1.00 42.63 ?  90  ARG A CD    1 
ATOM   742   N  NE    . ARG A 1 90  ? 112.856 134.835 81.467  1.00 44.13 ?  90  ARG A NE    1 
ATOM   743   C  CZ    . ARG A 1 90  ? 112.447 136.006 81.935  1.00 45.93 ?  90  ARG A CZ    1 
ATOM   744   N  NH1   . ARG A 1 90  ? 112.720 136.389 83.172  1.00 45.56 1  90  ARG A NH1   1 
ATOM   745   N  NH2   . ARG A 1 90  ? 111.746 136.812 81.144  1.00 43.70 ?  90  ARG A NH2   1 
ATOM   746   N  N     . PHE A 1 91  ? 116.995 132.416 85.688  1.00 36.18 ?  91  PHE A N     1 
ATOM   747   C  CA    . PHE A 1 91  ? 117.833 131.544 86.495  1.00 37.86 ?  91  PHE A CA    1 
ATOM   748   C  C     . PHE A 1 91  ? 118.003 130.207 85.783  1.00 43.33 ?  91  PHE A C     1 
ATOM   749   O  O     . PHE A 1 91  ? 117.006 129.571 85.424  1.00 44.55 ?  91  PHE A O     1 
ATOM   750   C  CB    . PHE A 1 91  ? 117.219 131.338 87.878  1.00 35.06 ?  91  PHE A CB    1 
ATOM   751   C  CG    . PHE A 1 91  ? 117.269 132.558 88.751  1.00 39.65 ?  91  PHE A CG    1 
ATOM   752   C  CD1   . PHE A 1 91  ? 118.408 132.862 89.476  1.00 41.67 ?  91  PHE A CD1   1 
ATOM   753   C  CD2   . PHE A 1 91  ? 116.177 133.404 88.845  1.00 38.52 ?  91  PHE A CD2   1 
ATOM   754   C  CE1   . PHE A 1 91  ? 118.457 133.984 90.281  1.00 39.51 ?  91  PHE A CE1   1 
ATOM   755   C  CE2   . PHE A 1 91  ? 116.220 134.527 89.649  1.00 38.91 ?  91  PHE A CE2   1 
ATOM   756   C  CZ    . PHE A 1 91  ? 117.362 134.817 90.366  1.00 38.48 ?  91  PHE A CZ    1 
ATOM   757   N  N     . PRO A 1 92  ? 119.238 129.749 85.556  1.00 43.39 ?  92  PRO A N     1 
ATOM   758   C  CA    . PRO A 1 92  ? 119.425 128.500 84.806  1.00 42.30 ?  92  PRO A CA    1 
ATOM   759   C  C     . PRO A 1 92  ? 119.145 127.248 85.614  1.00 43.13 ?  92  PRO A C     1 
ATOM   760   O  O     . PRO A 1 92  ? 118.903 126.190 85.019  1.00 44.76 ?  92  PRO A O     1 
ATOM   761   C  CB    . PRO A 1 92  ? 120.897 128.568 84.388  1.00 42.75 ?  92  PRO A CB    1 
ATOM   762   C  CG    . PRO A 1 92  ? 121.544 129.323 85.501  1.00 43.24 ?  92  PRO A CG    1 
ATOM   763   C  CD    . PRO A 1 92  ? 120.520 130.318 86.008  1.00 40.50 ?  92  PRO A CD    1 
ATOM   764   N  N     . SER A 1 93  ? 119.167 127.331 86.942  1.00 42.55 ?  93  SER A N     1 
ATOM   765   C  CA    . SER A 1 93  ? 118.947 126.185 87.806  1.00 41.96 ?  93  SER A CA    1 
ATOM   766   C  C     . SER A 1 93  ? 117.931 126.552 88.877  1.00 44.09 ?  93  SER A C     1 
ATOM   767   O  O     . SER A 1 93  ? 117.769 127.722 89.235  1.00 47.27 ?  93  SER A O     1 
ATOM   768   C  CB    . SER A 1 93  ? 120.253 125.709 88.453  1.00 43.27 ?  93  SER A CB    1 
ATOM   769   O  OG    . SER A 1 93  ? 120.518 126.422 89.648  1.00 45.05 ?  93  SER A OG    1 
ATOM   770   N  N     . PHE A 1 94  ? 117.234 125.530 89.378  1.00 43.75 ?  94  PHE A N     1 
ATOM   771   C  CA    . PHE A 1 94  ? 116.211 125.762 90.392  1.00 40.05 ?  94  PHE A CA    1 
ATOM   772   C  C     . PHE A 1 94  ? 116.817 126.320 91.672  1.00 42.38 ?  94  PHE A C     1 
ATOM   773   O  O     . PHE A 1 94  ? 116.228 127.197 92.315  1.00 44.10 ?  94  PHE A O     1 
ATOM   774   C  CB    . PHE A 1 94  ? 115.449 124.469 90.682  1.00 40.38 ?  94  PHE A CB    1 
ATOM   775   C  CG    . PHE A 1 94  ? 114.802 124.442 92.037  1.00 41.40 ?  94  PHE A CG    1 
ATOM   776   C  CD1   . PHE A 1 94  ? 113.684 125.214 92.300  1.00 41.31 ?  94  PHE A CD1   1 
ATOM   777   C  CD2   . PHE A 1 94  ? 115.314 123.649 93.049  1.00 44.07 ?  94  PHE A CD2   1 
ATOM   778   C  CE1   . PHE A 1 94  ? 113.092 125.198 93.546  1.00 41.35 ?  94  PHE A CE1   1 
ATOM   779   C  CE2   . PHE A 1 94  ? 114.724 123.627 94.297  1.00 45.35 ?  94  PHE A CE2   1 
ATOM   780   C  CZ    . PHE A 1 94  ? 113.611 124.402 94.545  1.00 41.55 ?  94  PHE A CZ    1 
ATOM   781   N  N     . MET A 1 95  ? 117.992 125.820 92.063  1.00 41.51 ?  95  MET A N     1 
ATOM   782   C  CA    . MET A 1 95  ? 118.587 126.243 93.324  1.00 39.30 ?  95  MET A CA    1 
ATOM   783   C  C     . MET A 1 95  ? 118.980 127.713 93.308  1.00 41.31 ?  95  MET A C     1 
ATOM   784   O  O     . MET A 1 95  ? 118.924 128.368 94.350  1.00 42.06 ?  95  MET A O     1 
ATOM   785   C  CB    . MET A 1 95  ? 119.798 125.370 93.657  1.00 40.51 ?  95  MET A CB    1 
ATOM   786   C  CG    . MET A 1 95  ? 120.390 125.588 95.050  1.00 43.89 ?  95  MET A CG    1 
ATOM   787   S  SD    . MET A 1 95  ? 119.362 125.201 96.491  1.00 54.57 ?  95  MET A SD    1 
ATOM   788   C  CE    . MET A 1 95  ? 118.191 124.008 95.848  1.00 45.92 ?  95  MET A CE    1 
ATOM   789   N  N     . SER A 1 96  ? 119.362 128.252 92.150  1.00 38.56 ?  96  SER A N     1 
ATOM   790   C  CA    . SER A 1 96  ? 119.689 129.674 92.073  1.00 34.14 ?  96  SER A CA    1 
ATOM   791   C  C     . SER A 1 96  ? 118.491 130.533 92.461  1.00 38.41 ?  96  SER A C     1 
ATOM   792   O  O     . SER A 1 96  ? 118.578 131.387 93.356  1.00 40.40 ?  96  SER A O     1 
ATOM   793   C  CB    . SER A 1 96  ? 120.163 130.019 90.662  1.00 32.01 ?  96  SER A CB    1 
ATOM   794   O  OG    . SER A 1 96  ? 121.048 129.033 90.166  1.00 36.90 ?  96  SER A OG    1 
ATOM   795   N  N     . ALA A 1 97  ? 117.352 130.298 91.807  1.00 38.59 ?  97  ALA A N     1 
ATOM   796   C  CA    . ALA A 1 97  ? 116.148 131.063 92.104  1.00 34.80 ?  97  ALA A CA    1 
ATOM   797   C  C     . ALA A 1 97  ? 115.656 130.790 93.516  1.00 35.83 ?  97  ALA A C     1 
ATOM   798   O  O     . ALA A 1 97  ? 115.199 131.708 94.207  1.00 41.87 ?  97  ALA A O     1 
ATOM   799   C  CB    . ALA A 1 97  ? 115.059 130.740 91.084  1.00 36.02 ?  97  ALA A CB    1 
ATOM   800   N  N     . PHE A 1 98  ? 115.730 129.534 93.959  1.00 37.46 ?  98  PHE A N     1 
ATOM   801   C  CA    . PHE A 1 98  ? 115.285 129.204 95.307  1.00 37.31 ?  98  PHE A CA    1 
ATOM   802   C  C     . PHE A 1 98  ? 116.114 129.937 96.353  1.00 37.48 ?  98  PHE A C     1 
ATOM   803   O  O     . PHE A 1 98  ? 115.563 130.518 97.294  1.00 46.19 ?  98  PHE A O     1 
ATOM   804   C  CB    . PHE A 1 98  ? 115.354 127.694 95.531  1.00 41.86 ?  98  PHE A CB    1 
ATOM   805   C  CG    . PHE A 1 98  ? 114.957 127.271 96.915  1.00 42.40 ?  98  PHE A CG    1 
ATOM   806   C  CD1   . PHE A 1 98  ? 113.621 127.175 97.265  1.00 42.56 ?  98  PHE A CD1   1 
ATOM   807   C  CD2   . PHE A 1 98  ? 115.917 126.977 97.868  1.00 41.56 ?  98  PHE A CD2   1 
ATOM   808   C  CE1   . PHE A 1 98  ? 113.251 126.790 98.537  1.00 43.31 ?  98  PHE A CE1   1 
ATOM   809   C  CE2   . PHE A 1 98  ? 115.552 126.592 99.142  1.00 42.84 ?  98  PHE A CE2   1 
ATOM   810   C  CZ    . PHE A 1 98  ? 114.217 126.498 99.477  1.00 44.36 ?  98  PHE A CZ    1 
ATOM   811   N  N     . LYS A 1 99  ? 117.438 129.936 96.194  1.00 38.45 ?  99  LYS A N     1 
ATOM   812   C  CA    . LYS A 1 99  ? 118.306 130.617 97.145  1.00 36.82 ?  99  LYS A CA    1 
ATOM   813   C  C     . LYS A 1 99  ? 118.075 132.119 97.124  1.00 38.12 ?  99  LYS A C     1 
ATOM   814   O  O     . LYS A 1 99  ? 118.058 132.760 98.182  1.00 43.28 ?  99  LYS A O     1 
ATOM   815   C  CB    . LYS A 1 99  ? 119.769 130.292 96.846  1.00 37.70 ?  99  LYS A CB    1 
ATOM   816   C  CG    . LYS A 1 99  ? 120.206 128.919 97.326  1.00 39.76 ?  99  LYS A CG    1 
ATOM   817   C  CD    . LYS A 1 99  ? 119.786 128.668 98.762  1.00 41.23 ?  99  LYS A CD    1 
ATOM   818   C  CE    . LYS A 1 99  ? 120.922 128.068 99.571  1.00 39.84 ?  99  LYS A CE    1 
ATOM   819   N  NZ    . LYS A 1 99  ? 120.669 128.176 101.034 1.00 43.67 1  99  LYS A NZ    1 
ATOM   820   N  N     . PHE A 1 100 ? 117.886 132.706 95.939  1.00 33.98 ?  100 PHE A N     1 
ATOM   821   C  CA    . PHE A 1 100 ? 117.634 134.142 95.899  1.00 32.03 ?  100 PHE A CA    1 
ATOM   822   C  C     . PHE A 1 100 ? 116.316 134.494 96.576  1.00 35.49 ?  100 PHE A C     1 
ATOM   823   O  O     . PHE A 1 100 ? 116.261 135.399 97.418  1.00 40.64 ?  100 PHE A O     1 
ATOM   824   C  CB    . PHE A 1 100 ? 117.635 134.670 94.468  1.00 29.77 ?  100 PHE A CB    1 
ATOM   825   C  CG    . PHE A 1 100 ? 117.206 136.103 94.378  1.00 36.38 ?  100 PHE A CG    1 
ATOM   826   C  CD1   . PHE A 1 100 ? 118.052 137.116 94.799  1.00 36.19 ?  100 PHE A CD1   1 
ATOM   827   C  CD2   . PHE A 1 100 ? 115.942 136.439 93.929  1.00 35.11 ?  100 PHE A CD2   1 
ATOM   828   C  CE1   . PHE A 1 100 ? 117.657 138.435 94.744  1.00 35.16 ?  100 PHE A CE1   1 
ATOM   829   C  CE2   . PHE A 1 100 ? 115.540 137.757 93.875  1.00 35.41 ?  100 PHE A CE2   1 
ATOM   830   C  CZ    . PHE A 1 100 ? 116.400 138.757 94.283  1.00 35.14 ?  100 PHE A CZ    1 
ATOM   831   N  N     . TYR A 1 101 ? 115.238 133.792 96.226  1.00 38.04 ?  101 TYR A N     1 
ATOM   832   C  CA    . TYR A 1 101 ? 113.921 134.143 96.735  1.00 37.60 ?  101 TYR A CA    1 
ATOM   833   C  C     . TYR A 1 101 ? 113.676 133.643 98.151  1.00 38.38 ?  101 TYR A C     1 
ATOM   834   O  O     . TYR A 1 101 ? 112.655 134.000 98.747  1.00 44.60 ?  101 TYR A O     1 
ATOM   835   C  CB    . TYR A 1 101 ? 112.839 133.613 95.791  1.00 36.13 ?  101 TYR A CB    1 
ATOM   836   C  CG    . TYR A 1 101 ? 112.719 134.424 94.522  1.00 32.59 ?  101 TYR A CG    1 
ATOM   837   C  CD1   . TYR A 1 101 ? 112.112 135.673 94.528  1.00 36.94 ?  101 TYR A CD1   1 
ATOM   838   C  CD2   . TYR A 1 101 ? 113.226 133.951 93.320  1.00 34.18 ?  101 TYR A CD2   1 
ATOM   839   C  CE1   . TYR A 1 101 ? 112.009 136.421 93.374  1.00 38.04 ?  101 TYR A CE1   1 
ATOM   840   C  CE2   . TYR A 1 101 ? 113.127 134.691 92.162  1.00 36.49 ?  101 TYR A CE2   1 
ATOM   841   C  CZ    . TYR A 1 101 ? 112.517 135.926 92.194  1.00 38.47 ?  101 TYR A CZ    1 
ATOM   842   O  OH    . TYR A 1 101 ? 112.415 136.668 91.040  1.00 41.93 ?  101 TYR A OH    1 
ATOM   843   N  N     . ASN A 1 102 ? 114.580 132.833 98.704  1.00 41.74 ?  102 ASN A N     1 
ATOM   844   C  CA    . ASN A 1 102 ? 114.493 132.430 100.099 1.00 45.03 ?  102 ASN A CA    1 
ATOM   845   C  C     . ASN A 1 102 ? 115.456 133.187 101.001 1.00 45.97 ?  102 ASN A C     1 
ATOM   846   O  O     . ASN A 1 102 ? 115.217 133.257 102.212 1.00 48.30 ?  102 ASN A O     1 
ATOM   847   C  CB    . ASN A 1 102 ? 114.763 130.926 100.231 1.00 42.99 ?  102 ASN A CB    1 
ATOM   848   C  CG    . ASN A 1 102 ? 113.490 130.111 100.336 1.00 46.78 ?  102 ASN A CG    1 
ATOM   849   O  OD1   . ASN A 1 102 ? 112.700 130.047 99.395  1.00 48.92 ?  102 ASN A OD1   1 
ATOM   850   N  ND2   . ASN A 1 102 ? 113.287 129.479 101.485 1.00 44.50 ?  102 ASN A ND2   1 
ATOM   851   N  N     . ASP A 1 103 ? 116.531 133.751 100.450 1.00 41.29 ?  103 ASP A N     1 
ATOM   852   C  CA    . ASP A 1 103 ? 117.545 134.420 101.251 1.00 41.46 ?  103 ASP A CA    1 
ATOM   853   C  C     . ASP A 1 103 ? 117.676 135.908 100.974 1.00 40.82 ?  103 ASP A C     1 
ATOM   854   O  O     . ASP A 1 103 ? 117.927 136.670 101.909 1.00 45.01 ?  103 ASP A O     1 
ATOM   855   C  CB    . ASP A 1 103 ? 118.914 133.763 101.031 1.00 44.47 ?  103 ASP A CB    1 
ATOM   856   C  CG    . ASP A 1 103 ? 118.986 132.361 101.596 1.00 48.51 ?  103 ASP A CG    1 
ATOM   857   O  OD1   . ASP A 1 103 ? 118.020 131.937 102.263 1.00 47.69 ?  103 ASP A OD1   1 
ATOM   858   O  OD2   . ASP A 1 103 ? 120.009 131.681 101.371 1.00 50.67 -1 103 ASP A OD2   1 
ATOM   859   N  N     . TYR A 1 104 ? 117.512 136.345 99.729  1.00 34.75 ?  104 TYR A N     1 
ATOM   860   C  CA    . TYR A 1 104 ? 117.828 137.715 99.353  1.00 38.48 ?  104 TYR A CA    1 
ATOM   861   C  C     . TYR A 1 104 ? 116.636 138.532 98.882  1.00 39.62 ?  104 TYR A C     1 
ATOM   862   O  O     . TYR A 1 104 ? 116.648 139.753 99.047  1.00 43.43 ?  104 TYR A O     1 
ATOM   863   C  CB    . TYR A 1 104 ? 118.903 137.729 98.255  1.00 38.18 ?  104 TYR A CB    1 
ATOM   864   C  CG    . TYR A 1 104 ? 120.183 137.043 98.668  1.00 40.21 ?  104 TYR A CG    1 
ATOM   865   C  CD1   . TYR A 1 104 ? 121.158 137.722 99.386  1.00 37.87 ?  104 TYR A CD1   1 
ATOM   866   C  CD2   . TYR A 1 104 ? 120.412 135.711 98.351  1.00 35.30 ?  104 TYR A CD2   1 
ATOM   867   C  CE1   . TYR A 1 104 ? 122.325 137.097 99.771  1.00 36.61 ?  104 TYR A CE1   1 
ATOM   868   C  CE2   . TYR A 1 104 ? 121.575 135.077 98.733  1.00 35.79 ?  104 TYR A CE2   1 
ATOM   869   C  CZ    . TYR A 1 104 ? 122.529 135.774 99.442  1.00 39.06 ?  104 TYR A CZ    1 
ATOM   870   O  OH    . TYR A 1 104 ? 123.691 135.146 99.823  1.00 40.64 ?  104 TYR A OH    1 
ATOM   871   N  N     . ALA A 1 105 ? 115.617 137.907 98.298  1.00 40.76 ?  105 ALA A N     1 
ATOM   872   C  CA    . ALA A 1 105 ? 114.460 138.659 97.833  1.00 38.14 ?  105 ALA A CA    1 
ATOM   873   C  C     . ALA A 1 105 ? 113.716 139.275 99.011  1.00 42.98 ?  105 ALA A C     1 
ATOM   874   O  O     . ALA A 1 105 ? 113.495 138.626 100.037 1.00 44.65 ?  105 ALA A O     1 
ATOM   875   C  CB    . ALA A 1 105 ? 113.523 137.757 97.032  1.00 37.75 ?  105 ALA A CB    1 
ATOM   876   N  N     . LEU A 1 106 ? 113.336 140.540 98.860  1.00 44.74 ?  106 LEU A N     1 
ATOM   877   C  CA    . LEU A 1 106 ? 112.621 141.236 99.920  1.00 40.94 ?  106 LEU A CA    1 
ATOM   878   C  C     . LEU A 1 106 ? 111.213 140.676 100.062 1.00 45.24 ?  106 LEU A C     1 
ATOM   879   O  O     . LEU A 1 106 ? 110.477 140.553 99.078  1.00 46.46 ?  106 LEU A O     1 
ATOM   880   C  CB    . LEU A 1 106 ? 112.570 142.735 99.633  1.00 44.43 ?  106 LEU A CB    1 
ATOM   881   C  CG    . LEU A 1 106 ? 111.883 143.605 100.687 1.00 43.46 ?  106 LEU A CG    1 
ATOM   882   C  CD1   . LEU A 1 106 ? 112.665 143.592 101.989 1.00 42.46 ?  106 LEU A CD1   1 
ATOM   883   C  CD2   . LEU A 1 106 ? 111.710 145.024 100.176 1.00 43.80 ?  106 LEU A CD2   1 
ATOM   884   N  N     . LYS A 1 107 ? 110.838 140.342 101.292 1.00 50.99 ?  107 LYS A N     1 
ATOM   885   C  CA    . LYS A 1 107 ? 109.525 139.802 101.599 1.00 50.88 ?  107 LYS A CA    1 
ATOM   886   C  C     . LYS A 1 107 ? 108.791 140.741 102.546 1.00 54.09 ?  107 LYS A C     1 
ATOM   887   O  O     . LYS A 1 107 ? 109.397 141.580 103.218 1.00 54.52 ?  107 LYS A O     1 
ATOM   888   C  CB    . LYS A 1 107 ? 109.628 138.404 102.222 1.00 51.63 ?  107 LYS A CB    1 
ATOM   889   C  CG    . LYS A 1 107 ? 110.694 137.520 101.597 1.00 50.31 ?  107 LYS A CG    1 
ATOM   890   C  CD    . LYS A 1 107 ? 110.080 136.488 100.668 1.00 50.99 ?  107 LYS A CD    1 
ATOM   891   C  CE    . LYS A 1 107 ? 110.584 135.090 100.987 1.00 54.46 ?  107 LYS A CE    1 
ATOM   892   N  NZ    . LYS A 1 107 ? 110.233 134.113 99.919  1.00 51.38 1  107 LYS A NZ    1 
ATOM   893   N  N     . THR A 1 108 ? 107.470 140.594 102.585 1.00 58.40 ?  108 THR A N     1 
ATOM   894   C  CA    . THR A 1 108 ? 106.650 141.389 103.483 1.00 57.21 ?  108 THR A CA    1 
ATOM   895   C  C     . THR A 1 108 ? 106.978 141.056 104.939 1.00 59.00 ?  108 THR A C     1 
ATOM   896   O  O     . THR A 1 108 ? 107.695 140.100 105.243 1.00 59.19 ?  108 THR A O     1 
ATOM   897   C  CB    . THR A 1 108 ? 105.168 141.151 103.204 1.00 57.88 ?  108 THR A CB    1 
ATOM   898   O  OG1   . THR A 1 108 ? 104.878 139.752 103.321 1.00 63.02 ?  108 THR A OG1   1 
ATOM   899   C  CG2   . THR A 1 108 ? 104.809 141.619 101.803 1.00 57.15 ?  108 THR A CG2   1 
ATOM   900   N  N     . ASN A 1 109 ? 106.441 141.871 105.850 1.00 60.83 ?  109 ASN A N     1 
ATOM   901   C  CA    . ASN A 1 109 ? 106.679 141.645 107.273 1.00 62.67 ?  109 ASN A CA    1 
ATOM   902   C  C     . ASN A 1 109 ? 106.140 140.295 107.726 1.00 64.04 ?  109 ASN A C     1 
ATOM   903   O  O     . ASN A 1 109 ? 106.671 139.697 108.668 1.00 64.25 ?  109 ASN A O     1 
ATOM   904   C  CB    . ASN A 1 109 ? 106.052 142.768 108.099 1.00 62.17 ?  109 ASN A CB    1 
ATOM   905   C  CG    . ASN A 1 109 ? 106.605 144.132 107.742 1.00 61.16 ?  109 ASN A CG    1 
ATOM   906   O  OD1   . ASN A 1 109 ? 106.901 144.409 106.581 1.00 60.42 ?  109 ASN A OD1   1 
ATOM   907   N  ND2   . ASN A 1 109 ? 106.749 144.993 108.742 1.00 61.63 ?  109 ASN A ND2   1 
ATOM   908   N  N     . ASP A 1 110 ? 105.093 139.801 107.072 1.00 65.81 ?  110 ASP A N     1 
ATOM   909   C  CA    . ASP A 1 110 ? 104.518 138.497 107.370 1.00 64.93 ?  110 ASP A CA    1 
ATOM   910   C  C     . ASP A 1 110 ? 105.221 137.354 106.649 1.00 67.09 ?  110 ASP A C     1 
ATOM   911   O  O     . ASP A 1 110 ? 104.865 136.192 106.870 1.00 67.07 ?  110 ASP A O     1 
ATOM   912   C  CB    . ASP A 1 110 ? 103.025 138.503 107.027 1.00 67.12 ?  110 ASP A CB    1 
ATOM   913   C  CG    . ASP A 1 110 ? 102.769 138.777 105.557 1.00 68.83 ?  110 ASP A CG    1 
ATOM   914   O  OD1   . ASP A 1 110 ? 103.746 139.037 104.824 1.00 68.34 ?  110 ASP A OD1   1 
ATOM   915   O  OD2   . ASP A 1 110 ? 101.596 138.743 105.136 1.00 66.30 -1 110 ASP A OD2   1 
ATOM   916   N  N     . LYS A 1 111 ? 106.206 137.658 105.798 1.00 66.76 ?  111 LYS A N     1 
ATOM   917   C  CA    . LYS A 1 111 ? 107.054 136.655 105.151 1.00 65.22 ?  111 LYS A CA    1 
ATOM   918   C  C     . LYS A 1 111 ? 106.249 135.650 104.328 1.00 67.30 ?  111 LYS A C     1 
ATOM   919   O  O     . LYS A 1 111 ? 106.602 134.471 104.257 1.00 68.62 ?  111 LYS A O     1 
ATOM   920   C  CB    . LYS A 1 111 ? 107.925 135.916 106.173 1.00 66.02 ?  111 LYS A CB    1 
ATOM   921   C  CG    . LYS A 1 111 ? 108.608 136.816 107.190 1.00 66.12 ?  111 LYS A CG    1 
ATOM   922   C  CD    . LYS A 1 111 ? 109.527 137.819 106.513 1.00 67.95 ?  111 LYS A CD    1 
ATOM   923   C  CE    . LYS A 1 111 ? 110.695 137.128 105.829 1.00 68.19 ?  111 LYS A CE    1 
ATOM   924   N  NZ    . LYS A 1 111 ? 111.637 138.107 105.215 1.00 65.71 1  111 LYS A NZ    1 
ATOM   925   N  N     . LYS A 1 112 ? 105.164 136.098 103.697 1.00 65.38 ?  112 LYS A N     1 
ATOM   926   C  CA    . LYS A 1 112 ? 104.372 135.233 102.835 1.00 66.35 ?  112 LYS A CA    1 
ATOM   927   C  C     . LYS A 1 112 ? 104.303 135.718 101.395 1.00 66.89 ?  112 LYS A C     1 
ATOM   928   O  O     . LYS A 1 112 ? 103.854 134.964 100.527 1.00 68.20 ?  112 LYS A O     1 
ATOM   929   C  CB    . LYS A 1 112 ? 102.944 135.087 103.380 1.00 67.22 ?  112 LYS A CB    1 
ATOM   930   C  CG    . LYS A 1 112 ? 102.034 136.255 103.046 1.00 67.45 ?  112 LYS A CG    1 
ATOM   931   C  CD    . LYS A 1 112 ? 100.573 135.904 103.270 1.00 67.24 ?  112 LYS A CD    1 
ATOM   932   C  CE    . LYS A 1 112 ? 100.351 135.323 104.657 1.00 69.30 ?  112 LYS A CE    1 
ATOM   933   N  NZ    . LYS A 1 112 ? 100.878 136.218 105.725 1.00 66.57 1  112 LYS A NZ    1 
ATOM   934   N  N     . LYS A 1 113 ? 104.731 136.947 101.120 1.00 59.81 ?  113 LYS A N     1 
ATOM   935   C  CA    . LYS A 1 113 ? 104.686 137.511 99.783  1.00 58.38 ?  113 LYS A CA    1 
ATOM   936   C  C     . LYS A 1 113 ? 106.068 138.016 99.399  1.00 59.83 ?  113 LYS A C     1 
ATOM   937   O  O     . LYS A 1 113 ? 106.886 138.352 100.259 1.00 60.10 ?  113 LYS A O     1 
ATOM   938   C  CB    . LYS A 1 113 ? 103.666 138.651 99.689  1.00 58.07 ?  113 LYS A CB    1 
ATOM   939   C  CG    . LYS A 1 113 ? 102.236 138.189 99.460  1.00 58.53 ?  113 LYS A CG    1 
ATOM   940   C  CD    . LYS A 1 113 ? 102.035 137.696 98.038  1.00 59.74 ?  113 LYS A CD    1 
ATOM   941   C  CE    . LYS A 1 113 ? 100.580 137.348 97.776  1.00 58.90 ?  113 LYS A CE    1 
ATOM   942   N  NZ    . LYS A 1 113 ? 100.373 136.813 96.402  1.00 60.00 1  113 LYS A NZ    1 
ATOM   943   N  N     . ILE A 1 114 ? 106.321 138.063 98.094  1.00 53.46 ?  114 ILE A N     1 
ATOM   944   C  CA    . ILE A 1 114 ? 107.609 138.472 97.549  1.00 51.44 ?  114 ILE A CA    1 
ATOM   945   C  C     . ILE A 1 114 ? 107.457 139.876 96.984  1.00 49.75 ?  114 ILE A C     1 
ATOM   946   O  O     . ILE A 1 114 ? 106.669 140.100 96.058  1.00 52.17 ?  114 ILE A O     1 
ATOM   947   C  CB    . ILE A 1 114 ? 108.106 137.492 96.476  1.00 51.20 ?  114 ILE A CB    1 
ATOM   948   C  CG1   . ILE A 1 114 ? 108.614 136.206 97.129  1.00 50.03 ?  114 ILE A CG1   1 
ATOM   949   C  CG2   . ILE A 1 114 ? 109.198 138.127 95.634  1.00 48.71 ?  114 ILE A CG2   1 
ATOM   950   C  CD1   . ILE A 1 114 ? 108.612 135.015 96.204  1.00 50.18 ?  114 ILE A CD1   1 
ATOM   951   N  N     . LEU A 1 115 ? 108.208 140.822 97.546  1.00 46.17 ?  115 LEU A N     1 
ATOM   952   C  CA    . LEU A 1 115 ? 108.172 142.201 97.079  1.00 46.36 ?  115 LEU A CA    1 
ATOM   953   C  C     . LEU A 1 115 ? 109.226 142.497 96.025  1.00 47.43 ?  115 LEU A C     1 
ATOM   954   O  O     . LEU A 1 115 ? 109.016 143.375 95.180  1.00 49.19 ?  115 LEU A O     1 
ATOM   955   C  CB    . LEU A 1 115 ? 108.353 143.161 98.257  1.00 47.39 ?  115 LEU A CB    1 
ATOM   956   C  CG    . LEU A 1 115 ? 107.231 143.178 99.294  1.00 48.80 ?  115 LEU A CG    1 
ATOM   957   C  CD1   . LEU A 1 115 ? 107.748 143.698 100.622 1.00 46.26 ?  115 LEU A CD1   1 
ATOM   958   C  CD2   . LEU A 1 115 ? 106.063 144.017 98.803  1.00 45.93 ?  115 LEU A CD2   1 
ATOM   959   N  N     . GLU A 1 116 ? 110.350 141.785 96.048  1.00 45.75 ?  116 GLU A N     1 
ATOM   960   C  CA    . GLU A 1 116 ? 111.472 142.056 95.162  1.00 42.66 ?  116 GLU A CA    1 
ATOM   961   C  C     . GLU A 1 116 ? 111.740 140.855 94.269  1.00 42.32 ?  116 GLU A C     1 
ATOM   962   O  O     . GLU A 1 116 ? 111.873 139.729 94.758  1.00 46.46 ?  116 GLU A O     1 
ATOM   963   C  CB    . GLU A 1 116 ? 112.734 142.391 95.960  1.00 43.84 ?  116 GLU A CB    1 
ATOM   964   C  CG    . GLU A 1 116 ? 113.084 143.864 95.981  1.00 44.60 ?  116 GLU A CG    1 
ATOM   965   C  CD    . GLU A 1 116 ? 114.337 144.149 96.783  1.00 43.95 ?  116 GLU A CD    1 
ATOM   966   O  OE1   . GLU A 1 116 ? 114.868 143.210 97.411  1.00 42.41 ?  116 GLU A OE1   1 
ATOM   967   O  OE2   . GLU A 1 116 ? 114.792 145.312 96.783  1.00 46.49 -1 116 GLU A OE2   1 
ATOM   968   N  N     . ARG A 1 117 ? 111.821 141.101 92.965  1.00 41.40 ?  117 ARG A N     1 
ATOM   969   C  CA    . ARG A 1 117 ? 112.358 140.122 92.037  1.00 42.35 ?  117 ARG A CA    1 
ATOM   970   C  C     . ARG A 1 117 ? 113.877 140.262 91.985  1.00 42.07 ?  117 ARG A C     1 
ATOM   971   O  O     . ARG A 1 117 ? 114.474 141.089 92.677  1.00 45.43 ?  117 ARG A O     1 
ATOM   972   C  CB    . ARG A 1 117 ? 111.734 140.298 90.656  1.00 42.96 ?  117 ARG A CB    1 
ATOM   973   C  CG    . ARG A 1 117 ? 110.221 140.145 90.628  1.00 43.74 ?  117 ARG A CG    1 
ATOM   974   C  CD    . ARG A 1 117 ? 109.735 139.705 89.259  1.00 46.22 ?  117 ARG A CD    1 
ATOM   975   N  NE    . ARG A 1 117 ? 109.623 138.255 89.156  1.00 47.84 ?  117 ARG A NE    1 
ATOM   976   C  CZ    . ARG A 1 117 ? 108.476 137.591 89.144  1.00 44.68 ?  117 ARG A CZ    1 
ATOM   977   N  NH1   . ARG A 1 117 ? 107.314 138.217 89.231  1.00 45.48 1  117 ARG A NH1   1 
ATOM   978   N  NH2   . ARG A 1 117 ? 108.495 136.265 89.039  1.00 45.28 ?  117 ARG A NH2   1 
ATOM   979   N  N     . TYR A 1 118 ? 114.520 139.437 91.157  1.00 35.82 ?  118 TYR A N     1 
ATOM   980   C  CA    . TYR A 1 118 ? 115.960 139.579 90.968  1.00 33.09 ?  118 TYR A CA    1 
ATOM   981   C  C     . TYR A 1 118 ? 116.297 140.921 90.333  1.00 35.83 ?  118 TYR A C     1 
ATOM   982   O  O     . TYR A 1 118 ? 117.237 141.603 90.759  1.00 36.46 ?  118 TYR A O     1 
ATOM   983   C  CB    . TYR A 1 118 ? 116.497 138.430 90.119  1.00 33.04 ?  118 TYR A CB    1 
ATOM   984   C  CG    . TYR A 1 118 ? 117.993 138.255 90.214  1.00 34.61 ?  118 TYR A CG    1 
ATOM   985   C  CD1   . TYR A 1 118 ? 118.633 138.251 91.445  1.00 34.13 ?  118 TYR A CD1   1 
ATOM   986   C  CD2   . TYR A 1 118 ? 118.767 138.100 89.075  1.00 32.57 ?  118 TYR A CD2   1 
ATOM   987   C  CE1   . TYR A 1 118 ? 119.999 138.091 91.537  1.00 32.21 ?  118 TYR A CE1   1 
ATOM   988   C  CE2   . TYR A 1 118 ? 120.134 137.938 89.156  1.00 28.54 ?  118 TYR A CE2   1 
ATOM   989   C  CZ    . TYR A 1 118 ? 120.745 137.934 90.390  1.00 33.42 ?  118 TYR A CZ    1 
ATOM   990   O  OH    . TYR A 1 118 ? 122.107 137.777 90.474  1.00 41.14 ?  118 TYR A OH    1 
ATOM   991   N  N     . GLU A 1 119 ? 115.525 141.322 89.321  1.00 38.05 ?  119 GLU A N     1 
ATOM   992   C  CA    . GLU A 1 119 ? 115.769 142.601 88.666  1.00 33.51 ?  119 GLU A CA    1 
ATOM   993   C  C     . GLU A 1 119 ? 115.517 143.766 89.615  1.00 34.98 ?  119 GLU A C     1 
ATOM   994   O  O     . GLU A 1 119 ? 116.246 144.761 89.585  1.00 41.26 ?  119 GLU A O     1 
ATOM   995   C  CB    . GLU A 1 119 ? 114.901 142.722 87.415  1.00 34.53 ?  119 GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 119 ? 115.287 141.766 86.298  1.00 33.42 ?  119 GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 119 ? 114.535 140.451 86.366  1.00 38.33 ?  119 GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 119 ? 114.156 140.034 87.481  1.00 40.04 ?  119 GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 119 ? 114.324 139.833 85.302  1.00 39.80 -1 119 GLU A OE2   1 
ATOM   1000  N  N     . ASP A 1 120 ? 114.496 143.661 90.470  1.00 38.34 ?  120 ASP A N     1 
ATOM   1001  C  CA    . ASP A 1 120 ? 114.220 144.729 91.427  1.00 35.32 ?  120 ASP A CA    1 
ATOM   1002  C  C     . ASP A 1 120 ? 115.363 144.888 92.422  1.00 36.45 ?  120 ASP A C     1 
ATOM   1003  O  O     . ASP A 1 120 ? 115.813 146.008 92.693  1.00 37.89 ?  120 ASP A O     1 
ATOM   1004  C  CB    . ASP A 1 120 ? 112.910 144.454 92.164  1.00 39.27 ?  120 ASP A CB    1 
ATOM   1005  C  CG    . ASP A 1 120 ? 111.747 144.251 91.224  1.00 44.42 ?  120 ASP A CG    1 
ATOM   1006  O  OD1   . ASP A 1 120 ? 111.640 145.011 90.241  1.00 42.64 ?  120 ASP A OD1   1 
ATOM   1007  O  OD2   . ASP A 1 120 ? 110.936 143.333 91.468  1.00 48.92 -1 120 ASP A OD2   1 
ATOM   1008  N  N     . ARG A 1 121 ? 115.838 143.774 92.983  1.00 35.02 ?  121 ARG A N     1 
ATOM   1009  C  CA    . ARG A 1 121 ? 116.944 143.840 93.931  1.00 32.20 ?  121 ARG A CA    1 
ATOM   1010  C  C     . ARG A 1 121 ? 118.202 144.376 93.264  1.00 33.06 ?  121 ARG A C     1 
ATOM   1011  O  O     . ARG A 1 121 ? 118.918 145.201 93.843  1.00 38.75 ?  121 ARG A O     1 
ATOM   1012  C  CB    . ARG A 1 121 ? 117.200 142.459 94.535  1.00 30.88 ?  121 ARG A CB    1 
ATOM   1013  C  CG    . ARG A 1 121 ? 118.436 142.380 95.417  1.00 30.04 ?  121 ARG A CG    1 
ATOM   1014  C  CD    . ARG A 1 121 ? 118.059 142.385 96.889  1.00 29.75 ?  121 ARG A CD    1 
ATOM   1015  N  NE    . ARG A 1 121 ? 117.489 143.661 97.306  1.00 37.01 ?  121 ARG A NE    1 
ATOM   1016  C  CZ    . ARG A 1 121 ? 118.169 144.627 97.908  1.00 36.31 ?  121 ARG A CZ    1 
ATOM   1017  N  NH1   . ARG A 1 121 ? 119.452 144.493 98.199  1.00 34.61 1  121 ARG A NH1   1 
ATOM   1018  N  NH2   . ARG A 1 121 ? 117.544 145.756 98.231  1.00 33.20 ?  121 ARG A NH2   1 
ATOM   1019  N  N     . ILE A 1 122 ? 118.483 143.924 92.040  1.00 30.77 ?  122 ILE A N     1 
ATOM   1020  C  CA    . ILE A 1 122 ? 119.667 144.396 91.330  1.00 28.80 ?  122 ILE A CA    1 
ATOM   1021  C  C     . ILE A 1 122 ? 119.563 145.889 91.043  1.00 30.77 ?  122 ILE A C     1 
ATOM   1022  O  O     . ILE A 1 122 ? 120.538 146.630 91.203  1.00 34.25 ?  122 ILE A O     1 
ATOM   1023  C  CB    . ILE A 1 122 ? 119.874 143.573 90.045  1.00 30.30 ?  122 ILE A CB    1 
ATOM   1024  C  CG1   . ILE A 1 122 ? 120.514 142.227 90.387  1.00 26.40 ?  122 ILE A CG1   1 
ATOM   1025  C  CG2   . ILE A 1 122 ? 120.725 144.336 89.039  1.00 28.94 ?  122 ILE A CG2   1 
ATOM   1026  C  CD1   . ILE A 1 122 ? 120.881 141.402 89.188  1.00 28.85 ?  122 ILE A CD1   1 
ATOM   1027  N  N     . SER A 1 123 ? 118.383 146.356 90.627  1.00 31.33 ?  123 SER A N     1 
ATOM   1028  C  CA    . SER A 1 123 ? 118.194 147.779 90.365  1.00 32.29 ?  123 SER A CA    1 
ATOM   1029  C  C     . SER A 1 123 ? 118.373 148.602 91.633  1.00 30.43 ?  123 SER A C     1 
ATOM   1030  O  O     . SER A 1 123 ? 118.985 149.675 91.603  1.00 32.18 ?  123 SER A O     1 
ATOM   1031  C  CB    . SER A 1 123 ? 116.809 148.026 89.770  1.00 28.37 ?  123 SER A CB    1 
ATOM   1032  O  OG    . SER A 1 123 ? 116.493 147.059 88.790  1.00 32.84 ?  123 SER A OG    1 
ATOM   1033  N  N     . ILE A 1 124 ? 117.838 148.120 92.756  1.00 30.02 ?  124 ILE A N     1 
ATOM   1034  C  CA    . ILE A 1 124 ? 117.975 148.853 94.010  1.00 32.25 ?  124 ILE A CA    1 
ATOM   1035  C  C     . ILE A 1 124 ? 119.436 148.921 94.435  1.00 32.94 ?  124 ILE A C     1 
ATOM   1036  O  O     . ILE A 1 124 ? 119.926 149.977 94.856  1.00 38.22 ?  124 ILE A O     1 
ATOM   1037  C  CB    . ILE A 1 124 ? 117.087 148.218 95.094  1.00 36.78 ?  124 ILE A CB    1 
ATOM   1038  C  CG1   . ILE A 1 124 ? 115.619 148.551 94.826  1.00 37.74 ?  124 ILE A CG1   1 
ATOM   1039  C  CG2   . ILE A 1 124 ? 117.500 148.691 96.479  1.00 29.38 ?  124 ILE A CG2   1 
ATOM   1040  C  CD1   . ILE A 1 124 ? 115.366 150.019 94.553  1.00 32.41 ?  124 ILE A CD1   1 
ATOM   1041  N  N     . VAL A 1 125 ? 120.160 147.804 94.319  1.00 30.55 ?  125 VAL A N     1 
ATOM   1042  C  CA    . VAL A 1 125 ? 121.571 147.797 94.693  1.00 29.88 ?  125 VAL A CA    1 
ATOM   1043  C  C     . VAL A 1 125 ? 122.371 148.713 93.773  1.00 24.99 ?  125 VAL A C     1 
ATOM   1044  O  O     . VAL A 1 125 ? 123.287 149.412 94.216  1.00 32.24 ?  125 VAL A O     1 
ATOM   1045  C  CB    . VAL A 1 125 ? 122.121 146.357 94.691  1.00 30.99 ?  125 VAL A CB    1 
ATOM   1046  C  CG1   . VAL A 1 125 ? 123.604 146.354 94.992  1.00 30.65 ?  125 VAL A CG1   1 
ATOM   1047  C  CG2   . VAL A 1 125 ? 121.389 145.516 95.717  1.00 25.85 ?  125 VAL A CG2   1 
ATOM   1048  N  N     . ALA A 1 126 ? 122.034 148.729 92.481  1.00 23.57 ?  126 ALA A N     1 
ATOM   1049  C  CA    . ALA A 1 126 ? 122.720 149.612 91.541  1.00 22.17 ?  126 ALA A CA    1 
ATOM   1050  C  C     . ALA A 1 126 ? 122.460 151.079 91.859  1.00 29.36 ?  126 ALA A C     1 
ATOM   1051  O  O     . ALA A 1 126 ? 123.381 151.904 91.810  1.00 33.76 ?  126 ALA A O     1 
ATOM   1052  C  CB    . ALA A 1 126 ? 122.283 149.292 90.114  1.00 29.36 ?  126 ALA A CB    1 
ATOM   1053  N  N     . LEU A 1 127 ? 121.211 151.424 92.175  1.00 31.34 ?  127 LEU A N     1 
ATOM   1054  C  CA    . LEU A 1 127 ? 120.888 152.802 92.529  1.00 27.26 ?  127 LEU A CA    1 
ATOM   1055  C  C     . LEU A 1 127 ? 121.596 153.216 93.811  1.00 30.16 ?  127 LEU A C     1 
ATOM   1056  O  O     . LEU A 1 127 ? 122.042 154.362 93.941  1.00 36.11 ?  127 LEU A O     1 
ATOM   1057  C  CB    . LEU A 1 127 ? 119.375 152.967 92.668  1.00 32.59 ?  127 LEU A CB    1 
ATOM   1058  C  CG    . LEU A 1 127 ? 118.563 152.866 91.377  1.00 30.20 ?  127 LEU A CG    1 
ATOM   1059  C  CD1   . LEU A 1 127 ? 117.113 152.535 91.683  1.00 35.03 ?  127 LEU A CD1   1 
ATOM   1060  C  CD2   . LEU A 1 127 ? 118.663 154.150 90.572  1.00 31.61 ?  127 LEU A CD2   1 
ATOM   1061  N  N     . PHE A 1 128 ? 121.701 152.299 94.773  1.00 29.65 ?  128 PHE A N     1 
ATOM   1062  C  CA    . PHE A 1 128 ? 122.465 152.587 95.980  1.00 27.44 ?  128 PHE A CA    1 
ATOM   1063  C  C     . PHE A 1 128 ? 123.943 152.788 95.663  1.00 27.67 ?  128 PHE A C     1 
ATOM   1064  O  O     . PHE A 1 128 ? 124.586 153.688 96.217  1.00 39.06 ?  128 PHE A O     1 
ATOM   1065  C  CB    . PHE A 1 128 ? 122.281 151.459 96.995  1.00 27.29 ?  128 PHE A CB    1 
ATOM   1066  C  CG    . PHE A 1 128 ? 123.188 151.563 98.183  1.00 32.64 ?  128 PHE A CG    1 
ATOM   1067  C  CD1   . PHE A 1 128 ? 124.318 150.770 98.280  1.00 28.84 ?  128 PHE A CD1   1 
ATOM   1068  C  CD2   . PHE A 1 128 ? 122.906 152.449 99.208  1.00 32.00 ?  128 PHE A CD2   1 
ATOM   1069  C  CE1   . PHE A 1 128 ? 125.153 150.867 99.370  1.00 31.85 ?  128 PHE A CE1   1 
ATOM   1070  C  CE2   . PHE A 1 128 ? 123.738 152.547 100.304 1.00 35.22 ?  128 PHE A CE2   1 
ATOM   1071  C  CZ    . PHE A 1 128 ? 124.862 151.754 100.385 1.00 33.47 ?  128 PHE A CZ    1 
ATOM   1072  N  N     . PHE A 1 129 ? 124.496 151.955 94.779  1.00 24.44 ?  129 PHE A N     1 
ATOM   1073  C  CA    . PHE A 1 129 ? 125.906 152.061 94.420  1.00 22.14 ?  129 PHE A CA    1 
ATOM   1074  C  C     . PHE A 1 129 ? 126.213 153.389 93.740  1.00 28.86 ?  129 PHE A C     1 
ATOM   1075  O  O     . PHE A 1 129 ? 127.215 154.041 94.053  1.00 28.00 ?  129 PHE A O     1 
ATOM   1076  C  CB    . PHE A 1 129 ? 126.300 150.909 93.498  1.00 22.02 ?  129 PHE A CB    1 
ATOM   1077  C  CG    . PHE A 1 129 ? 126.554 149.614 94.205  1.00 23.96 ?  129 PHE A CG    1 
ATOM   1078  C  CD1   . PHE A 1 129 ? 126.716 149.571 95.577  1.00 24.20 ?  129 PHE A CD1   1 
ATOM   1079  C  CD2   . PHE A 1 129 ? 126.642 148.434 93.487  1.00 22.46 ?  129 PHE A CD2   1 
ATOM   1080  C  CE1   . PHE A 1 129 ? 126.952 148.374 96.218  1.00 24.48 ?  129 PHE A CE1   1 
ATOM   1081  C  CE2   . PHE A 1 129 ? 126.882 147.236 94.125  1.00 24.48 ?  129 PHE A CE2   1 
ATOM   1082  C  CZ    . PHE A 1 129 ? 127.038 147.206 95.492  1.00 26.83 ?  129 PHE A CZ    1 
ATOM   1083  N  N     . ALA A 1 130 ? 125.362 153.802 92.798  1.00 30.83 ?  130 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 130 ? 125.684 154.954 91.962  1.00 31.96 ?  130 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 130 ? 125.629 156.263 92.738  1.00 40.33 ?  130 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 130 ? 126.312 157.226 92.368  1.00 42.45 ?  130 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 130 ? 124.742 155.008 90.765  1.00 32.00 ?  130 ALA A CB    1 
ATOM   1088  N  N     . ASN A 1 131 ? 124.823 156.321 93.800  1.00 40.41 ?  131 ASN A N     1 
ATOM   1089  C  CA    . ASN A 1 131 ? 124.739 157.497 94.670  1.00 38.34 ?  131 ASN A CA    1 
ATOM   1090  C  C     . ASN A 1 131 ? 124.321 158.747 93.895  1.00 41.21 ?  131 ASN A C     1 
ATOM   1091  O  O     . ASN A 1 131 ? 124.830 159.844 94.132  1.00 46.33 ?  131 ASN A O     1 
ATOM   1092  C  CB    . ASN A 1 131 ? 126.060 157.731 95.406  1.00 34.85 ?  131 ASN A CB    1 
ATOM   1093  C  CG    . ASN A 1 131 ? 125.868 158.405 96.749  1.00 43.68 ?  131 ASN A CG    1 
ATOM   1094  O  OD1   . ASN A 1 131 ? 124.823 158.264 97.383  1.00 43.08 ?  131 ASN A OD1   1 
ATOM   1095  N  ND2   . ASN A 1 131 ? 126.881 159.142 97.191  1.00 44.19 ?  131 ASN A ND2   1 
ATOM   1096  N  N     . GLY A 1 132 ? 123.386 158.584 92.961  1.00 39.55 ?  132 GLY A N     1 
ATOM   1097  C  CA    . GLY A 1 132 ? 122.803 159.700 92.244  1.00 39.30 ?  132 GLY A CA    1 
ATOM   1098  C  C     . GLY A 1 132 ? 123.116 159.761 90.764  1.00 43.26 ?  132 GLY A C     1 
ATOM   1099  O  O     . GLY A 1 132 ? 122.552 160.617 90.070  1.00 45.37 ?  132 GLY A O     1 
ATOM   1100  N  N     . ASP A 1 133 ? 123.986 158.893 90.254  1.00 43.29 ?  133 ASP A N     1 
ATOM   1101  C  CA    . ASP A 1 133 ? 124.364 158.895 88.844  1.00 41.14 ?  133 ASP A CA    1 
ATOM   1102  C  C     . ASP A 1 133 ? 123.541 157.841 88.111  1.00 42.99 ?  133 ASP A C     1 
ATOM   1103  O  O     . ASP A 1 133 ? 123.734 156.640 88.319  1.00 47.06 ?  133 ASP A O     1 
ATOM   1104  C  CB    . ASP A 1 133 ? 125.860 158.635 88.686  1.00 43.53 ?  133 ASP A CB    1 
ATOM   1105  C  CG    . ASP A 1 133 ? 126.394 159.085 87.341  1.00 46.21 ?  133 ASP A CG    1 
ATOM   1106  O  OD1   . ASP A 1 133 ? 125.579 159.411 86.452  1.00 48.02 ?  133 ASP A OD1   1 
ATOM   1107  O  OD2   . ASP A 1 133 ? 127.631 159.110 87.171  1.00 46.08 -1 133 ASP A OD2   1 
ATOM   1108  N  N     . THR A 1 134 ? 122.625 158.291 87.251  1.00 45.97 ?  134 THR A N     1 
ATOM   1109  C  CA    . THR A 1 134 ? 121.759 157.354 86.541  1.00 41.92 ?  134 THR A CA    1 
ATOM   1110  C  C     . THR A 1 134 ? 122.550 156.478 85.573  1.00 43.76 ?  134 THR A C     1 
ATOM   1111  O  O     . THR A 1 134 ? 122.275 155.280 85.451  1.00 44.74 ?  134 THR A O     1 
ATOM   1112  C  CB    . THR A 1 134 ? 120.649 158.111 85.807  1.00 45.87 ?  134 THR A CB    1 
ATOM   1113  O  OG1   . THR A 1 134 ? 119.932 157.209 84.954  1.00 48.16 ?  134 THR A OG1   1 
ATOM   1114  C  CG2   . THR A 1 134 ? 121.219 159.258 84.979  1.00 46.73 ?  134 THR A CG2   1 
ATOM   1115  N  N     . GLU A 1 135 ? 123.533 157.055 84.876  1.00 42.46 ?  135 GLU A N     1 
ATOM   1116  C  CA    . GLU A 1 135 ? 124.350 156.258 83.965  1.00 43.05 ?  135 GLU A CA    1 
ATOM   1117  C  C     . GLU A 1 135 ? 125.196 155.244 84.725  1.00 43.92 ?  135 GLU A C     1 
ATOM   1118  O  O     . GLU A 1 135 ? 125.329 154.092 84.296  1.00 43.52 ?  135 GLU A O     1 
ATOM   1119  C  CB    . GLU A 1 135 ? 125.235 157.171 83.118  1.00 43.57 ?  135 GLU A CB    1 
ATOM   1120  C  CG    . GLU A 1 135 ? 124.501 157.864 81.981  1.00 44.06 ?  135 GLU A CG    1 
ATOM   1121  C  CD    . GLU A 1 135 ? 123.296 157.080 81.498  1.00 47.86 ?  135 GLU A CD    1 
ATOM   1122  O  OE1   . GLU A 1 135 ? 123.480 156.136 80.702  1.00 47.89 ?  135 GLU A OE1   1 
ATOM   1123  O  OE2   . GLU A 1 135 ? 122.163 157.410 81.909  1.00 48.27 -1 135 GLU A OE2   1 
ATOM   1124  N  N     . LYS A 1 136 ? 125.771 155.652 85.857  1.00 35.81 ?  136 LYS A N     1 
ATOM   1125  C  CA    . LYS A 1 136 ? 126.514 154.713 86.690  1.00 32.22 ?  136 LYS A CA    1 
ATOM   1126  C  C     . LYS A 1 136 ? 125.597 153.625 87.235  1.00 33.99 ?  136 LYS A C     1 
ATOM   1127  O  O     . LYS A 1 136 ? 125.995 152.458 87.335  1.00 39.30 ?  136 LYS A O     1 
ATOM   1128  C  CB    . LYS A 1 136 ? 127.204 155.464 87.828  1.00 38.68 ?  136 LYS A CB    1 
ATOM   1129  C  CG    . LYS A 1 136 ? 128.195 154.635 88.621  1.00 37.05 ?  136 LYS A CG    1 
ATOM   1130  C  CD    . LYS A 1 136 ? 129.566 154.636 87.972  1.00 36.18 ?  136 LYS A CD    1 
ATOM   1131  C  CE    . LYS A 1 136 ? 130.625 154.133 88.938  1.00 38.80 ?  136 LYS A CE    1 
ATOM   1132  N  NZ    . LYS A 1 136 ? 132.000 154.324 88.403  1.00 39.04 1  136 LYS A NZ    1 
ATOM   1133  N  N     . ALA A 1 137 ? 124.365 153.990 87.596  1.00 33.83 ?  137 ALA A N     1 
ATOM   1134  C  CA    . ALA A 1 137 ? 123.403 152.995 88.059  1.00 30.50 ?  137 ALA A CA    1 
ATOM   1135  C  C     . ALA A 1 137 ? 123.076 151.992 86.961  1.00 31.42 ?  137 ALA A C     1 
ATOM   1136  O  O     . ALA A 1 137 ? 122.962 150.791 87.224  1.00 33.06 ?  137 ALA A O     1 
ATOM   1137  C  CB    . ALA A 1 137 ? 122.131 153.682 88.554  1.00 29.01 ?  137 ALA A CB    1 
ATOM   1138  N  N     . LYS A 1 138 ? 122.918 152.466 85.723  1.00 35.80 ?  138 LYS A N     1 
ATOM   1139  C  CA    . LYS A 1 138 ? 122.663 151.553 84.614  1.00 34.99 ?  138 LYS A CA    1 
ATOM   1140  C  C     . LYS A 1 138 ? 123.869 150.661 84.345  1.00 31.55 ?  138 LYS A C     1 
ATOM   1141  O  O     . LYS A 1 138 ? 123.713 149.486 83.996  1.00 33.93 ?  138 LYS A O     1 
ATOM   1142  C  CB    . LYS A 1 138 ? 122.282 152.339 83.360  1.00 39.13 ?  138 LYS A CB    1 
ATOM   1143  C  CG    . LYS A 1 138 ? 120.889 152.943 83.412  1.00 39.27 ?  138 LYS A CG    1 
ATOM   1144  C  CD    . LYS A 1 138 ? 120.803 154.205 82.571  1.00 37.78 ?  138 LYS A CD    1 
ATOM   1145  C  CE    . LYS A 1 138 ? 120.462 153.880 81.127  1.00 37.18 ?  138 LYS A CE    1 
ATOM   1146  N  NZ    . LYS A 1 138 ? 120.671 155.050 80.233  1.00 39.98 1  138 LYS A NZ    1 
ATOM   1147  N  N     . GLU A 1 139 ? 125.081 151.202 84.500  1.00 36.22 ?  139 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 139 ? 126.277 150.375 84.366  1.00 32.63 ?  139 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 139 ? 126.313 149.283 85.427  1.00 32.19 ?  139 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 139 ? 126.643 148.129 85.131  1.00 40.53 ?  139 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 139 ? 127.532 151.242 84.453  1.00 33.71 ?  139 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 139 ? 127.706 152.211 83.300  1.00 36.98 ?  139 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 139 ? 128.966 153.042 83.428  1.00 45.18 ?  139 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 139 ? 130.009 152.482 83.825  1.00 43.35 ?  139 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 139 ? 128.915 154.254 83.131  1.00 41.43 -1 139 GLU A OE2   1 
ATOM   1156  N  N     . TYR A 1 140 ? 125.972 149.627 86.671  1.00 23.52 ?  140 TYR A N     1 
ATOM   1157  C  CA    . TYR A 1 140 ? 125.917 148.624 87.730  1.00 27.69 ?  140 TYR A CA    1 
ATOM   1158  C  C     . TYR A 1 140 ? 124.840 147.584 87.451  1.00 28.10 ?  140 TYR A C     1 
ATOM   1159  O  O     . TYR A 1 140 ? 125.029 146.392 87.721  1.00 33.30 ?  140 TYR A O     1 
ATOM   1160  C  CB    . TYR A 1 140 ? 125.666 149.294 89.079  1.00 28.73 ?  140 TYR A CB    1 
ATOM   1161  C  CG    . TYR A 1 140 ? 126.881 149.939 89.696  1.00 30.16 ?  140 TYR A CG    1 
ATOM   1162  C  CD1   . TYR A 1 140 ? 128.034 149.207 89.937  1.00 28.80 ?  140 TYR A CD1   1 
ATOM   1163  C  CD2   . TYR A 1 140 ? 126.871 151.279 90.049  1.00 30.41 ?  140 TYR A CD2   1 
ATOM   1164  C  CE1   . TYR A 1 140 ? 129.143 149.794 90.505  1.00 29.52 ?  140 TYR A CE1   1 
ATOM   1165  C  CE2   . TYR A 1 140 ? 127.973 151.874 90.617  1.00 30.02 ?  140 TYR A CE2   1 
ATOM   1166  C  CZ    . TYR A 1 140 ? 129.106 151.129 90.843  1.00 25.73 ?  140 TYR A CZ    1 
ATOM   1167  O  OH    . TYR A 1 140 ? 130.203 151.727 91.411  1.00 31.30 ?  140 TYR A OH    1 
ATOM   1168  N  N     . VAL A 1 141 ? 123.693 148.023 86.930  1.00 32.97 ?  141 VAL A N     1 
ATOM   1169  C  CA    . VAL A 1 141 ? 122.616 147.095 86.599  1.00 30.44 ?  141 VAL A CA    1 
ATOM   1170  C  C     . VAL A 1 141 ? 123.062 146.129 85.509  1.00 29.32 ?  141 VAL A C     1 
ATOM   1171  O  O     . VAL A 1 141 ? 122.787 144.927 85.580  1.00 34.54 ?  141 VAL A O     1 
ATOM   1172  C  CB    . VAL A 1 141 ? 121.346 147.870 86.199  1.00 32.31 ?  141 VAL A CB    1 
ATOM   1173  C  CG1   . VAL A 1 141 ? 120.670 147.233 85.000  1.00 28.92 ?  141 VAL A CG1   1 
ATOM   1174  C  CG2   . VAL A 1 141 ? 120.382 147.924 87.365  1.00 32.26 ?  141 VAL A CG2   1 
ATOM   1175  N  N     . ASN A 1 142 ? 123.755 146.635 84.488  1.00 27.50 ?  142 ASN A N     1 
ATOM   1176  C  CA    . ASN A 1 142 ? 124.264 145.754 83.443  1.00 29.40 ?  142 ASN A CA    1 
ATOM   1177  C  C     . ASN A 1 142 ? 125.344 144.824 83.978  1.00 29.06 ?  142 ASN A C     1 
ATOM   1178  O  O     . ASN A 1 142 ? 125.471 143.688 83.508  1.00 36.97 ?  142 ASN A O     1 
ATOM   1179  C  CB    . ASN A 1 142 ? 124.803 146.578 82.276  1.00 29.77 ?  142 ASN A CB    1 
ATOM   1180  C  CG    . ASN A 1 142 ? 123.700 147.164 81.422  1.00 32.97 ?  142 ASN A CG    1 
ATOM   1181  O  OD1   . ASN A 1 142 ? 122.686 146.514 81.167  1.00 32.44 ?  142 ASN A OD1   1 
ATOM   1182  N  ND2   . ASN A 1 142 ? 123.890 148.399 80.974  1.00 33.88 ?  142 ASN A ND2   1 
ATOM   1183  N  N     . LEU A 1 143 ? 126.128 145.287 84.953  1.00 28.20 ?  143 LEU A N     1 
ATOM   1184  C  CA    . LEU A 1 143 ? 127.150 144.440 85.555  1.00 25.80 ?  143 LEU A CA    1 
ATOM   1185  C  C     . LEU A 1 143 ? 126.532 143.287 86.337  1.00 25.05 ?  143 LEU A C     1 
ATOM   1186  O  O     . LEU A 1 143 ? 126.989 142.144 86.235  1.00 28.27 ?  143 LEU A O     1 
ATOM   1187  C  CB    . LEU A 1 143 ? 128.043 145.282 86.463  1.00 23.48 ?  143 LEU A CB    1 
ATOM   1188  C  CG    . LEU A 1 143 ? 129.424 144.725 86.794  1.00 28.00 ?  143 LEU A CG    1 
ATOM   1189  C  CD1   . LEU A 1 143 ? 130.307 144.767 85.565  1.00 28.70 ?  143 LEU A CD1   1 
ATOM   1190  C  CD2   . LEU A 1 143 ? 130.042 145.515 87.931  1.00 29.39 ?  143 LEU A CD2   1 
ATOM   1191  N  N     . MET A 1 144 ? 125.498 143.571 87.127  1.00 28.78 ?  144 MET A N     1 
ATOM   1192  C  CA    . MET A 1 144 ? 124.900 142.558 87.990  1.00 23.13 ?  144 MET A CA    1 
ATOM   1193  C  C     . MET A 1 144 ? 123.882 141.676 87.279  1.00 25.40 ?  144 MET A C     1 
ATOM   1194  O  O     . MET A 1 144 ? 123.693 140.522 87.682  1.00 29.77 ?  144 MET A O     1 
ATOM   1195  C  CB    . MET A 1 144 ? 124.241 143.222 89.199  1.00 23.68 ?  144 MET A CB    1 
ATOM   1196  C  CG    . MET A 1 144 ? 125.155 144.168 89.948  1.00 26.24 ?  144 MET A CG    1 
ATOM   1197  S  SD    . MET A 1 144 ? 124.600 144.481 91.628  1.00 33.43 ?  144 MET A SD    1 
ATOM   1198  C  CE    . MET A 1 144 ? 124.107 146.193 91.472  1.00 28.66 ?  144 MET A CE    1 
ATOM   1199  N  N     . ILE A 1 145 ? 123.219 142.180 86.241  1.00 29.37 ?  145 ILE A N     1 
ATOM   1200  C  CA    . ILE A 1 145 ? 122.272 141.361 85.495  1.00 28.87 ?  145 ILE A CA    1 
ATOM   1201  C  C     . ILE A 1 145 ? 122.988 140.468 84.484  1.00 31.49 ?  145 ILE A C     1 
ATOM   1202  O  O     . ILE A 1 145 ? 122.480 139.399 84.137  1.00 35.53 ?  145 ILE A O     1 
ATOM   1203  C  CB    . ILE A 1 145 ? 121.206 142.243 84.818  1.00 27.96 ?  145 ILE A CB    1 
ATOM   1204  C  CG1   . ILE A 1 145 ? 119.896 141.467 84.656  1.00 30.70 ?  145 ILE A CG1   1 
ATOM   1205  C  CG2   . ILE A 1 145 ? 121.688 142.767 83.472  1.00 32.52 ?  145 ILE A CG2   1 
ATOM   1206  C  CD1   . ILE A 1 145 ? 119.265 141.045 85.961  1.00 28.51 ?  145 ILE A CD1   1 
ATOM   1207  N  N     . ASN A 1 146 ? 124.164 140.884 84.008  1.00 23.60 ?  146 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 146 ? 125.061 139.964 83.324  1.00 26.02 ?  146 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 146 ? 125.738 139.014 84.297  1.00 25.75 ?  146 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 146 ? 126.410 138.075 83.856  1.00 30.46 ?  146 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 146 ? 126.119 140.735 82.535  1.00 25.53 ?  146 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 146 ? 125.537 141.480 81.352  1.00 30.32 ?  146 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 146 ? 124.421 141.204 80.918  1.00 35.31 ?  146 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 146 ? 126.296 142.432 80.821  1.00 30.38 ?  146 ASN A ND2   1 
ATOM   1215  N  N     . GLN A 1 147 ? 125.579 139.250 85.600  1.00 23.38 ?  147 GLN A N     1 
ATOM   1216  C  CA    . GLN A 1 147 ? 126.151 138.412 86.651  1.00 20.38 ?  147 GLN A CA    1 
ATOM   1217  C  C     . GLN A 1 147 ? 127.671 138.348 86.541  1.00 26.35 ?  147 GLN A C     1 
ATOM   1218  O  O     . GLN A 1 147 ? 128.291 137.333 86.856  1.00 35.68 ?  147 GLN A O     1 
ATOM   1219  C  CB    . GLN A 1 147 ? 125.536 137.011 86.640  1.00 24.70 ?  147 GLN A CB    1 
ATOM   1220  C  CG    . GLN A 1 147 ? 124.101 136.975 87.138  1.00 23.57 ?  147 GLN A CG    1 
ATOM   1221  C  CD    . GLN A 1 147 ? 123.699 135.613 87.657  1.00 26.46 ?  147 GLN A CD    1 
ATOM   1222  O  OE1   . GLN A 1 147 ? 122.983 135.503 88.652  1.00 28.11 ?  147 GLN A OE1   1 
ATOM   1223  N  NE2   . GLN A 1 147 ? 124.159 134.565 86.986  1.00 35.92 ?  147 GLN A NE2   1 
ATOM   1224  N  N     . GLU A 1 148 ? 128.275 139.446 86.084  1.00 25.21 ?  148 GLU A N     1 
ATOM   1225  C  CA    . GLU A 1 148 ? 129.729 139.543 86.065  1.00 22.94 ?  148 GLU A CA    1 
ATOM   1226  C  C     . GLU A 1 148 ? 130.282 139.830 87.453  1.00 24.69 ?  148 GLU A C     1 
ATOM   1227  O  O     . GLU A 1 148 ? 131.328 139.294 87.833  1.00 29.83 ?  148 GLU A O     1 
ATOM   1228  C  CB    . GLU A 1 148 ? 130.169 140.627 85.081  1.00 20.80 ?  148 GLU A CB    1 
ATOM   1229  C  CG    . GLU A 1 148 ? 129.722 140.386 83.652  1.00 24.20 ?  148 GLU A CG    1 
ATOM   1230  C  CD    . GLU A 1 148 ? 129.841 141.624 82.789  1.00 33.09 ?  148 GLU A CD    1 
ATOM   1231  O  OE1   . GLU A 1 148 ? 128.947 142.492 82.865  1.00 36.31 ?  148 GLU A OE1   1 
ATOM   1232  O  OE2   . GLU A 1 148 ? 130.830 141.732 82.034  1.00 36.13 -1 148 GLU A OE2   1 
ATOM   1233  N  N     . TYR A 1 149 ? 129.593 140.665 88.222  1.00 18.43 ?  149 TYR A N     1 
ATOM   1234  C  CA    . TYR A 1 149 ? 129.999 141.006 89.575  1.00 20.58 ?  149 TYR A CA    1 
ATOM   1235  C  C     . TYR A 1 149 ? 128.836 140.767 90.522  1.00 22.59 ?  149 TYR A C     1 
ATOM   1236  O  O     . TYR A 1 149 ? 127.678 141.015 90.175  1.00 30.54 ?  149 TYR A O     1 
ATOM   1237  C  CB    . TYR A 1 149 ? 130.462 142.461 89.667  1.00 22.04 ?  149 TYR A CB    1 
ATOM   1238  C  CG    . TYR A 1 149 ? 130.628 142.964 91.081  1.00 21.96 ?  149 TYR A CG    1 
ATOM   1239  C  CD1   . TYR A 1 149 ? 131.602 142.437 91.917  1.00 17.07 ?  149 TYR A CD1   1 
ATOM   1240  C  CD2   . TYR A 1 149 ? 129.807 143.966 91.582  1.00 19.77 ?  149 TYR A CD2   1 
ATOM   1241  C  CE1   . TYR A 1 149 ? 131.755 142.896 93.211  1.00 22.13 ?  149 TYR A CE1   1 
ATOM   1242  C  CE2   . TYR A 1 149 ? 129.953 144.430 92.871  1.00 17.50 ?  149 TYR A CE2   1 
ATOM   1243  C  CZ    . TYR A 1 149 ? 130.929 143.891 93.682  1.00 19.19 ?  149 TYR A CZ    1 
ATOM   1244  O  OH    . TYR A 1 149 ? 131.077 144.351 94.969  1.00 20.73 ?  149 TYR A OH    1 
ATOM   1245  N  N     . GLN A 1 150 ? 129.151 140.283 91.716  1.00 19.43 ?  150 GLN A N     1 
ATOM   1246  C  CA    . GLN A 1 150 ? 128.152 139.991 92.738  1.00 14.05 ?  150 GLN A CA    1 
ATOM   1247  C  C     . GLN A 1 150 ? 128.587 140.657 94.033  1.00 17.22 ?  150 GLN A C     1 
ATOM   1248  O  O     . GLN A 1 150 ? 129.642 140.288 94.590  1.00 18.47 ?  150 GLN A O     1 
ATOM   1249  C  CB    . GLN A 1 150 ? 127.990 138.484 92.918  1.00 19.49 ?  150 GLN A CB    1 
ATOM   1250  C  CG    . GLN A 1 150 ? 127.138 138.065 94.101  1.00 20.50 ?  150 GLN A CG    1 
ATOM   1251  C  CD    . GLN A 1 150 ? 125.756 138.682 94.074  1.00 17.04 ?  150 GLN A CD    1 
ATOM   1252  O  OE1   . GLN A 1 150 ? 124.947 138.384 93.195  1.00 22.92 ?  150 GLN A OE1   1 
ATOM   1253  N  NE2   . GLN A 1 150 ? 125.476 139.543 95.041  1.00 19.47 ?  150 GLN A NE2   1 
ATOM   1254  N  N     . PRO A 1 151 ? 127.848 141.648 94.525  1.00 24.37 ?  151 PRO A N     1 
ATOM   1255  C  CA    . PRO A 1 151 ? 128.117 142.156 95.871  1.00 10.14 ?  151 PRO A CA    1 
ATOM   1256  C  C     . PRO A 1 151 ? 127.903 141.057 96.898  1.00 13.12 ?  151 PRO A C     1 
ATOM   1257  O  O     . PRO A 1 151 ? 127.109 140.137 96.697  1.00 25.36 ?  151 PRO A O     1 
ATOM   1258  C  CB    . PRO A 1 151 ? 127.099 143.291 96.038  1.00 19.55 ?  151 PRO A CB    1 
ATOM   1259  C  CG    . PRO A 1 151 ? 126.704 143.664 94.648  1.00 19.21 ?  151 PRO A CG    1 
ATOM   1260  C  CD    . PRO A 1 151 ? 126.782 142.402 93.848  1.00 19.61 ?  151 PRO A CD    1 
ATOM   1261  N  N     . SER A 1 152 ? 128.639 141.152 98.002  1.00 23.35 ?  152 SER A N     1 
ATOM   1262  C  CA    . SER A 1 152 ? 128.565 140.136 99.038  1.00 19.59 ?  152 SER A CA    1 
ATOM   1263  C  C     . SER A 1 152 ? 127.144 140.032 99.589  1.00 22.03 ?  152 SER A C     1 
ATOM   1264  O  O     . SER A 1 152 ? 126.285 140.882 99.348  1.00 27.11 ?  152 SER A O     1 
ATOM   1265  C  CB    . SER A 1 152 ? 129.544 140.454 100.164 1.00 19.84 ?  152 SER A CB    1 
ATOM   1266  O  OG    . SER A 1 152 ? 129.190 141.659 100.815 1.00 23.90 ?  152 SER A OG    1 
ATOM   1267  N  N     . THR A 1 153 ? 126.906 138.959 100.341 1.00 26.99 ?  153 THR A N     1 
ATOM   1268  C  CA    . THR A 1 153 ? 125.602 138.760 100.966 1.00 21.18 ?  153 THR A CA    1 
ATOM   1269  C  C     . THR A 1 153 ? 125.139 139.960 101.787 1.00 30.64 ?  153 THR A C     1 
ATOM   1270  O  O     . THR A 1 153 ? 123.972 140.357 101.631 1.00 32.29 ?  153 THR A O     1 
ATOM   1271  C  CB    . THR A 1 153 ? 125.628 137.485 101.823 1.00 26.27 ?  153 THR A CB    1 
ATOM   1272  O  OG1   . THR A 1 153 ? 125.679 136.334 100.971 1.00 31.38 ?  153 THR A OG1   1 
ATOM   1273  C  CG2   . THR A 1 153 ? 124.394 137.402 102.708 1.00 25.56 ?  153 THR A CG2   1 
ATOM   1274  N  N     . PRO A 1 154 ? 125.963 140.586 102.638 1.00 28.10 ?  154 PRO A N     1 
ATOM   1275  C  CA    . PRO A 1 154 ? 125.489 141.806 103.318 1.00 20.25 ?  154 PRO A CA    1 
ATOM   1276  C  C     . PRO A 1 154 ? 125.107 142.915 102.354 1.00 20.45 ?  154 PRO A C     1 
ATOM   1277  O  O     . PRO A 1 154 ? 124.009 143.477 102.461 1.00 28.25 ?  154 PRO A O     1 
ATOM   1278  C  CB    . PRO A 1 154 ? 126.684 142.202 104.196 1.00 22.33 ?  154 PRO A CB    1 
ATOM   1279  C  CG    . PRO A 1 154 ? 127.462 140.968 104.361 1.00 18.21 ?  154 PRO A CG    1 
ATOM   1280  C  CD    . PRO A 1 154 ? 127.307 140.198 103.104 1.00 19.76 ?  154 PRO A CD    1 
ATOM   1281  N  N     . THR A 1 155 ? 125.987 143.242 101.407 1.00 21.90 ?  155 THR A N     1 
ATOM   1282  C  CA    . THR A 1 155 ? 125.697 144.318 100.465 1.00 22.24 ?  155 THR A CA    1 
ATOM   1283  C  C     . THR A 1 155 ? 124.500 143.974 99.587  1.00 24.01 ?  155 THR A C     1 
ATOM   1284  O  O     . THR A 1 155 ? 123.580 144.782 99.432  1.00 25.79 ?  155 THR A O     1 
ATOM   1285  C  CB    . THR A 1 155 ? 126.927 144.608 99.604  1.00 20.44 ?  155 THR A CB    1 
ATOM   1286  O  OG1   . THR A 1 155 ? 128.074 144.771 100.446 1.00 26.23 ?  155 THR A OG1   1 
ATOM   1287  C  CG2   . THR A 1 155 ? 126.717 145.874 98.795  1.00 15.83 ?  155 THR A CG2   1 
ATOM   1288  N  N     . PHE A 1 156 ? 124.491 142.771 99.013  1.00 26.18 ?  156 PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 156 ? 123.410 142.396 98.106  1.00 22.55 ?  156 PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 156 ? 122.069 142.353 98.827  1.00 29.74 ?  156 PHE A C     1 
ATOM   1291  O  O     . PHE A 1 156 ? 121.047 142.784 98.281  1.00 25.60 ?  156 PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 156 ? 123.711 141.048 97.456  1.00 21.93 ?  156 PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 156 ? 122.874 140.761 96.246  1.00 27.63 ?  156 PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 156 ? 122.856 141.639 95.178  1.00 24.70 ?  156 PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 156 ? 122.103 139.613 96.178  1.00 23.84 ?  156 PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 156 ? 122.086 141.379 94.063  1.00 24.94 ?  156 PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 156 ? 121.332 139.347 95.065  1.00 25.17 ?  156 PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 156 ? 121.323 140.232 94.007  1.00 29.02 ?  156 PHE A CZ    1 
ATOM   1299  N  N     . LEU A 1 157 ? 122.050 141.831 100.053 1.00 29.89 ?  157 LEU A N     1 
ATOM   1300  C  CA    . LEU A 1 157 ? 120.799 141.678 100.785 1.00 24.18 ?  157 LEU A CA    1 
ATOM   1301  C  C     . LEU A 1 157 ? 120.296 143.002 101.351 1.00 27.71 ?  157 LEU A C     1 
ATOM   1302  O  O     . LEU A 1 157 ? 119.088 143.263 101.334 1.00 38.07 ?  157 LEU A O     1 
ATOM   1303  C  CB    . LEU A 1 157 ? 120.981 140.654 101.906 1.00 29.60 ?  157 LEU A CB    1 
ATOM   1304  C  CG    . LEU A 1 157 ? 119.888 140.573 102.971 1.00 30.16 ?  157 LEU A CG    1 
ATOM   1305  C  CD1   . LEU A 1 157 ? 118.749 139.694 102.497 1.00 31.34 ?  157 LEU A CD1   1 
ATOM   1306  C  CD2   . LEU A 1 157 ? 120.458 140.051 104.280 1.00 25.42 ?  157 LEU A CD2   1 
ATOM   1307  N  N     . ASN A 1 158 ? 121.196 143.854 101.842 1.00 29.43 ?  158 ASN A N     1 
ATOM   1308  C  CA    . ASN A 1 158 ? 120.796 144.989 102.659 1.00 28.29 ?  158 ASN A CA    1 
ATOM   1309  C  C     . ASN A 1 158 ? 120.866 146.332 101.943 1.00 29.21 ?  158 ASN A C     1 
ATOM   1310  O  O     . ASN A 1 158 ? 120.362 147.320 102.483 1.00 35.75 ?  158 ASN A O     1 
ATOM   1311  C  CB    . ASN A 1 158 ? 121.662 145.051 103.922 1.00 28.05 ?  158 ASN A CB    1 
ATOM   1312  C  CG    . ASN A 1 158 ? 121.448 143.862 104.832 1.00 33.65 ?  158 ASN A CG    1 
ATOM   1313  O  OD1   . ASN A 1 158 ? 120.315 143.459 105.090 1.00 37.04 ?  158 ASN A OD1   1 
ATOM   1314  N  ND2   . ASN A 1 158 ? 122.541 143.288 105.319 1.00 34.74 ?  158 ASN A ND2   1 
ATOM   1315  N  N     . ALA A 1 159 ? 121.471 146.404 100.760 1.00 27.74 ?  159 ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 159 ? 121.609 147.689 100.084 1.00 27.63 ?  159 ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 159 ? 120.240 148.263 99.749  1.00 33.43 ?  159 ALA A C     1 
ATOM   1318  O  O     . ALA A 1 159 ? 119.425 147.611 99.089  1.00 39.61 ?  159 ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 159 ? 122.445 147.543 98.814  1.00 29.21 ?  159 ALA A CB    1 
ATOM   1320  N  N     . GLY A 1 160 ? 119.990 149.486 100.210 1.00 36.32 ?  160 GLY A N     1 
ATOM   1321  C  CA    . GLY A 1 160 ? 118.741 150.161 99.946  1.00 36.92 ?  160 GLY A CA    1 
ATOM   1322  C  C     . GLY A 1 160 ? 117.592 149.789 100.856 1.00 39.04 ?  160 GLY A C     1 
ATOM   1323  O  O     . GLY A 1 160 ? 116.470 150.250 100.620 1.00 44.26 ?  160 GLY A O     1 
ATOM   1324  N  N     . ARG A 1 161 ? 117.826 148.977 101.882 1.00 41.42 ?  161 ARG A N     1 
ATOM   1325  C  CA    . ARG A 1 161 ? 116.774 148.530 102.787 1.00 41.58 ?  161 ARG A CA    1 
ATOM   1326  C  C     . ARG A 1 161 ? 116.896 149.252 104.122 1.00 43.09 ?  161 ARG A C     1 
ATOM   1327  O  O     . ARG A 1 161 ? 117.994 149.356 104.676 1.00 45.61 ?  161 ARG A O     1 
ATOM   1328  C  CB    . ARG A 1 161 ? 116.845 147.018 102.999 1.00 37.99 ?  161 ARG A CB    1 
ATOM   1329  C  CG    . ARG A 1 161 ? 116.497 146.201 101.769 1.00 40.07 ?  161 ARG A CG    1 
ATOM   1330  C  CD    . ARG A 1 161 ? 116.176 144.764 102.141 1.00 39.67 ?  161 ARG A CD    1 
ATOM   1331  N  NE    . ARG A 1 161 ? 116.124 143.898 100.970 1.00 42.62 ?  161 ARG A NE    1 
ATOM   1332  C  CZ    . ARG A 1 161 ? 116.088 142.573 101.020 1.00 43.82 ?  161 ARG A CZ    1 
ATOM   1333  N  NH1   . ARG A 1 161 ? 116.085 141.925 102.174 1.00 39.86 1  161 ARG A NH1   1 
ATOM   1334  N  NH2   . ARG A 1 161 ? 116.056 141.882 99.885  1.00 43.40 ?  161 ARG A NH2   1 
ATOM   1335  N  N     . LYS A 1 162 ? 115.768 149.752 104.632 1.00 48.38 ?  162 LYS A N     1 
ATOM   1336  C  CA    . LYS A 1 162 ? 115.783 150.446 105.917 1.00 50.04 ?  162 LYS A CA    1 
ATOM   1337  C  C     . LYS A 1 162 ? 115.985 149.468 107.070 1.00 49.96 ?  162 LYS A C     1 
ATOM   1338  O  O     . LYS A 1 162 ? 116.785 149.719 107.978 1.00 51.28 ?  162 LYS A O     1 
ATOM   1339  C  CB    . LYS A 1 162 ? 114.490 151.241 106.102 1.00 49.53 ?  162 LYS A CB    1 
ATOM   1340  C  CG    . LYS A 1 162 ? 114.524 152.205 107.278 1.00 48.91 ?  162 LYS A CG    1 
ATOM   1341  C  CD    . LYS A 1 162 ? 114.056 153.596 106.878 1.00 49.75 ?  162 LYS A CD    1 
ATOM   1342  C  CE    . LYS A 1 162 ? 112.669 153.559 106.263 1.00 52.02 ?  162 LYS A CE    1 
ATOM   1343  N  NZ    . LYS A 1 162 ? 112.495 154.607 105.220 1.00 52.03 1  162 LYS A NZ    1 
ATOM   1344  N  N     . ARG A 1 163 ? 115.265 148.348 107.050 1.00 49.65 ?  163 ARG A N     1 
ATOM   1345  C  CA    . ARG A 1 163 ? 115.418 147.305 108.064 1.00 51.16 ?  163 ARG A CA    1 
ATOM   1346  C  C     . ARG A 1 163 ? 116.559 146.403 107.617 1.00 52.31 ?  163 ARG A C     1 
ATOM   1347  O  O     . ARG A 1 163 ? 116.364 145.423 106.896 1.00 53.52 ?  163 ARG A O     1 
ATOM   1348  C  CB    . ARG A 1 163 ? 114.117 146.531 108.244 1.00 53.63 ?  163 ARG A CB    1 
ATOM   1349  C  CG    . ARG A 1 163 ? 113.831 146.091 109.674 1.00 52.96 ?  163 ARG A CG    1 
ATOM   1350  C  CD    . ARG A 1 163 ? 114.790 145.009 110.146 1.00 52.96 ?  163 ARG A CD    1 
ATOM   1351  N  NE    . ARG A 1 163 ? 114.964 143.954 109.155 1.00 53.32 ?  163 ARG A NE    1 
ATOM   1352  C  CZ    . ARG A 1 163 ? 116.069 143.233 109.016 1.00 53.85 ?  163 ARG A CZ    1 
ATOM   1353  N  NH1   . ARG A 1 163 ? 117.123 143.429 109.790 1.00 53.22 1  163 ARG A NH1   1 
ATOM   1354  N  NH2   . ARG A 1 163 ? 116.115 142.293 108.077 1.00 52.27 ?  163 ARG A NH2   1 
ATOM   1355  N  N     . ARG A 1 164 ? 117.772 146.739 108.050 1.00 50.24 ?  164 ARG A N     1 
ATOM   1356  C  CA    . ARG A 1 164 ? 118.962 146.077 107.540 1.00 50.56 ?  164 ARG A CA    1 
ATOM   1357  C  C     . ARG A 1 164 ? 120.064 146.111 108.587 1.00 49.30 ?  164 ARG A C     1 
ATOM   1358  O  O     . ARG A 1 164 ? 120.050 146.926 109.513 1.00 50.46 ?  164 ARG A O     1 
ATOM   1359  C  CB    . ARG A 1 164 ? 119.458 146.740 106.252 1.00 46.90 ?  164 ARG A CB    1 
ATOM   1360  C  CG    . ARG A 1 164 ? 120.212 148.040 106.497 1.00 43.57 ?  164 ARG A CG    1 
ATOM   1361  C  CD    . ARG A 1 164 ? 121.057 148.430 105.298 1.00 46.79 ?  164 ARG A CD    1 
ATOM   1362  N  NE    . ARG A 1 164 ? 121.693 149.733 105.461 1.00 46.54 ?  164 ARG A NE    1 
ATOM   1363  C  CZ    . ARG A 1 164 ? 122.759 149.959 106.215 1.00 49.60 ?  164 ARG A CZ    1 
ATOM   1364  N  NH1   . ARG A 1 164 ? 123.339 148.989 106.902 1.00 48.82 1  164 ARG A NH1   1 
ATOM   1365  N  NH2   . ARG A 1 164 ? 123.258 151.190 106.280 1.00 47.91 ?  164 ARG A NH2   1 
ATOM   1366  N  N     . GLY A 1 165 ? 121.022 145.201 108.426 1.00 43.35 ?  165 GLY A N     1 
ATOM   1367  C  CA    . GLY A 1 165 ? 122.279 145.269 109.137 1.00 42.46 ?  165 GLY A CA    1 
ATOM   1368  C  C     . GLY A 1 165 ? 123.304 146.066 108.354 1.00 45.44 ?  165 GLY A C     1 
ATOM   1369  O  O     . GLY A 1 165 ? 123.010 146.688 107.332 1.00 46.28 ?  165 GLY A O     1 
ATOM   1370  N  N     . GLU A 1 166 ? 124.537 146.039 108.848 1.00 39.87 ?  166 GLU A N     1 
ATOM   1371  C  CA    . GLU A 1 166 ? 125.606 146.729 108.146 1.00 37.89 ?  166 GLU A CA    1 
ATOM   1372  C  C     . GLU A 1 166 ? 125.985 145.974 106.874 1.00 38.58 ?  166 GLU A C     1 
ATOM   1373  O  O     . GLU A 1 166 ? 125.808 144.759 106.759 1.00 36.64 ?  166 GLU A O     1 
ATOM   1374  C  CB    . GLU A 1 166 ? 126.829 146.894 109.049 1.00 35.65 ?  166 GLU A CB    1 
ATOM   1375  C  CG    . GLU A 1 166 ? 126.988 148.290 109.638 1.00 38.87 ?  166 GLU A CG    1 
ATOM   1376  C  CD    . GLU A 1 166 ? 127.124 149.378 108.583 1.00 45.97 ?  166 GLU A CD    1 
ATOM   1377  O  OE1   . GLU A 1 166 ? 127.500 149.066 107.432 1.00 48.15 ?  166 GLU A OE1   1 
ATOM   1378  O  OE2   . GLU A 1 166 ? 126.854 150.554 108.907 1.00 43.24 -1 166 GLU A OE2   1 
ATOM   1379  N  N     . LEU A 1 167 ? 126.514 146.721 105.904 1.00 30.76 ?  167 LEU A N     1 
ATOM   1380  C  CA    . LEU A 1 167 ? 126.944 146.135 104.643 1.00 25.60 ?  167 LEU A CA    1 
ATOM   1381  C  C     . LEU A 1 167 ? 128.284 145.425 104.749 1.00 28.67 ?  167 LEU A C     1 
ATOM   1382  O  O     . LEU A 1 167 ? 128.679 144.735 103.803 1.00 30.69 ?  167 LEU A O     1 
ATOM   1383  C  CB    . LEU A 1 167 ? 127.019 147.214 103.563 1.00 26.21 ?  167 LEU A CB    1 
ATOM   1384  C  CG    . LEU A 1 167 ? 125.703 147.889 103.185 1.00 25.34 ?  167 LEU A CG    1 
ATOM   1385  C  CD1   . LEU A 1 167 ? 125.870 148.671 101.905 1.00 27.51 ?  167 LEU A CD1   1 
ATOM   1386  C  CD2   . LEU A 1 167 ? 124.600 146.863 103.036 1.00 27.01 ?  167 LEU A CD2   1 
ATOM   1387  N  N     . VAL A 1 168 ? 128.987 145.581 105.865 1.00 29.92 ?  168 VAL A N     1 
ATOM   1388  C  CA    . VAL A 1 168 ? 130.237 144.879 106.126 1.00 20.10 ?  168 VAL A CA    1 
ATOM   1389  C  C     . VAL A 1 168 ? 129.960 143.803 107.163 1.00 25.75 ?  168 VAL A C     1 
ATOM   1390  O  O     . VAL A 1 168 ? 129.285 144.059 108.168 1.00 33.49 ?  168 VAL A O     1 
ATOM   1391  C  CB    . VAL A 1 168 ? 131.328 145.847 106.615 1.00 24.69 ?  168 VAL A CB    1 
ATOM   1392  C  CG1   . VAL A 1 168 ? 132.639 145.109 106.828 1.00 29.31 ?  168 VAL A CG1   1 
ATOM   1393  C  CG2   . VAL A 1 168 ? 131.508 146.988 105.627 1.00 27.55 ?  168 VAL A CG2   1 
ATOM   1394  N  N     . SER A 1 169 ? 130.461 142.593 106.917 1.00 26.07 ?  169 SER A N     1 
ATOM   1395  C  CA    . SER A 1 169 ? 130.291 141.497 107.858 1.00 29.38 ?  169 SER A CA    1 
ATOM   1396  C  C     . SER A 1 169 ? 131.594 140.834 108.271 1.00 32.50 ?  169 SER A C     1 
ATOM   1397  O  O     . SER A 1 169 ? 131.557 139.859 109.029 1.00 38.92 ?  169 SER A O     1 
ATOM   1398  C  CB    . SER A 1 169 ? 129.340 140.437 107.290 1.00 30.68 ?  169 SER A CB    1 
ATOM   1399  O  OG    . SER A 1 169 ? 127.992 140.855 107.417 1.00 38.06 ?  169 SER A OG    1 
ATOM   1400  N  N     . CYS A 1 170 ? 132.738 141.317 107.800 1.00 26.32 ?  170 CYS A N     1 
ATOM   1401  C  CA    . CYS A 1 170 ? 134.031 140.842 108.270 1.00 24.16 ?  170 CYS A CA    1 
ATOM   1402  C  C     . CYS A 1 170 ? 134.684 141.956 109.078 1.00 23.58 ?  170 CYS A C     1 
ATOM   1403  O  O     . CYS A 1 170 ? 134.939 143.046 108.554 1.00 26.85 ?  170 CYS A O     1 
ATOM   1404  C  CB    . CYS A 1 170 ? 134.914 140.380 107.107 1.00 30.30 ?  170 CYS A CB    1 
ATOM   1405  S  SG    . CYS A 1 170 ? 135.580 141.657 106.015 1.00 48.74 ?  170 CYS A SG    1 
ATOM   1406  N  N     . PHE A 1 171 ? 134.913 141.692 110.360 1.00 23.10 ?  171 PHE A N     1 
ATOM   1407  C  CA    . PHE A 1 171 ? 135.508 142.656 111.272 1.00 10.69 ?  171 PHE A CA    1 
ATOM   1408  C  C     . PHE A 1 171 ? 136.653 141.992 112.012 1.00 15.01 ?  171 PHE A C     1 
ATOM   1409  O  O     . PHE A 1 171 ? 136.506 140.875 112.518 1.00 22.56 ?  171 PHE A O     1 
ATOM   1410  C  CB    . PHE A 1 171 ? 134.476 143.195 112.267 1.00 15.76 ?  171 PHE A CB    1 
ATOM   1411  C  CG    . PHE A 1 171 ? 133.313 143.880 111.618 1.00 17.29 ?  171 PHE A CG    1 
ATOM   1412  C  CD1   . PHE A 1 171 ? 133.459 145.140 111.069 1.00 19.36 ?  171 PHE A CD1   1 
ATOM   1413  C  CD2   . PHE A 1 171 ? 132.075 143.266 111.557 1.00 15.63 ?  171 PHE A CD2   1 
ATOM   1414  C  CE1   . PHE A 1 171 ? 132.395 145.773 110.467 1.00 14.98 ?  171 PHE A CE1   1 
ATOM   1415  C  CE2   . PHE A 1 171 ? 131.006 143.897 110.959 1.00 16.79 ?  171 PHE A CE2   1 
ATOM   1416  C  CZ    . PHE A 1 171 ? 131.167 145.152 110.414 1.00 16.17 ?  171 PHE A CZ    1 
ATOM   1417  N  N     . LEU A 1 172 ? 137.789 142.676 112.071 1.00 14.71 ?  172 LEU A N     1 
ATOM   1418  C  CA    . LEU A 1 172 ? 138.958 142.199 112.792 1.00 9.06  ?  172 LEU A CA    1 
ATOM   1419  C  C     . LEU A 1 172 ? 139.259 143.173 113.917 1.00 13.65 ?  172 LEU A C     1 
ATOM   1420  O  O     . LEU A 1 172 ? 139.437 144.371 113.672 1.00 16.89 ?  172 LEU A O     1 
ATOM   1421  C  CB    . LEU A 1 172 ? 140.166 142.062 111.864 1.00 14.71 ?  172 LEU A CB    1 
ATOM   1422  C  CG    . LEU A 1 172 ? 140.170 140.906 110.864 1.00 6.10  ?  172 LEU A CG    1 
ATOM   1423  C  CD1   . LEU A 1 172 ? 139.305 141.232 109.658 1.00 8.62  ?  172 LEU A CD1   1 
ATOM   1424  C  CD2   . LEU A 1 172 ? 141.588 140.597 110.436 1.00 13.30 ?  172 LEU A CD2   1 
ATOM   1425  N  N     . LEU A 1 173 ? 139.316 142.665 115.142 1.00 16.08 ?  173 LEU A N     1 
ATOM   1426  C  CA    . LEU A 1 173 ? 139.549 143.485 116.318 1.00 12.47 ?  173 LEU A CA    1 
ATOM   1427  C  C     . LEU A 1 173 ? 140.880 143.127 116.957 1.00 11.97 ?  173 LEU A C     1 
ATOM   1428  O  O     . LEU A 1 173 ? 141.230 141.949 117.073 1.00 16.59 ?  173 LEU A O     1 
ATOM   1429  C  CB    . LEU A 1 173 ? 138.429 143.316 117.346 1.00 16.96 ?  173 LEU A CB    1 
ATOM   1430  C  CG    . LEU A 1 173 ? 136.987 143.497 116.878 1.00 20.16 ?  173 LEU A CG    1 
ATOM   1431  C  CD1   . LEU A 1 173 ? 136.050 143.416 118.070 1.00 19.08 ?  173 LEU A CD1   1 
ATOM   1432  C  CD2   . LEU A 1 173 ? 136.811 144.813 116.139 1.00 16.49 ?  173 LEU A CD2   1 
ATOM   1433  N  N     . GLU A 1 174 ? 141.622 144.150 117.362 1.00 25.98 ?  174 GLU A N     1 
ATOM   1434  C  CA    . GLU A 1 174 ? 142.805 143.972 118.186 1.00 23.68 ?  174 GLU A CA    1 
ATOM   1435  C  C     . GLU A 1 174 ? 142.434 144.178 119.647 1.00 20.40 ?  174 GLU A C     1 
ATOM   1436  O  O     . GLU A 1 174 ? 141.796 145.174 120.001 1.00 29.43 ?  174 GLU A O     1 
ATOM   1437  C  CB    . GLU A 1 174 ? 143.903 144.955 117.778 1.00 26.29 ?  174 GLU A CB    1 
ATOM   1438  C  CG    . GLU A 1 174 ? 144.440 144.745 116.376 1.00 22.14 ?  174 GLU A CG    1 
ATOM   1439  C  CD    . GLU A 1 174 ? 145.750 143.988 116.366 1.00 25.00 ?  174 GLU A CD    1 
ATOM   1440  O  OE1   . GLU A 1 174 ? 146.299 143.733 117.457 1.00 28.05 ?  174 GLU A OE1   1 
ATOM   1441  O  OE2   . GLU A 1 174 ? 146.233 143.647 115.267 1.00 28.48 -1 174 GLU A OE2   1 
ATOM   1442  N  N     . VAL A 1 175 ? 142.831 143.234 120.491 1.00 19.84 ?  175 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 175 ? 142.537 143.279 121.919 1.00 20.81 ?  175 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 175 ? 143.840 143.532 122.662 1.00 18.94 ?  175 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 175 ? 144.783 142.736 122.567 1.00 26.83 ?  175 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 175 ? 141.866 141.985 122.404 1.00 22.21 ?  175 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 175 ? 141.291 142.175 123.798 1.00 14.41 ?  175 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 175 ? 140.786 141.550 121.426 1.00 19.87 ?  175 VAL A CG2   1 
ATOM   1449  N  N     . ASN A 1 176 ? 143.894 144.637 123.398 1.00 18.41 ?  176 ASN A N     1 
ATOM   1450  C  CA    . ASN A 1 176 ? 145.064 144.951 124.197 1.00 20.00 ?  176 ASN A CA    1 
ATOM   1451  C  C     . ASN A 1 176 ? 145.001 144.227 125.538 1.00 23.60 ?  176 ASN A C     1 
ATOM   1452  O  O     . ASN A 1 176 ? 143.939 143.797 125.996 1.00 24.22 ?  176 ASN A O     1 
ATOM   1453  C  CB    . ASN A 1 176 ? 145.180 146.460 124.409 1.00 18.83 ?  176 ASN A CB    1 
ATOM   1454  C  CG    . ASN A 1 176 ? 146.615 146.938 124.414 1.00 21.31 ?  176 ASN A CG    1 
ATOM   1455  O  OD1   . ASN A 1 176 ? 147.532 146.183 124.735 1.00 27.96 ?  176 ASN A OD1   1 
ATOM   1456  N  ND2   . ASN A 1 176 ? 146.818 148.200 124.055 1.00 20.44 ?  176 ASN A ND2   1 
ATOM   1457  N  N     . ASP A 1 177 ? 146.166 144.100 126.175 1.00 23.65 ?  177 ASP A N     1 
ATOM   1458  C  CA    . ASP A 1 177 ? 146.309 143.303 127.392 1.00 20.06 ?  177 ASP A CA    1 
ATOM   1459  C  C     . ASP A 1 177 ? 145.870 144.129 128.599 1.00 24.85 ?  177 ASP A C     1 
ATOM   1460  O  O     . ASP A 1 177 ? 146.678 144.631 129.384 1.00 35.39 ?  177 ASP A O     1 
ATOM   1461  C  CB    . ASP A 1 177 ? 147.744 142.814 127.538 1.00 19.80 ?  177 ASP A CB    1 
ATOM   1462  C  CG    . ASP A 1 177 ? 147.901 141.802 128.648 1.00 25.30 ?  177 ASP A CG    1 
ATOM   1463  O  OD1   . ASP A 1 177 ? 147.020 140.928 128.790 1.00 28.44 ?  177 ASP A OD1   1 
ATOM   1464  O  OD2   . ASP A 1 177 ? 148.909 141.878 129.380 1.00 31.09 -1 177 ASP A OD2   1 
ATOM   1465  N  N     . SER A 1 178 ? 144.555 144.264 128.745 1.00 20.57 ?  178 SER A N     1 
ATOM   1466  C  CA    . SER A 1 178 ? 143.982 144.948 129.896 1.00 17.37 ?  178 SER A CA    1 
ATOM   1467  C  C     . SER A 1 178 ? 142.534 144.511 130.051 1.00 17.74 ?  178 SER A C     1 
ATOM   1468  O  O     . SER A 1 178 ? 141.903 144.041 129.101 1.00 27.43 ?  178 SER A O     1 
ATOM   1469  C  CB    . SER A 1 178 ? 144.076 146.471 129.753 1.00 16.60 ?  178 SER A CB    1 
ATOM   1470  O  OG    . SER A 1 178 ? 142.914 147.001 129.146 1.00 20.62 ?  178 SER A OG    1 
ATOM   1471  N  N     . LEU A 1 179 ? 142.016 144.669 131.271 1.00 22.74 ?  179 LEU A N     1 
ATOM   1472  C  CA    . LEU A 1 179 ? 140.614 144.348 131.520 1.00 19.48 ?  179 LEU A CA    1 
ATOM   1473  C  C     . LEU A 1 179 ? 139.691 145.328 130.810 1.00 18.74 ?  179 LEU A C     1 
ATOM   1474  O  O     . LEU A 1 179 ? 138.638 144.936 130.295 1.00 22.22 ?  179 LEU A O     1 
ATOM   1475  C  CB    . LEU A 1 179 ? 140.331 144.340 133.021 1.00 26.25 ?  179 LEU A CB    1 
ATOM   1476  C  CG    . LEU A 1 179 ? 138.968 143.767 133.416 1.00 18.81 ?  179 LEU A CG    1 
ATOM   1477  C  CD1   . LEU A 1 179 ? 138.968 142.253 133.282 1.00 21.68 ?  179 LEU A CD1   1 
ATOM   1478  C  CD2   . LEU A 1 179 ? 138.590 144.187 134.825 1.00 18.45 ?  179 LEU A CD2   1 
ATOM   1479  N  N     . ASN A 1 180 ? 140.065 146.610 130.781 1.00 21.73 ?  180 ASN A N     1 
ATOM   1480  C  CA    . ASN A 1 180 ? 139.283 147.593 130.039 1.00 19.79 ?  180 ASN A CA    1 
ATOM   1481  C  C     . ASN A 1 180 ? 139.231 147.243 128.559 1.00 20.72 ?  180 ASN A C     1 
ATOM   1482  O  O     . ASN A 1 180 ? 138.166 147.303 127.934 1.00 24.18 ?  180 ASN A O     1 
ATOM   1483  C  CB    . ASN A 1 180 ? 139.875 148.989 130.234 1.00 21.19 ?  180 ASN A CB    1 
ATOM   1484  C  CG    . ASN A 1 180 ? 139.472 149.617 131.549 1.00 26.79 ?  180 ASN A CG    1 
ATOM   1485  O  OD1   . ASN A 1 180 ? 138.400 149.334 132.084 1.00 33.12 ?  180 ASN A OD1   1 
ATOM   1486  N  ND2   . ASN A 1 180 ? 140.333 150.474 132.081 1.00 26.38 ?  180 ASN A ND2   1 
ATOM   1487  N  N     . ASP A 1 181 ? 140.372 146.859 127.987 1.00 21.75 ?  181 ASP A N     1 
ATOM   1488  C  CA    . ASP A 1 181 ? 140.412 146.502 126.574 1.00 12.47 ?  181 ASP A CA    1 
ATOM   1489  C  C     . ASP A 1 181 ? 139.648 145.213 126.304 1.00 18.69 ?  181 ASP A C     1 
ATOM   1490  O  O     . ASP A 1 181 ? 138.997 145.083 125.265 1.00 26.03 ?  181 ASP A O     1 
ATOM   1491  C  CB    . ASP A 1 181 ? 141.861 146.384 126.107 1.00 20.67 ?  181 ASP A CB    1 
ATOM   1492  C  CG    . ASP A 1 181 ? 142.578 147.717 126.104 1.00 28.75 ?  181 ASP A CG    1 
ATOM   1493  O  OD1   . ASP A 1 181 ? 142.186 148.600 125.316 1.00 31.69 ?  181 ASP A OD1   1 
ATOM   1494  O  OD2   . ASP A 1 181 ? 143.537 147.882 126.887 1.00 29.88 -1 181 ASP A OD2   1 
ATOM   1495  N  N     . ILE A 1 182 ? 139.706 144.252 127.226 1.00 20.59 ?  182 ILE A N     1 
ATOM   1496  C  CA    . ILE A 1 182 ? 138.959 143.011 127.048 1.00 17.82 ?  182 ILE A CA    1 
ATOM   1497  C  C     . ILE A 1 182 ? 137.457 143.274 127.093 1.00 19.62 ?  182 ILE A C     1 
ATOM   1498  O  O     . ILE A 1 182 ? 136.694 142.752 126.269 1.00 25.76 ?  182 ILE A O     1 
ATOM   1499  C  CB    . ILE A 1 182 ? 139.392 141.977 128.102 1.00 18.58 ?  182 ILE A CB    1 
ATOM   1500  C  CG1   . ILE A 1 182 ? 140.724 141.346 127.695 1.00 20.04 ?  182 ILE A CG1   1 
ATOM   1501  C  CG2   . ILE A 1 182 ? 138.327 140.907 128.289 1.00 21.02 ?  182 ILE A CG2   1 
ATOM   1502  C  CD1   . ILE A 1 182 ? 141.405 140.606 128.805 1.00 21.69 ?  182 ILE A CD1   1 
ATOM   1503  N  N     . SER A 1 183 ? 137.008 144.089 128.049 1.00 20.91 ?  183 SER A N     1 
ATOM   1504  C  CA    . SER A 1 183 ? 135.592 144.427 128.128 1.00 19.31 ?  183 SER A CA    1 
ATOM   1505  C  C     . SER A 1 183 ? 135.141 145.208 126.900 1.00 23.27 ?  183 SER A C     1 
ATOM   1506  O  O     . SER A 1 183 ? 134.046 144.974 126.375 1.00 25.87 ?  183 SER A O     1 
ATOM   1507  C  CB    . SER A 1 183 ? 135.313 145.219 129.404 1.00 19.40 ?  183 SER A CB    1 
ATOM   1508  O  OG    . SER A 1 183 ? 135.981 146.467 129.385 1.00 29.39 ?  183 SER A OG    1 
ATOM   1509  N  N     . ARG A 1 184 ? 135.975 146.137 126.425 1.00 25.20 ?  184 ARG A N     1 
ATOM   1510  C  CA    . ARG A 1 184 ? 135.639 146.876 125.214 1.00 19.46 ?  184 ARG A CA    1 
ATOM   1511  C  C     . ARG A 1 184 ? 135.586 145.956 124.003 1.00 23.51 ?  184 ARG A C     1 
ATOM   1512  O  O     . ARG A 1 184 ? 134.740 146.133 123.124 1.00 28.66 ?  184 ARG A O     1 
ATOM   1513  C  CB    . ARG A 1 184 ? 136.642 148.005 124.991 1.00 15.25 ?  184 ARG A CB    1 
ATOM   1514  C  CG    . ARG A 1 184 ? 136.339 148.863 123.778 1.00 24.35 ?  184 ARG A CG    1 
ATOM   1515  C  CD    . ARG A 1 184 ? 134.927 149.410 123.823 1.00 24.56 ?  184 ARG A CD    1 
ATOM   1516  N  NE    . ARG A 1 184 ? 134.841 150.628 124.619 1.00 32.26 ?  184 ARG A NE    1 
ATOM   1517  C  CZ    . ARG A 1 184 ? 133.756 151.020 125.271 1.00 29.75 ?  184 ARG A CZ    1 
ATOM   1518  N  NH1   . ARG A 1 184 ? 132.641 150.309 125.248 1.00 25.23 1  184 ARG A NH1   1 
ATOM   1519  N  NH2   . ARG A 1 184 ? 133.790 152.154 125.964 1.00 26.89 ?  184 ARG A NH2   1 
ATOM   1520  N  N     . ALA A 1 185 ? 136.484 144.971 123.934 1.00 24.15 ?  185 ALA A N     1 
ATOM   1521  C  CA    . ALA A 1 185 ? 136.450 144.009 122.840 1.00 16.96 ?  185 ALA A CA    1 
ATOM   1522  C  C     . ALA A 1 185 ? 135.175 143.180 122.876 1.00 20.26 ?  185 ALA A C     1 
ATOM   1523  O  O     . ALA A 1 185 ? 134.568 142.919 121.833 1.00 23.61 ?  185 ALA A O     1 
ATOM   1524  C  CB    . ALA A 1 185 ? 137.680 143.104 122.897 1.00 16.52 ?  185 ALA A CB    1 
ATOM   1525  N  N     . ILE A 1 186 ? 134.753 142.759 124.071 1.00 23.68 ?  186 ILE A N     1 
ATOM   1526  C  CA    . ILE A 1 186 ? 133.496 142.025 124.204 1.00 20.75 ?  186 ILE A CA    1 
ATOM   1527  C  C     . ILE A 1 186 ? 132.329 142.890 123.741 1.00 20.06 ?  186 ILE A C     1 
ATOM   1528  O  O     . ILE A 1 186 ? 131.445 142.437 122.999 1.00 27.89 ?  186 ILE A O     1 
ATOM   1529  C  CB    . ILE A 1 186 ? 133.303 141.548 125.655 1.00 26.09 ?  186 ILE A CB    1 
ATOM   1530  C  CG1   . ILE A 1 186 ? 134.337 140.481 126.014 1.00 24.61 ?  186 ILE A CG1   1 
ATOM   1531  C  CG2   . ILE A 1 186 ? 131.892 141.018 125.867 1.00 24.04 ?  186 ILE A CG2   1 
ATOM   1532  C  CD1   . ILE A 1 186 ? 134.598 140.370 127.498 1.00 23.67 ?  186 ILE A CD1   1 
ATOM   1533  N  N     . ASP A 1 187 ? 132.314 144.155 124.167 1.00 21.52 ?  187 ASP A N     1 
ATOM   1534  C  CA    . ASP A 1 187 ? 131.241 145.064 123.778 1.00 19.03 ?  187 ASP A CA    1 
ATOM   1535  C  C     . ASP A 1 187 ? 131.208 145.267 122.267 1.00 23.82 ?  187 ASP A C     1 
ATOM   1536  O  O     . ASP A 1 187 ? 130.140 145.218 121.647 1.00 28.16 ?  187 ASP A O     1 
ATOM   1537  C  CB    . ASP A 1 187 ? 131.408 146.404 124.495 1.00 17.96 ?  187 ASP A CB    1 
ATOM   1538  C  CG    . ASP A 1 187 ? 130.685 147.535 123.794 1.00 28.50 ?  187 ASP A CG    1 
ATOM   1539  O  OD1   . ASP A 1 187 ? 129.460 147.419 123.579 1.00 30.94 ?  187 ASP A OD1   1 
ATOM   1540  O  OD2   . ASP A 1 187 ? 131.342 148.540 123.452 1.00 34.22 -1 187 ASP A OD2   1 
ATOM   1541  N  N     . ILE A 1 188 ? 132.373 145.497 121.659 1.00 22.45 ?  188 ILE A N     1 
ATOM   1542  C  CA    . ILE A 1 188 ? 132.434 145.738 120.221 1.00 21.59 ?  188 ILE A CA    1 
ATOM   1543  C  C     . ILE A 1 188 ? 132.043 144.485 119.450 1.00 23.18 ?  188 ILE A C     1 
ATOM   1544  O  O     . ILE A 1 188 ? 131.371 144.563 118.418 1.00 27.73 ?  188 ILE A O     1 
ATOM   1545  C  CB    . ILE A 1 188 ? 133.834 146.241 119.822 1.00 22.36 ?  188 ILE A CB    1 
ATOM   1546  C  CG1   . ILE A 1 188 ? 134.120 147.601 120.459 1.00 22.66 ?  188 ILE A CG1   1 
ATOM   1547  C  CG2   . ILE A 1 188 ? 133.952 146.366 118.318 1.00 21.91 ?  188 ILE A CG2   1 
ATOM   1548  C  CD1   . ILE A 1 188 ? 135.536 148.082 120.247 1.00 22.60 ?  188 ILE A CD1   1 
ATOM   1549  N  N     . SER A 1 189 ? 132.455 143.312 119.936 1.00 18.21 ?  189 SER A N     1 
ATOM   1550  C  CA    . SER A 1 189 ? 132.042 142.065 119.303 1.00 12.23 ?  189 SER A CA    1 
ATOM   1551  C  C     . SER A 1 189 ? 130.531 141.907 119.347 1.00 19.79 ?  189 SER A C     1 
ATOM   1552  O  O     . SER A 1 189 ? 129.912 141.505 118.356 1.00 28.18 ?  189 SER A O     1 
ATOM   1553  C  CB    . SER A 1 189 ? 132.725 140.882 119.988 1.00 20.99 ?  189 SER A CB    1 
ATOM   1554  O  OG    . SER A 1 189 ? 134.129 141.050 120.021 1.00 27.35 ?  189 SER A OG    1 
ATOM   1555  N  N     . MET A 1 190 ? 129.919 142.230 120.489 1.00 25.42 ?  190 MET A N     1 
ATOM   1556  C  CA    . MET A 1 190 ? 128.466 142.162 120.593 1.00 22.32 ?  190 MET A CA    1 
ATOM   1557  C  C     . MET A 1 190 ? 127.795 143.144 119.641 1.00 18.68 ?  190 MET A C     1 
ATOM   1558  O  O     . MET A 1 190 ? 126.804 142.806 118.984 1.00 22.42 ?  190 MET A O     1 
ATOM   1559  C  CB    . MET A 1 190 ? 128.035 142.441 122.030 1.00 25.23 ?  190 MET A CB    1 
ATOM   1560  C  CG    . MET A 1 190 ? 128.129 141.246 122.949 1.00 18.79 ?  190 MET A CG    1 
ATOM   1561  S  SD    . MET A 1 190 ? 128.162 141.757 124.671 1.00 37.97 ?  190 MET A SD    1 
ATOM   1562  C  CE    . MET A 1 190 ? 126.746 140.867 125.289 1.00 27.75 ?  190 MET A CE    1 
ATOM   1563  N  N     . GLN A 1 191 ? 128.322 144.367 119.554 1.00 21.05 ?  191 GLN A N     1 
ATOM   1564  C  CA    . GLN A 1 191 ? 127.719 145.376 118.689 1.00 22.57 ?  191 GLN A CA    1 
ATOM   1565  C  C     . GLN A 1 191 ? 127.841 144.996 117.219 1.00 24.99 ?  191 GLN A C     1 
ATOM   1566  O  O     . GLN A 1 191 ? 126.919 145.238 116.432 1.00 30.62 ?  191 GLN A O     1 
ATOM   1567  C  CB    . GLN A 1 191 ? 128.357 146.743 118.940 1.00 22.31 ?  191 GLN A CB    1 
ATOM   1568  C  CG    . GLN A 1 191 ? 128.219 147.252 120.363 1.00 21.20 ?  191 GLN A CG    1 
ATOM   1569  C  CD    . GLN A 1 191 ? 126.795 147.619 120.722 1.00 27.26 ?  191 GLN A CD    1 
ATOM   1570  O  OE1   . GLN A 1 191 ? 125.963 147.866 119.849 1.00 28.28 ?  191 GLN A OE1   1 
ATOM   1571  N  NE2   . GLN A 1 191 ? 126.507 147.662 122.017 1.00 25.51 ?  191 GLN A NE2   1 
ATOM   1572  N  N     . LEU A 1 192 ? 128.973 144.411 116.827 1.00 24.46 ?  192 LEU A N     1 
ATOM   1573  C  CA    . LEU A 1 192 ? 129.166 144.035 115.433 1.00 19.42 ?  192 LEU A CA    1 
ATOM   1574  C  C     . LEU A 1 192 ? 128.397 142.773 115.067 1.00 23.47 ?  192 LEU A C     1 
ATOM   1575  O  O     . LEU A 1 192 ? 127.943 142.643 113.925 1.00 33.19 ?  192 LEU A O     1 
ATOM   1576  C  CB    . LEU A 1 192 ? 130.654 143.857 115.136 1.00 20.09 ?  192 LEU A CB    1 
ATOM   1577  C  CG    . LEU A 1 192 ? 131.524 145.107 115.282 1.00 18.88 ?  192 LEU A CG    1 
ATOM   1578  C  CD1   . LEU A 1 192 ? 132.995 144.732 115.265 1.00 18.46 ?  192 LEU A CD1   1 
ATOM   1579  C  CD2   . LEU A 1 192 ? 131.210 146.129 114.203 1.00 16.55 ?  192 LEU A CD2   1 
ATOM   1580  N  N     . SER A 1 193 ? 128.245 141.833 116.003 1.00 19.30 ?  193 SER A N     1 
ATOM   1581  C  CA    . SER A 1 193 ? 127.369 140.693 115.762 1.00 21.10 ?  193 SER A CA    1 
ATOM   1582  C  C     . SER A 1 193 ? 125.915 141.133 115.684 1.00 30.66 ?  193 SER A C     1 
ATOM   1583  O  O     . SER A 1 193 ? 125.119 140.548 114.941 1.00 35.65 ?  193 SER A O     1 
ATOM   1584  C  CB    . SER A 1 193 ? 127.560 139.642 116.854 1.00 23.76 ?  193 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 193 ? 128.935 139.436 117.119 1.00 29.24 ?  193 SER A OG    1 
ATOM   1586  N  N     . LYS A 1 194 ? 125.550 142.160 116.455 1.00 28.35 ?  194 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 194 ? 124.220 142.747 116.341 1.00 26.81 ?  194 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 194 ? 123.992 143.313 114.946 1.00 33.98 ?  194 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 194 ? 122.897 143.187 114.386 1.00 37.52 ?  194 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 194 ? 124.045 143.831 117.405 1.00 25.61 ?  194 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 194 ? 122.826 144.710 117.220 1.00 31.84 ?  194 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 194 ? 122.828 145.866 118.204 1.00 34.30 ?  194 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 194 ? 121.495 146.595 118.202 1.00 30.41 ?  194 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 194 ? 121.501 147.764 119.121 1.00 33.10 1  194 LYS A NZ    1 
ATOM   1595  N  N     . LEU A 1 195 ? 125.018 143.937 114.367 1.00 34.63 ?  195 LEU A N     1 
ATOM   1596  C  CA    . LEU A 1 195 ? 124.942 144.437 113.000 1.00 32.10 ?  195 LEU A CA    1 
ATOM   1597  C  C     . LEU A 1 195 ? 124.944 143.321 111.965 1.00 34.27 ?  195 LEU A C     1 
ATOM   1598  O  O     . LEU A 1 195 ? 124.726 143.599 110.781 1.00 37.81 ?  195 LEU A O     1 
ATOM   1599  C  CB    . LEU A 1 195 ? 126.105 145.392 112.726 1.00 32.31 ?  195 LEU A CB    1 
ATOM   1600  C  CG    . LEU A 1 195 ? 126.096 146.708 113.504 1.00 35.80 ?  195 LEU A CG    1 
ATOM   1601  C  CD1   . LEU A 1 195 ? 127.366 147.497 113.232 1.00 35.62 ?  195 LEU A CD1   1 
ATOM   1602  C  CD2   . LEU A 1 195 ? 124.866 147.526 113.154 1.00 33.64 ?  195 LEU A CD2   1 
ATOM   1603  N  N     . GLY A 1 196 ? 125.190 142.080 112.375 1.00 34.97 ?  196 GLY A N     1 
ATOM   1604  C  CA    . GLY A 1 196 ? 125.212 140.965 111.456 1.00 33.07 ?  196 GLY A CA    1 
ATOM   1605  C  C     . GLY A 1 196 ? 126.575 140.584 110.933 1.00 37.29 ?  196 GLY A C     1 
ATOM   1606  O  O     . GLY A 1 196 ? 126.656 139.794 109.985 1.00 40.02 ?  196 GLY A O     1 
ATOM   1607  N  N     . GLY A 1 197 ? 127.646 141.110 111.516 1.00 34.21 ?  197 GLY A N     1 
ATOM   1608  C  CA    . GLY A 1 197 ? 128.979 140.847 111.021 1.00 24.52 ?  197 GLY A CA    1 
ATOM   1609  C  C     . GLY A 1 197 ? 129.711 139.761 111.787 1.00 23.86 ?  197 GLY A C     1 
ATOM   1610  O  O     . GLY A 1 197 ? 129.491 139.553 112.977 1.00 33.65 ?  197 GLY A O     1 
ATOM   1611  N  N     . GLY A 1 198 ? 130.591 139.060 111.073 1.00 17.12 ?  198 GLY A N     1 
ATOM   1612  C  CA    . GLY A 1 198 ? 131.484 138.107 111.709 1.00 16.73 ?  198 GLY A CA    1 
ATOM   1613  C  C     . GLY A 1 198 ? 132.699 138.827 112.257 1.00 17.59 ?  198 GLY A C     1 
ATOM   1614  O  O     . GLY A 1 198 ? 133.342 139.611 111.552 1.00 18.46 ?  198 GLY A O     1 
ATOM   1615  N  N     . VAL A 1 199 ? 133.018 138.561 113.519 1.00 21.76 ?  199 VAL A N     1 
ATOM   1616  C  CA    . VAL A 1 199 ? 134.033 139.308 114.251 1.00 13.39 ?  199 VAL A CA    1 
ATOM   1617  C  C     . VAL A 1 199 ? 135.208 138.392 114.542 1.00 11.65 ?  199 VAL A C     1 
ATOM   1618  O  O     . VAL A 1 199 ? 135.032 137.300 115.094 1.00 16.01 ?  199 VAL A O     1 
ATOM   1619  C  CB    . VAL A 1 199 ? 133.463 139.892 115.554 1.00 13.59 ?  199 VAL A CB    1 
ATOM   1620  C  CG1   . VAL A 1 199 ? 134.508 140.737 116.254 1.00 15.15 ?  199 VAL A CG1   1 
ATOM   1621  C  CG2   . VAL A 1 199 ? 132.218 140.700 115.265 1.00 18.65 ?  199 VAL A CG2   1 
ATOM   1622  N  N     . SER A 1 200 ? 136.405 138.838 114.179 1.00 15.20 ?  200 SER A N     1 
ATOM   1623  C  CA    . SER A 1 200 ? 137.644 138.147 114.497 1.00 3.66  ?  200 SER A CA    1 
ATOM   1624  C  C     . SER A 1 200 ? 138.440 138.998 115.474 1.00 11.73 ?  200 SER A C     1 
ATOM   1625  O  O     . SER A 1 200 ? 138.585 140.208 115.273 1.00 21.37 ?  200 SER A O     1 
ATOM   1626  C  CB    . SER A 1 200 ? 138.462 137.873 113.237 1.00 9.17  ?  200 SER A CB    1 
ATOM   1627  O  OG    . SER A 1 200 ? 139.518 136.968 113.499 1.00 16.25 ?  200 SER A OG    1 
ATOM   1628  N  N     . LEU A 1 201 ? 138.945 138.371 116.530 1.00 16.66 ?  201 LEU A N     1 
ATOM   1629  C  CA    . LEU A 1 201 ? 139.684 139.061 117.575 1.00 9.22  ?  201 LEU A CA    1 
ATOM   1630  C  C     . LEU A 1 201 ? 141.078 138.465 117.690 1.00 7.69  ?  201 LEU A C     1 
ATOM   1631  O  O     . LEU A 1 201 ? 141.233 137.240 117.725 1.00 9.39  ?  201 LEU A O     1 
ATOM   1632  C  CB    . LEU A 1 201 ? 138.957 138.966 118.919 1.00 16.07 ?  201 LEU A CB    1 
ATOM   1633  C  CG    . LEU A 1 201 ? 137.562 139.590 118.967 1.00 14.03 ?  201 LEU A CG    1 
ATOM   1634  C  CD1   . LEU A 1 201 ? 136.493 138.514 118.876 1.00 14.27 ?  201 LEU A CD1   1 
ATOM   1635  C  CD2   . LEU A 1 201 ? 137.387 140.421 120.223 1.00 15.95 ?  201 LEU A CD2   1 
ATOM   1636  N  N     . ASN A 1 202 ? 142.083 139.332 117.756 1.00 13.18 ?  202 ASN A N     1 
ATOM   1637  C  CA    . ASN A 1 202 ? 143.459 138.917 117.986 1.00 7.05  ?  202 ASN A CA    1 
ATOM   1638  C  C     . ASN A 1 202 ? 143.708 138.862 119.487 1.00 13.85 ?  202 ASN A C     1 
ATOM   1639  O  O     . ASN A 1 202 ? 143.566 139.873 120.183 1.00 25.93 ?  202 ASN A O     1 
ATOM   1640  C  CB    . ASN A 1 202 ? 144.432 139.882 117.311 1.00 8.39  ?  202 ASN A CB    1 
ATOM   1641  C  CG    . ASN A 1 202 ? 145.853 139.362 117.294 1.00 11.78 ?  202 ASN A CG    1 
ATOM   1642  O  OD1   . ASN A 1 202 ? 146.085 138.155 117.331 1.00 17.73 ?  202 ASN A OD1   1 
ATOM   1643  N  ND2   . ASN A 1 202 ? 146.814 140.274 117.235 1.00 14.87 ?  202 ASN A ND2   1 
ATOM   1644  N  N     . LEU A 1 203 ? 144.073 137.682 119.986 1.00 8.33  ?  203 LEU A N     1 
ATOM   1645  C  CA    . LEU A 1 203 ? 144.301 137.478 121.410 1.00 9.55  ?  203 LEU A CA    1 
ATOM   1646  C  C     . LEU A 1 203 ? 145.773 137.294 121.748 1.00 12.58 ?  203 LEU A C     1 
ATOM   1647  O  O     . LEU A 1 203 ? 146.096 136.918 122.879 1.00 14.59 ?  203 LEU A O     1 
ATOM   1648  C  CB    . LEU A 1 203 ? 143.493 136.278 121.906 1.00 15.42 ?  203 LEU A CB    1 
ATOM   1649  C  CG    . LEU A 1 203 ? 141.975 136.350 121.726 1.00 15.72 ?  203 LEU A CG    1 
ATOM   1650  C  CD1   . LEU A 1 203 ? 141.297 135.323 122.610 1.00 14.37 ?  203 LEU A CD1   1 
ATOM   1651  C  CD2   . LEU A 1 203 ? 141.446 137.745 122.021 1.00 12.05 ?  203 LEU A CD2   1 
ATOM   1652  N  N     . SER A 1 204 ? 146.673 137.557 120.798 1.00 17.27 ?  204 SER A N     1 
ATOM   1653  C  CA    . SER A 1 204 ? 148.095 137.339 121.036 1.00 15.28 ?  204 SER A CA    1 
ATOM   1654  C  C     . SER A 1 204 ? 148.682 138.358 122.004 1.00 17.32 ?  204 SER A C     1 
ATOM   1655  O  O     . SER A 1 204 ? 149.614 138.031 122.747 1.00 27.44 ?  204 SER A O     1 
ATOM   1656  C  CB    . SER A 1 204 ? 148.857 137.376 119.713 1.00 12.39 ?  204 SER A CB    1 
ATOM   1657  O  OG    . SER A 1 204 ? 148.295 136.472 118.779 1.00 20.84 ?  204 SER A OG    1 
ATOM   1658  N  N     . LYS A 1 205 ? 148.162 139.587 122.012 1.00 18.64 ?  205 LYS A N     1 
ATOM   1659  C  CA    . LYS A 1 205 ? 148.654 140.590 122.946 1.00 21.79 ?  205 LYS A CA    1 
ATOM   1660  C  C     . LYS A 1 205 ? 148.244 140.294 124.380 1.00 22.02 ?  205 LYS A C     1 
ATOM   1661  O  O     . LYS A 1 205 ? 148.885 140.793 125.310 1.00 28.08 ?  205 LYS A O     1 
ATOM   1662  C  CB    . LYS A 1 205 ? 148.157 141.976 122.539 1.00 22.28 ?  205 LYS A CB    1 
ATOM   1663  C  CG    . LYS A 1 205 ? 148.773 142.486 121.257 1.00 21.54 ?  205 LYS A CG    1 
ATOM   1664  C  CD    . LYS A 1 205 ? 148.282 143.876 120.923 1.00 25.34 ?  205 LYS A CD    1 
ATOM   1665  C  CE    . LYS A 1 205 ? 149.055 144.450 119.752 1.00 28.62 ?  205 LYS A CE    1 
ATOM   1666  N  NZ    . LYS A 1 205 ? 148.893 143.632 118.521 1.00 24.12 1  205 LYS A NZ    1 
ATOM   1667  N  N     . LEU A 1 206 ? 147.198 139.498 124.577 1.00 18.83 ?  206 LEU A N     1 
ATOM   1668  C  CA    . LEU A 1 206 ? 146.763 139.143 125.918 1.00 12.03 ?  206 LEU A CA    1 
ATOM   1669  C  C     . LEU A 1 206 ? 147.790 138.240 126.588 1.00 18.40 ?  206 LEU A C     1 
ATOM   1670  O  O     . LEU A 1 206 ? 148.302 137.298 125.979 1.00 24.65 ?  206 LEU A O     1 
ATOM   1671  C  CB    . LEU A 1 206 ? 145.407 138.447 125.863 1.00 16.39 ?  206 LEU A CB    1 
ATOM   1672  C  CG    . LEU A 1 206 ? 144.246 139.311 125.372 1.00 21.56 ?  206 LEU A CG    1 
ATOM   1673  C  CD1   . LEU A 1 206 ? 142.963 138.508 125.361 1.00 19.17 ?  206 LEU A CD1   1 
ATOM   1674  C  CD2   . LEU A 1 206 ? 144.100 140.550 126.236 1.00 21.52 ?  206 LEU A CD2   1 
ATOM   1675  N  N     . ARG A 1 207 ? 148.089 138.533 127.849 1.00 25.76 ?  207 ARG A N     1 
ATOM   1676  C  CA    . ARG A 1 207 ? 149.082 137.755 128.572 1.00 22.21 ?  207 ARG A CA    1 
ATOM   1677  C  C     . ARG A 1 207 ? 148.541 136.370 128.909 1.00 27.34 ?  207 ARG A C     1 
ATOM   1678  O  O     . ARG A 1 207 ? 147.336 136.170 129.079 1.00 33.02 ?  207 ARG A O     1 
ATOM   1679  C  CB    . ARG A 1 207 ? 149.520 138.492 129.837 1.00 25.46 ?  207 ARG A CB    1 
ATOM   1680  C  CG    . ARG A 1 207 ? 148.437 138.719 130.867 1.00 20.93 ?  207 ARG A CG    1 
ATOM   1681  C  CD    . ARG A 1 207 ? 148.939 139.630 131.974 1.00 21.04 ?  207 ARG A CD    1 
ATOM   1682  N  NE    . ARG A 1 207 ? 148.814 141.037 131.615 1.00 29.59 ?  207 ARG A NE    1 
ATOM   1683  C  CZ    . ARG A 1 207 ? 148.977 142.044 132.461 1.00 23.85 ?  207 ARG A CZ    1 
ATOM   1684  N  NH1   . ARG A 1 207 ? 149.293 141.837 133.728 1.00 28.40 1  207 ARG A NH1   1 
ATOM   1685  N  NH2   . ARG A 1 207 ? 148.817 143.290 132.025 1.00 19.28 ?  207 ARG A NH2   1 
ATOM   1686  N  N     . ALA A 1 208 ? 149.454 135.406 129.001 1.00 28.20 ?  208 ALA A N     1 
ATOM   1687  C  CA    . ALA A 1 208 ? 149.088 134.004 129.116 1.00 25.93 ?  208 ALA A CA    1 
ATOM   1688  C  C     . ALA A 1 208 ? 148.591 133.686 130.524 1.00 31.00 ?  208 ALA A C     1 
ATOM   1689  O  O     . ALA A 1 208 ? 148.554 134.540 131.412 1.00 33.88 ?  208 ALA A O     1 
ATOM   1690  C  CB    . ALA A 1 208 ? 150.271 133.117 128.737 1.00 27.47 ?  208 ALA A CB    1 
ATOM   1691  N  N     . LYS A 1 209 ? 148.190 132.435 130.726 1.00 30.80 ?  209 LYS A N     1 
ATOM   1692  C  CA    . LYS A 1 209 ? 147.711 132.003 132.031 1.00 25.81 ?  209 LYS A CA    1 
ATOM   1693  C  C     . LYS A 1 209 ? 148.879 131.872 133.000 1.00 33.73 ?  209 LYS A C     1 
ATOM   1694  O  O     . LYS A 1 209 ? 149.934 131.333 132.650 1.00 34.47 ?  209 LYS A O     1 
ATOM   1695  C  CB    . LYS A 1 209 ? 146.966 130.676 131.913 1.00 28.85 ?  209 LYS A CB    1 
ATOM   1696  C  CG    . LYS A 1 209 ? 146.348 130.198 133.214 1.00 32.40 ?  209 LYS A CG    1 
ATOM   1697  C  CD    . LYS A 1 209 ? 146.027 128.713 133.180 1.00 32.56 ?  209 LYS A CD    1 
ATOM   1698  C  CE    . LYS A 1 209 ? 147.092 127.920 132.441 1.00 35.58 ?  209 LYS A CE    1 
ATOM   1699  N  NZ    . LYS A 1 209 ? 146.734 126.479 132.339 1.00 35.06 1  209 LYS A NZ    1 
ATOM   1700  N  N     . GLY A 1 210 ? 148.685 132.355 134.223 1.00 37.65 ?  210 GLY A N     1 
ATOM   1701  C  CA    . GLY A 1 210 ? 149.741 132.344 135.212 1.00 32.83 ?  210 GLY A CA    1 
ATOM   1702  C  C     . GLY A 1 210 ? 150.634 133.560 135.211 1.00 35.30 ?  210 GLY A C     1 
ATOM   1703  O  O     . GLY A 1 210 ? 151.740 133.497 135.760 1.00 40.60 ?  210 GLY A O     1 
ATOM   1704  N  N     . GLU A 1 211 ? 150.198 134.661 134.610 1.00 33.92 ?  211 GLU A N     1 
ATOM   1705  C  CA    . GLU A 1 211 ? 150.960 135.899 134.591 1.00 31.71 ?  211 GLU A CA    1 
ATOM   1706  C  C     . GLU A 1 211 ? 150.496 136.824 135.710 1.00 34.75 ?  211 GLU A C     1 
ATOM   1707  O  O     . GLU A 1 211 ? 149.506 136.568 136.399 1.00 36.62 ?  211 GLU A O     1 
ATOM   1708  C  CB    . GLU A 1 211 ? 150.835 136.588 133.230 1.00 30.32 ?  211 GLU A CB    1 
ATOM   1709  C  CG    . GLU A 1 211 ? 151.453 135.795 132.097 1.00 33.60 ?  211 GLU A CG    1 
ATOM   1710  C  CD    . GLU A 1 211 ? 152.419 136.614 131.269 1.00 36.43 ?  211 GLU A CD    1 
ATOM   1711  O  OE1   . GLU A 1 211 ? 153.464 137.027 131.812 1.00 39.07 ?  211 GLU A OE1   1 
ATOM   1712  O  OE2   . GLU A 1 211 ? 152.143 136.833 130.072 1.00 30.88 -1 211 GLU A OE2   1 
ATOM   1713  N  N     . ALA A 1 212 ? 151.230 137.919 135.883 1.00 33.78 ?  212 ALA A N     1 
ATOM   1714  C  CA    . ALA A 1 212 ? 151.010 138.823 137.002 1.00 33.97 ?  212 ALA A CA    1 
ATOM   1715  C  C     . ALA A 1 212 ? 150.070 139.960 136.621 1.00 39.38 ?  212 ALA A C     1 
ATOM   1716  O  O     . ALA A 1 212 ? 150.174 140.534 135.533 1.00 41.12 ?  212 ALA A O     1 
ATOM   1717  C  CB    . ALA A 1 212 ? 152.338 139.394 137.499 1.00 35.82 ?  212 ALA A CB    1 
ATOM   1718  N  N     . ILE A 1 213 ? 149.149 140.276 137.529 1.00 32.09 ?  213 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 148.281 141.443 137.420 1.00 34.78 ?  213 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 148.609 142.352 138.594 1.00 36.14 ?  213 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 148.353 141.994 139.752 1.00 40.58 ?  213 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 146.794 141.063 137.414 1.00 34.49 ?  213 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 146.528 139.939 136.412 1.00 34.39 ?  213 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 145.937 142.277 137.097 1.00 29.79 ?  213 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 145.171 139.295 136.572 1.00 30.50 ?  213 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 149.162 143.530 138.300 1.00 41.13 ?  214 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 149.603 144.477 139.327 1.00 40.28 ?  214 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 150.573 143.819 140.304 1.00 46.68 ?  214 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 150.476 143.990 141.522 1.00 49.91 ?  214 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 148.412 145.093 140.063 1.00 40.44 ?  214 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 147.780 146.267 139.336 1.00 40.01 ?  214 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 146.608 146.842 140.112 1.00 42.30 ?  214 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 146.152 148.164 139.514 1.00 44.11 ?  214 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 144.987 148.735 140.243 1.00 42.67 1  214 LYS A NZ    1 
ATOM   1735  N  N     . ASP A 1 215 ? 151.513 143.047 139.756 1.00 47.70 ?  215 ASP A N     1 
ATOM   1736  C  CA    . ASP A 1 215 ? 152.609 142.447 140.521 1.00 49.79 ?  215 ASP A CA    1 
ATOM   1737  C  C     . ASP A 1 215 ? 152.108 141.472 141.585 1.00 48.44 ?  215 ASP A C     1 
ATOM   1738  O  O     . ASP A 1 215 ? 152.679 141.367 142.672 1.00 48.37 ?  215 ASP A O     1 
ATOM   1739  C  CB    . ASP A 1 215 ? 153.501 143.524 141.145 1.00 48.76 ?  215 ASP A CB    1 
ATOM   1740  C  CG    . ASP A 1 215 ? 154.055 144.490 140.115 1.00 52.47 ?  215 ASP A CG    1 
ATOM   1741  O  OD1   . ASP A 1 215 ? 154.438 144.034 139.018 1.00 51.00 ?  215 ASP A OD1   1 
ATOM   1742  O  OD2   . ASP A 1 215 ? 154.111 145.704 140.403 1.00 51.63 -1 215 ASP A OD2   1 
ATOM   1743  N  N     . VAL A 1 216 ? 151.035 140.749 141.276 1.00 43.69 ?  216 VAL A N     1 
ATOM   1744  C  CA    . VAL A 1 216 ? 150.619 139.584 142.049 1.00 45.86 ?  216 VAL A CA    1 
ATOM   1745  C  C     . VAL A 1 216 ? 150.685 138.377 141.119 1.00 46.94 ?  216 VAL A C     1 
ATOM   1746  O  O     . VAL A 1 216 ? 150.223 138.440 139.974 1.00 49.98 ?  216 VAL A O     1 
ATOM   1747  C  CB    . VAL A 1 216 ? 149.224 139.769 142.687 1.00 44.85 ?  216 VAL A CB    1 
ATOM   1748  C  CG1   . VAL A 1 216 ? 148.895 141.250 142.840 1.00 43.90 ?  216 VAL A CG1   1 
ATOM   1749  C  CG2   . VAL A 1 216 ? 148.122 139.040 141.925 1.00 43.37 ?  216 VAL A CG2   1 
ATOM   1750  N  N     . GLU A 1 217 ? 151.323 137.309 141.585 1.00 48.48 ?  217 GLU A N     1 
ATOM   1751  C  CA    . GLU A 1 217 ? 151.727 136.227 140.700 1.00 48.13 ?  217 GLU A CA    1 
ATOM   1752  C  C     . GLU A 1 217 ? 150.596 135.227 140.480 1.00 49.28 ?  217 GLU A C     1 
ATOM   1753  O  O     . GLU A 1 217 ? 149.684 135.083 141.300 1.00 51.39 ?  217 GLU A O     1 
ATOM   1754  C  CB    . GLU A 1 217 ? 152.956 135.508 141.260 1.00 50.28 ?  217 GLU A CB    1 
ATOM   1755  C  CG    . GLU A 1 217 ? 154.105 136.423 141.672 1.00 50.51 ?  217 GLU A CG    1 
ATOM   1756  C  CD    . GLU A 1 217 ? 154.241 137.646 140.782 1.00 52.26 ?  217 GLU A CD    1 
ATOM   1757  O  OE1   . GLU A 1 217 ? 154.852 137.528 139.700 1.00 53.56 ?  217 GLU A OE1   1 
ATOM   1758  O  OE2   . GLU A 1 217 ? 153.748 138.726 141.170 1.00 49.24 -1 217 GLU A OE2   1 
ATOM   1759  N  N     . ASN A 1 218 ? 150.677 134.525 139.345 1.00 44.02 ?  218 ASN A N     1 
ATOM   1760  C  CA    . ASN A 1 218 ? 149.746 133.451 138.989 1.00 44.04 ?  218 ASN A CA    1 
ATOM   1761  C  C     . ASN A 1 218 ? 148.296 133.929 139.031 1.00 47.82 ?  218 ASN A C     1 
ATOM   1762  O  O     . ASN A 1 218 ? 147.410 133.240 139.538 1.00 46.76 ?  218 ASN A O     1 
ATOM   1763  C  CB    . ASN A 1 218 ? 149.943 132.232 139.892 1.00 43.02 ?  218 ASN A CB    1 
ATOM   1764  C  CG    . ASN A 1 218 ? 149.815 130.923 139.140 1.00 48.15 ?  218 ASN A CG    1 
ATOM   1765  O  OD1   . ASN A 1 218 ? 150.391 130.752 138.065 1.00 50.06 ?  218 ASN A OD1   1 
ATOM   1766  N  ND2   . ASN A 1 218 ? 149.057 129.989 139.702 1.00 47.54 ?  218 ASN A ND2   1 
ATOM   1767  N  N     . ALA A 1 219 ? 148.052 135.120 138.488 1.00 38.03 ?  219 ALA A N     1 
ATOM   1768  C  CA    . ALA A 1 219 ? 146.744 135.753 138.577 1.00 33.65 ?  219 ALA A CA    1 
ATOM   1769  C  C     . ALA A 1 219 ? 145.955 135.715 137.279 1.00 35.31 ?  219 ALA A C     1 
ATOM   1770  O  O     . ALA A 1 219 ? 144.723 135.643 137.321 1.00 36.61 ?  219 ALA A O     1 
ATOM   1771  C  CB    . ALA A 1 219 ? 146.899 137.210 139.021 1.00 35.87 ?  219 ALA A CB    1 
ATOM   1772  N  N     . THR A 1 220 ? 146.626 135.763 136.132 1.00 36.45 ?  220 THR A N     1 
ATOM   1773  C  CA    . THR A 1 220 ? 145.922 135.839 134.860 1.00 30.45 ?  220 THR A CA    1 
ATOM   1774  C  C     . THR A 1 220 ? 145.268 134.506 134.521 1.00 34.14 ?  220 THR A C     1 
ATOM   1775  O  O     . THR A 1 220 ? 145.841 133.436 134.749 1.00 35.22 ?  220 THR A O     1 
ATOM   1776  C  CB    . THR A 1 220 ? 146.886 136.248 133.747 1.00 27.27 ?  220 THR A CB    1 
ATOM   1777  O  OG1   . THR A 1 220 ? 147.601 137.425 134.141 1.00 35.48 ?  220 THR A OG1   1 
ATOM   1778  C  CG2   . THR A 1 220 ? 146.126 136.539 132.465 1.00 29.46 ?  220 THR A CG2   1 
ATOM   1779  N  N     . LYS A 1 221 ? 144.055 134.576 133.973 1.00 35.92 ?  221 LYS A N     1 
ATOM   1780  C  CA    . LYS A 1 221 ? 143.359 133.390 133.495 1.00 30.05 ?  221 LYS A CA    1 
ATOM   1781  C  C     . LYS A 1 221 ? 143.798 132.973 132.099 1.00 33.95 ?  221 LYS A C     1 
ATOM   1782  O  O     . LYS A 1 221 ? 143.395 131.900 131.636 1.00 40.03 ?  221 LYS A O     1 
ATOM   1783  C  CB    . LYS A 1 221 ? 141.847 133.626 133.503 1.00 29.97 ?  221 LYS A CB    1 
ATOM   1784  C  CG    . LYS A 1 221 ? 141.241 133.692 134.889 1.00 32.25 ?  221 LYS A CG    1 
ATOM   1785  C  CD    . LYS A 1 221 ? 139.827 133.144 134.895 1.00 33.02 ?  221 LYS A CD    1 
ATOM   1786  C  CE    . LYS A 1 221 ? 139.364 132.839 136.306 1.00 33.42 ?  221 LYS A CE    1 
ATOM   1787  N  NZ    . LYS A 1 221 ? 138.090 132.070 136.318 1.00 36.29 1  221 LYS A NZ    1 
ATOM   1788  N  N     . GLY A 1 222 ? 144.604 133.783 131.427 1.00 31.76 ?  222 GLY A N     1 
ATOM   1789  C  CA    . GLY A 1 222 ? 145.039 133.472 130.087 1.00 26.99 ?  222 GLY A CA    1 
ATOM   1790  C  C     . GLY A 1 222 ? 144.029 133.903 129.041 1.00 27.61 ?  222 GLY A C     1 
ATOM   1791  O  O     . GLY A 1 222 ? 143.043 134.593 129.316 1.00 33.53 ?  222 GLY A O     1 
ATOM   1792  N  N     . VAL A 1 223 ? 144.295 133.480 127.806 1.00 25.41 ?  223 VAL A N     1 
ATOM   1793  C  CA    . VAL A 1 223 ? 143.389 133.805 126.712 1.00 24.51 ?  223 VAL A CA    1 
ATOM   1794  C  C     . VAL A 1 223 ? 142.163 132.905 126.695 1.00 18.93 ?  223 VAL A C     1 
ATOM   1795  O  O     . VAL A 1 223 ? 141.186 133.229 126.014 1.00 22.69 ?  223 VAL A O     1 
ATOM   1796  C  CB    . VAL A 1 223 ? 144.109 133.736 125.354 1.00 22.73 ?  223 VAL A CB    1 
ATOM   1797  C  CG1   . VAL A 1 223 ? 145.447 134.444 125.429 1.00 20.06 ?  223 VAL A CG1   1 
ATOM   1798  C  CG2   . VAL A 1 223 ? 144.286 132.291 124.914 1.00 20.14 ?  223 VAL A CG2   1 
ATOM   1799  N  N     . VAL A 1 224 ? 142.175 131.791 127.428 1.00 27.29 ?  224 VAL A N     1 
ATOM   1800  C  CA    . VAL A 1 224 ? 141.028 130.888 127.413 1.00 23.25 ?  224 VAL A CA    1 
ATOM   1801  C  C     . VAL A 1 224 ? 139.828 131.500 128.134 1.00 27.16 ?  224 VAL A C     1 
ATOM   1802  O  O     . VAL A 1 224 ? 138.685 131.331 127.693 1.00 29.49 ?  224 VAL A O     1 
ATOM   1803  C  CB    . VAL A 1 224 ? 141.417 129.526 128.010 1.00 30.45 ?  224 VAL A CB    1 
ATOM   1804  C  CG1   . VAL A 1 224 ? 140.218 128.596 128.053 1.00 28.30 ?  224 VAL A CG1   1 
ATOM   1805  C  CG2   . VAL A 1 224 ? 142.539 128.905 127.199 1.00 28.17 ?  224 VAL A CG2   1 
ATOM   1806  N  N     . GLY A 1 225 ? 140.052 132.216 129.236 1.00 26.05 ?  225 GLY A N     1 
ATOM   1807  C  CA    . GLY A 1 225 ? 138.951 132.917 129.880 1.00 23.64 ?  225 GLY A CA    1 
ATOM   1808  C  C     . GLY A 1 225 ? 138.370 134.006 128.999 1.00 21.95 ?  225 GLY A C     1 
ATOM   1809  O  O     . GLY A 1 225 ? 137.152 134.208 128.956 1.00 29.10 ?  225 GLY A O     1 
ATOM   1810  N  N     . VAL A 1 226 ? 139.236 134.720 128.277 1.00 22.04 ?  226 VAL A N     1 
ATOM   1811  C  CA    . VAL A 1 226 ? 138.767 135.721 127.326 1.00 21.14 ?  226 VAL A CA    1 
ATOM   1812  C  C     . VAL A 1 226 ? 137.978 135.058 126.206 1.00 19.41 ?  226 VAL A C     1 
ATOM   1813  O  O     . VAL A 1 226 ? 136.986 135.608 125.718 1.00 22.12 ?  226 VAL A O     1 
ATOM   1814  C  CB    . VAL A 1 226 ? 139.953 136.536 126.780 1.00 19.03 ?  226 VAL A CB    1 
ATOM   1815  C  CG1   . VAL A 1 226 ? 139.454 137.690 125.925 1.00 26.23 ?  226 VAL A CG1   1 
ATOM   1816  C  CG2   . VAL A 1 226 ? 140.811 137.042 127.921 1.00 16.46 ?  226 VAL A CG2   1 
ATOM   1817  N  N     . MET A 1 227 ? 138.407 133.869 125.780 1.00 21.13 ?  227 MET A N     1 
ATOM   1818  C  CA    . MET A 1 227 ? 137.662 133.137 124.761 1.00 23.66 ?  227 MET A CA    1 
ATOM   1819  C  C     . MET A 1 227 ? 136.297 132.712 125.277 1.00 23.17 ?  227 MET A C     1 
ATOM   1820  O  O     . MET A 1 227 ? 135.318 132.729 124.530 1.00 28.48 ?  227 MET A O     1 
ATOM   1821  C  CB    . MET A 1 227 ? 138.448 131.917 124.287 1.00 20.13 ?  227 MET A CB    1 
ATOM   1822  C  CG    . MET A 1 227 ? 139.714 132.242 123.532 1.00 17.73 ?  227 MET A CG    1 
ATOM   1823  S  SD    . MET A 1 227 ? 140.778 130.803 123.382 1.00 36.51 ?  227 MET A SD    1 
ATOM   1824  C  CE    . MET A 1 227 ? 139.800 129.805 122.267 1.00 24.79 ?  227 MET A CE    1 
ATOM   1825  N  N     . LYS A 1 228 ? 136.216 132.302 126.543 1.00 21.26 ?  228 LYS A N     1 
ATOM   1826  C  CA    . LYS A 1 228 ? 134.919 131.970 127.128 1.00 22.96 ?  228 LYS A CA    1 
ATOM   1827  C  C     . LYS A 1 228 ? 134.007 133.190 127.159 1.00 21.81 ?  228 LYS A C     1 
ATOM   1828  O  O     . LYS A 1 228 ? 132.817 133.100 126.823 1.00 24.62 ?  228 LYS A O     1 
ATOM   1829  C  CB    . LYS A 1 228 ? 135.103 131.409 128.537 1.00 24.81 ?  228 LYS A CB    1 
ATOM   1830  C  CG    . LYS A 1 228 ? 135.505 129.948 128.586 1.00 27.57 ?  228 LYS A CG    1 
ATOM   1831  C  CD    . LYS A 1 228 ? 135.928 129.554 129.993 1.00 30.30 ?  228 LYS A CD    1 
ATOM   1832  C  CE    . LYS A 1 228 ? 137.439 129.566 130.142 1.00 31.49 ?  228 LYS A CE    1 
ATOM   1833  N  NZ    . LYS A 1 228 ? 137.873 129.882 131.531 1.00 27.84 1  228 LYS A NZ    1 
ATOM   1834  N  N     . LEU A 1 229 ? 134.553 134.342 127.555 1.00 20.71 ?  229 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 229 ? 133.770 135.575 127.560 1.00 18.79 ?  229 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 229 ? 133.287 135.926 126.159 1.00 20.13 ?  229 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 229 ? 132.122 136.290 125.959 1.00 18.55 ?  229 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 229 ? 134.600 136.718 128.139 1.00 20.16 ?  229 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 229 ? 134.811 136.755 129.650 1.00 18.98 ?  229 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 229 ? 135.833 137.820 129.996 1.00 21.66 ?  229 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 229 ? 133.500 137.024 130.359 1.00 18.33 ?  229 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 230 ? 134.177 135.823 125.170 1.00 24.97 ?  230 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 230 ? 133.812 136.138 123.795 1.00 16.02 ?  230 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 230 ? 132.789 135.152 123.251 1.00 15.64 ?  230 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 230 ? 131.884 135.538 122.508 1.00 30.75 ?  230 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 230 ? 135.060 136.159 122.912 1.00 23.37 ?  230 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 230 ? 136.008 137.338 123.125 1.00 22.41 ?  230 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 230 ? 137.305 137.124 122.360 1.00 23.43 ?  230 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 230 ? 135.343 138.642 122.715 1.00 16.74 ?  230 LEU A CD2   1 
ATOM   1850  N  N     . ASP A 1 231 ? 132.924 133.872 123.599 1.00 23.35 ?  231 ASP A N     1 
ATOM   1851  C  CA    . ASP A 1 231 ? 131.958 132.873 123.162 1.00 23.77 ?  231 ASP A CA    1 
ATOM   1852  C  C     . ASP A 1 231 ? 130.581 133.159 123.741 1.00 22.03 ?  231 ASP A C     1 
ATOM   1853  O  O     . ASP A 1 231 ? 129.572 133.049 123.038 1.00 29.84 ?  231 ASP A O     1 
ATOM   1854  C  CB    . ASP A 1 231 ? 132.438 131.477 123.558 1.00 23.08 ?  231 ASP A CB    1 
ATOM   1855  C  CG    . ASP A 1 231 ? 131.413 130.401 123.268 1.00 36.05 ?  231 ASP A CG    1 
ATOM   1856  O  OD1   . ASP A 1 231 ? 130.981 130.289 122.102 1.00 42.35 ?  231 ASP A OD1   1 
ATOM   1857  O  OD2   . ASP A 1 231 ? 131.043 129.663 124.206 1.00 33.33 -1 231 ASP A OD2   1 
ATOM   1858  N  N     . ASN A 1 232 ? 130.520 133.541 125.018 1.00 27.62 ?  232 ASN A N     1 
ATOM   1859  C  CA    . ASN A 1 232 ? 129.238 133.929 125.599 1.00 25.45 ?  232 ASN A CA    1 
ATOM   1860  C  C     . ASN A 1 232 ? 128.675 135.173 124.921 1.00 21.44 ?  232 ASN A C     1 
ATOM   1861  O  O     . ASN A 1 232 ? 127.468 135.257 124.666 1.00 28.17 ?  232 ASN A O     1 
ATOM   1862  C  CB    . ASN A 1 232 ? 129.383 134.152 127.103 1.00 26.42 ?  232 ASN A CB    1 
ATOM   1863  C  CG    . ASN A 1 232 ? 128.327 133.417 127.899 1.00 32.00 ?  232 ASN A CG    1 
ATOM   1864  O  OD1   . ASN A 1 232 ? 127.143 133.744 127.828 1.00 34.71 ?  232 ASN A OD1   1 
ATOM   1865  N  ND2   . ASN A 1 232 ? 128.744 132.405 128.646 1.00 34.25 ?  232 ASN A ND2   1 
ATOM   1866  N  N     . ALA A 1 233 ? 129.537 136.148 124.624 1.00 17.49 ?  233 ALA A N     1 
ATOM   1867  C  CA    . ALA A 1 233 ? 129.082 137.362 123.956 1.00 19.25 ?  233 ALA A CA    1 
ATOM   1868  C  C     . ALA A 1 233 ? 128.530 137.060 122.567 1.00 27.61 ?  233 ALA A C     1 
ATOM   1869  O  O     . ALA A 1 233 ? 127.526 137.647 122.148 1.00 27.48 ?  233 ALA A O     1 
ATOM   1870  C  CB    . ALA A 1 233 ? 130.225 138.372 123.873 1.00 19.50 ?  233 ALA A CB    1 
ATOM   1871  N  N     . PHE A 1 234 ? 129.180 136.153 121.836 1.00 25.88 ?  234 PHE A N     1 
ATOM   1872  C  CA    . PHE A 1 234 ? 128.724 135.810 120.495 1.00 18.99 ?  234 PHE A CA    1 
ATOM   1873  C  C     . PHE A 1 234 ? 127.466 134.954 120.530 1.00 22.17 ?  234 PHE A C     1 
ATOM   1874  O  O     . PHE A 1 234 ? 126.625 135.058 119.632 1.00 29.06 ?  234 PHE A O     1 
ATOM   1875  C  CB    . PHE A 1 234 ? 129.834 135.098 119.723 1.00 24.21 ?  234 PHE A CB    1 
ATOM   1876  C  CG    . PHE A 1 234 ? 130.906 136.019 119.218 1.00 22.59 ?  234 PHE A CG    1 
ATOM   1877  C  CD1   . PHE A 1 234 ? 130.593 137.071 118.375 1.00 21.43 ?  234 PHE A CD1   1 
ATOM   1878  C  CD2   . PHE A 1 234 ? 132.226 135.832 119.581 1.00 21.36 ?  234 PHE A CD2   1 
ATOM   1879  C  CE1   . PHE A 1 234 ? 131.578 137.920 117.913 1.00 20.43 ?  234 PHE A CE1   1 
ATOM   1880  C  CE2   . PHE A 1 234 ? 133.214 136.679 119.123 1.00 22.33 ?  234 PHE A CE2   1 
ATOM   1881  C  CZ    . PHE A 1 234 ? 132.889 137.723 118.286 1.00 22.81 ?  234 PHE A CZ    1 
ATOM   1882  N  N     . ARG A 1 235 ? 127.321 134.101 121.546 1.00 24.66 ?  235 ARG A N     1 
ATOM   1883  C  CA    . ARG A 1 235 ? 126.068 133.374 121.714 1.00 25.84 ?  235 ARG A CA    1 
ATOM   1884  C  C     . ARG A 1 235 ? 124.924 134.332 122.016 1.00 31.07 ?  235 ARG A C     1 
ATOM   1885  O  O     . ARG A 1 235 ? 123.811 134.161 121.508 1.00 39.35 ?  235 ARG A O     1 
ATOM   1886  C  CB    . ARG A 1 235 ? 126.202 132.333 122.824 1.00 26.56 ?  235 ARG A CB    1 
ATOM   1887  C  CG    . ARG A 1 235 ? 127.111 131.170 122.479 1.00 32.06 ?  235 ARG A CG    1 
ATOM   1888  C  CD    . ARG A 1 235 ? 126.891 129.998 123.417 1.00 31.55 ?  235 ARG A CD    1 
ATOM   1889  N  NE    . ARG A 1 235 ? 128.071 129.731 124.230 1.00 33.93 ?  235 ARG A NE    1 
ATOM   1890  C  CZ    . ARG A 1 235 ? 128.286 130.257 125.428 1.00 35.96 ?  235 ARG A CZ    1 
ATOM   1891  N  NH1   . ARG A 1 235 ? 127.415 131.079 125.988 1.00 35.78 1  235 ARG A NH1   1 
ATOM   1892  N  NH2   . ARG A 1 235 ? 129.406 129.951 126.079 1.00 33.53 ?  235 ARG A NH2   1 
ATOM   1893  N  N     . TYR A 1 236 ? 125.182 135.348 122.842 1.00 25.37 ?  236 TYR A N     1 
ATOM   1894  C  CA    . TYR A 1 236 ? 124.138 136.306 123.184 1.00 21.11 ?  236 TYR A CA    1 
ATOM   1895  C  C     . TYR A 1 236 ? 123.732 137.143 121.975 1.00 24.21 ?  236 TYR A C     1 
ATOM   1896  O  O     . TYR A 1 236 ? 122.540 137.332 121.710 1.00 24.55 ?  236 TYR A O     1 
ATOM   1897  C  CB    . TYR A 1 236 ? 124.609 137.206 124.325 1.00 19.94 ?  236 TYR A CB    1 
ATOM   1898  C  CG    . TYR A 1 236 ? 123.528 138.111 124.859 1.00 23.99 ?  236 TYR A CG    1 
ATOM   1899  C  CD1   . TYR A 1 236 ? 122.517 137.608 125.662 1.00 21.35 ?  236 TYR A CD1   1 
ATOM   1900  C  CD2   . TYR A 1 236 ? 123.516 139.466 124.556 1.00 24.85 ?  236 TYR A CD2   1 
ATOM   1901  C  CE1   . TYR A 1 236 ? 121.525 138.425 126.153 1.00 24.71 ?  236 TYR A CE1   1 
ATOM   1902  C  CE2   . TYR A 1 236 ? 122.527 140.292 125.044 1.00 16.98 ?  236 TYR A CE2   1 
ATOM   1903  C  CZ    . TYR A 1 236 ? 121.535 139.765 125.842 1.00 21.52 ?  236 TYR A CZ    1 
ATOM   1904  O  OH    . TYR A 1 236 ? 120.544 140.576 126.333 1.00 25.78 ?  236 TYR A OH    1 
ATOM   1905  N  N     . ALA A 1 237 ? 124.711 137.653 121.231 1.00 30.61 ?  237 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 237 ? 124.459 138.502 120.066 1.00 30.91 ?  237 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 237 ? 124.416 137.604 118.834 1.00 35.59 ?  237 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 237 ? 125.446 137.269 118.249 1.00 39.55 ?  237 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 237 ? 125.523 139.585 119.944 1.00 30.89 ?  237 ALA A CB    1 
ATOM   1910  N  N     . ASP A 1 238 ? 123.207 137.220 118.434 1.00 50.35 ?  238 ASP A N     1 
ATOM   1911  C  CA    . ASP A 1 238 ? 122.994 136.261 117.355 1.00 54.69 ?  238 ASP A CA    1 
ATOM   1912  C  C     . ASP A 1 238 ? 121.999 136.808 116.337 1.00 59.58 ?  238 ASP A C     1 
ATOM   1913  O  O     . ASP A 1 238 ? 121.055 136.129 115.924 1.00 59.96 ?  238 ASP A O     1 
ATOM   1914  C  CB    . ASP A 1 238 ? 122.526 134.922 117.916 1.00 52.63 ?  238 ASP A CB    1 
ATOM   1915  C  CG    . ASP A 1 238 ? 121.332 135.062 118.837 1.00 55.48 ?  238 ASP A CG    1 
ATOM   1916  O  OD1   . ASP A 1 238 ? 121.006 136.204 119.222 1.00 55.79 ?  238 ASP A OD1   1 
ATOM   1917  O  OD2   . ASP A 1 238 ? 120.719 134.029 119.180 1.00 56.24 -1 238 ASP A OD2   1 
ATOM   1918  N  N     . GLN A 1 239 ? 122.207 138.061 115.920 1.00 65.05 ?  239 GLN A N     1 
ATOM   1919  C  CA    . GLN A 1 239 ? 121.393 138.706 114.885 1.00 64.51 ?  239 GLN A CA    1 
ATOM   1920  C  C     . GLN A 1 239 ? 119.905 138.672 115.228 1.00 64.87 ?  239 GLN A C     1 
ATOM   1921  O  O     . GLN A 1 239 ? 119.064 138.316 114.400 1.00 64.37 ?  239 GLN A O     1 
ATOM   1922  C  CB    . GLN A 1 239 ? 121.644 138.077 113.512 1.00 64.27 ?  239 GLN A CB    1 
ATOM   1923  C  CG    . GLN A 1 239 ? 122.829 138.647 112.762 1.00 63.60 ?  239 GLN A CG    1 
ATOM   1924  C  CD    . GLN A 1 239 ? 122.612 138.649 111.260 1.00 65.72 ?  239 GLN A CD    1 
ATOM   1925  O  OE1   . GLN A 1 239 ? 121.553 139.049 110.776 1.00 65.94 ?  239 GLN A OE1   1 
ATOM   1926  N  NE2   . GLN A 1 239 ? 123.612 138.194 110.515 1.00 64.99 ?  239 GLN A NE2   1 
ATOM   1927  N  N     . MET A 1 240 ? 119.583 139.050 116.466 1.00 68.51 ?  240 MET A N     1 
ATOM   1928  C  CA    . MET A 1 240 ? 118.201 139.072 116.947 1.00 68.14 ?  240 MET A CA    1 
ATOM   1929  C  C     . MET A 1 240 ? 117.547 137.698 116.815 1.00 69.94 ?  240 MET A C     1 
ATOM   1930  O  O     . MET A 1 240 ? 116.380 137.578 116.433 1.00 68.89 ?  240 MET A O     1 
ATOM   1931  C  CB    . MET A 1 240 ? 117.378 140.137 116.217 1.00 66.92 ?  240 MET A CB    1 
ATOM   1932  C  CG    . MET A 1 240 ? 117.744 141.570 116.567 1.00 68.38 ?  240 MET A CG    1 
ATOM   1933  S  SD    . MET A 1 240 ? 119.516 141.888 116.514 1.00 73.97 ?  240 MET A SD    1 
ATOM   1934  C  CE    . MET A 1 240 ? 119.522 143.659 116.254 1.00 65.29 ?  240 MET A CE    1 
ATOM   1935  N  N     . GLY A 1 241 ? 118.304 136.653 117.131 1.00 69.79 ?  241 GLY A N     1 
ATOM   1936  C  CA    . GLY A 1 241 ? 117.789 135.297 117.054 1.00 68.54 ?  241 GLY A CA    1 
ATOM   1937  C  C     . GLY A 1 241 ? 117.477 134.813 115.654 1.00 70.57 ?  241 GLY A C     1 
ATOM   1938  O  O     . GLY A 1 241 ? 116.455 134.147 115.447 1.00 71.99 ?  241 GLY A O     1 
ATOM   1939  N  N     . GLN A 1 242 ? 118.334 135.131 114.684 1.00 72.20 ?  242 GLN A N     1 
ATOM   1940  C  CA    . GLN A 1 242 ? 118.167 134.672 113.310 1.00 72.85 ?  242 GLN A CA    1 
ATOM   1941  C  C     . GLN A 1 242 ? 119.261 133.693 112.904 1.00 73.98 ?  242 GLN A C     1 
ATOM   1942  O  O     . GLN A 1 242 ? 118.964 132.587 112.443 1.00 74.28 ?  242 GLN A O     1 
ATOM   1943  C  CB    . GLN A 1 242 ? 118.134 135.872 112.354 1.00 72.37 ?  242 GLN A CB    1 
ATOM   1944  C  CG    . GLN A 1 242 ? 116.934 136.785 112.550 1.00 73.86 ?  242 GLN A CG    1 
ATOM   1945  C  CD    . GLN A 1 242 ? 116.693 137.694 111.363 1.00 75.01 ?  242 GLN A CD    1 
ATOM   1946  O  OE1   . GLN A 1 242 ? 117.303 137.530 110.306 1.00 75.76 ?  242 GLN A OE1   1 
ATOM   1947  N  NE2   . GLN A 1 242 ? 115.802 138.663 111.531 1.00 73.28 ?  242 GLN A NE2   1 
ATOM   1948  N  N     . ARG A 1 243 ? 120.526 134.072 113.066 1.00 64.01 ?  243 ARG A N     1 
ATOM   1949  C  CA    . ARG A 1 243 ? 121.655 133.202 112.778 1.00 63.58 ?  243 ARG A CA    1 
ATOM   1950  C  C     . ARG A 1 243 ? 122.493 133.031 114.037 1.00 62.97 ?  243 ARG A C     1 
ATOM   1951  O  O     . ARG A 1 243 ? 122.483 133.886 114.926 1.00 61.17 ?  243 ARG A O     1 
ATOM   1952  C  CB    . ARG A 1 243 ? 122.505 133.758 111.606 1.00 62.81 ?  243 ARG A CB    1 
ATOM   1953  C  CG    . ARG A 1 243 ? 123.195 135.120 111.825 1.00 63.98 ?  243 ARG A CG    1 
ATOM   1954  C  CD    . ARG A 1 243 ? 124.470 135.025 112.659 1.00 64.32 ?  243 ARG A CD    1 
ATOM   1955  N  NE    . ARG A 1 243 ? 125.093 136.319 112.908 1.00 65.06 ?  243 ARG A NE    1 
ATOM   1956  C  CZ    . ARG A 1 243 ? 126.156 136.776 112.264 1.00 64.23 ?  243 ARG A CZ    1 
ATOM   1957  N  NH1   . ARG A 1 243 ? 126.741 136.073 111.307 1.00 63.32 1  243 ARG A NH1   1 
ATOM   1958  N  NH2   . ARG A 1 243 ? 126.651 137.967 112.590 1.00 60.04 ?  243 ARG A NH2   1 
ATOM   1959  N  N     . GLN A 1 244 ? 123.219 131.919 114.107 1.00 64.35 ?  244 GLN A N     1 
ATOM   1960  C  CA    . GLN A 1 244 ? 124.093 131.674 115.246 1.00 62.85 ?  244 GLN A CA    1 
ATOM   1961  C  C     . GLN A 1 244 ? 125.271 132.639 115.220 1.00 62.96 ?  244 GLN A C     1 
ATOM   1962  O  O     . GLN A 1 244 ? 125.960 132.763 114.203 1.00 60.03 ?  244 GLN A O     1 
ATOM   1963  C  CB    . GLN A 1 244 ? 124.595 130.231 115.233 1.00 60.75 ?  244 GLN A CB    1 
ATOM   1964  C  CG    . GLN A 1 244 ? 123.576 129.208 115.704 1.00 62.26 ?  244 GLN A CG    1 
ATOM   1965  C  CD    . GLN A 1 244 ? 124.227 127.939 116.220 1.00 64.17 ?  244 GLN A CD    1 
ATOM   1966  O  OE1   . GLN A 1 244 ? 125.196 127.445 115.643 1.00 64.37 ?  244 GLN A OE1   1 
ATOM   1967  N  NE2   . GLN A 1 244 ? 123.698 127.406 117.315 1.00 61.33 ?  244 GLN A NE2   1 
ATOM   1968  N  N     . GLY A 1 245 ? 125.507 133.314 116.343 1.00 50.20 ?  245 GLY A N     1 
ATOM   1969  C  CA    . GLY A 1 245 ? 126.597 134.267 116.438 1.00 46.90 ?  245 GLY A CA    1 
ATOM   1970  C  C     . GLY A 1 245 ? 127.944 133.640 116.149 1.00 45.73 ?  245 GLY A C     1 
ATOM   1971  O  O     . GLY A 1 245 ? 128.349 132.684 116.816 1.00 43.83 ?  245 GLY A O     1 
ATOM   1972  N  N     . SER A 1 246 ? 128.649 134.175 115.157 1.00 40.73 ?  246 SER A N     1 
ATOM   1973  C  CA    . SER A 1 246 ? 129.892 133.595 114.667 1.00 32.62 ?  246 SER A CA    1 
ATOM   1974  C  C     . SER A 1 246 ? 131.050 134.518 115.017 1.00 31.43 ?  246 SER A C     1 
ATOM   1975  O  O     . SER A 1 246 ? 131.038 135.700 114.659 1.00 30.78 ?  246 SER A O     1 
ATOM   1976  C  CB    . SER A 1 246 ? 129.828 133.363 113.158 1.00 32.71 ?  246 SER A CB    1 
ATOM   1977  O  OG    . SER A 1 246 ? 128.846 132.396 112.830 1.00 44.32 ?  246 SER A OG    1 
ATOM   1978  N  N     . GLY A 1 247 ? 132.045 133.973 115.711 1.00 28.96 ?  247 GLY A N     1 
ATOM   1979  C  CA    . GLY A 1 247 ? 133.232 134.727 116.046 1.00 13.13 ?  247 GLY A CA    1 
ATOM   1980  C  C     . GLY A 1 247 ? 134.468 133.867 115.885 1.00 15.41 ?  247 GLY A C     1 
ATOM   1981  O  O     . GLY A 1 247 ? 134.408 132.636 115.915 1.00 23.68 ?  247 GLY A O     1 
ATOM   1982  N  N     . ALA A 1 248 ? 135.596 134.544 115.708 1.00 17.67 ?  248 ALA A N     1 
ATOM   1983  C  CA    . ALA A 1 248 ? 136.883 133.891 115.552 1.00 14.46 ?  248 ALA A CA    1 
ATOM   1984  C  C     . ALA A 1 248 ? 137.887 134.518 116.504 1.00 12.56 ?  248 ALA A C     1 
ATOM   1985  O  O     . ALA A 1 248 ? 137.844 135.719 116.775 1.00 16.39 ?  248 ALA A O     1 
ATOM   1986  C  CB    . ALA A 1 248 ? 137.400 133.989 114.110 1.00 8.12  ?  248 ALA A CB    1 
ATOM   1987  N  N     . ALA A 1 249 ? 138.791 133.689 117.012 1.00 16.30 ?  249 ALA A N     1 
ATOM   1988  C  CA    . ALA A 1 249 ? 139.880 134.134 117.868 1.00 5.45  ?  249 ALA A CA    1 
ATOM   1989  C  C     . ALA A 1 249 ? 141.192 133.654 117.271 1.00 11.13 ?  249 ALA A C     1 
ATOM   1990  O  O     . ALA A 1 249 ? 141.325 132.478 116.921 1.00 19.26 ?  249 ALA A O     1 
ATOM   1991  C  CB    . ALA A 1 249 ? 139.716 133.609 119.297 1.00 13.03 ?  249 ALA A CB    1 
ATOM   1992  N  N     . TYR A 1 250 ? 142.153 134.560 117.147 1.00 15.80 ?  250 TYR A N     1 
ATOM   1993  C  CA    . TYR A 1 250 ? 143.460 134.239 116.596 1.00 9.77  ?  250 TYR A CA    1 
ATOM   1994  C  C     . TYR A 1 250 ? 144.520 134.395 117.673 1.00 6.64  ?  250 TYR A C     1 
ATOM   1995  O  O     . TYR A 1 250 ? 144.537 135.395 118.397 1.00 17.12 ?  250 TYR A O     1 
ATOM   1996  C  CB    . TYR A 1 250 ? 143.787 135.129 115.398 1.00 10.64 ?  250 TYR A CB    1 
ATOM   1997  C  CG    . TYR A 1 250 ? 143.208 134.631 114.096 1.00 17.03 ?  250 TYR A CG    1 
ATOM   1998  C  CD1   . TYR A 1 250 ? 141.869 134.826 113.793 1.00 11.39 ?  250 TYR A CD1   1 
ATOM   1999  C  CD2   . TYR A 1 250 ? 143.999 133.960 113.174 1.00 13.62 ?  250 TYR A CD2   1 
ATOM   2000  C  CE1   . TYR A 1 250 ? 141.334 134.373 112.608 1.00 5.03  ?  250 TYR A CE1   1 
ATOM   2001  C  CE2   . TYR A 1 250 ? 143.470 133.501 111.985 1.00 9.66  ?  250 TYR A CE2   1 
ATOM   2002  C  CZ    . TYR A 1 250 ? 142.138 133.711 111.707 1.00 8.96  ?  250 TYR A CZ    1 
ATOM   2003  O  OH    . TYR A 1 250 ? 141.606 133.260 110.523 1.00 16.52 ?  250 TYR A OH    1 
ATOM   2004  N  N     . LEU A 1 251 ? 145.394 133.402 117.777 1.00 11.05 ?  251 LEU A N     1 
ATOM   2005  C  CA    . LEU A 1 251 ? 146.500 133.421 118.718 1.00 13.94 ?  251 LEU A CA    1 
ATOM   2006  C  C     . LEU A 1 251 ? 147.782 133.060 117.989 1.00 11.63 ?  251 LEU A C     1 
ATOM   2007  O  O     . LEU A 1 251 ? 147.794 132.152 117.153 1.00 16.73 ?  251 LEU A O     1 
ATOM   2008  C  CB    . LEU A 1 251 ? 146.269 132.447 119.875 1.00 17.48 ?  251 LEU A CB    1 
ATOM   2009  C  CG    . LEU A 1 251 ? 147.101 132.702 121.132 1.00 12.99 ?  251 LEU A CG    1 
ATOM   2010  C  CD1   . LEU A 1 251 ? 146.546 133.882 121.904 1.00 18.08 ?  251 LEU A CD1   1 
ATOM   2011  C  CD2   . LEU A 1 251 ? 147.149 131.461 122.001 1.00 13.39 ?  251 LEU A CD2   1 
ATOM   2012  N  N     . ASN A 1 252 ? 148.856 133.776 118.302 1.00 15.94 ?  252 ASN A N     1 
ATOM   2013  C  CA    . ASN A 1 252 ? 150.160 133.422 117.767 1.00 12.87 ?  252 ASN A CA    1 
ATOM   2014  C  C     . ASN A 1 252 ? 150.613 132.089 118.347 1.00 14.42 ?  252 ASN A C     1 
ATOM   2015  O  O     . ASN A 1 252 ? 150.356 131.781 119.513 1.00 25.53 ?  252 ASN A O     1 
ATOM   2016  C  CB    . ASN A 1 252 ? 151.179 134.515 118.079 1.00 15.10 ?  252 ASN A CB    1 
ATOM   2017  C  CG    . ASN A 1 252 ? 152.343 134.513 117.112 1.00 20.40 ?  252 ASN A CG    1 
ATOM   2018  O  OD1   . ASN A 1 252 ? 153.249 133.688 117.215 1.00 25.03 ?  252 ASN A OD1   1 
ATOM   2019  N  ND2   . ASN A 1 252 ? 152.318 135.433 116.157 1.00 17.33 ?  252 ASN A ND2   1 
ATOM   2020  N  N     . ILE A 1 253 ? 151.288 131.288 117.519 1.00 13.59 ?  253 ILE A N     1 
ATOM   2021  C  CA    . ILE A 1 253 ? 151.707 129.964 117.956 1.00 20.79 ?  253 ILE A CA    1 
ATOM   2022  C  C     . ILE A 1 253 ? 152.797 130.033 119.018 1.00 23.63 ?  253 ILE A C     1 
ATOM   2023  O  O     . ILE A 1 253 ? 153.031 129.045 119.723 1.00 25.79 ?  253 ILE A O     1 
ATOM   2024  C  CB    . ILE A 1 253 ? 152.158 129.121 116.748 1.00 19.47 ?  253 ILE A CB    1 
ATOM   2025  C  CG1   . ILE A 1 253 ? 152.028 127.630 117.062 1.00 23.14 ?  253 ILE A CG1   1 
ATOM   2026  C  CG2   . ILE A 1 253 ? 153.580 129.475 116.342 1.00 13.69 ?  253 ILE A CG2   1 
ATOM   2027  C  CD1   . ILE A 1 253 ? 151.780 126.769 115.853 1.00 21.73 ?  253 ILE A CD1   1 
ATOM   2028  N  N     . PHE A 1 254 ? 153.466 131.174 119.162 1.00 22.21 ?  254 PHE A N     1 
ATOM   2029  C  CA    . PHE A 1 254 ? 154.475 131.350 120.198 1.00 15.92 ?  254 PHE A CA    1 
ATOM   2030  C  C     . PHE A 1 254 ? 153.892 131.888 121.498 1.00 21.42 ?  254 PHE A C     1 
ATOM   2031  O  O     . PHE A 1 254 ? 154.620 131.995 122.490 1.00 29.46 ?  254 PHE A O     1 
ATOM   2032  C  CB    . PHE A 1 254 ? 155.589 132.271 119.693 1.00 22.92 ?  254 PHE A CB    1 
ATOM   2033  C  CG    . PHE A 1 254 ? 156.562 131.587 118.774 1.00 26.00 ?  254 PHE A CG    1 
ATOM   2034  C  CD1   . PHE A 1 254 ? 157.412 130.604 119.251 1.00 25.65 ?  254 PHE A CD1   1 
ATOM   2035  C  CD2   . PHE A 1 254 ? 156.610 131.909 117.429 1.00 23.77 ?  254 PHE A CD2   1 
ATOM   2036  C  CE1   . PHE A 1 254 ? 158.302 129.968 118.408 1.00 28.02 ?  254 PHE A CE1   1 
ATOM   2037  C  CE2   . PHE A 1 254 ? 157.496 131.274 116.580 1.00 26.10 ?  254 PHE A CE2   1 
ATOM   2038  C  CZ    . PHE A 1 254 ? 158.344 130.304 117.072 1.00 27.05 ?  254 PHE A CZ    1 
ATOM   2039  N  N     . HIS A 1 255 ? 152.609 132.238 121.510 1.00 26.58 ?  255 HIS A N     1 
ATOM   2040  C  CA    . HIS A 1 255 ? 151.915 132.506 122.761 1.00 17.25 ?  255 HIS A CA    1 
ATOM   2041  C  C     . HIS A 1 255 ? 151.866 131.230 123.590 1.00 19.54 ?  255 HIS A C     1 
ATOM   2042  O  O     . HIS A 1 255 ? 151.693 130.133 123.054 1.00 28.90 ?  255 HIS A O     1 
ATOM   2043  C  CB    . HIS A 1 255 ? 150.502 133.014 122.475 1.00 19.06 ?  255 HIS A CB    1 
ATOM   2044  C  CG    . HIS A 1 255 ? 149.826 133.649 123.650 1.00 23.16 ?  255 HIS A CG    1 
ATOM   2045  N  ND1   . HIS A 1 255 ? 149.379 132.929 124.735 1.00 21.46 ?  255 HIS A ND1   1 
ATOM   2046  C  CD2   . HIS A 1 255 ? 149.499 134.939 123.895 1.00 15.99 ?  255 HIS A CD2   1 
ATOM   2047  C  CE1   . HIS A 1 255 ? 148.819 133.749 125.605 1.00 16.84 ?  255 HIS A CE1   1 
ATOM   2048  N  NE2   . HIS A 1 255 ? 148.877 134.975 125.119 1.00 13.24 ?  255 HIS A NE2   1 
ATOM   2049  N  N     . ARG A 1 256 ? 152.029 131.370 124.907 1.00 21.55 ?  256 ARG A N     1 
ATOM   2050  C  CA    . ARG A 1 256 ? 152.140 130.180 125.743 1.00 21.81 ?  256 ARG A CA    1 
ATOM   2051  C  C     . ARG A 1 256 ? 150.815 129.434 125.824 1.00 27.23 ?  256 ARG A C     1 
ATOM   2052  O  O     . ARG A 1 256 ? 150.795 128.203 125.938 1.00 30.87 ?  256 ARG A O     1 
ATOM   2053  C  CB    . ARG A 1 256 ? 152.614 130.552 127.140 1.00 24.98 ?  256 ARG A CB    1 
ATOM   2054  C  CG    . ARG A 1 256 ? 153.052 129.350 127.941 1.00 29.78 ?  256 ARG A CG    1 
ATOM   2055  C  CD    . ARG A 1 256 ? 152.500 129.376 129.342 1.00 30.42 ?  256 ARG A CD    1 
ATOM   2056  N  NE    . ARG A 1 256 ? 151.078 129.688 129.378 1.00 29.67 ?  256 ARG A NE    1 
ATOM   2057  C  CZ    . ARG A 1 256 ? 150.142 128.813 129.715 1.00 31.62 ?  256 ARG A CZ    1 
ATOM   2058  N  NH1   . ARG A 1 256 ? 150.447 127.572 130.057 1.00 32.60 1  256 ARG A NH1   1 
ATOM   2059  N  NH2   . ARG A 1 256 ? 148.869 129.193 129.719 1.00 33.08 ?  256 ARG A NH2   1 
ATOM   2060  N  N     . ASP A 1 257 ? 149.701 130.156 125.763 1.00 22.54 ?  257 ASP A N     1 
ATOM   2061  C  CA    . ASP A 1 257 ? 148.368 129.561 125.825 1.00 19.25 ?  257 ASP A CA    1 
ATOM   2062  C  C     . ASP A 1 257 ? 148.016 128.757 124.596 1.00 24.96 ?  257 ASP A C     1 
ATOM   2063  O  O     . ASP A 1 257 ? 146.889 128.242 124.565 1.00 32.70 ?  257 ASP A O     1 
ATOM   2064  C  CB    . ASP A 1 257 ? 147.314 130.648 126.028 1.00 21.68 ?  257 ASP A CB    1 
ATOM   2065  C  CG    . ASP A 1 257 ? 147.276 131.175 127.444 1.00 30.64 ?  257 ASP A CG    1 
ATOM   2066  O  OD1   . ASP A 1 257 ? 147.762 130.476 128.355 1.00 28.10 ?  257 ASP A OD1   1 
ATOM   2067  O  OD2   . ASP A 1 257 ? 146.747 132.285 127.647 1.00 34.69 -1 257 ASP A OD2   1 
ATOM   2068  N  N     . ILE A 1 258 ? 148.936 128.622 123.636 1.00 26.12 ?  258 ILE A N     1 
ATOM   2069  C  CA    . ILE A 1 258 ? 148.592 128.058 122.334 1.00 25.64 ?  258 ILE A CA    1 
ATOM   2070  C  C     . ILE A 1 258 ? 148.002 126.662 122.488 1.00 23.84 ?  258 ILE A C     1 
ATOM   2071  O  O     . ILE A 1 258 ? 147.057 126.295 121.784 1.00 32.27 ?  258 ILE A O     1 
ATOM   2072  C  CB    . ILE A 1 258 ? 149.820 128.067 121.401 1.00 22.86 ?  258 ILE A CB    1 
ATOM   2073  C  CG1   . ILE A 1 258 ? 149.424 127.629 119.989 1.00 25.32 ?  258 ILE A CG1   1 
ATOM   2074  C  CG2   . ILE A 1 258 ? 150.948 127.201 121.953 1.00 19.03 ?  258 ILE A CG2   1 
ATOM   2075  C  CD1   . ILE A 1 258 ? 148.374 128.514 119.360 1.00 18.76 ?  258 ILE A CD1   1 
ATOM   2076  N  N     . ASN A 1 259 ? 148.537 125.868 123.417 1.00 23.42 ?  259 ASN A N     1 
ATOM   2077  C  CA    . ASN A 1 259 ? 147.971 124.544 123.653 1.00 23.87 ?  259 ASN A CA    1 
ATOM   2078  C  C     . ASN A 1 259 ? 146.568 124.651 124.234 1.00 27.63 ?  259 ASN A C     1 
ATOM   2079  O  O     . ASN A 1 259 ? 145.619 124.059 123.702 1.00 29.97 ?  259 ASN A O     1 
ATOM   2080  C  CB    . ASN A 1 259 ? 148.886 123.744 124.579 1.00 25.62 ?  259 ASN A CB    1 
ATOM   2081  C  CG    . ASN A 1 259 ? 150.141 123.263 123.881 1.00 30.57 ?  259 ASN A CG    1 
ATOM   2082  O  OD1   . ASN A 1 259 ? 150.086 122.412 122.994 1.00 31.68 ?  259 ASN A OD1   1 
ATOM   2083  N  ND2   . ASN A 1 259 ? 151.283 123.813 124.275 1.00 27.56 ?  259 ASN A ND2   1 
ATOM   2084  N  N     . ASP A 1 260 ? 146.406 125.443 125.297 1.00 26.94 ?  260 ASP A N     1 
ATOM   2085  C  CA    . ASP A 1 260 ? 145.089 125.608 125.905 1.00 26.40 ?  260 ASP A CA    1 
ATOM   2086  C  C     . ASP A 1 260 ? 144.108 126.200 124.905 1.00 21.16 ?  260 ASP A C     1 
ATOM   2087  O  O     . ASP A 1 260 ? 142.966 125.740 124.789 1.00 27.71 ?  260 ASP A O     1 
ATOM   2088  C  CB    . ASP A 1 260 ? 145.192 126.486 127.152 1.00 26.24 ?  260 ASP A CB    1 
ATOM   2089  C  CG    . ASP A 1 260 ? 146.372 126.121 128.029 1.00 36.42 ?  260 ASP A CG    1 
ATOM   2090  O  OD1   . ASP A 1 260 ? 146.935 127.029 128.676 1.00 35.80 ?  260 ASP A OD1   1 
ATOM   2091  O  OD2   . ASP A 1 260 ? 146.734 124.928 128.074 1.00 35.91 -1 260 ASP A OD2   1 
ATOM   2092  N  N     . PHE A 1 261 ? 144.547 127.226 124.171 1.00 26.31 ?  261 PHE A N     1 
ATOM   2093  C  CA    . PHE A 1 261 ? 143.839 127.719 122.997 1.00 23.74 ?  261 PHE A CA    1 
ATOM   2094  C  C     . PHE A 1 261 ? 143.344 126.562 122.139 1.00 20.08 ?  261 PHE A C     1 
ATOM   2095  O  O     . PHE A 1 261 ? 142.135 126.381 121.941 1.00 21.56 ?  261 PHE A O     1 
ATOM   2096  C  CB    . PHE A 1 261 ? 144.783 128.634 122.207 1.00 16.16 ?  261 PHE A CB    1 
ATOM   2097  C  CG    . PHE A 1 261 ? 144.139 129.345 121.053 1.00 22.45 ?  261 PHE A CG    1 
ATOM   2098  C  CD1   . PHE A 1 261 ? 143.355 130.464 121.262 1.00 18.74 ?  261 PHE A CD1   1 
ATOM   2099  C  CD2   . PHE A 1 261 ? 144.354 128.917 119.755 1.00 23.64 ?  261 PHE A CD2   1 
ATOM   2100  C  CE1   . PHE A 1 261 ? 142.774 131.126 120.201 1.00 13.75 ?  261 PHE A CE1   1 
ATOM   2101  C  CE2   . PHE A 1 261 ? 143.779 129.577 118.691 1.00 15.00 ?  261 PHE A CE2   1 
ATOM   2102  C  CZ    . PHE A 1 261 ? 142.989 130.684 118.915 1.00 18.00 ?  261 PHE A CZ    1 
ATOM   2103  N  N     . LEU A 1 262 ? 144.279 125.730 121.671 1.00 26.08 ?  262 LEU A N     1 
ATOM   2104  C  CA    . LEU A 1 262 ? 143.904 124.587 120.847 1.00 23.94 ?  262 LEU A CA    1 
ATOM   2105  C  C     . LEU A 1 262 ? 143.020 123.623 121.623 1.00 29.96 ?  262 LEU A C     1 
ATOM   2106  O  O     . LEU A 1 262 ? 142.090 123.028 121.063 1.00 28.96 ?  262 LEU A O     1 
ATOM   2107  C  CB    . LEU A 1 262 ? 145.159 123.880 120.338 1.00 23.93 ?  262 LEU A CB    1 
ATOM   2108  C  CG    . LEU A 1 262 ? 146.029 124.665 119.359 1.00 25.30 ?  262 LEU A CG    1 
ATOM   2109  C  CD1   . LEU A 1 262 ? 147.249 123.853 118.968 1.00 27.68 ?  262 LEU A CD1   1 
ATOM   2110  C  CD2   . LEU A 1 262 ? 145.231 125.073 118.135 1.00 23.46 ?  262 LEU A CD2   1 
ATOM   2111  N  N     . ASP A 1 263 ? 143.270 123.485 122.928 1.00 35.28 ?  263 ASP A N     1 
ATOM   2112  C  CA    . ASP A 1 263 ? 142.470 122.584 123.745 1.00 29.88 ?  263 ASP A CA    1 
ATOM   2113  C  C     . ASP A 1 263 ? 141.014 123.017 123.813 1.00 31.41 ?  263 ASP A C     1 
ATOM   2114  O  O     . ASP A 1 263 ? 140.162 122.221 124.222 1.00 39.37 ?  263 ASP A O     1 
ATOM   2115  C  CB    . ASP A 1 263 ? 143.053 122.492 125.155 1.00 33.59 ?  263 ASP A CB    1 
ATOM   2116  C  CG    . ASP A 1 263 ? 144.324 121.669 125.205 1.00 38.24 ?  263 ASP A CG    1 
ATOM   2117  O  OD1   . ASP A 1 263 ? 144.571 120.896 124.257 1.00 38.59 ?  263 ASP A OD1   1 
ATOM   2118  O  OD2   . ASP A 1 263 ? 145.075 121.794 126.195 1.00 38.50 -1 263 ASP A OD2   1 
ATOM   2119  N  N     . THR A 1 264 ? 140.707 124.257 123.426 1.00 34.25 ?  264 THR A N     1 
ATOM   2120  C  CA    . THR A 1 264 ? 139.316 124.685 123.402 1.00 32.61 ?  264 THR A CA    1 
ATOM   2121  C  C     . THR A 1 264 ? 138.516 123.994 122.306 1.00 37.29 ?  264 THR A C     1 
ATOM   2122  O  O     . THR A 1 264 ? 137.283 124.012 122.354 1.00 40.05 ?  264 THR A O     1 
ATOM   2123  C  CB    . THR A 1 264 ? 139.229 126.200 123.227 1.00 35.07 ?  264 THR A CB    1 
ATOM   2124  O  OG1   . THR A 1 264 ? 139.883 126.579 122.009 1.00 39.96 ?  264 THR A OG1   1 
ATOM   2125  C  CG2   . THR A 1 264 ? 139.892 126.906 124.398 1.00 31.28 ?  264 THR A CG2   1 
ATOM   2126  N  N     . LYS A 1 265 ? 139.182 123.384 121.323 1.00 36.99 ?  265 LYS A N     1 
ATOM   2127  C  CA    . LYS A 1 265 ? 138.491 122.721 120.226 1.00 36.97 ?  265 LYS A CA    1 
ATOM   2128  C  C     . LYS A 1 265 ? 138.508 121.204 120.325 1.00 39.83 ?  265 LYS A C     1 
ATOM   2129  O  O     . LYS A 1 265 ? 137.928 120.537 119.461 1.00 43.53 ?  265 LYS A O     1 
ATOM   2130  C  CB    . LYS A 1 265 ? 139.088 123.154 118.883 1.00 37.82 ?  265 LYS A CB    1 
ATOM   2131  C  CG    . LYS A 1 265 ? 138.569 124.486 118.384 1.00 37.62 ?  265 LYS A CG    1 
ATOM   2132  C  CD    . LYS A 1 265 ? 137.061 124.570 118.510 1.00 39.31 ?  265 LYS A CD    1 
ATOM   2133  C  CE    . LYS A 1 265 ? 136.550 125.931 118.083 1.00 36.10 ?  265 LYS A CE    1 
ATOM   2134  N  NZ    . LYS A 1 265 ? 135.113 126.109 118.422 1.00 37.78 1  265 LYS A NZ    1 
ATOM   2135  N  N     . LYS A 1 266 ? 139.152 120.638 121.340 1.00 45.49 ?  266 LYS A N     1 
ATOM   2136  C  CA    . LYS A 1 266 ? 139.136 119.193 121.508 1.00 46.34 ?  266 LYS A CA    1 
ATOM   2137  C  C     . LYS A 1 266 ? 137.772 118.729 122.005 1.00 50.98 ?  266 LYS A C     1 
ATOM   2138  O  O     . LYS A 1 266 ? 137.099 119.413 122.781 1.00 50.36 ?  266 LYS A O     1 
ATOM   2139  C  CB    . LYS A 1 266 ? 140.232 118.752 122.477 1.00 44.07 ?  266 LYS A CB    1 
ATOM   2140  C  CG    . LYS A 1 266 ? 141.608 118.661 121.840 1.00 47.04 ?  266 LYS A CG    1 
ATOM   2141  C  CD    . LYS A 1 266 ? 142.638 118.101 122.805 1.00 48.02 ?  266 LYS A CD    1 
ATOM   2142  C  CE    . LYS A 1 266 ? 143.951 117.815 122.094 1.00 48.71 ?  266 LYS A CE    1 
ATOM   2143  N  NZ    . LYS A 1 266 ? 145.059 117.541 123.049 1.00 47.04 1  266 LYS A NZ    1 
ATOM   2144  N  N     . ILE A 1 267 ? 137.361 117.550 121.535 1.00 57.94 ?  267 ILE A N     1 
ATOM   2145  C  CA    . ILE A 1 267 ? 136.079 116.990 121.955 1.00 59.55 ?  267 ILE A CA    1 
ATOM   2146  C  C     . ILE A 1 267 ? 136.123 116.604 123.428 1.00 59.12 ?  267 ILE A C     1 
ATOM   2147  O  O     . ILE A 1 267 ? 135.127 116.738 124.150 1.00 57.17 ?  267 ILE A O     1 
ATOM   2148  C  CB    . ILE A 1 267 ? 135.702 115.792 121.065 1.00 59.00 ?  267 ILE A CB    1 
ATOM   2149  C  CG1   . ILE A 1 267 ? 135.464 116.250 119.624 1.00 59.81 ?  267 ILE A CG1   1 
ATOM   2150  C  CG2   . ILE A 1 267 ? 134.471 115.090 121.617 1.00 57.14 ?  267 ILE A CG2   1 
ATOM   2151  C  CD1   . ILE A 1 267 ? 136.638 116.002 118.700 1.00 59.86 ?  267 ILE A CD1   1 
ATOM   2152  N  N     . SER A 1 268 ? 137.274 116.120 123.899 1.00 60.20 ?  268 SER A N     1 
ATOM   2153  C  CA    . SER A 1 268 ? 137.421 115.712 125.291 1.00 63.53 ?  268 SER A CA    1 
ATOM   2154  C  C     . SER A 1 268 ? 137.480 116.891 126.255 1.00 64.19 ?  268 SER A C     1 
ATOM   2155  O  O     . SER A 1 268 ? 137.468 116.670 127.471 1.00 63.68 ?  268 SER A O     1 
ATOM   2156  C  CB    . SER A 1 268 ? 138.676 114.854 125.454 1.00 63.60 ?  268 SER A CB    1 
ATOM   2157  O  OG    . SER A 1 268 ? 139.834 115.562 125.046 1.00 62.10 ?  268 SER A OG    1 
ATOM   2158  N  N     . ALA A 1 269 ? 137.552 118.120 125.751 1.00 66.10 ?  269 ALA A N     1 
ATOM   2159  C  CA    . ALA A 1 269 ? 137.636 119.286 126.619 1.00 65.74 ?  269 ALA A CA    1 
ATOM   2160  C  C     . ALA A 1 269 ? 136.376 119.425 127.466 1.00 66.79 ?  269 ALA A C     1 
ATOM   2161  O  O     . ALA A 1 269 ? 135.265 119.114 127.028 1.00 64.71 ?  269 ALA A O     1 
ATOM   2162  C  CB    . ALA A 1 269 ? 137.849 120.554 125.790 1.00 61.65 ?  269 ALA A CB    1 
ATOM   2163  N  N     . ASP A 1 270 ? 136.561 119.899 128.696 1.00 73.17 ?  270 ASP A N     1 
ATOM   2164  C  CA    . ASP A 1 270 ? 135.451 120.068 129.617 1.00 73.06 ?  270 ASP A CA    1 
ATOM   2165  C  C     . ASP A 1 270 ? 134.600 121.274 129.217 1.00 73.22 ?  270 ASP A C     1 
ATOM   2166  O  O     . ASP A 1 270 ? 134.937 122.040 128.309 1.00 73.93 ?  270 ASP A O     1 
ATOM   2167  C  CB    . ASP A 1 270 ? 135.960 120.229 131.048 1.00 73.27 ?  270 ASP A CB    1 
ATOM   2168  C  CG    . ASP A 1 270 ? 137.079 119.262 131.380 1.00 74.95 ?  270 ASP A CG    1 
ATOM   2169  O  OD1   . ASP A 1 270 ? 137.087 118.146 130.820 1.00 74.46 ?  270 ASP A OD1   1 
ATOM   2170  O  OD2   . ASP A 1 270 ? 137.949 119.617 132.203 1.00 73.37 -1 270 ASP A OD2   1 
ATOM   2171  N  N     . GLU A 1 271 ? 133.476 121.436 129.919 1.00 74.54 ?  271 GLU A N     1 
ATOM   2172  C  CA    . GLU A 1 271 ? 132.556 122.526 129.608 1.00 75.66 ?  271 GLU A CA    1 
ATOM   2173  C  C     . GLU A 1 271 ? 133.153 123.888 129.943 1.00 75.28 ?  271 GLU A C     1 
ATOM   2174  O  O     . GLU A 1 271 ? 132.787 124.891 129.320 1.00 74.37 ?  271 GLU A O     1 
ATOM   2175  C  CB    . GLU A 1 271 ? 131.237 122.327 130.353 1.00 74.59 ?  271 GLU A CB    1 
ATOM   2176  C  CG    . GLU A 1 271 ? 130.540 121.010 130.043 1.00 75.40 ?  271 GLU A CG    1 
ATOM   2177  C  CD    . GLU A 1 271 ? 130.504 120.700 128.559 1.00 76.58 ?  271 GLU A CD    1 
ATOM   2178  O  OE1   . GLU A 1 271 ? 130.084 121.577 127.773 1.00 75.75 ?  271 GLU A OE1   1 
ATOM   2179  O  OE2   . GLU A 1 271 ? 130.898 119.579 128.175 1.00 74.84 -1 271 GLU A OE2   1 
ATOM   2180  N  N     . ASP A 1 272 ? 134.062 123.947 130.912 1.00 69.39 ?  272 ASP A N     1 
ATOM   2181  C  CA    . ASP A 1 272 ? 134.725 125.192 131.275 1.00 70.33 ?  272 ASP A CA    1 
ATOM   2182  C  C     . ASP A 1 272 ? 135.956 125.473 130.424 1.00 70.67 ?  272 ASP A C     1 
ATOM   2183  O  O     . ASP A 1 272 ? 136.644 126.469 130.665 1.00 68.52 ?  272 ASP A O     1 
ATOM   2184  C  CB    . ASP A 1 272 ? 135.112 125.175 132.758 1.00 70.43 ?  272 ASP A CB    1 
ATOM   2185  C  CG    . ASP A 1 272 ? 136.173 124.138 133.075 1.00 71.48 ?  272 ASP A CG    1 
ATOM   2186  O  OD1   . ASP A 1 272 ? 136.275 123.141 132.331 1.00 70.47 ?  272 ASP A OD1   1 
ATOM   2187  O  OD2   . ASP A 1 272 ? 136.906 124.322 134.069 1.00 70.07 -1 272 ASP A OD2   1 
ATOM   2188  N  N     . VAL A 1 273 ? 136.256 124.614 129.448 1.00 65.21 ?  273 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 273 ? 137.401 124.784 128.568 1.00 64.67 ?  273 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 273 ? 136.978 124.990 127.120 1.00 62.53 ?  273 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 273 ? 137.540 125.839 126.418 1.00 65.25 ?  273 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 273 ? 138.370 123.586 128.685 1.00 66.28 ?  273 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 273 ? 139.416 123.622 127.580 1.00 63.57 ?  273 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 273 ? 139.031 123.569 130.053 1.00 64.79 ?  273 VAL A CG2   1 
ATOM   2195  N  N     . ARG A 1 274 ? 135.977 124.246 126.658 1.00 60.44 ?  274 ARG A N     1 
ATOM   2196  C  CA    . ARG A 1 274 ? 135.599 124.255 125.252 1.00 59.82 ?  274 ARG A CA    1 
ATOM   2197  C  C     . ARG A 1 274 ? 134.714 125.454 124.931 1.00 58.10 ?  274 ARG A C     1 
ATOM   2198  O  O     . ARG A 1 274 ? 133.778 125.764 125.674 1.00 58.12 ?  274 ARG A O     1 
ATOM   2199  C  CB    . ARG A 1 274 ? 134.873 122.957 124.896 1.00 59.95 ?  274 ARG A CB    1 
ATOM   2200  C  CG    . ARG A 1 274 ? 134.008 123.044 123.650 1.00 58.60 ?  274 ARG A CG    1 
ATOM   2201  C  CD    . ARG A 1 274 ? 133.848 121.687 122.985 1.00 58.80 ?  274 ARG A CD    1 
ATOM   2202  N  NE    . ARG A 1 274 ? 133.563 120.631 123.949 1.00 62.16 ?  274 ARG A NE    1 
ATOM   2203  C  CZ    . ARG A 1 274 ? 132.384 120.440 124.527 1.00 63.53 ?  274 ARG A CZ    1 
ATOM   2204  N  NH1   . ARG A 1 274 ? 131.347 121.217 124.256 1.00 62.50 1  274 ARG A NH1   1 
ATOM   2205  N  NH2   . ARG A 1 274 ? 132.241 119.443 125.395 1.00 63.03 ?  274 ARG A NH2   1 
ATOM   2206  N  N     . VAL A 1 275 ? 135.015 126.125 123.821 1.00 47.64 ?  275 VAL A N     1 
ATOM   2207  C  CA    . VAL A 1 275 ? 134.172 127.176 123.263 1.00 44.89 ?  275 VAL A CA    1 
ATOM   2208  C  C     . VAL A 1 275 ? 133.563 126.645 121.972 1.00 45.72 ?  275 VAL A C     1 
ATOM   2209  O  O     . VAL A 1 275 ? 134.280 126.138 121.102 1.00 47.61 ?  275 VAL A O     1 
ATOM   2210  C  CB    . VAL A 1 275 ? 134.965 128.474 123.022 1.00 44.54 ?  275 VAL A CB    1 
ATOM   2211  C  CG1   . VAL A 1 275 ? 135.244 129.173 124.343 1.00 42.69 ?  275 VAL A CG1   1 
ATOM   2212  C  CG2   . VAL A 1 275 ? 136.271 128.185 122.300 1.00 44.81 ?  275 VAL A CG2   1 
ATOM   2213  N  N     . LYS A 1 276 ? 132.240 126.746 121.855 1.00 46.73 ?  276 LYS A N     1 
ATOM   2214  C  CA    . LYS A 1 276 ? 131.523 126.099 120.763 1.00 47.97 ?  276 LYS A CA    1 
ATOM   2215  C  C     . LYS A 1 276 ? 131.216 127.022 119.593 1.00 47.05 ?  276 LYS A C     1 
ATOM   2216  O  O     . LYS A 1 276 ? 131.276 126.577 118.442 1.00 52.80 ?  276 LYS A O     1 
ATOM   2217  C  CB    . LYS A 1 276 ? 130.213 125.492 121.279 1.00 49.01 ?  276 LYS A CB    1 
ATOM   2218  C  CG    . LYS A 1 276 ? 129.357 126.449 122.095 1.00 52.48 ?  276 LYS A CG    1 
ATOM   2219  C  CD    . LYS A 1 276 ? 128.229 125.721 122.810 1.00 50.48 ?  276 LYS A CD    1 
ATOM   2220  C  CE    . LYS A 1 276 ? 128.734 124.474 123.520 1.00 49.46 ?  276 LYS A CE    1 
ATOM   2221  N  NZ    . LYS A 1 276 ? 129.811 124.789 124.501 1.00 48.12 1  276 LYS A NZ    1 
ATOM   2222  N  N     . THR A 1 277 ? 130.891 128.287 119.846 1.00 38.15 ?  277 THR A N     1 
ATOM   2223  C  CA    . THR A 1 277 ? 130.562 129.230 118.787 1.00 38.69 ?  277 THR A CA    1 
ATOM   2224  C  C     . THR A 1 277 ? 131.711 130.171 118.459 1.00 42.36 ?  277 THR A C     1 
ATOM   2225  O  O     . THR A 1 277 ? 131.503 131.168 117.762 1.00 41.83 ?  277 THR A O     1 
ATOM   2226  C  CB    . THR A 1 277 ? 129.317 130.036 119.162 1.00 41.43 ?  277 THR A CB    1 
ATOM   2227  O  OG1   . THR A 1 277 ? 129.664 131.036 120.129 1.00 35.00 ?  277 THR A OG1   1 
ATOM   2228  C  CG2   . THR A 1 277 ? 128.246 129.122 119.735 1.00 41.22 ?  277 THR A CG2   1 
ATOM   2229  N  N     . LEU A 1 278 ? 132.914 129.883 118.946 1.00 33.87 ?  278 LEU A N     1 
ATOM   2230  C  CA    . LEU A 1 278 ? 134.088 130.712 118.700 1.00 31.20 ?  278 LEU A CA    1 
ATOM   2231  C  C     . LEU A 1 278 ? 135.081 129.916 117.866 1.00 25.43 ?  278 LEU A C     1 
ATOM   2232  O  O     . LEU A 1 278 ? 135.725 128.992 118.372 1.00 34.43 ?  278 LEU A O     1 
ATOM   2233  C  CB    . LEU A 1 278 ? 134.721 131.165 120.014 1.00 28.77 ?  278 LEU A CB    1 
ATOM   2234  C  CG    . LEU A 1 278 ? 135.714 132.323 119.921 1.00 25.02 ?  278 LEU A CG    1 
ATOM   2235  C  CD1   . LEU A 1 278 ? 134.984 133.648 119.809 1.00 24.11 ?  278 LEU A CD1   1 
ATOM   2236  C  CD2   . LEU A 1 278 ? 136.646 132.324 121.119 1.00 31.95 ?  278 LEU A CD2   1 
ATOM   2237  N  N     . SER A 1 279 ? 135.201 130.272 116.592 1.00 26.11 ?  279 SER A N     1 
ATOM   2238  C  CA    . SER A 1 279 ? 136.243 129.703 115.753 1.00 21.19 ?  279 SER A CA    1 
ATOM   2239  C  C     . SER A 1 279 ? 137.612 130.148 116.251 1.00 20.60 ?  279 SER A C     1 
ATOM   2240  O  O     . SER A 1 279 ? 137.756 131.202 116.875 1.00 33.10 ?  279 SER A O     1 
ATOM   2241  C  CB    . SER A 1 279 ? 136.051 130.127 114.299 1.00 17.65 ?  279 SER A CB    1 
ATOM   2242  O  OG    . SER A 1 279 ? 134.902 129.518 113.737 1.00 25.68 ?  279 SER A OG    1 
ATOM   2243  N  N     . ILE A 1 280 ? 138.624 129.330 115.986 1.00 18.70 ?  280 ILE A N     1 
ATOM   2244  C  CA    . ILE A 1 280 ? 139.981 129.629 116.420 1.00 22.67 ?  280 ILE A CA    1 
ATOM   2245  C  C     . ILE A 1 280 ? 140.914 129.574 115.222 1.00 23.14 ?  280 ILE A C     1 
ATOM   2246  O  O     . ILE A 1 280 ? 140.748 128.738 114.327 1.00 26.18 ?  280 ILE A O     1 
ATOM   2247  C  CB    . ILE A 1 280 ? 140.464 128.676 117.535 1.00 17.83 ?  280 ILE A CB    1 
ATOM   2248  C  CG1   . ILE A 1 280 ? 140.519 127.231 117.046 1.00 23.84 ?  280 ILE A CG1   1 
ATOM   2249  C  CG2   . ILE A 1 280 ? 139.574 128.799 118.759 1.00 20.13 ?  280 ILE A CG2   1 
ATOM   2250  C  CD1   . ILE A 1 280 ? 141.524 126.385 117.798 1.00 18.96 ?  280 ILE A CD1   1 
ATOM   2251  N  N     . GLY A 1 281 ? 141.870 130.490 115.192 1.00 13.73 ?  281 GLY A N     1 
ATOM   2252  C  CA    . GLY A 1 281 ? 142.924 130.459 114.203 1.00 4.47  ?  281 GLY A CA    1 
ATOM   2253  C  C     . GLY A 1 281 ? 144.270 130.636 114.872 1.00 10.46 ?  281 GLY A C     1 
ATOM   2254  O  O     . GLY A 1 281 ? 144.395 131.305 115.896 1.00 18.34 ?  281 GLY A O     1 
ATOM   2255  N  N     . VAL A 1 282 ? 145.283 130.014 114.279 1.00 15.23 ?  282 VAL A N     1 
ATOM   2256  C  CA    . VAL A 1 282 ? 146.641 130.044 114.805 1.00 12.71 ?  282 VAL A CA    1 
ATOM   2257  C  C     . VAL A 1 282 ? 147.532 130.755 113.800 1.00 13.55 ?  282 VAL A C     1 
ATOM   2258  O  O     . VAL A 1 282 ? 147.508 130.441 112.604 1.00 17.64 ?  282 VAL A O     1 
ATOM   2259  C  CB    . VAL A 1 282 ? 147.163 128.628 115.107 1.00 14.51 ?  282 VAL A CB    1 
ATOM   2260  C  CG1   . VAL A 1 282 ? 148.656 128.654 115.365 1.00 19.00 ?  282 VAL A CG1   1 
ATOM   2261  C  CG2   . VAL A 1 282 ? 146.438 128.057 116.307 1.00 19.47 ?  282 VAL A CG2   1 
ATOM   2262  N  N     . VAL A 1 283 ? 148.305 131.721 114.284 1.00 12.13 ?  283 VAL A N     1 
ATOM   2263  C  CA    . VAL A 1 283 ? 149.267 132.445 113.463 1.00 11.66 ?  283 VAL A CA    1 
ATOM   2264  C  C     . VAL A 1 283 ? 150.627 131.785 113.638 1.00 16.58 ?  283 VAL A C     1 
ATOM   2265  O  O     . VAL A 1 283 ? 151.146 131.700 114.755 1.00 25.42 ?  283 VAL A O     1 
ATOM   2266  C  CB    . VAL A 1 283 ? 149.316 133.930 113.851 1.00 11.36 ?  283 VAL A CB    1 
ATOM   2267  C  CG1   . VAL A 1 283 ? 150.142 134.709 112.850 1.00 9.15  ?  283 VAL A CG1   1 
ATOM   2268  C  CG2   . VAL A 1 283 ? 147.906 134.489 113.941 1.00 14.54 ?  283 VAL A CG2   1 
ATOM   2269  N  N     . ILE A 1 284 ? 151.204 131.320 112.539 1.00 14.52 ?  284 ILE A N     1 
ATOM   2270  C  CA    . ILE A 1 284 ? 152.438 130.549 112.554 1.00 14.52 ?  284 ILE A CA    1 
ATOM   2271  C  C     . ILE A 1 284 ? 153.517 131.347 111.835 1.00 18.20 ?  284 ILE A C     1 
ATOM   2272  O  O     . ILE A 1 284 ? 153.544 131.406 110.605 1.00 20.15 ?  284 ILE A O     1 
ATOM   2273  C  CB    . ILE A 1 284 ? 152.247 129.166 111.907 1.00 16.43 ?  284 ILE A CB    1 
ATOM   2274  C  CG1   . ILE A 1 284 ? 151.144 128.391 112.629 1.00 16.93 ?  284 ILE A CG1   1 
ATOM   2275  C  CG2   . ILE A 1 284 ? 153.549 128.383 111.926 1.00 17.23 ?  284 ILE A CG2   1 
ATOM   2276  C  CD1   . ILE A 1 284 ? 150.993 126.963 112.160 1.00 19.37 ?  284 ILE A CD1   1 
ATOM   2277  N  N     . PRO A 1 285 ? 154.424 131.981 112.572 1.00 27.08 ?  285 PRO A N     1 
ATOM   2278  C  CA    . PRO A 1 285 ? 155.562 132.647 111.931 1.00 25.81 ?  285 PRO A CA    1 
ATOM   2279  C  C     . PRO A 1 285 ? 156.523 131.633 111.328 1.00 23.52 ?  285 PRO A C     1 
ATOM   2280  O  O     . PRO A 1 285 ? 156.485 130.438 111.628 1.00 25.24 ?  285 PRO A O     1 
ATOM   2281  C  CB    . PRO A 1 285 ? 156.220 133.422 113.078 1.00 19.49 ?  285 PRO A CB    1 
ATOM   2282  C  CG    . PRO A 1 285 ? 155.184 133.483 114.158 1.00 17.59 ?  285 PRO A CG    1 
ATOM   2283  C  CD    . PRO A 1 285 ? 154.388 132.228 114.021 1.00 21.54 ?  285 PRO A CD    1 
ATOM   2284  N  N     . ASP A 1 286 ? 157.396 132.136 110.450 1.00 26.51 ?  286 ASP A N     1 
ATOM   2285  C  CA    . ASP A 1 286 ? 158.384 131.269 109.817 1.00 24.40 ?  286 ASP A CA    1 
ATOM   2286  C  C     . ASP A 1 286 ? 159.325 130.648 110.839 1.00 29.80 ?  286 ASP A C     1 
ATOM   2287  O  O     . ASP A 1 286 ? 159.885 129.574 110.590 1.00 32.08 ?  286 ASP A O     1 
ATOM   2288  C  CB    . ASP A 1 286 ? 159.186 132.049 108.776 1.00 24.91 ?  286 ASP A CB    1 
ATOM   2289  C  CG    . ASP A 1 286 ? 158.659 131.855 107.371 1.00 36.92 ?  286 ASP A CG    1 
ATOM   2290  O  OD1   . ASP A 1 286 ? 157.525 131.355 107.226 1.00 36.04 ?  286 ASP A OD1   1 
ATOM   2291  O  OD2   . ASP A 1 286 ? 159.378 132.205 106.411 1.00 39.10 -1 286 ASP A OD2   1 
ATOM   2292  N  N     . LYS A 1 287 ? 159.519 131.304 111.985 1.00 30.46 ?  287 LYS A N     1 
ATOM   2293  C  CA    . LYS A 1 287 ? 160.414 130.768 113.004 1.00 28.00 ?  287 LYS A CA    1 
ATOM   2294  C  C     . LYS A 1 287 ? 159.911 129.433 113.537 1.00 29.31 ?  287 LYS A C     1 
ATOM   2295  O  O     . LYS A 1 287 ? 160.703 128.511 113.766 1.00 36.10 ?  287 LYS A O     1 
ATOM   2296  C  CB    . LYS A 1 287 ? 160.577 131.774 114.144 1.00 31.50 ?  287 LYS A CB    1 
ATOM   2297  C  CG    . LYS A 1 287 ? 161.694 131.423 115.110 1.00 27.46 ?  287 LYS A CG    1 
ATOM   2298  C  CD    . LYS A 1 287 ? 162.976 131.107 114.360 1.00 30.56 ?  287 LYS A CD    1 
ATOM   2299  C  CE    . LYS A 1 287 ? 164.150 130.952 115.306 1.00 31.46 ?  287 LYS A CE    1 
ATOM   2300  N  NZ    . LYS A 1 287 ? 165.428 130.753 114.570 1.00 34.93 1  287 LYS A NZ    1 
ATOM   2301  N  N     . PHE A 1 288 ? 158.599 129.309 113.745 1.00 24.06 ?  288 PHE A N     1 
ATOM   2302  C  CA    . PHE A 1 288 ? 158.043 128.041 114.208 1.00 24.02 ?  288 PHE A CA    1 
ATOM   2303  C  C     . PHE A 1 288 ? 158.262 126.938 113.182 1.00 24.75 ?  288 PHE A C     1 
ATOM   2304  O  O     . PHE A 1 288 ? 158.587 125.799 113.541 1.00 36.24 ?  288 PHE A O     1 
ATOM   2305  C  CB    . PHE A 1 288 ? 156.554 128.200 114.515 1.00 25.06 ?  288 PHE A CB    1 
ATOM   2306  C  CG    . PHE A 1 288 ? 155.917 126.959 115.072 1.00 26.56 ?  288 PHE A CG    1 
ATOM   2307  C  CD1   . PHE A 1 288 ? 156.005 126.667 116.422 1.00 27.58 ?  288 PHE A CD1   1 
ATOM   2308  C  CD2   . PHE A 1 288 ? 155.231 126.086 114.246 1.00 22.72 ?  288 PHE A CD2   1 
ATOM   2309  C  CE1   . PHE A 1 288 ? 155.421 125.527 116.937 1.00 26.22 ?  288 PHE A CE1   1 
ATOM   2310  C  CE2   . PHE A 1 288 ? 154.646 124.944 114.755 1.00 24.98 ?  288 PHE A CE2   1 
ATOM   2311  C  CZ    . PHE A 1 288 ? 154.740 124.665 116.102 1.00 29.33 ?  288 PHE A CZ    1 
ATOM   2312  N  N     . VAL A 1 289 ? 158.088 127.255 111.898 1.00 24.93 ?  289 VAL A N     1 
ATOM   2313  C  CA    . VAL A 1 289 ? 158.286 126.255 110.857 1.00 28.22 ?  289 VAL A CA    1 
ATOM   2314  C  C     . VAL A 1 289 ? 159.753 125.853 110.774 1.00 29.88 ?  289 VAL A C     1 
ATOM   2315  O  O     . VAL A 1 289 ? 160.076 124.682 110.550 1.00 33.12 ?  289 VAL A O     1 
ATOM   2316  C  CB    . VAL A 1 289 ? 157.760 126.776 109.507 1.00 31.83 ?  289 VAL A CB    1 
ATOM   2317  C  CG1   . VAL A 1 289 ? 157.712 125.653 108.486 1.00 25.97 ?  289 VAL A CG1   1 
ATOM   2318  C  CG2   . VAL A 1 289 ? 156.387 127.405 109.682 1.00 26.24 ?  289 VAL A CG2   1 
ATOM   2319  N  N     . GLU A 1 290 ? 160.665 126.814 110.950 1.00 33.29 ?  290 GLU A N     1 
ATOM   2320  C  CA    . GLU A 1 290 ? 162.088 126.486 110.965 1.00 32.38 ?  290 GLU A CA    1 
ATOM   2321  C  C     . GLU A 1 290 ? 162.438 125.602 112.155 1.00 35.00 ?  290 GLU A C     1 
ATOM   2322  O  O     . GLU A 1 290 ? 163.223 124.656 112.025 1.00 41.47 ?  290 GLU A O     1 
ATOM   2323  C  CB    . GLU A 1 290 ? 162.927 127.764 110.984 1.00 33.41 ?  290 GLU A CB    1 
ATOM   2324  C  CG    . GLU A 1 290 ? 163.084 128.434 109.629 1.00 38.34 ?  290 GLU A CG    1 
ATOM   2325  C  CD    . GLU A 1 290 ? 162.709 129.902 109.654 1.00 39.81 ?  290 GLU A CD    1 
ATOM   2326  O  OE1   . GLU A 1 290 ? 162.065 130.369 108.691 1.00 38.86 ?  290 GLU A OE1   1 
ATOM   2327  O  OE2   . GLU A 1 290 ? 163.057 130.591 110.636 1.00 40.07 -1 290 GLU A OE2   1 
ATOM   2328  N  N     . LEU A 1 291 ? 161.872 125.902 113.326 1.00 32.62 ?  291 LEU A N     1 
ATOM   2329  C  CA    . LEU A 1 291 ? 162.142 125.091 114.509 1.00 29.33 ?  291 LEU A CA    1 
ATOM   2330  C  C     . LEU A 1 291 ? 161.608 123.674 114.344 1.00 32.32 ?  291 LEU A C     1 
ATOM   2331  O  O     . LEU A 1 291 ? 162.278 122.706 114.720 1.00 39.75 ?  291 LEU A O     1 
ATOM   2332  C  CB    . LEU A 1 291 ? 161.537 125.753 115.747 1.00 31.03 ?  291 LEU A CB    1 
ATOM   2333  C  CG    . LEU A 1 291 ? 162.200 127.054 116.198 1.00 32.77 ?  291 LEU A CG    1 
ATOM   2334  C  CD1   . LEU A 1 291 ? 161.260 127.857 117.080 1.00 27.11 ?  291 LEU A CD1   1 
ATOM   2335  C  CD2   . LEU A 1 291 ? 163.505 126.768 116.917 1.00 32.96 ?  291 LEU A CD2   1 
ATOM   2336  N  N     . ALA A 1 292 ? 160.402 123.533 113.790 1.00 33.22 ?  292 ALA A N     1 
ATOM   2337  C  CA    . ALA A 1 292 ? 159.851 122.203 113.550 1.00 31.63 ?  292 ALA A CA    1 
ATOM   2338  C  C     . ALA A 1 292 ? 160.658 121.451 112.499 1.00 32.39 ?  292 ALA A C     1 
ATOM   2339  O  O     . ALA A 1 292 ? 160.872 120.239 112.620 1.00 37.80 ?  292 ALA A O     1 
ATOM   2340  C  CB    . ALA A 1 292 ? 158.386 122.309 113.132 1.00 30.62 ?  292 ALA A CB    1 
ATOM   2341  N  N     . ARG A 1 293 ? 161.110 122.155 111.458 1.00 34.05 ?  293 ARG A N     1 
ATOM   2342  C  CA    . ARG A 1 293 ? 161.873 121.518 110.390 1.00 33.45 ?  293 ARG A CA    1 
ATOM   2343  C  C     . ARG A 1 293 ? 163.191 120.956 110.904 1.00 39.26 ?  293 ARG A C     1 
ATOM   2344  O  O     . ARG A 1 293 ? 163.582 119.840 110.541 1.00 43.88 ?  293 ARG A O     1 
ATOM   2345  C  CB    . ARG A 1 293 ? 162.116 122.524 109.266 1.00 34.13 ?  293 ARG A CB    1 
ATOM   2346  C  CG    . ARG A 1 293 ? 162.964 122.010 108.121 1.00 34.36 ?  293 ARG A CG    1 
ATOM   2347  C  CD    . ARG A 1 293 ? 163.358 123.149 107.198 1.00 38.71 ?  293 ARG A CD    1 
ATOM   2348  N  NE    . ARG A 1 293 ? 162.233 124.040 106.941 1.00 40.23 ?  293 ARG A NE    1 
ATOM   2349  C  CZ    . ARG A 1 293 ? 162.288 125.362 107.034 1.00 39.33 ?  293 ARG A CZ    1 
ATOM   2350  N  NH1   . ARG A 1 293 ? 163.407 125.986 107.362 1.00 37.97 1  293 ARG A NH1   1 
ATOM   2351  N  NH2   . ARG A 1 293 ? 161.192 126.075 106.793 1.00 35.71 ?  293 ARG A NH2   1 
ATOM   2352  N  N     . GLU A 1 294 ? 163.888 121.710 111.749 1.00 41.45 ?  294 GLU A N     1 
ATOM   2353  C  CA    . GLU A 1 294 ? 165.157 121.266 112.311 1.00 39.06 ?  294 GLU A CA    1 
ATOM   2354  C  C     . GLU A 1 294 ? 164.984 120.410 113.557 1.00 40.16 ?  294 GLU A C     1 
ATOM   2355  O  O     . GLU A 1 294 ? 165.988 119.975 114.131 1.00 42.64 ?  294 GLU A O     1 
ATOM   2356  C  CB    . GLU A 1 294 ? 166.036 122.476 112.636 1.00 39.21 ?  294 GLU A CB    1 
ATOM   2357  C  CG    . GLU A 1 294 ? 166.658 123.136 111.417 1.00 41.33 ?  294 GLU A CG    1 
ATOM   2358  C  CD    . GLU A 1 294 ? 166.344 124.615 111.334 1.00 44.89 ?  294 GLU A CD    1 
ATOM   2359  O  OE1   . GLU A 1 294 ? 166.211 125.256 112.398 1.00 45.92 ?  294 GLU A OE1   1 
ATOM   2360  O  OE2   . GLU A 1 294 ? 166.229 125.138 110.206 1.00 46.51 -1 294 GLU A OE2   1 
ATOM   2361  N  N     . ASP A 1 295 ? 163.746 120.177 113.991 1.00 38.72 ?  295 ASP A N     1 
ATOM   2362  C  CA    . ASP A 1 295 ? 163.401 119.380 115.165 1.00 37.97 ?  295 ASP A CA    1 
ATOM   2363  C  C     . ASP A 1 295 ? 163.929 119.975 116.464 1.00 44.50 ?  295 ASP A C     1 
ATOM   2364  O  O     . ASP A 1 295 ? 163.881 119.313 117.506 1.00 44.19 ?  295 ASP A O     1 
ATOM   2365  C  CB    . ASP A 1 295 ? 163.882 117.929 115.027 1.00 40.78 ?  295 ASP A CB    1 
ATOM   2366  C  CG    . ASP A 1 295 ? 162.851 116.925 115.504 1.00 44.89 ?  295 ASP A CG    1 
ATOM   2367  O  OD1   . ASP A 1 295 ? 161.896 117.336 116.195 1.00 46.03 ?  295 ASP A OD1   1 
ATOM   2368  O  OD2   . ASP A 1 295 ? 162.998 115.726 115.189 1.00 42.65 -1 295 ASP A OD2   1 
ATOM   2369  N  N     . LYS A 1 296 ? 164.432 121.207 116.434 1.00 43.47 ?  296 LYS A N     1 
ATOM   2370  C  CA    . LYS A 1 296 ? 164.836 121.874 117.663 1.00 41.60 ?  296 LYS A CA    1 
ATOM   2371  C  C     . LYS A 1 296 ? 163.613 122.181 118.514 1.00 41.53 ?  296 LYS A C     1 
ATOM   2372  O  O     . LYS A 1 296 ? 162.568 122.588 118.001 1.00 45.89 ?  296 LYS A O     1 
ATOM   2373  C  CB    . LYS A 1 296 ? 165.592 123.166 117.354 1.00 42.27 ?  296 LYS A CB    1 
ATOM   2374  C  CG    . LYS A 1 296 ? 166.730 123.015 116.364 1.00 44.14 ?  296 LYS A CG    1 
ATOM   2375  C  CD    . LYS A 1 296 ? 166.940 124.301 115.583 1.00 42.91 ?  296 LYS A CD    1 
ATOM   2376  C  CE    . LYS A 1 296 ? 168.414 124.643 115.467 1.00 43.56 ?  296 LYS A CE    1 
ATOM   2377  N  NZ    . LYS A 1 296 ? 169.167 123.606 114.709 1.00 44.16 1  296 LYS A NZ    1 
ATOM   2378  N  N     . ALA A 1 297 ? 163.744 121.981 119.821 1.00 40.88 ?  297 ALA A N     1 
ATOM   2379  C  CA    . ALA A 1 297 ? 162.653 122.296 120.729 1.00 42.43 ?  297 ALA A CA    1 
ATOM   2380  C  C     . ALA A 1 297 ? 162.406 123.799 120.755 1.00 40.42 ?  297 ALA A C     1 
ATOM   2381  O  O     . ALA A 1 297 ? 163.342 124.598 120.835 1.00 41.09 ?  297 ALA A O     1 
ATOM   2382  C  CB    . ALA A 1 297 ? 162.965 121.787 122.133 1.00 37.53 ?  297 ALA A CB    1 
ATOM   2383  N  N     . ALA A 1 298 ? 161.135 124.181 120.689 1.00 35.05 ?  298 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 298 ? 160.751 125.578 120.627 1.00 34.96 ?  298 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 298 ? 160.351 126.074 122.012 1.00 35.60 ?  298 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 298 ? 160.242 125.309 122.973 1.00 39.04 ?  298 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 298 ? 159.615 125.776 119.622 1.00 33.74 ?  298 ALA A CB    1 
ATOM   2388  N  N     . TYR A 1 299 ? 160.120 127.379 122.110 1.00 33.59 ?  299 TYR A N     1 
ATOM   2389  C  CA    . TYR A 1 299 ? 159.696 128.004 123.353 1.00 27.91 ?  299 TYR A CA    1 
ATOM   2390  C  C     . TYR A 1 299 ? 158.448 128.830 123.093 1.00 29.08 ?  299 TYR A C     1 
ATOM   2391  O  O     . TYR A 1 299 ? 158.411 129.622 122.147 1.00 30.35 ?  299 TYR A O     1 
ATOM   2392  C  CB    . TYR A 1 299 ? 160.804 128.886 123.936 1.00 29.77 ?  299 TYR A CB    1 
ATOM   2393  C  CG    . TYR A 1 299 ? 161.930 128.108 124.572 1.00 31.98 ?  299 TYR A CG    1 
ATOM   2394  C  CD1   . TYR A 1 299 ? 161.817 127.614 125.864 1.00 34.99 ?  299 TYR A CD1   1 
ATOM   2395  C  CD2   . TYR A 1 299 ? 163.106 127.862 123.877 1.00 32.52 ?  299 TYR A CD2   1 
ATOM   2396  C  CE1   . TYR A 1 299 ? 162.845 126.900 126.447 1.00 35.03 ?  299 TYR A CE1   1 
ATOM   2397  C  CE2   . TYR A 1 299 ? 164.138 127.150 124.450 1.00 33.28 ?  299 TYR A CE2   1 
ATOM   2398  C  CZ    . TYR A 1 299 ? 164.003 126.671 125.735 1.00 35.74 ?  299 TYR A CZ    1 
ATOM   2399  O  OH    . TYR A 1 299 ? 165.029 125.960 126.312 1.00 39.40 ?  299 TYR A OH    1 
ATOM   2400  N  N     . VAL A 1 300 ? 157.432 128.638 123.925 1.00 32.74 ?  300 VAL A N     1 
ATOM   2401  C  CA    . VAL A 1 300 ? 156.244 129.484 123.922 1.00 27.48 ?  300 VAL A CA    1 
ATOM   2402  C  C     . VAL A 1 300 ? 156.400 130.502 125.040 1.00 28.99 ?  300 VAL A C     1 
ATOM   2403  O  O     . VAL A 1 300 ? 156.697 130.139 126.184 1.00 35.40 ?  300 VAL A O     1 
ATOM   2404  C  CB    . VAL A 1 300 ? 154.958 128.656 124.087 1.00 25.59 ?  300 VAL A CB    1 
ATOM   2405  C  CG1   . VAL A 1 300 ? 154.574 128.008 122.766 1.00 26.29 ?  300 VAL A CG1   1 
ATOM   2406  C  CG2   . VAL A 1 300 ? 155.126 127.606 125.173 1.00 28.34 ?  300 VAL A CG2   1 
ATOM   2407  N  N     . PHE A 1 301 ? 156.220 131.774 124.714 1.00 22.22 ?  301 PHE A N     1 
ATOM   2408  C  CA    . PHE A 1 301 ? 156.592 132.857 125.610 1.00 24.64 ?  301 PHE A CA    1 
ATOM   2409  C  C     . PHE A 1 301 ? 155.384 133.458 126.314 1.00 29.79 ?  301 PHE A C     1 
ATOM   2410  O  O     . PHE A 1 301 ? 154.264 133.446 125.799 1.00 32.59 ?  301 PHE A O     1 
ATOM   2411  C  CB    . PHE A 1 301 ? 157.342 133.949 124.846 1.00 23.17 ?  301 PHE A CB    1 
ATOM   2412  C  CG    . PHE A 1 301 ? 158.508 133.435 124.059 1.00 28.71 ?  301 PHE A CG    1 
ATOM   2413  C  CD1   . PHE A 1 301 ? 159.712 133.171 124.687 1.00 27.45 ?  301 PHE A CD1   1 
ATOM   2414  C  CD2   . PHE A 1 301 ? 158.401 133.201 122.699 1.00 27.89 ?  301 PHE A CD2   1 
ATOM   2415  C  CE1   . PHE A 1 301 ? 160.789 132.691 123.977 1.00 27.89 ?  301 PHE A CE1   1 
ATOM   2416  C  CE2   . PHE A 1 301 ? 159.479 132.722 121.982 1.00 26.73 ?  301 PHE A CE2   1 
ATOM   2417  C  CZ    . PHE A 1 301 ? 160.675 132.466 122.625 1.00 29.84 ?  301 PHE A CZ    1 
ATOM   2418  N  N     . TYR A 1 302 ? 155.633 133.977 127.514 1.00 27.90 ?  302 TYR A N     1 
ATOM   2419  C  CA    . TYR A 1 302 ? 154.646 134.751 128.249 1.00 24.69 ?  302 TYR A CA    1 
ATOM   2420  C  C     . TYR A 1 302 ? 154.651 136.175 127.712 1.00 28.70 ?  302 TYR A C     1 
ATOM   2421  O  O     . TYR A 1 302 ? 155.660 136.881 127.828 1.00 30.11 ?  302 TYR A O     1 
ATOM   2422  C  CB    . TYR A 1 302 ? 154.942 134.732 129.748 1.00 25.69 ?  302 TYR A CB    1 
ATOM   2423  C  CG    . TYR A 1 302 ? 154.661 133.406 130.417 1.00 28.28 ?  302 TYR A CG    1 
ATOM   2424  C  CD1   . TYR A 1 302 ? 155.482 132.309 130.204 1.00 27.90 ?  302 TYR A CD1   1 
ATOM   2425  C  CD2   . TYR A 1 302 ? 153.574 133.255 131.264 1.00 29.97 ?  302 TYR A CD2   1 
ATOM   2426  C  CE1   . TYR A 1 302 ? 155.226 131.099 130.817 1.00 26.48 ?  302 TYR A CE1   1 
ATOM   2427  C  CE2   . TYR A 1 302 ? 153.310 132.052 131.882 1.00 30.24 ?  302 TYR A CE2   1 
ATOM   2428  C  CZ    . TYR A 1 302 ? 154.141 130.978 131.660 1.00 33.79 ?  302 TYR A CZ    1 
ATOM   2429  O  OH    . TYR A 1 302 ? 153.879 129.774 132.271 1.00 34.01 ?  302 TYR A OH    1 
ATOM   2430  N  N     . PRO A 1 303 ? 153.552 136.620 127.103 1.00 24.50 ?  303 PRO A N     1 
ATOM   2431  C  CA    . PRO A 1 303 ? 153.561 137.931 126.434 1.00 21.46 ?  303 PRO A CA    1 
ATOM   2432  C  C     . PRO A 1 303 ? 153.828 139.102 127.361 1.00 28.11 ?  303 PRO A C     1 
ATOM   2433  O  O     . PRO A 1 303 ? 154.479 140.068 126.945 1.00 32.36 ?  303 PRO A O     1 
ATOM   2434  C  CB    . PRO A 1 303 ? 152.157 138.014 125.821 1.00 24.61 ?  303 PRO A CB    1 
ATOM   2435  C  CG    . PRO A 1 303 ? 151.705 136.602 125.721 1.00 26.14 ?  303 PRO A CG    1 
ATOM   2436  C  CD    . PRO A 1 303 ? 152.281 135.909 126.906 1.00 25.81 ?  303 PRO A CD    1 
ATOM   2437  N  N     . HIS A 1 304 ? 153.346 139.052 128.604 1.00 29.80 ?  304 HIS A N     1 
ATOM   2438  C  CA    . HIS A 1 304 ? 153.499 140.200 129.488 1.00 24.97 ?  304 HIS A CA    1 
ATOM   2439  C  C     . HIS A 1 304 ? 154.946 140.392 129.914 1.00 28.58 ?  304 HIS A C     1 
ATOM   2440  O  O     . HIS A 1 304 ? 155.392 141.530 130.078 1.00 36.19 ?  304 HIS A O     1 
ATOM   2441  C  CB    . HIS A 1 304 ? 152.600 140.055 130.714 1.00 28.66 ?  304 HIS A CB    1 
ATOM   2442  C  CG    . HIS A 1 304 ? 152.532 141.289 131.558 1.00 30.65 ?  304 HIS A CG    1 
ATOM   2443  N  ND1   . HIS A 1 304 ? 152.634 141.260 132.932 1.00 33.01 ?  304 HIS A ND1   1 
ATOM   2444  C  CD2   . HIS A 1 304 ? 152.375 142.592 131.220 1.00 29.10 ?  304 HIS A CD2   1 
ATOM   2445  C  CE1   . HIS A 1 304 ? 152.539 142.490 133.405 1.00 32.39 ?  304 HIS A CE1   1 
ATOM   2446  N  NE2   . HIS A 1 304 ? 152.382 143.317 132.387 1.00 30.65 ?  304 HIS A NE2   1 
ATOM   2447  N  N     . THR A 1 305 ? 155.691 139.300 130.105 1.00 29.10 ?  305 THR A N     1 
ATOM   2448  C  CA    . THR A 1 305 ? 157.109 139.428 130.425 1.00 32.57 ?  305 THR A CA    1 
ATOM   2449  C  C     . THR A 1 305 ? 157.877 140.060 129.270 1.00 27.80 ?  305 THR A C     1 
ATOM   2450  O  O     . THR A 1 305 ? 158.750 140.910 129.484 1.00 33.42 ?  305 THR A O     1 
ATOM   2451  C  CB    . THR A 1 305 ? 157.698 138.063 130.784 1.00 31.42 ?  305 THR A CB    1 
ATOM   2452  O  OG1   . THR A 1 305 ? 157.852 137.272 129.599 1.00 31.84 ?  305 THR A OG1   1 
ATOM   2453  C  CG2   . THR A 1 305 ? 156.787 137.334 131.756 1.00 29.19 ?  305 THR A CG2   1 
ATOM   2454  N  N     . ILE A 1 306 ? 157.555 139.665 128.037 1.00 32.77 ?  306 ILE A N     1 
ATOM   2455  C  CA    . ILE A 1 306 ? 158.180 140.281 126.870 1.00 32.57 ?  306 ILE A CA    1 
ATOM   2456  C  C     . ILE A 1 306 ? 157.821 141.760 126.795 1.00 31.32 ?  306 ILE A C     1 
ATOM   2457  O  O     . ILE A 1 306 ? 158.673 142.607 126.497 1.00 32.80 ?  306 ILE A O     1 
ATOM   2458  C  CB    . ILE A 1 306 ? 157.771 139.527 125.591 1.00 28.41 ?  306 ILE A CB    1 
ATOM   2459  C  CG1   . ILE A 1 306 ? 158.582 138.237 125.458 1.00 32.43 ?  306 ILE A CG1   1 
ATOM   2460  C  CG2   . ILE A 1 306 ? 157.940 140.408 124.364 1.00 31.73 ?  306 ILE A CG2   1 
ATOM   2461  C  CD1   . ILE A 1 306 ? 158.224 137.416 124.250 1.00 31.27 ?  306 ILE A CD1   1 
ATOM   2462  N  N     . TYR A 1 307 ? 156.557 142.095 127.060 1.00 31.91 ?  307 TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 307 ? 156.140 143.493 127.029 1.00 31.01 ?  307 TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 307 ? 156.862 144.310 128.093 1.00 33.45 ?  307 TYR A C     1 
ATOM   2465  O  O     . TYR A 1 307 ? 157.265 145.451 127.843 1.00 36.52 ?  307 TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 307 ? 154.625 143.595 127.209 1.00 28.97 ?  307 TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 307 ? 154.096 145.003 127.089 1.00 30.60 ?  307 TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 307 ? 153.901 145.585 125.844 1.00 30.65 ?  307 TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 307 ? 153.800 145.753 128.217 1.00 33.18 ?  307 TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 307 ? 153.425 146.869 125.727 1.00 33.00 ?  307 TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 307 ? 153.322 147.041 128.110 1.00 33.13 ?  307 TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 307 ? 153.136 147.592 126.861 1.00 34.63 ?  307 TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 307 ? 152.660 148.874 126.740 1.00 36.39 ?  307 TYR A OH    1 
ATOM   2474  N  N     . LYS A 1 308 ? 157.021 143.747 129.290 1.00 34.52 ?  308 LYS A N     1 
ATOM   2475  C  CA    . LYS A 1 308 ? 157.732 144.446 130.355 1.00 32.72 ?  308 LYS A CA    1 
ATOM   2476  C  C     . LYS A 1 308 ? 159.204 144.632 130.007 1.00 32.52 ?  308 LYS A C     1 
ATOM   2477  O  O     . LYS A 1 308 ? 159.788 145.681 130.299 1.00 38.35 ?  308 LYS A O     1 
ATOM   2478  C  CB    . LYS A 1 308 ? 157.584 143.685 131.671 1.00 33.87 ?  308 LYS A CB    1 
ATOM   2479  C  CG    . LYS A 1 308 ? 156.205 143.796 132.299 1.00 33.26 ?  308 LYS A CG    1 
ATOM   2480  C  CD    . LYS A 1 308 ? 156.176 143.170 133.683 1.00 36.34 ?  308 LYS A CD    1 
ATOM   2481  C  CE    . LYS A 1 308 ? 156.609 141.714 133.639 1.00 37.36 ?  308 LYS A CE    1 
ATOM   2482  N  NZ    . LYS A 1 308 ? 155.475 140.788 133.909 1.00 37.78 1  308 LYS A NZ    1 
ATOM   2483  N  N     . GLU A 1 309 ? 159.820 143.624 129.386 1.00 32.39 ?  309 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 309 ? 161.246 143.703 129.091 1.00 33.46 ?  309 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 309 ? 161.534 144.652 127.933 1.00 36.40 ?  309 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 309 ? 162.494 145.430 127.987 1.00 37.54 ?  309 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 309 ? 161.795 142.310 128.790 1.00 31.64 ?  309 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 309 ? 163.239 142.302 128.322 1.00 37.48 ?  309 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 309 ? 164.212 142.718 129.406 1.00 42.65 ?  309 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 309 ? 163.831 142.693 130.594 1.00 41.25 ?  309 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 309 ? 165.361 143.071 129.069 1.00 41.78 -1 309 GLU A OE2   1 
ATOM   2492  N  N     . TYR A 1 310 ? 160.717 144.610 126.880 1.00 37.05 ?  310 TYR A N     1 
ATOM   2493  C  CA    . TYR A 1 310 ? 161.013 145.328 125.649 1.00 36.10 ?  310 TYR A CA    1 
ATOM   2494  C  C     . TYR A 1 310 ? 160.087 146.505 125.378 1.00 33.12 ?  310 TYR A C     1 
ATOM   2495  O  O     . TYR A 1 310 ? 160.385 147.308 124.487 1.00 38.26 ?  310 TYR A O     1 
ATOM   2496  C  CB    . TYR A 1 310 ? 160.963 144.363 124.454 1.00 37.36 ?  310 TYR A CB    1 
ATOM   2497  C  CG    . TYR A 1 310 ? 161.932 143.208 124.568 1.00 33.85 ?  310 TYR A CG    1 
ATOM   2498  C  CD1   . TYR A 1 310 ? 163.247 143.337 124.146 1.00 34.94 ?  310 TYR A CD1   1 
ATOM   2499  C  CD2   . TYR A 1 310 ? 161.533 141.991 125.103 1.00 32.11 ?  310 TYR A CD2   1 
ATOM   2500  C  CE1   . TYR A 1 310 ? 164.137 142.288 124.251 1.00 36.55 ?  310 TYR A CE1   1 
ATOM   2501  C  CE2   . TYR A 1 310 ? 162.416 140.936 125.214 1.00 33.23 ?  310 TYR A CE2   1 
ATOM   2502  C  CZ    . TYR A 1 310 ? 163.717 141.090 124.784 1.00 37.01 ?  310 TYR A CZ    1 
ATOM   2503  O  OH    . TYR A 1 310 ? 164.599 140.041 124.892 1.00 41.12 ?  310 TYR A OH    1 
ATOM   2504  N  N     . GLY A 1 311 ? 158.985 146.639 126.111 1.00 27.93 ?  311 GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 311 ? 158.058 147.725 125.878 1.00 31.03 ?  311 GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 311 ? 157.132 147.534 124.699 1.00 36.06 ?  311 GLY A C     1 
ATOM   2507  O  O     . GLY A 1 311 ? 156.349 148.442 124.395 1.00 39.00 ?  311 GLY A O     1 
ATOM   2508  N  N     . GLN A 1 312 ? 157.199 146.389 124.023 1.00 35.59 ?  312 GLN A N     1 
ATOM   2509  C  CA    . GLN A 1 312 ? 156.338 146.082 122.894 1.00 32.40 ?  312 GLN A CA    1 
ATOM   2510  C  C     . GLN A 1 312 ? 155.758 144.688 123.074 1.00 34.00 ?  312 GLN A C     1 
ATOM   2511  O  O     . GLN A 1 312 ? 156.339 143.834 123.749 1.00 38.82 ?  312 GLN A O     1 
ATOM   2512  C  CB    . GLN A 1 312 ? 157.092 146.163 121.558 1.00 31.89 ?  312 GLN A CB    1 
ATOM   2513  C  CG    . GLN A 1 312 ? 158.338 147.031 121.585 1.00 34.46 ?  312 GLN A CG    1 
ATOM   2514  C  CD    . GLN A 1 312 ? 159.146 146.929 120.308 1.00 39.73 ?  312 GLN A CD    1 
ATOM   2515  O  OE1   . GLN A 1 312 ? 158.603 147.020 119.208 1.00 38.64 ?  312 GLN A OE1   1 
ATOM   2516  N  NE2   . GLN A 1 312 ? 160.452 146.736 120.447 1.00 38.75 ?  312 GLN A NE2   1 
ATOM   2517  N  N     . HIS A 1 313 ? 154.602 144.464 122.459 1.00 31.83 ?  313 HIS A N     1 
ATOM   2518  C  CA    . HIS A 1 313 ? 153.954 143.167 122.547 1.00 28.38 ?  313 HIS A CA    1 
ATOM   2519  C  C     . HIS A 1 313 ? 154.722 142.129 121.732 1.00 33.15 ?  313 HIS A C     1 
ATOM   2520  O  O     . HIS A 1 313 ? 155.457 142.451 120.796 1.00 35.26 ?  313 HIS A O     1 
ATOM   2521  C  CB    . HIS A 1 313 ? 152.507 143.256 122.062 1.00 28.95 ?  313 HIS A CB    1 
ATOM   2522  C  CG    . HIS A 1 313 ? 151.668 144.220 122.840 1.00 33.95 ?  313 HIS A CG    1 
ATOM   2523  N  ND1   . HIS A 1 313 ? 151.084 143.895 124.045 1.00 30.64 ?  313 HIS A ND1   1 
ATOM   2524  C  CD2   . HIS A 1 313 ? 151.309 145.499 122.582 1.00 32.84 ?  313 HIS A CD2   1 
ATOM   2525  C  CE1   . HIS A 1 313 ? 150.404 144.933 124.497 1.00 28.85 ?  313 HIS A CE1   1 
ATOM   2526  N  NE2   . HIS A 1 313 ? 150.525 145.920 123.628 1.00 30.06 ?  313 HIS A NE2   1 
ATOM   2527  N  N     . MET A 1 314 ? 154.540 140.860 122.110 1.00 34.61 ?  314 MET A N     1 
ATOM   2528  C  CA    . MET A 1 314 ? 155.252 139.776 121.441 1.00 27.28 ?  314 MET A CA    1 
ATOM   2529  C  C     . MET A 1 314 ? 154.871 139.684 119.969 1.00 31.93 ?  314 MET A C     1 
ATOM   2530  O  O     . MET A 1 314 ? 155.725 139.424 119.114 1.00 36.58 ?  314 MET A O     1 
ATOM   2531  C  CB    . MET A 1 314 ? 154.976 138.453 122.156 1.00 27.70 ?  314 MET A CB    1 
ATOM   2532  C  CG    . MET A 1 314 ? 155.753 137.272 121.603 1.00 28.99 ?  314 MET A CG    1 
ATOM   2533  S  SD    . MET A 1 314 ? 155.078 135.688 122.135 1.00 41.60 ?  314 MET A SD    1 
ATOM   2534  C  CE    . MET A 1 314 ? 153.323 136.019 122.035 1.00 30.84 ?  314 MET A CE    1 
ATOM   2535  N  N     . ASP A 1 315 ? 153.595 139.888 119.651 1.00 33.57 ?  315 ASP A N     1 
ATOM   2536  C  CA    . ASP A 1 315 ? 153.135 139.808 118.272 1.00 36.36 ?  315 ASP A CA    1 
ATOM   2537  C  C     . ASP A 1 315 ? 153.408 141.078 117.473 1.00 33.16 ?  315 ASP A C     1 
ATOM   2538  O  O     . ASP A 1 315 ? 153.139 141.097 116.267 1.00 35.57 ?  315 ASP A O     1 
ATOM   2539  C  CB    . ASP A 1 315 ? 151.639 139.480 118.235 1.00 27.80 ?  315 ASP A CB    1 
ATOM   2540  C  CG    . ASP A 1 315 ? 150.779 140.620 118.737 1.00 34.50 ?  315 ASP A CG    1 
ATOM   2541  O  OD1   . ASP A 1 315 ? 151.273 141.418 119.560 1.00 36.88 ?  315 ASP A OD1   1 
ATOM   2542  O  OD2   . ASP A 1 315 ? 149.610 140.717 118.310 1.00 31.81 -1 315 ASP A OD2   1 
ATOM   2543  N  N     . GLU A 1 316 ? 153.928 142.127 118.102 1.00 30.94 ?  316 GLU A N     1 
ATOM   2544  C  CA    . GLU A 1 316 ? 154.225 143.377 117.414 1.00 31.82 ?  316 GLU A CA    1 
ATOM   2545  C  C     . GLU A 1 316 ? 155.639 143.440 116.854 1.00 34.22 ?  316 GLU A C     1 
ATOM   2546  O  O     . GLU A 1 316 ? 155.957 144.386 116.128 1.00 36.40 ?  316 GLU A O     1 
ATOM   2547  C  CB    . GLU A 1 316 ? 154.001 144.563 118.356 1.00 34.66 ?  316 GLU A CB    1 
ATOM   2548  C  CG    . GLU A 1 316 ? 152.560 144.758 118.776 1.00 35.61 ?  316 GLU A CG    1 
ATOM   2549  C  CD    . GLU A 1 316 ? 151.846 145.783 117.923 1.00 39.42 ?  316 GLU A CD    1 
ATOM   2550  O  OE1   . GLU A 1 316 ? 152.058 145.784 116.692 1.00 36.52 ?  316 GLU A OE1   1 
ATOM   2551  O  OE2   . GLU A 1 316 ? 151.080 146.594 118.483 1.00 45.88 -1 316 GLU A OE2   1 
ATOM   2552  N  N     . MET A 1 317 ? 156.492 142.469 117.169 1.00 40.57 ?  317 MET A N     1 
ATOM   2553  C  CA    . MET A 1 317 ? 157.854 142.436 116.662 1.00 41.21 ?  317 MET A CA    1 
ATOM   2554  C  C     . MET A 1 317 ? 158.082 141.164 115.858 1.00 42.05 ?  317 MET A C     1 
ATOM   2555  O  O     . MET A 1 317 ? 157.350 140.179 115.989 1.00 38.59 ?  317 MET A O     1 
ATOM   2556  C  CB    . MET A 1 317 ? 158.884 142.528 117.795 1.00 40.57 ?  317 MET A CB    1 
ATOM   2557  C  CG    . MET A 1 317 ? 158.443 143.364 118.978 1.00 42.12 ?  317 MET A CG    1 
ATOM   2558  S  SD    . MET A 1 317 ? 159.645 143.314 120.318 1.00 51.18 ?  317 MET A SD    1 
ATOM   2559  C  CE    . MET A 1 317 ? 158.632 142.694 121.653 1.00 35.61 ?  317 MET A CE    1 
ATOM   2560  N  N     . ASP A 1 318 ? 159.121 141.194 115.026 1.00 43.69 ?  318 ASP A N     1 
ATOM   2561  C  CA    . ASP A 1 318 ? 159.449 140.074 114.151 1.00 41.03 ?  318 ASP A CA    1 
ATOM   2562  C  C     . ASP A 1 318 ? 160.059 138.957 114.985 1.00 40.87 ?  318 ASP A C     1 
ATOM   2563  O  O     . ASP A 1 318 ? 161.160 139.104 115.525 1.00 43.57 ?  318 ASP A O     1 
ATOM   2564  C  CB    . ASP A 1 318 ? 160.406 140.520 113.050 1.00 41.27 ?  318 ASP A CB    1 
ATOM   2565  C  CG    . ASP A 1 318 ? 160.896 139.364 112.202 1.00 47.77 ?  318 ASP A CG    1 
ATOM   2566  O  OD1   . ASP A 1 318 ? 160.074 138.487 111.862 1.00 46.74 ?  318 ASP A OD1   1 
ATOM   2567  O  OD2   . ASP A 1 318 ? 162.101 139.333 111.876 1.00 49.13 -1 318 ASP A OD2   1 
ATOM   2568  N  N     . MET A 1 319 ? 159.344 137.835 115.091 1.00 42.96 ?  319 MET A N     1 
ATOM   2569  C  CA    . MET A 1 319 ? 159.830 136.704 115.872 1.00 36.29 ?  319 MET A CA    1 
ATOM   2570  C  C     . MET A 1 319 ? 161.073 136.069 115.260 1.00 36.71 ?  319 MET A C     1 
ATOM   2571  O  O     . MET A 1 319 ? 161.857 135.455 115.987 1.00 41.37 ?  319 MET A O     1 
ATOM   2572  C  CB    . MET A 1 319 ? 158.714 135.665 116.025 1.00 33.84 ?  319 MET A CB    1 
ATOM   2573  C  CG    . MET A 1 319 ? 159.144 134.351 116.658 1.00 38.01 ?  319 MET A CG    1 
ATOM   2574  S  SD    . MET A 1 319 ? 159.074 134.349 118.462 1.00 45.80 ?  319 MET A SD    1 
ATOM   2575  C  CE    . MET A 1 319 ? 157.851 135.617 118.778 1.00 34.85 ?  319 MET A CE    1 
ATOM   2576  N  N     . ASN A 1 320 ? 161.291 136.231 113.954 1.00 38.02 ?  320 ASN A N     1 
ATOM   2577  C  CA    . ASN A 1 320 ? 162.471 135.642 113.330 1.00 41.12 ?  320 ASN A CA    1 
ATOM   2578  C  C     . ASN A 1 320 ? 163.754 136.215 113.918 1.00 41.90 ?  320 ASN A C     1 
ATOM   2579  O  O     . ASN A 1 320 ? 164.719 135.480 114.159 1.00 41.32 ?  320 ASN A O     1 
ATOM   2580  C  CB    . ASN A 1 320 ? 162.427 135.855 111.818 1.00 41.65 ?  320 ASN A CB    1 
ATOM   2581  C  CG    . ASN A 1 320 ? 161.655 134.768 111.102 1.00 43.37 ?  320 ASN A CG    1 
ATOM   2582  O  OD1   . ASN A 1 320 ? 160.424 134.754 111.113 1.00 38.61 ?  320 ASN A OD1   1 
ATOM   2583  N  ND2   . ASN A 1 320 ? 162.376 133.846 110.474 1.00 40.60 ?  320 ASN A ND2   1 
ATOM   2584  N  N     . GLU A 1 321 ? 163.784 137.524 114.161 1.00 42.91 ?  321 GLU A N     1 
ATOM   2585  C  CA    . GLU A 1 321 ? 164.943 138.168 114.764 1.00 44.57 ?  321 GLU A CA    1 
ATOM   2586  C  C     . GLU A 1 321 ? 164.831 138.313 116.276 1.00 42.96 ?  321 GLU A C     1 
ATOM   2587  O  O     . GLU A 1 321 ? 165.830 138.640 116.926 1.00 44.36 ?  321 GLU A O     1 
ATOM   2588  C  CB    . GLU A 1 321 ? 165.163 139.549 114.138 1.00 44.39 ?  321 GLU A CB    1 
ATOM   2589  C  CG    . GLU A 1 321 ? 164.076 140.557 114.469 1.00 47.17 ?  321 GLU A CG    1 
ATOM   2590  C  CD    . GLU A 1 321 ? 164.622 141.955 114.677 1.00 49.00 ?  321 GLU A CD    1 
ATOM   2591  O  OE1   . GLU A 1 321 ? 165.719 142.088 115.255 1.00 46.69 ?  321 GLU A OE1   1 
ATOM   2592  O  OE2   . GLU A 1 321 ? 163.950 142.923 114.259 1.00 47.46 -1 321 GLU A OE2   1 
ATOM   2593  N  N     . MET A 1 322 ? 163.652 138.076 116.850 1.00 41.35 ?  322 MET A N     1 
ATOM   2594  C  CA    . MET A 1 322 ? 163.428 138.272 118.275 1.00 35.79 ?  322 MET A CA    1 
ATOM   2595  C  C     . MET A 1 322 ? 163.426 136.976 119.076 1.00 33.07 ?  322 MET A C     1 
ATOM   2596  O  O     . MET A 1 322 ? 163.498 137.034 120.305 1.00 41.00 ?  322 MET A O     1 
ATOM   2597  C  CB    . MET A 1 322 ? 162.095 138.994 118.506 1.00 34.29 ?  322 MET A CB    1 
ATOM   2598  C  CG    . MET A 1 322 ? 162.192 140.508 118.604 1.00 39.93 ?  322 MET A CG    1 
ATOM   2599  S  SD    . MET A 1 322 ? 163.569 141.078 119.614 1.00 48.26 ?  322 MET A SD    1 
ATOM   2600  C  CE    . MET A 1 322 ? 164.562 141.904 118.375 1.00 39.75 ?  322 MET A CE    1 
ATOM   2601  N  N     . TYR A 1 323 ? 163.331 135.819 118.416 1.00 31.27 ?  323 TYR A N     1 
ATOM   2602  C  CA    . TYR A 1 323 ? 163.160 134.560 119.136 1.00 32.27 ?  323 TYR A CA    1 
ATOM   2603  C  C     . TYR A 1 323 ? 164.395 134.217 119.958 1.00 36.70 ?  323 TYR A C     1 
ATOM   2604  O  O     . TYR A 1 323 ? 164.286 133.810 121.121 1.00 38.05 ?  323 TYR A O     1 
ATOM   2605  C  CB    . TYR A 1 323 ? 162.840 133.438 118.148 1.00 30.02 ?  323 TYR A CB    1 
ATOM   2606  C  CG    . TYR A 1 323 ? 162.738 132.071 118.782 1.00 35.95 ?  323 TYR A CG    1 
ATOM   2607  C  CD1   . TYR A 1 323 ? 161.557 131.649 119.376 1.00 31.23 ?  323 TYR A CD1   1 
ATOM   2608  C  CD2   . TYR A 1 323 ? 163.820 131.202 118.786 1.00 33.51 ?  323 TYR A CD2   1 
ATOM   2609  C  CE1   . TYR A 1 323 ? 161.459 130.402 119.957 1.00 28.78 ?  323 TYR A CE1   1 
ATOM   2610  C  CE2   . TYR A 1 323 ? 163.731 129.955 119.363 1.00 26.53 ?  323 TYR A CE2   1 
ATOM   2611  C  CZ    . TYR A 1 323 ? 162.548 129.560 119.948 1.00 31.76 ?  323 TYR A CZ    1 
ATOM   2612  O  OH    . TYR A 1 323 ? 162.458 128.316 120.525 1.00 34.72 ?  323 TYR A OH    1 
ATOM   2613  N  N     . ASP A 1 324 ? 165.581 134.363 119.365 1.00 38.06 ?  324 ASP A N     1 
ATOM   2614  C  CA    . ASP A 1 324 ? 166.809 134.060 120.091 1.00 37.16 ?  324 ASP A CA    1 
ATOM   2615  C  C     . ASP A 1 324 ? 166.995 135.005 121.269 1.00 39.55 ?  324 ASP A C     1 
ATOM   2616  O  O     . ASP A 1 324 ? 167.432 134.587 122.347 1.00 45.08 ?  324 ASP A O     1 
ATOM   2617  C  CB    . ASP A 1 324 ? 168.008 134.131 119.148 1.00 40.36 ?  324 ASP A CB    1 
ATOM   2618  C  CG    . ASP A 1 324 ? 167.997 133.030 118.109 1.00 43.01 ?  324 ASP A CG    1 
ATOM   2619  O  OD1   . ASP A 1 324 ? 167.609 131.893 118.449 1.00 43.21 ?  324 ASP A OD1   1 
ATOM   2620  O  OD2   . ASP A 1 324 ? 168.378 133.300 116.951 1.00 43.38 -1 324 ASP A OD2   1 
ATOM   2621  N  N     . LYS A 1 325 ? 166.667 136.284 121.083 1.00 37.78 ?  325 LYS A N     1 
ATOM   2622  C  CA    . LYS A 1 325 ? 166.785 137.243 122.176 1.00 37.22 ?  325 LYS A CA    1 
ATOM   2623  C  C     . LYS A 1 325 ? 165.786 136.942 123.286 1.00 37.32 ?  325 LYS A C     1 
ATOM   2624  O  O     . LYS A 1 325 ? 166.103 137.101 124.469 1.00 44.63 ?  325 LYS A O     1 
ATOM   2625  C  CB    . LYS A 1 325 ? 166.603 138.664 121.647 1.00 40.71 ?  325 LYS A CB    1 
ATOM   2626  C  CG    . LYS A 1 325 ? 167.678 139.084 120.660 1.00 40.43 ?  325 LYS A CG    1 
ATOM   2627  C  CD    . LYS A 1 325 ? 167.413 140.469 120.101 1.00 40.26 ?  325 LYS A CD    1 
ATOM   2628  C  CE    . LYS A 1 325 ? 168.389 140.808 118.986 1.00 41.23 ?  325 LYS A CE    1 
ATOM   2629  N  NZ    . LYS A 1 325 ? 167.919 141.958 118.167 1.00 45.47 1  325 LYS A NZ    1 
ATOM   2630  N  N     . PHE A 1 326 ? 164.574 136.515 122.927 1.00 37.17 ?  326 PHE A N     1 
ATOM   2631  C  CA    . PHE A 1 326 ? 163.601 136.109 123.936 1.00 36.58 ?  326 PHE A CA    1 
ATOM   2632  C  C     . PHE A 1 326 ? 164.103 134.901 124.719 1.00 34.61 ?  326 PHE A C     1 
ATOM   2633  O  O     . PHE A 1 326 ? 164.002 134.858 125.950 1.00 41.38 ?  326 PHE A O     1 
ATOM   2634  C  CB    . PHE A 1 326 ? 162.257 135.788 123.281 1.00 34.54 ?  326 PHE A CB    1 
ATOM   2635  C  CG    . PHE A 1 326 ? 161.570 136.975 122.669 1.00 34.95 ?  326 PHE A CG    1 
ATOM   2636  C  CD1   . PHE A 1 326 ? 161.880 138.263 123.069 1.00 36.22 ?  326 PHE A CD1   1 
ATOM   2637  C  CD2   . PHE A 1 326 ? 160.608 136.799 121.689 1.00 34.82 ?  326 PHE A CD2   1 
ATOM   2638  C  CE1   . PHE A 1 326 ? 161.242 139.350 122.502 1.00 36.18 ?  326 PHE A CE1   1 
ATOM   2639  C  CE2   . PHE A 1 326 ? 159.968 137.881 121.121 1.00 36.20 ?  326 PHE A CE2   1 
ATOM   2640  C  CZ    . PHE A 1 326 ? 160.285 139.158 121.528 1.00 38.81 ?  326 PHE A CZ    1 
ATOM   2641  N  N     . VAL A 1 327 ? 164.647 133.909 124.013 1.00 38.25 ?  327 VAL A N     1 
ATOM   2642  C  CA    . VAL A 1 327 ? 165.117 132.693 124.671 1.00 39.48 ?  327 VAL A CA    1 
ATOM   2643  C  C     . VAL A 1 327 ? 166.294 132.997 125.590 1.00 42.72 ?  327 VAL A C     1 
ATOM   2644  O  O     . VAL A 1 327 ? 166.362 132.498 126.720 1.00 44.58 ?  327 VAL A O     1 
ATOM   2645  C  CB    . VAL A 1 327 ? 165.473 131.624 123.621 1.00 37.45 ?  327 VAL A CB    1 
ATOM   2646  C  CG1   . VAL A 1 327 ? 166.187 130.452 124.273 1.00 40.17 ?  327 VAL A CG1   1 
ATOM   2647  C  CG2   . VAL A 1 327 ? 164.221 131.152 122.904 1.00 32.45 ?  327 VAL A CG2   1 
ATOM   2648  N  N     . ASP A 1 328 ? 167.231 133.824 125.129 1.00 40.53 ?  328 ASP A N     1 
ATOM   2649  C  CA    . ASP A 1 328 ? 168.417 134.148 125.912 1.00 39.72 ?  328 ASP A CA    1 
ATOM   2650  C  C     . ASP A 1 328 ? 168.155 135.184 126.996 1.00 43.46 ?  328 ASP A C     1 
ATOM   2651  O  O     . ASP A 1 328 ? 169.048 135.441 127.809 1.00 47.01 ?  328 ASP A O     1 
ATOM   2652  C  CB    . ASP A 1 328 ? 169.533 134.645 124.991 1.00 41.20 ?  328 ASP A CB    1 
ATOM   2653  C  CG    . ASP A 1 328 ? 170.037 133.568 124.051 1.00 48.04 ?  328 ASP A CG    1 
ATOM   2654  O  OD1   . ASP A 1 328 ? 169.424 132.480 124.008 1.00 46.00 ?  328 ASP A OD1   1 
ATOM   2655  O  OD2   . ASP A 1 328 ? 171.046 133.808 123.356 1.00 47.87 -1 328 ASP A OD2   1 
ATOM   2656  N  N     . ASN A 1 329 ? 166.966 135.782 127.032 1.00 40.52 ?  329 ASN A N     1 
ATOM   2657  C  CA    . ASN A 1 329 ? 166.654 136.791 128.035 1.00 40.00 ?  329 ASN A CA    1 
ATOM   2658  C  C     . ASN A 1 329 ? 166.127 136.117 129.293 1.00 43.33 ?  329 ASN A C     1 
ATOM   2659  O  O     . ASN A 1 329 ? 165.074 135.467 129.238 1.00 43.25 ?  329 ASN A O     1 
ATOM   2660  C  CB    . ASN A 1 329 ? 165.626 137.775 127.505 1.00 36.36 ?  329 ASN A CB    1 
ATOM   2661  C  CG    . ASN A 1 329 ? 165.620 139.081 128.271 1.00 38.87 ?  329 ASN A CG    1 
ATOM   2662  O  OD1   . ASN A 1 329 ? 165.596 139.093 129.501 1.00 45.50 ?  329 ASN A OD1   1 
ATOM   2663  N  ND2   . ASN A 1 329 ? 165.648 140.191 127.545 1.00 36.20 ?  329 ASN A ND2   1 
ATOM   2664  N  N     . PRO A 1 330 ? 166.814 136.232 130.433 1.00 43.62 ?  330 PRO A N     1 
ATOM   2665  C  CA    . PRO A 1 330 ? 166.291 135.616 131.661 1.00 38.70 ?  330 PRO A CA    1 
ATOM   2666  C  C     . PRO A 1 330 ? 165.008 136.257 132.158 1.00 38.18 ?  330 PRO A C     1 
ATOM   2667  O  O     . PRO A 1 330 ? 164.212 135.584 132.825 1.00 41.07 ?  330 PRO A O     1 
ATOM   2668  C  CB    . PRO A 1 330 ? 167.440 135.803 132.662 1.00 40.51 ?  330 PRO A CB    1 
ATOM   2669  C  CG    . PRO A 1 330 ? 168.179 136.996 132.160 1.00 38.95 ?  330 PRO A CG    1 
ATOM   2670  C  CD    . PRO A 1 330 ? 168.087 136.937 130.662 1.00 40.23 ?  330 PRO A CD    1 
ATOM   2671  N  N     . ARG A 1 331 ? 164.778 137.534 131.854 1.00 37.03 ?  331 ARG A N     1 
ATOM   2672  C  CA    . ARG A 1 331 ? 163.580 138.226 132.313 1.00 38.27 ?  331 ARG A CA    1 
ATOM   2673  C  C     . ARG A 1 331 ? 162.355 137.917 131.464 1.00 39.55 ?  331 ARG A C     1 
ATOM   2674  O  O     . ARG A 1 331 ? 161.255 138.363 131.810 1.00 38.55 ?  331 ARG A O     1 
ATOM   2675  C  CB    . ARG A 1 331 ? 163.827 139.736 132.342 1.00 36.84 ?  331 ARG A CB    1 
ATOM   2676  C  CG    . ARG A 1 331 ? 164.765 140.175 133.454 1.00 38.30 ?  331 ARG A CG    1 
ATOM   2677  C  CD    . ARG A 1 331 ? 165.277 141.588 133.231 1.00 38.69 ?  331 ARG A CD    1 
ATOM   2678  N  NE    . ARG A 1 331 ? 165.920 141.742 131.931 1.00 41.16 ?  331 ARG A NE    1 
ATOM   2679  C  CZ    . ARG A 1 331 ? 167.112 141.253 131.618 1.00 40.35 ?  331 ARG A CZ    1 
ATOM   2680  N  NH1   . ARG A 1 331 ? 167.834 140.573 132.494 1.00 42.22 1  331 ARG A NH1   1 
ATOM   2681  N  NH2   . ARG A 1 331 ? 167.594 141.453 130.395 1.00 35.96 ?  331 ARG A NH2   1 
ATOM   2682  N  N     . VAL A 1 332 ? 162.515 137.177 130.373 1.00 35.93 ?  332 VAL A N     1 
ATOM   2683  C  CA    . VAL A 1 332 ? 161.399 136.713 129.560 1.00 34.17 ?  332 VAL A CA    1 
ATOM   2684  C  C     . VAL A 1 332 ? 161.088 135.283 129.978 1.00 37.50 ?  332 VAL A C     1 
ATOM   2685  O  O     . VAL A 1 332 ? 161.952 134.403 129.900 1.00 37.78 ?  332 VAL A O     1 
ATOM   2686  C  CB    . VAL A 1 332 ? 161.724 136.795 128.060 1.00 34.74 ?  332 VAL A CB    1 
ATOM   2687  C  CG1   . VAL A 1 332 ? 160.757 135.936 127.259 1.00 34.04 ?  332 VAL A CG1   1 
ATOM   2688  C  CG2   . VAL A 1 332 ? 161.682 138.237 127.586 1.00 35.22 ?  332 VAL A CG2   1 
ATOM   2689  N  N     . LYS A 1 333 ? 159.860 135.050 130.431 1.00 33.45 ?  333 LYS A N     1 
ATOM   2690  C  CA    . LYS A 1 333 ? 159.442 133.729 130.873 1.00 31.89 ?  333 LYS A CA    1 
ATOM   2691  C  C     . LYS A 1 333 ? 158.918 132.929 129.689 1.00 32.22 ?  333 LYS A C     1 
ATOM   2692  O  O     . LYS A 1 333 ? 158.168 133.447 128.857 1.00 36.70 ?  333 LYS A O     1 
ATOM   2693  C  CB    . LYS A 1 333 ? 158.372 133.838 131.960 1.00 29.77 ?  333 LYS A CB    1 
ATOM   2694  C  CG    . LYS A 1 333 ? 157.982 132.512 132.587 1.00 32.83 ?  333 LYS A CG    1 
ATOM   2695  C  CD    . LYS A 1 333 ? 157.140 132.721 133.833 1.00 33.72 ?  333 LYS A CD    1 
ATOM   2696  C  CE    . LYS A 1 333 ? 156.973 131.428 134.611 1.00 36.46 ?  333 LYS A CE    1 
ATOM   2697  N  NZ    . LYS A 1 333 ? 155.563 131.218 135.039 1.00 38.82 1  333 LYS A NZ    1 
ATOM   2698  N  N     . LYS A 1 334 ? 159.320 131.662 129.618 1.00 35.19 ?  334 LYS A N     1 
ATOM   2699  C  CA    . LYS A 1 334 ? 158.984 130.821 128.480 1.00 33.26 ?  334 LYS A CA    1 
ATOM   2700  C  C     . LYS A 1 334 ? 158.845 129.378 128.939 1.00 37.91 ?  334 LYS A C     1 
ATOM   2701  O  O     . LYS A 1 334 ? 159.350 128.988 129.995 1.00 40.87 ?  334 LYS A O     1 
ATOM   2702  C  CB    . LYS A 1 334 ? 160.044 130.924 127.378 1.00 31.87 ?  334 LYS A CB    1 
ATOM   2703  C  CG    . LYS A 1 334 ? 161.439 130.554 127.840 1.00 34.69 ?  334 LYS A CG    1 
ATOM   2704  C  CD    . LYS A 1 334 ? 162.498 131.232 126.996 1.00 33.81 ?  334 LYS A CD    1 
ATOM   2705  C  CE    . LYS A 1 334 ? 163.148 132.375 127.754 1.00 35.60 ?  334 LYS A CE    1 
ATOM   2706  N  NZ    . LYS A 1 334 ? 163.925 131.896 128.929 1.00 37.49 1  334 LYS A NZ    1 
ATOM   2707  N  N     . GLU A 1 335 ? 158.147 128.588 128.128 1.00 35.08 ?  335 GLU A N     1 
ATOM   2708  C  CA    . GLU A 1 335 ? 157.958 127.167 128.373 1.00 35.23 ?  335 GLU A CA    1 
ATOM   2709  C  C     . GLU A 1 335 ? 158.427 126.367 127.166 1.00 39.41 ?  335 GLU A C     1 
ATOM   2710  O  O     . GLU A 1 335 ? 158.192 126.754 126.017 1.00 44.34 ?  335 GLU A O     1 
ATOM   2711  C  CB    . GLU A 1 335 ? 156.493 126.840 128.682 1.00 34.11 ?  335 GLU A CB    1 
ATOM   2712  C  CG    . GLU A 1 335 ? 155.865 127.753 129.720 1.00 43.30 ?  335 GLU A CG    1 
ATOM   2713  C  CD    . GLU A 1 335 ? 155.482 127.015 130.988 1.00 43.64 ?  335 GLU A CD    1 
ATOM   2714  O  OE1   . GLU A 1 335 ? 156.335 126.280 131.530 1.00 40.96 ?  335 GLU A OE1   1 
ATOM   2715  O  OE2   . GLU A 1 335 ? 154.332 127.172 131.447 1.00 38.15 -1 335 GLU A OE2   1 
ATOM   2716  N  N     . LYS A 1 336 ? 159.096 125.251 127.443 1.00 38.66 ?  336 LYS A N     1 
ATOM   2717  C  CA    . LYS A 1 336 ? 159.612 124.369 126.406 1.00 34.38 ?  336 LYS A CA    1 
ATOM   2718  C  C     . LYS A 1 336 ? 158.475 123.587 125.759 1.00 38.68 ?  336 LYS A C     1 
ATOM   2719  O  O     . LYS A 1 336 ? 157.613 123.040 126.454 1.00 41.63 ?  336 LYS A O     1 
ATOM   2720  C  CB    . LYS A 1 336 ? 160.636 123.410 127.010 1.00 40.52 ?  336 LYS A CB    1 
ATOM   2721  C  CG    . LYS A 1 336 ? 161.829 123.087 126.130 1.00 42.05 ?  336 LYS A CG    1 
ATOM   2722  C  CD    . LYS A 1 336 ? 162.558 121.864 126.671 1.00 41.51 ?  336 LYS A CD    1 
ATOM   2723  C  CE    . LYS A 1 336 ? 163.355 121.157 125.593 1.00 40.22 ?  336 LYS A CE    1 
ATOM   2724  N  NZ    . LYS A 1 336 ? 163.768 119.789 126.010 1.00 41.73 1  336 LYS A NZ    1 
ATOM   2725  N  N     . ILE A 1 337 ? 158.474 123.534 124.425 1.00 36.69 ?  337 ILE A N     1 
ATOM   2726  C  CA    . ILE A 1 337 ? 157.510 122.749 123.665 1.00 33.68 ?  337 ILE A CA    1 
ATOM   2727  C  C     . ILE A 1 337 ? 158.238 122.062 122.519 1.00 32.64 ?  337 ILE A C     1 
ATOM   2728  O  O     . ILE A 1 337 ? 159.360 122.422 122.158 1.00 36.49 ?  337 ILE A O     1 
ATOM   2729  C  CB    . ILE A 1 337 ? 156.346 123.603 123.112 1.00 34.61 ?  337 ILE A CB    1 
ATOM   2730  C  CG1   . ILE A 1 337 ? 156.889 124.763 122.277 1.00 33.71 ?  337 ILE A CG1   1 
ATOM   2731  C  CG2   . ILE A 1 337 ? 155.456 124.103 124.240 1.00 35.33 ?  337 ILE A CG2   1 
ATOM   2732  C  CD1   . ILE A 1 337 ? 156.100 125.029 121.019 1.00 31.06 ?  337 ILE A CD1   1 
ATOM   2733  N  N     . ASN A 1 338 ? 157.579 121.058 121.943 1.00 33.74 ?  338 ASN A N     1 
ATOM   2734  C  CA    . ASN A 1 338 ? 158.087 120.411 120.746 1.00 35.16 ?  338 ASN A CA    1 
ATOM   2735  C  C     . ASN A 1 338 ? 157.309 120.931 119.549 1.00 32.98 ?  338 ASN A C     1 
ATOM   2736  O  O     . ASN A 1 338 ? 156.108 120.642 119.433 1.00 34.04 ?  338 ASN A O     1 
ATOM   2737  C  CB    . ASN A 1 338 ? 157.962 118.893 120.848 1.00 35.34 ?  338 ASN A CB    1 
ATOM   2738  C  CG    . ASN A 1 338 ? 158.672 118.174 119.718 1.00 36.98 ?  338 ASN A CG    1 
ATOM   2739  O  OD1   . ASN A 1 338 ? 158.168 117.192 119.177 1.00 37.66 ?  338 ASN A OD1   1 
ATOM   2740  N  ND2   . ASN A 1 338 ? 159.851 118.666 119.355 1.00 37.68 ?  338 ASN A ND2   1 
ATOM   2741  N  N     . PRO A 1 339 ? 157.925 121.706 118.653 1.00 35.25 ?  339 PRO A N     1 
ATOM   2742  C  CA    . PRO A 1 339 ? 157.168 122.257 117.517 1.00 31.07 ?  339 PRO A CA    1 
ATOM   2743  C  C     . PRO A 1 339 ? 156.570 121.199 116.607 1.00 32.75 ?  339 PRO A C     1 
ATOM   2744  O  O     . PRO A 1 339 ? 155.489 121.420 116.050 1.00 37.31 ?  339 PRO A O     1 
ATOM   2745  C  CB    . PRO A 1 339 ? 158.210 123.113 116.783 1.00 31.83 ?  339 PRO A CB    1 
ATOM   2746  C  CG    . PRO A 1 339 ? 159.526 122.583 117.225 1.00 34.70 ?  339 PRO A CG    1 
ATOM   2747  C  CD    . PRO A 1 339 ? 159.337 122.119 118.632 1.00 33.83 ?  339 PRO A CD    1 
ATOM   2748  N  N     . ARG A 1 340 ? 157.237 120.057 116.431 1.00 32.40 ?  340 ARG A N     1 
ATOM   2749  C  CA    . ARG A 1 340 ? 156.660 118.991 115.620 1.00 27.98 ?  340 ARG A CA    1 
ATOM   2750  C  C     . ARG A 1 340 ? 155.437 118.386 116.297 1.00 31.44 ?  340 ARG A C     1 
ATOM   2751  O  O     . ARG A 1 340 ? 154.445 118.066 115.631 1.00 37.96 ?  340 ARG A O     1 
ATOM   2752  C  CB    . ARG A 1 340 ? 157.710 117.920 115.331 1.00 30.71 ?  340 ARG A CB    1 
ATOM   2753  C  CG    . ARG A 1 340 ? 158.727 118.341 114.287 1.00 30.19 ?  340 ARG A CG    1 
ATOM   2754  C  CD    . ARG A 1 340 ? 159.475 117.153 113.715 1.00 27.86 ?  340 ARG A CD    1 
ATOM   2755  N  NE    . ARG A 1 340 ? 160.483 117.577 112.750 1.00 30.37 ?  340 ARG A NE    1 
ATOM   2756  C  CZ    . ARG A 1 340 ? 161.337 116.760 112.150 1.00 32.54 ?  340 ARG A CZ    1 
ATOM   2757  N  NH1   . ARG A 1 340 ? 161.334 115.460 112.389 1.00 32.83 1  340 ARG A NH1   1 
ATOM   2758  N  NH2   . ARG A 1 340 ? 162.215 117.262 111.286 1.00 32.68 ?  340 ARG A NH2   1 
ATOM   2759  N  N     . LYS A 1 341 ? 155.485 118.229 117.621 1.00 33.69 ?  341 LYS A N     1 
ATOM   2760  C  CA    . LYS A 1 341 ? 154.305 117.783 118.352 1.00 32.33 ?  341 LYS A CA    1 
ATOM   2761  C  C     . LYS A 1 341 ? 153.168 118.787 118.220 1.00 31.94 ?  341 LYS A C     1 
ATOM   2762  O  O     . LYS A 1 341 ? 152.002 118.402 118.093 1.00 35.86 ?  341 LYS A O     1 
ATOM   2763  C  CB    . LYS A 1 341 ? 154.648 117.550 119.823 1.00 35.30 ?  341 LYS A CB    1 
ATOM   2764  C  CG    . LYS A 1 341 ? 155.277 116.198 120.110 1.00 37.81 ?  341 LYS A CG    1 
ATOM   2765  C  CD    . LYS A 1 341 ? 154.477 115.067 119.486 1.00 36.37 ?  341 LYS A CD    1 
ATOM   2766  C  CE    . LYS A 1 341 ? 155.386 113.951 119.004 1.00 38.19 ?  341 LYS A CE    1 
ATOM   2767  N  NZ    . LYS A 1 341 ? 156.391 114.441 118.020 1.00 38.23 1  341 LYS A NZ    1 
ATOM   2768  N  N     . LEU A 1 342 ? 153.489 120.081 118.251 1.00 29.81 ?  342 LEU A N     1 
ATOM   2769  C  CA    . LEU A 1 342 ? 152.459 121.102 118.083 1.00 27.23 ?  342 LEU A CA    1 
ATOM   2770  C  C     . LEU A 1 342 ? 151.860 121.057 116.681 1.00 29.81 ?  342 LEU A C     1 
ATOM   2771  O  O     . LEU A 1 342 ? 150.647 121.229 116.512 1.00 36.01 ?  342 LEU A O     1 
ATOM   2772  C  CB    . LEU A 1 342 ? 153.040 122.483 118.384 1.00 28.01 ?  342 LEU A CB    1 
ATOM   2773  C  CG    . LEU A 1 342 ? 152.052 123.630 118.591 1.00 27.34 ?  342 LEU A CG    1 
ATOM   2774  C  CD1   . LEU A 1 342 ? 150.850 123.165 119.393 1.00 26.87 ?  342 LEU A CD1   1 
ATOM   2775  C  CD2   . LEU A 1 342 ? 152.739 124.792 119.287 1.00 28.36 ?  342 LEU A CD2   1 
ATOM   2776  N  N     . LEU A 1 343 ? 152.693 120.830 115.662 1.00 28.68 ?  343 LEU A N     1 
ATOM   2777  C  CA    . LEU A 1 343 ? 152.182 120.689 114.301 1.00 24.60 ?  343 LEU A CA    1 
ATOM   2778  C  C     . LEU A 1 343 ? 151.279 119.469 114.173 1.00 31.50 ?  343 LEU A C     1 
ATOM   2779  O  O     . LEU A 1 343 ? 150.234 119.524 113.513 1.00 36.23 ?  343 LEU A O     1 
ATOM   2780  C  CB    . LEU A 1 343 ? 153.345 120.598 113.314 1.00 28.60 ?  343 LEU A CB    1 
ATOM   2781  C  CG    . LEU A 1 343 ? 153.949 121.918 112.836 1.00 31.05 ?  343 LEU A CG    1 
ATOM   2782  C  CD1   . LEU A 1 343 ? 154.971 121.667 111.741 1.00 27.29 ?  343 LEU A CD1   1 
ATOM   2783  C  CD2   . LEU A 1 343 ? 152.861 122.860 112.349 1.00 30.62 ?  343 LEU A CD2   1 
ATOM   2784  N  N     . GLU A 1 344 ? 151.673 118.354 114.792 1.00 34.59 ?  344 GLU A N     1 
ATOM   2785  C  CA    . GLU A 1 344 ? 150.832 117.162 114.768 1.00 30.94 ?  344 GLU A CA    1 
ATOM   2786  C  C     . GLU A 1 344 ? 149.519 117.406 115.499 1.00 30.40 ?  344 GLU A C     1 
ATOM   2787  O  O     . GLU A 1 344 ? 148.468 116.910 115.081 1.00 39.33 ?  344 GLU A O     1 
ATOM   2788  C  CB    . GLU A 1 344 ? 151.580 115.977 115.378 1.00 31.41 ?  344 GLU A CB    1 
ATOM   2789  C  CG    . GLU A 1 344 ? 152.784 115.528 114.568 1.00 33.61 ?  344 GLU A CG    1 
ATOM   2790  C  CD    . GLU A 1 344 ? 153.736 114.665 115.371 1.00 40.44 ?  344 GLU A CD    1 
ATOM   2791  O  OE1   . GLU A 1 344 ? 153.329 114.166 116.440 1.00 41.47 ?  344 GLU A OE1   1 
ATOM   2792  O  OE2   . GLU A 1 344 ? 154.894 114.490 114.935 1.00 40.14 -1 344 GLU A OE2   1 
ATOM   2793  N  N     . LYS A 1 345 ? 149.559 118.164 116.596 1.00 29.13 ?  345 LYS A N     1 
ATOM   2794  C  CA    . LYS A 1 345 ? 148.331 118.523 117.299 1.00 29.09 ?  345 LYS A CA    1 
ATOM   2795  C  C     . LYS A 1 345 ? 147.431 119.391 116.429 1.00 29.83 ?  345 LYS A C     1 
ATOM   2796  O  O     . LYS A 1 345 ? 146.208 119.205 116.415 1.00 31.83 ?  345 LYS A O     1 
ATOM   2797  C  CB    . LYS A 1 345 ? 148.667 119.239 118.607 1.00 26.73 ?  345 LYS A CB    1 
ATOM   2798  C  CG    . LYS A 1 345 ? 147.450 119.610 119.436 1.00 29.26 ?  345 LYS A CG    1 
ATOM   2799  C  CD    . LYS A 1 345 ? 147.846 120.287 120.735 1.00 30.18 ?  345 LYS A CD    1 
ATOM   2800  C  CE    . LYS A 1 345 ? 146.620 120.688 121.537 1.00 32.03 ?  345 LYS A CE    1 
ATOM   2801  N  NZ    . LYS A 1 345 ? 146.980 121.403 122.791 1.00 31.82 1  345 LYS A NZ    1 
ATOM   2802  N  N     . LEU A 1 346 ? 148.015 120.344 115.699 1.00 32.88 ?  346 LEU A N     1 
ATOM   2803  C  CA    . LEU A 1 346 ? 147.232 121.158 114.774 1.00 25.13 ?  346 LEU A CA    1 
ATOM   2804  C  C     . LEU A 1 346 ? 146.579 120.295 113.704 1.00 26.69 ?  346 LEU A C     1 
ATOM   2805  O  O     . LEU A 1 346 ? 145.395 120.468 113.392 1.00 32.19 ?  346 LEU A O     1 
ATOM   2806  C  CB    . LEU A 1 346 ? 148.115 122.222 114.121 1.00 24.17 ?  346 LEU A CB    1 
ATOM   2807  C  CG    . LEU A 1 346 ? 148.755 123.302 114.993 1.00 26.88 ?  346 LEU A CG    1 
ATOM   2808  C  CD1   . LEU A 1 346 ? 149.890 123.973 114.243 1.00 27.67 ?  346 LEU A CD1   1 
ATOM   2809  C  CD2   . LEU A 1 346 ? 147.725 124.325 115.413 1.00 28.49 ?  346 LEU A CD2   1 
ATOM   2810  N  N     . ALA A 1 347 ? 147.338 119.359 113.131 1.00 25.65 ?  347 ALA A N     1 
ATOM   2811  C  CA    . ALA A 1 347 ? 146.788 118.485 112.100 1.00 26.16 ?  347 ALA A CA    1 
ATOM   2812  C  C     . ALA A 1 347 ? 145.681 117.596 112.655 1.00 29.62 ?  347 ALA A C     1 
ATOM   2813  O  O     . ALA A 1 347 ? 144.650 117.398 112.003 1.00 35.76 ?  347 ALA A O     1 
ATOM   2814  C  CB    . ALA A 1 347 ? 147.898 117.638 111.481 1.00 26.21 ?  347 ALA A CB    1 
ATOM   2815  N  N     . MET A 1 348 ? 145.875 117.054 113.861 1.00 31.30 ?  348 MET A N     1 
ATOM   2816  C  CA    . MET A 1 348 ? 144.850 116.217 114.473 1.00 34.50 ?  348 MET A CA    1 
ATOM   2817  C  C     . MET A 1 348 ? 143.583 117.013 114.752 1.00 31.34 ?  348 MET A C     1 
ATOM   2818  O  O     . MET A 1 348 ? 142.472 116.539 114.492 1.00 36.47 ?  348 MET A O     1 
ATOM   2819  C  CB    . MET A 1 348 ? 145.390 115.592 115.760 1.00 32.72 ?  348 MET A CB    1 
ATOM   2820  C  CG    . MET A 1 348 ? 144.324 115.027 116.683 1.00 37.45 ?  348 MET A CG    1 
ATOM   2821  S  SD    . MET A 1 348 ? 144.130 115.992 118.195 1.00 55.87 ?  348 MET A SD    1 
ATOM   2822  C  CE    . MET A 1 348 ? 145.757 115.818 118.920 1.00 38.89 ?  348 MET A CE    1 
ATOM   2823  N  N     . LEU A 1 349 ? 143.731 118.233 115.273 1.00 27.73 ?  349 LEU A N     1 
ATOM   2824  C  CA    . LEU A 1 349 ? 142.566 119.065 115.553 1.00 22.99 ?  349 LEU A CA    1 
ATOM   2825  C  C     . LEU A 1 349 ? 141.837 119.443 114.271 1.00 28.25 ?  349 LEU A C     1 
ATOM   2826  O  O     . LEU A 1 349 ? 140.602 119.485 114.242 1.00 30.06 ?  349 LEU A O     1 
ATOM   2827  C  CB    . LEU A 1 349 ? 142.990 120.314 116.319 1.00 26.16 ?  349 LEU A CB    1 
ATOM   2828  C  CG    . LEU A 1 349 ? 142.930 120.192 117.840 1.00 32.55 ?  349 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A 1 349 ? 143.873 121.187 118.475 1.00 30.67 ?  349 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A 1 349 ? 141.511 120.397 118.341 1.00 34.59 ?  349 LEU A CD2   1 
ATOM   2831  N  N     . ARG A 1 350 ? 142.583 119.734 113.203 1.00 29.88 ?  350 ARG A N     1 
ATOM   2832  C  CA    . ARG A 1 350 ? 141.947 120.030 111.926 1.00 24.31 ?  350 ARG A CA    1 
ATOM   2833  C  C     . ARG A 1 350 ? 141.238 118.809 111.356 1.00 30.19 ?  350 ARG A C     1 
ATOM   2834  O  O     . ARG A 1 350 ? 140.193 118.946 110.711 1.00 34.35 ?  350 ARG A O     1 
ATOM   2835  C  CB    . ARG A 1 350 ? 142.980 120.564 110.936 1.00 26.02 ?  350 ARG A CB    1 
ATOM   2836  C  CG    . ARG A 1 350 ? 143.410 121.995 111.212 1.00 24.05 ?  350 ARG A CG    1 
ATOM   2837  C  CD    . ARG A 1 350 ? 144.655 122.363 110.428 1.00 23.05 ?  350 ARG A CD    1 
ATOM   2838  N  NE    . ARG A 1 350 ? 144.390 122.414 108.996 1.00 34.27 ?  350 ARG A NE    1 
ATOM   2839  C  CZ    . ARG A 1 350 ? 143.772 123.413 108.381 1.00 31.39 ?  350 ARG A CZ    1 
ATOM   2840  N  NH1   . ARG A 1 350 ? 143.353 124.481 109.041 1.00 24.59 1  350 ARG A NH1   1 
ATOM   2841  N  NH2   . ARG A 1 350 ? 143.566 123.338 107.069 1.00 28.80 ?  350 ARG A NH2   1 
ATOM   2842  N  N     . SER A 1 351 ? 141.791 117.615 111.570 1.00 33.50 ?  351 SER A N     1 
ATOM   2843  C  CA    . SER A 1 351 ? 141.101 116.401 111.151 1.00 30.16 ?  351 SER A CA    1 
ATOM   2844  C  C     . SER A 1 351 ? 139.802 116.211 111.925 1.00 31.45 ?  351 SER A C     1 
ATOM   2845  O  O     . SER A 1 351 ? 138.774 115.841 111.346 1.00 38.80 ?  351 SER A O     1 
ATOM   2846  C  CB    . SER A 1 351 ? 142.014 115.190 111.330 1.00 30.96 ?  351 SER A CB    1 
ATOM   2847  O  OG    . SER A 1 351 ? 143.024 115.161 110.338 1.00 39.77 ?  351 SER A OG    1 
ATOM   2848  N  N     . GLU A 1 352 ? 139.828 116.460 113.236 1.00 29.70 ?  352 GLU A N     1 
ATOM   2849  C  CA    . GLU A 1 352 ? 138.634 116.251 114.051 1.00 30.98 ?  352 GLU A CA    1 
ATOM   2850  C  C     . GLU A 1 352 ? 137.553 117.285 113.748 1.00 34.19 ?  352 GLU A C     1 
ATOM   2851  O  O     . GLU A 1 352 ? 136.380 116.934 113.573 1.00 39.10 ?  352 GLU A O     1 
ATOM   2852  C  CB    . GLU A 1 352 ? 138.989 116.273 115.539 1.00 33.49 ?  352 GLU A CB    1 
ATOM   2853  C  CG    . GLU A 1 352 ? 140.093 115.313 115.944 1.00 33.65 ?  352 GLU A CG    1 
ATOM   2854  C  CD    . GLU A 1 352 ? 140.556 115.528 117.372 1.00 42.38 ?  352 GLU A CD    1 
ATOM   2855  O  OE1   . GLU A 1 352 ? 141.123 114.586 117.963 1.00 41.46 ?  352 GLU A OE1   1 
ATOM   2856  O  OE2   . GLU A 1 352 ? 140.353 116.640 117.903 1.00 41.70 -1 352 GLU A OE2   1 
ATOM   2857  N  N     . SER A 1 353 ? 137.921 118.567 113.685 1.00 34.69 ?  353 SER A N     1 
ATOM   2858  C  CA    . SER A 1 353 ? 136.931 119.633 113.620 1.00 34.74 ?  353 SER A CA    1 
ATOM   2859  C  C     . SER A 1 353 ? 137.199 120.692 112.558 1.00 30.47 ?  353 SER A C     1 
ATOM   2860  O  O     . SER A 1 353 ? 136.382 121.607 112.410 1.00 31.06 ?  353 SER A O     1 
ATOM   2861  C  CB    . SER A 1 353 ? 136.813 120.326 114.986 1.00 34.34 ?  353 SER A CB    1 
ATOM   2862  O  OG    . SER A 1 353 ? 138.027 120.964 115.342 1.00 32.37 ?  353 SER A OG    1 
ATOM   2863  N  N     . GLY A 1 354 ? 138.303 120.606 111.822 1.00 27.70 ?  354 GLY A N     1 
ATOM   2864  C  CA    . GLY A 1 354 ? 138.632 121.623 110.847 1.00 27.40 ?  354 GLY A CA    1 
ATOM   2865  C  C     . GLY A 1 354 ? 139.300 122.854 111.412 1.00 21.81 ?  354 GLY A C     1 
ATOM   2866  O  O     . GLY A 1 354 ? 139.620 123.772 110.647 1.00 25.58 ?  354 GLY A O     1 
ATOM   2867  N  N     . TYR A 1 355 ? 139.525 122.904 112.720 1.00 22.77 ?  355 TYR A N     1 
ATOM   2868  C  CA    . TYR A 1 355 ? 140.156 124.011 113.408 1.00 17.75 ?  355 TYR A CA    1 
ATOM   2869  C  C     . TYR A 1 355 ? 141.564 123.624 113.849 1.00 22.19 ?  355 TYR A C     1 
ATOM   2870  O  O     . TYR A 1 355 ? 141.844 122.443 114.074 1.00 28.86 ?  355 TYR A O     1 
ATOM   2871  C  CB    . TYR A 1 355 ? 139.336 124.432 114.633 1.00 23.82 ?  355 TYR A CB    1 
ATOM   2872  C  CG    . TYR A 1 355 ? 138.031 125.109 114.292 1.00 26.78 ?  355 TYR A CG    1 
ATOM   2873  C  CD1   . TYR A 1 355 ? 138.005 126.248 113.501 1.00 20.43 ?  355 TYR A CD1   1 
ATOM   2874  C  CD2   . TYR A 1 355 ? 136.824 124.608 114.759 1.00 25.91 ?  355 TYR A CD2   1 
ATOM   2875  C  CE1   . TYR A 1 355 ? 136.814 126.869 113.186 1.00 27.50 ?  355 TYR A CE1   1 
ATOM   2876  C  CE2   . TYR A 1 355 ? 135.628 125.222 114.450 1.00 26.03 ?  355 TYR A CE2   1 
ATOM   2877  C  CZ    . TYR A 1 355 ? 135.629 126.352 113.663 1.00 30.59 ?  355 TYR A CZ    1 
ATOM   2878  O  OH    . TYR A 1 355 ? 134.439 126.969 113.351 1.00 31.21 ?  355 TYR A OH    1 
ATOM   2879  N  N     . PRO A 1 356 ? 142.476 124.590 113.991 1.00 22.84 ?  356 PRO A N     1 
ATOM   2880  C  CA    . PRO A 1 356 ? 142.320 126.035 113.786 1.00 17.73 ?  356 PRO A CA    1 
ATOM   2881  C  C     . PRO A 1 356 ? 142.580 126.478 112.355 1.00 15.52 ?  356 PRO A C     1 
ATOM   2882  O  O     . PRO A 1 356 ? 143.108 125.723 111.547 1.00 19.50 ?  356 PRO A O     1 
ATOM   2883  C  CB    . PRO A 1 356 ? 143.370 126.612 114.736 1.00 18.27 ?  356 PRO A CB    1 
ATOM   2884  C  CG    . PRO A 1 356 ? 144.487 125.615 114.646 1.00 17.73 ?  356 PRO A CG    1 
ATOM   2885  C  CD    . PRO A 1 356 ? 143.821 124.266 114.501 1.00 13.52 ?  356 PRO A CD    1 
ATOM   2886  N  N     . TYR A 1 357 ? 142.210 127.710 112.015 1.00 18.54 ?  357 TYR A N     1 
ATOM   2887  C  CA    . TYR A 1 357 ? 142.730 128.322 110.804 1.00 11.30 ?  357 TYR A CA    1 
ATOM   2888  C  C     . TYR A 1 357 ? 144.225 128.562 110.961 1.00 16.15 ?  357 TYR A C     1 
ATOM   2889  O  O     . TYR A 1 357 ? 144.717 128.863 112.051 1.00 25.34 ?  357 TYR A O     1 
ATOM   2890  C  CB    . TYR A 1 357 ? 142.018 129.644 110.507 1.00 15.07 ?  357 TYR A CB    1 
ATOM   2891  C  CG    . TYR A 1 357 ? 140.517 129.631 110.693 1.00 18.99 ?  357 TYR A CG    1 
ATOM   2892  C  CD1   . TYR A 1 357 ? 139.766 128.506 110.387 1.00 14.29 ?  357 TYR A CD1   1 
ATOM   2893  C  CD2   . TYR A 1 357 ? 139.849 130.748 111.171 1.00 18.46 ?  357 TYR A CD2   1 
ATOM   2894  C  CE1   . TYR A 1 357 ? 138.399 128.492 110.549 1.00 14.64 ?  357 TYR A CE1   1 
ATOM   2895  C  CE2   . TYR A 1 357 ? 138.480 130.745 111.340 1.00 17.60 ?  357 TYR A CE2   1 
ATOM   2896  C  CZ    . TYR A 1 357 ? 137.760 129.613 111.027 1.00 21.97 ?  357 TYR A CZ    1 
ATOM   2897  O  OH    . TYR A 1 357 ? 136.395 129.598 111.190 1.00 26.52 ?  357 TYR A OH    1 
ATOM   2898  N  N     . ILE A 1 358 ? 144.955 128.417 109.861 1.00 14.85 ?  358 ILE A N     1 
ATOM   2899  C  CA    . ILE A 1 358 ? 146.403 128.568 109.855 1.00 13.71 ?  358 ILE A CA    1 
ATOM   2900  C  C     . ILE A 1 358 ? 146.751 129.850 109.116 1.00 16.73 ?  358 ILE A C     1 
ATOM   2901  O  O     . ILE A 1 358 ? 146.364 130.028 107.955 1.00 25.12 ?  358 ILE A O     1 
ATOM   2902  C  CB    . ILE A 1 358 ? 147.097 127.357 109.208 1.00 18.73 ?  358 ILE A CB    1 
ATOM   2903  C  CG1   . ILE A 1 358 ? 146.593 126.054 109.831 1.00 21.88 ?  358 ILE A CG1   1 
ATOM   2904  C  CG2   . ILE A 1 358 ? 148.605 127.474 109.351 1.00 17.24 ?  358 ILE A CG2   1 
ATOM   2905  C  CD1   . ILE A 1 358 ? 146.959 125.889 111.286 1.00 18.48 ?  358 ILE A CD1   1 
ATOM   2906  N  N     . MET A 1 359 ? 147.473 130.741 109.787 1.00 10.67 ?  359 MET A N     1 
ATOM   2907  C  CA    . MET A 1 359 ? 148.003 131.949 109.169 1.00 8.82  ?  359 MET A CA    1 
ATOM   2908  C  C     . MET A 1 359 ? 149.520 131.857 109.167 1.00 10.43 ?  359 MET A C     1 
ATOM   2909  O  O     . MET A 1 359 ? 150.143 131.791 110.232 1.00 21.36 ?  359 MET A O     1 
ATOM   2910  C  CB    . MET A 1 359 ? 147.544 133.205 109.908 1.00 11.87 ?  359 MET A CB    1 
ATOM   2911  C  CG    . MET A 1 359 ? 147.151 134.342 108.982 1.00 12.10 ?  359 MET A CG    1 
ATOM   2912  S  SD    . MET A 1 359 ? 147.386 135.993 109.660 1.00 33.65 ?  359 MET A SD    1 
ATOM   2913  C  CE    . MET A 1 359 ? 149.169 136.113 109.678 1.00 12.22 ?  359 MET A CE    1 
ATOM   2914  N  N     . PHE A 1 360 ? 150.109 131.845 107.977 1.00 10.78 ?  360 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 360 ? 151.561 131.861 107.829 1.00 11.58 ?  360 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 360 ? 151.996 133.320 107.818 1.00 15.89 ?  360 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 360 ? 151.911 133.998 106.792 1.00 25.75 ?  360 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 360 ? 151.978 131.118 106.566 1.00 9.13  ?  360 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 360 ? 151.637 129.655 106.593 1.00 17.71 ?  360 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 360 ? 152.137 128.836 107.590 1.00 16.06 ?  360 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 360 ? 150.808 129.103 105.633 1.00 13.68 ?  360 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 360 ? 151.822 127.492 107.625 1.00 11.57 ?  360 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 360 ? 150.491 127.762 105.663 1.00 17.28 ?  360 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 360 ? 150.999 126.955 106.660 1.00 15.05 ?  360 PHE A CZ    1 
ATOM   2925  N  N     . GLN A 1 361 ? 152.463 133.799 108.973 1.00 11.68 ?  361 GLN A N     1 
ATOM   2926  C  CA    . GLN A 1 361 ? 152.683 135.229 109.171 1.00 11.92 ?  361 GLN A CA    1 
ATOM   2927  C  C     . GLN A 1 361 ? 153.677 135.791 108.163 1.00 15.94 ?  361 GLN A C     1 
ATOM   2928  O  O     . GLN A 1 361 ? 153.446 136.852 107.569 1.00 20.44 ?  361 GLN A O     1 
ATOM   2929  C  CB    . GLN A 1 361 ? 153.168 135.484 110.597 1.00 23.22 ?  361 GLN A CB    1 
ATOM   2930  C  CG    . GLN A 1 361 ? 153.116 136.940 111.018 1.00 17.97 ?  361 GLN A CG    1 
ATOM   2931  C  CD    . GLN A 1 361 ? 152.712 137.114 112.464 1.00 20.29 ?  361 GLN A CD    1 
ATOM   2932  O  OE1   . GLN A 1 361 ? 153.020 136.277 113.311 1.00 24.15 ?  361 GLN A OE1   1 
ATOM   2933  N  NE2   . GLN A 1 361 ? 152.022 138.209 112.756 1.00 23.91 ?  361 GLN A NE2   1 
ATOM   2934  N  N     . ASP A 1 362 ? 154.797 135.097 107.960 1.00 18.11 ?  362 ASP A N     1 
ATOM   2935  C  CA    . ASP A 1 362 ? 155.818 135.618 107.058 1.00 17.14 ?  362 ASP A CA    1 
ATOM   2936  C  C     . ASP A 1 362 ? 155.386 135.529 105.602 1.00 18.27 ?  362 ASP A C     1 
ATOM   2937  O  O     . ASP A 1 362 ? 155.762 136.387 104.799 1.00 19.69 ?  362 ASP A O     1 
ATOM   2938  C  CB    . ASP A 1 362 ? 157.137 134.886 107.280 1.00 18.97 ?  362 ASP A CB    1 
ATOM   2939  C  CG    . ASP A 1 362 ? 157.643 135.027 108.700 1.00 30.49 ?  362 ASP A CG    1 
ATOM   2940  O  OD1   . ASP A 1 362 ? 156.851 134.803 109.640 1.00 27.74 ?  362 ASP A OD1   1 
ATOM   2941  O  OD2   . ASP A 1 362 ? 158.832 135.363 108.877 1.00 34.52 -1 362 ASP A OD2   1 
ATOM   2942  N  N     . ASN A 1 363 ? 154.588 134.520 105.246 1.00 18.08 ?  363 ASN A N     1 
ATOM   2943  C  CA    . ASN A 1 363 ? 154.036 134.465 103.896 1.00 10.98 ?  363 ASN A CA    1 
ATOM   2944  C  C     . ASN A 1 363 ? 153.138 135.665 103.626 1.00 13.44 ?  363 ASN A C     1 
ATOM   2945  O  O     . ASN A 1 363 ? 153.116 136.197 102.510 1.00 21.41 ?  363 ASN A O     1 
ATOM   2946  C  CB    . ASN A 1 363 ? 153.268 133.160 103.693 1.00 11.67 ?  363 ASN A CB    1 
ATOM   2947  C  CG    . ASN A 1 363 ? 154.179 131.989 103.395 1.00 18.13 ?  363 ASN A CG    1 
ATOM   2948  O  OD1   . ASN A 1 363 ? 155.370 132.162 103.143 1.00 19.36 ?  363 ASN A OD1   1 
ATOM   2949  N  ND2   . ASN A 1 363 ? 153.622 130.786 103.421 1.00 18.77 ?  363 ASN A ND2   1 
ATOM   2950  N  N     . VAL A 1 364 ? 152.382 136.099 104.634 1.00 9.09  ?  364 VAL A N     1 
ATOM   2951  C  CA    . VAL A 1 364 ? 151.542 137.282 104.481 1.00 10.59 ?  364 VAL A CA    1 
ATOM   2952  C  C     . VAL A 1 364 ? 152.397 138.541 104.406 1.00 17.38 ?  364 VAL A C     1 
ATOM   2953  O  O     . VAL A 1 364 ? 152.170 139.417 103.563 1.00 16.12 ?  364 VAL A O     1 
ATOM   2954  C  CB    . VAL A 1 364 ? 150.524 137.370 105.632 1.00 1.48  ?  364 VAL A CB    1 
ATOM   2955  C  CG1   . VAL A 1 364 ? 149.597 138.553 105.424 1.00 4.43  ?  364 VAL A CG1   1 
ATOM   2956  C  CG2   . VAL A 1 364 ? 149.736 136.081 105.750 1.00 8.10  ?  364 VAL A CG2   1 
ATOM   2957  N  N     . ASN A 1 365 ? 153.396 138.649 105.281 1.00 21.00 ?  365 ASN A N     1 
ATOM   2958  C  CA    . ASN A 1 365 ? 154.100 139.907 105.484 1.00 11.91 ?  365 ASN A CA    1 
ATOM   2959  C  C     . ASN A 1 365 ? 155.279 140.120 104.543 1.00 15.26 ?  365 ASN A C     1 
ATOM   2960  O  O     . ASN A 1 365 ? 155.782 141.246 104.463 1.00 21.76 ?  365 ASN A O     1 
ATOM   2961  C  CB    . ASN A 1 365 ? 154.580 140.005 106.935 1.00 13.85 ?  365 ASN A CB    1 
ATOM   2962  C  CG    . ASN A 1 365 ? 153.449 140.285 107.900 1.00 15.71 ?  365 ASN A CG    1 
ATOM   2963  O  OD1   . ASN A 1 365 ? 152.708 141.254 107.740 1.00 12.41 ?  365 ASN A OD1   1 
ATOM   2964  N  ND2   . ASN A 1 365 ? 153.304 139.432 108.905 1.00 18.99 ?  365 ASN A ND2   1 
ATOM   2965  N  N     . LYS A 1 366 ? 155.733 139.091 103.828 1.00 19.00 ?  366 LYS A N     1 
ATOM   2966  C  CA    . LYS A 1 366 ? 156.786 139.288 102.842 1.00 15.84 ?  366 LYS A CA    1 
ATOM   2967  C  C     . LYS A 1 366 ? 156.270 139.925 101.562 1.00 19.99 ?  366 LYS A C     1 
ATOM   2968  O  O     . LYS A 1 366 ? 157.073 140.424 100.767 1.00 29.30 ?  366 LYS A O     1 
ATOM   2969  C  CB    . LYS A 1 366 ? 157.468 137.954 102.526 1.00 13.23 ?  366 LYS A CB    1 
ATOM   2970  C  CG    . LYS A 1 366 ? 156.744 137.104 101.499 1.00 19.82 ?  366 LYS A CG    1 
ATOM   2971  C  CD    . LYS A 1 366 ? 157.064 135.630 101.691 1.00 23.35 ?  366 LYS A CD    1 
ATOM   2972  C  CE    . LYS A 1 366 ? 156.234 134.756 100.765 1.00 26.32 ?  366 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A 1 366 ? 154.839 135.256 100.620 1.00 25.54 1  366 LYS A NZ    1 
ATOM   2974  N  N     . VAL A 1 367 ? 154.956 139.918 101.350 1.00 25.26 ?  367 VAL A N     1 
ATOM   2975  C  CA    . VAL A 1 367 ? 154.321 140.609 100.238 1.00 15.02 ?  367 VAL A CA    1 
ATOM   2976  C  C     . VAL A 1 367 ? 153.347 141.674 100.706 1.00 14.05 ?  367 VAL A C     1 
ATOM   2977  O  O     . VAL A 1 367 ? 152.674 142.291 99.875  1.00 18.32 ?  367 VAL A O     1 
ATOM   2978  C  CB    . VAL A 1 367 ? 153.615 139.615 99.294  1.00 13.12 ?  367 VAL A CB    1 
ATOM   2979  C  CG1   . VAL A 1 367 ? 154.632 138.914 98.411  1.00 17.27 ?  367 VAL A CG1   1 
ATOM   2980  C  CG2   . VAL A 1 367 ? 152.825 138.603 100.099 1.00 4.98  ?  367 VAL A CG2   1 
ATOM   2981  N  N     . HIS A 1 368 ? 153.250 141.908 102.012 1.00 14.46 ?  368 HIS A N     1 
ATOM   2982  C  CA    . HIS A 1 368 ? 152.365 142.937 102.540 1.00 6.03  ?  368 HIS A CA    1 
ATOM   2983  C  C     . HIS A 1 368 ? 152.870 144.316 102.138 1.00 15.52 ?  368 HIS A C     1 
ATOM   2984  O  O     . HIS A 1 368 ? 154.043 144.644 102.339 1.00 25.03 ?  368 HIS A O     1 
ATOM   2985  C  CB    . HIS A 1 368 ? 152.279 142.822 104.059 1.00 12.53 ?  368 HIS A CB    1 
ATOM   2986  C  CG    . HIS A 1 368 ? 151.237 143.701 104.676 1.00 8.17  ?  368 HIS A CG    1 
ATOM   2987  N  ND1   . HIS A 1 368 ? 151.417 144.325 105.891 1.00 13.52 ?  368 HIS A ND1   1 
ATOM   2988  C  CD2   . HIS A 1 368 ? 150.005 144.060 104.248 1.00 10.74 ?  368 HIS A CD2   1 
ATOM   2989  C  CE1   . HIS A 1 368 ? 150.340 145.029 106.185 1.00 15.09 ?  368 HIS A CE1   1 
ATOM   2990  N  NE2   . HIS A 1 368 ? 149.467 144.885 105.204 1.00 7.25  ?  368 HIS A NE2   1 
ATOM   2991  N  N     . ALA A 1 369 ? 151.978 145.126 101.569 1.00 18.25 ?  369 ALA A N     1 
ATOM   2992  C  CA    . ALA A 1 369 ? 152.364 146.443 101.087 1.00 12.50 ?  369 ALA A CA    1 
ATOM   2993  C  C     . ALA A 1 369 ? 152.374 147.500 102.181 1.00 17.79 ?  369 ALA A C     1 
ATOM   2994  O  O     . ALA A 1 369 ? 152.974 148.561 101.989 1.00 25.01 ?  369 ALA A O     1 
ATOM   2995  C  CB    . ALA A 1 369 ? 151.426 146.884 99.964  1.00 8.96  ?  369 ALA A CB    1 
ATOM   2996  N  N     . ASN A 1 370 ? 151.742 147.236 103.320 1.00 17.23 ?  370 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 370 ? 151.583 148.224 104.379 1.00 12.34 ?  370 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 370 ? 152.217 147.748 105.679 1.00 12.14 ?  370 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 370 ? 151.639 147.882 106.759 1.00 21.21 ?  370 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 370 ? 150.108 148.556 104.590 1.00 12.21 ?  370 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 370 ? 149.446 149.072 103.332 1.00 10.47 ?  370 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 370 ? 149.856 150.088 102.774 1.00 26.58 ?  370 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 370 ? 148.418 148.372 102.874 1.00 12.40 ?  370 ASN A ND2   1 
ATOM   3004  N  N     . ASN A 1 371 ? 153.423 147.183 105.590 1.00 14.37 ?  371 ASN A N     1 
ATOM   3005  C  CA    . ASN A 1 371 ? 154.144 146.782 106.791 1.00 11.15 ?  371 ASN A CA    1 
ATOM   3006  C  C     . ASN A 1 371 ? 154.572 147.975 107.633 1.00 16.52 ?  371 ASN A C     1 
ATOM   3007  O  O     . ASN A 1 371 ? 154.774 147.823 108.841 1.00 19.08 ?  371 ASN A O     1 
ATOM   3008  C  CB    . ASN A 1 371 ? 155.366 145.943 106.420 1.00 8.50  ?  371 ASN A CB    1 
ATOM   3009  C  CG    . ASN A 1 371 ? 155.032 144.478 106.244 1.00 16.56 ?  371 ASN A CG    1 
ATOM   3010  O  OD1   . ASN A 1 371 ? 154.047 143.986 106.791 1.00 20.95 ?  371 ASN A OD1   1 
ATOM   3011  N  ND2   . ASN A 1 371 ? 155.853 143.772 105.477 1.00 18.37 ?  371 ASN A ND2   1 
ATOM   3012  N  N     . HIS A 1 372 ? 154.725 149.152 107.020 1.00 19.53 ?  372 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 372 ? 155.066 150.347 107.784 1.00 15.92 ?  372 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 372 ? 153.959 150.708 108.767 1.00 16.49 ?  372 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 372 ? 154.236 151.090 109.910 1.00 25.78 ?  372 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 372 ? 155.344 151.512 106.835 1.00 18.05 ?  372 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 372 ? 154.141 151.968 106.071 1.00 18.35 ?  372 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 372 ? 153.469 151.153 105.186 1.00 23.68 ?  372 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 372 ? 153.483 153.151 106.067 1.00 18.43 ?  372 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 372 ? 152.449 151.815 104.669 1.00 17.06 ?  372 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 372 ? 152.437 153.030 105.184 1.00 17.38 ?  372 HIS A NE2   1 
ATOM   3022  N  N     . ILE A 1 373 ? 152.700 150.605 108.337 1.00 16.32 ?  373 ILE A N     1 
ATOM   3023  C  CA    . ILE A 1 373 ? 151.583 150.831 109.249 1.00 18.68 ?  373 ILE A CA    1 
ATOM   3024  C  C     . ILE A 1 373 ? 151.584 149.779 110.346 1.00 15.16 ?  373 ILE A C     1 
ATOM   3025  O  O     . ILE A 1 373 ? 151.547 150.095 111.542 1.00 28.13 ?  373 ILE A O     1 
ATOM   3026  C  CB    . ILE A 1 373 ? 150.252 150.828 108.477 1.00 19.22 ?  373 ILE A CB    1 
ATOM   3027  C  CG1   . ILE A 1 373 ? 150.252 151.911 107.401 1.00 15.45 ?  373 ILE A CG1   1 
ATOM   3028  C  CG2   . ILE A 1 373 ? 149.079 151.008 109.428 1.00 19.60 ?  373 ILE A CG2   1 
ATOM   3029  C  CD1   . ILE A 1 373 ? 149.123 151.783 106.409 1.00 15.20 ?  373 ILE A CD1   1 
ATOM   3030  N  N     . SER A 1 374 ? 151.655 148.509 109.949 1.00 16.92 ?  374 SER A N     1 
ATOM   3031  C  CA    . SER A 1 374 ? 151.675 147.377 110.862 1.00 12.66 ?  374 SER A CA    1 
ATOM   3032  C  C     . SER A 1 374 ? 151.867 146.096 110.067 1.00 14.27 ?  374 SER A C     1 
ATOM   3033  O  O     . SER A 1 374 ? 151.521 146.039 108.884 1.00 21.20 ?  374 SER A O     1 
ATOM   3034  C  CB    . SER A 1 374 ? 150.381 147.304 111.674 1.00 19.05 ?  374 SER A CB    1 
ATOM   3035  O  OG    . SER A 1 374 ? 150.502 146.384 112.741 1.00 24.05 ?  374 SER A OG    1 
ATOM   3036  N  N     . LYS A 1 375 ? 152.419 145.066 110.695 1.00 22.39 ?  375 LYS A N     1 
ATOM   3037  C  CA    . LYS A 1 375 ? 152.426 143.753 110.075 1.00 19.34 ?  375 LYS A CA    1 
ATOM   3038  C  C     . LYS A 1 375 ? 151.099 143.055 110.335 1.00 15.28 ?  375 LYS A C     1 
ATOM   3039  O  O     . LYS A 1 375 ? 150.454 143.264 111.365 1.00 22.44 ?  375 LYS A O     1 
ATOM   3040  C  CB    . LYS A 1 375 ? 153.587 142.910 110.602 1.00 12.06 ?  375 LYS A CB    1 
ATOM   3041  C  CG    . LYS A 1 375 ? 154.930 143.293 110.007 1.00 16.85 ?  375 LYS A CG    1 
ATOM   3042  C  CD    . LYS A 1 375 ? 155.950 142.184 110.172 1.00 24.65 ?  375 LYS A CD    1 
ATOM   3043  C  CE    . LYS A 1 375 ? 157.228 142.504 109.418 1.00 24.19 ?  375 LYS A CE    1 
ATOM   3044  N  NZ    . LYS A 1 375 ? 158.182 141.363 109.423 1.00 29.43 1  375 LYS A NZ    1 
ATOM   3045  N  N     . VAL A 1 376 ? 150.681 142.234 109.376 1.00 15.10 ?  376 VAL A N     1 
ATOM   3046  C  CA    . VAL A 1 376 ? 149.431 141.493 109.510 1.00 15.74 ?  376 VAL A CA    1 
ATOM   3047  C  C     . VAL A 1 376 ? 149.622 140.443 110.600 1.00 13.96 ?  376 VAL A C     1 
ATOM   3048  O  O     . VAL A 1 376 ? 150.395 139.496 110.433 1.00 20.44 ?  376 VAL A O     1 
ATOM   3049  C  CB    . VAL A 1 376 ? 149.008 140.855 108.184 1.00 10.94 ?  376 VAL A CB    1 
ATOM   3050  C  CG1   . VAL A 1 376 ? 147.671 140.156 108.338 1.00 8.26  ?  376 VAL A CG1   1 
ATOM   3051  C  CG2   . VAL A 1 376 ? 148.944 141.906 107.089 1.00 3.91  ?  376 VAL A CG2   1 
ATOM   3052  N  N     . LYS A 1 377 ? 148.922 140.612 111.721 1.00 12.77 ?  377 LYS A N     1 
ATOM   3053  C  CA    . LYS A 1 377 ? 149.079 139.723 112.862 1.00 11.43 ?  377 LYS A CA    1 
ATOM   3054  C  C     . LYS A 1 377 ? 148.036 138.619 112.918 1.00 10.48 ?  377 LYS A C     1 
ATOM   3055  O  O     . LYS A 1 377 ? 148.271 137.608 113.585 1.00 24.90 ?  377 LYS A O     1 
ATOM   3056  C  CB    . LYS A 1 377 ? 149.019 140.517 114.171 1.00 15.92 ?  377 LYS A CB    1 
ATOM   3057  C  CG    . LYS A 1 377 ? 149.970 141.691 114.241 1.00 12.28 ?  377 LYS A CG    1 
ATOM   3058  C  CD    . LYS A 1 377 ? 149.384 142.781 115.112 1.00 21.26 ?  377 LYS A CD    1 
ATOM   3059  C  CE    . LYS A 1 377 ? 150.037 144.118 114.843 1.00 23.69 ?  377 LYS A CE    1 
ATOM   3060  N  NZ    . LYS A 1 377 ? 149.187 145.246 115.312 1.00 26.00 1  377 LYS A NZ    1 
ATOM   3061  N  N     . PHE A 1 378 ? 146.899 138.788 112.250 1.00 8.60  ?  378 PHE A N     1 
ATOM   3062  C  CA    . PHE A 1 378 ? 145.832 137.800 112.300 1.00 7.85  ?  378 PHE A CA    1 
ATOM   3063  C  C     . PHE A 1 378 ? 144.904 138.025 111.116 1.00 8.00  ?  378 PHE A C     1 
ATOM   3064  O  O     . PHE A 1 378 ? 145.038 138.997 110.370 1.00 15.64 ?  378 PHE A O     1 
ATOM   3065  C  CB    . PHE A 1 378 ? 145.075 137.858 113.633 1.00 6.52  ?  378 PHE A CB    1 
ATOM   3066  C  CG    . PHE A 1 378 ? 144.216 139.082 113.805 1.00 8.31  ?  378 PHE A CG    1 
ATOM   3067  C  CD1   . PHE A 1 378 ? 144.772 140.351 113.780 1.00 9.59  ?  378 PHE A CD1   1 
ATOM   3068  C  CD2   . PHE A 1 378 ? 142.855 138.959 114.017 1.00 5.15  ?  378 PHE A CD2   1 
ATOM   3069  C  CE1   . PHE A 1 378 ? 143.986 141.469 113.946 1.00 4.02  ?  378 PHE A CE1   1 
ATOM   3070  C  CE2   . PHE A 1 378 ? 142.065 140.075 114.184 1.00 9.56  ?  378 PHE A CE2   1 
ATOM   3071  C  CZ    . PHE A 1 378 ? 142.632 141.332 114.149 1.00 11.53 ?  378 PHE A CZ    1 
ATOM   3072  N  N     . SER A 1 379 ? 143.962 137.104 110.951 1.00 3.31  ?  379 SER A N     1 
ATOM   3073  C  CA    . SER A 1 379 ? 143.028 137.111 109.834 1.00 4.14  ?  379 SER A CA    1 
ATOM   3074  C  C     . SER A 1 379 ? 141.599 137.211 110.365 1.00 5.96  ?  379 SER A C     1 
ATOM   3075  O  O     . SER A 1 379 ? 141.368 137.411 111.559 1.00 12.37 ?  379 SER A O     1 
ATOM   3076  C  CB    . SER A 1 379 ? 143.225 135.868 108.965 1.00 5.03  ?  379 SER A CB    1 
ATOM   3077  O  OG    . SER A 1 379 ? 142.796 136.107 107.637 1.00 8.38  ?  379 SER A OG    1 
ATOM   3078  N  N     . ASN A 1 380 ? 140.636 137.074 109.460 1.00 11.92 ?  380 ASN A N     1 
ATOM   3079  C  CA    . ASN A 1 380 ? 139.231 137.223 109.787 1.00 9.17  ?  380 ASN A CA    1 
ATOM   3080  C  C     . ASN A 1 380 ? 138.612 135.863 110.103 1.00 9.46  ?  380 ASN A C     1 
ATOM   3081  O  O     . ASN A 1 380 ? 139.301 134.845 110.210 1.00 9.92  ?  380 ASN A O     1 
ATOM   3082  C  CB    . ASN A 1 380 ? 138.495 137.925 108.645 1.00 2.71  ?  380 ASN A CB    1 
ATOM   3083  C  CG    . ASN A 1 380 ? 138.374 137.060 107.411 1.00 3.90  ?  380 ASN A CG    1 
ATOM   3084  O  OD1   . ASN A 1 380 ? 139.359 136.507 106.925 1.00 12.64 ?  380 ASN A OD1   1 
ATOM   3085  N  ND2   . ASN A 1 380 ? 137.159 136.938 106.894 1.00 10.73 ?  380 ASN A ND2   1 
ATOM   3086  N  N     . LEU A 1 381 ? 137.287 135.850 110.262 1.00 17.84 ?  381 LEU A N     1 
ATOM   3087  C  CA    . LEU A 1 381 ? 136.563 134.612 110.524 1.00 6.52  ?  381 LEU A CA    1 
ATOM   3088  C  C     . LEU A 1 381 ? 136.641 133.638 109.355 1.00 6.70  ?  381 LEU A C     1 
ATOM   3089  O  O     . LEU A 1 381 ? 136.560 132.425 109.569 1.00 15.30 ?  381 LEU A O     1 
ATOM   3090  C  CB    . LEU A 1 381 ? 135.105 134.937 110.855 1.00 11.71 ?  381 LEU A CB    1 
ATOM   3091  C  CG    . LEU A 1 381 ? 134.089 133.806 111.022 1.00 20.37 ?  381 LEU A CG    1 
ATOM   3092  C  CD1   . LEU A 1 381 ? 134.419 132.943 112.226 1.00 14.47 ?  381 LEU A CD1   1 
ATOM   3093  C  CD2   . LEU A 1 381 ? 132.688 134.378 111.136 1.00 15.89 ?  381 LEU A CD2   1 
ATOM   3094  N  N     . CYS A 1 382 ? 136.805 134.136 108.132 1.00 8.83  ?  382 CYS A N     1 
ATOM   3095  C  CA    . CYS A 1 382 ? 136.943 133.292 106.955 1.00 6.39  ?  382 CYS A CA    1 
ATOM   3096  C  C     . CYS A 1 382 ? 138.390 133.131 106.513 1.00 10.63 ?  382 CYS A C     1 
ATOM   3097  O  O     . CYS A 1 382 ? 138.645 132.460 105.506 1.00 17.01 ?  382 CYS A O     1 
ATOM   3098  C  CB    . CYS A 1 382 ? 136.105 133.853 105.802 1.00 15.57 ?  382 CYS A CB    1 
ATOM   3099  S  SG    . CYS A 1 382 ? 134.357 134.093 106.201 1.00 35.34 ?  382 CYS A SG    1 
ATOM   3100  N  N     . SER A 1 383 ? 139.337 133.726 107.240 1.00 11.05 ?  383 SER A N     1 
ATOM   3101  C  CA    . SER A 1 383 ? 140.771 133.560 106.994 1.00 8.94  ?  383 SER A CA    1 
ATOM   3102  C  C     . SER A 1 383 ? 141.164 133.979 105.579 1.00 12.51 ?  383 SER A C     1 
ATOM   3103  O  O     . SER A 1 383 ? 141.907 133.279 104.890 1.00 22.80 ?  383 SER A O     1 
ATOM   3104  C  CB    . SER A 1 383 ? 141.215 132.122 107.274 1.00 12.13 ?  383 SER A CB    1 
ATOM   3105  O  OG    . SER A 1 383 ? 140.826 131.259 106.222 1.00 20.92 ?  383 SER A OG    1 
ATOM   3106  N  N     . GLU A 1 384 ? 140.660 135.129 105.134 1.00 8.02  ?  384 GLU A N     1 
ATOM   3107  C  CA    . GLU A 1 384 ? 141.097 135.703 103.869 1.00 11.46 ?  384 GLU A CA    1 
ATOM   3108  C  C     . GLU A 1 384 ? 141.408 137.190 103.947 1.00 13.32 ?  384 GLU A C     1 
ATOM   3109  O  O     . GLU A 1 384 ? 142.051 137.713 103.030 1.00 22.51 ?  384 GLU A O     1 
ATOM   3110  C  CB    . GLU A 1 384 ? 140.051 135.453 102.767 1.00 6.55  ?  384 GLU A CB    1 
ATOM   3111  C  CG    . GLU A 1 384 ? 139.202 136.648 102.362 1.00 7.25  ?  384 GLU A CG    1 
ATOM   3112  C  CD    . GLU A 1 384 ? 138.038 136.888 103.296 1.00 16.76 ?  384 GLU A CD    1 
ATOM   3113  O  OE1   . GLU A 1 384 ? 137.700 135.972 104.071 1.00 19.97 ?  384 GLU A OE1   1 
ATOM   3114  O  OE2   . GLU A 1 384 ? 137.448 137.985 103.240 1.00 21.02 -1 384 GLU A OE2   1 
ATOM   3115  N  N     . VAL A 1 385 ? 141.001 137.879 105.006 1.00 13.29 ?  385 VAL A N     1 
ATOM   3116  C  CA    . VAL A 1 385 ? 141.329 139.288 105.190 1.00 3.12  ?  385 VAL A CA    1 
ATOM   3117  C  C     . VAL A 1 385 ? 142.669 139.376 105.905 1.00 15.14 ?  385 VAL A C     1 
ATOM   3118  O  O     . VAL A 1 385 ? 142.818 138.880 107.027 1.00 19.40 ?  385 VAL A O     1 
ATOM   3119  C  CB    . VAL A 1 385 ? 140.235 140.018 105.980 1.00 3.77  ?  385 VAL A CB    1 
ATOM   3120  C  CG1   . VAL A 1 385 ? 140.582 141.480 106.110 1.00 10.14 ?  385 VAL A CG1   1 
ATOM   3121  C  CG2   . VAL A 1 385 ? 138.895 139.854 105.302 1.00 8.54  ?  385 VAL A CG2   1 
ATOM   3122  N  N     . LEU A 1 386 ? 143.646 140.005 105.257 1.00 16.86 ?  386 LEU A N     1 
ATOM   3123  C  CA    . LEU A 1 386 ? 144.998 140.135 105.794 1.00 3.54  ?  386 LEU A CA    1 
ATOM   3124  C  C     . LEU A 1 386 ? 145.431 141.588 105.638 1.00 7.34  ?  386 LEU A C     1 
ATOM   3125  O  O     . LEU A 1 386 ? 145.890 141.996 104.568 1.00 8.00  ?  386 LEU A O     1 
ATOM   3126  C  CB    . LEU A 1 386 ? 145.959 139.187 105.090 1.00 3.17  ?  386 LEU A CB    1 
ATOM   3127  C  CG    . LEU A 1 386 ? 145.622 137.712 105.290 1.00 7.86  ?  386 LEU A CG    1 
ATOM   3128  C  CD1   . LEU A 1 386 ? 146.483 136.858 104.404 1.00 9.37  ?  386 LEU A CD1   1 
ATOM   3129  C  CD2   . LEU A 1 386 ? 145.796 137.324 106.746 1.00 6.77  ?  386 LEU A CD2   1 
ATOM   3130  N  N     . GLN A 1 387 ? 145.286 142.365 106.708 1.00 14.69 ?  387 GLN A N     1 
ATOM   3131  C  CA    . GLN A 1 387 ? 145.538 143.795 106.663 1.00 4.40  ?  387 GLN A CA    1 
ATOM   3132  C  C     . GLN A 1 387 ? 146.314 144.225 107.897 1.00 6.85  ?  387 GLN A C     1 
ATOM   3133  O  O     . GLN A 1 387 ? 146.341 143.534 108.917 1.00 18.95 ?  387 GLN A O     1 
ATOM   3134  C  CB    . GLN A 1 387 ? 144.233 144.594 106.566 1.00 6.31  ?  387 GLN A CB    1 
ATOM   3135  C  CG    . GLN A 1 387 ? 143.362 144.204 105.396 1.00 8.48  ?  387 GLN A CG    1 
ATOM   3136  C  CD    . GLN A 1 387 ? 142.207 145.151 105.203 1.00 6.84  ?  387 GLN A CD    1 
ATOM   3137  O  OE1   . GLN A 1 387 ? 142.139 146.200 105.839 1.00 19.59 ?  387 GLN A OE1   1 
ATOM   3138  N  NE2   . GLN A 1 387 ? 141.297 144.793 104.314 1.00 8.43  ?  387 GLN A NE2   1 
ATOM   3139  N  N     . ALA A 1 388 ? 146.963 145.379 107.781 1.00 10.17 ?  388 ALA A N     1 
ATOM   3140  C  CA    . ALA A 1 388 ? 147.636 145.980 108.922 1.00 9.47  ?  388 ALA A CA    1 
ATOM   3141  C  C     . ALA A 1 388 ? 146.615 146.462 109.944 1.00 14.32 ?  388 ALA A C     1 
ATOM   3142  O  O     . ALA A 1 388 ? 145.594 147.059 109.593 1.00 25.46 ?  388 ALA A O     1 
ATOM   3143  C  CB    . ALA A 1 388 ? 148.513 147.145 108.467 1.00 12.02 ?  388 ALA A CB    1 
ATOM   3144  N  N     . SER A 1 389 ? 146.891 146.191 111.216 1.00 17.96 ?  389 SER A N     1 
ATOM   3145  C  CA    . SER A 1 389 ? 146.022 146.620 112.300 1.00 8.83  ?  389 SER A CA    1 
ATOM   3146  C  C     . SER A 1 389 ? 146.867 147.169 113.437 1.00 13.12 ?  389 SER A C     1 
ATOM   3147  O  O     . SER A 1 389 ? 147.943 146.642 113.732 1.00 24.46 ?  389 SER A O     1 
ATOM   3148  C  CB    . SER A 1 389 ? 145.146 145.470 112.808 1.00 16.70 ?  389 SER A CB    1 
ATOM   3149  O  OG    . SER A 1 389 ? 145.894 144.273 112.931 1.00 21.83 ?  389 SER A OG    1 
ATOM   3150  N  N     . GLN A 1 390 ? 146.373 148.227 114.072 1.00 17.64 ?  390 GLN A N     1 
ATOM   3151  C  CA    . GLN A 1 390 ? 147.013 148.820 115.237 1.00 14.92 ?  390 GLN A CA    1 
ATOM   3152  C  C     . GLN A 1 390 ? 146.084 148.670 116.430 1.00 13.36 ?  390 GLN A C     1 
ATOM   3153  O  O     . GLN A 1 390 ? 144.898 149.000 116.343 1.00 17.32 ?  390 GLN A O     1 
ATOM   3154  C  CB    . GLN A 1 390 ? 147.346 150.294 114.998 1.00 10.33 ?  390 GLN A CB    1 
ATOM   3155  C  CG    . GLN A 1 390 ? 148.508 150.517 114.046 1.00 15.85 ?  390 GLN A CG    1 
ATOM   3156  C  CD    . GLN A 1 390 ? 148.626 151.957 113.593 1.00 25.93 ?  390 GLN A CD    1 
ATOM   3157  O  OE1   . GLN A 1 390 ? 147.763 152.784 113.886 1.00 24.72 ?  390 GLN A OE1   1 
ATOM   3158  N  NE2   . GLN A 1 390 ? 149.697 152.264 112.871 1.00 21.61 ?  390 GLN A NE2   1 
ATOM   3159  N  N     . VAL A 1 391 ? 146.625 148.165 117.540 1.00 24.05 ?  391 VAL A N     1 
ATOM   3160  C  CA    . VAL A 1 391 ? 145.814 147.946 118.728 1.00 20.62 ?  391 VAL A CA    1 
ATOM   3161  C  C     . VAL A 1 391 ? 145.394 149.286 119.323 1.00 22.62 ?  391 VAL A C     1 
ATOM   3162  O  O     . VAL A 1 391 ? 146.082 150.306 119.180 1.00 24.03 ?  391 VAL A O     1 
ATOM   3163  C  CB    . VAL A 1 391 ? 146.572 147.085 119.756 1.00 19.09 ?  391 VAL A CB    1 
ATOM   3164  C  CG1   . VAL A 1 391 ? 147.570 147.925 120.540 1.00 20.19 ?  391 VAL A CG1   1 
ATOM   3165  C  CG2   . VAL A 1 391 ? 145.598 146.385 120.690 1.00 17.61 ?  391 VAL A CG2   1 
ATOM   3166  N  N     . SER A 1 392 ? 144.240 149.288 119.978 1.00 27.56 ?  392 SER A N     1 
ATOM   3167  C  CA    . SER A 1 392 ? 143.719 150.471 120.642 1.00 19.89 ?  392 SER A CA    1 
ATOM   3168  C  C     . SER A 1 392 ? 143.920 150.355 122.146 1.00 29.15 ?  392 SER A C     1 
ATOM   3169  O  O     . SER A 1 392 ? 143.865 149.264 122.718 1.00 29.80 ?  392 SER A O     1 
ATOM   3170  C  CB    . SER A 1 392 ? 142.235 150.667 120.329 1.00 20.67 ?  392 SER A CB    1 
ATOM   3171  O  OG    . SER A 1 392 ? 142.014 150.773 118.934 1.00 27.89 ?  392 SER A OG    1 
ATOM   3172  N  N     . SER A 1 393 ? 144.159 151.495 122.783 1.00 31.70 ?  393 SER A N     1 
ATOM   3173  C  CA    . SER A 1 393 ? 144.325 151.575 124.232 1.00 28.10 ?  393 SER A CA    1 
ATOM   3174  C  C     . SER A 1 393 ? 143.041 152.164 124.805 1.00 30.16 ?  393 SER A C     1 
ATOM   3175  O  O     . SER A 1 393 ? 142.897 153.382 124.928 1.00 34.98 ?  393 SER A O     1 
ATOM   3176  C  CB    . SER A 1 393 ? 145.544 152.412 124.603 1.00 30.37 ?  393 SER A CB    1 
ATOM   3177  O  OG    . SER A 1 393 ? 146.742 151.687 124.394 1.00 36.82 ?  393 SER A OG    1 
ATOM   3178  N  N     . TYR A 1 394 ? 142.101 151.289 125.147 1.00 29.20 ?  394 TYR A N     1 
ATOM   3179  C  CA    . TYR A 1 394 ? 140.853 151.709 125.770 1.00 28.90 ?  394 TYR A CA    1 
ATOM   3180  C  C     . TYR A 1 394 ? 141.095 151.872 127.265 1.00 28.85 ?  394 TYR A C     1 
ATOM   3181  O  O     . TYR A 1 394 ? 141.258 150.885 127.987 1.00 33.55 ?  394 TYR A O     1 
ATOM   3182  C  CB    . TYR A 1 394 ? 139.749 150.695 125.490 1.00 24.98 ?  394 TYR A CB    1 
ATOM   3183  C  CG    . TYR A 1 394 ? 139.309 150.663 124.045 1.00 28.24 ?  394 TYR A CG    1 
ATOM   3184  C  CD1   . TYR A 1 394 ? 138.533 151.683 123.512 1.00 29.50 ?  394 TYR A CD1   1 
ATOM   3185  C  CD2   . TYR A 1 394 ? 139.678 149.615 123.210 1.00 26.55 ?  394 TYR A CD2   1 
ATOM   3186  C  CE1   . TYR A 1 394 ? 138.130 151.657 122.192 1.00 28.34 ?  394 TYR A CE1   1 
ATOM   3187  C  CE2   . TYR A 1 394 ? 139.278 149.582 121.890 1.00 27.08 ?  394 TYR A CE2   1 
ATOM   3188  C  CZ    . TYR A 1 394 ? 138.506 150.605 121.386 1.00 36.10 ?  394 TYR A CZ    1 
ATOM   3189  O  OH    . TYR A 1 394 ? 138.108 150.575 120.069 1.00 38.36 ?  394 TYR A OH    1 
ATOM   3190  N  N     . THR A 1 395 ? 141.121 153.117 127.727 1.00 35.82 ?  395 THR A N     1 
ATOM   3191  C  CA    . THR A 1 395 ? 141.456 153.428 129.106 1.00 37.45 ?  395 THR A CA    1 
ATOM   3192  C  C     . THR A 1 395 ? 140.206 153.347 129.981 1.00 38.54 ?  395 THR A C     1 
ATOM   3193  O  O     . THR A 1 395 ? 139.157 152.850 129.564 1.00 38.57 ?  395 THR A O     1 
ATOM   3194  C  CB    . THR A 1 395 ? 142.115 154.804 129.185 1.00 36.92 ?  395 THR A CB    1 
ATOM   3195  O  OG1   . THR A 1 395 ? 141.229 155.789 128.640 1.00 38.62 ?  395 THR A OG1   1 
ATOM   3196  C  CG2   . THR A 1 395 ? 143.416 154.813 128.399 1.00 35.25 ?  395 THR A CG2   1 
ATOM   3197  N  N     . ASP A 1 396 ? 140.312 153.835 131.214 1.00 36.30 ?  396 ASP A N     1 
ATOM   3198  C  CA    . ASP A 1 396 ? 139.182 153.851 132.128 1.00 36.61 ?  396 ASP A CA    1 
ATOM   3199  C  C     . ASP A 1 396 ? 138.125 154.841 131.639 1.00 38.06 ?  396 ASP A C     1 
ATOM   3200  O  O     . ASP A 1 396 ? 138.280 155.506 130.611 1.00 42.28 ?  396 ASP A O     1 
ATOM   3201  C  CB    . ASP A 1 396 ? 139.642 154.211 133.539 1.00 38.06 ?  396 ASP A CB    1 
ATOM   3202  C  CG    . ASP A 1 396 ? 140.743 153.302 134.048 1.00 42.51 ?  396 ASP A CG    1 
ATOM   3203  O  OD1   . ASP A 1 396 ? 140.834 152.149 133.576 1.00 43.52 ?  396 ASP A OD1   1 
ATOM   3204  O  OD2   . ASP A 1 396 ? 141.514 153.740 134.925 1.00 44.02 -1 396 ASP A OD2   1 
ATOM   3205  N  N     . TYR A 1 397 ? 137.031 154.936 132.391 1.00 37.44 ?  397 TYR A N     1 
ATOM   3206  C  CA    . TYR A 1 397 ? 136.023 155.938 132.097 1.00 34.06 ?  397 TYR A CA    1 
ATOM   3207  C  C     . TYR A 1 397 ? 136.619 157.336 132.265 1.00 37.34 ?  397 TYR A C     1 
ATOM   3208  O  O     . TYR A 1 397 ? 137.725 157.507 132.776 1.00 39.74 ?  397 TYR A O     1 
ATOM   3209  C  CB    . TYR A 1 397 ? 134.802 155.751 132.997 1.00 33.65 ?  397 TYR A CB    1 
ATOM   3210  C  CG    . TYR A 1 397 ? 133.520 156.289 132.402 1.00 33.80 ?  397 TYR A CG    1 
ATOM   3211  C  CD1   . TYR A 1 397 ? 132.772 155.526 131.517 1.00 36.07 ?  397 TYR A CD1   1 
ATOM   3212  C  CD2   . TYR A 1 397 ? 133.058 157.558 132.728 1.00 34.56 ?  397 TYR A CD2   1 
ATOM   3213  C  CE1   . TYR A 1 397 ? 131.601 156.012 130.971 1.00 33.88 ?  397 TYR A CE1   1 
ATOM   3214  C  CE2   . TYR A 1 397 ? 131.890 158.052 132.187 1.00 31.84 ?  397 TYR A CE2   1 
ATOM   3215  C  CZ    . TYR A 1 397 ? 131.165 157.275 131.311 1.00 34.09 ?  397 TYR A CZ    1 
ATOM   3216  O  OH    . TYR A 1 397 ? 129.999 157.764 130.770 1.00 39.73 ?  397 TYR A OH    1 
ATOM   3217  N  N     . ASP A 1 398 ? 135.883 158.330 131.757 1.00 41.00 ?  398 ASP A N     1 
ATOM   3218  C  CA    . ASP A 1 398 ? 136.219 159.756 131.732 1.00 42.01 ?  398 ASP A CA    1 
ATOM   3219  C  C     . ASP A 1 398 ? 137.700 159.981 131.434 1.00 44.08 ?  398 ASP A C     1 
ATOM   3220  O  O     . ASP A 1 398 ? 138.319 160.925 131.935 1.00 41.83 ?  398 ASP A O     1 
ATOM   3221  C  CB    . ASP A 1 398 ? 135.749 160.469 133.023 1.00 41.67 ?  398 ASP A CB    1 
ATOM   3222  C  CG    . ASP A 1 398 ? 136.672 160.282 134.237 1.00 44.94 ?  398 ASP A CG    1 
ATOM   3223  O  OD1   . ASP A 1 398 ? 136.450 161.007 135.229 1.00 45.96 ?  398 ASP A OD1   1 
ATOM   3224  O  OD2   . ASP A 1 398 ? 137.605 159.464 134.237 1.00 42.18 -1 398 ASP A OD2   1 
ATOM   3225  N  N     . GLU A 1 399 ? 138.256 159.125 130.578 1.00 48.02 ?  399 GLU A N     1 
ATOM   3226  C  CA    . GLU A 1 399 ? 139.637 159.201 130.133 1.00 43.95 ?  399 GLU A CA    1 
ATOM   3227  C  C     . GLU A 1 399 ? 139.671 158.904 128.643 1.00 44.55 ?  399 GLU A C     1 
ATOM   3228  O  O     . GLU A 1 399 ? 138.997 157.982 128.172 1.00 42.49 ?  399 GLU A O     1 
ATOM   3229  C  CB    . GLU A 1 399 ? 140.526 158.212 130.897 1.00 39.19 ?  399 GLU A CB    1 
ATOM   3230  C  CG    . GLU A 1 399 ? 141.946 158.698 131.127 1.00 42.93 ?  399 GLU A CG    1 
ATOM   3231  C  CD    . GLU A 1 399 ? 142.897 157.572 131.484 1.00 48.39 ?  399 GLU A CD    1 
ATOM   3232  O  OE1   . GLU A 1 399 ? 142.469 156.626 132.177 1.00 47.56 ?  399 GLU A OE1   1 
ATOM   3233  O  OE2   . GLU A 1 399 ? 144.074 157.635 131.073 1.00 47.06 -1 399 GLU A OE2   1 
ATOM   3234  N  N     . GLU A 1 400 ? 140.451 159.687 127.904 1.00 44.73 ?  400 GLU A N     1 
ATOM   3235  C  CA    . GLU A 1 400 ? 140.458 159.571 126.452 1.00 40.43 ?  400 GLU A CA    1 
ATOM   3236  C  C     . GLU A 1 400 ? 141.118 158.270 126.017 1.00 43.83 ?  400 GLU A C     1 
ATOM   3237  O  O     . GLU A 1 400 ? 142.226 157.944 126.454 1.00 43.14 ?  400 GLU A O     1 
ATOM   3238  C  CB    . GLU A 1 400 ? 141.179 160.766 125.832 1.00 40.22 ?  400 GLU A CB    1 
ATOM   3239  C  CG    . GLU A 1 400 ? 140.483 161.345 124.610 1.00 45.83 ?  400 GLU A CG    1 
ATOM   3240  C  CD    . GLU A 1 400 ? 139.056 161.776 124.896 1.00 48.85 ?  400 GLU A CD    1 
ATOM   3241  O  OE1   . GLU A 1 400 ? 138.804 162.320 125.991 1.00 46.49 ?  400 GLU A OE1   1 
ATOM   3242  O  OE2   . GLU A 1 400 ? 138.186 161.570 124.024 1.00 47.21 -1 400 GLU A OE2   1 
ATOM   3243  N  N     . ASP A 1 401 ? 140.432 157.528 125.152 1.00 35.69 ?  401 ASP A N     1 
ATOM   3244  C  CA    . ASP A 1 401 ? 140.982 156.301 124.597 1.00 33.74 ?  401 ASP A CA    1 
ATOM   3245  C  C     . ASP A 1 401 ? 141.923 156.615 123.442 1.00 34.42 ?  401 ASP A C     1 
ATOM   3246  O  O     . ASP A 1 401 ? 141.771 157.621 122.744 1.00 38.08 ?  401 ASP A O     1 
ATOM   3247  C  CB    . ASP A 1 401 ? 139.864 155.378 124.112 1.00 32.53 ?  401 ASP A CB    1 
ATOM   3248  C  CG    . ASP A 1 401 ? 138.822 155.108 125.177 1.00 37.68 ?  401 ASP A CG    1 
ATOM   3249  O  OD1   . ASP A 1 401 ? 139.189 154.601 126.256 1.00 42.07 ?  401 ASP A OD1   1 
ATOM   3250  O  OD2   . ASP A 1 401 ? 137.634 155.402 124.932 1.00 38.40 -1 401 ASP A OD2   1 
ATOM   3251  N  N     . GLU A 1 402 ? 142.903 155.739 123.243 1.00 31.60 ?  402 GLU A N     1 
ATOM   3252  C  CA    . GLU A 1 402 ? 143.799 155.817 122.092 1.00 29.37 ?  402 GLU A CA    1 
ATOM   3253  C  C     . GLU A 1 402 ? 143.230 154.860 121.051 1.00 24.85 ?  402 GLU A C     1 
ATOM   3254  O  O     . GLU A 1 402 ? 143.348 153.640 121.179 1.00 30.34 ?  402 GLU A O     1 
ATOM   3255  C  CB    . GLU A 1 402 ? 145.234 155.473 122.484 1.00 31.18 ?  402 GLU A CB    1 
ATOM   3256  C  CG    . GLU A 1 402 ? 146.187 155.209 121.316 1.00 36.78 ?  402 GLU A CG    1 
ATOM   3257  C  CD    . GLU A 1 402 ? 146.263 153.748 120.908 1.00 40.42 ?  402 GLU A CD    1 
ATOM   3258  O  OE1   . GLU A 1 402 ? 146.773 152.931 121.701 1.00 35.31 ?  402 GLU A OE1   1 
ATOM   3259  O  OE2   . GLU A 1 402 ? 145.818 153.418 119.789 1.00 34.93 -1 402 GLU A OE2   1 
ATOM   3260  N  N     . ILE A 1 403 ? 142.579 155.416 120.036 1.00 27.50 ?  403 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 403 ? 141.897 154.608 119.033 1.00 26.57 ?  403 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 403 ? 142.898 154.181 117.969 1.00 28.07 ?  403 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 403 ? 143.583 155.017 117.369 1.00 28.44 ?  403 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 403 ? 140.722 155.384 118.416 1.00 24.55 ?  403 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 403 ? 139.708 155.764 119.496 1.00 24.49 ?  403 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 403 ? 140.056 154.564 117.325 1.00 20.31 ?  403 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 403 ? 139.275 154.607 120.367 1.00 26.84 ?  403 ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 404 ? 142.987 152.879 117.738 1.00 23.34 ?  404 GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 404 ? 143.859 152.305 116.737 1.00 9.27  ?  404 GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 404 ? 143.131 152.005 115.444 1.00 19.17 ?  404 GLY A C     1 
ATOM   3271  O  O     . GLY A 1 404 ? 142.181 152.698 115.061 1.00 31.31 ?  404 GLY A O     1 
ATOM   3272  N  N     . LEU A 1 405 ? 143.581 150.956 114.760 1.00 22.22 ?  405 LEU A N     1 
ATOM   3273  C  CA    . LEU A 1 405 ? 142.999 150.533 113.493 1.00 7.02  ?  405 LEU A CA    1 
ATOM   3274  C  C     . LEU A 1 405 ? 142.500 149.103 113.632 1.00 8.34  ?  405 LEU A C     1 
ATOM   3275  O  O     . LEU A 1 405 ? 143.283 148.196 113.929 1.00 18.34 ?  405 LEU A O     1 
ATOM   3276  C  CB    . LEU A 1 405 ? 144.020 150.637 112.358 1.00 17.23 ?  405 LEU A CB    1 
ATOM   3277  C  CG    . LEU A 1 405 ? 144.600 152.024 112.081 1.00 18.22 ?  405 LEU A CG    1 
ATOM   3278  C  CD1   . LEU A 1 405 ? 145.711 151.945 111.048 1.00 21.75 ?  405 LEU A CD1   1 
ATOM   3279  C  CD2   . LEU A 1 405 ? 143.513 152.983 111.631 1.00 15.48 ?  405 LEU A CD2   1 
ATOM   3280  N  N     . ASP A 1 406 ? 141.204 148.906 113.413 1.00 22.38 ?  406 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 406 ? 140.594 147.584 113.396 1.00 17.43 ?  406 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 406 ? 140.068 147.305 111.996 1.00 19.13 ?  406 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 406 ? 139.324 148.114 111.435 1.00 31.28 ?  406 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 406 ? 139.467 147.481 114.424 1.00 18.37 ?  406 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 406 ? 139.970 147.129 115.810 1.00 29.15 ?  406 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 406 ? 141.202 147.032 115.995 1.00 32.47 ?  406 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 406 ? 139.133 146.953 116.718 1.00 28.37 -1 406 ASP A OD2   1 
ATOM   3288  N  N     . ILE A 1 407 ? 140.439 146.158 111.450 1.00 21.24 ?  407 ILE A N     1 
ATOM   3289  C  CA    . ILE A 1 407 ? 140.210 145.868 110.041 1.00 15.66 ?  407 ILE A CA    1 
ATOM   3290  C  C     . ILE A 1 407 ? 138.737 145.585 109.792 1.00 14.81 ?  407 ILE A C     1 
ATOM   3291  O  O     . ILE A 1 407 ? 138.082 144.864 110.555 1.00 21.70 ?  407 ILE A O     1 
ATOM   3292  C  CB    . ILE A 1 407 ? 141.084 144.684 109.594 1.00 10.60 ?  407 ILE A CB    1 
ATOM   3293  C  CG1   . ILE A 1 407 ? 142.564 145.007 109.789 1.00 6.69  ?  407 ILE A CG1   1 
ATOM   3294  C  CG2   . ILE A 1 407 ? 140.796 144.332 108.157 1.00 16.52 ?  407 ILE A CG2   1 
ATOM   3295  C  CD1   . ILE A 1 407 ? 143.388 143.807 110.167 1.00 10.78 ?  407 ILE A CD1   1 
ATOM   3296  N  N     . SER A 1 408 ? 138.210 146.163 108.714 1.00 25.69 ?  408 SER A N     1 
ATOM   3297  C  CA    . SER A 1 408 ? 136.872 145.840 108.230 1.00 21.75 ?  408 SER A CA    1 
ATOM   3298  C  C     . SER A 1 408 ? 136.865 146.101 106.732 1.00 24.54 ?  408 SER A C     1 
ATOM   3299  O  O     . SER A 1 408 ? 136.698 147.248 106.307 1.00 30.62 ?  408 SER A O     1 
ATOM   3300  C  CB    . SER A 1 408 ? 135.809 146.674 108.938 1.00 26.05 ?  408 SER A CB    1 
ATOM   3301  O  OG    . SER A 1 408 ? 135.989 148.053 108.671 1.00 29.29 ?  408 SER A OG    1 
ATOM   3302  N  N     . CYS A 1 409 ? 137.043 145.053 105.936 1.00 20.52 ?  409 CYS A N     1 
ATOM   3303  C  CA    . CYS A 1 409 ? 137.112 145.208 104.492 1.00 26.32 ?  409 CYS A CA    1 
ATOM   3304  C  C     . CYS A 1 409 ? 135.757 144.923 103.855 1.00 30.59 ?  409 CYS A C     1 
ATOM   3305  O  O     . CYS A 1 409 ? 134.859 144.336 104.464 1.00 25.65 ?  409 CYS A O     1 
ATOM   3306  C  CB    . CYS A 1 409 ? 138.186 144.300 103.887 1.00 23.24 ?  409 CYS A CB    1 
ATOM   3307  S  SG    . CYS A 1 409 ? 137.627 142.675 103.361 1.00 41.88 ?  409 CYS A SG    1 
ATOM   3308  N  N     . ASN A 1 410 ? 135.629 145.353 102.607 1.00 30.01 ?  410 ASN A N     1 
ATOM   3309  C  CA    . ASN A 1 410 ? 134.368 145.363 101.882 1.00 18.67 ?  410 ASN A CA    1 
ATOM   3310  C  C     . ASN A 1 410 ? 134.396 144.263 100.831 1.00 21.72 ?  410 ASN A C     1 
ATOM   3311  O  O     . ASN A 1 410 ? 135.257 144.274 99.947  1.00 29.59 ?  410 ASN A O     1 
ATOM   3312  C  CB    . ASN A 1 410 ? 134.158 146.729 101.236 1.00 26.98 ?  410 ASN A CB    1 
ATOM   3313  C  CG    . ASN A 1 410 ? 132.739 146.965 100.818 1.00 32.40 ?  410 ASN A CG    1 
ATOM   3314  O  OD1   . ASN A 1 410 ? 131.850 146.158 101.084 1.00 35.72 ?  410 ASN A OD1   1 
ATOM   3315  N  ND2   . ASN A 1 410 ? 132.514 148.079 100.149 1.00 34.49 ?  410 ASN A ND2   1 
ATOM   3316  N  N     . LEU A 1 411 ? 133.451 143.331 100.916 1.00 21.50 ?  411 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 411 ? 133.479 142.131 100.092 1.00 11.76 ?  411 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 411 ? 132.674 142.303 98.808  1.00 16.12 ?  411 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 411 ? 131.662 143.008 98.770  1.00 26.82 ?  411 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 411 ? 132.941 140.930 100.871 1.00 19.14 ?  411 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 411 ? 133.934 139.926 101.457 1.00 20.45 ?  411 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 411 ? 135.092 140.638 102.122 1.00 19.01 ?  411 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 411 ? 133.235 139.000 102.438 1.00 18.70 ?  411 LEU A CD2   1 
ATOM   3324  N  N     . GLY A 1 412 ? 133.138 141.634 97.755  1.00 22.65 ?  412 GLY A N     1 
ATOM   3325  C  CA    . GLY A 1 412 ? 132.476 141.598 96.465  1.00 13.61 ?  412 GLY A CA    1 
ATOM   3326  C  C     . GLY A 1 412 ? 133.229 140.673 95.531  1.00 13.30 ?  412 GLY A C     1 
ATOM   3327  O  O     . GLY A 1 412 ? 134.463 140.697 95.517  1.00 23.34 ?  412 GLY A O     1 
ATOM   3328  N  N     . SER A 1 413 ? 132.527 139.856 94.748  1.00 14.80 ?  413 SER A N     1 
ATOM   3329  C  CA    . SER A 1 413 ? 133.162 138.780 93.998  1.00 10.91 ?  413 SER A CA    1 
ATOM   3330  C  C     . SER A 1 413 ? 132.891 138.913 92.508  1.00 17.65 ?  413 SER A C     1 
ATOM   3331  O  O     . SER A 1 413 ? 131.747 139.116 92.094  1.00 21.51 ?  413 SER A O     1 
ATOM   3332  C  CB    . SER A 1 413 ? 132.681 137.416 94.492  1.00 9.74  ?  413 SER A CB    1 
ATOM   3333  O  OG    . SER A 1 413 ? 133.090 137.195 95.828  1.00 32.49 ?  413 SER A OG    1 
ATOM   3334  N  N     . LEU A 1 414 ? 133.943 138.782 91.708  1.00 18.32 ?  414 LEU A N     1 
ATOM   3335  C  CA    . LEU A 1 414 ? 133.789 138.661 90.267  1.00 12.54 ?  414 LEU A CA    1 
ATOM   3336  C  C     . LEU A 1 414 ? 133.400 137.234 89.907  1.00 19.08 ?  414 LEU A C     1 
ATOM   3337  O  O     . LEU A 1 414 ? 133.919 136.272 90.478  1.00 24.42 ?  414 LEU A O     1 
ATOM   3338  C  CB    . LEU A 1 414 ? 135.087 139.038 89.555  1.00 17.56 ?  414 LEU A CB    1 
ATOM   3339  C  CG    . LEU A 1 414 ? 135.786 140.319 90.004  1.00 20.23 ?  414 LEU A CG    1 
ATOM   3340  C  CD1   . LEU A 1 414 ? 137.194 140.371 89.443  1.00 22.49 ?  414 LEU A CD1   1 
ATOM   3341  C  CD2   . LEU A 1 414 ? 134.991 141.537 89.573  1.00 20.11 ?  414 LEU A CD2   1 
ATOM   3342  N  N     . ASN A 1 415 ? 132.479 137.099 88.959  1.00 25.67 ?  415 ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 415 ? 132.132 135.794 88.401  1.00 24.25 ?  415 ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 415 ? 133.050 135.563 87.209  1.00 22.60 ?  415 ASN A C     1 
ATOM   3345  O  O     . ASN A 1 415 ? 132.856 136.146 86.140  1.00 27.33 ?  415 ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 415 ? 130.660 135.744 88.013  1.00 20.70 ?  415 ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 415 ? 130.157 134.329 87.802  1.00 25.69 ?  415 ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 415 ? 130.746 133.551 87.053  1.00 33.28 ?  415 ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 415 ? 129.061 133.988 88.468  1.00 29.90 ?  415 ASN A ND2   1 
ATOM   3350  N  N     . ILE A 1 416 ? 134.057 134.705 87.395  1.00 21.84 ?  416 ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 416 ? 135.118 134.556 86.403  1.00 24.00 ?  416 ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 416 ? 134.552 134.092 85.069  1.00 26.98 ?  416 ILE A C     1 
ATOM   3353  O  O     . ILE A 1 416 ? 134.962 134.571 84.005  1.00 29.35 ?  416 ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 416 ? 136.205 133.597 86.924  1.00 20.69 ?  416 ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 416 ? 136.883 134.184 88.160  1.00 18.38 ?  416 ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 416 ? 137.227 133.304 85.841  1.00 14.34 ?  416 ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 416 ? 137.793 133.218 88.871  1.00 19.31 ?  416 ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 417 ? 133.598 133.161 85.101  1.00 20.94 ?  417 LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 417 ? 132.995 132.685 83.861  1.00 22.96 ?  417 LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 417 ? 132.279 133.815 83.132  1.00 23.58 ?  417 LEU A C     1 
ATOM   3361  O  O     . LEU A 1 417 ? 132.529 134.062 81.945  1.00 34.84 ?  417 LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 417 ? 132.036 131.531 84.160  1.00 25.83 ?  417 LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 417 ? 131.275 130.923 82.981  1.00 28.56 ?  417 LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 417 ? 131.443 129.417 82.971  1.00 25.37 ?  417 LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 417 ? 129.804 131.292 83.044  1.00 28.76 ?  417 LEU A CD2   1 
ATOM   3366  N  N     . ASN A 1 418 ? 131.400 134.530 83.838  1.00 25.55 ?  418 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 418 ? 130.638 135.605 83.210  1.00 25.79 ?  418 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 418 ? 131.536 136.773 82.821  1.00 27.32 ?  418 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 418 ? 131.326 137.401 81.777  1.00 29.87 ?  418 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 418 ? 129.521 136.068 84.144  1.00 25.54 ?  418 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 418 ? 128.470 134.999 84.364  1.00 29.11 ?  418 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 418 ? 128.123 134.262 83.444  1.00 29.68 ?  418 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 418 ? 127.961 134.907 85.586  1.00 29.21 ?  418 ASN A ND2   1 
ATOM   3374  N  N     . VAL A 1 419 ? 132.536 137.083 83.650  1.00 31.03 ?  419 VAL A N     1 
ATOM   3375  C  CA    . VAL A 1 419 ? 133.452 138.175 83.333  1.00 28.81 ?  419 VAL A CA    1 
ATOM   3376  C  C     . VAL A 1 419 ? 134.257 137.854 82.080  1.00 29.87 ?  419 VAL A C     1 
ATOM   3377  O  O     . VAL A 1 419 ? 134.421 138.704 81.197  1.00 32.16 ?  419 VAL A O     1 
ATOM   3378  C  CB    . VAL A 1 419 ? 134.368 138.472 84.536  1.00 26.42 ?  419 VAL A CB    1 
ATOM   3379  C  CG1   . VAL A 1 419 ? 135.556 139.306 84.109  1.00 27.47 ?  419 VAL A CG1   1 
ATOM   3380  C  CG2   . VAL A 1 419 ? 133.596 139.203 85.612  1.00 28.81 ?  419 VAL A CG2   1 
ATOM   3381  N  N     . MET A 1 420 ? 134.765 136.625 81.974  1.00 32.84 ?  420 MET A N     1 
ATOM   3382  C  CA    . MET A 1 420 ? 135.642 136.308 80.855  1.00 33.42 ?  420 MET A CA    1 
ATOM   3383  C  C     . MET A 1 420 ? 134.869 136.043 79.570  1.00 30.71 ?  420 MET A C     1 
ATOM   3384  O  O     . MET A 1 420 ? 135.386 136.316 78.481  1.00 35.76 ?  420 MET A O     1 
ATOM   3385  C  CB    . MET A 1 420 ? 136.537 135.117 81.197  1.00 31.20 ?  420 MET A CB    1 
ATOM   3386  C  CG    . MET A 1 420 ? 137.823 135.534 81.900  1.00 26.08 ?  420 MET A CG    1 
ATOM   3387  S  SD    . MET A 1 420 ? 139.256 135.744 80.829  1.00 47.11 ?  420 MET A SD    1 
ATOM   3388  C  CE    . MET A 1 420 ? 139.219 134.246 79.860  1.00 33.81 ?  420 MET A CE    1 
ATOM   3389  N  N     . GLU A 1 421 ? 133.644 135.515 79.657  1.00 32.30 ?  421 GLU A N     1 
ATOM   3390  C  CA    . GLU A 1 421 ? 132.863 135.329 78.438  1.00 37.53 ?  421 GLU A CA    1 
ATOM   3391  C  C     . GLU A 1 421 ? 132.385 136.654 77.864  1.00 37.35 ?  421 GLU A C     1 
ATOM   3392  O  O     . GLU A 1 421 ? 132.113 136.733 76.662  1.00 40.20 ?  421 GLU A O     1 
ATOM   3393  C  CB    . GLU A 1 421 ? 131.664 134.412 78.691  1.00 34.43 ?  421 GLU A CB    1 
ATOM   3394  C  CG    . GLU A 1 421 ? 130.635 134.965 79.656  1.00 39.15 ?  421 GLU A CG    1 
ATOM   3395  C  CD    . GLU A 1 421 ? 129.391 134.102 79.733  1.00 43.34 ?  421 GLU A CD    1 
ATOM   3396  O  OE1   . GLU A 1 421 ? 129.184 133.276 78.820  1.00 44.06 ?  421 GLU A OE1   1 
ATOM   3397  O  OE2   . GLU A 1 421 ? 128.621 134.249 80.703  1.00 40.29 -1 421 GLU A OE2   1 
ATOM   3398  N  N     . HIS A 1 422 ? 132.279 137.690 78.692  1.00 35.77 ?  422 HIS A N     1 
ATOM   3399  C  CA    . HIS A 1 422 ? 131.950 139.033 78.236  1.00 35.28 ?  422 HIS A CA    1 
ATOM   3400  C  C     . HIS A 1 422 ? 133.183 139.845 77.869  1.00 39.14 ?  422 HIS A C     1 
ATOM   3401  O  O     . HIS A 1 422 ? 133.040 140.976 77.394  1.00 39.84 ?  422 HIS A O     1 
ATOM   3402  C  CB    . HIS A 1 422 ? 131.154 139.777 79.313  1.00 32.46 ?  422 HIS A CB    1 
ATOM   3403  C  CG    . HIS A 1 422 ? 129.727 139.339 79.421  1.00 36.58 ?  422 HIS A CG    1 
ATOM   3404  N  ND1   . HIS A 1 422 ? 129.315 138.359 80.298  1.00 36.83 ?  422 HIS A ND1   1 
ATOM   3405  C  CD2   . HIS A 1 422 ? 128.617 139.747 78.763  1.00 36.85 ?  422 HIS A CD2   1 
ATOM   3406  C  CE1   . HIS A 1 422 ? 128.011 138.182 80.177  1.00 38.65 ?  422 HIS A CE1   1 
ATOM   3407  N  NE2   . HIS A 1 422 ? 127.564 139.011 79.251  1.00 39.61 ?  422 HIS A NE2   1 
ATOM   3408  N  N     . LYS A 1 423 ? 134.380 139.293 78.076  1.00 40.10 ?  423 LYS A N     1 
ATOM   3409  C  CA    . LYS A 1 423 ? 135.640 139.972 77.771  1.00 39.49 ?  423 LYS A CA    1 
ATOM   3410  C  C     . LYS A 1 423 ? 135.702 141.341 78.442  1.00 42.48 ?  423 LYS A C     1 
ATOM   3411  O  O     . LYS A 1 423 ? 136.097 142.344 77.842  1.00 42.19 ?  423 LYS A O     1 
ATOM   3412  C  CB    . LYS A 1 423 ? 135.847 140.086 76.260  1.00 37.95 ?  423 LYS A CB    1 
ATOM   3413  C  CG    . LYS A 1 423 ? 135.972 138.748 75.552  1.00 38.37 ?  423 LYS A CG    1 
ATOM   3414  C  CD    . LYS A 1 423 ? 135.959 138.919 74.042  1.00 40.56 ?  423 LYS A CD    1 
ATOM   3415  C  CE    . LYS A 1 423 ? 135.828 137.581 73.338  1.00 40.10 ?  423 LYS A CE    1 
ATOM   3416  N  NZ    . LYS A 1 423 ? 136.768 136.569 73.895  1.00 43.35 1  423 LYS A NZ    1 
ATOM   3417  N  N     . SER A 1 424 ? 135.305 141.377 79.711  1.00 32.26 ?  424 SER A N     1 
ATOM   3418  C  CA    . SER A 1 424 ? 135.139 142.620 80.455  1.00 29.82 ?  424 SER A CA    1 
ATOM   3419  C  C     . SER A 1 424 ? 135.814 142.532 81.816  1.00 32.67 ?  424 SER A C     1 
ATOM   3420  O  O     . SER A 1 424 ? 135.224 142.857 82.847  1.00 32.96 ?  424 SER A O     1 
ATOM   3421  C  CB    . SER A 1 424 ? 133.659 142.954 80.614  1.00 34.00 ?  424 SER A CB    1 
ATOM   3422  O  OG    . SER A 1 424 ? 133.038 142.074 81.534  1.00 31.39 ?  424 SER A OG    1 
ATOM   3423  N  N     . ILE A 1 425 ? 137.068 142.080 81.844  1.00 31.72 ?  425 ILE A N     1 
ATOM   3424  C  CA    . ILE A 1 425 ? 137.811 142.064 83.101  1.00 23.87 ?  425 ILE A CA    1 
ATOM   3425  C  C     . ILE A 1 425 ? 138.012 143.484 83.616  1.00 29.13 ?  425 ILE A C     1 
ATOM   3426  O  O     . ILE A 1 425 ? 137.747 143.780 84.787  1.00 37.02 ?  425 ILE A O     1 
ATOM   3427  C  CB    . ILE A 1 425 ? 139.155 141.333 82.930  1.00 26.96 ?  425 ILE A CB    1 
ATOM   3428  C  CG1   . ILE A 1 425 ? 138.940 139.823 82.823  1.00 31.42 ?  425 ILE A CG1   1 
ATOM   3429  C  CG2   . ILE A 1 425 ? 140.086 141.645 84.092  1.00 27.22 ?  425 ILE A CG2   1 
ATOM   3430  C  CD1   . ILE A 1 425 ? 140.208 139.053 82.530  1.00 29.41 ?  425 ILE A CD1   1 
ATOM   3431  N  N     . GLU A 1 426 ? 138.461 144.388 82.742  1.00 25.95 ?  426 GLU A N     1 
ATOM   3432  C  CA    . GLU A 1 426 ? 138.764 145.753 83.166  1.00 26.36 ?  426 GLU A CA    1 
ATOM   3433  C  C     . GLU A 1 426 ? 137.519 146.472 83.668  1.00 27.33 ?  426 GLU A C     1 
ATOM   3434  O  O     . GLU A 1 426 ? 137.513 147.032 84.771  1.00 32.66 ?  426 GLU A O     1 
ATOM   3435  C  CB    . GLU A 1 426 ? 139.396 146.525 82.009  1.00 26.18 ?  426 GLU A CB    1 
ATOM   3436  C  CG    . GLU A 1 426 ? 139.351 148.033 82.175  1.00 28.32 ?  426 GLU A CG    1 
ATOM   3437  C  CD    . GLU A 1 426 ? 140.012 148.763 81.025  1.00 36.93 ?  426 GLU A CD    1 
ATOM   3438  O  OE1   . GLU A 1 426 ? 140.403 148.097 80.043  1.00 34.16 ?  426 GLU A OE1   1 
ATOM   3439  O  OE2   . GLU A 1 426 ? 140.139 150.003 81.100  1.00 37.58 -1 426 GLU A OE2   1 
ATOM   3440  N  N     . LYS A 1 427 ? 136.454 146.473 82.862  1.00 27.52 ?  427 LYS A N     1 
ATOM   3441  C  CA    . LYS A 1 427 ? 135.247 147.205 83.231  1.00 24.47 ?  427 LYS A CA    1 
ATOM   3442  C  C     . LYS A 1 427 ? 134.620 146.636 84.495  1.00 26.33 ?  427 LYS A C     1 
ATOM   3443  O  O     . LYS A 1 427 ? 134.213 147.388 85.388  1.00 31.77 ?  427 LYS A O     1 
ATOM   3444  C  CB    . LYS A 1 427 ? 134.251 147.183 82.071  1.00 31.26 ?  427 LYS A CB    1 
ATOM   3445  C  CG    . LYS A 1 427 ? 132.818 147.505 82.464  1.00 28.72 ?  427 LYS A CG    1 
ATOM   3446  C  CD    . LYS A 1 427 ? 131.825 146.727 81.615  1.00 32.81 ?  427 LYS A CD    1 
ATOM   3447  C  CE    . LYS A 1 427 ? 131.516 145.373 82.226  1.00 32.53 ?  427 LYS A CE    1 
ATOM   3448  N  NZ    . LYS A 1 427 ? 130.434 144.660 81.490  1.00 29.00 1  427 LYS A NZ    1 
ATOM   3449  N  N     . THR A 1 428 ? 134.543 145.307 84.595  1.00 26.39 ?  428 THR A N     1 
ATOM   3450  C  CA    . THR A 1 428 ? 133.958 144.694 85.781  1.00 21.30 ?  428 THR A CA    1 
ATOM   3451  C  C     . THR A 1 428 ? 134.787 144.989 87.022  1.00 23.90 ?  428 THR A C     1 
ATOM   3452  O  O     . THR A 1 428 ? 134.232 145.316 88.075  1.00 31.41 ?  428 THR A O     1 
ATOM   3453  C  CB    . THR A 1 428 ? 133.812 143.187 85.588  1.00 25.35 ?  428 THR A CB    1 
ATOM   3454  O  OG1   . THR A 1 428 ? 133.160 142.926 84.340  1.00 29.04 ?  428 THR A OG1   1 
ATOM   3455  C  CG2   . THR A 1 428 ? 132.992 142.587 86.716  1.00 24.41 ?  428 THR A CG2   1 
ATOM   3456  N  N     . VAL A 1 429 ? 136.114 144.887 86.918  1.00 24.51 ?  429 VAL A N     1 
ATOM   3457  C  CA    . VAL A 1 429 ? 136.964 145.146 88.076  1.00 24.24 ?  429 VAL A CA    1 
ATOM   3458  C  C     . VAL A 1 429 ? 136.829 146.594 88.524  1.00 23.22 ?  429 VAL A C     1 
ATOM   3459  O  O     . VAL A 1 429 ? 136.704 146.878 89.720  1.00 26.22 ?  429 VAL A O     1 
ATOM   3460  C  CB    . VAL A 1 429 ? 138.428 144.780 87.764  1.00 21.22 ?  429 VAL A CB    1 
ATOM   3461  C  CG1   . VAL A 1 429 ? 139.362 145.430 88.767  1.00 18.94 ?  429 VAL A CG1   1 
ATOM   3462  C  CG2   . VAL A 1 429 ? 138.611 143.275 87.779  1.00 23.02 ?  429 VAL A CG2   1 
ATOM   3463  N  N     . LYS A 1 430 ? 136.832 147.534 87.574  1.00 22.34 ?  430 LYS A N     1 
ATOM   3464  C  CA    . LYS A 1 430 ? 136.744 148.943 87.945  1.00 20.97 ?  430 LYS A CA    1 
ATOM   3465  C  C     . LYS A 1 430 ? 135.382 149.284 88.538  1.00 23.22 ?  430 LYS A C     1 
ATOM   3466  O  O     . LYS A 1 430 ? 135.299 150.023 89.528  1.00 30.05 ?  430 LYS A O     1 
ATOM   3467  C  CB    . LYS A 1 430 ? 137.052 149.823 86.736  1.00 19.83 ?  430 LYS A CB    1 
ATOM   3468  C  CG    . LYS A 1 430 ? 138.478 149.674 86.234  1.00 23.31 ?  430 LYS A CG    1 
ATOM   3469  C  CD    . LYS A 1 430 ? 138.918 150.874 85.422  1.00 27.87 ?  430 LYS A CD    1 
ATOM   3470  C  CE    . LYS A 1 430 ? 140.408 150.822 85.143  1.00 28.43 ?  430 LYS A CE    1 
ATOM   3471  N  NZ    . LYS A 1 430 ? 140.882 152.041 84.435  1.00 30.72 1  430 LYS A NZ    1 
ATOM   3472  N  N     . LEU A 1 431 ? 134.300 148.753 87.964  1.00 26.98 ?  431 LEU A N     1 
ATOM   3473  C  CA    . LEU A 1 431 ? 132.976 149.026 88.510  1.00 22.52 ?  431 LEU A CA    1 
ATOM   3474  C  C     . LEU A 1 431 ? 132.802 148.391 89.885  1.00 21.71 ?  431 LEU A C     1 
ATOM   3475  O  O     . LEU A 1 431 ? 132.192 148.990 90.779  1.00 28.12 ?  431 LEU A O     1 
ATOM   3476  C  CB    . LEU A 1 431 ? 131.899 148.537 87.545  1.00 27.33 ?  431 LEU A CB    1 
ATOM   3477  C  CG    . LEU A 1 431 ? 131.384 149.560 86.531  1.00 30.18 ?  431 LEU A CG    1 
ATOM   3478  C  CD1   . LEU A 1 431 ? 130.600 148.871 85.428  1.00 26.87 ?  431 LEU A CD1   1 
ATOM   3479  C  CD2   . LEU A 1 431 ? 130.531 150.611 87.221  1.00 28.35 ?  431 LEU A CD2   1 
ATOM   3480  N  N     . ALA A 1 432 ? 133.330 147.180 90.074  1.00 20.35 ?  432 ALA A N     1 
ATOM   3481  C  CA    . ALA A 1 432 ? 133.277 146.543 91.383  1.00 19.22 ?  432 ALA A CA    1 
ATOM   3482  C  C     . ALA A 1 432 ? 134.085 147.327 92.406  1.00 24.76 ?  432 ALA A C     1 
ATOM   3483  O  O     . ALA A 1 432 ? 133.671 147.462 93.561  1.00 26.67 ?  432 ALA A O     1 
ATOM   3484  C  CB    . ALA A 1 432 ? 133.783 145.106 91.285  1.00 26.31 ?  432 ALA A CB    1 
ATOM   3485  N  N     . THR A 1 433 ? 135.244 147.849 91.998  1.00 22.76 ?  433 THR A N     1 
ATOM   3486  C  CA    . THR A 1 433 ? 136.039 148.684 92.890  1.00 17.94 ?  433 THR A CA    1 
ATOM   3487  C  C     . THR A 1 433 ? 135.283 149.948 93.276  1.00 22.72 ?  433 THR A C     1 
ATOM   3488  O  O     . THR A 1 433 ? 135.309 150.363 94.439  1.00 27.81 ?  433 THR A O     1 
ATOM   3489  C  CB    . THR A 1 433 ? 137.370 149.039 92.225  1.00 20.26 ?  433 THR A CB    1 
ATOM   3490  O  OG1   . THR A 1 433 ? 138.021 147.841 91.785  1.00 25.56 ?  433 THR A OG1   1 
ATOM   3491  C  CG2   . THR A 1 433 ? 138.277 149.775 93.196  1.00 24.42 ?  433 THR A CG2   1 
ATOM   3492  N  N     . ASP A 1 434 ? 134.604 150.573 92.312  1.00 20.19 ?  434 ASP A N     1 
ATOM   3493  C  CA    . ASP A 1 434 ? 133.818 151.765 92.616  1.00 15.86 ?  434 ASP A CA    1 
ATOM   3494  C  C     . ASP A 1 434 ? 132.678 151.451 93.580  1.00 19.40 ?  434 ASP A C     1 
ATOM   3495  O  O     . ASP A 1 434 ? 132.420 152.213 94.519  1.00 25.70 ?  434 ASP A O     1 
ATOM   3496  C  CB    . ASP A 1 434 ? 133.275 152.377 91.325  1.00 23.42 ?  434 ASP A CB    1 
ATOM   3497  C  CG    . ASP A 1 434 ? 134.368 152.928 90.438  1.00 31.37 ?  434 ASP A CG    1 
ATOM   3498  O  OD1   . ASP A 1 434 ? 135.427 153.319 90.972  1.00 29.06 ?  434 ASP A OD1   1 
ATOM   3499  O  OD2   . ASP A 1 434 ? 134.171 152.970 89.206  1.00 30.81 -1 434 ASP A OD2   1 
ATOM   3500  N  N     . SER A 1 435 ? 131.983 150.332 93.364  1.00 20.41 ?  435 SER A N     1 
ATOM   3501  C  CA    . SER A 1 435 ? 130.896 149.949 94.262  1.00 17.04 ?  435 SER A CA    1 
ATOM   3502  C  C     . SER A 1 435 ? 131.413 149.644 95.663  1.00 25.13 ?  435 SER A C     1 
ATOM   3503  O  O     . SER A 1 435 ? 130.788 150.026 96.661  1.00 34.54 ?  435 SER A O     1 
ATOM   3504  C  CB    . SER A 1 435 ? 130.148 148.745 93.694  1.00 19.28 ?  435 SER A CB    1 
ATOM   3505  O  OG    . SER A 1 435 ? 130.925 147.567 93.794  1.00 23.37 ?  435 SER A OG    1 
ATOM   3506  N  N     . LEU A 1 436 ? 132.549 148.950 95.756  1.00 18.68 ?  436 LEU A N     1 
ATOM   3507  C  CA    . LEU A 1 436 ? 133.133 148.650 97.057  1.00 13.11 ?  436 LEU A CA    1 
ATOM   3508  C  C     . LEU A 1 436 ? 133.584 149.921 97.763  1.00 15.45 ?  436 LEU A C     1 
ATOM   3509  O  O     . LEU A 1 436 ? 133.424 150.052 98.981  1.00 27.01 ?  436 LEU A O     1 
ATOM   3510  C  CB    . LEU A 1 436 ? 134.298 147.676 96.895  1.00 20.26 ?  436 LEU A CB    1 
ATOM   3511  C  CG    . LEU A 1 436 ? 133.910 146.252 96.500  1.00 17.84 ?  436 LEU A CG    1 
ATOM   3512  C  CD1   . LEU A 1 436 ? 135.142 145.411 96.219  1.00 17.53 ?  436 LEU A CD1   1 
ATOM   3513  C  CD2   . LEU A 1 436 ? 133.061 145.621 97.582  1.00 18.63 ?  436 LEU A CD2   1 
ATOM   3514  N  N     . THR A 1 437 ? 134.147 150.871 97.012  1.00 19.99 ?  437 THR A N     1 
ATOM   3515  C  CA    . THR A 1 437 ? 134.511 152.159 97.588  1.00 20.52 ?  437 THR A CA    1 
ATOM   3516  C  C     . THR A 1 437 ? 133.284 152.891 98.111  1.00 23.63 ?  437 THR A C     1 
ATOM   3517  O  O     . THR A 1 437 ? 133.316 153.472 99.200  1.00 25.90 ?  437 THR A O     1 
ATOM   3518  C  CB    . THR A 1 437 ? 135.236 153.009 96.545  1.00 18.17 ?  437 THR A CB    1 
ATOM   3519  O  OG1   . THR A 1 437 ? 136.364 152.287 96.039  1.00 17.98 ?  437 THR A OG1   1 
ATOM   3520  C  CG2   . THR A 1 437 ? 135.709 154.314 97.156  1.00 22.56 ?  437 THR A CG2   1 
ATOM   3521  N  N     . HIS A 1 438 ? 132.187 152.869 97.349  1.00 22.47 ?  438 HIS A N     1 
ATOM   3522  C  CA    . HIS A 1 438 ? 130.965 153.524 97.799  1.00 23.06 ?  438 HIS A CA    1 
ATOM   3523  C  C     . HIS A 1 438 ? 130.434 152.889 99.078  1.00 22.61 ?  438 HIS A C     1 
ATOM   3524  O  O     . HIS A 1 438 ? 130.035 153.595 100.011 1.00 26.43 ?  438 HIS A O     1 
ATOM   3525  C  CB    . HIS A 1 438 ? 129.904 153.476 96.703  1.00 26.74 ?  438 HIS A CB    1 
ATOM   3526  C  CG    . HIS A 1 438 ? 128.545 153.896 97.167  1.00 27.35 ?  438 HIS A CG    1 
ATOM   3527  N  ND1   . HIS A 1 438 ? 128.171 155.218 97.274  1.00 25.41 ?  438 HIS A ND1   1 
ATOM   3528  C  CD2   . HIS A 1 438 ? 127.474 153.169 97.561  1.00 23.58 ?  438 HIS A CD2   1 
ATOM   3529  C  CE1   . HIS A 1 438 ? 126.926 155.287 97.711  1.00 30.51 ?  438 HIS A CE1   1 
ATOM   3530  N  NE2   . HIS A 1 438 ? 126.480 154.058 97.892  1.00 29.10 ?  438 HIS A NE2   1 
ATOM   3531  N  N     . VAL A 1 439 ? 130.423 151.556 99.140  1.00 24.67 ?  439 VAL A N     1 
ATOM   3532  C  CA    . VAL A 1 439 ? 129.909 150.889 100.333 1.00 20.20 ?  439 VAL A CA    1 
ATOM   3533  C  C     . VAL A 1 439 ? 130.819 151.140 101.530 1.00 27.85 ?  439 VAL A C     1 
ATOM   3534  O  O     . VAL A 1 439 ? 130.339 151.313 102.657 1.00 36.63 ?  439 VAL A O     1 
ATOM   3535  C  CB    . VAL A 1 439 ? 129.716 149.386 100.063 1.00 20.52 ?  439 VAL A CB    1 
ATOM   3536  C  CG1   . VAL A 1 439 ? 129.516 148.621 101.362 1.00 21.99 ?  439 VAL A CG1   1 
ATOM   3537  C  CG2   . VAL A 1 439 ? 128.546 149.167 99.135  1.00 30.53 ?  439 VAL A CG2   1 
ATOM   3538  N  N     . SER A 1 440 ? 132.137 151.179 101.315 1.00 21.50 ?  440 SER A N     1 
ATOM   3539  C  CA    . SER A 1 440 ? 133.056 151.499 102.402 1.00 20.63 ?  440 SER A CA    1 
ATOM   3540  C  C     . SER A 1 440 ? 132.858 152.928 102.892 1.00 24.45 ?  440 SER A C     1 
ATOM   3541  O  O     . SER A 1 440 ? 132.938 153.194 104.097 1.00 26.57 ?  440 SER A O     1 
ATOM   3542  C  CB    . SER A 1 440 ? 134.499 151.279 101.947 1.00 25.67 ?  440 SER A CB    1 
ATOM   3543  O  OG    . SER A 1 440 ? 135.415 151.589 102.981 1.00 24.86 ?  440 SER A OG    1 
ATOM   3544  N  N     . GLU A 1 441 ? 132.603 153.863 101.973 1.00 26.21 ?  441 GLU A N     1 
ATOM   3545  C  CA    . GLU A 1 441 ? 132.396 155.252 102.364 1.00 23.41 ?  441 GLU A CA    1 
ATOM   3546  C  C     . GLU A 1 441 ? 131.063 155.449 103.072 1.00 30.31 ?  441 GLU A C     1 
ATOM   3547  O  O     . GLU A 1 441 ? 130.949 156.324 103.937 1.00 38.74 ?  441 GLU A O     1 
ATOM   3548  C  CB    . GLU A 1 441 ? 132.478 156.162 101.138 1.00 25.90 ?  441 GLU A CB    1 
ATOM   3549  C  CG    . GLU A 1 441 ? 133.882 156.362 100.599 1.00 29.16 ?  441 GLU A CG    1 
ATOM   3550  C  CD    . GLU A 1 441 ? 133.889 156.714 99.126  1.00 36.38 ?  441 GLU A CD    1 
ATOM   3551  O  OE1   . GLU A 1 441 ? 132.856 156.500 98.457  1.00 34.67 ?  441 GLU A OE1   1 
ATOM   3552  O  OE2   . GLU A 1 441 ? 134.926 157.209 98.635  1.00 36.67 -1 441 GLU A OE2   1 
ATOM   3553  N  N     . THR A 1 442 ? 130.051 154.659 102.724 1.00 30.88 ?  442 THR A N     1 
ATOM   3554  C  CA    . THR A 1 442 ? 128.736 154.782 103.339 1.00 29.96 ?  442 THR A CA    1 
ATOM   3555  C  C     . THR A 1 442 ? 128.599 153.966 104.616 1.00 30.74 ?  442 THR A C     1 
ATOM   3556  O  O     . THR A 1 442 ? 127.522 153.966 105.220 1.00 38.69 ?  442 THR A O     1 
ATOM   3557  C  CB    . THR A 1 442 ? 127.642 154.367 102.350 1.00 29.97 ?  442 THR A CB    1 
ATOM   3558  O  OG1   . THR A 1 442 ? 127.931 153.063 101.832 1.00 33.39 ?  442 THR A OG1   1 
ATOM   3559  C  CG2   . THR A 1 442 ? 127.558 155.359 101.202 1.00 29.67 ?  442 THR A CG2   1 
ATOM   3560  N  N     . THR A 1 443 ? 129.654 153.276 105.040 1.00 29.39 ?  443 THR A N     1 
ATOM   3561  C  CA    . THR A 1 443 ? 129.628 152.514 106.280 1.00 32.14 ?  443 THR A CA    1 
ATOM   3562  C  C     . THR A 1 443 ? 130.061 153.407 107.435 1.00 37.04 ?  443 THR A C     1 
ATOM   3563  O  O     . THR A 1 443 ? 131.135 154.015 107.389 1.00 39.75 ?  443 THR A O     1 
ATOM   3564  C  CB    . THR A 1 443 ? 130.540 151.291 106.187 1.00 32.36 ?  443 THR A CB    1 
ATOM   3565  O  OG1   . THR A 1 443 ? 130.023 150.382 105.207 1.00 36.65 ?  443 THR A OG1   1 
ATOM   3566  C  CG2   . THR A 1 443 ? 130.622 150.585 107.530 1.00 26.65 ?  443 THR A CG2   1 
ATOM   3567  N  N     . ASP A 1 444 ? 129.221 153.485 108.465 1.00 43.45 ?  444 ASP A N     1 
ATOM   3568  C  CA    . ASP A 1 444 ? 129.497 154.308 109.643 1.00 42.13 ?  444 ASP A CA    1 
ATOM   3569  C  C     . ASP A 1 444 ? 129.031 153.529 110.869 1.00 41.49 ?  444 ASP A C     1 
ATOM   3570  O  O     . ASP A 1 444 ? 127.829 153.450 111.141 1.00 42.15 ?  444 ASP A O     1 
ATOM   3571  C  CB    . ASP A 1 444 ? 128.806 155.662 109.546 1.00 43.52 ?  444 ASP A CB    1 
ATOM   3572  C  CG    . ASP A 1 444 ? 129.736 156.814 109.868 1.00 47.76 ?  444 ASP A CG    1 
ATOM   3573  O  OD1   . ASP A 1 444 ? 130.956 156.577 109.993 1.00 46.38 ?  444 ASP A OD1   1 
ATOM   3574  O  OD2   . ASP A 1 444 ? 129.248 157.956 109.993 1.00 47.26 -1 444 ASP A OD2   1 
ATOM   3575  N  N     . ILE A 1 445 ? 129.981 152.963 111.605 1.00 34.72 ?  445 ILE A N     1 
ATOM   3576  C  CA    . ILE A 1 445 ? 129.694 152.165 112.789 1.00 37.80 ?  445 ILE A CA    1 
ATOM   3577  C  C     . ILE A 1 445 ? 130.017 153.003 114.016 1.00 38.51 ?  445 ILE A C     1 
ATOM   3578  O  O     . ILE A 1 445 ? 131.172 153.391 114.230 1.00 39.84 ?  445 ILE A O     1 
ATOM   3579  C  CB    . ILE A 1 445 ? 130.489 150.851 112.785 1.00 36.80 ?  445 ILE A CB    1 
ATOM   3580  C  CG1   . ILE A 1 445 ? 130.061 149.989 111.596 1.00 34.86 ?  445 ILE A CG1   1 
ATOM   3581  C  CG2   . ILE A 1 445 ? 130.284 150.100 114.088 1.00 37.90 ?  445 ILE A CG2   1 
ATOM   3582  C  CD1   . ILE A 1 445 ? 130.949 148.801 111.354 1.00 34.17 ?  445 ILE A CD1   1 
ATOM   3583  N  N     . ARG A 1 446 ? 128.998 153.283 114.824 1.00 40.85 ?  446 ARG A N     1 
ATOM   3584  C  CA    . ARG A 1 446 ? 129.111 154.205 115.944 1.00 46.28 ?  446 ARG A CA    1 
ATOM   3585  C  C     . ARG A 1 446 ? 129.460 153.517 117.257 1.00 44.95 ?  446 ARG A C     1 
ATOM   3586  O  O     . ARG A 1 446 ? 129.562 154.195 118.284 1.00 41.08 ?  446 ARG A O     1 
ATOM   3587  C  CB    . ARG A 1 446 ? 127.806 154.993 116.108 1.00 44.76 ?  446 ARG A CB    1 
ATOM   3588  C  CG    . ARG A 1 446 ? 126.964 155.075 114.842 1.00 43.05 ?  446 ARG A CG    1 
ATOM   3589  C  CD    . ARG A 1 446 ? 127.611 155.961 113.784 1.00 45.48 ?  446 ARG A CD    1 
ATOM   3590  N  NE    . ARG A 1 446 ? 127.385 157.379 114.034 1.00 47.02 ?  446 ARG A NE    1 
ATOM   3591  C  CZ    . ARG A 1 446 ? 126.243 158.009 113.791 1.00 47.76 ?  446 ARG A CZ    1 
ATOM   3592  N  NH1   . ARG A 1 446 ? 125.193 157.373 113.298 1.00 43.40 1  446 ARG A NH1   1 
ATOM   3593  N  NH2   . ARG A 1 446 ? 126.154 159.311 114.049 1.00 47.17 ?  446 ARG A NH2   1 
ATOM   3594  N  N     . ASN A 1 447 ? 129.644 152.197 117.253 1.00 34.40 ?  447 ASN A N     1 
ATOM   3595  C  CA    . ASN A 1 447 ? 129.993 151.460 118.457 1.00 29.03 ?  447 ASN A CA    1 
ATOM   3596  C  C     . ASN A 1 447 ? 131.328 150.739 118.348 1.00 32.18 ?  447 ASN A C     1 
ATOM   3597  O  O     . ASN A 1 447 ? 131.743 150.085 119.311 1.00 35.53 ?  447 ASN A O     1 
ATOM   3598  C  CB    . ASN A 1 447 ? 128.891 150.451 118.799 1.00 32.55 ?  447 ASN A CB    1 
ATOM   3599  C  CG    . ASN A 1 447 ? 127.819 151.041 119.688 1.00 29.77 ?  447 ASN A CG    1 
ATOM   3600  O  OD1   . ASN A 1 447 ? 128.092 151.909 120.515 1.00 28.36 ?  447 ASN A OD1   1 
ATOM   3601  N  ND2   . ASN A 1 447 ? 126.587 150.580 119.514 1.00 32.26 ?  447 ASN A ND2   1 
ATOM   3602  N  N     . ALA A 1 448 ? 132.007 150.836 117.205 1.00 34.16 ?  448 ALA A N     1 
ATOM   3603  C  CA    . ALA A 1 448 ? 133.340 150.270 117.006 1.00 29.31 ?  448 ALA A CA    1 
ATOM   3604  C  C     . ALA A 1 448 ? 134.254 151.407 116.570 1.00 29.15 ?  448 ALA A C     1 
ATOM   3605  O  O     . ALA A 1 448 ? 134.348 151.715 115.370 1.00 29.10 ?  448 ALA A O     1 
ATOM   3606  C  CB    . ALA A 1 448 ? 133.317 149.143 115.979 1.00 24.41 ?  448 ALA A CB    1 
ATOM   3607  N  N     . PRO A 1 449 ? 134.938 152.066 117.508 1.00 28.77 ?  449 PRO A N     1 
ATOM   3608  C  CA    . PRO A 1 449 ? 135.720 153.255 117.129 1.00 22.93 ?  449 PRO A CA    1 
ATOM   3609  C  C     . PRO A 1 449 ? 136.896 152.937 116.227 1.00 27.34 ?  449 PRO A C     1 
ATOM   3610  O  O     . PRO A 1 449 ? 137.137 153.663 115.254 1.00 22.25 ?  449 PRO A O     1 
ATOM   3611  C  CB    . PRO A 1 449 ? 136.181 153.824 118.482 1.00 19.14 ?  449 PRO A CB    1 
ATOM   3612  C  CG    . PRO A 1 449 ? 135.441 153.049 119.531 1.00 25.18 ?  449 PRO A CG    1 
ATOM   3613  C  CD    . PRO A 1 449 ? 135.077 151.740 118.935 1.00 23.69 ?  449 PRO A CD    1 
ATOM   3614  N  N     . ALA A 1 450 ? 137.637 151.866 116.519 1.00 25.81 ?  450 ALA A N     1 
ATOM   3615  C  CA    . ALA A 1 450 ? 138.788 151.523 115.694 1.00 16.45 ?  450 ALA A CA    1 
ATOM   3616  C  C     . ALA A 1 450 ? 138.364 151.003 114.326 1.00 22.90 ?  450 ALA A C     1 
ATOM   3617  O  O     . ALA A 1 450 ? 139.036 151.280 113.329 1.00 26.91 ?  450 ALA A O     1 
ATOM   3618  C  CB    . ALA A 1 450 ? 139.665 150.500 116.412 1.00 19.28 ?  450 ALA A CB    1 
ATOM   3619  N  N     . VAL A 1 451 ? 137.250 150.271 114.256 1.00 28.04 ?  451 VAL A N     1 
ATOM   3620  C  CA    . VAL A 1 451 ? 136.735 149.820 112.964 1.00 18.02 ?  451 VAL A CA    1 
ATOM   3621  C  C     . VAL A 1 451 ? 136.370 151.017 112.096 1.00 21.83 ?  451 VAL A C     1 
ATOM   3622  O  O     . VAL A 1 451 ? 136.719 151.079 110.912 1.00 30.56 ?  451 VAL A O     1 
ATOM   3623  C  CB    . VAL A 1 451 ? 135.533 148.880 113.162 1.00 21.98 ?  451 VAL A CB    1 
ATOM   3624  C  CG1   . VAL A 1 451 ? 134.742 148.742 111.872 1.00 23.76 ?  451 VAL A CG1   1 
ATOM   3625  C  CG2   . VAL A 1 451 ? 135.992 147.520 113.653 1.00 22.51 ?  451 VAL A CG2   1 
ATOM   3626  N  N     . ARG A 1 452 ? 135.666 151.991 112.678 1.00 20.50 ?  452 ARG A N     1 
ATOM   3627  C  CA    . ARG A 1 452 ? 135.283 153.183 111.930 1.00 22.77 ?  452 ARG A CA    1 
ATOM   3628  C  C     . ARG A 1 452 ? 136.504 153.989 111.505 1.00 23.83 ?  452 ARG A C     1 
ATOM   3629  O  O     . ARG A 1 452 ? 136.578 154.470 110.365 1.00 33.52 ?  452 ARG A O     1 
ATOM   3630  C  CB    . ARG A 1 452 ? 134.339 154.039 112.774 1.00 21.08 ?  452 ARG A CB    1 
ATOM   3631  C  CG    . ARG A 1 452 ? 134.073 155.423 112.217 1.00 26.53 ?  452 ARG A CG    1 
ATOM   3632  C  CD    . ARG A 1 452 ? 133.061 156.162 113.073 1.00 27.26 ?  452 ARG A CD    1 
ATOM   3633  N  NE    . ARG A 1 452 ? 133.367 156.040 114.493 1.00 38.94 ?  452 ARG A NE    1 
ATOM   3634  C  CZ    . ARG A 1 452 ? 132.635 156.566 115.466 1.00 41.10 ?  452 ARG A CZ    1 
ATOM   3635  N  NH1   . ARG A 1 452 ? 131.537 157.258 115.209 1.00 34.44 1  452 ARG A NH1   1 
ATOM   3636  N  NH2   . ARG A 1 452 ? 133.015 156.394 116.729 1.00 29.62 ?  452 ARG A NH2   1 
ATOM   3637  N  N     . ARG A 1 453 ? 137.477 154.144 112.406 1.00 21.78 ?  453 ARG A N     1 
ATOM   3638  C  CA    . ARG A 1 453 ? 138.677 154.905 112.075 1.00 20.91 ?  453 ARG A CA    1 
ATOM   3639  C  C     . ARG A 1 453 ? 139.463 154.235 110.956 1.00 25.75 ?  453 ARG A C     1 
ATOM   3640  O  O     . ARG A 1 453 ? 139.937 154.907 110.033 1.00 29.91 ?  453 ARG A O     1 
ATOM   3641  C  CB    . ARG A 1 453 ? 139.549 155.080 113.320 1.00 20.33 ?  453 ARG A CB    1 
ATOM   3642  C  CG    . ARG A 1 453 ? 140.987 155.466 113.021 1.00 23.78 ?  453 ARG A CG    1 
ATOM   3643  C  CD    . ARG A 1 453 ? 141.650 156.137 114.211 1.00 21.86 ?  453 ARG A CD    1 
ATOM   3644  N  NE    . ARG A 1 453 ? 142.872 155.449 114.608 1.00 21.77 ?  453 ARG A NE    1 
ATOM   3645  C  CZ    . ARG A 1 453 ? 144.064 155.674 114.073 1.00 23.79 ?  453 ARG A CZ    1 
ATOM   3646  N  NH1   . ARG A 1 453 ? 144.234 156.565 113.111 1.00 24.12 1  453 ARG A NH1   1 
ATOM   3647  N  NH2   . ARG A 1 453 ? 145.113 154.985 114.513 1.00 25.71 ?  453 ARG A NH2   1 
ATOM   3648  N  N     . ALA A 1 454 ? 139.600 152.908 111.012 1.00 23.64 ?  454 ALA A N     1 
ATOM   3649  C  CA    . ALA A 1 454 ? 140.327 152.197 109.968 1.00 18.39 ?  454 ALA A CA    1 
ATOM   3650  C  C     . ALA A 1 454 ? 139.559 152.182 108.655 1.00 18.15 ?  454 ALA A C     1 
ATOM   3651  O  O     . ALA A 1 454 ? 140.174 152.184 107.585 1.00 23.75 ?  454 ALA A O     1 
ATOM   3652  C  CB    . ALA A 1 454 ? 140.639 150.773 110.420 1.00 20.65 ?  454 ALA A CB    1 
ATOM   3653  N  N     . ASN A 1 455 ? 138.227 152.163 108.705 1.00 20.68 ?  455 ASN A N     1 
ATOM   3654  C  CA    . ASN A 1 455 ? 137.452 152.268 107.475 1.00 21.99 ?  455 ASN A CA    1 
ATOM   3655  C  C     . ASN A 1 455 ? 137.638 153.634 106.829 1.00 25.45 ?  455 ASN A C     1 
ATOM   3656  O  O     . ASN A 1 455 ? 137.764 153.736 105.603 1.00 30.27 ?  455 ASN A O     1 
ATOM   3657  C  CB    . ASN A 1 455 ? 135.975 151.999 107.756 1.00 19.31 ?  455 ASN A CB    1 
ATOM   3658  C  CG    . ASN A 1 455 ? 135.126 152.040 106.503 1.00 27.04 ?  455 ASN A CG    1 
ATOM   3659  O  OD1   . ASN A 1 455 ? 135.372 151.301 105.550 1.00 31.25 ?  455 ASN A OD1   1 
ATOM   3660  N  ND2   . ASN A 1 455 ? 134.121 152.906 106.496 1.00 26.78 ?  455 ASN A ND2   1 
ATOM   3661  N  N     . LYS A 1 456 ? 137.655 154.695 107.639 1.00 24.12 ?  456 LYS A N     1 
ATOM   3662  C  CA    . LYS A 1 456 ? 137.866 156.033 107.093 1.00 25.23 ?  456 LYS A CA    1 
ATOM   3663  C  C     . LYS A 1 456 ? 139.284 156.205 106.559 1.00 23.97 ?  456 LYS A C     1 
ATOM   3664  O  O     . LYS A 1 456 ? 139.487 156.842 105.520 1.00 29.54 ?  456 LYS A O     1 
ATOM   3665  C  CB    . LYS A 1 456 ? 137.566 157.087 108.158 1.00 27.55 ?  456 LYS A CB    1 
ATOM   3666  C  CG    . LYS A 1 456 ? 136.216 157.769 107.998 1.00 30.26 ?  456 LYS A CG    1 
ATOM   3667  C  CD    . LYS A 1 456 ? 135.518 157.975 109.340 1.00 33.55 ?  456 LYS A CD    1 
ATOM   3668  C  CE    . LYS A 1 456 ? 136.515 158.168 110.475 1.00 33.77 ?  456 LYS A CE    1 
ATOM   3669  N  NZ    . LYS A 1 456 ? 135.847 158.267 111.801 1.00 31.84 1  456 LYS A NZ    1 
ATOM   3670  N  N     . ALA A 1 457 ? 140.275 155.645 107.254 1.00 19.17 ?  457 ALA A N     1 
ATOM   3671  C  CA    . ALA A 1 457 ? 141.671 155.888 106.906 1.00 17.96 ?  457 ALA A CA    1 
ATOM   3672  C  C     . ALA A 1 457 ? 142.153 154.953 105.801 1.00 24.71 ?  457 ALA A C     1 
ATOM   3673  O  O     . ALA A 1 457 ? 142.590 155.402 104.737 1.00 29.05 ?  457 ALA A O     1 
ATOM   3674  C  CB    . ALA A 1 457 ? 142.548 155.739 108.152 1.00 15.33 ?  457 ALA A CB    1 
ATOM   3675  N  N     . MET A 1 458 ? 142.086 153.645 106.047 1.00 23.82 ?  458 MET A N     1 
ATOM   3676  C  CA    . MET A 1 458 ? 142.634 152.661 105.122 1.00 19.43 ?  458 MET A CA    1 
ATOM   3677  C  C     . MET A 1 458 ? 141.832 152.560 103.831 1.00 23.77 ?  458 MET A C     1 
ATOM   3678  O  O     . MET A 1 458 ? 142.417 152.327 102.768 1.00 30.03 ?  458 MET A O     1 
ATOM   3679  C  CB    . MET A 1 458 ? 142.701 151.296 105.806 1.00 22.61 ?  458 MET A CB    1 
ATOM   3680  C  CG    . MET A 1 458 ? 143.530 151.285 107.078 1.00 14.51 ?  458 MET A CG    1 
ATOM   3681  S  SD    . MET A 1 458 ? 145.287 151.520 106.758 1.00 33.37 ?  458 MET A SD    1 
ATOM   3682  C  CE    . MET A 1 458 ? 145.882 149.838 106.908 1.00 22.54 ?  458 MET A CE    1 
ATOM   3683  N  N     . LYS A 1 459 ? 140.509 152.722 103.903 1.00 18.14 ?  459 LYS A N     1 
ATOM   3684  C  CA    . LYS A 1 459 ? 139.633 152.583 102.738 1.00 21.43 ?  459 LYS A CA    1 
ATOM   3685  C  C     . LYS A 1 459 ? 139.842 151.233 102.058 1.00 21.56 ?  459 LYS A C     1 
ATOM   3686  O  O     . LYS A 1 459 ? 139.846 151.121 100.831 1.00 27.81 ?  459 LYS A O     1 
ATOM   3687  C  CB    . LYS A 1 459 ? 139.838 153.727 101.744 1.00 22.37 ?  459 LYS A CB    1 
ATOM   3688  C  CG    . LYS A 1 459 ? 139.634 155.112 102.327 1.00 24.94 ?  459 LYS A CG    1 
ATOM   3689  C  CD    . LYS A 1 459 ? 140.813 156.015 102.011 1.00 25.12 ?  459 LYS A CD    1 
ATOM   3690  C  CE    . LYS A 1 459 ? 140.400 157.475 102.009 1.00 27.52 ?  459 LYS A CE    1 
ATOM   3691  N  NZ    . LYS A 1 459 ? 139.185 157.708 102.838 1.00 30.30 1  459 LYS A NZ    1 
ATOM   3692  N  N     . SER A 1 460 ? 140.022 150.196 102.869 1.00 20.55 ?  460 SER A N     1 
ATOM   3693  C  CA    . SER A 1 460 ? 140.337 148.875 102.349 1.00 11.16 ?  460 SER A CA    1 
ATOM   3694  C  C     . SER A 1 460 ? 139.075 148.162 101.886 1.00 15.54 ?  460 SER A C     1 
ATOM   3695  O  O     . SER A 1 460 ? 138.049 148.171 102.572 1.00 26.00 ?  460 SER A O     1 
ATOM   3696  C  CB    . SER A 1 460 ? 141.051 148.042 103.411 1.00 13.25 ?  460 SER A CB    1 
ATOM   3697  O  OG    . SER A 1 460 ? 140.148 147.167 104.059 1.00 13.78 ?  460 SER A OG    1 
ATOM   3698  N  N     . ILE A 1 461 ? 139.160 147.545 100.710 1.00 17.07 ?  461 ILE A N     1 
ATOM   3699  C  CA    . ILE A 1 461 ? 138.068 146.773 100.139 1.00 11.44 ?  461 ILE A CA    1 
ATOM   3700  C  C     . ILE A 1 461 ? 138.601 145.396 99.774  1.00 18.03 ?  461 ILE A C     1 
ATOM   3701  O  O     . ILE A 1 461 ? 139.802 145.199 99.583  1.00 18.23 ?  461 ILE A O     1 
ATOM   3702  C  CB    . ILE A 1 461 ? 137.454 147.458 98.900  1.00 13.11 ?  461 ILE A CB    1 
ATOM   3703  C  CG1   . ILE A 1 461 ? 138.520 147.650 97.820  1.00 8.92  ?  461 ILE A CG1   1 
ATOM   3704  C  CG2   . ILE A 1 461 ? 136.829 148.791 99.282  1.00 13.75 ?  461 ILE A CG2   1 
ATOM   3705  C  CD1   . ILE A 1 461 ? 137.971 148.089 96.489  1.00 8.18  ?  461 ILE A CD1   1 
ATOM   3706  N  N     . GLY A 1 462 ? 137.693 144.429 99.706  1.00 17.97 ?  462 GLY A N     1 
ATOM   3707  C  CA    . GLY A 1 462 ? 138.060 143.116 99.225  1.00 8.19  ?  462 GLY A CA    1 
ATOM   3708  C  C     . GLY A 1 462 ? 137.297 142.717 97.981  1.00 5.51  ?  462 GLY A C     1 
ATOM   3709  O  O     . GLY A 1 462 ? 136.101 142.423 98.050  1.00 19.62 ?  462 GLY A O     1 
ATOM   3710  N  N     . LEU A 1 463 ? 137.976 142.684 96.842  1.00 11.37 ?  463 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 463 ? 137.376 142.260 95.583  1.00 9.14  ?  463 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 463 ? 137.798 140.820 95.322  1.00 11.19 ?  463 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 463 ? 138.967 140.551 95.032  1.00 20.03 ?  463 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 463 ? 137.794 143.176 94.438  1.00 18.61 ?  463 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 463 ? 137.223 142.831 93.060  1.00 18.85 ?  463 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 463 ? 135.719 142.640 93.137  1.00 9.23  ?  463 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 463 ? 137.579 143.906 92.049  1.00 15.50 ?  463 LEU A CD2   1 
ATOM   3718  N  N     . GLY A 1 464 ? 136.844 139.895 95.430  1.00 12.27 ?  464 GLY A N     1 
ATOM   3719  C  CA    . GLY A 1 464 ? 137.110 138.489 95.238  1.00 8.91  ?  464 GLY A CA    1 
ATOM   3720  C  C     . GLY A 1 464 ? 136.687 137.994 93.863  1.00 14.99 ?  464 GLY A C     1 
ATOM   3721  O  O     . GLY A 1 464 ? 136.219 138.738 93.005  1.00 21.90 ?  464 GLY A O     1 
ATOM   3722  N  N     . ALA A 1 465 ? 136.872 136.693 93.670  1.00 14.56 ?  465 ALA A N     1 
ATOM   3723  C  CA    . ALA A 1 465 ? 136.476 136.027 92.442  1.00 10.65 ?  465 ALA A CA    1 
ATOM   3724  C  C     . ALA A 1 465 ? 135.829 134.695 92.789  1.00 13.06 ?  465 ALA A C     1 
ATOM   3725  O  O     . ALA A 1 465 ? 136.104 134.109 93.838  1.00 22.50 ?  465 ALA A O     1 
ATOM   3726  C  CB    . ALA A 1 465 ? 137.668 135.809 91.504  1.00 16.40 ?  465 ALA A CB    1 
ATOM   3727  N  N     . MET A 1 466 ? 134.958 134.231 91.898  1.00 13.84 ?  466 MET A N     1 
ATOM   3728  C  CA    . MET A 1 466 ? 134.295 132.949 92.070  1.00 20.15 ?  466 MET A CA    1 
ATOM   3729  C  C     . MET A 1 466 ? 134.076 132.331 90.697  1.00 20.70 ?  466 MET A C     1 
ATOM   3730  O  O     . MET A 1 466 ? 134.361 132.944 89.666  1.00 27.41 ?  466 MET A O     1 
ATOM   3731  C  CB    . MET A 1 466 ? 132.971 133.097 92.824  1.00 25.63 ?  466 MET A CB    1 
ATOM   3732  C  CG    . MET A 1 466 ? 131.938 133.913 92.079  1.00 21.84 ?  466 MET A CG    1 
ATOM   3733  S  SD    . MET A 1 466 ? 130.483 134.280 93.067  1.00 34.17 ?  466 MET A SD    1 
ATOM   3734  C  CE    . MET A 1 466 ? 129.703 135.495 92.018  1.00 25.31 ?  466 MET A CE    1 
ATOM   3735  N  N     . ASN A 1 467 ? 133.563 131.100 90.702  1.00 13.45 ?  467 ASN A N     1 
ATOM   3736  C  CA    . ASN A 1 467 ? 133.313 130.329 89.484  1.00 16.31 ?  467 ASN A CA    1 
ATOM   3737  C  C     . ASN A 1 467 ? 134.601 130.035 88.723  1.00 18.38 ?  467 ASN A C     1 
ATOM   3738  O  O     . ASN A 1 467 ? 134.592 129.913 87.497  1.00 23.98 ?  467 ASN A O     1 
ATOM   3739  C  CB    . ASN A 1 467 ? 132.306 131.031 88.567  1.00 20.54 ?  467 ASN A CB    1 
ATOM   3740  C  CG    . ASN A 1 467 ? 131.364 130.061 87.887  1.00 23.54 ?  467 ASN A CG    1 
ATOM   3741  O  OD1   . ASN A 1 467 ? 131.370 128.867 88.178  1.00 31.27 ?  467 ASN A OD1   1 
ATOM   3742  N  ND2   . ASN A 1 467 ? 130.546 130.571 86.976  1.00 23.37 ?  467 ASN A ND2   1 
ATOM   3743  N  N     . LEU A 1 468 ? 135.720 129.926 89.439  1.00 18.69 ?  468 LEU A N     1 
ATOM   3744  C  CA    . LEU A 1 468 ? 136.969 129.543 88.790  1.00 13.32 ?  468 LEU A CA    1 
ATOM   3745  C  C     . LEU A 1 468 ? 136.900 128.108 88.288  1.00 20.58 ?  468 LEU A C     1 
ATOM   3746  O  O     . LEU A 1 468 ? 137.186 127.832 87.117  1.00 21.33 ?  468 LEU A O     1 
ATOM   3747  C  CB    . LEU A 1 468 ? 138.141 129.716 89.754  1.00 22.42 ?  468 LEU A CB    1 
ATOM   3748  C  CG    . LEU A 1 468 ? 139.484 129.163 89.273  1.00 19.10 ?  468 LEU A CG    1 
ATOM   3749  C  CD1   . LEU A 1 468 ? 140.027 129.987 88.116  1.00 16.67 ?  468 LEU A CD1   1 
ATOM   3750  C  CD2   . LEU A 1 468 ? 140.484 129.104 90.411  1.00 14.68 ?  468 LEU A CD2   1 
ATOM   3751  N  N     . HIS A 1 469 ? 136.499 127.181 89.160  1.00 25.22 ?  469 HIS A N     1 
ATOM   3752  C  CA    . HIS A 1 469 ? 136.386 125.788 88.749  1.00 16.21 ?  469 HIS A CA    1 
ATOM   3753  C  C     . HIS A 1 469 ? 135.268 125.605 87.736  1.00 25.21 ?  469 HIS A C     1 
ATOM   3754  O  O     . HIS A 1 469 ? 135.398 124.811 86.802  1.00 33.67 ?  469 HIS A O     1 
ATOM   3755  C  CB    . HIS A 1 469 ? 136.159 124.887 89.961  1.00 17.64 ?  469 HIS A CB    1 
ATOM   3756  C  CG    . HIS A 1 469 ? 136.335 123.431 89.662  1.00 22.56 ?  469 HIS A CG    1 
ATOM   3757  N  ND1   . HIS A 1 469 ? 135.997 122.440 90.556  1.00 27.87 ?  469 HIS A ND1   1 
ATOM   3758  C  CD2   . HIS A 1 469 ? 136.816 122.799 88.565  1.00 23.49 ?  469 HIS A CD2   1 
ATOM   3759  C  CE1   . HIS A 1 469 ? 136.260 121.260 90.023  1.00 23.94 ?  469 HIS A CE1   1 
ATOM   3760  N  NE2   . HIS A 1 469 ? 136.758 121.451 88.816  1.00 28.10 ?  469 HIS A NE2   1 
ATOM   3761  N  N     . GLY A 1 470 ? 134.157 126.324 87.907  1.00 24.88 ?  470 GLY A N     1 
ATOM   3762  C  CA    . GLY A 1 470 ? 133.101 126.266 86.911  1.00 20.72 ?  470 GLY A CA    1 
ATOM   3763  C  C     . GLY A 1 470 ? 133.579 126.717 85.546  1.00 18.09 ?  470 GLY A C     1 
ATOM   3764  O  O     . GLY A 1 470 ? 133.344 126.045 84.539  1.00 35.24 ?  470 GLY A O     1 
ATOM   3765  N  N     . TYR A 1 471 ? 134.282 127.850 85.499  1.00 17.42 ?  471 TYR A N     1 
ATOM   3766  C  CA    . TYR A 1 471 ? 134.791 128.348 84.227  1.00 21.95 ?  471 TYR A CA    1 
ATOM   3767  C  C     . TYR A 1 471 ? 135.779 127.365 83.609  1.00 25.73 ?  471 TYR A C     1 
ATOM   3768  O  O     . TYR A 1 471 ? 135.751 127.118 82.399  1.00 28.80 ?  471 TYR A O     1 
ATOM   3769  C  CB    . TYR A 1 471 ? 135.454 129.713 84.411  1.00 22.09 ?  471 TYR A CB    1 
ATOM   3770  C  CG    . TYR A 1 471 ? 136.144 130.191 83.157  1.00 19.48 ?  471 TYR A CG    1 
ATOM   3771  C  CD1   . TYR A 1 471 ? 135.418 130.771 82.125  1.00 23.38 ?  471 TYR A CD1   1 
ATOM   3772  C  CD2   . TYR A 1 471 ? 137.512 130.033 82.984  1.00 18.44 ?  471 TYR A CD2   1 
ATOM   3773  C  CE1   . TYR A 1 471 ? 136.035 131.199 80.970  1.00 25.73 ?  471 TYR A CE1   1 
ATOM   3774  C  CE2   . TYR A 1 471 ? 138.138 130.455 81.828  1.00 22.96 ?  471 TYR A CE2   1 
ATOM   3775  C  CZ    . TYR A 1 471 ? 137.394 131.038 80.826  1.00 25.21 ?  471 TYR A CZ    1 
ATOM   3776  O  OH    . TYR A 1 471 ? 138.008 131.459 79.673  1.00 31.66 ?  471 TYR A OH    1 
ATOM   3777  N  N     . LEU A 1 472 ? 136.676 126.810 84.427  1.00 27.82 ?  472 LEU A N     1 
ATOM   3778  C  CA    . LEU A 1 472 ? 137.677 125.883 83.906  1.00 24.74 ?  472 LEU A CA    1 
ATOM   3779  C  C     . LEU A 1 472 ? 137.037 124.596 83.398  1.00 27.35 ?  472 LEU A C     1 
ATOM   3780  O  O     . LEU A 1 472 ? 137.450 124.059 82.365  1.00 32.46 ?  472 LEU A O     1 
ATOM   3781  C  CB    . LEU A 1 472 ? 138.722 125.581 84.981  1.00 25.71 ?  472 LEU A CB    1 
ATOM   3782  C  CG    . LEU A 1 472 ? 139.625 126.742 85.399  1.00 24.59 ?  472 LEU A CG    1 
ATOM   3783  C  CD1   . LEU A 1 472 ? 140.374 126.406 86.679  1.00 23.05 ?  472 LEU A CD1   1 
ATOM   3784  C  CD2   . LEU A 1 472 ? 140.595 127.096 84.284  1.00 23.35 ?  472 LEU A CD2   1 
ATOM   3785  N  N     . ALA A 1 473 ? 136.035 124.082 84.114  1.00 26.73 ?  473 ALA A N     1 
ATOM   3786  C  CA    . ALA A 1 473 ? 135.392 122.838 83.710  1.00 24.56 ?  473 ALA A CA    1 
ATOM   3787  C  C     . ALA A 1 473 ? 134.546 123.028 82.456  1.00 35.21 ?  473 ALA A C     1 
ATOM   3788  O  O     . ALA A 1 473 ? 134.534 122.161 81.576  1.00 42.98 ?  473 ALA A O     1 
ATOM   3789  C  CB    . ALA A 1 473 ? 134.546 122.293 84.857  1.00 27.08 ?  473 ALA A CB    1 
ATOM   3790  N  N     . GLN A 1 474 ? 133.833 124.154 82.353  1.00 29.14 ?  474 GLN A N     1 
ATOM   3791  C  CA    . GLN A 1 474 ? 133.061 124.427 81.147  1.00 29.13 ?  474 GLN A CA    1 
ATOM   3792  C  C     . GLN A 1 474 ? 133.936 124.776 79.951  1.00 32.16 ?  474 GLN A C     1 
ATOM   3793  O  O     . GLN A 1 474 ? 133.416 124.877 78.835  1.00 36.34 ?  474 GLN A O     1 
ATOM   3794  C  CB    . GLN A 1 474 ? 132.057 125.553 81.395  1.00 28.84 ?  474 GLN A CB    1 
ATOM   3795  C  CG    . GLN A 1 474 ? 131.149 125.332 82.588  1.00 30.82 ?  474 GLN A CG    1 
ATOM   3796  C  CD    . GLN A 1 474 ? 129.824 126.047 82.448  1.00 32.74 ?  474 GLN A CD    1 
ATOM   3797  O  OE1   . GLN A 1 474 ? 129.241 126.090 81.365  1.00 37.49 ?  474 GLN A OE1   1 
ATOM   3798  N  NE2   . GLN A 1 474 ? 129.341 126.619 83.544  1.00 31.46 ?  474 GLN A NE2   1 
ATOM   3799  N  N     . ASN A 1 475 ? 135.241 124.964 80.150  1.00 33.08 ?  475 ASN A N     1 
ATOM   3800  C  CA    . ASN A 1 475 ? 136.173 125.225 79.063  1.00 35.90 ?  475 ASN A CA    1 
ATOM   3801  C  C     . ASN A 1 475 ? 137.129 124.059 78.833  1.00 35.04 ?  475 ASN A C     1 
ATOM   3802  O  O     . ASN A 1 475 ? 138.150 124.222 78.158  1.00 33.44 ?  475 ASN A O     1 
ATOM   3803  C  CB    . ASN A 1 475 ? 136.953 126.511 79.334  1.00 32.28 ?  475 ASN A CB    1 
ATOM   3804  C  CG    . ASN A 1 475 ? 136.116 127.752 79.114  1.00 31.54 ?  475 ASN A CG    1 
ATOM   3805  O  OD1   . ASN A 1 475 ? 136.066 128.294 78.011  1.00 33.91 ?  475 ASN A OD1   1 
ATOM   3806  N  ND2   . ASN A 1 475 ? 135.439 128.200 80.163  1.00 29.10 ?  475 ASN A ND2   1 
ATOM   3807  N  N     . GLY A 1 476 ? 136.812 122.888 79.377  1.00 29.82 ?  476 GLY A N     1 
ATOM   3808  C  CA    . GLY A 1 476 ? 137.646 121.713 79.177  1.00 29.15 ?  476 GLY A CA    1 
ATOM   3809  C  C     . GLY A 1 476 ? 139.028 121.823 79.781  1.00 35.07 ?  476 GLY A C     1 
ATOM   3810  O  O     . GLY A 1 476 ? 140.013 121.426 79.146  1.00 37.01 ?  476 GLY A O     1 
ATOM   3811  N  N     . ILE A 1 477 ? 139.127 122.356 80.996  1.00 31.50 ?  477 ILE A N     1 
ATOM   3812  C  CA    . ILE A 1 477 ? 140.400 122.514 81.687  1.00 26.83 ?  477 ILE A CA    1 
ATOM   3813  C  C     . ILE A 1 477 ? 140.276 121.914 83.079  1.00 31.18 ?  477 ILE A C     1 
ATOM   3814  O  O     . ILE A 1 477 ? 139.378 122.285 83.842  1.00 34.93 ?  477 ILE A O     1 
ATOM   3815  C  CB    . ILE A 1 477 ? 140.826 123.992 81.773  1.00 27.36 ?  477 ILE A CB    1 
ATOM   3816  C  CG1   . ILE A 1 477 ? 141.040 124.565 80.373  1.00 30.88 ?  477 ILE A CG1   1 
ATOM   3817  C  CG2   . ILE A 1 477 ? 142.090 124.131 82.598  1.00 28.51 ?  477 ILE A CG2   1 
ATOM   3818  C  CD1   . ILE A 1 477 ? 141.057 126.068 80.335  1.00 30.35 ?  477 ILE A CD1   1 
ATOM   3819  N  N     . ALA A 1 478 ? 141.173 120.989 83.406  1.00 31.04 ?  478 ALA A N     1 
ATOM   3820  C  CA    . ALA A 1 478 ? 141.196 120.408 84.739  1.00 27.78 ?  478 ALA A CA    1 
ATOM   3821  C  C     . ALA A 1 478 ? 141.725 121.421 85.746  1.00 30.47 ?  478 ALA A C     1 
ATOM   3822  O  O     . ALA A 1 478 ? 142.657 122.175 85.458  1.00 31.20 ?  478 ALA A O     1 
ATOM   3823  C  CB    . ALA A 1 478 ? 142.059 119.147 84.757  1.00 28.28 ?  478 ALA A CB    1 
ATOM   3824  N  N     . TYR A 1 479 ? 141.121 121.431 86.937  1.00 29.75 ?  479 TYR A N     1 
ATOM   3825  C  CA    . TYR A 1 479 ? 141.516 122.390 87.964  1.00 22.93 ?  479 TYR A CA    1 
ATOM   3826  C  C     . TYR A 1 479 ? 142.970 122.208 88.378  1.00 27.34 ?  479 TYR A C     1 
ATOM   3827  O  O     . TYR A 1 479 ? 143.645 123.186 88.719  1.00 33.22 ?  479 TYR A O     1 
ATOM   3828  C  CB    . TYR A 1 479 ? 140.593 122.256 89.176  1.00 21.32 ?  479 TYR A CB    1 
ATOM   3829  C  CG    . TYR A 1 479 ? 140.796 123.300 90.253  1.00 28.50 ?  479 TYR A CG    1 
ATOM   3830  C  CD1   . TYR A 1 479 ? 141.701 123.093 91.287  1.00 26.50 ?  479 TYR A CD1   1 
ATOM   3831  C  CD2   . TYR A 1 479 ? 140.072 124.482 90.244  1.00 22.04 ?  479 TYR A CD2   1 
ATOM   3832  C  CE1   . TYR A 1 479 ? 141.885 124.039 92.274  1.00 22.41 ?  479 TYR A CE1   1 
ATOM   3833  C  CE2   . TYR A 1 479 ? 140.248 125.434 91.228  1.00 22.90 ?  479 TYR A CE2   1 
ATOM   3834  C  CZ    . TYR A 1 479 ? 141.155 125.207 92.240  1.00 29.54 ?  479 TYR A CZ    1 
ATOM   3835  O  OH    . TYR A 1 479 ? 141.333 126.154 93.222  1.00 31.36 ?  479 TYR A OH    1 
ATOM   3836  N  N     . GLU A 1 480 ? 143.471 120.977 88.354  1.00 30.91 ?  480 GLU A N     1 
ATOM   3837  C  CA    . GLU A 1 480 ? 144.847 120.693 88.736  1.00 29.89 ?  480 GLU A CA    1 
ATOM   3838  C  C     . GLU A 1 480 ? 145.825 120.803 87.576  1.00 32.47 ?  480 GLU A C     1 
ATOM   3839  O  O     . GLU A 1 480 ? 147.030 120.629 87.784  1.00 37.66 ?  480 GLU A O     1 
ATOM   3840  C  CB    . GLU A 1 480 ? 144.944 119.295 89.347  1.00 29.48 ?  480 GLU A CB    1 
ATOM   3841  C  CG    . GLU A 1 480 ? 144.036 119.062 90.536  1.00 30.62 ?  480 GLU A CG    1 
ATOM   3842  C  CD    . GLU A 1 480 ? 143.667 117.603 90.694  1.00 37.66 ?  480 GLU A CD    1 
ATOM   3843  O  OE1   . GLU A 1 480 ? 142.761 117.136 89.973  1.00 38.85 ?  480 GLU A OE1   1 
ATOM   3844  O  OE2   . GLU A 1 480 ? 144.288 116.920 91.535  1.00 38.05 -1 480 GLU A OE2   1 
ATOM   3845  N  N     . SER A 1 481 ? 145.344 121.083 86.370  1.00 30.10 ?  481 SER A N     1 
ATOM   3846  C  CA    . SER A 1 481 ? 146.223 121.141 85.215  1.00 27.49 ?  481 SER A CA    1 
ATOM   3847  C  C     . SER A 1 481 ? 147.085 122.402 85.255  1.00 31.91 ?  481 SER A C     1 
ATOM   3848  O  O     . SER A 1 481 ? 146.685 123.421 85.825  1.00 32.24 ?  481 SER A O     1 
ATOM   3849  C  CB    . SER A 1 481 ? 145.409 121.110 83.926  1.00 29.10 ?  481 SER A CB    1 
ATOM   3850  O  OG    . SER A 1 481 ? 144.998 122.412 83.553  1.00 33.68 ?  481 SER A OG    1 
ATOM   3851  N  N     . PRO A 1 482 ? 148.282 122.354 84.664  1.00 37.78 ?  482 PRO A N     1 
ATOM   3852  C  CA    . PRO A 1 482 ? 149.087 123.582 84.550  1.00 30.91 ?  482 PRO A CA    1 
ATOM   3853  C  C     . PRO A 1 482 ? 148.403 124.669 83.743  1.00 29.86 ?  482 PRO A C     1 
ATOM   3854  O  O     . PRO A 1 482 ? 148.677 125.855 83.961  1.00 34.98 ?  482 PRO A O     1 
ATOM   3855  C  CB    . PRO A 1 482 ? 150.374 123.095 83.871  1.00 30.41 ?  482 PRO A CB    1 
ATOM   3856  C  CG    . PRO A 1 482 ? 150.423 121.631 84.143  1.00 32.89 ?  482 PRO A CG    1 
ATOM   3857  C  CD    . PRO A 1 482 ? 148.999 121.174 84.158  1.00 31.72 ?  482 PRO A CD    1 
ATOM   3858  N  N     . GLU A 1 483 ? 147.524 124.299 82.809  1.00 36.10 ?  483 GLU A N     1 
ATOM   3859  C  CA    . GLU A 1 483 ? 146.773 125.298 82.055  1.00 32.70 ?  483 GLU A CA    1 
ATOM   3860  C  C     . GLU A 1 483 ? 145.829 126.079 82.960  1.00 31.18 ?  483 GLU A C     1 
ATOM   3861  O  O     . GLU A 1 483 ? 145.648 127.288 82.781  1.00 35.55 ?  483 GLU A O     1 
ATOM   3862  C  CB    . GLU A 1 483 ? 145.995 124.627 80.923  1.00 33.67 ?  483 GLU A CB    1 
ATOM   3863  C  CG    . GLU A 1 483 ? 146.861 124.177 79.759  1.00 36.84 ?  483 GLU A CG    1 
ATOM   3864  C  CD    . GLU A 1 483 ? 147.422 122.781 79.952  1.00 39.71 ?  483 GLU A CD    1 
ATOM   3865  O  OE1   . GLU A 1 483 ? 147.356 122.262 81.086  1.00 37.12 ?  483 GLU A OE1   1 
ATOM   3866  O  OE2   . GLU A 1 483 ? 147.931 122.205 78.970  1.00 41.10 -1 483 GLU A OE2   1 
ATOM   3867  N  N     . ALA A 1 484 ? 145.210 125.401 83.929  1.00 26.19 ?  484 ALA A N     1 
ATOM   3868  C  CA    . ALA A 1 484 ? 144.346 126.096 84.878  1.00 25.77 ?  484 ALA A CA    1 
ATOM   3869  C  C     . ALA A 1 484 ? 145.132 127.106 85.702  1.00 25.99 ?  484 ALA A C     1 
ATOM   3870  O  O     . ALA A 1 484 ? 144.665 128.227 85.935  1.00 25.65 ?  484 ALA A O     1 
ATOM   3871  C  CB    . ALA A 1 484 ? 143.650 125.090 85.790  1.00 20.79 ?  484 ALA A CB    1 
ATOM   3872  N  N     . ARG A 1 485 ? 146.328 126.727 86.155  1.00 27.55 ?  485 ARG A N     1 
ATOM   3873  C  CA    . ARG A 1 485 ? 147.160 127.662 86.903  1.00 21.77 ?  485 ARG A CA    1 
ATOM   3874  C  C     . ARG A 1 485 ? 147.637 128.811 86.025  1.00 22.14 ?  485 ARG A C     1 
ATOM   3875  O  O     . ARG A 1 485 ? 147.736 129.946 86.499  1.00 30.74 ?  485 ARG A O     1 
ATOM   3876  C  CB    . ARG A 1 485 ? 148.350 126.933 87.522  1.00 24.49 ?  485 ARG A CB    1 
ATOM   3877  C  CG    . ARG A 1 485 ? 147.978 126.044 88.692  1.00 25.08 ?  485 ARG A CG    1 
ATOM   3878  C  CD    . ARG A 1 485 ? 149.213 125.532 89.406  1.00 26.67 ?  485 ARG A CD    1 
ATOM   3879  N  NE    . ARG A 1 485 ? 150.051 124.717 88.534  1.00 27.79 ?  485 ARG A NE    1 
ATOM   3880  C  CZ    . ARG A 1 485 ? 149.858 123.425 88.307  1.00 29.59 ?  485 ARG A CZ    1 
ATOM   3881  N  NH1   . ARG A 1 485 ? 148.855 122.768 88.863  1.00 27.74 1  485 ARG A NH1   1 
ATOM   3882  N  NH2   . ARG A 1 485 ? 150.694 122.777 87.502  1.00 25.12 ?  485 ARG A NH2   1 
ATOM   3883  N  N     . ASP A 1 486 ? 147.935 128.539 84.755  1.00 29.60 ?  486 ASP A N     1 
ATOM   3884  C  CA    . ASP A 1 486 ? 148.290 129.605 83.824  1.00 28.93 ?  486 ASP A CA    1 
ATOM   3885  C  C     . ASP A 1 486 ? 147.142 130.594 83.661  1.00 29.97 ?  486 ASP A C     1 
ATOM   3886  O  O     . ASP A 1 486 ? 147.344 131.818 83.683  1.00 35.68 ?  486 ASP A O     1 
ATOM   3887  C  CB    . ASP A 1 486 ? 148.680 128.998 82.478  1.00 33.99 ?  486 ASP A CB    1 
ATOM   3888  C  CG    . ASP A 1 486 ? 149.244 130.018 81.519  1.00 39.53 ?  486 ASP A CG    1 
ATOM   3889  O  OD1   . ASP A 1 486 ? 150.240 130.685 81.870  1.00 38.33 ?  486 ASP A OD1   1 
ATOM   3890  O  OD2   . ASP A 1 486 ? 148.691 130.146 80.408  1.00 40.45 -1 486 ASP A OD2   1 
ATOM   3891  N  N     . PHE A 1 487 ? 145.922 130.078 83.501  1.00 27.52 ?  487 PHE A N     1 
ATOM   3892  C  CA    . PHE A 1 487 ? 144.765 130.955 83.392  1.00 24.06 ?  487 PHE A CA    1 
ATOM   3893  C  C     . PHE A 1 487 ? 144.560 131.760 84.664  1.00 23.48 ?  487 PHE A C     1 
ATOM   3894  O  O     . PHE A 1 487 ? 144.249 132.952 84.603  1.00 28.50 ?  487 PHE A O     1 
ATOM   3895  C  CB    . PHE A 1 487 ? 143.497 130.162 83.082  1.00 23.47 ?  487 PHE A CB    1 
ATOM   3896  C  CG    . PHE A 1 487 ? 142.243 130.937 83.356  1.00 24.82 ?  487 PHE A CG    1 
ATOM   3897  C  CD1   . PHE A 1 487 ? 141.815 131.910 82.470  1.00 22.38 ?  487 PHE A CD1   1 
ATOM   3898  C  CD2   . PHE A 1 487 ? 141.513 130.724 84.514  1.00 24.88 ?  487 PHE A CD2   1 
ATOM   3899  C  CE1   . PHE A 1 487 ? 140.676 132.642 82.723  1.00 24.63 ?  487 PHE A CE1   1 
ATOM   3900  C  CE2   . PHE A 1 487 ? 140.374 131.454 84.771  1.00 25.98 ?  487 PHE A CE2   1 
ATOM   3901  C  CZ    . PHE A 1 487 ? 139.955 132.415 83.874  1.00 24.61 ?  487 PHE A CZ    1 
ATOM   3902  N  N     . ALA A 1 488 ? 144.686 131.117 85.826  1.00 20.43 ?  488 ALA A N     1 
ATOM   3903  C  CA    . ALA A 1 488 ? 144.513 131.836 87.081  1.00 16.31 ?  488 ALA A CA    1 
ATOM   3904  C  C     . ALA A 1 488 ? 145.554 132.935 87.221  1.00 23.39 ?  488 ALA A C     1 
ATOM   3905  O  O     . ALA A 1 488 ? 145.230 134.065 87.607  1.00 28.14 ?  488 ALA A O     1 
ATOM   3906  C  CB    . ALA A 1 488 ? 144.587 130.868 88.259  1.00 22.74 ?  488 ALA A CB    1 
ATOM   3907  N  N     . ASN A 1 489 ? 146.808 132.628 86.881  1.00 25.91 ?  489 ASN A N     1 
ATOM   3908  C  CA    . ASN A 1 489 ? 147.867 133.627 86.918  1.00 21.39 ?  489 ASN A CA    1 
ATOM   3909  C  C     . ASN A 1 489 ? 147.514 134.827 86.055  1.00 20.60 ?  489 ASN A C     1 
ATOM   3910  O  O     . ASN A 1 489 ? 147.525 135.970 86.527  1.00 23.98 ?  489 ASN A O     1 
ATOM   3911  C  CB    . ASN A 1 489 ? 149.182 132.999 86.453  1.00 17.63 ?  489 ASN A CB    1 
ATOM   3912  C  CG    . ASN A 1 489 ? 150.370 133.906 86.664  1.00 25.69 ?  489 ASN A CG    1 
ATOM   3913  O  OD1   . ASN A 1 489 ? 150.515 134.526 87.716  1.00 31.29 ?  489 ASN A OD1   1 
ATOM   3914  N  ND2   . ASN A 1 489 ? 151.236 133.985 85.662  1.00 28.39 ?  489 ASN A ND2   1 
ATOM   3915  N  N     . THR A 1 490 ? 147.165 134.585 84.790  1.00 22.74 ?  490 THR A N     1 
ATOM   3916  C  CA    . THR A 1 490 ? 146.879 135.696 83.887  1.00 21.31 ?  490 THR A CA    1 
ATOM   3917  C  C     . THR A 1 490 ? 145.649 136.477 84.339  1.00 22.67 ?  490 THR A C     1 
ATOM   3918  O  O     . THR A 1 490 ? 145.677 137.712 84.412  1.00 24.89 ?  490 THR A O     1 
ATOM   3919  C  CB    . THR A 1 490 ? 146.696 135.188 82.459  1.00 28.93 ?  490 THR A CB    1 
ATOM   3920  O  OG1   . THR A 1 490 ? 147.812 134.366 82.098  1.00 33.78 ?  490 THR A OG1   1 
ATOM   3921  C  CG2   . THR A 1 490 ? 146.599 136.358 81.495  1.00 22.59 ?  490 THR A CG2   1 
ATOM   3922  N  N     . PHE A 1 491 ? 144.563 135.770 84.658  1.00 19.82 ?  491 PHE A N     1 
ATOM   3923  C  CA    . PHE A 1 491 ? 143.308 136.427 85.007  1.00 17.95 ?  491 PHE A CA    1 
ATOM   3924  C  C     . PHE A 1 491 ? 143.466 137.278 86.256  1.00 22.82 ?  491 PHE A C     1 
ATOM   3925  O  O     . PHE A 1 491 ? 143.026 138.432 86.294  1.00 22.93 ?  491 PHE A O     1 
ATOM   3926  C  CB    . PHE A 1 491 ? 142.210 135.379 85.200  1.00 22.92 ?  491 PHE A CB    1 
ATOM   3927  C  CG    . PHE A 1 491 ? 140.914 135.943 85.716  1.00 19.23 ?  491 PHE A CG    1 
ATOM   3928  C  CD1   . PHE A 1 491 ? 139.966 136.440 84.842  1.00 17.23 ?  491 PHE A CD1   1 
ATOM   3929  C  CD2   . PHE A 1 491 ? 140.641 135.966 87.075  1.00 17.98 ?  491 PHE A CD2   1 
ATOM   3930  C  CE1   . PHE A 1 491 ? 138.777 136.960 85.308  1.00 15.75 ?  491 PHE A CE1   1 
ATOM   3931  C  CE2   . PHE A 1 491 ? 139.455 136.486 87.548  1.00 17.31 ?  491 PHE A CE2   1 
ATOM   3932  C  CZ    . PHE A 1 491 ? 138.520 136.983 86.662  1.00 19.56 ?  491 PHE A CZ    1 
ATOM   3933  N  N     . PHE A 1 492 ? 144.105 136.734 87.291  1.00 23.17 ?  492 PHE A N     1 
ATOM   3934  C  CA    . PHE A 1 492 ? 144.248 137.492 88.521  1.00 12.41 ?  492 PHE A CA    1 
ATOM   3935  C  C     . PHE A 1 492 ? 145.329 138.557 88.430  1.00 14.90 ?  492 PHE A C     1 
ATOM   3936  O  O     . PHE A 1 492 ? 145.246 139.554 89.150  1.00 20.08 ?  492 PHE A O     1 
ATOM   3937  C  CB    . PHE A 1 492 ? 144.505 136.540 89.687  1.00 19.66 ?  492 PHE A CB    1 
ATOM   3938  C  CG    . PHE A 1 492 ? 143.274 135.805 90.132  1.00 16.33 ?  492 PHE A CG    1 
ATOM   3939  C  CD1   . PHE A 1 492 ? 142.330 136.435 90.925  1.00 11.74 ?  492 PHE A CD1   1 
ATOM   3940  C  CD2   . PHE A 1 492 ? 143.042 134.501 89.733  1.00 16.15 ?  492 PHE A CD2   1 
ATOM   3941  C  CE1   . PHE A 1 492 ? 141.192 135.770 91.328  1.00 12.40 ?  492 PHE A CE1   1 
ATOM   3942  C  CE2   . PHE A 1 492 ? 141.902 133.831 90.133  1.00 14.11 ?  492 PHE A CE2   1 
ATOM   3943  C  CZ    . PHE A 1 492 ? 140.977 134.467 90.932  1.00 16.69 ?  492 PHE A CZ    1 
ATOM   3944  N  N     . MET A 1 493 ? 146.306 138.413 87.530  1.00 19.05 ?  493 MET A N     1 
ATOM   3945  C  CA    . MET A 1 493 ? 147.210 139.529 87.286  1.00 16.78 ?  493 MET A CA    1 
ATOM   3946  C  C     . MET A 1 493 ? 146.469 140.680 86.621  1.00 16.20 ?  493 MET A C     1 
ATOM   3947  O  O     . MET A 1 493 ? 146.690 141.843 86.968  1.00 22.30 ?  493 MET A O     1 
ATOM   3948  C  CB    . MET A 1 493 ? 148.417 139.057 86.462  1.00 17.19 ?  493 MET A CB    1 
ATOM   3949  C  CG    . MET A 1 493 ? 149.239 140.098 85.662  1.00 17.53 ?  493 MET A CG    1 
ATOM   3950  S  SD    . MET A 1 493 ? 148.484 141.169 84.415  1.00 32.83 ?  493 MET A SD    1 
ATOM   3951  C  CE    . MET A 1 493 ? 148.355 140.025 83.050  1.00 21.93 ?  493 MET A CE    1 
ATOM   3952  N  N     . MET A 1 494 ? 145.582 140.381 85.664  1.00 20.52 ?  494 MET A N     1 
ATOM   3953  C  CA    . MET A 1 494 ? 144.762 141.445 85.083  1.00 19.50 ?  494 MET A CA    1 
ATOM   3954  C  C     . MET A 1 494 ? 143.829 142.057 86.121  1.00 21.79 ?  494 MET A C     1 
ATOM   3955  O  O     . MET A 1 494 ? 143.611 143.275 86.126  1.00 24.82 ?  494 MET A O     1 
ATOM   3956  C  CB    . MET A 1 494 ? 143.957 140.931 83.888  1.00 17.94 ?  494 MET A CB    1 
ATOM   3957  C  CG    . MET A 1 494 ? 144.733 140.093 82.896  1.00 22.98 ?  494 MET A CG    1 
ATOM   3958  S  SD    . MET A 1 494 ? 143.924 139.952 81.292  1.00 39.60 ?  494 MET A SD    1 
ATOM   3959  C  CE    . MET A 1 494 ? 142.898 141.418 81.289  1.00 24.17 ?  494 MET A CE    1 
ATOM   3960  N  N     . VAL A 1 495 ? 143.258 141.228 86.997  1.00 19.25 ?  495 VAL A N     1 
ATOM   3961  C  CA    . VAL A 1 495 ? 142.388 141.746 88.050  1.00 14.86 ?  495 VAL A CA    1 
ATOM   3962  C  C     . VAL A 1 495 ? 143.163 142.691 88.959  1.00 21.00 ?  495 VAL A C     1 
ATOM   3963  O  O     . VAL A 1 495 ? 142.691 143.781 89.294  1.00 32.06 ?  495 VAL A O     1 
ATOM   3964  C  CB    . VAL A 1 495 ? 141.754 140.591 88.846  1.00 19.73 ?  495 VAL A CB    1 
ATOM   3965  C  CG1   . VAL A 1 495 ? 141.091 141.117 90.109  1.00 13.65 ?  495 VAL A CG1   1 
ATOM   3966  C  CG2   . VAL A 1 495 ? 140.741 139.853 87.992  1.00 14.21 ?  495 VAL A CG2   1 
ATOM   3967  N  N     . ASN A 1 496 ? 144.372 142.290 89.361  1.00 18.39 ?  496 ASN A N     1 
ATOM   3968  C  CA    . ASN A 1 496 ? 145.208 143.152 90.189  1.00 11.72 ?  496 ASN A CA    1 
ATOM   3969  C  C     . ASN A 1 496 ? 145.583 144.431 89.453  1.00 16.27 ?  496 ASN A C     1 
ATOM   3970  O  O     . ASN A 1 496 ? 145.570 145.518 90.040  1.00 26.76 ?  496 ASN A O     1 
ATOM   3971  C  CB    . ASN A 1 496 ? 146.464 142.396 90.624  1.00 17.45 ?  496 ASN A CB    1 
ATOM   3972  C  CG    . ASN A 1 496 ? 147.134 143.025 91.826  1.00 18.49 ?  496 ASN A CG    1 
ATOM   3973  O  OD1   . ASN A 1 496 ? 146.480 143.647 92.660  1.00 24.08 ?  496 ASN A OD1   1 
ATOM   3974  N  ND2   . ASN A 1 496 ? 148.446 142.865 91.920  1.00 18.71 ?  496 ASN A ND2   1 
ATOM   3975  N  N     . PHE A 1 497 ? 145.915 144.322 88.165  1.00 18.94 ?  497 PHE A N     1 
ATOM   3976  C  CA    . PHE A 1 497 ? 146.289 145.494 87.382  1.00 14.12 ?  497 PHE A CA    1 
ATOM   3977  C  C     . PHE A 1 497 ? 145.151 146.501 87.332  1.00 19.38 ?  497 PHE A C     1 
ATOM   3978  O  O     . PHE A 1 497 ? 145.345 147.693 87.599  1.00 24.23 ?  497 PHE A O     1 
ATOM   3979  C  CB    . PHE A 1 497 ? 146.694 145.063 85.970  1.00 17.00 ?  497 PHE A CB    1 
ATOM   3980  C  CG    . PHE A 1 497 ? 147.097 146.200 85.073  1.00 20.91 ?  497 PHE A CG    1 
ATOM   3981  C  CD1   . PHE A 1 497 ? 146.155 146.859 84.299  1.00 20.09 ?  497 PHE A CD1   1 
ATOM   3982  C  CD2   . PHE A 1 497 ? 148.419 146.599 84.989  1.00 25.45 ?  497 PHE A CD2   1 
ATOM   3983  C  CE1   . PHE A 1 497 ? 146.523 147.901 83.474  1.00 22.74 ?  497 PHE A CE1   1 
ATOM   3984  C  CE2   . PHE A 1 497 ? 148.792 147.642 84.163  1.00 23.32 ?  497 PHE A CE2   1 
ATOM   3985  C  CZ    . PHE A 1 497 ? 147.842 148.292 83.404  1.00 22.22 ?  497 PHE A CZ    1 
ATOM   3986  N  N     . TYR A 1 498 ? 143.945 146.037 87.009  1.00 25.25 ?  498 TYR A N     1 
ATOM   3987  C  CA    . TYR A 1 498 ? 142.826 146.961 86.877  1.00 18.22 ?  498 TYR A CA    1 
ATOM   3988  C  C     . TYR A 1 498 ? 142.331 147.444 88.234  1.00 23.26 ?  498 TYR A C     1 
ATOM   3989  O  O     . TYR A 1 498 ? 141.838 148.570 88.339  1.00 29.58 ?  498 TYR A O     1 
ATOM   3990  C  CB    . TYR A 1 498 ? 141.703 146.310 86.072  1.00 19.42 ?  498 TYR A CB    1 
ATOM   3991  C  CG    . TYR A 1 498 ? 142.082 146.112 84.624  1.00 22.71 ?  498 TYR A CG    1 
ATOM   3992  C  CD1   . TYR A 1 498 ? 142.502 147.185 83.848  1.00 23.96 ?  498 TYR A CD1   1 
ATOM   3993  C  CD2   . TYR A 1 498 ? 142.045 144.855 84.039  1.00 23.81 ?  498 TYR A CD2   1 
ATOM   3994  C  CE1   . TYR A 1 498 ? 142.861 147.012 82.527  1.00 19.02 ?  498 TYR A CE1   1 
ATOM   3995  C  CE2   . TYR A 1 498 ? 142.402 144.673 82.719  1.00 26.18 ?  498 TYR A CE2   1 
ATOM   3996  C  CZ    . TYR A 1 498 ? 142.808 145.755 81.967  1.00 27.69 ?  498 TYR A CZ    1 
ATOM   3997  O  OH    . TYR A 1 498 ? 143.164 145.578 80.650  1.00 33.10 ?  498 TYR A OH    1 
ATOM   3998  N  N     . SER A 1 499 ? 142.489 146.638 89.286  1.00 21.40 ?  499 SER A N     1 
ATOM   3999  C  CA    . SER A 1 499 ? 142.152 147.101 90.627  1.00 7.93  ?  499 SER A CA    1 
ATOM   4000  C  C     . SER A 1 499 ? 143.094 148.212 91.071  1.00 13.95 ?  499 SER A C     1 
ATOM   4001  O  O     . SER A 1 499 ? 142.656 149.228 91.623  1.00 20.78 ?  499 SER A O     1 
ATOM   4002  C  CB    . SER A 1 499 ? 142.192 145.929 91.607  1.00 10.95 ?  499 SER A CB    1 
ATOM   4003  O  OG    . SER A 1 499 ? 141.444 146.212 92.774  1.00 23.91 ?  499 SER A OG    1 
ATOM   4004  N  N     . ILE A 1 500 ? 144.396 148.042 90.825  1.00 13.96 ?  500 ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 500 ? 145.360 149.088 91.149  1.00 17.91 ?  500 ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 500 ? 145.100 150.330 90.310  1.00 18.43 ?  500 ILE A C     1 
ATOM   4007  O  O     . ILE A 1 500 ? 145.184 151.459 90.805  1.00 27.23 ?  500 ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 500 ? 146.798 148.568 90.959  1.00 20.89 ?  500 ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 500 ? 147.123 147.497 91.996  1.00 17.96 ?  500 ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 500 ? 147.796 149.702 91.069  1.00 14.38 ?  500 ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 500 ? 148.306 146.638 91.626  1.00 17.65 ?  500 ILE A CD1   1 
ATOM   4012  N  N     . GLN A 1 501 ? 144.784 150.143 89.027  1.00 21.74 ?  501 GLN A N     1 
ATOM   4013  C  CA    . GLN A 1 501 ? 144.498 151.281 88.162  1.00 21.17 ?  501 GLN A CA    1 
ATOM   4014  C  C     . GLN A 1 501 ? 143.272 152.045 88.641  1.00 23.95 ?  501 GLN A C     1 
ATOM   4015  O  O     . GLN A 1 501 ? 143.279 153.278 88.676  1.00 33.02 ?  501 GLN A O     1 
ATOM   4016  C  CB    . GLN A 1 501 ? 144.311 150.807 86.721  1.00 26.40 ?  501 GLN A CB    1 
ATOM   4017  C  CG    . GLN A 1 501 ? 144.755 151.814 85.676  1.00 26.12 ?  501 GLN A CG    1 
ATOM   4018  C  CD    . GLN A 1 501 ? 144.536 151.318 84.264  1.00 29.50 ?  501 GLN A CD    1 
ATOM   4019  O  OE1   . GLN A 1 501 ? 143.439 150.885 83.909  1.00 30.35 ?  501 GLN A OE1   1 
ATOM   4020  N  NE2   . GLN A 1 501 ? 145.580 151.376 83.446  1.00 31.13 ?  501 GLN A NE2   1 
ATOM   4021  N  N     . ARG A 1 502 ? 142.212 151.330 89.025  1.00 22.64 ?  502 ARG A N     1 
ATOM   4022  C  CA    . ARG A 1 502 ? 141.014 151.994 89.529  1.00 21.00 ?  502 ARG A CA    1 
ATOM   4023  C  C     . ARG A 1 502 ? 141.281 152.688 90.858  1.00 21.54 ?  502 ARG A C     1 
ATOM   4024  O  O     . ARG A 1 502 ? 140.773 153.787 91.098  1.00 25.89 ?  502 ARG A O     1 
ATOM   4025  C  CB    . ARG A 1 502 ? 139.874 150.987 89.668  1.00 19.91 ?  502 ARG A CB    1 
ATOM   4026  C  CG    . ARG A 1 502 ? 138.521 151.630 89.908  1.00 22.74 ?  502 ARG A CG    1 
ATOM   4027  C  CD    . ARG A 1 502 ? 138.213 152.671 88.848  1.00 23.43 ?  502 ARG A CD    1 
ATOM   4028  N  NE    . ARG A 1 502 ? 137.226 153.639 89.308  1.00 26.60 ?  502 ARG A NE    1 
ATOM   4029  C  CZ    . ARG A 1 502 ? 137.219 154.920 88.968  1.00 25.59 ?  502 ARG A CZ    1 
ATOM   4030  N  NH1   . ARG A 1 502 ? 138.127 155.423 88.150  1.00 29.04 1  502 ARG A NH1   1 
ATOM   4031  N  NH2   . ARG A 1 502 ? 136.275 155.716 89.460  1.00 26.36 ?  502 ARG A NH2   1 
ATOM   4032  N  N     . SER A 1 503 ? 142.068 152.062 91.737  1.00 19.21 ?  503 SER A N     1 
ATOM   4033  C  CA    . SER A 1 503 ? 142.408 152.701 93.005  1.00 20.41 ?  503 SER A CA    1 
ATOM   4034  C  C     . SER A 1 503 ? 143.193 153.986 92.776  1.00 23.19 ?  503 SER A C     1 
ATOM   4035  O  O     . SER A 1 503 ? 142.922 155.012 93.412  1.00 26.02 ?  503 SER A O     1 
ATOM   4036  C  CB    . SER A 1 503 ? 143.204 151.731 93.879  1.00 19.03 ?  503 SER A CB    1 
ATOM   4037  O  OG    . SER A 1 503 ? 143.186 152.130 95.237  1.00 23.30 ?  503 SER A OG    1 
ATOM   4038  N  N     . ALA A 1 504 ? 144.156 153.957 91.853  1.00 24.12 ?  504 ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 504 ? 144.930 155.152 91.546  1.00 21.09 ?  504 ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 504 ? 144.067 156.217 90.880  1.00 28.52 ?  504 ALA A C     1 
ATOM   4041  O  O     . ALA A 1 504 ? 144.240 157.413 91.138  1.00 37.22 ?  504 ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 504 ? 146.121 154.791 90.659  1.00 24.49 ?  504 ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 505 ? 143.129 155.803 90.027  1.00 26.33 ?  505 GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 505 ? 142.226 156.759 89.395  1.00 26.93 ?  505 GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 505 ? 141.316 157.421 90.421  1.00 29.67 ?  505 GLU A C     1 
ATOM   4046  O  O     . GLU A 1 505 ? 141.065 158.627 90.346  1.00 35.60 ?  505 GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 505 ? 141.401 156.063 88.312  1.00 26.49 ?  505 GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 505 ? 142.166 155.775 87.032  1.00 27.33 ?  505 GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 505 ? 141.589 154.605 86.260  1.00 33.62 ?  505 GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 505 ? 140.577 154.033 86.714  1.00 34.56 ?  505 GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 505 ? 142.149 154.256 85.200  1.00 35.30 -1 505 GLU A OE2   1 
ATOM   4052  N  N     . ILE A 1 506 ? 140.812 156.649 91.384  1.00 26.44 ?  506 ILE A N     1 
ATOM   4053  C  CA    . ILE A 1 506 ? 139.987 157.221 92.443  1.00 24.78 ?  506 ILE A CA    1 
ATOM   4054  C  C     . ILE A 1 506 ? 140.810 158.165 93.310  1.00 28.62 ?  506 ILE A C     1 
ATOM   4055  O  O     . ILE A 1 506 ? 140.334 159.231 93.715  1.00 34.21 ?  506 ILE A O     1 
ATOM   4056  C  CB    . ILE A 1 506 ? 139.332 156.102 93.275  1.00 23.01 ?  506 ILE A CB    1 
ATOM   4057  C  CG1   . ILE A 1 506 ? 138.339 155.313 92.421  1.00 26.55 ?  506 ILE A CG1   1 
ATOM   4058  C  CG2   . ILE A 1 506 ? 138.631 156.677 94.494  1.00 23.61 ?  506 ILE A CG2   1 
ATOM   4059  C  CD1   . ILE A 1 506 ? 137.915 153.999 93.036  1.00 21.55 ?  506 ILE A CD1   1 
ATOM   4060  N  N     . ALA A 1 507 ? 142.059 157.791 93.605  1.00 30.57 ?  507 ALA A N     1 
ATOM   4061  C  CA    . ALA A 1 507 ? 142.933 158.676 94.370  1.00 28.17 ?  507 ALA A CA    1 
ATOM   4062  C  C     . ALA A 1 507 ? 143.182 159.984 93.627  1.00 30.16 ?  507 ALA A C     1 
ATOM   4063  O  O     . ALA A 1 507 ? 143.188 161.060 94.236  1.00 33.75 ?  507 ALA A O     1 
ATOM   4064  C  CB    . ALA A 1 507 ? 144.255 157.973 94.673  1.00 24.00 ?  507 ALA A CB    1 
ATOM   4065  N  N     . LYS A 1 508 ? 143.395 159.909 92.313  1.00 34.66 ?  508 LYS A N     1 
ATOM   4066  C  CA    . LYS A 1 508 ? 143.601 161.114 91.517  1.00 32.34 ?  508 LYS A CA    1 
ATOM   4067  C  C     . LYS A 1 508 ? 142.341 161.971 91.466  1.00 37.17 ?  508 LYS A C     1 
ATOM   4068  O  O     . LYS A 1 508 ? 142.415 163.201 91.575  1.00 43.61 ?  508 LYS A O     1 
ATOM   4069  C  CB    . LYS A 1 508 ? 144.051 160.730 90.107  1.00 34.75 ?  508 LYS A CB    1 
ATOM   4070  C  CG    . LYS A 1 508 ? 144.045 161.875 89.111  1.00 36.97 ?  508 LYS A CG    1 
ATOM   4071  C  CD    . LYS A 1 508 ? 144.218 161.365 87.691  1.00 38.51 ?  508 LYS A CD    1 
ATOM   4072  C  CE    . LYS A 1 508 ? 144.254 162.509 86.694  1.00 37.16 ?  508 LYS A CE    1 
ATOM   4073  N  NZ    . LYS A 1 508 ? 145.120 162.197 85.523  1.00 40.86 1  508 LYS A NZ    1 
ATOM   4074  N  N     . GLU A 1 509 ? 141.176 161.341 91.296  1.00 35.71 ?  509 GLU A N     1 
ATOM   4075  C  CA    . GLU A 1 509 ? 139.927 162.090 91.205  1.00 34.30 ?  509 GLU A CA    1 
ATOM   4076  C  C     . GLU A 1 509 ? 139.603 162.786 92.521  1.00 37.22 ?  509 GLU A C     1 
ATOM   4077  O  O     . GLU A 1 509 ? 139.303 163.986 92.542  1.00 41.97 ?  509 GLU A O     1 
ATOM   4078  C  CB    . GLU A 1 509 ? 138.786 161.155 90.799  1.00 33.13 ?  509 GLU A CB    1 
ATOM   4079  C  CG    . GLU A 1 509 ? 138.828 160.719 89.344  1.00 40.38 ?  509 GLU A CG    1 
ATOM   4080  C  CD    . GLU A 1 509 ? 138.187 159.361 89.126  1.00 43.69 ?  509 GLU A CD    1 
ATOM   4081  O  OE1   . GLU A 1 509 ? 137.543 158.847 90.065  1.00 42.01 ?  509 GLU A OE1   1 
ATOM   4082  O  OE2   . GLU A 1 509 ? 138.330 158.807 88.016  1.00 40.06 -1 509 GLU A OE2   1 
ATOM   4083  N  N     . LYS A 1 510 ? 139.658 162.050 93.628  1.00 33.73 ?  510 LYS A N     1 
ATOM   4084  C  CA    . LYS A 1 510 ? 139.359 162.617 94.935  1.00 30.44 ?  510 LYS A CA    1 
ATOM   4085  C  C     . LYS A 1 510 ? 140.529 163.385 95.533  1.00 32.19 ?  510 LYS A C     1 
ATOM   4086  O  O     . LYS A 1 510 ? 140.336 164.106 96.517  1.00 38.71 ?  510 LYS A O     1 
ATOM   4087  C  CB    . LYS A 1 510 ? 138.922 161.511 95.898  1.00 29.73 ?  510 LYS A CB    1 
ATOM   4088  C  CG    . LYS A 1 510 ? 137.764 160.673 95.384  1.00 29.83 ?  510 LYS A CG    1 
ATOM   4089  C  CD    . LYS A 1 510 ? 137.295 159.674 96.425  1.00 30.57 ?  510 LYS A CD    1 
ATOM   4090  C  CE    . LYS A 1 510 ? 135.800 159.427 96.319  1.00 35.93 ?  510 LYS A CE    1 
ATOM   4091  N  NZ    . LYS A 1 510 ? 135.468 157.977 96.377  1.00 35.29 1  510 LYS A NZ    1 
ATOM   4092  N  N     . GLY A 1 511 ? 141.728 163.249 94.970  1.00 31.46 ?  511 GLY A N     1 
ATOM   4093  C  CA    . GLY A 1 511 ? 142.880 163.956 95.487  1.00 28.76 ?  511 GLY A CA    1 
ATOM   4094  C  C     . GLY A 1 511 ? 143.429 163.422 96.787  1.00 36.85 ?  511 GLY A C     1 
ATOM   4095  O  O     . GLY A 1 511 ? 144.258 164.089 97.412  1.00 40.96 ?  511 GLY A O     1 
ATOM   4096  N  N     . GLU A 1 512 ? 142.994 162.240 97.218  1.00 29.37 ?  512 GLU A N     1 
ATOM   4097  C  CA    . GLU A 1 512 ? 143.426 161.674 98.486  1.00 27.23 ?  512 GLU A CA    1 
ATOM   4098  C  C     . GLU A 1 512 ? 143.727 160.193 98.316  1.00 29.79 ?  512 GLU A C     1 
ATOM   4099  O  O     . GLU A 1 512 ? 143.069 159.492 97.543  1.00 29.31 ?  512 GLU A O     1 
ATOM   4100  C  CB    . GLU A 1 512 ? 142.365 161.867 99.578  1.00 29.38 ?  512 GLU A CB    1 
ATOM   4101  C  CG    . GLU A 1 512 ? 140.996 161.316 99.216  1.00 31.17 ?  512 GLU A CG    1 
ATOM   4102  C  CD    . GLU A 1 512 ? 140.154 161.000 100.434 1.00 33.54 ?  512 GLU A CD    1 
ATOM   4103  O  OE1   . GLU A 1 512 ? 140.735 160.670 101.489 1.00 31.95 ?  512 GLU A OE1   1 
ATOM   4104  O  OE2   . GLU A 1 512 ? 138.912 161.081 100.338 1.00 30.20 -1 512 GLU A OE2   1 
ATOM   4105  N  N     . THR A 1 513 ? 144.733 159.728 99.046  1.00 31.54 ?  513 THR A N     1 
ATOM   4106  C  CA    . THR A 1 513 ? 145.091 158.323 99.135  1.00 24.41 ?  513 THR A CA    1 
ATOM   4107  C  C     . THR A 1 513 ? 144.662 157.790 100.500 1.00 26.94 ?  513 THR A C     1 
ATOM   4108  O  O     . THR A 1 513 ? 144.039 158.501 101.298 1.00 31.85 ?  513 THR A O     1 
ATOM   4109  C  CB    . THR A 1 513 ? 146.591 158.145 98.899  1.00 26.12 ?  513 THR A CB    1 
ATOM   4110  O  OG1   . THR A 1 513 ? 147.314 158.616 100.042 1.00 35.94 ?  513 THR A OG1   1 
ATOM   4111  C  CG2   . THR A 1 513 ? 147.030 158.931 97.675  1.00 25.68 ?  513 THR A CG2   1 
ATOM   4112  N  N     . PHE A 1 514 ? 144.991 156.533 100.775 1.00 23.23 ?  514 PHE A N     1 
ATOM   4113  C  CA    . PHE A 1 514 ? 144.733 155.996 102.099 1.00 23.53 ?  514 PHE A CA    1 
ATOM   4114  C  C     . PHE A 1 514 ? 145.802 156.478 103.071 1.00 19.94 ?  514 PHE A C     1 
ATOM   4115  O  O     . PHE A 1 514 ? 146.914 156.836 102.674 1.00 28.21 ?  514 PHE A O     1 
ATOM   4116  C  CB    . PHE A 1 514 ? 144.663 154.467 102.079 1.00 16.82 ?  514 PHE A CB    1 
ATOM   4117  C  CG    . PHE A 1 514 ? 145.954 153.789 101.711 1.00 18.74 ?  514 PHE A CG    1 
ATOM   4118  C  CD1   . PHE A 1 514 ? 146.268 153.538 100.388 1.00 18.81 ?  514 PHE A CD1   1 
ATOM   4119  C  CD2   . PHE A 1 514 ? 146.836 153.369 102.692 1.00 19.05 ?  514 PHE A CD2   1 
ATOM   4120  C  CE1   . PHE A 1 514 ? 147.444 152.900 100.050 1.00 12.80 ?  514 PHE A CE1   1 
ATOM   4121  C  CE2   . PHE A 1 514 ? 148.013 152.734 102.359 1.00 16.19 ?  514 PHE A CE2   1 
ATOM   4122  C  CZ    . PHE A 1 514 ? 148.318 152.499 101.036 1.00 15.17 ?  514 PHE A CZ    1 
ATOM   4123  N  N     . ASP A 1 515 ? 145.445 156.508 104.352 1.00 22.86 ?  515 ASP A N     1 
ATOM   4124  C  CA    . ASP A 1 515 ? 146.352 157.032 105.363 1.00 26.17 ?  515 ASP A CA    1 
ATOM   4125  C  C     . ASP A 1 515 ? 147.637 156.215 105.409 1.00 27.64 ?  515 ASP A C     1 
ATOM   4126  O  O     . ASP A 1 515 ? 147.613 154.983 105.338 1.00 32.62 ?  515 ASP A O     1 
ATOM   4127  C  CB    . ASP A 1 515 ? 145.677 157.037 106.733 1.00 27.91 ?  515 ASP A CB    1 
ATOM   4128  C  CG    . ASP A 1 515 ? 144.675 158.164 106.882 1.00 30.13 ?  515 ASP A CG    1 
ATOM   4129  O  OD1   . ASP A 1 515 ? 144.215 158.693 105.849 1.00 30.97 ?  515 ASP A OD1   1 
ATOM   4130  O  OD2   . ASP A 1 515 ? 144.348 158.525 108.033 1.00 31.63 -1 515 ASP A OD2   1 
ATOM   4131  N  N     . GLN A 1 516 ? 148.763 156.920 105.524 1.00 29.29 ?  516 GLN A N     1 
ATOM   4132  C  CA    . GLN A 1 516 ? 150.095 156.316 105.531 1.00 27.02 ?  516 GLN A CA    1 
ATOM   4133  C  C     . GLN A 1 516 ? 150.380 155.555 104.240 1.00 24.74 ?  516 GLN A C     1 
ATOM   4134  O  O     . GLN A 1 516 ? 151.044 154.517 104.254 1.00 31.63 ?  516 GLN A O     1 
ATOM   4135  C  CB    . GLN A 1 516 ? 150.287 155.399 106.743 1.00 23.58 ?  516 GLN A CB    1 
ATOM   4136  C  CG    . GLN A 1 516 ? 150.096 156.083 108.084 1.00 27.32 ?  516 GLN A CG    1 
ATOM   4137  C  CD    . GLN A 1 516 ? 150.117 155.103 109.241 1.00 28.96 ?  516 GLN A CD    1 
ATOM   4138  O  OE1   . GLN A 1 516 ? 151.173 154.601 109.624 1.00 24.45 ?  516 GLN A OE1   1 
ATOM   4139  N  NE2   . GLN A 1 516 ? 148.947 154.825 109.802 1.00 30.70 ?  516 GLN A NE2   1 
ATOM   4140  N  N     . TYR A 1 517 ? 149.877 156.057 103.110 1.00 21.14 ?  517 TYR A N     1 
ATOM   4141  C  CA    . TYR A 1 517 ? 150.201 155.440 101.828 1.00 19.39 ?  517 TYR A CA    1 
ATOM   4142  C  C     . TYR A 1 517 ? 151.654 155.678 101.442 1.00 29.46 ?  517 TYR A C     1 
ATOM   4143  O  O     . TYR A 1 517 ? 152.268 154.827 100.790 1.00 36.04 ?  517 TYR A O     1 
ATOM   4144  C  CB    . TYR A 1 517 ? 149.273 155.963 100.732 1.00 18.68 ?  517 TYR A CB    1 
ATOM   4145  C  CG    . TYR A 1 517 ? 149.900 155.954 99.354  1.00 27.03 ?  517 TYR A CG    1 
ATOM   4146  C  CD1   . TYR A 1 517 ? 149.949 154.789 98.601  1.00 23.94 ?  517 TYR A CD1   1 
ATOM   4147  C  CD2   . TYR A 1 517 ? 150.448 157.109 98.810  1.00 29.69 ?  517 TYR A CD2   1 
ATOM   4148  C  CE1   . TYR A 1 517 ? 150.525 154.773 97.347  1.00 27.36 ?  517 TYR A CE1   1 
ATOM   4149  C  CE2   . TYR A 1 517 ? 151.029 157.102 97.560  1.00 25.86 ?  517 TYR A CE2   1 
ATOM   4150  C  CZ    . TYR A 1 517 ? 151.065 155.932 96.833  1.00 29.69 ?  517 TYR A CZ    1 
ATOM   4151  O  OH    . TYR A 1 517 ? 151.638 155.923 95.584  1.00 34.33 ?  517 TYR A OH    1 
ATOM   4152  N  N     . GLU A 1 518 ? 152.215 156.826 101.832 1.00 31.48 ?  518 GLU A N     1 
ATOM   4153  C  CA    . GLU A 1 518 ? 153.560 157.191 101.399 1.00 33.30 ?  518 GLU A CA    1 
ATOM   4154  C  C     . GLU A 1 518 ? 154.598 156.172 101.849 1.00 37.36 ?  518 GLU A C     1 
ATOM   4155  O  O     . GLU A 1 518 ? 155.616 155.985 101.172 1.00 39.66 ?  518 GLU A O     1 
ATOM   4156  C  CB    . GLU A 1 518 ? 153.930 158.586 101.919 1.00 32.58 ?  518 GLU A CB    1 
ATOM   4157  C  CG    . GLU A 1 518 ? 152.938 159.710 101.595 1.00 34.94 ?  518 GLU A CG    1 
ATOM   4158  C  CD    . GLU A 1 518 ? 151.612 159.588 102.328 1.00 42.69 ?  518 GLU A CD    1 
ATOM   4159  O  OE1   . GLU A 1 518 ? 150.587 160.059 101.790 1.00 41.60 ?  518 GLU A OE1   1 
ATOM   4160  O  OE2   . GLU A 1 518 ? 151.596 159.019 103.440 1.00 40.31 -1 518 GLU A OE2   1 
ATOM   4161  N  N     . GLY A 1 519 ? 154.366 155.508 102.979 1.00 26.93 ?  519 GLY A N     1 
ATOM   4162  C  CA    . GLY A 1 519 ? 155.269 154.466 103.422 1.00 23.56 ?  519 GLY A CA    1 
ATOM   4163  C  C     . GLY A 1 519 ? 155.032 153.105 102.808 1.00 23.79 ?  519 GLY A C     1 
ATOM   4164  O  O     . GLY A 1 519 ? 155.831 152.192 103.034 1.00 28.85 ?  519 GLY A O     1 
ATOM   4165  N  N     . SER A 1 520 ? 153.960 152.949 102.035 1.00 22.77 ?  520 SER A N     1 
ATOM   4166  C  CA    . SER A 1 520 ? 153.624 151.655 101.467 1.00 24.37 ?  520 SER A CA    1 
ATOM   4167  C  C     . SER A 1 520 ? 154.531 151.323 100.286 1.00 22.49 ?  520 SER A C     1 
ATOM   4168  O  O     . SER A 1 520 ? 155.187 152.190 99.703  1.00 31.54 ?  520 SER A O     1 
ATOM   4169  C  CB    . SER A 1 520 ? 152.160 151.626 101.025 1.00 19.01 ?  520 SER A CB    1 
ATOM   4170  O  OG    . SER A 1 520 ? 151.920 152.568 99.995  1.00 21.50 ?  520 SER A OG    1 
ATOM   4171  N  N     . THR A 1 521 ? 154.564 150.034 99.940  1.00 20.34 ?  521 THR A N     1 
ATOM   4172  C  CA    . THR A 1 521 ? 155.348 149.589 98.795  1.00 21.16 ?  521 THR A CA    1 
ATOM   4173  C  C     . THR A 1 521 ? 154.763 150.072 97.474  1.00 23.54 ?  521 THR A C     1 
ATOM   4174  O  O     . THR A 1 521 ? 155.475 150.081 96.465  1.00 24.52 ?  521 THR A O     1 
ATOM   4175  C  CB    . THR A 1 521 ? 155.460 148.065 98.790  1.00 22.76 ?  521 THR A CB    1 
ATOM   4176  O  OG1   . THR A 1 521 ? 154.187 147.490 98.476  1.00 23.73 ?  521 THR A OG1   1 
ATOM   4177  C  CG2   . THR A 1 521 ? 155.914 147.562 100.151 1.00 19.65 ?  521 THR A CG2   1 
ATOM   4178  N  N     . TYR A 1 522 ? 153.485 150.458 97.455  1.00 26.55 ?  522 TYR A N     1 
ATOM   4179  C  CA    . TYR A 1 522 ? 152.927 151.105 96.273  1.00 18.97 ?  522 TYR A CA    1 
ATOM   4180  C  C     . TYR A 1 522 ? 153.626 152.431 96.005  1.00 23.87 ?  522 TYR A C     1 
ATOM   4181  O  O     . TYR A 1 522 ? 153.985 152.743 94.864  1.00 25.62 ?  522 TYR A O     1 
ATOM   4182  C  CB    . TYR A 1 522 ? 151.424 151.326 96.447  1.00 17.28 ?  522 TYR A CB    1 
ATOM   4183  C  CG    . TYR A 1 522 ? 150.612 150.066 96.632  1.00 17.83 ?  522 TYR A CG    1 
ATOM   4184  C  CD1   . TYR A 1 522 ? 150.482 149.141 95.606  1.00 19.28 ?  522 TYR A CD1   1 
ATOM   4185  C  CD2   . TYR A 1 522 ? 149.955 149.813 97.829  1.00 21.38 ?  522 TYR A CD2   1 
ATOM   4186  C  CE1   . TYR A 1 522 ? 149.734 147.993 95.771  1.00 18.02 ?  522 TYR A CE1   1 
ATOM   4187  C  CE2   . TYR A 1 522 ? 149.202 148.669 98.001  1.00 18.03 ?  522 TYR A CE2   1 
ATOM   4188  C  CZ    . TYR A 1 522 ? 149.098 147.762 96.971  1.00 19.92 ?  522 TYR A CZ    1 
ATOM   4189  O  OH    . TYR A 1 522 ? 148.351 146.621 97.141  1.00 25.93 ?  522 TYR A OH    1 
ATOM   4190  N  N     . ALA A 1 523 ? 153.829 153.228 97.058  1.00 25.50 ?  523 ALA A N     1 
ATOM   4191  C  CA    . ALA A 1 523 ? 154.468 154.530 96.897  1.00 26.43 ?  523 ALA A CA    1 
ATOM   4192  C  C     . ALA A 1 523 ? 155.927 154.386 96.488  1.00 31.21 ?  523 ALA A C     1 
ATOM   4193  O  O     . ALA A 1 523 ? 156.418 155.140 95.640  1.00 32.89 ?  523 ALA A O     1 
ATOM   4194  C  CB    . ALA A 1 523 ? 154.347 155.333 98.190  1.00 25.19 ?  523 ALA A CB    1 
ATOM   4195  N  N     . THR A 1 524 ? 156.638 153.426 97.079  1.00 24.86 ?  524 THR A N     1 
ATOM   4196  C  CA    . THR A 1 524 ? 158.040 153.209 96.755  1.00 24.67 ?  524 THR A CA    1 
ATOM   4197  C  C     . THR A 1 524 ? 158.237 152.432 95.461  1.00 30.74 ?  524 THR A C     1 
ATOM   4198  O  O     . THR A 1 524 ? 159.373 152.340 94.982  1.00 36.80 ?  524 THR A O     1 
ATOM   4199  C  CB    . THR A 1 524 ? 158.739 152.472 97.901  1.00 28.88 ?  524 THR A CB    1 
ATOM   4200  O  OG1   . THR A 1 524 ? 158.351 151.093 97.894  1.00 30.78 ?  524 THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1 524 ? 158.362 153.090 99.237  1.00 26.81 ?  524 THR A CG2   1 
ATOM   4202  N  N     . GLY A 1 525 ? 157.173 151.873 94.888  1.00 26.63 ?  525 GLY A N     1 
ATOM   4203  C  CA    . GLY A 1 525 ? 157.273 151.113 93.663  1.00 24.39 ?  525 GLY A CA    1 
ATOM   4204  C  C     . GLY A 1 525 ? 157.753 149.690 93.826  1.00 29.59 ?  525 GLY A C     1 
ATOM   4205  O  O     . GLY A 1 525 ? 157.887 148.981 92.819  1.00 32.79 ?  525 GLY A O     1 
ATOM   4206  N  N     . GLU A 1 526 ? 158.020 149.247 95.056  1.00 29.06 ?  526 GLU A N     1 
ATOM   4207  C  CA    . GLU A 1 526 ? 158.477 147.878 95.273  1.00 29.80 ?  526 GLU A CA    1 
ATOM   4208  C  C     . GLU A 1 526 ? 157.398 146.871 94.896  1.00 31.92 ?  526 GLU A C     1 
ATOM   4209  O  O     . GLU A 1 526 ? 157.698 145.804 94.345  1.00 37.13 ?  526 GLU A O     1 
ATOM   4210  C  CB    . GLU A 1 526 ? 158.903 147.698 96.730  1.00 30.68 ?  526 GLU A CB    1 
ATOM   4211  C  CG    . GLU A 1 526 ? 159.046 146.253 97.172  1.00 31.72 ?  526 GLU A CG    1 
ATOM   4212  C  CD    . GLU A 1 526 ? 159.042 146.103 98.681  1.00 36.24 ?  526 GLU A CD    1 
ATOM   4213  O  OE1   . GLU A 1 526 ? 159.238 147.118 99.380  1.00 35.08 ?  526 GLU A OE1   1 
ATOM   4214  O  OE2   . GLU A 1 526 ? 158.839 144.971 99.168  1.00 34.53 -1 526 GLU A OE2   1 
ATOM   4215  N  N     . TYR A 1 527 ? 156.133 147.200 95.176  1.00 31.75 ?  527 TYR A N     1 
ATOM   4216  C  CA    . TYR A 1 527 ? 155.029 146.289 94.887  1.00 22.45 ?  527 TYR A CA    1 
ATOM   4217  C  C     . TYR A 1 527 ? 155.016 145.870 93.423  1.00 24.31 ?  527 TYR A C     1 
ATOM   4218  O  O     . TYR A 1 527 ? 154.682 144.725 93.098  1.00 30.71 ?  527 TYR A O     1 
ATOM   4219  C  CB    . TYR A 1 527 ? 153.701 146.950 95.263  1.00 18.46 ?  527 TYR A CB    1 
ATOM   4220  C  CG    . TYR A 1 527 ? 152.493 146.060 95.079  1.00 25.45 ?  527 TYR A CG    1 
ATOM   4221  C  CD1   . TYR A 1 527 ? 151.830 145.995 93.860  1.00 23.33 ?  527 TYR A CD1   1 
ATOM   4222  C  CD2   . TYR A 1 527 ? 152.013 145.289 96.127  1.00 24.14 ?  527 TYR A CD2   1 
ATOM   4223  C  CE1   . TYR A 1 527 ? 150.730 145.182 93.691  1.00 20.19 ?  527 TYR A CE1   1 
ATOM   4224  C  CE2   . TYR A 1 527 ? 150.912 144.476 95.966  1.00 22.64 ?  527 TYR A CE2   1 
ATOM   4225  C  CZ    . TYR A 1 527 ? 150.274 144.427 94.747  1.00 23.29 ?  527 TYR A CZ    1 
ATOM   4226  O  OH    . TYR A 1 527 ? 149.175 143.616 94.585  1.00 29.93 ?  527 TYR A OH    1 
ATOM   4227  N  N     . PHE A 1 528 ? 155.380 146.782 92.527  1.00 26.54 ?  528 PHE A N     1 
ATOM   4228  C  CA    . PHE A 1 528 ? 155.340 146.531 91.094  1.00 27.56 ?  528 PHE A CA    1 
ATOM   4229  C  C     . PHE A 1 528 ? 156.589 145.836 90.571  1.00 31.65 ?  528 PHE A C     1 
ATOM   4230  O  O     . PHE A 1 528 ? 156.668 145.574 89.367  1.00 37.05 ?  528 PHE A O     1 
ATOM   4231  C  CB    . PHE A 1 528 ? 155.133 147.847 90.339  1.00 28.67 ?  528 PHE A CB    1 
ATOM   4232  C  CG    . PHE A 1 528 ? 153.914 148.607 90.772  1.00 31.81 ?  528 PHE A CG    1 
ATOM   4233  C  CD1   . PHE A 1 528 ? 152.690 148.379 90.166  1.00 27.01 ?  528 PHE A CD1   1 
ATOM   4234  C  CD2   . PHE A 1 528 ? 153.988 149.547 91.786  1.00 29.35 ?  528 PHE A CD2   1 
ATOM   4235  C  CE1   . PHE A 1 528 ? 151.565 149.074 90.561  1.00 27.38 ?  528 PHE A CE1   1 
ATOM   4236  C  CE2   . PHE A 1 528 ? 152.867 150.244 92.187  1.00 29.22 ?  528 PHE A CE2   1 
ATOM   4237  C  CZ    . PHE A 1 528 ? 151.654 150.006 91.573  1.00 28.09 ?  528 PHE A CZ    1 
ATOM   4238  N  N     . ASP A 1 529 ? 157.557 145.531 91.441  1.00 30.61 ?  529 ASP A N     1 
ATOM   4239  C  CA    . ASP A 1 529 ? 158.815 144.936 90.996  1.00 29.55 ?  529 ASP A CA    1 
ATOM   4240  C  C     . ASP A 1 529 ? 158.572 143.682 90.163  1.00 33.50 ?  529 ASP A C     1 
ATOM   4241  O  O     . ASP A 1 529 ? 158.910 143.631 88.974  1.00 35.83 ?  529 ASP A O     1 
ATOM   4242  C  CB    . ASP A 1 529 ? 159.693 144.618 92.208  1.00 32.37 ?  529 ASP A CB    1 
ATOM   4243  C  CG    . ASP A 1 529 ? 160.425 145.837 92.731  1.00 39.19 ?  529 ASP A CG    1 
ATOM   4244  O  OD1   . ASP A 1 529 ? 160.329 146.908 92.096  1.00 36.61 ?  529 ASP A OD1   1 
ATOM   4245  O  OD2   . ASP A 1 529 ? 161.096 145.724 93.779  1.00 39.06 -1 529 ASP A OD2   1 
ATOM   4246  N  N     . LYS A 1 530 ? 157.940 142.671 90.765  1.00 34.90 ?  530 LYS A N     1 
ATOM   4247  C  CA    . LYS A 1 530 ? 157.662 141.434 90.046  1.00 32.53 ?  530 LYS A CA    1 
ATOM   4248  C  C     . LYS A 1 530 ? 156.773 141.663 88.832  1.00 32.70 ?  530 LYS A C     1 
ATOM   4249  O  O     . LYS A 1 530 ? 156.742 140.819 87.931  1.00 34.96 ?  530 LYS A O     1 
ATOM   4250  C  CB    . LYS A 1 530 ? 157.008 140.416 90.980  1.00 31.49 ?  530 LYS A CB    1 
ATOM   4251  C  CG    . LYS A 1 530 ? 155.494 140.376 90.878  1.00 29.76 ?  530 LYS A CG    1 
ATOM   4252  C  CD    . LYS A 1 530 ? 154.880 139.567 91.997  1.00 31.93 ?  530 LYS A CD    1 
ATOM   4253  C  CE    . LYS A 1 530 ? 153.392 139.400 91.782  1.00 27.82 ?  530 LYS A CE    1 
ATOM   4254  N  NZ    . LYS A 1 530 ? 152.622 139.769 92.999  1.00 33.29 1  530 LYS A NZ    1 
ATOM   4255  N  N     . TYR A 1 531 ? 156.055 142.782 88.788  1.00 30.64 ?  531 TYR A N     1 
ATOM   4256  C  CA    . TYR A 1 531 ? 155.206 143.092 87.650  1.00 28.11 ?  531 TYR A CA    1 
ATOM   4257  C  C     . TYR A 1 531 ? 155.944 143.827 86.542  1.00 26.93 ?  531 TYR A C     1 
ATOM   4258  O  O     . TYR A 1 531 ? 155.508 143.768 85.387  1.00 32.56 ?  531 TYR A O     1 
ATOM   4259  C  CB    . TYR A 1 531 ? 154.005 143.921 88.107  1.00 27.82 ?  531 TYR A CB    1 
ATOM   4260  C  CG    . TYR A 1 531 ? 152.967 143.115 88.849  1.00 28.79 ?  531 TYR A CG    1 
ATOM   4261  C  CD1   . TYR A 1 531 ? 152.402 141.984 88.278  1.00 23.74 ?  531 TYR A CD1   1 
ATOM   4262  C  CD2   . TYR A 1 531 ? 152.552 143.485 90.121  1.00 25.66 ?  531 TYR A CD2   1 
ATOM   4263  C  CE1   . TYR A 1 531 ? 151.452 141.244 88.950  1.00 29.88 ?  531 TYR A CE1   1 
ATOM   4264  C  CE2   . TYR A 1 531 ? 151.602 142.750 90.801  1.00 25.40 ?  531 TYR A CE2   1 
ATOM   4265  C  CZ    . TYR A 1 531 ? 151.056 141.631 90.211  1.00 28.75 ?  531 TYR A CZ    1 
ATOM   4266  O  OH    . TYR A 1 531 ? 150.109 140.897 90.884  1.00 26.64 ?  531 TYR A OH    1 
ATOM   4267  N  N     . VAL A 1 532 ? 157.047 144.514 86.858  1.00 36.73 ?  532 VAL A N     1 
ATOM   4268  C  CA    . VAL A 1 532 ? 157.816 145.205 85.829  1.00 35.08 ?  532 VAL A CA    1 
ATOM   4269  C  C     . VAL A 1 532 ? 158.961 144.357 85.299  1.00 36.69 ?  532 VAL A C     1 
ATOM   4270  O  O     . VAL A 1 532 ? 159.694 144.806 84.408  1.00 41.15 ?  532 VAL A O     1 
ATOM   4271  C  CB    . VAL A 1 532 ? 158.358 146.555 86.344  1.00 35.29 ?  532 VAL A CB    1 
ATOM   4272  C  CG1   . VAL A 1 532 ? 157.216 147.444 86.808  1.00 34.97 ?  532 VAL A CG1   1 
ATOM   4273  C  CG2   . VAL A 1 532 ? 159.364 146.341 87.458  1.00 33.74 ?  532 VAL A CG2   1 
ATOM   4274  N  N     . SER A 1 533 ? 159.135 143.142 85.813  1.00 37.31 ?  533 SER A N     1 
ATOM   4275  C  CA    . SER A 1 533 ? 160.188 142.243 85.365  1.00 39.93 ?  533 SER A CA    1 
ATOM   4276  C  C     . SER A 1 533 ? 159.676 140.911 84.843  1.00 40.94 ?  533 SER A C     1 
ATOM   4277  O  O     . SER A 1 533 ? 160.301 140.338 83.947  1.00 43.31 ?  533 SER A O     1 
ATOM   4278  C  CB    . SER A 1 533 ? 161.182 141.977 86.506  1.00 41.14 ?  533 SER A CB    1 
ATOM   4279  O  OG    . SER A 1 533 ? 160.608 141.142 87.496  1.00 44.41 ?  533 SER A OG    1 
ATOM   4280  N  N     . THR A 1 534 ? 158.565 140.405 85.369  1.00 40.28 ?  534 THR A N     1 
ATOM   4281  C  CA    . THR A 1 534 ? 158.007 139.124 84.960  1.00 38.86 ?  534 THR A CA    1 
ATOM   4282  C  C     . THR A 1 534 ? 156.757 139.359 84.124  1.00 38.19 ?  534 THR A C     1 
ATOM   4283  O  O     . THR A 1 534 ? 155.857 140.097 84.539  1.00 43.56 ?  534 THR A O     1 
ATOM   4284  C  CB    . THR A 1 534 ? 157.669 138.258 86.177  1.00 39.36 ?  534 THR A CB    1 
ATOM   4285  O  OG1   . THR A 1 534 ? 158.875 137.909 86.868  1.00 42.76 ?  534 THR A OG1   1 
ATOM   4286  C  CG2   . THR A 1 534 ? 156.951 136.987 85.747  1.00 38.66 ?  534 THR A CG2   1 
ATOM   4287  N  N     . ASP A 1 535 ? 156.709 138.735 82.952  1.00 40.64 ?  535 ASP A N     1 
ATOM   4288  C  CA    . ASP A 1 535 ? 155.542 138.805 82.085  1.00 39.74 ?  535 ASP A CA    1 
ATOM   4289  C  C     . ASP A 1 535 ? 154.558 137.710 82.478  1.00 41.84 ?  535 ASP A C     1 
ATOM   4290  O  O     . ASP A 1 535 ? 154.926 136.534 82.555  1.00 42.89 ?  535 ASP A O     1 
ATOM   4291  C  CB    . ASP A 1 535 ? 155.949 138.658 80.619  1.00 38.68 ?  535 ASP A CB    1 
ATOM   4292  C  CG    . ASP A 1 535 ? 154.885 139.161 79.666  1.00 44.50 ?  535 ASP A CG    1 
ATOM   4293  O  OD1   . ASP A 1 535 ? 154.640 140.385 79.636  1.00 45.74 ?  535 ASP A OD1   1 
ATOM   4294  O  OD2   . ASP A 1 535 ? 154.296 138.330 78.944  1.00 45.92 -1 535 ASP A OD2   1 
ATOM   4295  N  N     . PHE A 1 536 ? 153.308 138.101 82.726  1.00 34.20 ?  536 PHE A N     1 
ATOM   4296  C  CA    . PHE A 1 536 ? 152.280 137.176 83.184  1.00 26.98 ?  536 PHE A CA    1 
ATOM   4297  C  C     . PHE A 1 536 ? 151.288 136.823 82.082  1.00 31.33 ?  536 PHE A C     1 
ATOM   4298  O  O     . PHE A 1 536 ? 150.163 136.403 82.373  1.00 37.66 ?  536 PHE A O     1 
ATOM   4299  C  CB    . PHE A 1 536 ? 151.555 137.755 84.398  1.00 29.06 ?  536 PHE A CB    1 
ATOM   4300  C  CG    . PHE A 1 536 ? 152.411 137.838 85.630  1.00 27.91 ?  536 PHE A CG    1 
ATOM   4301  C  CD1   . PHE A 1 536 ? 152.536 136.752 86.477  1.00 27.98 ?  536 PHE A CD1   1 
ATOM   4302  C  CD2   . PHE A 1 536 ? 153.097 139.000 85.936  1.00 27.54 ?  536 PHE A CD2   1 
ATOM   4303  C  CE1   . PHE A 1 536 ? 153.325 136.823 87.608  1.00 28.05 ?  536 PHE A CE1   1 
ATOM   4304  C  CE2   . PHE A 1 536 ? 153.888 139.076 87.066  1.00 32.24 ?  536 PHE A CE2   1 
ATOM   4305  C  CZ    . PHE A 1 536 ? 154.001 137.988 87.903  1.00 28.77 ?  536 PHE A CZ    1 
ATOM   4306  N  N     . SER A 1 537 ? 151.682 136.993 80.823  1.00 37.02 ?  537 SER A N     1 
ATOM   4307  C  CA    . SER A 1 537 ? 150.863 136.542 79.713  1.00 33.64 ?  537 SER A CA    1 
ATOM   4308  C  C     . SER A 1 537 ? 150.778 135.016 79.719  1.00 38.82 ?  537 SER A C     1 
ATOM   4309  O  O     . SER A 1 537 ? 151.693 134.339 80.196  1.00 39.19 ?  537 SER A O     1 
ATOM   4310  C  CB    . SER A 1 537 ? 151.448 137.035 78.391  1.00 37.25 ?  537 SER A CB    1 
ATOM   4311  O  OG    . SER A 1 537 ? 150.988 136.272 77.291  1.00 44.12 ?  537 SER A OG    1 
ATOM   4312  N  N     . PRO A 1 538 ? 149.678 134.451 79.218  1.00 37.27 ?  538 PRO A N     1 
ATOM   4313  C  CA    . PRO A 1 538 ? 149.529 132.991 79.240  1.00 34.32 ?  538 PRO A CA    1 
ATOM   4314  C  C     . PRO A 1 538 ? 150.644 132.294 78.474  1.00 39.19 ?  538 PRO A C     1 
ATOM   4315  O  O     . PRO A 1 538 ? 151.054 132.731 77.397  1.00 39.38 ?  538 PRO A O     1 
ATOM   4316  C  CB    . PRO A 1 538 ? 148.168 132.765 78.577  1.00 37.31 ?  538 PRO A CB    1 
ATOM   4317  C  CG    . PRO A 1 538 ? 147.435 134.043 78.774  1.00 34.46 ?  538 PRO A CG    1 
ATOM   4318  C  CD    . PRO A 1 538 ? 148.475 135.115 78.687  1.00 33.65 ?  538 PRO A CD    1 
ATOM   4319  N  N     . LYS A 1 539 ? 151.131 131.195 79.047  1.00 44.39 ?  539 LYS A N     1 
ATOM   4320  C  CA    . LYS A 1 539 ? 152.157 130.378 78.416  1.00 44.62 ?  539 LYS A CA    1 
ATOM   4321  C  C     . LYS A 1 539 ? 151.577 129.262 77.560  1.00 44.99 ?  539 LYS A C     1 
ATOM   4322  O  O     . LYS A 1 539 ? 152.334 128.581 76.860  1.00 47.43 ?  539 LYS A O     1 
ATOM   4323  C  CB    . LYS A 1 539 ? 153.080 129.775 79.480  1.00 43.77 ?  539 LYS A CB    1 
ATOM   4324  C  CG    . LYS A 1 539 ? 153.590 130.779 80.498  1.00 42.84 ?  539 LYS A CG    1 
ATOM   4325  C  CD    . LYS A 1 539 ? 154.845 131.479 80.003  1.00 45.68 ?  539 LYS A CD    1 
ATOM   4326  C  CE    . LYS A 1 539 ? 155.197 132.665 80.886  1.00 45.50 ?  539 LYS A CE    1 
ATOM   4327  N  NZ    . LYS A 1 539 ? 154.686 133.946 80.324  1.00 44.13 1  539 LYS A NZ    1 
ATOM   4328  N  N     . TYR A 1 540 ? 150.263 129.062 77.596  1.00 42.49 ?  540 TYR A N     1 
ATOM   4329  C  CA    . TYR A 1 540 ? 149.593 128.031 76.819  1.00 41.58 ?  540 TYR A CA    1 
ATOM   4330  C  C     . TYR A 1 540 ? 148.685 128.682 75.786  1.00 42.99 ?  540 TYR A C     1 
ATOM   4331  O  O     . TYR A 1 540 ? 148.056 129.710 76.057  1.00 44.81 ?  540 TYR A O     1 
ATOM   4332  C  CB    . TYR A 1 540 ? 148.783 127.100 77.725  1.00 42.66 ?  540 TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1 540 ? 149.634 126.270 78.655  1.00 44.40 ?  540 TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1 540 ? 150.000 126.747 79.907  1.00 42.75 ?  540 TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1 540 ? 150.080 125.010 78.279  1.00 45.61 ?  540 TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1 540 ? 150.781 125.992 80.759  1.00 45.50 ?  540 TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1 540 ? 150.862 124.248 79.125  1.00 40.60 ?  540 TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1 540 ? 151.209 124.743 80.363  1.00 45.33 ?  540 TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1 540 ? 151.987 123.985 81.205  1.00 46.48 ?  540 TYR A OH    1 
ATOM   4340  N  N     . GLU A 1 541 ? 148.629 128.079 74.595  1.00 47.04 ?  541 GLU A N     1 
ATOM   4341  C  CA    . GLU A 1 541 ? 147.828 128.644 73.514  1.00 47.04 ?  541 GLU A CA    1 
ATOM   4342  C  C     . GLU A 1 541 ? 146.344 128.635 73.858  1.00 47.07 ?  541 GLU A C     1 
ATOM   4343  O  O     . GLU A 1 541 ? 145.606 129.552 73.479  1.00 44.24 ?  541 GLU A O     1 
ATOM   4344  C  CB    . GLU A 1 541 ? 148.081 127.875 72.217  1.00 45.13 ?  541 GLU A CB    1 
ATOM   4345  C  CG    . GLU A 1 541 ? 147.803 128.674 70.956  1.00 46.40 ?  541 GLU A CG    1 
ATOM   4346  C  CD    . GLU A 1 541 ? 147.669 127.794 69.730  1.00 52.19 ?  541 GLU A CD    1 
ATOM   4347  O  OE1   . GLU A 1 541 ? 147.478 126.571 69.893  1.00 52.67 ?  541 GLU A OE1   1 
ATOM   4348  O  OE2   . GLU A 1 541 ? 147.757 128.324 68.601  1.00 50.07 -1 541 GLU A OE2   1 
ATOM   4349  N  N     . LYS A 1 542 ? 145.885 127.601 74.567  1.00 42.45 ?  542 LYS A N     1 
ATOM   4350  C  CA    . LYS A 1 542 ? 144.475 127.519 74.931  1.00 41.73 ?  542 LYS A CA    1 
ATOM   4351  C  C     . LYS A 1 542 ? 144.070 128.677 75.838  1.00 43.05 ?  542 LYS A C     1 
ATOM   4352  O  O     . LYS A 1 542 ? 143.014 129.290 75.642  1.00 41.93 ?  542 LYS A O     1 
ATOM   4353  C  CB    . LYS A 1 542 ? 144.190 126.179 75.609  1.00 40.93 ?  542 LYS A CB    1 
ATOM   4354  C  CG    . LYS A 1 542 ? 142.726 125.928 75.913  1.00 43.00 ?  542 LYS A CG    1 
ATOM   4355  C  CD    . LYS A 1 542 ? 142.533 124.574 76.573  1.00 39.38 ?  542 LYS A CD    1 
ATOM   4356  C  CE    . LYS A 1 542 ? 141.061 124.241 76.732  1.00 41.15 ?  542 LYS A CE    1 
ATOM   4357  N  NZ    . LYS A 1 542 ? 140.862 122.857 77.243  1.00 42.60 1  542 LYS A NZ    1 
ATOM   4358  N  N     . ILE A 1 543 ? 144.908 129.003 76.822  1.00 38.22 ?  543 ILE A N     1 
ATOM   4359  C  CA    . ILE A 1 543 ? 144.590 130.103 77.727  1.00 36.34 ?  543 ILE A CA    1 
ATOM   4360  C  C     . ILE A 1 543 ? 144.641 131.435 76.985  1.00 38.94 ?  543 ILE A C     1 
ATOM   4361  O  O     . ILE A 1 543 ? 143.817 132.328 77.224  1.00 41.41 ?  543 ILE A O     1 
ATOM   4362  C  CB    . ILE A 1 543 ? 145.538 130.088 78.940  1.00 35.88 ?  543 ILE A CB    1 
ATOM   4363  C  CG1   . ILE A 1 543 ? 145.413 128.777 79.721  1.00 39.31 ?  543 ILE A CG1   1 
ATOM   4364  C  CG2   . ILE A 1 543 ? 145.232 131.250 79.860  1.00 37.77 ?  543 ILE A CG2   1 
ATOM   4365  C  CD1   . ILE A 1 543 ? 144.012 128.205 79.779  1.00 37.09 ?  543 ILE A CD1   1 
ATOM   4366  N  N     . ALA A 1 544 ? 145.602 131.587 76.071  1.00 37.81 ?  544 ALA A N     1 
ATOM   4367  C  CA    . ALA A 1 544 ? 145.678 132.806 75.273  1.00 40.47 ?  544 ALA A CA    1 
ATOM   4368  C  C     . ALA A 1 544 ? 144.433 132.981 74.412  1.00 42.32 ?  544 ALA A C     1 
ATOM   4369  O  O     . ALA A 1 544 ? 143.919 134.096 74.269  1.00 42.94 ?  544 ALA A O     1 
ATOM   4370  C  CB    . ALA A 1 544 ? 146.935 132.786 74.404  1.00 40.60 ?  544 ALA A CB    1 
ATOM   4371  N  N     . ASN A 1 545 ? 143.935 131.888 73.827  1.00 43.74 ?  545 ASN A N     1 
ATOM   4372  C  CA    . ASN A 1 545 ? 142.685 131.958 73.078  1.00 44.64 ?  545 ASN A CA    1 
ATOM   4373  C  C     . ASN A 1 545 ? 141.505 132.254 73.992  1.00 44.81 ?  545 ASN A C     1 
ATOM   4374  O  O     . ASN A 1 545 ? 140.543 132.906 73.570  1.00 47.71 ?  545 ASN A O     1 
ATOM   4375  C  CB    . ASN A 1 545 ? 142.454 130.653 72.315  1.00 44.57 ?  545 ASN A CB    1 
ATOM   4376  C  CG    . ASN A 1 545 ? 143.560 130.353 71.327  1.00 47.93 ?  545 ASN A CG    1 
ATOM   4377  O  OD1   . ASN A 1 545 ? 144.262 131.255 70.871  1.00 47.94 ?  545 ASN A OD1   1 
ATOM   4378  N  ND2   . ASN A 1 545 ? 143.726 129.079 70.992  1.00 47.29 ?  545 ASN A ND2   1 
ATOM   4379  N  N     . LEU A 1 546 ? 141.555 131.777 75.237  1.00 40.52 ?  546 LEU A N     1 
ATOM   4380  C  CA    . LEU A 1 546 ? 140.532 132.150 76.210  1.00 38.34 ?  546 LEU A CA    1 
ATOM   4381  C  C     . LEU A 1 546 ? 140.538 133.652 76.459  1.00 38.77 ?  546 LEU A C     1 
ATOM   4382  O  O     . LEU A 1 546 ? 139.476 134.275 76.577  1.00 40.95 ?  546 LEU A O     1 
ATOM   4383  C  CB    . LEU A 1 546 ? 140.746 131.392 77.519  1.00 35.29 ?  546 LEU A CB    1 
ATOM   4384  C  CG    . LEU A 1 546 ? 140.352 129.917 77.536  1.00 38.57 ?  546 LEU A CG    1 
ATOM   4385  C  CD1   . LEU A 1 546 ? 140.512 129.356 78.935  1.00 36.37 ?  546 LEU A CD1   1 
ATOM   4386  C  CD2   . LEU A 1 546 ? 138.926 129.742 77.044  1.00 34.75 ?  546 LEU A CD2   1 
ATOM   4387  N  N     . PHE A 1 547 ? 141.723 134.251 76.539  1.00 37.80 ?  547 PHE A N     1 
ATOM   4388  C  CA    . PHE A 1 547 ? 141.859 135.684 76.765  1.00 36.82 ?  547 PHE A CA    1 
ATOM   4389  C  C     . PHE A 1 547 ? 141.763 136.500 75.481  1.00 37.34 ?  547 PHE A C     1 
ATOM   4390  O  O     . PHE A 1 547 ? 142.035 137.704 75.509  1.00 38.01 ?  547 PHE A O     1 
ATOM   4391  C  CB    . PHE A 1 547 ? 143.183 135.986 77.468  1.00 35.38 ?  547 PHE A CB    1 
ATOM   4392  C  CG    . PHE A 1 547 ? 143.160 135.715 78.940  1.00 35.44 ?  547 PHE A CG    1 
ATOM   4393  C  CD1   . PHE A 1 547 ? 142.641 136.648 79.821  1.00 34.89 ?  547 PHE A CD1   1 
ATOM   4394  C  CD2   . PHE A 1 547 ? 143.655 134.528 79.446  1.00 32.16 ?  547 PHE A CD2   1 
ATOM   4395  C  CE1   . PHE A 1 547 ? 142.618 136.401 81.179  1.00 31.83 ?  547 PHE A CE1   1 
ATOM   4396  C  CE2   . PHE A 1 547 ? 143.634 134.276 80.802  1.00 34.52 ?  547 PHE A CE2   1 
ATOM   4397  C  CZ    . PHE A 1 547 ? 143.113 135.213 81.668  1.00 33.71 ?  547 PHE A CZ    1 
ATOM   4398  N  N     . GLU A 1 548 ? 141.391 135.878 74.365  1.00 43.65 ?  548 GLU A N     1 
ATOM   4399  C  CA    . GLU A 1 548 ? 141.276 136.605 73.108  1.00 46.68 ?  548 GLU A CA    1 
ATOM   4400  C  C     . GLU A 1 548 ? 140.188 137.668 73.199  1.00 47.86 ?  548 GLU A C     1 
ATOM   4401  O  O     . GLU A 1 548 ? 139.139 137.460 73.815  1.00 47.21 ?  548 GLU A O     1 
ATOM   4402  C  CB    . GLU A 1 548 ? 140.973 135.640 71.961  1.00 45.30 ?  548 GLU A CB    1 
ATOM   4403  C  CG    . GLU A 1 548 ? 141.819 135.873 70.722  1.00 46.87 ?  548 GLU A CG    1 
ATOM   4404  C  CD    . GLU A 1 548 ? 143.293 135.635 70.973  1.00 49.11 ?  548 GLU A CD    1 
ATOM   4405  O  OE1   . GLU A 1 548 ? 143.725 134.464 70.924  1.00 48.26 ?  548 GLU A OE1   1 
ATOM   4406  O  OE2   . GLU A 1 548 ? 144.022 136.619 71.220  1.00 47.53 -1 548 GLU A OE2   1 
ATOM   4407  N  N     . GLY A 1 549 ? 140.446 138.816 72.576  1.00 44.32 ?  549 GLY A N     1 
ATOM   4408  C  CA    . GLY A 1 549 ? 139.543 139.944 72.635  1.00 40.96 ?  549 GLY A CA    1 
ATOM   4409  C  C     . GLY A 1 549 ? 139.743 140.858 73.823  1.00 43.69 ?  549 GLY A C     1 
ATOM   4410  O  O     . GLY A 1 549 ? 139.021 141.855 73.943  1.00 44.76 ?  549 GLY A O     1 
ATOM   4411  N  N     . MET A 1 550 ? 140.696 140.552 74.700  1.00 43.09 ?  550 MET A N     1 
ATOM   4412  C  CA    . MET A 1 550 ? 140.968 141.346 75.890  1.00 40.92 ?  550 MET A CA    1 
ATOM   4413  C  C     . MET A 1 550 ? 142.448 141.689 75.926  1.00 41.67 ?  550 MET A C     1 
ATOM   4414  O  O     . MET A 1 550 ? 143.293 140.819 75.687  1.00 42.25 ?  550 MET A O     1 
ATOM   4415  C  CB    . MET A 1 550 ? 140.578 140.588 77.160  1.00 38.56 ?  550 MET A CB    1 
ATOM   4416  C  CG    . MET A 1 550 ? 139.345 141.123 77.855  1.00 42.56 ?  550 MET A CG    1 
ATOM   4417  S  SD    . MET A 1 550 ? 138.972 140.174 79.335  1.00 55.69 ?  550 MET A SD    1 
ATOM   4418  C  CE    . MET A 1 550 ? 138.819 138.528 78.647  1.00 41.52 ?  550 MET A CE    1 
ATOM   4419  N  N     . HIS A 1 551 ? 142.763 142.945 76.227  1.00 38.98 ?  551 HIS A N     1 
ATOM   4420  C  CA    . HIS A 1 551 ? 144.156 143.360 76.320  1.00 38.16 ?  551 HIS A CA    1 
ATOM   4421  C  C     . HIS A 1 551 ? 144.762 142.840 77.618  1.00 38.90 ?  551 HIS A C     1 
ATOM   4422  O  O     . HIS A 1 551 ? 144.261 143.132 78.708  1.00 40.01 ?  551 HIS A O     1 
ATOM   4423  C  CB    . HIS A 1 551 ? 144.266 144.880 76.247  1.00 39.46 ?  551 HIS A CB    1 
ATOM   4424  C  CG    . HIS A 1 551 ? 145.641 145.397 76.530  1.00 41.61 ?  551 HIS A CG    1 
ATOM   4425  N  ND1   . HIS A 1 551 ? 146.735 145.059 75.763  1.00 42.78 ?  551 HIS A ND1   1 
ATOM   4426  C  CD2   . HIS A 1 551 ? 146.102 146.226 77.497  1.00 42.39 ?  551 HIS A CD2   1 
ATOM   4427  C  CE1   . HIS A 1 551 ? 147.810 145.658 76.243  1.00 40.85 ?  551 HIS A CE1   1 
ATOM   4428  N  NE2   . HIS A 1 551 ? 147.454 146.372 77.295  1.00 41.74 ?  551 HIS A NE2   1 
ATOM   4429  N  N     . ILE A 1 552 ? 145.836 142.069 77.498  1.00 35.62 ?  552 ILE A N     1 
ATOM   4430  C  CA    . ILE A 1 552 ? 146.537 141.514 78.651  1.00 31.64 ?  552 ILE A CA    1 
ATOM   4431  C  C     . ILE A 1 552 ? 147.664 142.475 79.021  1.00 33.24 ?  552 ILE A C     1 
ATOM   4432  O  O     . ILE A 1 552 ? 148.545 142.724 78.184  1.00 36.10 ?  552 ILE A O     1 
ATOM   4433  C  CB    . ILE A 1 552 ? 147.084 140.114 78.352  1.00 33.70 ?  552 ILE A CB    1 
ATOM   4434  C  CG1   . ILE A 1 552 ? 145.933 139.147 78.071  1.00 32.99 ?  552 ILE A CG1   1 
ATOM   4435  C  CG2   . ILE A 1 552 ? 147.937 139.615 79.505  1.00 34.38 ?  552 ILE A CG2   1 
ATOM   4436  C  CD1   . ILE A 1 552 ? 146.382 137.802 77.559  1.00 34.55 ?  552 ILE A CD1   1 
ATOM   4437  N  N     . PRO A 1 553 ? 147.668 143.036 80.229  1.00 38.28 ?  553 PRO A N     1 
ATOM   4438  C  CA    . PRO A 1 553 ? 148.717 143.997 80.595  1.00 32.24 ?  553 PRO A CA    1 
ATOM   4439  C  C     . PRO A 1 553 ? 150.099 143.363 80.541  1.00 35.19 ?  553 PRO A C     1 
ATOM   4440  O  O     . PRO A 1 553 ? 150.328 142.277 81.079  1.00 36.48 ?  553 PRO A O     1 
ATOM   4441  C  CB    . PRO A 1 553 ? 148.337 144.408 82.022  1.00 31.02 ?  553 PRO A CB    1 
ATOM   4442  C  CG    . PRO A 1 553 ? 146.875 144.110 82.125  1.00 30.52 ?  553 PRO A CG    1 
ATOM   4443  C  CD    . PRO A 1 553 ? 146.656 142.891 81.287  1.00 32.28 ?  553 PRO A CD    1 
ATOM   4444  N  N     . THR A 1 554 ? 151.023 144.055 79.885  1.00 39.01 ?  554 THR A N     1 
ATOM   4445  C  CA    . THR A 1 554 ? 152.393 143.603 79.734  1.00 38.97 ?  554 THR A CA    1 
ATOM   4446  C  C     . THR A 1 554 ? 153.273 144.267 80.789  1.00 37.81 ?  554 THR A C     1 
ATOM   4447  O  O     . THR A 1 554 ? 152.789 144.942 81.701  1.00 39.91 ?  554 THR A O     1 
ATOM   4448  C  CB    . THR A 1 554 ? 152.890 143.896 78.317  1.00 37.93 ?  554 THR A CB    1 
ATOM   4449  O  OG1   . THR A 1 554 ? 153.005 145.311 78.133  1.00 40.49 ?  554 THR A OG1   1 
ATOM   4450  C  CG2   . THR A 1 554 ? 151.922 143.335 77.287  1.00 35.01 ?  554 THR A CG2   1 
ATOM   4451  N  N     . THR A 1 555 ? 154.588 144.073 80.669  1.00 38.74 ?  555 THR A N     1 
ATOM   4452  C  CA    . THR A 1 555 ? 155.512 144.725 81.589  1.00 36.20 ?  555 THR A CA    1 
ATOM   4453  C  C     . THR A 1 555 ? 155.544 146.232 81.377  1.00 38.34 ?  555 THR A C     1 
ATOM   4454  O  O     . THR A 1 555 ? 155.708 146.987 82.340  1.00 40.28 ?  555 THR A O     1 
ATOM   4455  C  CB    . THR A 1 555 ? 156.915 144.138 81.438  1.00 38.61 ?  555 THR A CB    1 
ATOM   4456  O  OG1   . THR A 1 555 ? 157.255 144.056 80.048  1.00 41.79 ?  555 THR A OG1   1 
ATOM   4457  C  CG2   . THR A 1 555 ? 156.978 142.748 82.055  1.00 37.28 ?  555 THR A CG2   1 
ATOM   4458  N  N     . GLU A 1 556 ? 155.398 146.689 80.130  1.00 39.91 ?  556 GLU A N     1 
ATOM   4459  C  CA    . GLU A 1 556 ? 155.332 148.124 79.872  1.00 39.82 ?  556 GLU A CA    1 
ATOM   4460  C  C     . GLU A 1 556 ? 154.069 148.734 80.470  1.00 38.55 ?  556 GLU A C     1 
ATOM   4461  O  O     . GLU A 1 556 ? 154.107 149.834 81.035  1.00 40.13 ?  556 GLU A O     1 
ATOM   4462  C  CB    . GLU A 1 556 ? 155.400 148.391 78.369  1.00 40.74 ?  556 GLU A CB    1 
ATOM   4463  C  CG    . GLU A 1 556 ? 155.620 149.849 78.008  1.00 43.25 ?  556 GLU A CG    1 
ATOM   4464  C  CD    . GLU A 1 556 ? 156.883 150.418 78.626  1.00 44.78 ?  556 GLU A CD    1 
ATOM   4465  O  OE1   . GLU A 1 556 ? 157.910 149.705 78.648  1.00 41.96 ?  556 GLU A OE1   1 
ATOM   4466  O  OE2   . GLU A 1 556 ? 156.850 151.576 79.091  1.00 44.90 -1 556 GLU A OE2   1 
ATOM   4467  N  N     . ASP A 1 557 ? 152.938 148.035 80.349  1.00 40.02 ?  557 ASP A N     1 
ATOM   4468  C  CA    . ASP A 1 557 ? 151.706 148.506 80.971  1.00 36.22 ?  557 ASP A CA    1 
ATOM   4469  C  C     . ASP A 1 557 ? 151.848 148.565 82.485  1.00 36.15 ?  557 ASP A C     1 
ATOM   4470  O  O     . ASP A 1 557 ? 151.357 149.500 83.128  1.00 37.41 ?  557 ASP A O     1 
ATOM   4471  C  CB    . ASP A 1 557 ? 150.539 147.603 80.575  1.00 35.10 ?  557 ASP A CB    1 
ATOM   4472  C  CG    . ASP A 1 557 ? 150.029 147.892 79.178  1.00 40.32 ?  557 ASP A CG    1 
ATOM   4473  O  OD1   . ASP A 1 557 ? 150.074 149.067 78.759  1.00 43.55 ?  557 ASP A OD1   1 
ATOM   4474  O  OD2   . ASP A 1 557 ? 149.586 146.943 78.498  1.00 42.22 -1 557 ASP A OD2   1 
ATOM   4475  N  N     . TRP A 1 558 ? 152.524 147.576 83.074  1.00 29.19 ?  558 TRP A N     1 
ATOM   4476  C  CA    . TRP A 1 558 ? 152.752 147.596 84.513  1.00 27.33 ?  558 TRP A CA    1 
ATOM   4477  C  C     . TRP A 1 558 ? 153.694 148.722 84.920  1.00 29.30 ?  558 TRP A C     1 
ATOM   4478  O  O     . TRP A 1 558 ? 153.519 149.311 85.990  1.00 33.21 ?  558 TRP A O     1 
ATOM   4479  C  CB    . TRP A 1 558 ? 153.296 146.248 84.975  1.00 29.55 ?  558 TRP A CB    1 
ATOM   4480  C  CG    . TRP A 1 558 ? 152.225 145.270 85.339  1.00 27.37 ?  558 TRP A CG    1 
ATOM   4481  C  CD1   . TRP A 1 558 ? 151.835 144.177 84.624  1.00 27.28 ?  558 TRP A CD1   1 
ATOM   4482  C  CD2   . TRP A 1 558 ? 151.403 145.297 86.511  1.00 28.16 ?  558 TRP A CD2   1 
ATOM   4483  N  NE1   . TRP A 1 558 ? 150.824 143.519 85.279  1.00 30.85 ?  558 TRP A NE1   1 
ATOM   4484  C  CE2   . TRP A 1 558 ? 150.542 144.185 86.442  1.00 28.47 ?  558 TRP A CE2   1 
ATOM   4485  C  CE3   . TRP A 1 558 ? 151.316 146.148 87.616  1.00 30.88 ?  558 TRP A CE3   1 
ATOM   4486  C  CZ2   . TRP A 1 558 ? 149.605 143.905 87.432  1.00 26.24 ?  558 TRP A CZ2   1 
ATOM   4487  C  CZ3   . TRP A 1 558 ? 150.385 145.868 88.598  1.00 26.03 ?  558 TRP A CZ3   1 
ATOM   4488  C  CH2   . TRP A 1 558 ? 149.543 144.757 88.499  1.00 22.82 ?  558 TRP A CH2   1 
ATOM   4489  N  N     . LYS A 1 559 ? 154.691 149.036 84.090  1.00 36.33 ?  559 LYS A N     1 
ATOM   4490  C  CA    . LYS A 1 559 ? 155.554 150.181 84.372  1.00 32.59 ?  559 LYS A CA    1 
ATOM   4491  C  C     . LYS A 1 559 ? 154.766 151.484 84.323  1.00 31.12 ?  559 LYS A C     1 
ATOM   4492  O  O     . LYS A 1 559 ? 154.956 152.370 85.166  1.00 34.31 ?  559 LYS A O     1 
ATOM   4493  C  CB    . LYS A 1 559 ? 156.712 150.222 83.375  1.00 36.36 ?  559 LYS A CB    1 
ATOM   4494  C  CG    . LYS A 1 559 ? 157.883 149.328 83.735  1.00 38.00 ?  559 LYS A CG    1 
ATOM   4495  C  CD    . LYS A 1 559 ? 158.580 148.815 82.488  1.00 39.16 ?  559 LYS A CD    1 
ATOM   4496  C  CE    . LYS A 1 559 ? 159.584 147.727 82.820  1.00 37.84 ?  559 LYS A CE    1 
ATOM   4497  N  NZ    . LYS A 1 559 ? 160.769 147.774 81.921  1.00 39.17 1  559 LYS A NZ    1 
ATOM   4498  N  N     . LYS A 1 560 ? 153.878 151.617 83.337  1.00 33.31 ?  560 LYS A N     1 
ATOM   4499  C  CA    . LYS A 1 560 ? 153.027 152.800 83.258  1.00 32.75 ?  560 LYS A CA    1 
ATOM   4500  C  C     . LYS A 1 560 ? 152.112 152.899 84.472  1.00 36.91 ?  560 LYS A C     1 
ATOM   4501  O  O     . LYS A 1 560 ? 151.905 153.990 85.014  1.00 36.57 ?  560 LYS A O     1 
ATOM   4502  C  CB    . LYS A 1 560 ? 152.208 152.775 81.969  1.00 32.44 ?  560 LYS A CB    1 
ATOM   4503  C  CG    . LYS A 1 560 ? 153.032 152.936 80.705  1.00 37.98 ?  560 LYS A CG    1 
ATOM   4504  C  CD    . LYS A 1 560 ? 152.168 152.781 79.465  1.00 38.81 ?  560 LYS A CD    1 
ATOM   4505  C  CE    . LYS A 1 560 ? 153.016 152.643 78.213  1.00 35.97 ?  560 LYS A CE    1 
ATOM   4506  N  NZ    . LYS A 1 560 ? 152.228 152.105 77.072  1.00 38.72 1  560 LYS A NZ    1 
ATOM   4507  N  N     . LEU A 1 561 ? 151.555 151.769 84.912  1.00 35.84 ?  561 LEU A N     1 
ATOM   4508  C  CA    . LEU A 1 561 ? 150.718 151.770 86.108  1.00 28.48 ?  561 LEU A CA    1 
ATOM   4509  C  C     . LEU A 1 561 ? 151.524 152.132 87.349  1.00 28.17 ?  561 LEU A C     1 
ATOM   4510  O  O     . LEU A 1 561 ? 151.028 152.836 88.234  1.00 30.26 ?  561 LEU A O     1 
ATOM   4511  C  CB    . LEU A 1 561 ? 150.046 150.409 86.284  1.00 28.29 ?  561 LEU A CB    1 
ATOM   4512  C  CG    . LEU A 1 561 ? 149.115 150.304 87.494  1.00 29.77 ?  561 LEU A CG    1 
ATOM   4513  C  CD1   . LEU A 1 561 ? 148.038 151.371 87.419  1.00 26.57 ?  561 LEU A CD1   1 
ATOM   4514  C  CD2   . LEU A 1 561 ? 148.497 148.923 87.593  1.00 24.71 ?  561 LEU A CD2   1 
ATOM   4515  N  N     . LYS A 1 562 ? 152.764 151.647 87.439  1.00 29.68 ?  562 LYS A N     1 
ATOM   4516  C  CA    . LYS A 1 562 ? 153.626 152.003 88.561  1.00 30.82 ?  562 LYS A CA    1 
ATOM   4517  C  C     . LYS A 1 562 ? 153.908 153.499 88.584  1.00 35.47 ?  562 LYS A C     1 
ATOM   4518  O  O     . LYS A 1 562 ? 153.861 154.132 89.645  1.00 35.60 ?  562 LYS A O     1 
ATOM   4519  C  CB    . LYS A 1 562 ? 154.930 151.209 88.481  1.00 28.95 ?  562 LYS A CB    1 
ATOM   4520  C  CG    . LYS A 1 562 ? 155.986 151.615 89.490  1.00 29.87 ?  562 LYS A CG    1 
ATOM   4521  C  CD    . LYS A 1 562 ? 157.308 150.933 89.184  1.00 30.17 ?  562 LYS A CD    1 
ATOM   4522  C  CE    . LYS A 1 562 ? 158.376 151.304 90.195  1.00 32.22 ?  562 LYS A CE    1 
ATOM   4523  N  NZ    . LYS A 1 562 ? 159.493 150.321 90.194  1.00 34.97 1  562 LYS A NZ    1 
ATOM   4524  N  N     . ALA A 1 563 ? 154.192 154.083 87.417  1.00 34.18 ?  563 ALA A N     1 
ATOM   4525  C  CA    . ALA A 1 563 ? 154.401 155.527 87.347  1.00 31.91 ?  563 ALA A CA    1 
ATOM   4526  C  C     . ALA A 1 563 ? 153.130 156.286 87.712  1.00 31.32 ?  563 ALA A C     1 
ATOM   4527  O  O     . ALA A 1 563 ? 153.186 157.314 88.399  1.00 37.17 ?  563 ALA A O     1 
ATOM   4528  C  CB    . ALA A 1 563 ? 154.881 155.920 85.949  1.00 33.30 ?  563 ALA A CB    1 
ATOM   4529  N  N     . PHE A 1 564 ? 151.975 155.795 87.259  1.00 33.10 ?  564 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 564 ? 150.706 156.435 87.587  1.00 30.55 ?  564 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 564 ? 150.439 156.398 89.086  1.00 31.17 ?  564 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 564 ? 149.962 157.380 89.665  1.00 35.80 ?  564 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 564 ? 149.575 155.752 86.817  1.00 30.41 ?  564 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 564 ? 148.292 156.529 86.799  1.00 30.40 ?  564 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 564 ? 148.076 157.514 85.851  1.00 32.82 ?  564 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 564 ? 147.294 156.264 87.720  1.00 33.53 ?  564 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 564 ? 146.893 158.226 85.829  1.00 38.30 ?  564 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 564 ? 146.110 156.973 87.704  1.00 34.07 ?  564 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 564 ? 145.908 157.954 86.758  1.00 36.68 ?  564 PHE A CZ    1 
ATOM   4540  N  N     . VAL A 1 565 ? 150.734 155.268 89.730  1.00 32.53 ?  565 VAL A N     1 
ATOM   4541  C  CA    . VAL A 1 565 ? 150.555 155.156 91.174  1.00 27.22 ?  565 VAL A CA    1 
ATOM   4542  C  C     . VAL A 1 565 ? 151.533 156.068 91.904  1.00 31.96 ?  565 VAL A C     1 
ATOM   4543  O  O     . VAL A 1 565 ? 151.184 156.693 92.912  1.00 36.49 ?  565 VAL A O     1 
ATOM   4544  C  CB    . VAL A 1 565 ? 150.705 153.688 91.613  1.00 26.89 ?  565 VAL A CB    1 
ATOM   4545  C  CG1   . VAL A 1 565 ? 150.877 153.585 93.120  1.00 28.44 ?  565 VAL A CG1   1 
ATOM   4546  C  CG2   . VAL A 1 565 ? 149.503 152.885 91.162  1.00 30.95 ?  565 VAL A CG2   1 
ATOM   4547  N  N     . ALA A 1 566 ? 152.767 156.166 91.407  1.00 35.27 ?  566 ALA A N     1 
ATOM   4548  C  CA    . ALA A 1 566 ? 153.738 157.066 92.018  1.00 33.21 ?  566 ALA A CA    1 
ATOM   4549  C  C     . ALA A 1 566 ? 153.276 158.516 91.931  1.00 36.36 ?  566 ALA A C     1 
ATOM   4550  O  O     . ALA A 1 566 ? 153.435 159.286 92.886  1.00 36.75 ?  566 ALA A O     1 
ATOM   4551  C  CB    . ALA A 1 566 ? 155.103 156.896 91.354  1.00 32.08 ?  566 ALA A CB    1 
ATOM   4552  N  N     . GLU A 1 567 ? 152.702 158.906 90.793  1.00 36.78 ?  567 GLU A N     1 
ATOM   4553  C  CA    . GLU A 1 567 ? 152.273 160.291 90.620  1.00 35.42 ?  567 GLU A CA    1 
ATOM   4554  C  C     . GLU A 1 567 ? 151.004 160.597 91.410  1.00 38.61 ?  567 GLU A C     1 
ATOM   4555  O  O     . GLU A 1 567 ? 150.891 161.668 92.017  1.00 41.33 ?  567 GLU A O     1 
ATOM   4556  C  CB    . GLU A 1 567 ? 152.065 160.595 89.137  1.00 37.27 ?  567 GLU A CB    1 
ATOM   4557  C  CG    . GLU A 1 567 ? 153.246 161.290 88.474  1.00 42.63 ?  567 GLU A CG    1 
ATOM   4558  C  CD    . GLU A 1 567 ? 154.492 160.428 88.440  1.00 45.29 ?  567 GLU A CD    1 
ATOM   4559  O  OE1   . GLU A 1 567 ? 155.382 160.631 89.293  1.00 42.73 ?  567 GLU A OE1   1 
ATOM   4560  O  OE2   . GLU A 1 567 ? 154.588 159.553 87.554  1.00 42.47 -1 567 GLU A OE2   1 
ATOM   4561  N  N     . HIS A 1 568 ? 150.039 159.674 91.420  1.00 39.00 ?  568 HIS A N     1 
ATOM   4562  C  CA    . HIS A 1 568 ? 148.713 159.957 91.949  1.00 36.41 ?  568 HIS A CA    1 
ATOM   4563  C  C     . HIS A 1 568 ? 148.384 159.229 93.245  1.00 35.41 ?  568 HIS A C     1 
ATOM   4564  O  O     . HIS A 1 568 ? 147.420 159.609 93.916  1.00 41.18 ?  568 HIS A O     1 
ATOM   4565  C  CB    . HIS A 1 568 ? 147.646 159.612 90.901  1.00 33.87 ?  568 HIS A CB    1 
ATOM   4566  C  CG    . HIS A 1 568 ? 147.649 160.523 89.714  1.00 38.50 ?  568 HIS A CG    1 
ATOM   4567  N  ND1   . HIS A 1 568 ? 147.514 161.890 89.825  1.00 36.84 ?  568 HIS A ND1   1 
ATOM   4568  C  CD2   . HIS A 1 568 ? 147.776 160.263 88.391  1.00 37.26 ?  568 HIS A CD2   1 
ATOM   4569  C  CE1   . HIS A 1 568 ? 147.555 162.433 88.621  1.00 40.24 ?  568 HIS A CE1   1 
ATOM   4570  N  NE2   . HIS A 1 568 ? 147.713 161.468 87.734  1.00 40.01 ?  568 HIS A NE2   1 
ATOM   4571  N  N     . GLY A 1 569 ? 149.146 158.209 93.619  1.00 28.17 ?  569 GLY A N     1 
ATOM   4572  C  CA    . GLY A 1 569 ? 148.832 157.456 94.811  1.00 28.04 ?  569 GLY A CA    1 
ATOM   4573  C  C     . GLY A 1 569 ? 147.793 156.380 94.560  1.00 28.41 ?  569 GLY A C     1 
ATOM   4574  O  O     . GLY A 1 569 ? 147.386 156.105 93.430  1.00 34.15 ?  569 GLY A O     1 
ATOM   4575  N  N     . MET A 1 570 ? 147.363 155.756 95.654  1.00 25.27 ?  570 MET A N     1 
ATOM   4576  C  CA    . MET A 1 570 ? 146.366 154.695 95.612  1.00 25.78 ?  570 MET A CA    1 
ATOM   4577  C  C     . MET A 1 570 ? 145.329 154.952 96.694  1.00 24.58 ?  570 MET A C     1 
ATOM   4578  O  O     . MET A 1 570 ? 145.684 155.207 97.848  1.00 27.32 ?  570 MET A O     1 
ATOM   4579  C  CB    . MET A 1 570 ? 147.017 153.321 95.799  1.00 24.02 ?  570 MET A CB    1 
ATOM   4580  C  CG    . MET A 1 570 ? 147.518 152.700 94.504  1.00 20.26 ?  570 MET A CG    1 
ATOM   4581  S  SD    . MET A 1 570 ? 147.596 150.902 94.545  1.00 39.13 ?  570 MET A SD    1 
ATOM   4582  C  CE    . MET A 1 570 ? 146.361 150.534 95.782  1.00 25.71 ?  570 MET A CE    1 
ATOM   4583  N  N     . TYR A 1 571 ? 144.052 154.886 96.318  1.00 21.91 ?  571 TYR A N     1 
ATOM   4584  C  CA    . TYR A 1 571 ? 142.981 155.219 97.251  1.00 14.14 ?  571 TYR A CA    1 
ATOM   4585  C  C     . TYR A 1 571 ? 142.754 154.133 98.294  1.00 20.21 ?  571 TYR A C     1 
ATOM   4586  O  O     . TYR A 1 571 ? 142.441 154.447 99.447  1.00 24.53 ?  571 TYR A O     1 
ATOM   4587  C  CB    . TYR A 1 571 ? 141.683 155.483 96.490  1.00 22.96 ?  571 TYR A CB    1 
ATOM   4588  C  CG    . TYR A 1 571 ? 140.582 156.061 97.349  1.00 24.15 ?  571 TYR A CG    1 
ATOM   4589  C  CD1   . TYR A 1 571 ? 140.577 157.406 97.688  1.00 23.12 ?  571 TYR A CD1   1 
ATOM   4590  C  CD2   . TYR A 1 571 ? 139.553 155.260 97.825  1.00 18.53 ?  571 TYR A CD2   1 
ATOM   4591  C  CE1   . TYR A 1 571 ? 139.577 157.938 98.474  1.00 22.43 ?  571 TYR A CE1   1 
ATOM   4592  C  CE2   . TYR A 1 571 ? 138.549 155.784 98.613  1.00 19.81 ?  571 TYR A CE2   1 
ATOM   4593  C  CZ    . TYR A 1 571 ? 138.564 157.124 98.932  1.00 25.46 ?  571 TYR A CZ    1 
ATOM   4594  O  OH    . TYR A 1 571 ? 137.566 157.652 99.716  1.00 28.14 ?  571 TYR A OH    1 
ATOM   4595  N  N     . HIS A 1 572 ? 142.903 152.866 97.921  1.00 22.73 ?  572 HIS A N     1 
ATOM   4596  C  CA    . HIS A 1 572 ? 142.620 151.751 98.814  1.00 13.70 ?  572 HIS A CA    1 
ATOM   4597  C  C     . HIS A 1 572 ? 143.920 151.150 99.325  1.00 10.41 ?  572 HIS A C     1 
ATOM   4598  O  O     . HIS A 1 572 ? 144.830 150.867 98.541  1.00 22.35 ?  572 HIS A O     1 
ATOM   4599  C  CB    . HIS A 1 572 ? 141.795 150.675 98.106  1.00 14.68 ?  572 HIS A CB    1 
ATOM   4600  C  CG    . HIS A 1 572 ? 140.599 151.207 97.381  1.00 15.57 ?  572 HIS A CG    1 
ATOM   4601  N  ND1   . HIS A 1 572 ? 140.638 151.581 96.055  1.00 16.85 ?  572 HIS A ND1   1 
ATOM   4602  C  CD2   . HIS A 1 572 ? 139.328 151.424 97.795  1.00 9.72  ?  572 HIS A CD2   1 
ATOM   4603  C  CE1   . HIS A 1 572 ? 139.445 152.008 95.685  1.00 16.23 ?  572 HIS A CE1   1 
ATOM   4604  N  NE2   . HIS A 1 572 ? 138.632 151.923 96.722  1.00 23.78 ?  572 HIS A NE2   1 
ATOM   4605  N  N     . SER A 1 573 ? 144.005 150.966 100.644 1.00 5.57  ?  573 SER A N     1 
ATOM   4606  C  CA    . SER A 1 573 ? 145.140 150.249 101.212 1.00 7.60  ?  573 SER A CA    1 
ATOM   4607  C  C     . SER A 1 573 ? 145.141 148.793 100.769 1.00 11.79 ?  573 SER A C     1 
ATOM   4608  O  O     . SER A 1 573 ? 146.203 148.217 100.507 1.00 19.77 ?  573 SER A O     1 
ATOM   4609  C  CB    . SER A 1 573 ? 145.112 150.348 102.735 1.00 15.52 ?  573 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 573 ? 143.874 149.891 103.244 1.00 22.99 ?  573 SER A OG    1 
ATOM   4611  N  N     . TYR A 1 574 ? 143.961 148.183 100.688 1.00 12.39 ?  574 TYR A N     1 
ATOM   4612  C  CA    . TYR A 1 574 ? 143.806 146.814 100.223 1.00 1.15  ?  574 TYR A CA    1 
ATOM   4613  C  C     . TYR A 1 574 ? 142.632 146.761 99.261  1.00 8.90  ?  574 TYR A C     1 
ATOM   4614  O  O     . TYR A 1 574 ? 141.635 147.463 99.453  1.00 16.56 ?  574 TYR A O     1 
ATOM   4615  C  CB    . TYR A 1 574 ? 143.594 145.850 101.396 1.00 11.68 ?  574 TYR A CB    1 
ATOM   4616  C  CG    . TYR A 1 574 ? 144.669 145.960 102.452 1.00 8.23  ?  574 TYR A CG    1 
ATOM   4617  C  CD1   . TYR A 1 574 ? 144.560 146.884 103.481 1.00 10.27 ?  574 TYR A CD1   1 
ATOM   4618  C  CD2   . TYR A 1 574 ? 145.794 145.151 102.415 1.00 8.46  ?  574 TYR A CD2   1 
ATOM   4619  C  CE1   . TYR A 1 574 ? 145.538 147.000 104.441 1.00 6.62  ?  574 TYR A CE1   1 
ATOM   4620  C  CE2   . TYR A 1 574 ? 146.778 145.258 103.374 1.00 11.12 ?  574 TYR A CE2   1 
ATOM   4621  C  CZ    . TYR A 1 574 ? 146.643 146.184 104.386 1.00 5.82  ?  574 TYR A CZ    1 
ATOM   4622  O  OH    . TYR A 1 574 ? 147.618 146.297 105.347 1.00 18.04 ?  574 TYR A OH    1 
ATOM   4623  N  N     . ARG A 1 575 ? 142.755 145.937 98.227  1.00 11.09 ?  575 ARG A N     1 
ATOM   4624  C  CA    . ARG A 1 575 ? 141.765 145.893 97.158  1.00 4.65  ?  575 ARG A CA    1 
ATOM   4625  C  C     . ARG A 1 575 ? 141.156 144.519 96.943  1.00 9.69  ?  575 ARG A C     1 
ATOM   4626  O  O     . ARG A 1 575 ? 139.949 144.417 96.714  1.00 19.78 ?  575 ARG A O     1 
ATOM   4627  C  CB    . ARG A 1 575 ? 142.392 146.367 95.842  1.00 17.10 ?  575 ARG A CB    1 
ATOM   4628  C  CG    . ARG A 1 575 ? 142.886 147.799 95.857  1.00 11.51 ?  575 ARG A CG    1 
ATOM   4629  C  CD    . ARG A 1 575 ? 143.996 147.988 94.840  1.00 11.59 ?  575 ARG A CD    1 
ATOM   4630  N  NE    . ARG A 1 575 ? 145.214 147.292 95.238  1.00 16.30 ?  575 ARG A NE    1 
ATOM   4631  C  CZ    . ARG A 1 575 ? 145.627 146.144 94.717  1.00 14.92 ?  575 ARG A CZ    1 
ATOM   4632  N  NH1   . ARG A 1 575 ? 144.946 145.534 93.762  1.00 12.79 1  575 ARG A NH1   1 
ATOM   4633  N  NH2   . ARG A 1 575 ? 146.751 145.596 95.166  1.00 14.91 ?  575 ARG A NH2   1 
ATOM   4634  N  N     . LEU A 1 576 ? 141.954 143.456 97.006  1.00 19.64 ?  576 LEU A N     1 
ATOM   4635  C  CA    . LEU A 1 576 ? 141.524 142.130 96.592  1.00 12.26 ?  576 LEU A CA    1 
ATOM   4636  C  C     . LEU A 1 576 ? 141.608 141.162 97.762  1.00 3.41  ?  576 LEU A C     1 
ATOM   4637  O  O     . LEU A 1 576 ? 142.650 141.063 98.416  1.00 19.60 ?  576 LEU A O     1 
ATOM   4638  C  CB    . LEU A 1 576 ? 142.382 141.617 95.433  1.00 4.91  ?  576 LEU A CB    1 
ATOM   4639  C  CG    . LEU A 1 576 ? 142.578 142.558 94.243  1.00 8.38  ?  576 LEU A CG    1 
ATOM   4640  C  CD1   . LEU A 1 576 ? 143.601 141.982 93.282  1.00 11.87 ?  576 LEU A CD1   1 
ATOM   4641  C  CD2   . LEU A 1 576 ? 141.263 142.819 93.533  1.00 10.83 ?  576 LEU A CD2   1 
ATOM   4642  N  N     . CYS A 1 577 ? 140.511 140.456 98.021  1.00 1.85  ?  577 CYS A N     1 
ATOM   4643  C  CA    . CYS A 1 577 ? 140.508 139.323 98.935  1.00 6.52  ?  577 CYS A CA    1 
ATOM   4644  C  C     . CYS A 1 577 ? 139.429 138.362 98.465  1.00 16.04 ?  577 CYS A C     1 
ATOM   4645  O  O     . CYS A 1 577 ? 138.326 138.791 98.117  1.00 21.38 ?  577 CYS A O     1 
ATOM   4646  C  CB    . CYS A 1 577 ? 140.270 139.757 100.389 1.00 5.82  ?  577 CYS A CB    1 
ATOM   4647  S  SG    . CYS A 1 577 ? 138.550 140.029 100.878 1.00 27.63 ?  577 CYS A SG    1 
ATOM   4648  N  N     . ILE A 1 578 ? 139.752 137.074 98.434  1.00 8.13  ?  578 ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 578 ? 138.860 136.057 97.891  1.00 11.51 ?  578 ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 578 ? 138.147 135.396 99.064  1.00 8.57  ?  578 ILE A C     1 
ATOM   4651  O  O     . ILE A 1 578 ? 138.719 134.564 99.772  1.00 10.89 ?  578 ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 578 ? 139.617 135.042 97.032  1.00 12.84 ?  578 ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 578 ? 140.407 135.767 95.941  1.00 0.32  ?  578 ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 578 ? 138.650 134.053 96.409  1.00 8.42  ?  578 ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 578 ? 140.911 134.860 94.852  1.00 9.81  ?  578 ILE A CD1   1 
ATOM   4656  N  N     . ALA A 1 579 ? 136.889 135.769 99.265  1.00 16.56 ?  579 ALA A N     1 
ATOM   4657  C  CA    . ALA A 1 579 ? 136.012 135.258 100.304 1.00 8.89  ?  579 ALA A CA    1 
ATOM   4658  C  C     . ALA A 1 579 ? 135.392 133.932 99.877  1.00 16.81 ?  579 ALA A C     1 
ATOM   4659  O  O     . ALA A 1 579 ? 135.373 133.599 98.690  1.00 21.14 ?  579 ALA A O     1 
ATOM   4660  C  CB    . ALA A 1 579 ? 134.919 136.281 100.609 1.00 13.01 ?  579 ALA A CB    1 
ATOM   4661  N  N     . PRO A 1 580 ? 134.898 133.135 100.831 1.00 24.08 ?  580 PRO A N     1 
ATOM   4662  C  CA    . PRO A 1 580 ? 134.286 131.847 100.460 1.00 20.95 ?  580 PRO A CA    1 
ATOM   4663  C  C     . PRO A 1 580 ? 133.078 131.966 99.542  1.00 25.56 ?  580 PRO A C     1 
ATOM   4664  O  O     . PRO A 1 580 ? 132.850 131.058 98.731  1.00 31.34 ?  580 PRO A O     1 
ATOM   4665  C  CB    . PRO A 1 580 ? 133.904 131.234 101.817 1.00 17.28 ?  580 PRO A CB    1 
ATOM   4666  C  CG    . PRO A 1 580 ? 133.993 132.352 102.805 1.00 20.67 ?  580 PRO A CG    1 
ATOM   4667  C  CD    . PRO A 1 580 ? 135.045 133.267 102.289 1.00 20.22 ?  580 PRO A CD    1 
ATOM   4668  N  N     . THR A 1 581 ? 132.299 133.044 99.642  1.00 21.90 ?  581 THR A N     1 
ATOM   4669  C  CA    . THR A 1 581 ? 131.107 133.261 98.816  1.00 27.67 ?  581 THR A CA    1 
ATOM   4670  C  C     . THR A 1 581 ? 130.128 132.091 98.950  1.00 31.22 ?  581 THR A C     1 
ATOM   4671  O  O     . THR A 1 581 ? 129.868 131.340 98.011  1.00 32.14 ?  581 THR A O     1 
ATOM   4672  C  CB    . THR A 1 581 ? 131.474 133.495 97.346  1.00 27.73 ?  581 THR A CB    1 
ATOM   4673  O  OG1   . THR A 1 581 ? 131.750 132.240 96.710  1.00 23.00 ?  581 THR A OG1   1 
ATOM   4674  C  CG2   . THR A 1 581 ? 132.683 134.402 97.225  1.00 28.64 ?  581 THR A CG2   1 
ATOM   4675  N  N     . GLY A 1 582 ? 129.591 131.960 100.160 1.00 28.49 ?  582 GLY A N     1 
ATOM   4676  C  CA    . GLY A 1 582 ? 128.751 130.829 100.504 1.00 31.03 ?  582 GLY A CA    1 
ATOM   4677  C  C     . GLY A 1 582 ? 127.472 130.684 99.703  1.00 34.80 ?  582 GLY A C     1 
ATOM   4678  O  O     . GLY A 1 582 ? 127.335 129.737 98.922  1.00 33.60 ?  582 GLY A O     1 
ATOM   4679  N  N     . SER A 1 583 ? 126.529 131.609 99.876  1.00 34.42 ?  583 SER A N     1 
ATOM   4680  C  CA    . SER A 1 583 ? 125.212 131.477 99.267  1.00 38.66 ?  583 SER A CA    1 
ATOM   4681  C  C     . SER A 1 583 ? 125.035 132.299 98.000  1.00 35.70 ?  583 SER A C     1 
ATOM   4682  O  O     . SER A 1 583 ? 124.166 131.972 97.186  1.00 34.27 ?  583 SER A O     1 
ATOM   4683  C  CB    . SER A 1 583 ? 124.120 131.869 100.269 1.00 40.58 ?  583 SER A CB    1 
ATOM   4684  O  OG    . SER A 1 583 ? 123.950 130.865 101.254 1.00 41.67 ?  583 SER A OG    1 
ATOM   4685  N  N     . ILE A 1 584 ? 125.827 133.357 97.808  1.00 32.67 ?  584 ILE A N     1 
ATOM   4686  C  CA    . ILE A 1 584 ? 125.718 134.140 96.583  1.00 26.88 ?  584 ILE A CA    1 
ATOM   4687  C  C     . ILE A 1 584 ? 126.175 133.349 95.366  1.00 29.09 ?  584 ILE A C     1 
ATOM   4688  O  O     . ILE A 1 584 ? 125.792 133.679 94.240  1.00 36.37 ?  584 ILE A O     1 
ATOM   4689  C  CB    . ILE A 1 584 ? 126.512 135.456 96.700  1.00 33.33 ?  584 ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1 584 ? 127.975 135.173 97.048  1.00 34.20 ?  584 ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1 584 ? 125.865 136.381 97.719  1.00 34.09 ?  584 ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1 584 ? 128.731 136.381 97.558  1.00 28.91 ?  584 ILE A CD1   1 
ATOM   4693  N  N     . SER A 1 585 ? 126.991 132.311 95.563  1.00 30.54 ?  585 SER A N     1 
ATOM   4694  C  CA    . SER A 1 585 ? 127.400 131.472 94.442  1.00 27.64 ?  585 SER A CA    1 
ATOM   4695  C  C     . SER A 1 585 ? 126.222 130.698 93.866  1.00 26.77 ?  585 SER A C     1 
ATOM   4696  O  O     . SER A 1 585 ? 126.215 130.381 92.671  1.00 27.43 ?  585 SER A O     1 
ATOM   4697  C  CB    . SER A 1 585 ? 128.506 130.514 94.878  1.00 24.39 ?  585 SER A CB    1 
ATOM   4698  O  OG    . SER A 1 585 ? 128.079 129.698 95.954  1.00 31.13 ?  585 SER A OG    1 
ATOM   4699  N  N     . TYR A 1 586 ? 125.227 130.376 94.696  1.00 34.80 ?  586 TYR A N     1 
ATOM   4700  C  CA    . TYR A 1 586 ? 124.017 129.735 94.193  1.00 33.30 ?  586 TYR A CA    1 
ATOM   4701  C  C     . TYR A 1 586 ? 123.241 130.678 93.285  1.00 31.89 ?  586 TYR A C     1 
ATOM   4702  O  O     . TYR A 1 586 ? 122.876 130.313 92.162  1.00 35.40 ?  586 TYR A O     1 
ATOM   4703  C  CB    . TYR A 1 586 ? 123.139 129.285 95.359  1.00 32.22 ?  586 TYR A CB    1 
ATOM   4704  C  CG    . TYR A 1 586 ? 123.650 128.078 96.108  1.00 30.72 ?  586 TYR A CG    1 
ATOM   4705  C  CD1   . TYR A 1 586 ? 123.991 128.169 97.451  1.00 33.44 ?  586 TYR A CD1   1 
ATOM   4706  C  CD2   . TYR A 1 586 ? 123.782 126.848 95.481  1.00 34.07 ?  586 TYR A CD2   1 
ATOM   4707  C  CE1   . TYR A 1 586 ? 124.457 127.071 98.145  1.00 35.12 ?  586 TYR A CE1   1 
ATOM   4708  C  CE2   . TYR A 1 586 ? 124.247 125.743 96.168  1.00 34.78 ?  586 TYR A CE2   1 
ATOM   4709  C  CZ    . TYR A 1 586 ? 124.582 125.860 97.500  1.00 36.82 ?  586 TYR A CZ    1 
ATOM   4710  O  OH    . TYR A 1 586 ? 125.046 124.765 98.190  1.00 38.57 ?  586 TYR A OH    1 
ATOM   4711  N  N     . VAL A 1 587 ? 122.992 131.903 93.754  1.00 29.42 ?  587 VAL A N     1 
ATOM   4712  C  CA    . VAL A 1 587 ? 122.197 132.864 92.995  1.00 27.19 ?  587 VAL A CA    1 
ATOM   4713  C  C     . VAL A 1 587 ? 122.873 133.193 91.672  1.00 29.12 ?  587 VAL A C     1 
ATOM   4714  O  O     . VAL A 1 587 ? 122.208 133.371 90.643  1.00 34.89 ?  587 VAL A O     1 
ATOM   4715  C  CB    . VAL A 1 587 ? 121.951 134.130 93.836  1.00 31.21 ?  587 VAL A CB    1 
ATOM   4716  C  CG1   . VAL A 1 587 ? 121.074 135.110 93.082  1.00 31.59 ?  587 VAL A CG1   1 
ATOM   4717  C  CG2   . VAL A 1 587 ? 121.327 133.764 95.172  1.00 33.64 ?  587 VAL A CG2   1 
ATOM   4718  N  N     . GLN A 1 588 ? 124.199 133.274 91.673  1.00 31.49 ?  588 GLN A N     1 
ATOM   4719  C  CA    . GLN A 1 588 ? 124.952 133.561 90.461  1.00 26.60 ?  588 GLN A CA    1 
ATOM   4720  C  C     . GLN A 1 588 ? 125.179 132.328 89.603  1.00 28.18 ?  588 GLN A C     1 
ATOM   4721  O  O     . GLN A 1 588 ? 125.787 132.447 88.532  1.00 29.80 ?  588 GLN A O     1 
ATOM   4722  C  CB    . GLN A 1 588 ? 126.297 134.194 90.819  1.00 24.80 ?  588 GLN A CB    1 
ATOM   4723  C  CG    . GLN A 1 588 ? 126.184 135.592 91.394  1.00 23.53 ?  588 GLN A CG    1 
ATOM   4724  C  CD    . GLN A 1 588 ? 126.400 136.663 90.348  1.00 26.75 ?  588 GLN A CD    1 
ATOM   4725  O  OE1   . GLN A 1 588 ? 127.240 136.518 89.461  1.00 24.74 ?  588 GLN A OE1   1 
ATOM   4726  N  NE2   . GLN A 1 588 ? 125.644 137.749 90.448  1.00 32.10 ?  588 GLN A NE2   1 
ATOM   4727  N  N     . SER A 1 589 ? 124.700 131.163 90.037  1.00 29.68 ?  589 SER A N     1 
ATOM   4728  C  CA    . SER A 1 589 ? 124.940 129.891 89.361  1.00 26.27 ?  589 SER A CA    1 
ATOM   4729  C  C     . SER A 1 589 ? 126.434 129.709 89.097  1.00 28.13 ?  589 SER A C     1 
ATOM   4730  O  O     . SER A 1 589 ? 126.895 129.606 87.959  1.00 30.35 ?  589 SER A O     1 
ATOM   4731  C  CB    . SER A 1 589 ? 124.123 129.790 88.069  1.00 28.07 ?  589 SER A CB    1 
ATOM   4732  O  OG    . SER A 1 589 ? 124.732 130.513 87.015  1.00 34.21 ?  589 SER A OG    1 
ATOM   4733  N  N     . SER A 1 590 ? 127.189 129.680 90.191  1.00 27.77 ?  590 SER A N     1 
ATOM   4734  C  CA    . SER A 1 590 ? 128.639 129.650 90.134  1.00 22.98 ?  590 SER A CA    1 
ATOM   4735  C  C     . SER A 1 590 ? 129.167 128.719 91.212  1.00 24.82 ?  590 SER A C     1 
ATOM   4736  O  O     . SER A 1 590 ? 128.505 128.460 92.220  1.00 29.39 ?  590 SER A O     1 
ATOM   4737  C  CB    . SER A 1 590 ? 129.230 131.054 90.314  1.00 22.09 ?  590 SER A CB    1 
ATOM   4738  O  OG    . SER A 1 590 ? 129.538 131.306 91.672  1.00 29.32 ?  590 SER A OG    1 
ATOM   4739  N  N     . THR A 1 591 ? 130.372 128.205 90.984  1.00 23.96 ?  591 THR A N     1 
ATOM   4740  C  CA    . THR A 1 591 ? 131.069 127.453 92.012  1.00 24.18 ?  591 THR A CA    1 
ATOM   4741  C  C     . THR A 1 591 ? 131.624 128.407 93.062  1.00 23.05 ?  591 THR A C     1 
ATOM   4742  O  O     . THR A 1 591 ? 131.977 129.552 92.767  1.00 17.67 ?  591 THR A O     1 
ATOM   4743  C  CB    . THR A 1 591 ? 132.193 126.613 91.404  1.00 26.23 ?  591 THR A CB    1 
ATOM   4744  O  OG1   . THR A 1 591 ? 133.265 127.467 90.990  1.00 30.00 ?  591 THR A OG1   1 
ATOM   4745  C  CG2   . THR A 1 591 ? 131.679 125.840 90.202  1.00 25.88 ?  591 THR A CG2   1 
ATOM   4746  N  N     . ALA A 1 592 ? 131.694 127.926 94.300  1.00 22.30 ?  592 ALA A N     1 
ATOM   4747  C  CA    . ALA A 1 592 ? 132.029 128.797 95.418  1.00 22.38 ?  592 ALA A CA    1 
ATOM   4748  C  C     . ALA A 1 592 ? 133.501 129.182 95.387  1.00 22.73 ?  592 ALA A C     1 
ATOM   4749  O  O     . ALA A 1 592 ? 134.380 128.316 95.372  1.00 27.19 ?  592 ALA A O     1 
ATOM   4750  C  CB    . ALA A 1 592 ? 131.690 128.112 96.741  1.00 24.34 ?  592 ALA A CB    1 
ATOM   4751  N  N     . SER A 1 593 ? 133.760 130.484 95.382  1.00 24.21 ?  593 SER A N     1 
ATOM   4752  C  CA    . SER A 1 593 ? 135.101 131.061 95.492  1.00 16.30 ?  593 SER A CA    1 
ATOM   4753  C  C     . SER A 1 593 ? 135.988 130.508 94.375  1.00 15.94 ?  593 SER A C     1 
ATOM   4754  O  O     . SER A 1 593 ? 135.502 130.121 93.307  1.00 23.75 ?  593 SER A O     1 
ATOM   4755  C  CB    . SER A 1 593 ? 135.625 130.817 96.897  1.00 25.18 ?  593 SER A CB    1 
ATOM   4756  O  OG    . SER A 1 593 ? 136.781 131.590 97.156  1.00 24.78 ?  593 SER A OG    1 
ATOM   4757  N  N     . VAL A 1 594 ? 137.299 130.477 94.607  1.00 21.63 ?  594 VAL A N     1 
ATOM   4758  C  CA    . VAL A 1 594 ? 138.235 129.822 93.705  1.00 19.48 ?  594 VAL A CA    1 
ATOM   4759  C  C     . VAL A 1 594 ? 138.483 128.375 94.112  1.00 18.95 ?  594 VAL A C     1 
ATOM   4760  O  O     . VAL A 1 594 ? 139.366 127.717 93.556  1.00 18.36 ?  594 VAL A O     1 
ATOM   4761  C  CB    . VAL A 1 594 ? 139.557 130.599 93.619  1.00 21.54 ?  594 VAL A CB    1 
ATOM   4762  C  CG1   . VAL A 1 594 ? 139.332 131.953 92.963  1.00 9.11  ?  594 VAL A CG1   1 
ATOM   4763  C  CG2   . VAL A 1 594 ? 140.165 130.763 95.000  1.00 17.90 ?  594 VAL A CG2   1 
ATOM   4764  N  N     . MET A 1 595 ? 137.723 127.869 95.079  1.00 25.45 ?  595 MET A N     1 
ATOM   4765  C  CA    . MET A 1 595 ? 137.867 126.493 95.513  1.00 18.76 ?  595 MET A CA    1 
ATOM   4766  C  C     . MET A 1 595 ? 137.342 125.540 94.441  1.00 24.58 ?  595 MET A C     1 
ATOM   4767  O  O     . MET A 1 595 ? 136.440 125.887 93.674  1.00 32.18 ?  595 MET A O     1 
ATOM   4768  C  CB    . MET A 1 595 ? 137.100 126.262 96.813  1.00 22.37 ?  595 MET A CB    1 
ATOM   4769  C  CG    . MET A 1 595 ? 137.768 126.670 98.144  1.00 25.47 ?  595 MET A CG    1 
ATOM   4770  S  SD    . MET A 1 595 ? 139.523 126.345 98.461  1.00 31.61 ?  595 MET A SD    1 
ATOM   4771  C  CE    . MET A 1 595 ? 140.361 127.583 97.478  1.00 18.71 ?  595 MET A CE    1 
ATOM   4772  N  N     . PRO A 1 596 ? 137.897 124.334 94.362  1.00 27.55 ?  596 PRO A N     1 
ATOM   4773  C  CA    . PRO A 1 596 ? 137.274 123.292 93.541  1.00 22.18 ?  596 PRO A CA    1 
ATOM   4774  C  C     . PRO A 1 596 ? 135.976 122.811 94.170  1.00 27.22 ?  596 PRO A C     1 
ATOM   4775  O  O     . PRO A 1 596 ? 135.755 122.926 95.378  1.00 31.05 ?  596 PRO A O     1 
ATOM   4776  C  CB    . PRO A 1 596 ? 138.328 122.181 93.512  1.00 23.92 ?  596 PRO A CB    1 
ATOM   4777  C  CG    . PRO A 1 596 ? 139.148 122.406 94.736  1.00 28.34 ?  596 PRO A CG    1 
ATOM   4778  C  CD    . PRO A 1 596 ? 139.161 123.885 94.970  1.00 28.46 ?  596 PRO A CD    1 
ATOM   4779  N  N     . ILE A 1 597 ? 135.102 122.269 93.321  1.00 29.21 ?  597 ILE A N     1 
ATOM   4780  C  CA    . ILE A 1 597 ? 133.790 121.836 93.784  1.00 31.33 ?  597 ILE A CA    1 
ATOM   4781  C  C     . ILE A 1 597 ? 133.932 120.630 94.706  1.00 34.65 ?  597 ILE A C     1 
ATOM   4782  O  O     . ILE A 1 597 ? 134.773 119.745 94.496  1.00 36.12 ?  597 ILE A O     1 
ATOM   4783  C  CB    . ILE A 1 597 ? 132.866 121.522 92.593  1.00 32.00 ?  597 ILE A CB    1 
ATOM   4784  C  CG1   . ILE A 1 597 ? 133.395 120.327 91.795  1.00 31.16 ?  597 ILE A CG1   1 
ATOM   4785  C  CG2   . ILE A 1 597 ? 132.731 122.735 91.696  1.00 31.63 ?  597 ILE A CG2   1 
ATOM   4786  C  CD1   . ILE A 1 597 ? 132.330 119.593 91.019  1.00 31.93 ?  597 ILE A CD1   1 
ATOM   4787  N  N     . MET A 1 598 ? 133.105 120.600 95.751  1.00 39.86 ?  598 MET A N     1 
ATOM   4788  C  CA    . MET A 1 598 ? 133.113 119.469 96.669  1.00 38.55 ?  598 MET A CA    1 
ATOM   4789  C  C     . MET A 1 598 ? 132.366 118.276 96.088  1.00 38.59 ?  598 MET A C     1 
ATOM   4790  O  O     . MET A 1 598 ? 132.832 117.137 96.189  1.00 44.29 ?  598 MET A O     1 
ATOM   4791  C  CB    . MET A 1 598 ? 132.505 119.878 98.009  1.00 37.06 ?  598 MET A CB    1 
ATOM   4792  C  CG    . MET A 1 598 ? 133.486 120.538 98.958  1.00 35.00 ?  598 MET A CG    1 
ATOM   4793  S  SD    . MET A 1 598 ? 132.684 121.229 100.416 1.00 53.18 ?  598 MET A SD    1 
ATOM   4794  C  CE    . MET A 1 598 ? 131.714 122.538 99.675  1.00 39.51 ?  598 MET A CE    1 
ATOM   4795  N  N     . GLU A 1 599 ? 131.205 118.521 95.486  1.00 38.15 ?  599 GLU A N     1 
ATOM   4796  C  CA    . GLU A 1 599 ? 130.399 117.487 94.858  1.00 37.01 ?  599 GLU A CA    1 
ATOM   4797  C  C     . GLU A 1 599 ? 129.947 117.971 93.490  1.00 36.30 ?  599 GLU A C     1 
ATOM   4798  O  O     . GLU A 1 599 ? 129.750 119.168 93.274  1.00 40.49 ?  599 GLU A O     1 
ATOM   4799  C  CB    . GLU A 1 599 ? 129.171 117.127 95.710  1.00 38.85 ?  599 GLU A CB    1 
ATOM   4800  C  CG    . GLU A 1 599 ? 129.446 117.025 97.202  1.00 39.53 ?  599 GLU A CG    1 
ATOM   4801  C  CD    . GLU A 1 599 ? 128.221 117.324 98.043  1.00 43.17 ?  599 GLU A CD    1 
ATOM   4802  O  OE1   . GLU A 1 599 ? 127.899 118.517 98.226  1.00 40.97 ?  599 GLU A OE1   1 
ATOM   4803  O  OE2   . GLU A 1 599 ? 127.579 116.366 98.523  1.00 45.94 -1 599 GLU A OE2   1 
ATOM   4804  N  N     . ARG A 1 600 ? 129.790 117.030 92.557  1.00 38.66 ?  600 ARG A N     1 
ATOM   4805  C  CA    . ARG A 1 600 ? 129.261 117.389 91.246  1.00 35.38 ?  600 ARG A CA    1 
ATOM   4806  C  C     . ARG A 1 600 ? 127.787 117.760 91.342  1.00 34.16 ?  600 ARG A C     1 
ATOM   4807  O  O     . ARG A 1 600 ? 127.352 118.776 90.788  1.00 37.87 ?  600 ARG A O     1 
ATOM   4808  C  CB    . ARG A 1 600 ? 129.467 116.240 90.262  1.00 34.71 ?  600 ARG A CB    1 
ATOM   4809  C  CG    . ARG A 1 600 ? 130.870 116.164 89.707  1.00 35.12 ?  600 ARG A CG    1 
ATOM   4810  C  CD    . ARG A 1 600 ? 130.973 115.101 88.639  1.00 34.48 ?  600 ARG A CD    1 
ATOM   4811  N  NE    . ARG A 1 600 ? 132.322 114.995 88.097  1.00 34.15 ?  600 ARG A NE    1 
ATOM   4812  C  CZ    . ARG A 1 600 ? 133.290 114.272 88.642  1.00 37.48 ?  600 ARG A CZ    1 
ATOM   4813  N  NH1   . ARG A 1 600 ? 133.096 113.585 89.755  1.00 36.61 1  600 ARG A NH1   1 
ATOM   4814  N  NH2   . ARG A 1 600 ? 134.483 114.239 88.055  1.00 37.83 ?  600 ARG A NH2   1 
ATOM   4815  N  N     . ILE A 1 601 ? 127.005 116.941 92.037  1.00 39.12 ?  601 ILE A N     1 
ATOM   4816  C  CA    . ILE A 1 601 ? 125.615 117.239 92.355  1.00 41.28 ?  601 ILE A CA    1 
ATOM   4817  C  C     . ILE A 1 601 ? 125.473 117.153 93.866  1.00 40.35 ?  601 ILE A C     1 
ATOM   4818  O  O     . ILE A 1 601 ? 125.812 116.126 94.469  1.00 41.59 ?  601 ILE A O     1 
ATOM   4819  C  CB    . ILE A 1 601 ? 124.644 116.275 91.657  1.00 40.71 ?  601 ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1 601 ? 124.916 116.235 90.152  1.00 41.03 ?  601 ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1 601 ? 123.206 116.686 91.924  1.00 37.03 ?  601 ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1 601 ? 124.184 115.130 89.432  1.00 39.55 ?  601 ILE A CD1   1 
ATOM   4823  N  N     . GLU A 1 602 ? 124.981 118.223 94.477  1.00 45.16 ?  602 GLU A N     1 
ATOM   4824  C  CA    . GLU A 1 602 ? 124.820 118.283 95.921  1.00 47.44 ?  602 GLU A CA    1 
ATOM   4825  C  C     . GLU A 1 602 ? 123.363 118.066 96.304  1.00 48.63 ?  602 GLU A C     1 
ATOM   4826  O  O     . GLU A 1 602 ? 122.451 118.629 95.689  1.00 48.67 ?  602 GLU A O     1 
ATOM   4827  C  CB    . GLU A 1 602 ? 125.323 119.618 96.479  1.00 45.19 ?  602 GLU A CB    1 
ATOM   4828  C  CG    . GLU A 1 602 ? 124.743 120.844 95.806  1.00 47.09 ?  602 GLU A CG    1 
ATOM   4829  C  CD    . GLU A 1 602 ? 125.108 122.126 96.527  1.00 50.58 ?  602 GLU A CD    1 
ATOM   4830  O  OE1   . GLU A 1 602 ? 126.260 122.584 96.382  1.00 50.27 ?  602 GLU A OE1   1 
ATOM   4831  O  OE2   . GLU A 1 602 ? 124.241 122.676 97.239  1.00 51.85 -1 602 GLU A OE2   1 
ATOM   4832  N  N     . GLU A 1 603 ? 123.155 117.232 97.317  1.00 56.87 ?  603 GLU A N     1 
ATOM   4833  C  CA    . GLU A 1 603 ? 121.833 116.916 97.837  1.00 57.73 ?  603 GLU A CA    1 
ATOM   4834  C  C     . GLU A 1 603 ? 121.587 117.718 99.107  1.00 57.59 ?  603 GLU A C     1 
ATOM   4835  O  O     . GLU A 1 603 ? 122.386 117.660 100.047 1.00 57.50 ?  603 GLU A O     1 
ATOM   4836  C  CB    . GLU A 1 603 ? 121.713 115.419 98.125  1.00 57.17 ?  603 GLU A CB    1 
ATOM   4837  C  CG    . GLU A 1 603 ? 120.364 114.990 98.666  1.00 58.95 ?  603 GLU A CG    1 
ATOM   4838  C  CD    . GLU A 1 603 ? 120.468 113.809 99.609  1.00 60.15 ?  603 GLU A CD    1 
ATOM   4839  O  OE1   . GLU A 1 603 ? 120.766 114.025 100.803 1.00 60.48 ?  603 GLU A OE1   1 
ATOM   4840  O  OE2   . GLU A 1 603 ? 120.253 112.666 99.158  1.00 59.56 -1 603 GLU A OE2   1 
ATOM   4841  N  N     . ARG A 1 604 ? 120.484 118.462 99.134  1.00 58.62 ?  604 ARG A N     1 
ATOM   4842  C  CA    . ARG A 1 604 ? 120.138 119.282 100.283 1.00 59.06 ?  604 ARG A CA    1 
ATOM   4843  C  C     . ARG A 1 604 ? 118.727 118.951 100.745 1.00 59.92 ?  604 ARG A C     1 
ATOM   4844  O  O     . ARG A 1 604 ? 117.900 118.466 99.971  1.00 59.33 ?  604 ARG A O     1 
ATOM   4845  C  CB    . ARG A 1 604 ? 120.250 120.778 99.965  1.00 58.99 ?  604 ARG A CB    1 
ATOM   4846  C  CG    . ARG A 1 604 ? 121.626 121.204 99.486  1.00 58.38 ?  604 ARG A CG    1 
ATOM   4847  C  CD    . ARG A 1 604 ? 122.494 121.663 100.645 1.00 58.50 ?  604 ARG A CD    1 
ATOM   4848  N  NE    . ARG A 1 604 ? 123.425 120.625 101.072 1.00 58.72 ?  604 ARG A NE    1 
ATOM   4849  C  CZ    . ARG A 1 604 ? 124.655 120.481 100.599 1.00 59.29 ?  604 ARG A CZ    1 
ATOM   4850  N  NH1   . ARG A 1 604 ? 125.141 121.294 99.676  1.00 57.85 1  604 ARG A NH1   1 
ATOM   4851  N  NH2   . ARG A 1 604 ? 125.417 119.494 101.062 1.00 57.26 ?  604 ARG A NH2   1 
ATOM   4852  N  N     . THR A 1 605 ? 118.467 119.204 102.024 1.00 65.73 ?  605 THR A N     1 
ATOM   4853  C  CA    . THR A 1 605 ? 117.162 118.961 102.630 1.00 66.61 ?  605 THR A CA    1 
ATOM   4854  C  C     . THR A 1 605 ? 116.617 120.286 103.143 1.00 66.54 ?  605 THR A C     1 
ATOM   4855  O  O     . THR A 1 605 ? 117.153 120.855 104.100 1.00 65.70 ?  605 THR A O     1 
ATOM   4856  C  CB    . THR A 1 605 ? 117.261 117.937 103.761 1.00 66.19 ?  605 THR A CB    1 
ATOM   4857  O  OG1   . THR A 1 605 ? 117.873 116.738 103.273 1.00 66.36 ?  605 THR A OG1   1 
ATOM   4858  C  CG2   . THR A 1 605 ? 115.878 117.610 104.304 1.00 66.87 ?  605 THR A CG2   1 
ATOM   4859  N  N     . TYR A 1 606 ? 115.556 120.778 102.510 1.00 66.48 ?  606 TYR A N     1 
ATOM   4860  C  CA    . TYR A 1 606 ? 114.871 121.986 102.947 1.00 68.28 ?  606 TYR A CA    1 
ATOM   4861  C  C     . TYR A 1 606 ? 113.475 121.615 103.422 1.00 70.28 ?  606 TYR A C     1 
ATOM   4862  O  O     . TYR A 1 606 ? 112.708 120.989 102.680 1.00 69.13 ?  606 TYR A O     1 
ATOM   4863  C  CB    . TYR A 1 606 ? 114.801 123.024 101.823 1.00 66.57 ?  606 TYR A CB    1 
ATOM   4864  C  CG    . TYR A 1 606 ? 116.153 123.554 101.403 1.00 68.29 ?  606 TYR A CG    1 
ATOM   4865  C  CD1   . TYR A 1 606 ? 116.926 124.311 102.274 1.00 66.92 ?  606 TYR A CD1   1 
ATOM   4866  C  CD2   . TYR A 1 606 ? 116.654 123.303 100.135 1.00 67.97 ?  606 TYR A CD2   1 
ATOM   4867  C  CE1   . TYR A 1 606 ? 118.162 124.798 101.893 1.00 66.54 ?  606 TYR A CE1   1 
ATOM   4868  C  CE2   . TYR A 1 606 ? 117.888 123.786 99.745  1.00 65.78 ?  606 TYR A CE2   1 
ATOM   4869  C  CZ    . TYR A 1 606 ? 118.638 124.532 100.626 1.00 67.46 ?  606 TYR A CZ    1 
ATOM   4870  O  OH    . TYR A 1 606 ? 119.867 125.014 100.238 1.00 66.96 ?  606 TYR A OH    1 
ATOM   4871  N  N     . GLY A 1 607 ? 113.148 122.006 104.650 1.00 75.36 ?  607 GLY A N     1 
ATOM   4872  C  CA    . GLY A 1 607 ? 111.911 121.537 105.251 1.00 74.97 ?  607 GLY A CA    1 
ATOM   4873  C  C     . GLY A 1 607 ? 111.929 120.026 105.344 1.00 75.53 ?  607 GLY A C     1 
ATOM   4874  O  O     . GLY A 1 607 ? 112.863 119.424 105.884 1.00 75.04 ?  607 GLY A O     1 
ATOM   4875  N  N     . ASN A 1 608 ? 110.885 119.396 104.807 1.00 78.59 ?  608 ASN A N     1 
ATOM   4876  C  CA    . ASN A 1 608 ? 110.820 117.946 104.696 1.00 80.29 ?  608 ASN A CA    1 
ATOM   4877  C  C     . ASN A 1 608 ? 111.006 117.477 103.257 1.00 79.21 ?  608 ASN A C     1 
ATOM   4878  O  O     . ASN A 1 608 ? 110.608 116.359 102.915 1.00 78.37 ?  608 ASN A O     1 
ATOM   4879  C  CB    . ASN A 1 608 ? 109.497 117.427 105.261 1.00 79.45 ?  608 ASN A CB    1 
ATOM   4880  C  CG    . ASN A 1 608 ? 109.470 117.436 106.777 1.00 79.47 ?  608 ASN A CG    1 
ATOM   4881  O  OD1   . ASN A 1 608 ? 110.500 117.618 107.427 1.00 79.06 ?  608 ASN A OD1   1 
ATOM   4882  N  ND2   . ASN A 1 608 ? 108.289 117.237 107.349 1.00 78.01 ?  608 ASN A ND2   1 
ATOM   4883  N  N     . SER A 1 609 ? 111.607 118.310 102.411 1.00 73.08 ?  609 SER A N     1 
ATOM   4884  C  CA    . SER A 1 609 ? 111.767 118.017 100.997 1.00 72.48 ?  609 SER A CA    1 
ATOM   4885  C  C     . SER A 1 609 ? 113.244 117.941 100.635 1.00 73.03 ?  609 SER A C     1 
ATOM   4886  O  O     . SER A 1 609 ? 114.090 118.598 101.250 1.00 72.83 ?  609 SER A O     1 
ATOM   4887  C  CB    . SER A 1 609 ? 111.076 119.076 100.133 1.00 71.53 ?  609 SER A CB    1 
ATOM   4888  O  OG    . SER A 1 609 ? 111.644 120.357 100.345 1.00 70.80 ?  609 SER A OG    1 
ATOM   4889  N  N     . LYS A 1 610 ? 113.544 117.119 99.634  1.00 65.08 ?  610 LYS A N     1 
ATOM   4890  C  CA    . LYS A 1 610 ? 114.900 116.941 99.139  1.00 62.96 ?  610 LYS A CA    1 
ATOM   4891  C  C     . LYS A 1 610 ? 115.068 117.692 97.825  1.00 63.45 ?  610 LYS A C     1 
ATOM   4892  O  O     . LYS A 1 610 ? 114.138 117.766 97.017  1.00 64.05 ?  610 LYS A O     1 
ATOM   4893  C  CB    . LYS A 1 610 ? 115.218 115.458 98.940  1.00 62.17 ?  610 LYS A CB    1 
ATOM   4894  C  CG    . LYS A 1 610 ? 116.701 115.131 98.959  1.00 63.41 ?  610 LYS A CG    1 
ATOM   4895  C  CD    . LYS A 1 610 ? 116.975 113.894 99.802  1.00 64.78 ?  610 LYS A CD    1 
ATOM   4896  C  CE    . LYS A 1 610 ? 117.053 114.232 101.283 1.00 64.27 ?  610 LYS A CE    1 
ATOM   4897  N  NZ    . LYS A 1 610 ? 118.352 114.853 101.656 1.00 62.54 1  610 LYS A NZ    1 
ATOM   4898  N  N     . THR A 1 611 ? 116.257 118.251 97.618  1.00 61.72 ?  611 THR A N     1 
ATOM   4899  C  CA    . THR A 1 611 ? 116.552 119.015 96.418  1.00 58.73 ?  611 THR A CA    1 
ATOM   4900  C  C     . THR A 1 611 ? 117.960 118.686 95.946  1.00 57.57 ?  611 THR A C     1 
ATOM   4901  O  O     . THR A 1 611 ? 118.827 118.283 96.728  1.00 56.69 ?  611 THR A O     1 
ATOM   4902  C  CB    . THR A 1 611 ? 116.407 120.522 96.656  1.00 58.99 ?  611 THR A CB    1 
ATOM   4903  O  OG1   . THR A 1 611 ? 116.631 121.225 95.429  1.00 61.87 ?  611 THR A OG1   1 
ATOM   4904  C  CG2   . THR A 1 611 ? 117.406 120.988 97.693  1.00 59.35 ?  611 THR A CG2   1 
ATOM   4905  N  N     . TYR A 1 612 ? 118.176 118.873 94.647  1.00 53.41 ?  612 TYR A N     1 
ATOM   4906  C  CA    . TYR A 1 612 ? 119.394 118.439 93.975  1.00 51.64 ?  612 TYR A CA    1 
ATOM   4907  C  C     . TYR A 1 612 ? 119.944 119.604 93.169  1.00 54.03 ?  612 TYR A C     1 
ATOM   4908  O  O     . TYR A 1 612 ? 119.253 120.132 92.292  1.00 56.09 ?  612 TYR A O     1 
ATOM   4909  C  CB    . TYR A 1 612 ? 119.096 117.244 93.065  1.00 53.90 ?  612 TYR A CB    1 
ATOM   4910  C  CG    . TYR A 1 612 ? 118.805 115.971 93.824  1.00 55.12 ?  612 TYR A CG    1 
ATOM   4911  C  CD1   . TYR A 1 612 ? 119.682 115.494 94.786  1.00 54.59 ?  612 TYR A CD1   1 
ATOM   4912  C  CD2   . TYR A 1 612 ? 117.621 115.277 93.617  1.00 54.58 ?  612 TYR A CD2   1 
ATOM   4913  C  CE1   . TYR A 1 612 ? 119.409 114.337 95.486  1.00 55.95 ?  612 TYR A CE1   1 
ATOM   4914  C  CE2   . TYR A 1 612 ? 117.334 114.123 94.320  1.00 55.96 ?  612 TYR A CE2   1 
ATOM   4915  C  CZ    . TYR A 1 612 ? 118.233 113.657 95.253  1.00 57.43 ?  612 TYR A CZ    1 
ATOM   4916  O  OH    . TYR A 1 612 ? 117.959 112.507 95.958  1.00 58.99 ?  612 TYR A OH    1 
ATOM   4917  N  N     . TYR A 1 613 ? 121.177 120.007 93.463  1.00 46.07 ?  613 TYR A N     1 
ATOM   4918  C  CA    . TYR A 1 613 ? 121.839 121.084 92.728  1.00 40.41 ?  613 TYR A CA    1 
ATOM   4919  C  C     . TYR A 1 613 ? 123.065 120.549 92.008  1.00 39.86 ?  613 TYR A C     1 
ATOM   4920  O  O     . TYR A 1 613 ? 124.094 120.273 92.649  1.00 39.39 ?  613 TYR A O     1 
ATOM   4921  C  CB    . TYR A 1 613 ? 122.231 122.228 93.661  1.00 40.96 ?  613 TYR A CB    1 
ATOM   4922  C  CG    . TYR A 1 613 ? 122.916 123.374 92.949  1.00 37.21 ?  613 TYR A CG    1 
ATOM   4923  C  CD1   . TYR A 1 613 ? 122.317 123.999 91.864  1.00 37.85 ?  613 TYR A CD1   1 
ATOM   4924  C  CD2   . TYR A 1 613 ? 124.163 123.827 93.359  1.00 37.53 ?  613 TYR A CD2   1 
ATOM   4925  C  CE1   . TYR A 1 613 ? 122.937 125.046 91.211  1.00 41.31 ?  613 TYR A CE1   1 
ATOM   4926  C  CE2   . TYR A 1 613 ? 124.790 124.873 92.711  1.00 39.98 ?  613 TYR A CE2   1 
ATOM   4927  C  CZ    . TYR A 1 613 ? 124.174 125.478 91.638  1.00 44.91 ?  613 TYR A CZ    1 
ATOM   4928  O  OH    . TYR A 1 613 ? 124.793 126.521 90.989  1.00 41.53 ?  613 TYR A OH    1 
ATOM   4929  N  N     . PRO A 1 614 ? 123.000 120.347 90.696  1.00 41.29 ?  614 PRO A N     1 
ATOM   4930  C  CA    . PRO A 1 614 ? 124.225 120.076 89.940  1.00 38.89 ?  614 PRO A CA    1 
ATOM   4931  C  C     . PRO A 1 614 ? 125.081 121.327 89.853  1.00 39.14 ?  614 PRO A C     1 
ATOM   4932  O  O     . PRO A 1 614 ? 124.584 122.454 89.910  1.00 37.77 ?  614 PRO A O     1 
ATOM   4933  C  CB    . PRO A 1 614 ? 123.712 119.654 88.557  1.00 35.09 ?  614 PRO A CB    1 
ATOM   4934  C  CG    . PRO A 1 614 ? 122.239 119.410 88.728  1.00 39.46 ?  614 PRO A CG    1 
ATOM   4935  C  CD    . PRO A 1 614 ? 121.803 120.296 89.844  1.00 39.99 ?  614 PRO A CD    1 
ATOM   4936  N  N     . MET A 1 615 ? 126.387 121.120 89.722  1.00 37.84 ?  615 MET A N     1 
ATOM   4937  C  CA    . MET A 1 615 ? 127.285 122.246 89.544  1.00 35.62 ?  615 MET A CA    1 
ATOM   4938  C  C     . MET A 1 615 ? 126.986 122.948 88.221  1.00 38.19 ?  615 MET A C     1 
ATOM   4939  O  O     . MET A 1 615 ? 126.560 122.310 87.254  1.00 40.78 ?  615 MET A O     1 
ATOM   4940  C  CB    . MET A 1 615 ? 128.739 121.786 89.604  1.00 36.41 ?  615 MET A CB    1 
ATOM   4941  C  CG    . MET A 1 615 ? 129.253 121.656 91.028  1.00 37.79 ?  615 MET A CG    1 
ATOM   4942  S  SD    . MET A 1 615 ? 128.397 122.806 92.126  1.00 44.79 ?  615 MET A SD    1 
ATOM   4943  C  CE    . MET A 1 615 ? 128.695 122.069 93.727  1.00 37.65 ?  615 MET A CE    1 
ATOM   4944  N  N     . PRO A 1 616 ? 127.167 124.266 88.162  1.00 38.31 ?  616 PRO A N     1 
ATOM   4945  C  CA    . PRO A 1 616 ? 126.742 125.022 86.976  1.00 35.48 ?  616 PRO A CA    1 
ATOM   4946  C  C     . PRO A 1 616 ? 127.452 124.548 85.718  1.00 36.21 ?  616 PRO A C     1 
ATOM   4947  O  O     . PRO A 1 616 ? 128.672 124.375 85.698  1.00 38.12 ?  616 PRO A O     1 
ATOM   4948  C  CB    . PRO A 1 616 ? 127.117 126.466 87.327  1.00 36.48 ?  616 PRO A CB    1 
ATOM   4949  C  CG    . PRO A 1 616 ? 127.220 126.481 88.818  1.00 35.50 ?  616 PRO A CG    1 
ATOM   4950  C  CD    . PRO A 1 616 ? 127.732 125.140 89.203  1.00 35.95 ?  616 PRO A CD    1 
ATOM   4951  N  N     . GLY A 1 617 ? 126.674 124.344 84.659  1.00 37.13 ?  617 GLY A N     1 
ATOM   4952  C  CA    . GLY A 1 617 ? 127.222 123.871 83.406  1.00 36.09 ?  617 GLY A CA    1 
ATOM   4953  C  C     . GLY A 1 617 ? 127.614 122.413 83.386  1.00 40.13 ?  617 GLY A C     1 
ATOM   4954  O  O     . GLY A 1 617 ? 128.270 121.978 82.435  1.00 42.08 ?  617 GLY A O     1 
ATOM   4955  N  N     . LEU A 1 618 ? 127.236 121.642 84.403  1.00 41.11 ?  618 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 618 ? 127.596 120.232 84.446  1.00 37.11 ?  618 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 618 ? 126.804 119.451 83.405  1.00 39.55 ?  618 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 618 ? 125.583 119.595 83.296  1.00 44.58 ?  618 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 618 ? 127.347 119.657 85.839  1.00 37.34 ?  618 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 618 ? 127.711 118.186 86.045  1.00 38.46 ?  618 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 618 ? 129.179 117.947 85.740  1.00 38.88 ?  618 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 618 ? 127.379 117.745 87.460  1.00 39.00 ?  618 LEU A CD2   1 
ATOM   4963  N  N     . ALA A 1 619 ? 127.507 118.621 82.640  1.00 45.15 ?  619 ALA A N     1 
ATOM   4964  C  CA    . ALA A 1 619 ? 126.891 117.780 81.629  1.00 45.77 ?  619 ALA A CA    1 
ATOM   4965  C  C     . ALA A 1 619 ? 127.734 116.521 81.483  1.00 49.12 ?  619 ALA A C     1 
ATOM   4966  O  O     . ALA A 1 619 ? 128.674 116.288 82.246  1.00 51.63 ?  619 ALA A O     1 
ATOM   4967  C  CB    . ALA A 1 619 ? 126.751 118.525 80.298  1.00 44.64 ?  619 ALA A CB    1 
ATOM   4968  N  N     . SER A 1 620 ? 127.389 115.701 80.489  1.00 50.10 ?  620 SER A N     1 
ATOM   4969  C  CA    . SER A 1 620 ? 128.158 114.487 80.244  1.00 49.28 ?  620 SER A CA    1 
ATOM   4970  C  C     . SER A 1 620 ? 129.538 114.810 79.686  1.00 49.15 ?  620 SER A C     1 
ATOM   4971  O  O     . SER A 1 620 ? 130.514 114.112 79.987  1.00 51.61 ?  620 SER A O     1 
ATOM   4972  C  CB    . SER A 1 620 ? 127.393 113.568 79.292  1.00 52.72 ?  620 SER A CB    1 
ATOM   4973  O  OG    . SER A 1 620 ? 126.084 113.316 79.771  1.00 54.05 ?  620 SER A OG    1 
ATOM   4974  N  N     . ASN A 1 621 ? 129.642 115.864 78.873  1.00 47.90 ?  621 ASN A N     1 
ATOM   4975  C  CA    . ASN A 1 621 ? 130.920 116.196 78.252  1.00 50.30 ?  621 ASN A CA    1 
ATOM   4976  C  C     . ASN A 1 621 ? 131.920 116.727 79.274  1.00 50.21 ?  621 ASN A C     1 
ATOM   4977  O  O     . ASN A 1 621 ? 133.113 116.415 79.199  1.00 50.40 ?  621 ASN A O     1 
ATOM   4978  C  CB    . ASN A 1 621 ? 130.708 117.209 77.129  1.00 49.26 ?  621 ASN A CB    1 
ATOM   4979  C  CG    . ASN A 1 621 ? 129.572 118.168 77.416  1.00 51.92 ?  621 ASN A CG    1 
ATOM   4980  O  OD1   . ASN A 1 621 ? 129.586 118.883 78.418  1.00 50.98 ?  621 ASN A OD1   1 
ATOM   4981  N  ND2   . ASN A 1 621 ? 128.577 118.186 76.538  1.00 51.57 ?  621 ASN A ND2   1 
ATOM   4982  N  N     . ASN A 1 622 ? 131.455 117.530 80.232  1.00 40.26 ?  622 ASN A N     1 
ATOM   4983  C  CA    . ASN A 1 622 ? 132.329 118.127 81.234  1.00 39.73 ?  622 ASN A CA    1 
ATOM   4984  C  C     . ASN A 1 622 ? 132.178 117.472 82.604  1.00 43.21 ?  622 ASN A C     1 
ATOM   4985  O  O     . ASN A 1 622 ? 132.565 118.067 83.615  1.00 47.91 ?  622 ASN A O     1 
ATOM   4986  C  CB    . ASN A 1 622 ? 132.082 119.635 81.327  1.00 40.12 ?  622 ASN A CB    1 
ATOM   4987  C  CG    . ASN A 1 622 ? 130.627 119.978 81.590  1.00 41.94 ?  622 ASN A CG    1 
ATOM   4988  O  OD1   . ASN A 1 622 ? 129.832 119.126 81.981  1.00 47.40 ?  622 ASN A OD1   1 
ATOM   4989  N  ND2   . ASN A 1 622 ? 130.273 121.238 81.370  1.00 38.35 ?  622 ASN A ND2   1 
ATOM   4990  N  N     . TRP A 1 623 ? 131.617 116.263 82.657  1.00 40.70 ?  623 TRP A N     1 
ATOM   4991  C  CA    . TRP A 1 623 ? 131.509 115.553 83.927  1.00 40.55 ?  623 TRP A CA    1 
ATOM   4992  C  C     . TRP A 1 623 ? 132.887 115.229 84.491  1.00 41.55 ?  623 TRP A C     1 
ATOM   4993  O  O     . TRP A 1 623 ? 133.112 115.332 85.703  1.00 40.00 ?  623 TRP A O     1 
ATOM   4994  C  CB    . TRP A 1 623 ? 130.684 114.278 83.746  1.00 41.25 ?  623 TRP A CB    1 
ATOM   4995  C  CG    . TRP A 1 623 ? 130.608 113.414 84.971  1.00 40.04 ?  623 TRP A CG    1 
ATOM   4996  C  CD1   . TRP A 1 623 ? 131.511 112.472 85.369  1.00 37.86 ?  623 TRP A CD1   1 
ATOM   4997  C  CD2   . TRP A 1 623 ? 129.565 113.408 85.953  1.00 39.38 ?  623 TRP A CD2   1 
ATOM   4998  N  NE1   . TRP A 1 623 ? 131.097 111.884 86.539  1.00 37.74 ?  623 TRP A NE1   1 
ATOM   4999  C  CE2   . TRP A 1 623 ? 129.904 112.439 86.916  1.00 37.65 ?  623 TRP A CE2   1 
ATOM   5000  C  CE3   . TRP A 1 623 ? 128.378 114.129 86.109  1.00 38.03 ?  623 TRP A CE3   1 
ATOM   5001  C  CZ2   . TRP A 1 623 ? 129.101 112.175 88.024  1.00 38.90 ?  623 TRP A CZ2   1 
ATOM   5002  C  CZ3   . TRP A 1 623 ? 127.582 113.865 87.208  1.00 39.91 ?  623 TRP A CZ3   1 
ATOM   5003  C  CH2   . TRP A 1 623 ? 127.947 112.897 88.151  1.00 39.28 ?  623 TRP A CH2   1 
ATOM   5004  N  N     . PHE A 1 624 ? 133.823 114.832 83.626  1.00 43.25 ?  624 PHE A N     1 
ATOM   5005  C  CA    . PHE A 1 624 ? 135.168 114.505 84.081  1.00 43.02 ?  624 PHE A CA    1 
ATOM   5006  C  C     . PHE A 1 624 ? 135.945 115.746 84.502  1.00 41.73 ?  624 PHE A C     1 
ATOM   5007  O  O     . PHE A 1 624 ? 136.732 115.684 85.452  1.00 45.72 ?  624 PHE A O     1 
ATOM   5008  C  CB    . PHE A 1 624 ? 135.908 113.726 82.986  1.00 41.79 ?  624 PHE A CB    1 
ATOM   5009  C  CG    . PHE A 1 624 ? 137.398 113.958 82.955  1.00 45.02 ?  624 PHE A CG    1 
ATOM   5010  C  CD1   . PHE A 1 624 ? 137.944 115.013 82.236  1.00 42.97 ?  624 PHE A CD1   1 
ATOM   5011  C  CD2   . PHE A 1 624 ? 138.252 113.116 83.648  1.00 44.13 ?  624 PHE A CD2   1 
ATOM   5012  C  CE1   . PHE A 1 624 ? 139.309 115.220 82.210  1.00 43.88 ?  624 PHE A CE1   1 
ATOM   5013  C  CE2   . PHE A 1 624 ? 139.618 113.320 83.625  1.00 43.74 ?  624 PHE A CE2   1 
ATOM   5014  C  CZ    . PHE A 1 624 ? 140.146 114.373 82.906  1.00 44.28 ?  624 PHE A CZ    1 
ATOM   5015  N  N     . PHE A 1 625 ? 135.742 116.873 83.814  1.00 35.51 ?  625 PHE A N     1 
ATOM   5016  C  CA    . PHE A 1 625 ? 136.437 118.100 84.183  1.00 34.02 ?  625 PHE A CA    1 
ATOM   5017  C  C     . PHE A 1 625 ? 135.901 118.702 85.474  1.00 33.14 ?  625 PHE A C     1 
ATOM   5018  O  O     . PHE A 1 625 ? 136.607 119.486 86.115  1.00 35.40 ?  625 PHE A O     1 
ATOM   5019  C  CB    . PHE A 1 625 ? 136.344 119.123 83.051  1.00 32.94 ?  625 PHE A CB    1 
ATOM   5020  C  CG    . PHE A 1 625 ? 137.175 118.773 81.852  1.00 34.92 ?  625 PHE A CG    1 
ATOM   5021  C  CD1   . PHE A 1 625 ? 138.554 118.893 81.890  1.00 33.87 ?  625 PHE A CD1   1 
ATOM   5022  C  CD2   . PHE A 1 625 ? 136.579 118.322 80.687  1.00 34.90 ?  625 PHE A CD2   1 
ATOM   5023  C  CE1   . PHE A 1 625 ? 139.323 118.570 80.789  1.00 35.98 ?  625 PHE A CE1   1 
ATOM   5024  C  CE2   . PHE A 1 625 ? 137.341 117.999 79.582  1.00 36.21 ?  625 PHE A CE2   1 
ATOM   5025  C  CZ    . PHE A 1 625 ? 138.715 118.123 79.633  1.00 38.49 ?  625 PHE A CZ    1 
ATOM   5026  N  N     . TYR A 1 626 ? 134.677 118.354 85.871  1.00 29.63 ?  626 TYR A N     1 
ATOM   5027  C  CA    . TYR A 1 626 ? 134.146 118.806 87.150  1.00 32.34 ?  626 TYR A CA    1 
ATOM   5028  C  C     . TYR A 1 626 ? 134.579 117.861 88.262  1.00 31.25 ?  626 TYR A C     1 
ATOM   5029  O  O     . TYR A 1 626 ? 133.745 117.357 89.019  1.00 34.79 ?  626 TYR A O     1 
ATOM   5030  C  CB    . TYR A 1 626 ? 132.621 118.908 87.102  1.00 32.25 ?  626 TYR A CB    1 
ATOM   5031  C  CG    . TYR A 1 626 ? 132.124 120.302 86.802  1.00 31.54 ?  626 TYR A CG    1 
ATOM   5032  C  CD1   . TYR A 1 626 ? 132.242 121.316 87.742  1.00 34.40 ?  626 TYR A CD1   1 
ATOM   5033  C  CD2   . TYR A 1 626 ? 131.536 120.603 85.583  1.00 30.33 ?  626 TYR A CD2   1 
ATOM   5034  C  CE1   . TYR A 1 626 ? 131.793 122.590 87.475  1.00 34.43 ?  626 TYR A CE1   1 
ATOM   5035  C  CE2   . TYR A 1 626 ? 131.081 121.875 85.306  1.00 32.29 ?  626 TYR A CE2   1 
ATOM   5036  C  CZ    . TYR A 1 626 ? 131.214 122.864 86.257  1.00 33.86 ?  626 TYR A CZ    1 
ATOM   5037  O  OH    . TYR A 1 626 ? 130.766 124.135 85.990  1.00 36.02 ?  626 TYR A OH    1 
ATOM   5038  N  N     . LYS A 1 627 ? 135.884 117.623 88.365  1.00 31.15 ?  627 LYS A N     1 
ATOM   5039  C  CA    . LYS A 1 627 ? 136.409 116.720 89.378  1.00 30.24 ?  627 LYS A CA    1 
ATOM   5040  C  C     . LYS A 1 627 ? 136.104 117.248 90.773  1.00 34.65 ?  627 LYS A C     1 
ATOM   5041  O  O     . LYS A 1 627 ? 136.186 118.451 91.031  1.00 40.73 ?  627 LYS A O     1 
ATOM   5042  C  CB    . LYS A 1 627 ? 137.916 116.551 89.189  1.00 35.22 ?  627 LYS A CB    1 
ATOM   5043  C  CG    . LYS A 1 627 ? 138.553 115.490 90.063  1.00 34.08 ?  627 LYS A CG    1 
ATOM   5044  C  CD    . LYS A 1 627 ? 139.990 115.248 89.640  1.00 31.12 ?  627 LYS A CD    1 
ATOM   5045  C  CE    . LYS A 1 627 ? 140.701 114.312 90.597  1.00 36.23 ?  627 LYS A CE    1 
ATOM   5046  N  NZ    . LYS A 1 627 ? 142.158 114.233 90.305  1.00 36.73 1  627 LYS A NZ    1 
ATOM   5047  N  N     . GLU A 1 628 ? 135.733 116.342 91.672  1.00 38.83 ?  628 GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 628 ? 135.440 116.741 93.039  1.00 36.13 ?  628 GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 628 ? 136.723 117.107 93.775  1.00 38.43 ?  628 GLU A C     1 
ATOM   5050  O  O     . GLU A 1 628 ? 137.805 116.590 93.483  1.00 40.81 ?  628 GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 628 ? 134.700 115.626 93.775  1.00 37.33 ?  628 GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 628 ? 133.242 115.493 93.367  1.00 39.57 ?  628 GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 628 ? 132.578 114.268 93.956  1.00 43.19 ?  628 GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 628 ? 133.181 113.632 94.845  1.00 45.12 ?  628 GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 628 ? 131.451 113.940 93.530  1.00 39.83 -1 628 GLU A OE2   1 
ATOM   5056  N  N     . ALA A 1 629 ? 136.590 118.021 94.739  1.00 39.43 ?  629 ALA A N     1 
ATOM   5057  C  CA    . ALA A 1 629 ? 137.760 118.541 95.442  1.00 33.25 ?  629 ALA A CA    1 
ATOM   5058  C  C     . ALA A 1 629 ? 138.470 117.452 96.234  1.00 35.69 ?  629 ALA A C     1 
ATOM   5059  O  O     . ALA A 1 629 ? 139.703 117.437 96.314  1.00 42.03 ?  629 ALA A O     1 
ATOM   5060  C  CB    . ALA A 1 629 ? 137.347 119.689 96.362  1.00 30.29 ?  629 ALA A CB    1 
ATOM   5061  N  N     . TYR A 1 630 ? 137.708 116.536 96.837  1.00 40.56 ?  630 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 630 ? 138.318 115.490 97.650  1.00 36.66 ?  630 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 630 ? 139.152 114.533 96.809  1.00 41.15 ?  630 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 630 ? 140.182 114.036 97.279  1.00 44.81 ?  630 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 630 ? 137.240 114.728 98.416  1.00 35.20 ?  630 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 630 ? 136.391 115.610 99.301  1.00 36.69 ?  630 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 630 ? 136.852 116.028 100.543 1.00 34.53 ?  630 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 630 ? 135.133 116.028 98.895  1.00 37.62 ?  630 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 630 ? 136.080 116.833 101.354 1.00 37.48 ?  630 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 630 ? 134.355 116.834 99.700  1.00 38.03 ?  630 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 630 ? 134.834 117.235 100.928 1.00 44.44 ?  630 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 630 ? 134.060 118.038 101.733 1.00 44.97 ?  630 TYR A OH    1 
ATOM   5073  N  N     . ASP A 1 631 ? 138.734 114.264 95.574  1.00 38.93 ?  631 ASP A N     1 
ATOM   5074  C  CA    . ASP A 1 631 ? 139.495 113.401 94.683  1.00 38.97 ?  631 ASP A CA    1 
ATOM   5075  C  C     . ASP A 1 631 ? 140.757 114.064 94.149  1.00 41.98 ?  631 ASP A C     1 
ATOM   5076  O  O     . ASP A 1 631 ? 141.606 113.371 93.579  1.00 43.81 ?  631 ASP A O     1 
ATOM   5077  C  CB    . ASP A 1 631 ? 138.621 112.956 93.508  1.00 39.94 ?  631 ASP A CB    1 
ATOM   5078  C  CG    . ASP A 1 631 ? 137.347 112.269 93.957  1.00 45.71 ?  631 ASP A CG    1 
ATOM   5079  O  OD1   . ASP A 1 631 ? 137.375 111.584 95.001  1.00 46.44 ?  631 ASP A OD1   1 
ATOM   5080  O  OD2   . ASP A 1 631 ? 136.316 112.416 93.267  1.00 43.66 -1 631 ASP A OD2   1 
ATOM   5081  N  N     . MET A 1 632 ? 140.902 115.373 94.324  1.00 35.51 ?  632 MET A N     1 
ATOM   5082  C  CA    . MET A 1 632 ? 142.028 116.100 93.762  1.00 32.76 ?  632 MET A CA    1 
ATOM   5083  C  C     . MET A 1 632 ? 143.261 115.977 94.650  1.00 37.18 ?  632 MET A C     1 
ATOM   5084  O  O     . MET A 1 632 ? 143.176 115.716 95.853  1.00 35.27 ?  632 MET A O     1 
ATOM   5085  C  CB    . MET A 1 632 ? 141.677 117.575 93.576  1.00 31.39 ?  632 MET A CB    1 
ATOM   5086  C  CG    . MET A 1 632 ? 140.702 117.845 92.453  1.00 35.86 ?  632 MET A CG    1 
ATOM   5087  S  SD    . MET A 1 632 ? 140.421 119.605 92.207  1.00 39.76 ?  632 MET A SD    1 
ATOM   5088  C  CE    . MET A 1 632 ? 139.152 119.556 90.951  1.00 33.94 ?  632 MET A CE    1 
ATOM   5089  N  N     . ASP A 1 633 ? 144.422 116.174 94.032  1.00 33.46 ?  633 ASP A N     1 
ATOM   5090  C  CA    . ASP A 1 633 ? 145.678 116.255 94.765  1.00 31.47 ?  633 ASP A CA    1 
ATOM   5091  C  C     . ASP A 1 633 ? 145.763 117.617 95.442  1.00 31.69 ?  633 ASP A C     1 
ATOM   5092  O  O     . ASP A 1 633 ? 145.729 118.652 94.769  1.00 35.01 ?  633 ASP A O     1 
ATOM   5093  C  CB    . ASP A 1 633 ? 146.860 116.041 93.824  1.00 29.78 ?  633 ASP A CB    1 
ATOM   5094  C  CG    . ASP A 1 633 ? 148.177 115.892 94.561  1.00 36.13 ?  633 ASP A CG    1 
ATOM   5095  O  OD1   . ASP A 1 633 ? 148.165 115.832 95.808  1.00 38.03 ?  633 ASP A OD1   1 
ATOM   5096  O  OD2   . ASP A 1 633 ? 149.228 115.838 93.889  1.00 37.92 -1 633 ASP A OD2   1 
ATOM   5097  N  N     . MET A 1 634 ? 145.868 117.618 96.772  1.00 27.77 ?  634 MET A N     1 
ATOM   5098  C  CA    . MET A 1 634 ? 145.895 118.876 97.508  1.00 25.57 ?  634 MET A CA    1 
ATOM   5099  C  C     . MET A 1 634 ? 147.142 119.698 97.215  1.00 27.47 ?  634 MET A C     1 
ATOM   5100  O  O     . MET A 1 634 ? 147.116 120.918 97.400  1.00 26.26 ?  634 MET A O     1 
ATOM   5101  C  CB    . MET A 1 634 ? 145.782 118.613 99.009  1.00 27.41 ?  634 MET A CB    1 
ATOM   5102  C  CG    . MET A 1 634 ? 144.351 118.507 99.501  1.00 28.92 ?  634 MET A CG    1 
ATOM   5103  S  SD    . MET A 1 634 ? 143.379 119.970 99.096  1.00 43.53 ?  634 MET A SD    1 
ATOM   5104  C  CE    . MET A 1 634 ? 142.175 119.276 97.967  1.00 28.34 ?  634 MET A CE    1 
ATOM   5105  N  N     . PHE A 1 635 ? 148.225 119.067 96.761  1.00 26.68 ?  635 PHE A N     1 
ATOM   5106  C  CA    . PHE A 1 635 ? 149.412 119.828 96.384  1.00 23.26 ?  635 PHE A CA    1 
ATOM   5107  C  C     . PHE A 1 635 ? 149.142 120.701 95.164  1.00 21.66 ?  635 PHE A C     1 
ATOM   5108  O  O     . PHE A 1 635 ? 149.589 121.851 95.105  1.00 25.79 ?  635 PHE A O     1 
ATOM   5109  C  CB    . PHE A 1 635 ? 150.585 118.883 96.126  1.00 23.22 ?  635 PHE A CB    1 
ATOM   5110  C  CG    . PHE A 1 635 ? 151.360 118.531 97.363  1.00 24.30 ?  635 PHE A CG    1 
ATOM   5111  C  CD1   . PHE A 1 635 ? 150.708 118.186 98.534  1.00 23.65 ?  635 PHE A CD1   1 
ATOM   5112  C  CD2   . PHE A 1 635 ? 152.744 118.545 97.355  1.00 27.13 ?  635 PHE A CD2   1 
ATOM   5113  C  CE1   . PHE A 1 635 ? 151.418 117.862 99.672  1.00 22.91 ?  635 PHE A CE1   1 
ATOM   5114  C  CE2   . PHE A 1 635 ? 153.461 118.223 98.490  1.00 29.75 ?  635 PHE A CE2   1 
ATOM   5115  C  CZ    . PHE A 1 635 ? 152.796 117.881 99.650  1.00 26.44 ?  635 PHE A CZ    1 
ATOM   5116  N  N     . LYS A 1 636 ? 148.399 120.180 94.187  1.00 23.36 ?  636 LYS A N     1 
ATOM   5117  C  CA    . LYS A 1 636 ? 148.081 120.977 93.007  1.00 26.62 ?  636 LYS A CA    1 
ATOM   5118  C  C     . LYS A 1 636 ? 147.053 122.059 93.320  1.00 27.24 ?  636 LYS A C     1 
ATOM   5119  O  O     . LYS A 1 636 ? 147.105 123.151 92.738  1.00 32.63 ?  636 LYS A O     1 
ATOM   5120  C  CB    . LYS A 1 636 ? 147.595 120.064 91.884  1.00 28.33 ?  636 LYS A CB    1 
ATOM   5121  C  CG    . LYS A 1 636 ? 148.689 119.152 91.347  1.00 28.04 ?  636 LYS A CG    1 
ATOM   5122  C  CD    . LYS A 1 636 ? 148.182 118.245 90.245  1.00 33.47 ?  636 LYS A CD    1 
ATOM   5123  C  CE    . LYS A 1 636 ? 149.200 117.171 89.899  1.00 32.60 ?  636 LYS A CE    1 
ATOM   5124  N  NZ    . LYS A 1 636 ? 148.620 116.131 89.005  1.00 33.68 1  636 LYS A NZ    1 
ATOM   5125  N  N     . VAL A 1 637 ? 146.128 121.788 94.242  1.00 23.94 ?  637 VAL A N     1 
ATOM   5126  C  CA    . VAL A 1 637 ? 145.224 122.834 94.713  1.00 16.29 ?  637 VAL A CA    1 
ATOM   5127  C  C     . VAL A 1 637 ? 146.013 123.934 95.414  1.00 23.84 ?  637 VAL A C     1 
ATOM   5128  O  O     . VAL A 1 637 ? 145.737 125.126 95.235  1.00 27.23 ?  637 VAL A O     1 
ATOM   5129  C  CB    . VAL A 1 637 ? 144.143 122.235 95.630  1.00 20.35 ?  637 VAL A CB    1 
ATOM   5130  C  CG1   . VAL A 1 637 ? 143.119 123.292 96.006  1.00 21.92 ?  637 VAL A CG1   1 
ATOM   5131  C  CG2   . VAL A 1 637 ? 143.469 121.056 94.951  1.00 25.87 ?  637 VAL A CG2   1 
ATOM   5132  N  N     . VAL A 1 638 ? 147.008 123.550 96.218  1.00 25.45 ?  638 VAL A N     1 
ATOM   5133  C  CA    . VAL A 1 638 ? 147.885 124.531 96.853  1.00 21.79 ?  638 VAL A CA    1 
ATOM   5134  C  C     . VAL A 1 638 ? 148.630 125.337 95.799  1.00 17.02 ?  638 VAL A C     1 
ATOM   5135  O  O     . VAL A 1 638 ? 148.800 126.553 95.932  1.00 25.22 ?  638 VAL A O     1 
ATOM   5136  C  CB    . VAL A 1 638 ? 148.859 123.833 97.822  1.00 20.12 ?  638 VAL A CB    1 
ATOM   5137  C  CG1   . VAL A 1 638 ? 150.036 124.737 98.141  1.00 15.90 ?  638 VAL A CG1   1 
ATOM   5138  C  CG2   . VAL A 1 638 ? 148.148 123.423 99.096  1.00 18.74 ?  638 VAL A CG2   1 
ATOM   5139  N  N     . ASP A 1 639 ? 149.097 124.671 94.743  1.00 20.16 ?  639 ASP A N     1 
ATOM   5140  C  CA    . ASP A 1 639 ? 149.806 125.371 93.675  1.00 17.42 ?  639 ASP A CA    1 
ATOM   5141  C  C     . ASP A 1 639 ? 148.910 126.400 92.998  1.00 23.65 ?  639 ASP A C     1 
ATOM   5142  O  O     . ASP A 1 639 ? 149.333 127.534 92.746  1.00 34.49 ?  639 ASP A O     1 
ATOM   5143  C  CB    . ASP A 1 639 ? 150.333 124.366 92.652  1.00 22.23 ?  639 ASP A CB    1 
ATOM   5144  C  CG    . ASP A 1 639 ? 151.579 123.649 93.126  1.00 30.93 ?  639 ASP A CG    1 
ATOM   5145  O  OD1   . ASP A 1 639 ? 152.416 124.290 93.794  1.00 31.40 ?  639 ASP A OD1   1 
ATOM   5146  O  OD2   . ASP A 1 639 ? 151.721 122.445 92.832  1.00 30.53 -1 639 ASP A OD2   1 
ATOM   5147  N  N     . MET A 1 640 ? 147.663 126.024 92.704  1.00 23.94 ?  640 MET A N     1 
ATOM   5148  C  CA    . MET A 1 640 ? 146.731 126.972 92.101  1.00 17.59 ?  640 MET A CA    1 
ATOM   5149  C  C     . MET A 1 640 ? 146.431 128.134 93.040  1.00 19.97 ?  640 MET A C     1 
ATOM   5150  O  O     . MET A 1 640 ? 146.380 129.297 92.611  1.00 30.73 ?  640 MET A O     1 
ATOM   5151  C  CB    . MET A 1 640 ? 145.437 126.262 91.704  1.00 23.08 ?  640 MET A CB    1 
ATOM   5152  C  CG    . MET A 1 640 ? 144.218 127.170 91.707  1.00 26.44 ?  640 MET A CG    1 
ATOM   5153  S  SD    . MET A 1 640 ? 143.825 127.835 90.081  1.00 31.92 ?  640 MET A SD    1 
ATOM   5154  C  CE    . MET A 1 640 ? 143.550 126.332 89.158  1.00 23.12 ?  640 MET A CE    1 
ATOM   5155  N  N     . ILE A 1 641 ? 146.225 127.843 94.325  1.00 15.77 ?  641 ILE A N     1 
ATOM   5156  C  CA    . ILE A 1 641 ? 145.902 128.908 95.266  1.00 18.94 ?  641 ILE A CA    1 
ATOM   5157  C  C     . ILE A 1 641 ? 147.088 129.846 95.443  1.00 19.32 ?  641 ILE A C     1 
ATOM   5158  O  O     . ILE A 1 641 ? 146.905 131.055 95.591  1.00 24.40 ?  641 ILE A O     1 
ATOM   5159  C  CB    . ILE A 1 641 ? 145.420 128.317 96.603  1.00 20.90 ?  641 ILE A CB    1 
ATOM   5160  C  CG1   . ILE A 1 641 ? 144.112 127.554 96.392  1.00 17.33 ?  641 ILE A CG1   1 
ATOM   5161  C  CG2   . ILE A 1 641 ? 145.192 129.414 97.629  1.00 16.43 ?  641 ILE A CG2   1 
ATOM   5162  C  CD1   . ILE A 1 641 ? 143.156 128.239 95.438  1.00 20.72 ?  641 ILE A CD1   1 
ATOM   5163  N  N     . ALA A 1 642 ? 148.315 129.322 95.409  1.00 15.52 ?  642 ALA A N     1 
ATOM   5164  C  CA    . ALA A 1 642 ? 149.495 130.182 95.473  1.00 16.76 ?  642 ALA A CA    1 
ATOM   5165  C  C     . ALA A 1 642 ? 149.638 131.018 94.209  1.00 19.56 ?  642 ALA A C     1 
ATOM   5166  O  O     . ALA A 1 642 ? 150.026 132.194 94.270  1.00 30.33 ?  642 ALA A O     1 
ATOM   5167  C  CB    . ALA A 1 642 ? 150.746 129.337 95.703  1.00 17.60 ?  642 ALA A CB    1 
ATOM   5168  N  N     . THR A 1 643 ? 149.331 130.425 93.053  1.00 16.40 ?  643 THR A N     1 
ATOM   5169  C  CA    . THR A 1 643 ? 149.355 131.172 91.803  1.00 16.82 ?  643 THR A CA    1 
ATOM   5170  C  C     . THR A 1 643 ? 148.384 132.345 91.852  1.00 20.72 ?  643 THR A C     1 
ATOM   5171  O  O     . THR A 1 643 ? 148.710 133.452 91.412  1.00 23.15 ?  643 THR A O     1 
ATOM   5172  C  CB    . THR A 1 643 ? 149.019 130.240 90.639  1.00 18.01 ?  643 THR A CB    1 
ATOM   5173  O  OG1   . THR A 1 643 ? 150.074 129.287 90.469  1.00 22.20 ?  643 THR A OG1   1 
ATOM   5174  C  CG2   . THR A 1 643 ? 148.844 131.023 89.359  1.00 14.96 ?  643 THR A CG2   1 
ATOM   5175  N  N     . ILE A 1 644 ? 147.186 132.121 92.393  1.00 17.72 ?  644 ILE A N     1 
ATOM   5176  C  CA    . ILE A 1 644 ? 146.239 133.221 92.556  1.00 11.61 ?  644 ILE A CA    1 
ATOM   5177  C  C     . ILE A 1 644 ? 146.735 134.207 93.610  1.00 15.14 ?  644 ILE A C     1 
ATOM   5178  O  O     . ILE A 1 644 ? 146.636 135.427 93.432  1.00 19.99 ?  644 ILE A O     1 
ATOM   5179  C  CB    . ILE A 1 644 ? 144.842 132.677 92.903  1.00 15.27 ?  644 ILE A CB    1 
ATOM   5180  C  CG1   . ILE A 1 644 ? 144.345 131.738 91.805  1.00 18.05 ?  644 ILE A CG1   1 
ATOM   5181  C  CG2   . ILE A 1 644 ? 143.867 133.820 93.104  1.00 9.24  ?  644 ILE A CG2   1 
ATOM   5182  C  CD1   . ILE A 1 644 ? 143.155 130.903 92.216  1.00 21.85 ?  644 ILE A CD1   1 
ATOM   5183  N  N     . GLN A 1 645 ? 147.285 133.696 94.715  1.00 13.04 ?  645 GLN A N     1 
ATOM   5184  C  CA    . GLN A 1 645 ? 147.683 134.533 95.840  1.00 14.10 ?  645 GLN A CA    1 
ATOM   5185  C  C     . GLN A 1 645 ? 148.808 135.485 95.473  1.00 15.57 ?  645 GLN A C     1 
ATOM   5186  O  O     . GLN A 1 645 ? 148.928 136.561 96.070  1.00 19.84 ?  645 GLN A O     1 
ATOM   5187  C  CB    . GLN A 1 645 ? 148.102 133.651 97.016  1.00 12.50 ?  645 GLN A CB    1 
ATOM   5188  C  CG    . GLN A 1 645 ? 148.410 134.406 98.293  1.00 8.73  ?  645 GLN A CG    1 
ATOM   5189  C  CD    . GLN A 1 645 ? 147.167 134.973 98.941  1.00 11.82 ?  645 GLN A CD    1 
ATOM   5190  O  OE1   . GLN A 1 645 ? 146.495 134.295 99.716  1.00 17.05 ?  645 GLN A OE1   1 
ATOM   5191  N  NE2   . GLN A 1 645 ? 146.854 136.223 98.627  1.00 6.56  ?  645 GLN A NE2   1 
ATOM   5192  N  N     . GLN A 1 646 ? 149.638 135.114 94.501  1.00 20.80 ?  646 GLN A N     1 
ATOM   5193  C  CA    . GLN A 1 646 ? 150.697 136.026 94.089  1.00 14.50 ?  646 GLN A CA    1 
ATOM   5194  C  C     . GLN A 1 646 ? 150.153 137.307 93.466  1.00 13.51 ?  646 GLN A C     1 
ATOM   5195  O  O     . GLN A 1 646 ? 150.907 138.273 93.325  1.00 17.75 ?  646 GLN A O     1 
ATOM   5196  C  CB    . GLN A 1 646 ? 151.649 135.326 93.119  1.00 17.94 ?  646 GLN A CB    1 
ATOM   5197  C  CG    . GLN A 1 646 ? 151.203 135.339 91.676  1.00 21.82 ?  646 GLN A CG    1 
ATOM   5198  C  CD    . GLN A 1 646 ? 152.055 134.444 90.801  1.00 26.95 ?  646 GLN A CD    1 
ATOM   5199  O  OE1   . GLN A 1 646 ? 153.245 134.691 90.616  1.00 25.36 ?  646 GLN A OE1   1 
ATOM   5200  N  NE2   . GLN A 1 646 ? 151.449 133.394 90.261  1.00 22.86 ?  646 GLN A NE2   1 
ATOM   5201  N  N     . HIS A 1 647 ? 148.867 137.347 93.109  1.00 21.28 ?  647 HIS A N     1 
ATOM   5202  C  CA    . HIS A 1 647 ? 148.241 138.546 92.563  1.00 14.87 ?  647 HIS A CA    1 
ATOM   5203  C  C     . HIS A 1 647 ? 147.179 139.130 93.485  1.00 11.61 ?  647 HIS A C     1 
ATOM   5204  O  O     . HIS A 1 647 ? 146.502 140.089 93.101  1.00 19.13 ?  647 HIS A O     1 
ATOM   5205  C  CB    . HIS A 1 647 ? 147.628 138.246 91.193  1.00 10.26 ?  647 HIS A CB    1 
ATOM   5206  C  CG    . HIS A 1 647 ? 148.596 137.654 90.221  1.00 15.52 ?  647 HIS A CG    1 
ATOM   5207  N  ND1   . HIS A 1 647 ? 149.706 138.336 89.771  1.00 16.09 ?  647 HIS A ND1   1 
ATOM   5208  C  CD2   . HIS A 1 647 ? 148.628 136.443 89.618  1.00 13.32 ?  647 HIS A CD2   1 
ATOM   5209  C  CE1   . HIS A 1 647 ? 150.378 137.570 88.930  1.00 18.02 ?  647 HIS A CE1   1 
ATOM   5210  N  NE2   . HIS A 1 647 ? 149.744 136.417 88.820  1.00 19.55 ?  647 HIS A NE2   1 
ATOM   5211  N  N     . ILE A 1 648 ? 147.013 138.582 94.685  1.00 11.14 ?  648 ILE A N     1 
ATOM   5212  C  CA    . ILE A 1 648 ? 146.033 139.060 95.653  1.00 13.31 ?  648 ILE A CA    1 
ATOM   5213  C  C     . ILE A 1 648 ? 146.791 139.657 96.831  1.00 13.02 ?  648 ILE A C     1 
ATOM   5214  O  O     . ILE A 1 648 ? 147.643 138.991 97.430  1.00 23.58 ?  648 ILE A O     1 
ATOM   5215  C  CB    . ILE A 1 648 ? 145.096 137.930 96.111  1.00 11.46 ?  648 ILE A CB    1 
ATOM   5216  C  CG1   . ILE A 1 648 ? 144.430 137.258 94.907  1.00 7.66  ?  648 ILE A CG1   1 
ATOM   5217  C  CG2   . ILE A 1 648 ? 144.045 138.460 97.066  1.00 9.21  ?  648 ILE A CG2   1 
ATOM   5218  C  CD1   . ILE A 1 648 ? 143.428 138.133 94.188  1.00 9.58  ?  648 ILE A CD1   1 
ATOM   5219  N  N     . ASP A 1 649 ? 146.490 140.918 97.154  1.00 6.66  ?  649 ASP A N     1 
ATOM   5220  C  CA    . ASP A 1 649 ? 147.203 141.587 98.238  1.00 11.95 ?  649 ASP A CA    1 
ATOM   5221  C  C     . ASP A 1 649 ? 146.808 141.019 99.595  1.00 9.56  ?  649 ASP A C     1 
ATOM   5222  O  O     . ASP A 1 649 ? 147.654 140.882 100.487 1.00 28.87 ?  649 ASP A O     1 
ATOM   5223  C  CB    . ASP A 1 649 ? 146.952 143.093 98.186  1.00 21.67 ?  649 ASP A CB    1 
ATOM   5224  C  CG    . ASP A 1 649 ? 145.512 143.432 97.879  1.00 18.65 ?  649 ASP A CG    1 
ATOM   5225  O  OD1   . ASP A 1 649 ? 144.860 142.651 97.160  1.00 24.11 ?  649 ASP A OD1   1 
ATOM   5226  O  OD2   . ASP A 1 649 ? 145.032 144.480 98.355  1.00 15.97 -1 649 ASP A OD2   1 
ATOM   5227  N  N     . GLN A 1 650 ? 145.536 140.692 99.776  1.00 10.05 ?  650 GLN A N     1 
ATOM   5228  C  CA    . GLN A 1 650 ? 145.072 140.025 100.982 1.00 6.55  ?  650 GLN A CA    1 
ATOM   5229  C  C     . GLN A 1 650 ? 145.115 138.514 100.753 1.00 5.55  ?  650 GLN A C     1 
ATOM   5230  O  O     . GLN A 1 650 ? 145.730 138.037 99.795  1.00 16.73 ?  650 GLN A O     1 
ATOM   5231  C  CB    . GLN A 1 650 ? 143.680 140.538 101.363 1.00 3.48  ?  650 GLN A CB    1 
ATOM   5232  C  CG    . GLN A 1 650 ? 143.623 142.030 101.629 1.00 4.86  ?  650 GLN A CG    1 
ATOM   5233  C  CD    . GLN A 1 650 ? 142.228 142.502 101.966 1.00 10.24 ?  650 GLN A CD    1 
ATOM   5234  O  OE1   . GLN A 1 650 ? 141.717 142.234 103.052 1.00 21.25 ?  650 GLN A OE1   1 
ATOM   5235  N  NE2   . GLN A 1 650 ? 141.603 143.211 101.036 1.00 5.10  ?  650 GLN A NE2   1 
ATOM   5236  N  N     . GLY A 1 651 ? 144.481 137.741 101.631 1.00 6.66  ?  651 GLY A N     1 
ATOM   5237  C  CA    . GLY A 1 651 ? 144.510 136.299 101.530 1.00 8.64  ?  651 GLY A CA    1 
ATOM   5238  C  C     . GLY A 1 651 ? 143.349 135.732 100.737 1.00 6.35  ?  651 GLY A C     1 
ATOM   5239  O  O     . GLY A 1 651 ? 142.469 136.440 100.251 1.00 9.60  ?  651 GLY A O     1 
ATOM   5240  N  N     . ILE A 1 652 ? 143.366 134.409 100.611 1.00 18.34 ?  652 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 652 ? 142.327 133.647 99.935  1.00 8.90  ?  652 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 652 ? 141.789 132.623 100.920 1.00 7.64  ?  652 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 652 ? 142.569 131.927 101.583 1.00 19.66 ?  652 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 652 ? 142.863 132.949 98.672  1.00 6.86  ?  652 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 652 ? 143.478 133.967 97.713  1.00 0.00  ?  652 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 652 ? 141.763 132.158 97.989  1.00 10.78 ?  652 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 652 ? 144.336 133.336 96.650  1.00 4.02  ?  652 ILE A CD1   1 
ATOM   5248  N  N     . SER A 1 653 ? 140.468 132.534 101.027 1.00 15.16 ?  653 SER A N     1 
ATOM   5249  C  CA    . SER A 1 653 ? 139.852 131.505 101.860 1.00 12.99 ?  653 SER A CA    1 
ATOM   5250  C  C     . SER A 1 653 ? 140.149 130.153 101.228 1.00 13.55 ?  653 SER A C     1 
ATOM   5251  O  O     . SER A 1 653 ? 139.533 129.765 100.234 1.00 26.18 ?  653 SER A O     1 
ATOM   5252  C  CB    . SER A 1 653 ? 138.355 131.744 101.996 1.00 12.53 ?  653 SER A CB    1 
ATOM   5253  O  OG    . SER A 1 653 ? 138.043 132.284 103.266 1.00 15.77 ?  653 SER A OG    1 
ATOM   5254  N  N     . PHE A 1 654 ? 141.099 129.431 101.809 1.00 18.67 ?  654 PHE A N     1 
ATOM   5255  C  CA    . PHE A 1 654 ? 141.636 128.200 101.236 1.00 9.68  ?  654 PHE A CA    1 
ATOM   5256  C  C     . PHE A 1 654 ? 141.255 127.045 102.154 1.00 15.65 ?  654 PHE A C     1 
ATOM   5257  O  O     . PHE A 1 654 ? 141.875 126.838 103.200 1.00 24.30 ?  654 PHE A O     1 
ATOM   5258  C  CB    . PHE A 1 654 ? 143.148 128.311 101.063 1.00 9.20  ?  654 PHE A CB    1 
ATOM   5259  C  CG    . PHE A 1 654 ? 143.781 127.121 100.399 1.00 16.73 ?  654 PHE A CG    1 
ATOM   5260  C  CD1   . PHE A 1 654 ? 143.027 126.232 99.651  1.00 22.93 ?  654 PHE A CD1   1 
ATOM   5261  C  CD2   . PHE A 1 654 ? 145.139 126.894 100.525 1.00 18.70 ?  654 PHE A CD2   1 
ATOM   5262  C  CE1   . PHE A 1 654 ? 143.614 125.142 99.047  1.00 14.90 ?  654 PHE A CE1   1 
ATOM   5263  C  CE2   . PHE A 1 654 ? 145.731 125.806 99.921  1.00 20.49 ?  654 PHE A CE2   1 
ATOM   5264  C  CZ    . PHE A 1 654 ? 144.967 124.929 99.182  1.00 15.99 ?  654 PHE A CZ    1 
ATOM   5265  N  N     . THR A 1 655 ? 140.240 126.289 101.750 1.00 20.69 ?  655 THR A N     1 
ATOM   5266  C  CA    . THR A 1 655 ? 139.805 125.113 102.486 1.00 16.46 ?  655 THR A CA    1 
ATOM   5267  C  C     . THR A 1 655 ? 140.513 123.880 101.941 1.00 23.11 ?  655 THR A C     1 
ATOM   5268  O  O     . THR A 1 655 ? 140.541 123.659 100.727 1.00 28.79 ?  655 THR A O     1 
ATOM   5269  C  CB    . THR A 1 655 ? 138.288 124.944 102.382 1.00 23.48 ?  655 THR A CB    1 
ATOM   5270  O  OG1   . THR A 1 655 ? 137.637 125.949 103.171 1.00 23.66 ?  655 THR A OG1   1 
ATOM   5271  C  CG2   . THR A 1 655 ? 137.862 123.568 102.870 1.00 24.36 ?  655 THR A CG2   1 
ATOM   5272  N  N     . LEU A 1 656 ? 141.098 123.092 102.839 1.00 31.95 ?  656 LEU A N     1 
ATOM   5273  C  CA    . LEU A 1 656 ? 141.660 121.806 102.457 1.00 28.61 ?  656 LEU A CA    1 
ATOM   5274  C  C     . LEU A 1 656 ? 140.549 120.771 102.359 1.00 27.54 ?  656 LEU A C     1 
ATOM   5275  O  O     . LEU A 1 656 ? 139.625 120.756 103.173 1.00 31.16 ?  656 LEU A O     1 
ATOM   5276  C  CB    . LEU A 1 656 ? 142.707 121.349 103.472 1.00 29.59 ?  656 LEU A CB    1 
ATOM   5277  C  CG    . LEU A 1 656 ? 143.940 122.238 103.621 1.00 30.46 ?  656 LEU A CG    1 
ATOM   5278  C  CD1   . LEU A 1 656 ? 144.994 121.552 104.475 1.00 26.80 ?  656 LEU A CD1   1 
ATOM   5279  C  CD2   . LEU A 1 656 ? 144.500 122.619 102.260 1.00 27.73 ?  656 LEU A CD2   1 
ATOM   5280  N  N     . PHE A 1 657 ? 140.636 119.912 101.349 1.00 26.53 ?  657 PHE A N     1 
ATOM   5281  C  CA    . PHE A 1 657 ? 139.647 118.863 101.124 1.00 28.20 ?  657 PHE A CA    1 
ATOM   5282  C  C     . PHE A 1 657 ? 140.353 117.521 101.239 1.00 36.33 ?  657 PHE A C     1 
ATOM   5283  O  O     . PHE A 1 657 ? 141.113 117.136 100.344 1.00 37.74 ?  657 PHE A O     1 
ATOM   5284  C  CB    . PHE A 1 657 ? 138.974 119.028 99.765  1.00 29.41 ?  657 PHE A CB    1 
ATOM   5285  C  CG    . PHE A 1 657 ? 138.366 120.383 99.557  1.00 32.69 ?  657 PHE A CG    1 
ATOM   5286  C  CD1   . PHE A 1 657 ? 137.095 120.664 100.021 1.00 30.22 ?  657 PHE A CD1   1 
ATOM   5287  C  CD2   . PHE A 1 657 ? 139.068 121.378 98.896  1.00 33.87 ?  657 PHE A CD2   1 
ATOM   5288  C  CE1   . PHE A 1 657 ? 136.536 121.911 99.833  1.00 32.64 ?  657 PHE A CE1   1 
ATOM   5289  C  CE2   . PHE A 1 657 ? 138.511 122.624 98.700  1.00 29.81 ?  657 PHE A CE2   1 
ATOM   5290  C  CZ    . PHE A 1 657 ? 137.244 122.892 99.171  1.00 32.98 ?  657 PHE A CZ    1 
ATOM   5291  N  N     . LEU A 1 658 ? 140.102 116.812 102.333 1.00 40.31 ?  658 LEU A N     1 
ATOM   5292  C  CA    . LEU A 1 658 ? 140.822 115.596 102.661 1.00 42.67 ?  658 LEU A CA    1 
ATOM   5293  C  C     . LEU A 1 658 ? 139.892 114.393 102.616 1.00 45.45 ?  658 LEU A C     1 
ATOM   5294  O  O     . LEU A 1 658 ? 138.682 114.509 102.832 1.00 46.68 ?  658 LEU A O     1 
ATOM   5295  C  CB    . LEU A 1 658 ? 141.458 115.698 104.048 1.00 40.37 ?  658 LEU A CB    1 
ATOM   5296  C  CG    . LEU A 1 658 ? 141.957 117.085 104.453 1.00 39.41 ?  658 LEU A CG    1 
ATOM   5297  C  CD1   . LEU A 1 658 ? 142.167 117.146 105.954 1.00 41.38 ?  658 LEU A CD1   1 
ATOM   5298  C  CD2   . LEU A 1 658 ? 143.233 117.445 103.711 1.00 42.05 ?  658 LEU A CD2   1 
ATOM   5299  N  N     . LYS A 1 659 ? 140.469 113.240 102.305 1.00 51.27 ?  659 LYS A N     1 
ATOM   5300  C  CA    . LYS A 1 659 ? 139.780 111.968 102.438 1.00 51.78 ?  659 LYS A CA    1 
ATOM   5301  C  C     . LYS A 1 659 ? 139.973 111.425 103.850 1.00 52.89 ?  659 LYS A C     1 
ATOM   5302  O  O     . LYS A 1 659 ? 140.921 111.779 104.553 1.00 54.58 ?  659 LYS A O     1 
ATOM   5303  C  CB    . LYS A 1 659 ? 140.296 110.962 101.409 1.00 54.80 ?  659 LYS A CB    1 
ATOM   5304  C  CG    . LYS A 1 659 ? 140.206 111.442 99.970  1.00 53.58 ?  659 LYS A CG    1 
ATOM   5305  C  CD    . LYS A 1 659 ? 140.526 110.323 98.993  1.00 53.18 ?  659 LYS A CD    1 
ATOM   5306  C  CE    . LYS A 1 659 ? 140.411 110.795 97.553  1.00 53.02 ?  659 LYS A CE    1 
ATOM   5307  N  NZ    . LYS A 1 659 ? 140.362 109.657 96.594  1.00 52.86 1  659 LYS A NZ    1 
ATOM   5308  N  N     . ASP A 1 660 ? 139.047 110.557 104.263 1.00 57.82 ?  660 ASP A N     1 
ATOM   5309  C  CA    . ASP A 1 660 ? 139.161 109.933 105.575 1.00 57.29 ?  660 ASP A CA    1 
ATOM   5310  C  C     . ASP A 1 660 ? 140.364 109.003 105.669 1.00 55.49 ?  660 ASP A C     1 
ATOM   5311  O  O     . ASP A 1 660 ? 140.796 108.679 106.780 1.00 56.14 ?  660 ASP A O     1 
ATOM   5312  C  CB    . ASP A 1 660 ? 137.879 109.169 105.909 1.00 58.51 ?  660 ASP A CB    1 
ATOM   5313  C  CG    . ASP A 1 660 ? 137.272 108.491 104.696 1.00 61.52 ?  660 ASP A CG    1 
ATOM   5314  O  OD1   . ASP A 1 660 ? 138.015 107.820 103.951 1.00 59.08 ?  660 ASP A OD1   1 
ATOM   5315  O  OD2   . ASP A 1 660 ? 136.049 108.633 104.487 1.00 61.60 -1 660 ASP A OD2   1 
ATOM   5316  N  N     . THR A 1 661 ? 140.913 108.572 104.531 1.00 53.18 ?  661 THR A N     1 
ATOM   5317  C  CA    . THR A 1 661 ? 142.042 107.647 104.559 1.00 55.32 ?  661 THR A CA    1 
ATOM   5318  C  C     . THR A 1 661 ? 143.330 108.346 104.975 1.00 54.64 ?  661 THR A C     1 
ATOM   5319  O  O     . THR A 1 661 ? 144.131 107.780 105.729 1.00 55.17 ?  661 THR A O     1 
ATOM   5320  C  CB    . THR A 1 661 ? 142.214 106.986 103.192 1.00 56.55 ?  661 THR A CB    1 
ATOM   5321  O  OG1   . THR A 1 661 ? 142.975 107.847 102.336 1.00 56.41 ?  661 THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1 661 ? 140.859 106.715 102.557 1.00 54.38 ?  661 THR A CG2   1 
ATOM   5323  N  N     . MET A 1 662 ? 143.553 109.569 104.497 1.00 52.78 ?  662 MET A N     1 
ATOM   5324  C  CA    . MET A 1 662 ? 144.799 110.258 104.799 1.00 52.47 ?  662 MET A CA    1 
ATOM   5325  C  C     . MET A 1 662 ? 144.866 110.639 106.274 1.00 51.28 ?  662 MET A C     1 
ATOM   5326  O  O     . MET A 1 662 ? 143.853 110.919 106.920 1.00 49.11 ?  662 MET A O     1 
ATOM   5327  C  CB    . MET A 1 662 ? 144.966 111.494 103.911 1.00 50.11 ?  662 MET A CB    1 
ATOM   5328  C  CG    . MET A 1 662 ? 144.569 112.814 104.545 1.00 51.94 ?  662 MET A CG    1 
ATOM   5329  S  SD    . MET A 1 662 ? 144.730 114.174 103.373 1.00 62.99 ?  662 MET A SD    1 
ATOM   5330  C  CE    . MET A 1 662 ? 143.755 113.558 102.006 1.00 48.13 ?  662 MET A CE    1 
ATOM   5331  N  N     . THR A 1 663 ? 146.083 110.622 106.805 1.00 45.64 ?  663 THR A N     1 
ATOM   5332  C  CA    . THR A 1 663 ? 146.342 110.788 108.224 1.00 44.52 ?  663 THR A CA    1 
ATOM   5333  C  C     . THR A 1 663 ? 146.766 112.225 108.519 1.00 44.92 ?  663 THR A C     1 
ATOM   5334  O  O     . THR A 1 663 ? 146.750 113.095 107.644 1.00 46.43 ?  663 THR A O     1 
ATOM   5335  C  CB    . THR A 1 663 ? 147.402 109.781 108.668 1.00 43.39 ?  663 THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 663 ? 148.706 110.340 108.465 1.00 42.25 ?  663 THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 663 ? 147.279 108.500 107.857 1.00 44.97 ?  663 THR A CG2   1 
ATOM   5338  N  N     . THR A 1 664 ? 147.150 112.483 109.772 1.00 39.16 ?  664 THR A N     1 
ATOM   5339  C  CA    . THR A 1 664 ? 147.617 113.812 110.143 1.00 38.73 ?  664 THR A CA    1 
ATOM   5340  C  C     . THR A 1 664 ? 148.959 114.150 109.511 1.00 37.04 ?  664 THR A C     1 
ATOM   5341  O  O     . THR A 1 664 ? 149.273 115.334 109.356 1.00 40.13 ?  664 THR A O     1 
ATOM   5342  C  CB    . THR A 1 664 ? 147.718 113.945 111.664 1.00 39.50 ?  664 THR A CB    1 
ATOM   5343  O  OG1   . THR A 1 664 ? 148.856 113.214 112.138 1.00 39.06 ?  664 THR A OG1   1 
ATOM   5344  C  CG2   . THR A 1 664 ? 146.458 113.422 112.332 1.00 36.70 ?  664 THR A CG2   1 
ATOM   5345  N  N     . ARG A 1 665 ? 149.758 113.144 109.147 1.00 37.74 ?  665 ARG A N     1 
ATOM   5346  C  CA    . ARG A 1 665 ? 150.997 113.416 108.427 1.00 34.74 ?  665 ARG A CA    1 
ATOM   5347  C  C     . ARG A 1 665 ? 150.710 114.044 107.070 1.00 39.12 ?  665 ARG A C     1 
ATOM   5348  O  O     . ARG A 1 665 ? 151.403 114.977 106.652 1.00 44.89 ?  665 ARG A O     1 
ATOM   5349  C  CB    . ARG A 1 665 ? 151.809 112.135 108.261 1.00 37.03 ?  665 ARG A CB    1 
ATOM   5350  C  CG    . ARG A 1 665 ? 152.880 112.218 107.184 1.00 35.80 ?  665 ARG A CG    1 
ATOM   5351  C  CD    . ARG A 1 665 ? 154.189 111.612 107.651 1.00 37.90 ?  665 ARG A CD    1 
ATOM   5352  N  NE    . ARG A 1 665 ? 155.187 111.588 106.589 1.00 40.76 ?  665 ARG A NE    1 
ATOM   5353  C  CZ    . ARG A 1 665 ? 155.367 110.577 105.751 1.00 42.19 ?  665 ARG A CZ    1 
ATOM   5354  N  NH1   . ARG A 1 665 ? 154.628 109.482 105.822 1.00 41.36 1  665 ARG A NH1   1 
ATOM   5355  N  NH2   . ARG A 1 665 ? 156.312 110.667 104.820 1.00 41.42 ?  665 ARG A NH2   1 
ATOM   5356  N  N     . ASP A 1 666 ? 149.688 113.550 106.369 1.00 37.63 ?  666 ASP A N     1 
ATOM   5357  C  CA    . ASP A 1 666 ? 149.320 114.136 105.085 1.00 36.14 ?  666 ASP A CA    1 
ATOM   5358  C  C     . ASP A 1 666 ? 148.811 115.563 105.252 1.00 39.97 ?  666 ASP A C     1 
ATOM   5359  O  O     . ASP A 1 666 ? 149.136 116.441 104.446 1.00 44.17 ?  666 ASP A O     1 
ATOM   5360  C  CB    . ASP A 1 666 ? 148.273 113.264 104.395 1.00 42.08 ?  666 ASP A CB    1 
ATOM   5361  C  CG    . ASP A 1 666 ? 148.792 111.878 104.075 1.00 46.23 ?  666 ASP A CG    1 
ATOM   5362  O  OD1   . ASP A 1 666 ? 149.869 111.776 103.454 1.00 44.32 ?  666 ASP A OD1   1 
ATOM   5363  O  OD2   . ASP A 1 666 ? 148.125 110.889 104.449 1.00 46.85 -1 666 ASP A OD2   1 
ATOM   5364  N  N     . LEU A 1 667 ? 148.012 115.811 106.292 1.00 33.15 ?  667 LEU A N     1 
ATOM   5365  C  CA    . LEU A 1 667 ? 147.540 117.166 106.556 1.00 30.35 ?  667 LEU A CA    1 
ATOM   5366  C  C     . LEU A 1 667 ? 148.703 118.103 106.852 1.00 30.18 ?  667 LEU A C     1 
ATOM   5367  O  O     . LEU A 1 667 ? 148.752 119.230 106.343 1.00 33.76 ?  667 LEU A O     1 
ATOM   5368  C  CB    . LEU A 1 667 ? 146.555 117.154 107.726 1.00 33.25 ?  667 LEU A CB    1 
ATOM   5369  C  CG    . LEU A 1 667 ? 145.361 118.108 107.683 1.00 35.96 ?  667 LEU A CG    1 
ATOM   5370  C  CD1   . LEU A 1 667 ? 144.356 117.723 108.753 1.00 35.10 ?  667 LEU A CD1   1 
ATOM   5371  C  CD2   . LEU A 1 667 ? 145.791 119.554 107.853 1.00 33.24 ?  667 LEU A CD2   1 
ATOM   5372  N  N     . ASN A 1 668 ? 149.653 117.651 107.673 1.00 30.42 ?  668 ASN A N     1 
ATOM   5373  C  CA    . ASN A 1 668 ? 150.823 118.465 107.975 1.00 27.03 ?  668 ASN A CA    1 
ATOM   5374  C  C     . ASN A 1 668 ? 151.663 118.705 106.729 1.00 27.13 ?  668 ASN A C     1 
ATOM   5375  O  O     . ASN A 1 668 ? 152.222 119.790 106.552 1.00 33.76 ?  668 ASN A O     1 
ATOM   5376  C  CB    . ASN A 1 668 ? 151.660 117.799 109.066 1.00 28.88 ?  668 ASN A CB    1 
ATOM   5377  C  CG    . ASN A 1 668 ? 151.204 118.170 110.460 1.00 31.15 ?  668 ASN A CG    1 
ATOM   5378  O  OD1   . ASN A 1 668 ? 151.292 117.365 111.385 1.00 39.82 ?  668 ASN A OD1   1 
ATOM   5379  N  ND2   . ASN A 1 668 ? 150.714 119.392 110.617 1.00 28.99 ?  668 ASN A ND2   1 
ATOM   5380  N  N     . ARG A 1 669 ? 151.773 117.699 105.860 1.00 29.15 ?  669 ARG A N     1 
ATOM   5381  C  CA    . ARG A 1 669 ? 152.511 117.873 104.613 1.00 30.94 ?  669 ARG A CA    1 
ATOM   5382  C  C     . ARG A 1 669 ? 151.844 118.905 103.717 1.00 28.85 ?  669 ARG A C     1 
ATOM   5383  O  O     . ARG A 1 669 ? 152.526 119.725 103.093 1.00 28.98 ?  669 ARG A O     1 
ATOM   5384  C  CB    . ARG A 1 669 ? 152.641 116.538 103.884 1.00 31.95 ?  669 ARG A CB    1 
ATOM   5385  C  CG    . ARG A 1 669 ? 154.036 115.948 103.919 1.00 29.86 ?  669 ARG A CG    1 
ATOM   5386  C  CD    . ARG A 1 669 ? 154.119 114.676 103.091 1.00 35.06 ?  669 ARG A CD    1 
ATOM   5387  N  NE    . ARG A 1 669 ? 154.352 114.950 101.678 1.00 33.74 ?  669 ARG A NE    1 
ATOM   5388  C  CZ    . ARG A 1 669 ? 155.502 115.374 101.170 1.00 34.89 ?  669 ARG A CZ    1 
ATOM   5389  N  NH1   . ARG A 1 669 ? 156.562 115.581 101.935 1.00 33.74 1  669 ARG A NH1   1 
ATOM   5390  N  NH2   . ARG A 1 669 ? 155.591 115.594 99.863  1.00 37.58 ?  669 ARG A NH2   1 
ATOM   5391  N  N     . ILE A 1 670 ? 150.511 118.878 103.634 1.00 25.18 ?  670 ILE A N     1 
ATOM   5392  C  CA    . ILE A 1 670 ? 149.801 119.888 102.854 1.00 25.57 ?  670 ILE A CA    1 
ATOM   5393  C  C     . ILE A 1 670 ? 150.024 121.274 103.448 1.00 27.89 ?  670 ILE A C     1 
ATOM   5394  O  O     . ILE A 1 670 ? 150.252 122.246 102.719 1.00 32.77 ?  670 ILE A O     1 
ATOM   5395  C  CB    . ILE A 1 670 ? 148.302 119.549 102.760 1.00 28.03 ?  670 ILE A CB    1 
ATOM   5396  C  CG1   . ILE A 1 670 ? 148.098 118.194 102.082 1.00 30.18 ?  670 ILE A CG1   1 
ATOM   5397  C  CG2   . ILE A 1 670 ? 147.562 120.629 101.993 1.00 25.40 ?  670 ILE A CG2   1 
ATOM   5398  C  CD1   . ILE A 1 670 ? 146.771 117.548 102.407 1.00 26.89 ?  670 ILE A CD1   1 
ATOM   5399  N  N     . ASP A 1 671 ? 149.966 121.386 104.777 1.00 24.47 ?  671 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 671 ? 150.195 122.678 105.421 1.00 21.06 ?  671 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 671 ? 151.610 123.186 105.165 1.00 25.88 ?  671 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 671 ? 151.812 124.375 104.892 1.00 27.34 ?  671 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 671 ? 149.933 122.569 106.923 1.00 22.89 ?  671 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 671 ? 148.502 122.185 107.239 1.00 34.47 ?  671 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 671 ? 147.626 122.387 106.372 1.00 34.26 ?  671 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 671 ? 148.253 121.679 108.354 1.00 35.03 -1 671 ASP A OD2   1 
ATOM   5407  N  N     . LEU A 1 672 ? 152.602 122.300 105.245 1.00 23.57 ?  672 LEU A N     1 
ATOM   5408  C  CA    . LEU A 1 672 ? 153.986 122.709 105.034 1.00 19.62 ?  672 LEU A CA    1 
ATOM   5409  C  C     . LEU A 1 672 ? 154.261 123.042 103.575 1.00 18.97 ?  672 LEU A C     1 
ATOM   5410  O  O     . LEU A 1 672 ? 155.078 123.922 103.289 1.00 24.16 ?  672 LEU A O     1 
ATOM   5411  C  CB    . LEU A 1 672 ? 154.935 121.615 105.520 1.00 27.26 ?  672 LEU A CB    1 
ATOM   5412  C  CG    . LEU A 1 672 ? 154.923 121.346 107.025 1.00 23.67 ?  672 LEU A CG    1 
ATOM   5413  C  CD1   . LEU A 1 672 ? 155.614 120.030 107.335 1.00 21.82 ?  672 LEU A CD1   1 
ATOM   5414  C  CD2   . LEU A 1 672 ? 155.568 122.493 107.781 1.00 20.76 ?  672 LEU A CD2   1 
ATOM   5415  N  N     . TYR A 1 673 ? 153.602 122.352 102.642 1.00 21.31 ?  673 TYR A N     1 
ATOM   5416  C  CA    . TYR A 1 673 ? 153.740 122.704 101.234 1.00 18.01 ?  673 TYR A CA    1 
ATOM   5417  C  C     . TYR A 1 673 ? 153.054 124.029 100.934 1.00 21.32 ?  673 TYR A C     1 
ATOM   5418  O  O     . TYR A 1 673 ? 153.528 124.806 100.097 1.00 23.54 ?  673 TYR A O     1 
ATOM   5419  C  CB    . TYR A 1 673 ? 153.172 121.589 100.356 1.00 16.74 ?  673 TYR A CB    1 
ATOM   5420  C  CG    . TYR A 1 673 ? 153.363 121.823 98.878  1.00 22.24 ?  673 TYR A CG    1 
ATOM   5421  C  CD1   . TYR A 1 673 ? 154.633 121.845 98.319  1.00 23.24 ?  673 TYR A CD1   1 
ATOM   5422  C  CD2   . TYR A 1 673 ? 152.275 122.022 98.040  1.00 20.22 ?  673 TYR A CD2   1 
ATOM   5423  C  CE1   . TYR A 1 673 ? 154.814 122.058 96.969  1.00 18.97 ?  673 TYR A CE1   1 
ATOM   5424  C  CE2   . TYR A 1 673 ? 152.446 122.237 96.689  1.00 22.76 ?  673 TYR A CE2   1 
ATOM   5425  C  CZ    . TYR A 1 673 ? 153.716 122.252 96.159  1.00 21.41 ?  673 TYR A CZ    1 
ATOM   5426  O  OH    . TYR A 1 673 ? 153.894 122.466 94.812  1.00 26.15 ?  673 TYR A OH    1 
ATOM   5427  N  N     . ALA A 1 674 ? 151.932 124.300 101.603 1.00 21.02 ?  674 ALA A N     1 
ATOM   5428  C  CA    . ALA A 1 674 ? 151.292 125.605 101.487 1.00 16.37 ?  674 ALA A CA    1 
ATOM   5429  C  C     . ALA A 1 674 ? 152.204 126.705 102.011 1.00 16.90 ?  674 ALA A C     1 
ATOM   5430  O  O     . ALA A 1 674 ? 152.339 127.764 101.388 1.00 25.79 ?  674 ALA A O     1 
ATOM   5431  C  CB    . ALA A 1 674 ? 149.962 125.597 102.238 1.00 18.01 ?  674 ALA A CB    1 
ATOM   5432  N  N     . HIS A 1 675 ? 152.846 126.466 103.155 1.00 15.15 ?  675 HIS A N     1 
ATOM   5433  C  CA    . HIS A 1 675 ? 153.810 127.427 103.680 1.00 15.76 ?  675 HIS A CA    1 
ATOM   5434  C  C     . HIS A 1 675 ? 154.978 127.615 102.719 1.00 20.74 ?  675 HIS A C     1 
ATOM   5435  O  O     . HIS A 1 675 ? 155.452 128.738 102.516 1.00 27.09 ?  675 HIS A O     1 
ATOM   5436  C  CB    . HIS A 1 675 ? 154.306 126.971 105.052 1.00 12.33 ?  675 HIS A CB    1 
ATOM   5437  C  CG    . HIS A 1 675 ? 155.383 127.837 105.622 1.00 21.52 ?  675 HIS A CG    1 
ATOM   5438  N  ND1   . HIS A 1 675 ? 156.717 127.496 105.569 1.00 24.93 ?  675 HIS A ND1   1 
ATOM   5439  C  CD2   . HIS A 1 675 ? 155.325 129.033 106.253 1.00 19.57 ?  675 HIS A CD2   1 
ATOM   5440  C  CE1   . HIS A 1 675 ? 157.434 128.444 106.143 1.00 25.63 ?  675 HIS A CE1   1 
ATOM   5441  N  NE2   . HIS A 1 675 ? 156.614 129.388 106.567 1.00 22.92 ?  675 HIS A NE2   1 
ATOM   5442  N  N     . HIS A 1 676 ? 155.456 126.523 102.122 1.00 19.67 ?  676 HIS A N     1 
ATOM   5443  C  CA    . HIS A 1 676 ? 156.566 126.603 101.178 1.00 20.42 ?  676 HIS A CA    1 
ATOM   5444  C  C     . HIS A 1 676 ? 156.167 127.342 99.906  1.00 24.31 ?  676 HIS A C     1 
ATOM   5445  O  O     . HIS A 1 676 ? 156.963 128.109 99.352  1.00 25.05 ?  676 HIS A O     1 
ATOM   5446  C  CB    . HIS A 1 676 ? 157.066 125.198 100.847 1.00 23.92 ?  676 HIS A CB    1 
ATOM   5447  C  CG    . HIS A 1 676 ? 158.015 125.148 99.691  1.00 25.00 ?  676 HIS A CG    1 
ATOM   5448  N  ND1   . HIS A 1 676 ? 159.294 125.659 99.755  1.00 20.88 ?  676 HIS A ND1   1 
ATOM   5449  C  CD2   . HIS A 1 676 ? 157.872 124.648 98.441  1.00 19.79 ?  676 HIS A CD2   1 
ATOM   5450  C  CE1   . HIS A 1 676 ? 159.897 125.476 98.595  1.00 25.77 ?  676 HIS A CE1   1 
ATOM   5451  N  NE2   . HIS A 1 676 ? 159.056 124.865 97.780  1.00 28.82 ?  676 HIS A NE2   1 
ATOM   5452  N  N     . ARG A 1 677 ? 154.943 127.127 99.430  1.00 21.42 ?  677 ARG A N     1 
ATOM   5453  C  CA    . ARG A 1 677 ? 154.492 127.712 98.173  1.00 20.36 ?  677 ARG A CA    1 
ATOM   5454  C  C     . ARG A 1 677 ? 154.005 129.146 98.323  1.00 24.10 ?  677 ARG A C     1 
ATOM   5455  O  O     . ARG A 1 677 ? 153.607 129.754 97.324  1.00 25.29 ?  677 ARG A O     1 
ATOM   5456  C  CB    . ARG A 1 677 ? 153.383 126.853 97.563  1.00 18.85 ?  677 ARG A CB    1 
ATOM   5457  C  CG    . ARG A 1 677 ? 153.892 125.689 96.733  1.00 20.21 ?  677 ARG A CG    1 
ATOM   5458  C  CD    . ARG A 1 677 ? 154.577 126.170 95.466  1.00 20.22 ?  677 ARG A CD    1 
ATOM   5459  N  NE    . ARG A 1 677 ? 153.632 126.349 94.370  1.00 25.02 ?  677 ARG A NE    1 
ATOM   5460  C  CZ    . ARG A 1 677 ? 153.330 127.520 93.826  1.00 27.26 ?  677 ARG A CZ    1 
ATOM   5461  N  NH1   . ARG A 1 677 ? 153.882 128.643 94.253  1.00 21.21 1  677 ARG A NH1   1 
ATOM   5462  N  NH2   . ARG A 1 677 ? 152.452 127.564 92.828  1.00 22.30 ?  677 ARG A NH2   1 
ATOM   5463  N  N     . GLY A 1 678 ? 154.027 129.699 99.532  1.00 20.70 ?  678 GLY A N     1 
ATOM   5464  C  CA    . GLY A 1 678 ? 153.602 131.066 99.742  1.00 16.08 ?  678 GLY A CA    1 
ATOM   5465  C  C     . GLY A 1 678 ? 152.142 131.242 100.078 1.00 16.22 ?  678 GLY A C     1 
ATOM   5466  O  O     . GLY A 1 678 ? 151.631 132.363 99.974  1.00 23.71 ?  678 GLY A O     1 
ATOM   5467  N  N     . ILE A 1 679 ? 151.448 130.174 100.470 1.00 15.50 ?  679 ILE A N     1 
ATOM   5468  C  CA    . ILE A 1 679 ? 150.057 130.298 100.887 1.00 11.34 ?  679 ILE A CA    1 
ATOM   5469  C  C     . ILE A 1 679 ? 149.996 131.121 102.164 1.00 15.26 ?  679 ILE A C     1 
ATOM   5470  O  O     . ILE A 1 679 ? 150.743 130.874 103.120 1.00 23.09 ?  679 ILE A O     1 
ATOM   5471  C  CB    . ILE A 1 679 ? 149.426 128.913 101.085 1.00 15.65 ?  679 ILE A CB    1 
ATOM   5472  C  CG1   . ILE A 1 679 ? 149.320 128.175 99.750  1.00 15.46 ?  679 ILE A CG1   1 
ATOM   5473  C  CG2   . ILE A 1 679 ? 148.062 129.032 101.743 1.00 15.73 ?  679 ILE A CG2   1 
ATOM   5474  C  CD1   . ILE A 1 679 ? 148.579 128.938 98.705  1.00 13.41 ?  679 ILE A CD1   1 
ATOM   5475  N  N     . LYS A 1 680 ? 149.112 132.114 102.182 1.00 13.20 ?  680 LYS A N     1 
ATOM   5476  C  CA    . LYS A 1 680 ? 149.009 133.012 103.324 1.00 8.26  ?  680 LYS A CA    1 
ATOM   5477  C  C     . LYS A 1 680 ? 148.140 132.430 104.435 1.00 8.16  ?  680 LYS A C     1 
ATOM   5478  O  O     . LYS A 1 680 ? 148.517 132.479 105.609 1.00 16.91 ?  680 LYS A O     1 
ATOM   5479  C  CB    . LYS A 1 680 ? 148.458 134.366 102.872 1.00 8.86  ?  680 LYS A CB    1 
ATOM   5480  C  CG    . LYS A 1 680 ? 149.414 135.174 102.014 1.00 0.00  ?  680 LYS A CG    1 
ATOM   5481  C  CD    . LYS A 1 680 ? 148.804 136.509 101.632 1.00 6.45  ?  680 LYS A CD    1 
ATOM   5482  C  CE    . LYS A 1 680 ? 149.573 137.173 100.510 1.00 13.22 ?  680 LYS A CE    1 
ATOM   5483  N  NZ    . LYS A 1 680 ? 149.025 138.515 100.182 1.00 10.77 1  680 LYS A NZ    1 
ATOM   5484  N  N     . THR A 1 681 ? 146.981 131.881 104.084 1.00 15.71 ?  681 THR A N     1 
ATOM   5485  C  CA    . THR A 1 681 ? 146.049 131.339 105.060 1.00 8.89  ?  681 THR A CA    1 
ATOM   5486  C  C     . THR A 1 681 ? 145.509 130.000 104.582 1.00 15.33 ?  681 THR A C     1 
ATOM   5487  O  O     . THR A 1 681 ? 145.371 129.760 103.380 1.00 22.36 ?  681 THR A O     1 
ATOM   5488  C  CB    . THR A 1 681 ? 144.869 132.290 105.316 1.00 16.05 ?  681 THR A CB    1 
ATOM   5489  O  OG1   . THR A 1 681 ? 144.304 132.704 104.066 1.00 30.21 ?  681 THR A OG1   1 
ATOM   5490  C  CG2   . THR A 1 681 ? 145.315 133.513 106.089 1.00 3.10  ?  681 THR A CG2   1 
ATOM   5491  N  N     . ILE A 1 682 ? 145.201 129.131 105.540 1.00 15.27 ?  682 ILE A N     1 
ATOM   5492  C  CA    . ILE A 1 682 ? 144.484 127.888 105.289 1.00 9.32  ?  682 ILE A CA    1 
ATOM   5493  C  C     . ILE A 1 682 ? 143.198 127.926 106.102 1.00 13.63 ?  682 ILE A C     1 
ATOM   5494  O  O     . ILE A 1 682 ? 143.238 128.103 107.324 1.00 21.07 ?  682 ILE A O     1 
ATOM   5495  C  CB    . ILE A 1 682 ? 145.327 126.654 105.649 1.00 12.93 ?  682 ILE A CB    1 
ATOM   5496  C  CG1   . ILE A 1 682 ? 146.792 126.873 105.272 1.00 17.99 ?  682 ILE A CG1   1 
ATOM   5497  C  CG2   . ILE A 1 682 ? 144.794 125.439 104.933 1.00 20.80 ?  682 ILE A CG2   1 
ATOM   5498  C  CD1   . ILE A 1 682 ? 147.654 125.645 105.450 1.00 19.45 ?  682 ILE A CD1   1 
ATOM   5499  N  N     . TYR A 1 683 ? 142.061 127.772 105.422 1.00 18.77 ?  683 TYR A N     1 
ATOM   5500  C  CA    . TYR A 1 683 ? 140.773 128.004 106.076 1.00 12.07 ?  683 TYR A CA    1 
ATOM   5501  C  C     . TYR A 1 683 ? 140.290 126.775 106.842 1.00 19.43 ?  683 TYR A C     1 
ATOM   5502  O  O     . TYR A 1 683 ? 140.187 126.796 108.071 1.00 32.31 ?  683 TYR A O     1 
ATOM   5503  C  CB    . TYR A 1 683 ? 139.738 128.440 105.034 1.00 18.00 ?  683 TYR A CB    1 
ATOM   5504  C  CG    . TYR A 1 683 ? 138.411 128.880 105.613 1.00 16.18 ?  683 TYR A CG    1 
ATOM   5505  C  CD1   . TYR A 1 683 ? 138.314 129.318 106.927 1.00 12.18 ?  683 TYR A CD1   1 
ATOM   5506  C  CD2   . TYR A 1 683 ? 137.258 128.866 104.842 1.00 9.75  ?  683 TYR A CD2   1 
ATOM   5507  C  CE1   . TYR A 1 683 ? 137.109 129.722 107.457 1.00 15.88 ?  683 TYR A CE1   1 
ATOM   5508  C  CE2   . TYR A 1 683 ? 136.046 129.270 105.365 1.00 18.37 ?  683 TYR A CE2   1 
ATOM   5509  C  CZ    . TYR A 1 683 ? 135.979 129.697 106.672 1.00 19.26 ?  683 TYR A CZ    1 
ATOM   5510  O  OH    . TYR A 1 683 ? 134.774 130.100 107.199 1.00 26.27 ?  683 TYR A OH    1 
ATOM   5511  N  N     . TYR A 1 684 ? 140.009 125.686 106.135 1.00 29.27 ?  684 TYR A N     1 
ATOM   5512  C  CA    . TYR A 1 684 ? 139.333 124.556 106.748 1.00 25.72 ?  684 TYR A CA    1 
ATOM   5513  C  C     . TYR A 1 684 ? 139.935 123.256 106.244 1.00 32.85 ?  684 TYR A C     1 
ATOM   5514  O  O     . TYR A 1 684 ? 140.526 123.203 105.162 1.00 36.53 ?  684 TYR A O     1 
ATOM   5515  C  CB    . TYR A 1 684 ? 137.827 124.576 106.453 1.00 23.92 ?  684 TYR A CB    1 
ATOM   5516  C  CG    . TYR A 1 684 ? 136.989 125.158 107.567 1.00 22.24 ?  684 TYR A CG    1 
ATOM   5517  C  CD1   . TYR A 1 684 ? 137.051 124.640 108.853 1.00 26.54 ?  684 TYR A CD1   1 
ATOM   5518  C  CD2   . TYR A 1 684 ? 136.134 126.226 107.331 1.00 29.36 ?  684 TYR A CD2   1 
ATOM   5519  C  CE1   . TYR A 1 684 ? 136.283 125.169 109.874 1.00 30.37 ?  684 TYR A CE1   1 
ATOM   5520  C  CE2   . TYR A 1 684 ? 135.364 126.764 108.345 1.00 26.07 ?  684 TYR A CE2   1 
ATOM   5521  C  CZ    . TYR A 1 684 ? 135.443 126.232 109.613 1.00 29.63 ?  684 TYR A CZ    1 
ATOM   5522  O  OH    . TYR A 1 684 ? 134.679 126.763 110.625 1.00 32.26 ?  684 TYR A OH    1 
ATOM   5523  N  N     . ALA A 1 685 ? 139.779 122.209 107.047 1.00 31.03 ?  685 ALA A N     1 
ATOM   5524  C  CA    . ALA A 1 685 ? 140.162 120.850 106.682 1.00 32.41 ?  685 ALA A CA    1 
ATOM   5525  C  C     . ALA A 1 685 ? 138.881 120.021 106.683 1.00 36.55 ?  685 ALA A C     1 
ATOM   5526  O  O     . ALA A 1 685 ? 138.529 119.400 107.689 1.00 43.59 ?  685 ALA A O     1 
ATOM   5527  C  CB    . ALA A 1 685 ? 141.206 120.290 107.639 1.00 32.11 ?  685 ALA A CB    1 
ATOM   5528  N  N     . ARG A 1 686 ? 138.180 120.023 105.552 1.00 32.51 ?  686 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 686 ? 136.938 119.279 105.413 1.00 33.05 ?  686 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 686 ? 137.257 117.846 105.007 1.00 38.70 ?  686 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 686 ? 137.823 117.611 103.935 1.00 40.64 ?  686 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 686 ? 136.038 119.944 104.374 1.00 38.13 ?  686 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 686 ? 135.485 121.291 104.801 1.00 38.73 ?  686 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 686 ? 134.302 121.697 103.940 1.00 39.90 ?  686 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 686 ? 133.261 120.677 103.919 1.00 42.70 ?  686 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 686 ? 131.962 120.934 103.976 1.00 42.66 ?  686 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 686 ? 131.505 122.174 104.055 1.00 41.77 1  686 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 686 ? 131.098 119.923 103.953 1.00 42.47 ?  686 ARG A NH2   1 
ATOM   5539  N  N     . THR A 1 687 ? 136.900 116.894 105.863 1.00 48.40 ?  687 THR A N     1 
ATOM   5540  C  CA    . THR A 1 687 ? 137.135 115.481 105.605 1.00 46.64 ?  687 THR A CA    1 
ATOM   5541  C  C     . THR A 1 687 ? 135.874 114.847 105.035 1.00 47.93 ?  687 THR A C     1 
ATOM   5542  O  O     . THR A 1 687 ? 134.778 115.024 105.574 1.00 50.75 ?  687 THR A O     1 
ATOM   5543  C  CB    . THR A 1 687 ? 137.560 114.755 106.884 1.00 46.66 ?  687 THR A CB    1 
ATOM   5544  O  OG1   . THR A 1 687 ? 138.910 115.109 107.213 1.00 48.39 ?  687 THR A OG1   1 
ATOM   5545  C  CG2   . THR A 1 687 ? 137.471 113.246 106.703 1.00 47.30 ?  687 THR A CG2   1 
ATOM   5546  N  N     . LYS A 1 688 ? 136.038 114.110 103.942 1.00 48.04 ?  688 LYS A N     1 
ATOM   5547  C  CA    . LYS A 1 688 ? 134.913 113.454 103.287 1.00 48.98 ?  688 LYS A CA    1 
ATOM   5548  C  C     . LYS A 1 688 ? 134.546 112.159 104.005 1.00 53.36 ?  688 LYS A C     1 
ATOM   5549  O  O     . LYS A 1 688 ? 135.404 111.496 104.586 1.00 55.18 ?  688 LYS A O     1 
ATOM   5550  C  CB    . LYS A 1 688 ? 135.236 113.169 101.820 1.00 49.54 ?  688 LYS A CB    1 
ATOM   5551  C  CG    . LYS A 1 688 ? 134.059 112.647 101.017 1.00 48.07 ?  688 LYS A CG    1 
ATOM   5552  C  CD    . LYS A 1 688 ? 134.428 112.446 99.558  1.00 47.51 ?  688 LYS A CD    1 
ATOM   5553  C  CE    . LYS A 1 688 ? 133.232 111.979 98.748  1.00 51.68 ?  688 LYS A CE    1 
ATOM   5554  N  NZ    . LYS A 1 688 ? 133.571 111.804 97.308  1.00 52.23 ?  688 LYS A NZ    1 
ATOM   5555  N  N     . VAL B 1 6   ? 151.041 117.431 164.560 1.00 57.44 ?  6   VAL B N     1 
ATOM   5556  C  CA    . VAL B 1 6   ? 150.058 118.480 164.803 1.00 58.35 ?  6   VAL B CA    1 
ATOM   5557  C  C     . VAL B 1 6   ? 150.620 119.530 165.756 1.00 60.21 ?  6   VAL B C     1 
ATOM   5558  O  O     . VAL B 1 6   ? 151.363 119.201 166.680 1.00 58.78 ?  6   VAL B O     1 
ATOM   5559  C  CB    . VAL B 1 6   ? 148.743 117.893 165.349 1.00 58.16 ?  6   VAL B CB    1 
ATOM   5560  C  CG1   . VAL B 1 6   ? 148.004 117.144 164.251 1.00 58.66 ?  6   VAL B CG1   1 
ATOM   5561  C  CG2   . VAL B 1 6   ? 149.019 116.977 166.527 1.00 58.25 ?  6   VAL B CG2   1 
ATOM   5562  N  N     . PRO B 1 7   ? 150.273 120.792 165.522 1.00 57.76 ?  7   PRO B N     1 
ATOM   5563  C  CA    . PRO B 1 7   ? 150.772 121.870 166.382 1.00 53.33 ?  7   PRO B CA    1 
ATOM   5564  C  C     . PRO B 1 7   ? 150.213 121.773 167.793 1.00 52.92 ?  7   PRO B C     1 
ATOM   5565  O  O     . PRO B 1 7   ? 149.144 121.209 168.037 1.00 55.02 ?  7   PRO B O     1 
ATOM   5566  C  CB    . PRO B 1 7   ? 150.287 123.144 165.683 1.00 52.57 ?  7   PRO B CB    1 
ATOM   5567  C  CG    . PRO B 1 7   ? 149.943 122.731 164.291 1.00 52.52 ?  7   PRO B CG    1 
ATOM   5568  C  CD    . PRO B 1 7   ? 149.514 121.303 164.369 1.00 54.44 ?  7   PRO B CD    1 
ATOM   5569  N  N     . LYS B 1 8   ? 150.972 122.338 168.736 1.00 50.58 ?  8   LYS B N     1 
ATOM   5570  C  CA    . LYS B 1 8   ? 150.571 122.298 170.139 1.00 49.37 ?  8   LYS B CA    1 
ATOM   5571  C  C     . LYS B 1 8   ? 149.265 123.048 170.367 1.00 52.20 ?  8   LYS B C     1 
ATOM   5572  O  O     . LYS B 1 8   ? 148.385 122.571 171.096 1.00 54.02 ?  8   LYS B O     1 
ATOM   5573  C  CB    . LYS B 1 8   ? 151.681 122.873 171.016 1.00 51.24 ?  8   LYS B CB    1 
ATOM   5574  C  CG    . LYS B 1 8   ? 151.232 123.252 172.417 1.00 52.38 ?  8   LYS B CG    1 
ATOM   5575  C  CD    . LYS B 1 8   ? 152.387 123.211 173.401 1.00 51.18 ?  8   LYS B CD    1 
ATOM   5576  C  CE    . LYS B 1 8   ? 151.898 123.386 174.829 1.00 51.50 ?  8   LYS B CE    1 
ATOM   5577  N  NZ    . LYS B 1 8   ? 152.026 124.795 175.292 1.00 52.01 1  8   LYS B NZ    1 
ATOM   5578  N  N     . TRP B 1 9   ? 149.118 124.226 169.754 1.00 53.51 ?  9   TRP B N     1 
ATOM   5579  C  CA    . TRP B 1 9   ? 147.878 124.977 169.911 1.00 51.21 ?  9   TRP B CA    1 
ATOM   5580  C  C     . TRP B 1 9   ? 146.700 124.240 169.292 1.00 49.73 ?  9   TRP B C     1 
ATOM   5581  O  O     . TRP B 1 9   ? 145.577 124.340 169.796 1.00 51.44 ?  9   TRP B O     1 
ATOM   5582  C  CB    . TRP B 1 9   ? 148.010 126.373 169.300 1.00 51.68 ?  9   TRP B CB    1 
ATOM   5583  C  CG    . TRP B 1 9   ? 148.427 126.389 167.863 1.00 49.36 ?  9   TRP B CG    1 
ATOM   5584  C  CD1   . TRP B 1 9   ? 147.606 126.360 166.774 1.00 48.25 ?  9   TRP B CD1   1 
ATOM   5585  C  CD2   . TRP B 1 9   ? 149.764 126.464 167.356 1.00 49.96 ?  9   TRP B CD2   1 
ATOM   5586  N  NE1   . TRP B 1 9   ? 148.349 126.401 165.620 1.00 47.82 ?  9   TRP B NE1   1 
ATOM   5587  C  CE2   . TRP B 1 9   ? 149.676 126.467 165.950 1.00 49.58 ?  9   TRP B CE2   1 
ATOM   5588  C  CE3   . TRP B 1 9   ? 151.026 126.523 167.953 1.00 47.79 ?  9   TRP B CE3   1 
ATOM   5589  C  CZ2   . TRP B 1 9   ? 150.802 126.525 165.133 1.00 48.99 ?  9   TRP B CZ2   1 
ATOM   5590  C  CZ3   . TRP B 1 9   ? 152.142 126.581 167.140 1.00 49.28 ?  9   TRP B CZ3   1 
ATOM   5591  C  CH2   . TRP B 1 9   ? 152.022 126.580 165.745 1.00 50.26 ?  9   TRP B CH2   1 
ATOM   5592  N  N     . ILE B 1 10  ? 146.934 123.491 168.213 1.00 52.27 ?  10  ILE B N     1 
ATOM   5593  C  CA    . ILE B 1 10  ? 145.869 122.694 167.618 1.00 52.32 ?  10  ILE B CA    1 
ATOM   5594  C  C     . ILE B 1 10  ? 145.400 121.618 168.591 1.00 53.45 ?  10  ILE B C     1 
ATOM   5595  O  O     . ILE B 1 10  ? 144.195 121.390 168.753 1.00 55.24 ?  10  ILE B O     1 
ATOM   5596  C  CB    . ILE B 1 10  ? 146.345 122.089 166.285 1.00 52.71 ?  10  ILE B CB    1 
ATOM   5597  C  CG1   . ILE B 1 10  ? 146.420 123.174 165.207 1.00 52.31 ?  10  ILE B CG1   1 
ATOM   5598  C  CG2   . ILE B 1 10  ? 145.434 120.948 165.855 1.00 53.05 ?  10  ILE B CG2   1 
ATOM   5599  C  CD1   . ILE B 1 10  ? 145.159 123.331 164.395 1.00 53.46 ?  10  ILE B CD1   1 
ATOM   5600  N  N     . GLN B 1 11  ? 146.342 120.947 169.260 1.00 53.92 ?  11  GLN B N     1 
ATOM   5601  C  CA    . GLN B 1 11  ? 145.972 119.951 170.261 1.00 55.14 ?  11  GLN B CA    1 
ATOM   5602  C  C     . GLN B 1 11  ? 145.226 120.589 171.426 1.00 54.84 ?  11  GLN B C     1 
ATOM   5603  O  O     . GLN B 1 11  ? 144.237 120.034 171.920 1.00 57.06 ?  11  GLN B O     1 
ATOM   5604  C  CB    . GLN B 1 11  ? 147.218 119.222 170.765 1.00 56.03 ?  11  GLN B CB    1 
ATOM   5605  C  CG    . GLN B 1 11  ? 148.051 118.581 169.671 1.00 56.59 ?  11  GLN B CG    1 
ATOM   5606  C  CD    . GLN B 1 11  ? 149.496 118.388 170.083 1.00 58.95 ?  11  GLN B CD    1 
ATOM   5607  O  OE1   . GLN B 1 11  ? 150.398 118.392 169.246 1.00 58.89 ?  11  GLN B OE1   1 
ATOM   5608  N  NE2   . GLN B 1 11  ? 149.724 118.220 171.380 1.00 55.94 ?  11  GLN B NE2   1 
ATOM   5609  N  N     . LEU B 1 12  ? 145.684 121.758 171.880 1.00 51.73 ?  12  LEU B N     1 
ATOM   5610  C  CA    . LEU B 1 12  ? 145.007 122.430 172.984 1.00 50.64 ?  12  LEU B CA    1 
ATOM   5611  C  C     . LEU B 1 12  ? 143.591 122.842 172.597 1.00 51.29 ?  12  LEU B C     1 
ATOM   5612  O  O     . LEU B 1 12  ? 142.668 122.758 173.415 1.00 53.55 ?  12  LEU B O     1 
ATOM   5613  C  CB    . LEU B 1 12  ? 145.820 123.640 173.438 1.00 52.10 ?  12  LEU B CB    1 
ATOM   5614  C  CG    . LEU B 1 12  ? 146.982 123.327 174.380 1.00 52.39 ?  12  LEU B CG    1 
ATOM   5615  C  CD1   . LEU B 1 12  ? 147.951 124.497 174.453 1.00 52.91 ?  12  LEU B CD1   1 
ATOM   5616  C  CD2   . LEU B 1 12  ? 146.466 122.966 175.762 1.00 51.76 ?  12  LEU B CD2   1 
ATOM   5617  N  N     . ASN B 1 13  ? 143.402 123.292 171.355 1.00 51.33 ?  13  ASN B N     1 
ATOM   5618  C  CA    . ASN B 1 13  ? 142.068 123.659 170.891 1.00 49.42 ?  13  ASN B CA    1 
ATOM   5619  C  C     . ASN B 1 13  ? 141.176 122.434 170.743 1.00 52.08 ?  13  ASN B C     1 
ATOM   5620  O  O     . ASN B 1 13  ? 139.975 122.496 171.029 1.00 56.58 ?  13  ASN B O     1 
ATOM   5621  C  CB    . ASN B 1 13  ? 142.166 124.421 169.569 1.00 51.33 ?  13  ASN B CB    1 
ATOM   5622  C  CG    . ASN B 1 13  ? 140.810 124.759 168.991 1.00 50.05 ?  13  ASN B CG    1 
ATOM   5623  O  OD1   . ASN B 1 13  ? 140.378 124.167 168.005 1.00 50.41 ?  13  ASN B OD1   1 
ATOM   5624  N  ND2   . ASN B 1 13  ? 140.128 125.719 169.606 1.00 51.28 ?  13  ASN B ND2   1 
ATOM   5625  N  N     . ASN B 1 14  ? 141.737 121.312 170.288 1.00 53.76 ?  14  ASN B N     1 
ATOM   5626  C  CA    . ASN B 1 14  ? 140.959 120.081 170.204 1.00 52.32 ?  14  ASN B CA    1 
ATOM   5627  C  C     . ASN B 1 14  ? 140.653 119.502 171.577 1.00 53.34 ?  14  ASN B C     1 
ATOM   5628  O  O     . ASN B 1 14  ? 139.725 118.698 171.706 1.00 56.59 ?  14  ASN B O     1 
ATOM   5629  C  CB    . ASN B 1 14  ? 141.695 119.046 169.353 1.00 52.91 ?  14  ASN B CB    1 
ATOM   5630  C  CG    . ASN B 1 14  ? 141.769 119.441 167.894 1.00 55.92 ?  14  ASN B CG    1 
ATOM   5631  O  OD1   . ASN B 1 14  ? 141.154 120.421 167.476 1.00 58.01 ?  14  ASN B OD1   1 
ATOM   5632  N  ND2   . ASN B 1 14  ? 142.522 118.680 167.111 1.00 54.69 ?  14  ASN B ND2   1 
ATOM   5633  N  N     . GLU B 1 15  ? 141.415 119.893 172.600 1.00 56.23 ?  15  GLU B N     1 
ATOM   5634  C  CA    . GLU B 1 15  ? 141.147 119.444 173.961 1.00 56.56 ?  15  GLU B CA    1 
ATOM   5635  C  C     . GLU B 1 15  ? 139.847 120.001 174.529 1.00 57.08 ?  15  GLU B C     1 
ATOM   5636  O  O     . GLU B 1 15  ? 139.418 119.545 175.593 1.00 60.06 ?  15  GLU B O     1 
ATOM   5637  C  CB    . GLU B 1 15  ? 142.312 119.824 174.876 1.00 55.53 ?  15  GLU B CB    1 
ATOM   5638  C  CG    . GLU B 1 15  ? 143.314 118.703 175.100 1.00 57.49 ?  15  GLU B CG    1 
ATOM   5639  C  CD    . GLU B 1 15  ? 144.683 119.211 175.505 1.00 61.35 ?  15  GLU B CD    1 
ATOM   5640  O  OE1   . GLU B 1 15  ? 144.823 119.695 176.648 1.00 60.81 ?  15  GLU B OE1   1 
ATOM   5641  O  OE2   . GLU B 1 15  ? 145.619 119.125 174.683 1.00 60.08 -1 15  GLU B OE2   1 
ATOM   5642  N  N     . ILE B 1 16  ? 139.225 120.975 173.861 1.00 56.73 ?  16  ILE B N     1 
ATOM   5643  C  CA    . ILE B 1 16  ? 137.954 121.515 174.342 1.00 56.54 ?  16  ILE B CA    1 
ATOM   5644  C  C     . ILE B 1 16  ? 136.883 120.432 174.343 1.00 56.57 ?  16  ILE B C     1 
ATOM   5645  O  O     . ILE B 1 16  ? 136.138 120.268 175.316 1.00 54.26 ?  16  ILE B O     1 
ATOM   5646  C  CB    . ILE B 1 16  ? 137.522 122.719 173.486 1.00 55.92 ?  16  ILE B CB    1 
ATOM   5647  C  CG1   . ILE B 1 16  ? 138.550 123.845 173.563 1.00 55.42 ?  16  ILE B CG1   1 
ATOM   5648  C  CG2   . ILE B 1 16  ? 136.154 123.223 173.924 1.00 56.40 ?  16  ILE B CG2   1 
ATOM   5649  C  CD1   . ILE B 1 16  ? 138.397 124.858 172.457 1.00 54.74 ?  16  ILE B CD1   1 
ATOM   5650  N  N     . MET B 1 17  ? 136.793 119.674 173.249 1.00 56.33 ?  17  MET B N     1 
ATOM   5651  C  CA    . MET B 1 17  ? 135.739 118.678 173.107 1.00 56.69 ?  17  MET B CA    1 
ATOM   5652  C  C     . MET B 1 17  ? 135.969 117.446 173.968 1.00 57.42 ?  17  MET B C     1 
ATOM   5653  O  O     . MET B 1 17  ? 135.014 116.705 174.228 1.00 56.86 ?  17  MET B O     1 
ATOM   5654  C  CB    . MET B 1 17  ? 135.602 118.266 171.643 1.00 57.47 ?  17  MET B CB    1 
ATOM   5655  C  CG    . MET B 1 17  ? 135.448 119.440 170.702 1.00 57.59 ?  17  MET B CG    1 
ATOM   5656  S  SD    . MET B 1 17  ? 133.971 120.413 171.046 1.00 63.33 ?  17  MET B SD    1 
ATOM   5657  C  CE    . MET B 1 17  ? 132.823 119.729 169.855 1.00 55.92 ?  17  MET B CE    1 
ATOM   5658  N  N     . ILE B 1 18  ? 137.200 117.205 174.412 1.00 59.62 ?  18  ILE B N     1 
ATOM   5659  C  CA    . ILE B 1 18  ? 137.457 116.123 175.352 1.00 58.94 ?  18  ILE B CA    1 
ATOM   5660  C  C     . ILE B 1 18  ? 136.871 116.544 176.692 1.00 60.09 ?  18  ILE B C     1 
ATOM   5661  O  O     . ILE B 1 18  ? 137.435 117.392 177.394 1.00 59.84 ?  18  ILE B O     1 
ATOM   5662  C  CB    . ILE B 1 18  ? 138.958 115.802 175.461 1.00 60.01 ?  18  ILE B CB    1 
ATOM   5663  C  CG1   . ILE B 1 18  ? 139.455 115.160 174.164 1.00 60.22 ?  18  ILE B CG1   1 
ATOM   5664  C  CG2   . ILE B 1 18  ? 139.224 114.873 176.636 1.00 59.20 ?  18  ILE B CG2   1 
ATOM   5665  C  CD1   . ILE B 1 18  ? 140.695 115.810 173.595 1.00 60.47 ?  18  ILE B CD1   1 
ATOM   5666  N  N     . GLN B 1 19  ? 135.726 115.967 177.044 1.00 62.58 ?  19  GLN B N     1 
ATOM   5667  C  CA    . GLN B 1 19  ? 135.000 116.409 178.224 1.00 62.09 ?  19  GLN B CA    1 
ATOM   5668  C  C     . GLN B 1 19  ? 135.692 115.939 179.496 1.00 64.61 ?  19  GLN B C     1 
ATOM   5669  O  O     . GLN B 1 19  ? 136.196 114.815 179.574 1.00 66.56 ?  19  GLN B O     1 
ATOM   5670  C  CB    . GLN B 1 19  ? 133.563 115.890 178.186 1.00 64.69 ?  19  GLN B CB    1 
ATOM   5671  C  CG    . GLN B 1 19  ? 133.016 115.694 176.782 1.00 64.60 ?  19  GLN B CG    1 
ATOM   5672  C  CD    . GLN B 1 19  ? 131.565 116.111 176.655 1.00 64.39 ?  19  GLN B CD    1 
ATOM   5673  O  OE1   . GLN B 1 19  ? 130.785 115.981 177.599 1.00 64.88 ?  19  GLN B OE1   1 
ATOM   5674  N  NE2   . GLN B 1 19  ? 131.194 116.617 175.485 1.00 64.21 ?  19  GLN B NE2   1 
ATOM   5675  N  N     . LYS B 1 20  ? 135.717 116.816 180.496 1.00 67.86 ?  20  LYS B N     1 
ATOM   5676  C  CA    . LYS B 1 20  ? 136.233 116.499 181.821 1.00 69.26 ?  20  LYS B CA    1 
ATOM   5677  C  C     . LYS B 1 20  ? 135.097 116.673 182.817 1.00 69.23 ?  20  LYS B C     1 
ATOM   5678  O  O     . LYS B 1 20  ? 134.526 117.764 182.925 1.00 68.81 ?  20  LYS B O     1 
ATOM   5679  C  CB    . LYS B 1 20  ? 137.421 117.393 182.181 1.00 67.79 ?  20  LYS B CB    1 
ATOM   5680  C  CG    . LYS B 1 20  ? 137.654 117.557 183.673 1.00 68.45 ?  20  LYS B CG    1 
ATOM   5681  C  CD    . LYS B 1 20  ? 139.088 117.969 183.964 1.00 69.24 ?  20  LYS B CD    1 
ATOM   5682  C  CE    . LYS B 1 20  ? 139.189 119.464 184.219 1.00 69.19 ?  20  LYS B CE    1 
ATOM   5683  N  NZ    . LYS B 1 20  ? 140.600 119.938 184.195 1.00 68.51 1  20  LYS B NZ    1 
ATOM   5684  N  N     . ASP B 1 21  ? 134.770 115.597 183.535 1.00 71.38 ?  21  ASP B N     1 
ATOM   5685  C  CA    . ASP B 1 21  ? 133.641 115.578 184.467 1.00 71.25 ?  21  ASP B CA    1 
ATOM   5686  C  C     . ASP B 1 21  ? 132.337 115.949 183.764 1.00 72.08 ?  21  ASP B C     1 
ATOM   5687  O  O     . ASP B 1 21  ? 131.477 116.631 184.326 1.00 71.47 ?  21  ASP B O     1 
ATOM   5688  C  CB    . ASP B 1 21  ? 133.895 116.493 185.667 1.00 71.76 ?  21  ASP B CB    1 
ATOM   5689  C  CG    . ASP B 1 21  ? 135.297 116.346 186.225 1.00 73.48 ?  21  ASP B CG    1 
ATOM   5690  O  OD1   . ASP B 1 21  ? 135.785 115.200 186.317 1.00 72.23 ?  21  ASP B OD1   1 
ATOM   5691  O  OD2   . ASP B 1 21  ? 135.911 117.377 186.572 1.00 72.92 -1 21  ASP B OD2   1 
ATOM   5692  N  N     . GLY B 1 22  ? 132.188 115.496 182.520 1.00 68.63 ?  22  GLY B N     1 
ATOM   5693  C  CA    . GLY B 1 22  ? 130.977 115.728 181.762 1.00 66.05 ?  22  GLY B CA    1 
ATOM   5694  C  C     . GLY B 1 22  ? 130.806 117.124 181.212 1.00 67.44 ?  22  GLY B C     1 
ATOM   5695  O  O     . GLY B 1 22  ? 129.723 117.444 180.709 1.00 67.11 ?  22  GLY B O     1 
ATOM   5696  N  N     . LYS B 1 23  ? 131.834 117.966 181.285 1.00 66.70 ?  23  LYS B N     1 
ATOM   5697  C  CA    . LYS B 1 23  ? 131.754 119.344 180.828 1.00 63.82 ?  23  LYS B CA    1 
ATOM   5698  C  C     . LYS B 1 23  ? 132.857 119.627 179.817 1.00 63.01 ?  23  LYS B C     1 
ATOM   5699  O  O     . LYS B 1 23  ? 133.956 119.071 179.900 1.00 64.84 ?  23  LYS B O     1 
ATOM   5700  C  CB    . LYS B 1 23  ? 131.868 120.328 182.000 1.00 63.78 ?  23  LYS B CB    1 
ATOM   5701  C  CG    . LYS B 1 23  ? 131.105 119.906 183.241 1.00 65.44 ?  23  LYS B CG    1 
ATOM   5702  C  CD    . LYS B 1 23  ? 129.606 119.951 183.005 1.00 65.22 ?  23  LYS B CD    1 
ATOM   5703  C  CE    . LYS B 1 23  ? 129.091 121.378 183.047 1.00 64.91 ?  23  LYS B CE    1 
ATOM   5704  N  NZ    . LYS B 1 23  ? 129.843 122.201 184.032 1.00 63.67 1  23  LYS B NZ    1 
ATOM   5705  N  N     . PHE B 1 24  ? 132.550 120.499 178.859 1.00 59.23 ?  24  PHE B N     1 
ATOM   5706  C  CA    . PHE B 1 24  ? 133.537 120.901 177.867 1.00 57.17 ?  24  PHE B CA    1 
ATOM   5707  C  C     . PHE B 1 24  ? 134.655 121.699 178.523 1.00 56.29 ?  24  PHE B C     1 
ATOM   5708  O  O     . PHE B 1 24  ? 134.428 122.460 179.468 1.00 56.56 ?  24  PHE B O     1 
ATOM   5709  C  CB    . PHE B 1 24  ? 132.879 121.733 176.766 1.00 55.54 ?  24  PHE B CB    1 
ATOM   5710  C  CG    . PHE B 1 24  ? 132.107 120.920 175.766 1.00 55.27 ?  24  PHE B CG    1 
ATOM   5711  C  CD1   . PHE B 1 24  ? 132.762 120.222 174.767 1.00 57.16 ?  24  PHE B CD1   1 
ATOM   5712  C  CD2   . PHE B 1 24  ? 130.725 120.867 175.818 1.00 55.44 ?  24  PHE B CD2   1 
ATOM   5713  C  CE1   . PHE B 1 24  ? 132.053 119.477 173.844 1.00 56.09 ?  24  PHE B CE1   1 
ATOM   5714  C  CE2   . PHE B 1 24  ? 130.012 120.124 174.897 1.00 56.44 ?  24  PHE B CE2   1 
ATOM   5715  C  CZ    . PHE B 1 24  ? 130.678 119.429 173.909 1.00 55.50 ?  24  PHE B CZ    1 
ATOM   5716  N  N     . GLN B 1 25  ? 135.875 121.522 178.013 1.00 57.29 ?  25  GLN B N     1 
ATOM   5717  C  CA    . GLN B 1 25  ? 137.044 122.235 178.531 1.00 57.15 ?  25  GLN B CA    1 
ATOM   5718  C  C     . GLN B 1 25  ? 137.230 123.515 177.720 1.00 57.88 ?  25  GLN B C     1 
ATOM   5719  O  O     . GLN B 1 25  ? 138.110 123.631 176.865 1.00 59.45 ?  25  GLN B O     1 
ATOM   5720  C  CB    . GLN B 1 25  ? 138.280 121.346 178.482 1.00 57.43 ?  25  GLN B CB    1 
ATOM   5721  C  CG    . GLN B 1 25  ? 138.133 120.039 179.240 1.00 57.27 ?  25  GLN B CG    1 
ATOM   5722  C  CD    . GLN B 1 25  ? 139.387 119.192 179.183 1.00 58.27 ?  25  GLN B CD    1 
ATOM   5723  O  OE1   . GLN B 1 25  ? 140.218 119.232 180.090 1.00 58.75 ?  25  GLN B OE1   1 
ATOM   5724  N  NE2   . GLN B 1 25  ? 139.531 118.418 178.113 1.00 58.57 ?  25  GLN B NE2   1 
ATOM   5725  N  N     . PHE B 1 26  ? 136.369 124.495 178.004 1.00 51.55 ?  26  PHE B N     1 
ATOM   5726  C  CA    . PHE B 1 26  ? 136.429 125.764 177.286 1.00 52.93 ?  26  PHE B CA    1 
ATOM   5727  C  C     . PHE B 1 26  ? 137.717 126.518 177.595 1.00 53.51 ?  26  PHE B C     1 
ATOM   5728  O  O     . PHE B 1 26  ? 138.293 127.160 176.709 1.00 52.89 ?  26  PHE B O     1 
ATOM   5729  C  CB    . PHE B 1 26  ? 135.209 126.617 177.631 1.00 50.12 ?  26  PHE B CB    1 
ATOM   5730  C  CG    . PHE B 1 26  ? 133.906 126.023 177.179 1.00 51.96 ?  26  PHE B CG    1 
ATOM   5731  C  CD1   . PHE B 1 26  ? 133.701 125.704 175.847 1.00 51.08 ?  26  PHE B CD1   1 
ATOM   5732  C  CD2   . PHE B 1 26  ? 132.888 125.782 178.085 1.00 50.64 ?  26  PHE B CD2   1 
ATOM   5733  C  CE1   . PHE B 1 26  ? 132.504 125.158 175.427 1.00 49.46 ?  26  PHE B CE1   1 
ATOM   5734  C  CE2   . PHE B 1 26  ? 131.689 125.235 177.671 1.00 49.81 ?  26  PHE B CE2   1 
ATOM   5735  C  CZ    . PHE B 1 26  ? 131.497 124.924 176.341 1.00 49.40 ?  26  PHE B CZ    1 
ATOM   5736  N  N     . ASP B 1 27  ? 138.182 126.451 178.847 1.00 57.05 ?  27  ASP B N     1 
ATOM   5737  C  CA    . ASP B 1 27  ? 139.389 127.175 179.234 1.00 54.92 ?  27  ASP B CA    1 
ATOM   5738  C  C     . ASP B 1 27  ? 140.602 126.728 178.429 1.00 55.84 ?  27  ASP B C     1 
ATOM   5739  O  O     . ASP B 1 27  ? 141.520 127.525 178.199 1.00 55.38 ?  27  ASP B O     1 
ATOM   5740  C  CB    . ASP B 1 27  ? 139.649 126.995 180.730 1.00 55.14 ?  27  ASP B CB    1 
ATOM   5741  C  CG    . ASP B 1 27  ? 139.260 125.617 181.227 1.00 59.58 ?  27  ASP B CG    1 
ATOM   5742  O  OD1   . ASP B 1 27  ? 139.565 124.625 180.534 1.00 58.90 ?  27  ASP B OD1   1 
ATOM   5743  O  OD2   . ASP B 1 27  ? 138.647 125.526 182.311 1.00 60.21 -1 27  ASP B OD2   1 
ATOM   5744  N  N     . LYS B 1 28  ? 140.617 125.468 177.983 1.00 55.09 ?  28  LYS B N     1 
ATOM   5745  C  CA    . LYS B 1 28  ? 141.707 124.990 177.138 1.00 55.69 ?  28  LYS B CA    1 
ATOM   5746  C  C     . LYS B 1 28  ? 141.883 125.883 175.918 1.00 55.91 ?  28  LYS B C     1 
ATOM   5747  O  O     . LYS B 1 28  ? 143.014 126.128 175.476 1.00 58.39 ?  28  LYS B O     1 
ATOM   5748  C  CB    . LYS B 1 28  ? 141.449 123.546 176.711 1.00 56.35 ?  28  LYS B CB    1 
ATOM   5749  C  CG    . LYS B 1 28  ? 141.747 122.510 177.782 1.00 56.47 ?  28  LYS B CG    1 
ATOM   5750  C  CD    . LYS B 1 28  ? 143.240 122.380 178.025 1.00 56.20 ?  28  LYS B CD    1 
ATOM   5751  C  CE    . LYS B 1 28  ? 143.530 121.437 179.181 1.00 56.98 ?  28  LYS B CE    1 
ATOM   5752  N  NZ    . LYS B 1 28  ? 144.387 122.074 180.217 1.00 55.47 1  28  LYS B NZ    1 
ATOM   5753  N  N     . ASP B 1 29  ? 140.774 126.399 175.379 1.00 54.35 ?  29  ASP B N     1 
ATOM   5754  C  CA    . ASP B 1 29  ? 140.839 127.316 174.246 1.00 52.22 ?  29  ASP B CA    1 
ATOM   5755  C  C     . ASP B 1 29  ? 141.802 128.459 174.528 1.00 52.26 ?  29  ASP B C     1 
ATOM   5756  O  O     . ASP B 1 29  ? 142.672 128.768 173.706 1.00 52.34 ?  29  ASP B O     1 
ATOM   5757  C  CB    . ASP B 1 29  ? 139.446 127.860 173.933 1.00 52.42 ?  29  ASP B CB    1 
ATOM   5758  C  CG    . ASP B 1 29  ? 139.303 128.302 172.491 1.00 54.90 ?  29  ASP B CG    1 
ATOM   5759  O  OD1   . ASP B 1 29  ? 140.011 127.748 171.624 1.00 55.08 ?  29  ASP B OD1   1 
ATOM   5760  O  OD2   . ASP B 1 29  ? 138.481 129.202 172.225 1.00 52.90 -1 29  ASP B OD2   1 
ATOM   5761  N  N     . LYS B 1 30  ? 141.682 129.072 175.709 1.00 52.18 ?  30  LYS B N     1 
ATOM   5762  C  CA    . LYS B 1 30  ? 142.584 130.157 176.076 1.00 53.26 ?  30  LYS B CA    1 
ATOM   5763  C  C     . LYS B 1 30  ? 144.032 129.699 175.998 1.00 51.63 ?  30  LYS B C     1 
ATOM   5764  O  O     . LYS B 1 30  ? 144.878 130.367 175.387 1.00 55.03 ?  30  LYS B O     1 
ATOM   5765  C  CB    . LYS B 1 30  ? 142.251 130.662 177.481 1.00 52.12 ?  30  LYS B CB    1 
ATOM   5766  C  CG    . LYS B 1 30  ? 143.113 131.824 177.942 1.00 51.47 ?  30  LYS B CG    1 
ATOM   5767  C  CD    . LYS B 1 30  ? 142.690 132.315 179.316 1.00 53.30 ?  30  LYS B CD    1 
ATOM   5768  C  CE    . LYS B 1 30  ? 143.566 133.467 179.782 1.00 55.90 ?  30  LYS B CE    1 
ATOM   5769  N  NZ    . LYS B 1 30  ? 143.163 133.960 181.128 1.00 55.29 1  30  LYS B NZ    1 
ATOM   5770  N  N     . GLU B 1 31  ? 144.324 128.529 176.573 1.00 53.21 ?  31  GLU B N     1 
ATOM   5771  C  CA    . GLU B 1 31  ? 145.676 127.988 176.501 1.00 52.85 ?  31  GLU B CA    1 
ATOM   5772  C  C     . GLU B 1 31  ? 146.149 127.922 175.058 1.00 52.18 ?  31  GLU B C     1 
ATOM   5773  O  O     . GLU B 1 31  ? 147.274 128.332 174.744 1.00 54.46 ?  31  GLU B O     1 
ATOM   5774  C  CB    . GLU B 1 31  ? 145.722 126.603 177.147 1.00 52.70 ?  31  GLU B CB    1 
ATOM   5775  C  CG    . GLU B 1 31  ? 145.384 126.599 178.629 1.00 54.76 ?  31  GLU B CG    1 
ATOM   5776  C  CD    . GLU B 1 31  ? 145.177 125.200 179.174 1.00 57.88 ?  31  GLU B CD    1 
ATOM   5777  O  OE1   . GLU B 1 31  ? 145.884 124.276 178.724 1.00 59.45 ?  31  GLU B OE1   1 
ATOM   5778  O  OE2   . GLU B 1 31  ? 144.306 125.024 180.051 1.00 56.50 -1 31  GLU B OE2   1 
ATOM   5779  N  N     . ALA B 1 32  ? 145.272 127.469 174.158 1.00 43.56 ?  32  ALA B N     1 
ATOM   5780  C  CA    . ALA B 1 32  ? 145.629 127.371 172.749 1.00 44.58 ?  32  ALA B CA    1 
ATOM   5781  C  C     . ALA B 1 32  ? 146.147 128.702 172.227 1.00 48.74 ?  32  ALA B C     1 
ATOM   5782  O  O     . ALA B 1 32  ? 147.222 128.765 171.616 1.00 50.09 ?  32  ALA B O     1 
ATOM   5783  C  CB    . ALA B 1 32  ? 144.426 126.899 171.933 1.00 44.78 ?  32  ALA B CB    1 
ATOM   5784  N  N     . VAL B 1 33  ? 145.423 129.791 172.514 1.00 49.04 ?  33  VAL B N     1 
ATOM   5785  C  CA    . VAL B 1 33  ? 145.854 131.101 172.031 1.00 47.36 ?  33  VAL B CA    1 
ATOM   5786  C  C     . VAL B 1 33  ? 147.265 131.390 172.517 1.00 47.53 ?  33  VAL B C     1 
ATOM   5787  O  O     . VAL B 1 33  ? 148.141 131.782 171.735 1.00 49.67 ?  33  VAL B O     1 
ATOM   5788  C  CB    . VAL B 1 33  ? 144.873 132.204 172.465 1.00 45.21 ?  33  VAL B CB    1 
ATOM   5789  C  CG1   . VAL B 1 33  ? 144.692 133.215 171.346 1.00 45.04 ?  33  VAL B CG1   1 
ATOM   5790  C  CG2   . VAL B 1 33  ? 143.541 131.615 172.855 1.00 47.96 ?  33  VAL B CG2   1 
ATOM   5791  N  N     . HIS B 1 34  ? 147.517 131.143 173.806 1.00 44.02 ?  34  HIS B N     1 
ATOM   5792  C  CA    . HIS B 1 34  ? 148.859 131.341 174.337 1.00 45.18 ?  34  HIS B CA    1 
ATOM   5793  C  C     . HIS B 1 34  ? 149.873 130.559 173.518 1.00 45.96 ?  34  HIS B C     1 
ATOM   5794  O  O     . HIS B 1 34  ? 150.853 131.124 173.017 1.00 49.13 ?  34  HIS B O     1 
ATOM   5795  C  CB    . HIS B 1 34  ? 148.911 130.930 175.808 1.00 50.39 ?  34  HIS B CB    1 
ATOM   5796  C  CG    . HIS B 1 34  ? 149.960 131.649 176.596 1.00 49.36 ?  34  HIS B CG    1 
ATOM   5797  N  ND1   . HIS B 1 34  ? 151.154 131.062 176.956 1.00 48.47 ?  34  HIS B ND1   1 
ATOM   5798  C  CD2   . HIS B 1 34  ? 149.996 132.909 177.091 1.00 49.42 ?  34  HIS B CD2   1 
ATOM   5799  C  CE1   . HIS B 1 34  ? 151.880 131.929 177.640 1.00 50.02 ?  34  HIS B CE1   1 
ATOM   5800  N  NE2   . HIS B 1 34  ? 151.200 133.057 177.735 1.00 51.44 ?  34  HIS B NE2   1 
ATOM   5801  N  N     . SER B 1 35  ? 149.611 129.265 173.312 1.00 46.26 ?  35  SER B N     1 
ATOM   5802  C  CA    . SER B 1 35  ? 150.493 128.468 172.471 1.00 47.37 ?  35  SER B CA    1 
ATOM   5803  C  C     . SER B 1 35  ? 150.617 129.096 171.093 1.00 46.78 ?  35  SER B C     1 
ATOM   5804  O  O     . SER B 1 35  ? 151.729 129.344 170.607 1.00 50.48 ?  35  SER B O     1 
ATOM   5805  C  CB    . SER B 1 35  ? 149.972 127.034 172.372 1.00 48.20 ?  35  SER B CB    1 
ATOM   5806  O  OG    . SER B 1 35  ? 150.624 126.326 171.334 1.00 48.65 ?  35  SER B OG    1 
ATOM   5807  N  N     . TYR B 1 36  ? 149.476 129.446 170.488 1.00 47.40 ?  36  TYR B N     1 
ATOM   5808  C  CA    . TYR B 1 36  ? 149.484 130.003 169.142 1.00 45.60 ?  36  TYR B CA    1 
ATOM   5809  C  C     . TYR B 1 36  ? 150.334 131.260 169.070 1.00 46.42 ?  36  TYR B C     1 
ATOM   5810  O  O     . TYR B 1 36  ? 150.851 131.599 168.001 1.00 47.08 ?  36  TYR B O     1 
ATOM   5811  C  CB    . TYR B 1 36  ? 148.054 130.300 168.689 1.00 44.83 ?  36  TYR B CB    1 
ATOM   5812  C  CG    . TYR B 1 36  ? 147.941 130.765 167.257 1.00 45.26 ?  36  TYR B CG    1 
ATOM   5813  C  CD1   . TYR B 1 36  ? 148.384 129.969 166.209 1.00 44.63 ?  36  TYR B CD1   1 
ATOM   5814  C  CD2   . TYR B 1 36  ? 147.389 132.001 166.949 1.00 42.99 ?  36  TYR B CD2   1 
ATOM   5815  C  CE1   . TYR B 1 36  ? 148.280 130.388 164.899 1.00 43.22 ?  36  TYR B CE1   1 
ATOM   5816  C  CE2   . TYR B 1 36  ? 147.281 132.430 165.642 1.00 44.18 ?  36  TYR B CE2   1 
ATOM   5817  C  CZ    . TYR B 1 36  ? 147.728 131.619 164.621 1.00 44.46 ?  36  TYR B CZ    1 
ATOM   5818  O  OH    . TYR B 1 36  ? 147.623 132.043 163.316 1.00 43.59 ?  36  TYR B OH    1 
ATOM   5819  N  N     . PHE B 1 37  ? 150.505 131.951 170.195 1.00 49.89 ?  37  PHE B N     1 
ATOM   5820  C  CA    . PHE B 1 37  ? 151.358 133.129 170.206 1.00 49.17 ?  37  PHE B CA    1 
ATOM   5821  C  C     . PHE B 1 37  ? 152.779 132.809 170.645 1.00 51.17 ?  37  PHE B C     1 
ATOM   5822  O  O     . PHE B 1 37  ? 153.728 133.400 170.124 1.00 55.25 ?  37  PHE B O     1 
ATOM   5823  C  CB    . PHE B 1 37  ? 150.751 134.208 171.104 1.00 49.72 ?  37  PHE B CB    1 
ATOM   5824  C  CG    . PHE B 1 37  ? 149.709 135.038 170.417 1.00 50.79 ?  37  PHE B CG    1 
ATOM   5825  C  CD1   . PHE B 1 37  ? 150.073 136.122 169.639 1.00 51.43 ?  37  PHE B CD1   1 
ATOM   5826  C  CD2   . PHE B 1 37  ? 148.367 134.725 170.535 1.00 50.28 ?  37  PHE B CD2   1 
ATOM   5827  C  CE1   . PHE B 1 37  ? 149.117 136.884 169.000 1.00 50.45 ?  37  PHE B CE1   1 
ATOM   5828  C  CE2   . PHE B 1 37  ? 147.408 135.484 169.898 1.00 48.78 ?  37  PHE B CE2   1 
ATOM   5829  C  CZ    . PHE B 1 37  ? 147.784 136.563 169.127 1.00 48.83 ?  37  PHE B CZ    1 
ATOM   5830  N  N     . VAL B 1 38  ? 152.958 131.872 171.582 1.00 52.14 ?  38  VAL B N     1 
ATOM   5831  C  CA    . VAL B 1 38  ? 154.307 131.609 172.082 1.00 51.44 ?  38  VAL B CA    1 
ATOM   5832  C  C     . VAL B 1 38  ? 155.070 130.626 171.212 1.00 53.54 ?  38  VAL B C     1 
ATOM   5833  O  O     . VAL B 1 38  ? 156.262 130.399 171.453 1.00 56.53 ?  38  VAL B O     1 
ATOM   5834  C  CB    . VAL B 1 38  ? 154.299 131.085 173.531 1.00 50.73 ?  38  VAL B CB    1 
ATOM   5835  C  CG1   . VAL B 1 38  ? 153.558 132.054 174.443 1.00 50.91 ?  38  VAL B CG1   1 
ATOM   5836  C  CG2   . VAL B 1 38  ? 153.696 129.693 173.597 1.00 49.68 ?  38  VAL B CG2   1 
ATOM   5837  N  N     . ASP B 1 39  ? 154.424 130.041 170.208 1.00 50.18 ?  39  ASP B N     1 
ATOM   5838  C  CA    . ASP B 1 39  ? 155.075 129.093 169.321 1.00 51.31 ?  39  ASP B CA    1 
ATOM   5839  C  C     . ASP B 1 39  ? 155.012 129.474 167.850 1.00 53.35 ?  39  ASP B C     1 
ATOM   5840  O  O     . ASP B 1 39  ? 155.900 129.077 167.093 1.00 56.10 ?  39  ASP B O     1 
ATOM   5841  C  CB    . ASP B 1 39  ? 154.464 127.692 169.494 1.00 52.76 ?  39  ASP B CB    1 
ATOM   5842  C  CG    . ASP B 1 39  ? 154.415 127.254 170.944 1.00 54.28 ?  39  ASP B CG    1 
ATOM   5843  O  OD1   . ASP B 1 39  ? 155.354 127.581 171.697 1.00 54.59 ?  39  ASP B OD1   1 
ATOM   5844  O  OD2   . ASP B 1 39  ? 153.436 126.581 171.329 1.00 53.25 -1 39  ASP B OD2   1 
ATOM   5845  N  N     . TYR B 1 40  ? 153.996 130.223 167.420 1.00 53.18 ?  40  TYR B N     1 
ATOM   5846  C  CA    . TYR B 1 40  ? 153.861 130.581 166.011 1.00 53.04 ?  40  TYR B CA    1 
ATOM   5847  C  C     . TYR B 1 40  ? 153.921 132.083 165.772 1.00 55.10 ?  40  TYR B C     1 
ATOM   5848  O  O     . TYR B 1 40  ? 154.748 132.535 164.974 1.00 55.56 ?  40  TYR B O     1 
ATOM   5849  C  CB    . TYR B 1 40  ? 152.555 130.008 165.447 1.00 52.98 ?  40  TYR B CB    1 
ATOM   5850  C  CG    . TYR B 1 40  ? 152.502 129.998 163.936 1.00 52.53 ?  40  TYR B CG    1 
ATOM   5851  C  CD1   . TYR B 1 40  ? 153.160 129.017 163.207 1.00 53.26 ?  40  TYR B CD1   1 
ATOM   5852  C  CD2   . TYR B 1 40  ? 151.798 130.972 163.240 1.00 51.96 ?  40  TYR B CD2   1 
ATOM   5853  C  CE1   . TYR B 1 40  ? 153.116 129.004 161.826 1.00 55.40 ?  40  TYR B CE1   1 
ATOM   5854  C  CE2   . TYR B 1 40  ? 151.750 130.968 161.859 1.00 52.85 ?  40  TYR B CE2   1 
ATOM   5855  C  CZ    . TYR B 1 40  ? 152.410 129.981 161.158 1.00 56.50 ?  40  TYR B CZ    1 
ATOM   5856  O  OH    . TYR B 1 40  ? 152.365 129.971 159.782 1.00 57.66 ?  40  TYR B OH    1 
ATOM   5857  N  N     . ILE B 1 41  ? 153.076 132.875 166.434 1.00 55.05 ?  41  ILE B N     1 
ATOM   5858  C  CA    . ILE B 1 41  ? 152.932 134.280 166.058 1.00 53.28 ?  41  ILE B CA    1 
ATOM   5859  C  C     . ILE B 1 41  ? 154.179 135.072 166.432 1.00 52.04 ?  41  ILE B C     1 
ATOM   5860  O  O     . ILE B 1 41  ? 154.697 135.853 165.626 1.00 54.19 ?  41  ILE B O     1 
ATOM   5861  C  CB    . ILE B 1 41  ? 151.667 134.883 166.692 1.00 50.85 ?  41  ILE B CB    1 
ATOM   5862  C  CG1   . ILE B 1 41  ? 150.421 134.143 166.202 1.00 48.55 ?  41  ILE B CG1   1 
ATOM   5863  C  CG2   . ILE B 1 41  ? 151.562 136.363 166.365 1.00 49.09 ?  41  ILE B CG2   1 
ATOM   5864  C  CD1   . ILE B 1 41  ? 150.342 134.015 164.700 1.00 49.11 ?  41  ILE B CD1   1 
ATOM   5865  N  N     . ASN B 1 42  ? 154.682 134.885 167.654 1.00 50.52 ?  42  ASN B N     1 
ATOM   5866  C  CA    . ASN B 1 42  ? 155.856 135.640 168.079 1.00 51.96 ?  42  ASN B CA    1 
ATOM   5867  C  C     . ASN B 1 42  ? 157.100 135.231 167.302 1.00 54.31 ?  42  ASN B C     1 
ATOM   5868  O  O     . ASN B 1 42  ? 157.986 136.062 167.071 1.00 54.08 ?  42  ASN B O     1 
ATOM   5869  C  CB    . ASN B 1 42  ? 156.083 135.467 169.580 1.00 53.11 ?  42  ASN B CB    1 
ATOM   5870  C  CG    . ASN B 1 42  ? 154.986 136.103 170.411 1.00 53.45 ?  42  ASN B CG    1 
ATOM   5871  O  OD1   . ASN B 1 42  ? 154.146 136.836 169.893 1.00 56.58 ?  42  ASN B OD1   1 
ATOM   5872  N  ND2   . ASN B 1 42  ? 154.990 135.822 171.709 1.00 53.35 ?  42  ASN B ND2   1 
ATOM   5873  N  N     . GLN B 1 43  ? 157.190 133.964 166.896 1.00 58.65 ?  43  GLN B N     1 
ATOM   5874  C  CA    . GLN B 1 43  ? 158.326 133.522 166.096 1.00 57.83 ?  43  GLN B CA    1 
ATOM   5875  C  C     . GLN B 1 43  ? 158.205 133.978 164.646 1.00 56.26 ?  43  GLN B C     1 
ATOM   5876  O  O     . GLN B 1 43  ? 159.212 134.314 164.015 1.00 58.13 ?  43  GLN B O     1 
ATOM   5877  C  CB    . GLN B 1 43  ? 158.461 132.002 166.170 1.00 58.46 ?  43  GLN B CB    1 
ATOM   5878  C  CG    . GLN B 1 43  ? 159.371 131.518 167.286 1.00 58.98 ?  43  GLN B CG    1 
ATOM   5879  C  CD    . GLN B 1 43  ? 158.659 131.416 168.619 1.00 60.06 ?  43  GLN B CD    1 
ATOM   5880  O  OE1   . GLN B 1 43  ? 158.053 130.393 168.934 1.00 59.73 ?  43  GLN B OE1   1 
ATOM   5881  N  NE2   . GLN B 1 43  ? 158.728 132.480 169.411 1.00 59.72 ?  43  GLN B NE2   1 
ATOM   5882  N  N     . ASN B 1 44  ? 156.990 133.997 164.104 1.00 56.45 ?  44  ASN B N     1 
ATOM   5883  C  CA    . ASN B 1 44  ? 156.769 134.384 162.718 1.00 56.94 ?  44  ASN B CA    1 
ATOM   5884  C  C     . ASN B 1 44  ? 156.597 135.886 162.539 1.00 55.64 ?  44  ASN B C     1 
ATOM   5885  O  O     . ASN B 1 44  ? 156.510 136.352 161.398 1.00 56.35 ?  44  ASN B O     1 
ATOM   5886  C  CB    . ASN B 1 44  ? 155.543 133.659 162.154 1.00 55.57 ?  44  ASN B CB    1 
ATOM   5887  C  CG    . ASN B 1 44  ? 155.899 132.345 161.491 1.00 56.91 ?  44  ASN B CG    1 
ATOM   5888  O  OD1   . ASN B 1 44  ? 156.724 131.585 161.998 1.00 58.79 ?  44  ASN B OD1   1 
ATOM   5889  N  ND2   . ASN B 1 44  ? 155.276 132.068 160.352 1.00 58.76 ?  44  ASN B ND2   1 
ATOM   5890  N  N     . THR B 1 45  ? 156.542 136.652 163.622 1.00 55.50 ?  45  THR B N     1 
ATOM   5891  C  CA    . THR B 1 45  ? 156.446 138.098 163.507 1.00 56.66 ?  45  THR B CA    1 
ATOM   5892  C  C     . THR B 1 45  ? 157.809 138.695 163.180 1.00 57.37 ?  45  THR B C     1 
ATOM   5893  O  O     . THR B 1 45  ? 158.857 138.124 163.498 1.00 60.83 ?  45  THR B O     1 
ATOM   5894  C  CB    . THR B 1 45  ? 155.886 138.713 164.795 1.00 56.50 ?  45  THR B CB    1 
ATOM   5895  O  OG1   . THR B 1 45  ? 155.605 140.101 164.583 1.00 56.05 ?  45  THR B OG1   1 
ATOM   5896  C  CG2   . THR B 1 45  ? 156.868 138.570 165.950 1.00 55.69 ?  45  THR B CG2   1 
ATOM   5897  N  N     . VAL B 1 46  ? 157.786 139.840 162.506 1.00 56.32 ?  46  VAL B N     1 
ATOM   5898  C  CA    . VAL B 1 46  ? 158.998 140.563 162.142 1.00 57.35 ?  46  VAL B CA    1 
ATOM   5899  C  C     . VAL B 1 46  ? 159.118 141.768 163.064 1.00 57.06 ?  46  VAL B C     1 
ATOM   5900  O  O     . VAL B 1 46  ? 158.273 142.671 163.034 1.00 58.31 ?  46  VAL B O     1 
ATOM   5901  C  CB    . VAL B 1 46  ? 158.976 140.993 160.667 1.00 56.58 ?  46  VAL B CB    1 
ATOM   5902  C  CG1   . VAL B 1 46  ? 160.050 142.033 160.402 1.00 55.16 ?  46  VAL B CG1   1 
ATOM   5903  C  CG2   . VAL B 1 46  ? 159.168 139.790 159.764 1.00 55.55 ?  46  VAL B CG2   1 
ATOM   5904  N  N     . PHE B 1 47  ? 160.162 141.782 163.884 1.00 58.54 ?  47  PHE B N     1 
ATOM   5905  C  CA    . PHE B 1 47  ? 160.384 142.857 164.838 1.00 60.28 ?  47  PHE B CA    1 
ATOM   5906  C  C     . PHE B 1 47  ? 161.485 143.786 164.346 1.00 60.60 ?  47  PHE B C     1 
ATOM   5907  O  O     . PHE B 1 47  ? 162.477 143.351 163.756 1.00 61.43 ?  47  PHE B O     1 
ATOM   5908  C  CB    . PHE B 1 47  ? 160.750 142.303 166.216 1.00 60.54 ?  47  PHE B CB    1 
ATOM   5909  C  CG    . PHE B 1 47  ? 160.527 143.277 167.337 1.00 60.62 ?  47  PHE B CG    1 
ATOM   5910  C  CD1   . PHE B 1 47  ? 159.273 143.819 167.563 1.00 59.97 ?  47  PHE B CD1   1 
ATOM   5911  C  CD2   . PHE B 1 47  ? 161.574 143.654 168.163 1.00 60.05 ?  47  PHE B CD2   1 
ATOM   5912  C  CE1   . PHE B 1 47  ? 159.065 144.715 168.594 1.00 60.86 ?  47  PHE B CE1   1 
ATOM   5913  C  CE2   . PHE B 1 47  ? 161.372 144.550 169.196 1.00 60.57 ?  47  PHE B CE2   1 
ATOM   5914  C  CZ    . PHE B 1 47  ? 160.116 145.082 169.411 1.00 61.43 ?  47  PHE B CZ    1 
ATOM   5915  N  N     . PHE B 1 48  ? 161.296 145.076 164.596 1.00 56.81 ?  48  PHE B N     1 
ATOM   5916  C  CA    . PHE B 1 48  ? 162.260 146.104 164.241 1.00 56.47 ?  48  PHE B CA    1 
ATOM   5917  C  C     . PHE B 1 48  ? 162.791 146.753 165.511 1.00 59.30 ?  48  PHE B C     1 
ATOM   5918  O  O     . PHE B 1 48  ? 162.255 146.554 166.605 1.00 59.94 ?  48  PHE B O     1 
ATOM   5919  C  CB    . PHE B 1 48  ? 161.638 147.165 163.323 1.00 56.72 ?  48  PHE B CB    1 
ATOM   5920  C  CG    . PHE B 1 48  ? 161.114 146.617 162.024 1.00 57.71 ?  48  PHE B CG    1 
ATOM   5921  C  CD1   . PHE B 1 48  ? 159.903 145.947 161.973 1.00 56.37 ?  48  PHE B CD1   1 
ATOM   5922  C  CD2   . PHE B 1 48  ? 161.833 146.777 160.852 1.00 57.45 ?  48  PHE B CD2   1 
ATOM   5923  C  CE1   . PHE B 1 48  ? 159.421 145.448 160.779 1.00 56.89 ?  48  PHE B CE1   1 
ATOM   5924  C  CE2   . PHE B 1 48  ? 161.356 146.278 159.656 1.00 56.57 ?  48  PHE B CE2   1 
ATOM   5925  C  CZ    . PHE B 1 48  ? 160.149 145.612 159.619 1.00 56.22 ?  48  PHE B CZ    1 
ATOM   5926  N  N     . HIS B 1 49  ? 163.864 147.532 165.356 1.00 62.05 ?  49  HIS B N     1 
ATOM   5927  C  CA    . HIS B 1 49  ? 164.462 148.194 166.512 1.00 62.83 ?  49  HIS B CA    1 
ATOM   5928  C  C     . HIS B 1 49  ? 163.483 149.169 167.154 1.00 63.07 ?  49  HIS B C     1 
ATOM   5929  O  O     . HIS B 1 49  ? 163.372 149.229 168.383 1.00 64.37 ?  49  HIS B O     1 
ATOM   5930  C  CB    . HIS B 1 49  ? 165.748 148.911 166.102 1.00 64.35 ?  49  HIS B CB    1 
ATOM   5931  C  CG    . HIS B 1 49  ? 166.483 149.529 167.250 1.00 65.21 ?  49  HIS B CG    1 
ATOM   5932  N  ND1   . HIS B 1 49  ? 166.837 148.817 168.376 1.00 63.91 ?  49  HIS B ND1   1 
ATOM   5933  C  CD2   . HIS B 1 49  ? 166.928 150.792 167.449 1.00 63.74 ?  49  HIS B CD2   1 
ATOM   5934  C  CE1   . HIS B 1 49  ? 167.470 149.614 169.218 1.00 63.98 ?  49  HIS B CE1   1 
ATOM   5935  N  NE2   . HIS B 1 49  ? 167.538 150.819 168.680 1.00 63.41 ?  49  HIS B NE2   1 
ATOM   5936  N  N     . ASN B 1 50  ? 162.766 149.938 166.339 1.00 61.05 ?  50  ASN B N     1 
ATOM   5937  C  CA    . ASN B 1 50  ? 161.707 150.808 166.829 1.00 62.50 ?  50  ASN B CA    1 
ATOM   5938  C  C     . ASN B 1 50  ? 160.652 150.941 165.739 1.00 60.99 ?  50  ASN B C     1 
ATOM   5939  O  O     . ASN B 1 50  ? 160.748 150.327 164.673 1.00 58.84 ?  50  ASN B O     1 
ATOM   5940  C  CB    . ASN B 1 50  ? 162.256 152.172 167.263 1.00 61.56 ?  50  ASN B CB    1 
ATOM   5941  C  CG    . ASN B 1 50  ? 163.108 152.826 166.197 1.00 62.99 ?  50  ASN B CG    1 
ATOM   5942  O  OD1   . ASN B 1 50  ? 163.325 152.261 165.128 1.00 62.27 ?  50  ASN B OD1   1 
ATOM   5943  N  ND2   . ASN B 1 50  ? 163.594 154.027 166.483 1.00 63.03 ?  50  ASN B ND2   1 
ATOM   5944  N  N     . LEU B 1 51  ? 159.631 151.754 166.019 1.00 55.35 ?  51  LEU B N     1 
ATOM   5945  C  CA    . LEU B 1 51  ? 158.531 151.915 165.074 1.00 54.03 ?  51  LEU B CA    1 
ATOM   5946  C  C     . LEU B 1 51  ? 158.978 152.622 163.800 1.00 56.24 ?  51  LEU B C     1 
ATOM   5947  O  O     . LEU B 1 51  ? 158.379 152.418 162.737 1.00 56.85 ?  51  LEU B O     1 
ATOM   5948  C  CB    . LEU B 1 51  ? 157.385 152.679 165.737 1.00 55.44 ?  51  LEU B CB    1 
ATOM   5949  C  CG    . LEU B 1 51  ? 156.083 152.808 164.946 1.00 53.80 ?  51  LEU B CG    1 
ATOM   5950  C  CD1   . LEU B 1 51  ? 155.472 151.440 164.689 1.00 51.80 ?  51  LEU B CD1   1 
ATOM   5951  C  CD2   . LEU B 1 51  ? 155.108 153.707 165.681 1.00 53.40 ?  51  LEU B CD2   1 
ATOM   5952  N  N     . LYS B 1 52  ? 160.017 153.456 163.885 1.00 56.71 ?  52  LYS B N     1 
ATOM   5953  C  CA    . LYS B 1 52  ? 160.480 154.186 162.708 1.00 55.26 ?  52  LYS B CA    1 
ATOM   5954  C  C     . LYS B 1 52  ? 160.971 153.233 161.626 1.00 56.32 ?  52  LYS B C     1 
ATOM   5955  O  O     . LYS B 1 52  ? 160.616 153.376 160.450 1.00 57.80 ?  52  LYS B O     1 
ATOM   5956  C  CB    . LYS B 1 52  ? 161.585 155.167 163.100 1.00 56.33 ?  52  LYS B CB    1 
ATOM   5957  C  CG    . LYS B 1 52  ? 161.290 156.614 162.737 1.00 57.26 ?  52  LYS B CG    1 
ATOM   5958  C  CD    . LYS B 1 52  ? 161.291 156.822 161.233 1.00 58.35 ?  52  LYS B CD    1 
ATOM   5959  C  CE    . LYS B 1 52  ? 160.686 158.168 160.866 1.00 58.29 ?  52  LYS B CE    1 
ATOM   5960  N  NZ    . LYS B 1 52  ? 160.539 158.329 159.393 1.00 58.58 1  52  LYS B NZ    1 
ATOM   5961  N  N     . GLU B 1 53  ? 161.788 152.248 162.008 1.00 59.10 ?  53  GLU B N     1 
ATOM   5962  C  CA    . GLU B 1 53  ? 162.290 151.286 161.032 1.00 59.32 ?  53  GLU B CA    1 
ATOM   5963  C  C     . GLU B 1 53  ? 161.158 150.457 160.444 1.00 57.39 ?  53  GLU B C     1 
ATOM   5964  O  O     . GLU B 1 53  ? 161.152 150.168 159.243 1.00 59.82 ?  53  GLU B O     1 
ATOM   5965  C  CB    . GLU B 1 53  ? 163.343 150.382 161.670 1.00 59.95 ?  53  GLU B CB    1 
ATOM   5966  C  CG    . GLU B 1 53  ? 164.420 151.128 162.433 1.00 60.72 ?  53  GLU B CG    1 
ATOM   5967  C  CD    . GLU B 1 53  ? 165.798 150.536 162.222 1.00 62.00 ?  53  GLU B CD    1 
ATOM   5968  O  OE1   . GLU B 1 53  ? 166.005 149.360 162.590 1.00 62.82 ?  53  GLU B OE1   1 
ATOM   5969  O  OE2   . GLU B 1 53  ? 166.675 151.246 161.686 1.00 61.66 -1 53  GLU B OE2   1 
ATOM   5970  N  N     . LYS B 1 54  ? 160.188 150.067 161.274 1.00 54.54 ?  54  LYS B N     1 
ATOM   5971  C  CA    . LYS B 1 54  ? 159.050 149.301 160.778 1.00 54.20 ?  54  LYS B CA    1 
ATOM   5972  C  C     . LYS B 1 54  ? 158.260 150.097 159.749 1.00 52.54 ?  54  LYS B C     1 
ATOM   5973  O  O     . LYS B 1 54  ? 157.932 149.588 158.669 1.00 52.90 ?  54  LYS B O     1 
ATOM   5974  C  CB    . LYS B 1 54  ? 158.150 148.893 161.944 1.00 53.29 ?  54  LYS B CB    1 
ATOM   5975  C  CG    . LYS B 1 54  ? 156.835 148.272 161.515 1.00 54.25 ?  54  LYS B CG    1 
ATOM   5976  C  CD    . LYS B 1 54  ? 156.243 147.428 162.622 1.00 53.22 ?  54  LYS B CD    1 
ATOM   5977  C  CE    . LYS B 1 54  ? 154.953 146.766 162.182 1.00 53.86 ?  54  LYS B CE    1 
ATOM   5978  N  NZ    . LYS B 1 54  ? 154.665 145.543 162.979 1.00 54.25 1  54  LYS B NZ    1 
ATOM   5979  N  N     . LEU B 1 55  ? 157.948 151.354 160.068 1.00 52.77 ?  55  LEU B N     1 
ATOM   5980  C  CA    . LEU B 1 55  ? 157.183 152.181 159.142 1.00 53.11 ?  55  LEU B CA    1 
ATOM   5981  C  C     . LEU B 1 55  ? 157.958 152.436 157.857 1.00 56.57 ?  55  LEU B C     1 
ATOM   5982  O  O     . LEU B 1 55  ? 157.383 152.391 156.764 1.00 60.90 ?  55  LEU B O     1 
ATOM   5983  C  CB    . LEU B 1 55  ? 156.797 153.500 159.810 1.00 55.67 ?  55  LEU B CB    1 
ATOM   5984  C  CG    . LEU B 1 55  ? 155.556 153.465 160.703 1.00 55.50 ?  55  LEU B CG    1 
ATOM   5985  C  CD1   . LEU B 1 55  ? 154.967 154.856 160.817 1.00 56.44 ?  55  LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B 1 55  ? 154.522 152.484 160.170 1.00 54.78 ?  55  LEU B CD2   1 
ATOM   5987  N  N     . ASP B 1 56  ? 159.263 152.701 157.963 1.00 56.68 ?  56  ASP B N     1 
ATOM   5988  C  CA    . ASP B 1 56  ? 160.065 152.918 156.765 1.00 56.24 ?  56  ASP B CA    1 
ATOM   5989  C  C     . ASP B 1 56  ? 160.107 151.668 155.895 1.00 57.03 ?  56  ASP B C     1 
ATOM   5990  O  O     . ASP B 1 56  ? 159.953 151.749 154.672 1.00 57.75 ?  56  ASP B O     1 
ATOM   5991  C  CB    . ASP B 1 56  ? 161.478 153.354 157.152 1.00 59.58 ?  56  ASP B CB    1 
ATOM   5992  C  CG    . ASP B 1 56  ? 161.500 154.690 157.867 1.00 60.61 ?  56  ASP B CG    1 
ATOM   5993  O  OD1   . ASP B 1 56  ? 160.440 155.348 157.934 1.00 61.48 ?  56  ASP B OD1   1 
ATOM   5994  O  OD2   . ASP B 1 56  ? 162.576 155.083 158.363 1.00 59.36 -1 56  ASP B OD2   1 
ATOM   5995  N  N     . TYR B 1 57  ? 160.304 150.499 156.510 1.00 55.74 ?  57  TYR B N     1 
ATOM   5996  C  CA    . TYR B 1 57  ? 160.343 149.259 155.745 1.00 56.06 ?  57  TYR B CA    1 
ATOM   5997  C  C     . TYR B 1 57  ? 159.009 148.995 155.063 1.00 56.30 ?  57  TYR B C     1 
ATOM   5998  O  O     . TYR B 1 57  ? 158.970 148.558 153.908 1.00 60.11 ?  57  TYR B O     1 
ATOM   5999  C  CB    . TYR B 1 57  ? 160.724 148.091 156.658 1.00 55.53 ?  57  TYR B CB    1 
ATOM   6000  C  CG    . TYR B 1 57  ? 160.603 146.727 156.012 1.00 56.81 ?  57  TYR B CG    1 
ATOM   6001  C  CD1   . TYR B 1 57  ? 161.651 146.194 155.275 1.00 57.13 ?  57  TYR B CD1   1 
ATOM   6002  C  CD2   . TYR B 1 57  ? 159.446 145.969 156.148 1.00 59.01 ?  57  TYR B CD2   1 
ATOM   6003  C  CE1   . TYR B 1 57  ? 161.549 144.949 154.685 1.00 57.09 ?  57  TYR B CE1   1 
ATOM   6004  C  CE2   . TYR B 1 57  ? 159.335 144.725 155.560 1.00 59.36 ?  57  TYR B CE2   1 
ATOM   6005  C  CZ    . TYR B 1 57  ? 160.390 144.218 154.831 1.00 59.35 ?  57  TYR B CZ    1 
ATOM   6006  O  OH    . TYR B 1 57  ? 160.282 142.978 154.245 1.00 59.74 ?  57  TYR B OH    1 
ATOM   6007  N  N     . LEU B 1 58  ? 157.901 149.255 155.760 1.00 53.38 ?  58  LEU B N     1 
ATOM   6008  C  CA    . LEU B 1 58  ? 156.592 149.026 155.160 1.00 52.61 ?  58  LEU B CA    1 
ATOM   6009  C  C     . LEU B 1 58  ? 156.273 150.056 154.084 1.00 51.55 ?  58  LEU B C     1 
ATOM   6010  O  O     . LEU B 1 58  ? 155.482 149.775 153.177 1.00 53.00 ?  58  LEU B O     1 
ATOM   6011  C  CB    . LEU B 1 58  ? 155.515 149.024 156.245 1.00 52.55 ?  58  LEU B CB    1 
ATOM   6012  C  CG    . LEU B 1 58  ? 155.609 147.857 157.232 1.00 52.17 ?  58  LEU B CG    1 
ATOM   6013  C  CD1   . LEU B 1 58  ? 154.801 148.135 158.487 1.00 52.11 ?  58  LEU B CD1   1 
ATOM   6014  C  CD2   . LEU B 1 58  ? 155.160 146.562 156.578 1.00 53.03 ?  58  LEU B CD2   1 
ATOM   6015  N  N     . VAL B 1 59  ? 156.871 151.245 154.159 1.00 55.47 ?  59  VAL B N     1 
ATOM   6016  C  CA    . VAL B 1 59  ? 156.584 152.277 153.170 1.00 56.82 ?  59  VAL B CA    1 
ATOM   6017  C  C     . VAL B 1 59  ? 157.398 152.056 151.899 1.00 57.98 ?  59  VAL B C     1 
ATOM   6018  O  O     . VAL B 1 59  ? 156.853 152.065 150.789 1.00 56.51 ?  59  VAL B O     1 
ATOM   6019  C  CB    . VAL B 1 59  ? 156.831 153.673 153.769 1.00 56.13 ?  59  VAL B CB    1 
ATOM   6020  C  CG1   . VAL B 1 59  ? 157.113 154.688 152.672 1.00 55.82 ?  59  VAL B CG1   1 
ATOM   6021  C  CG2   . VAL B 1 59  ? 155.638 154.107 154.606 1.00 55.43 ?  59  VAL B CG2   1 
ATOM   6022  N  N     . GLU B 1 60  ? 158.713 151.853 152.035 1.00 59.74 ?  60  GLU B N     1 
ATOM   6023  C  CA    . GLU B 1 60  ? 159.550 151.701 150.847 1.00 59.69 ?  60  GLU B CA    1 
ATOM   6024  C  C     . GLU B 1 60  ? 159.291 150.384 150.125 1.00 59.71 ?  60  GLU B C     1 
ATOM   6025  O  O     . GLU B 1 60  ? 159.452 150.314 148.901 1.00 61.21 ?  60  GLU B O     1 
ATOM   6026  C  CB    . GLU B 1 60  ? 161.033 151.822 151.204 1.00 59.21 ?  60  GLU B CB    1 
ATOM   6027  C  CG    . GLU B 1 60  ? 161.362 152.910 152.209 1.00 60.66 ?  60  GLU B CG    1 
ATOM   6028  C  CD    . GLU B 1 60  ? 162.459 152.498 153.171 1.00 62.93 ?  60  GLU B CD    1 
ATOM   6029  O  OE1   . GLU B 1 60  ? 162.996 153.377 153.876 1.00 59.92 ?  60  GLU B OE1   1 
ATOM   6030  O  OE2   . GLU B 1 60  ? 162.786 151.293 153.223 1.00 61.95 -1 60  GLU B OE2   1 
ATOM   6031  N  N     . ASN B 1 61  ? 158.899 149.337 150.848 1.00 55.81 ?  61  ASN B N     1 
ATOM   6032  C  CA    . ASN B 1 61  ? 158.624 148.042 150.242 1.00 56.10 ?  61  ASN B CA    1 
ATOM   6033  C  C     . ASN B 1 61  ? 157.208 147.940 149.688 1.00 56.29 ?  61  ASN B C     1 
ATOM   6034  O  O     . ASN B 1 61  ? 156.731 146.828 149.433 1.00 58.43 ?  61  ASN B O     1 
ATOM   6035  C  CB    . ASN B 1 61  ? 158.880 146.920 151.250 1.00 56.83 ?  61  ASN B CB    1 
ATOM   6036  C  CG    . ASN B 1 61  ? 160.355 146.710 151.523 1.00 58.89 ?  61  ASN B CG    1 
ATOM   6037  O  OD1   . ASN B 1 61  ? 160.989 145.838 150.930 1.00 58.92 ?  61  ASN B OD1   1 
ATOM   6038  N  ND2   . ASN B 1 61  ? 160.911 147.517 152.419 1.00 58.89 ?  61  ASN B ND2   1 
ATOM   6039  N  N     . GLN B 1 62  ? 156.534 149.077 149.500 1.00 55.77 ?  62  GLN B N     1 
ATOM   6040  C  CA    . GLN B 1 62  ? 155.207 149.134 148.883 1.00 57.06 ?  62  GLN B CA    1 
ATOM   6041  C  C     . GLN B 1 62  ? 154.186 148.294 149.648 1.00 55.48 ?  62  GLN B C     1 
ATOM   6042  O  O     . GLN B 1 62  ? 153.303 147.669 149.060 1.00 56.00 ?  62  GLN B O     1 
ATOM   6043  C  CB    . GLN B 1 62  ? 155.264 148.714 147.411 1.00 54.59 ?  62  GLN B CB    1 
ATOM   6044  C  CG    . GLN B 1 62  ? 156.366 149.394 146.615 1.00 55.59 ?  62  GLN B CG    1 
ATOM   6045  C  CD    . GLN B 1 62  ? 156.409 150.894 146.835 1.00 58.59 ?  62  GLN B CD    1 
ATOM   6046  O  OE1   . GLN B 1 62  ? 155.518 151.623 146.398 1.00 58.31 ?  62  GLN B OE1   1 
ATOM   6047  N  NE2   . GLN B 1 62  ? 157.449 151.363 147.514 1.00 57.60 ?  62  GLN B NE2   1 
ATOM   6048  N  N     . TYR B 1 63  ? 154.309 148.277 150.974 1.00 52.92 ?  63  TYR B N     1 
ATOM   6049  C  CA    . TYR B 1 63  ? 153.284 147.681 151.822 1.00 52.23 ?  63  TYR B CA    1 
ATOM   6050  C  C     . TYR B 1 63  ? 152.250 148.709 152.259 1.00 52.08 ?  63  TYR B C     1 
ATOM   6051  O  O     . TYR B 1 63  ? 151.056 148.397 152.331 1.00 51.06 ?  63  TYR B O     1 
ATOM   6052  C  CB    . TYR B 1 63  ? 153.915 147.035 153.058 1.00 51.41 ?  63  TYR B CB    1 
ATOM   6053  C  CG    . TYR B 1 63  ? 154.666 145.756 152.779 1.00 53.74 ?  63  TYR B CG    1 
ATOM   6054  C  CD1   . TYR B 1 63  ? 154.009 144.634 152.298 1.00 51.61 ?  63  TYR B CD1   1 
ATOM   6055  C  CD2   . TYR B 1 63  ? 156.032 145.670 153.008 1.00 53.83 ?  63  TYR B CD2   1 
ATOM   6056  C  CE1   . TYR B 1 63  ? 154.693 143.461 152.046 1.00 54.06 ?  63  TYR B CE1   1 
ATOM   6057  C  CE2   . TYR B 1 63  ? 156.724 144.504 152.760 1.00 52.91 ?  63  TYR B CE2   1 
ATOM   6058  C  CZ    . TYR B 1 63  ? 156.052 143.403 152.279 1.00 55.02 ?  63  TYR B CZ    1 
ATOM   6059  O  OH    . TYR B 1 63  ? 156.742 142.241 152.030 1.00 55.71 ?  63  TYR B OH    1 
ATOM   6060  N  N     . TYR B 1 64  ? 152.690 149.929 152.549 1.00 49.23 ?  64  TYR B N     1 
ATOM   6061  C  CA    . TYR B 1 64  ? 151.828 150.994 153.033 1.00 46.99 ?  64  TYR B CA    1 
ATOM   6062  C  C     . TYR B 1 64  ? 151.830 152.160 152.056 1.00 48.94 ?  64  TYR B C     1 
ATOM   6063  O  O     . TYR B 1 64  ? 152.837 152.441 151.401 1.00 50.62 ?  64  TYR B O     1 
ATOM   6064  C  CB    . TYR B 1 64  ? 152.282 151.496 154.406 1.00 47.69 ?  64  TYR B CB    1 
ATOM   6065  C  CG    . TYR B 1 64  ? 151.900 150.606 155.560 1.00 47.26 ?  64  TYR B CG    1 
ATOM   6066  C  CD1   . TYR B 1 64  ? 151.121 149.473 155.366 1.00 47.65 ?  64  TYR B CD1   1 
ATOM   6067  C  CD2   . TYR B 1 64  ? 152.323 150.898 156.847 1.00 47.78 ?  64  TYR B CD2   1 
ATOM   6068  C  CE1   . TYR B 1 64  ? 150.774 148.659 156.423 1.00 45.62 ?  64  TYR B CE1   1 
ATOM   6069  C  CE2   . TYR B 1 64  ? 151.982 150.093 157.906 1.00 48.04 ?  64  TYR B CE2   1 
ATOM   6070  C  CZ    . TYR B 1 64  ? 151.209 148.975 157.692 1.00 47.45 ?  64  TYR B CZ    1 
ATOM   6071  O  OH    . TYR B 1 64  ? 150.873 148.176 158.756 1.00 49.14 ?  64  TYR B OH    1 
ATOM   6072  N  N     . GLU B 1 65  ? 150.688 152.834 151.964 1.00 51.99 ?  65  GLU B N     1 
ATOM   6073  C  CA    . GLU B 1 65  ? 150.639 154.114 151.275 1.00 51.96 ?  65  GLU B CA    1 
ATOM   6074  C  C     . GLU B 1 65  ? 151.286 155.180 152.150 1.00 54.39 ?  65  GLU B C     1 
ATOM   6075  O  O     . GLU B 1 65  ? 150.978 155.291 153.340 1.00 55.86 ?  65  GLU B O     1 
ATOM   6076  C  CB    . GLU B 1 65  ? 149.195 154.491 150.949 1.00 50.39 ?  65  GLU B CB    1 
ATOM   6077  C  CG    . GLU B 1 65  ? 148.452 153.445 150.134 1.00 51.97 ?  65  GLU B CG    1 
ATOM   6078  C  CD    . GLU B 1 65  ? 146.997 153.806 149.911 1.00 55.50 ?  65  GLU B CD    1 
ATOM   6079  O  OE1   . GLU B 1 65  ? 146.397 154.444 150.801 1.00 54.42 ?  65  GLU B OE1   1 
ATOM   6080  O  OE2   . GLU B 1 65  ? 146.453 153.451 148.844 1.00 54.21 -1 65  GLU B OE2   1 
ATOM   6081  N  N     . GLU B 1 66  ? 152.195 155.959 151.566 1.00 52.84 ?  66  GLU B N     1 
ATOM   6082  C  CA    . GLU B 1 66  ? 152.907 156.966 152.341 1.00 54.72 ?  66  GLU B CA    1 
ATOM   6083  C  C     . GLU B 1 66  ? 152.098 158.240 152.540 1.00 54.99 ?  66  GLU B C     1 
ATOM   6084  O  O     . GLU B 1 66  ? 152.441 159.043 153.414 1.00 54.13 ?  66  GLU B O     1 
ATOM   6085  C  CB    . GLU B 1 66  ? 154.242 157.298 151.668 1.00 55.88 ?  66  GLU B CB    1 
ATOM   6086  C  CG    . GLU B 1 66  ? 154.137 158.291 150.525 1.00 55.41 ?  66  GLU B CG    1 
ATOM   6087  C  CD    . GLU B 1 66  ? 155.480 158.879 150.142 1.00 56.78 ?  66  GLU B CD    1 
ATOM   6088  O  OE1   . GLU B 1 66  ? 156.483 158.135 150.171 1.00 55.65 ?  66  GLU B OE1   1 
ATOM   6089  O  OE2   . GLU B 1 66  ? 155.532 160.082 149.814 1.00 56.59 -1 66  GLU B OE2   1 
ATOM   6090  N  N     . GLU B 1 67  ? 151.029 158.434 151.767 1.00 53.83 ?  67  GLU B N     1 
ATOM   6091  C  CA    . GLU B 1 67  ? 150.271 159.679 151.846 1.00 53.55 ?  67  GLU B CA    1 
ATOM   6092  C  C     . GLU B 1 67  ? 149.547 159.807 153.180 1.00 55.20 ?  67  GLU B C     1 
ATOM   6093  O  O     . GLU B 1 67  ? 149.598 160.861 153.824 1.00 55.05 ?  67  GLU B O     1 
ATOM   6094  C  CB    . GLU B 1 67  ? 149.279 159.780 150.682 1.00 54.00 ?  67  GLU B CB    1 
ATOM   6095  C  CG    . GLU B 1 67  ? 149.864 159.562 149.284 1.00 55.13 ?  67  GLU B CG    1 
ATOM   6096  C  CD    . GLU B 1 67  ? 150.212 158.115 148.989 1.00 58.09 ?  67  GLU B CD    1 
ATOM   6097  O  OE1   . GLU B 1 67  ? 151.376 157.845 148.625 1.00 57.11 ?  67  GLU B OE1   1 
ATOM   6098  O  OE2   . GLU B 1 67  ? 149.322 157.249 149.120 1.00 56.98 -1 67  GLU B OE2   1 
ATOM   6099  N  N     . PHE B 1 68  ? 148.863 158.745 153.614 1.00 50.07 ?  68  PHE B N     1 
ATOM   6100  C  CA    . PHE B 1 68  ? 148.103 158.831 154.857 1.00 46.19 ?  68  PHE B CA    1 
ATOM   6101  C  C     . PHE B 1 68  ? 149.020 158.901 156.072 1.00 46.50 ?  68  PHE B C     1 
ATOM   6102  O  O     . PHE B 1 68  ? 148.665 159.527 157.077 1.00 50.04 ?  68  PHE B O     1 
ATOM   6103  C  CB    . PHE B 1 68  ? 147.127 157.656 154.967 1.00 47.47 ?  68  PHE B CB    1 
ATOM   6104  C  CG    . PHE B 1 68  ? 147.677 156.460 155.694 1.00 47.17 ?  68  PHE B CG    1 
ATOM   6105  C  CD1   . PHE B 1 68  ? 148.443 155.522 155.029 1.00 45.17 ?  68  PHE B CD1   1 
ATOM   6106  C  CD2   . PHE B 1 68  ? 147.400 156.262 157.036 1.00 43.14 ?  68  PHE B CD2   1 
ATOM   6107  C  CE1   . PHE B 1 68  ? 148.942 154.419 155.693 1.00 44.22 ?  68  PHE B CE1   1 
ATOM   6108  C  CE2   . PHE B 1 68  ? 147.895 155.162 157.705 1.00 42.72 ?  68  PHE B CE2   1 
ATOM   6109  C  CZ    . PHE B 1 68  ? 148.665 154.238 157.031 1.00 44.93 ?  68  PHE B CZ    1 
ATOM   6110  N  N     . LEU B 1 69  ? 150.194 158.272 156.003 1.00 49.73 ?  69  LEU B N     1 
ATOM   6111  C  CA    . LEU B 1 69  ? 151.165 158.379 157.083 1.00 47.63 ?  69  LEU B CA    1 
ATOM   6112  C  C     . LEU B 1 69  ? 151.894 159.714 157.083 1.00 48.62 ?  69  LEU B C     1 
ATOM   6113  O  O     . LEU B 1 69  ? 152.406 160.124 158.131 1.00 52.37 ?  69  LEU B O     1 
ATOM   6114  C  CB    . LEU B 1 69  ? 152.184 157.241 156.994 1.00 47.53 ?  69  LEU B CB    1 
ATOM   6115  C  CG    . LEU B 1 69  ? 151.734 155.877 157.519 1.00 47.12 ?  69  LEU B CG    1 
ATOM   6116  C  CD1   . LEU B 1 69  ? 152.753 154.803 157.170 1.00 48.48 ?  69  LEU B CD1   1 
ATOM   6117  C  CD2   . LEU B 1 69  ? 151.495 155.928 159.019 1.00 47.04 ?  69  LEU B CD2   1 
ATOM   6118  N  N     . SER B 1 70  ? 151.955 160.400 155.939 1.00 48.36 ?  70  SER B N     1 
ATOM   6119  C  CA    . SER B 1 70  ? 152.651 161.680 155.874 1.00 47.28 ?  70  SER B CA    1 
ATOM   6120  C  C     . SER B 1 70  ? 151.864 162.805 156.533 1.00 49.11 ?  70  SER B C     1 
ATOM   6121  O  O     . SER B 1 70  ? 152.438 163.865 156.805 1.00 51.02 ?  70  SER B O     1 
ATOM   6122  C  CB    . SER B 1 70  ? 152.952 162.041 154.419 1.00 49.35 ?  70  SER B CB    1 
ATOM   6123  O  OG    . SER B 1 70  ? 151.799 162.546 153.769 1.00 49.06 ?  70  SER B OG    1 
ATOM   6124  N  N     . LEU B 1 71  ? 150.572 162.606 156.794 1.00 46.46 ?  71  LEU B N     1 
ATOM   6125  C  CA    . LEU B 1 71  ? 149.768 163.624 157.454 1.00 45.72 ?  71  LEU B CA    1 
ATOM   6126  C  C     . LEU B 1 71  ? 150.065 163.742 158.941 1.00 45.67 ?  71  LEU B C     1 
ATOM   6127  O  O     . LEU B 1 71  ? 149.602 164.696 159.574 1.00 46.85 ?  71  LEU B O     1 
ATOM   6128  C  CB    . LEU B 1 71  ? 148.278 163.335 157.254 1.00 44.59 ?  71  LEU B CB    1 
ATOM   6129  C  CG    . LEU B 1 71  ? 147.791 163.221 155.810 1.00 47.01 ?  71  LEU B CG    1 
ATOM   6130  C  CD1   . LEU B 1 71  ? 146.738 162.134 155.690 1.00 49.18 ?  71  LEU B CD1   1 
ATOM   6131  C  CD2   . LEU B 1 71  ? 147.247 164.553 155.325 1.00 45.72 ?  71  LEU B CD2   1 
ATOM   6132  N  N     . TYR B 1 72  ? 150.816 162.804 159.509 1.00 43.56 ?  72  TYR B N     1 
ATOM   6133  C  CA    . TYR B 1 72  ? 151.184 162.824 160.916 1.00 44.85 ?  72  TYR B CA    1 
ATOM   6134  C  C     . TYR B 1 72  ? 152.696 162.898 161.050 1.00 46.70 ?  72  TYR B C     1 
ATOM   6135  O  O     . TYR B 1 72  ? 153.428 162.267 160.279 1.00 48.51 ?  72  TYR B O     1 
ATOM   6136  C  CB    . TYR B 1 72  ? 150.686 161.576 161.657 1.00 45.55 ?  72  TYR B CB    1 
ATOM   6137  C  CG    . TYR B 1 72  ? 149.247 161.197 161.402 1.00 42.98 ?  72  TYR B CG    1 
ATOM   6138  C  CD1   . TYR B 1 72  ? 148.890 160.461 160.279 1.00 42.35 ?  72  TYR B CD1   1 
ATOM   6139  C  CD2   . TYR B 1 72  ? 148.249 161.548 162.299 1.00 42.77 ?  72  TYR B CD2   1 
ATOM   6140  C  CE1   . TYR B 1 72  ? 147.579 160.104 160.049 1.00 40.87 ?  72  TYR B CE1   1 
ATOM   6141  C  CE2   . TYR B 1 72  ? 146.935 161.194 162.079 1.00 42.72 ?  72  TYR B CE2   1 
ATOM   6142  C  CZ    . TYR B 1 72  ? 146.606 160.474 160.951 1.00 42.62 ?  72  TYR B CZ    1 
ATOM   6143  O  OH    . TYR B 1 72  ? 145.299 160.119 160.723 1.00 45.08 ?  72  TYR B OH    1 
ATOM   6144  N  N     . SER B 1 73  ? 153.161 163.668 162.027 1.00 52.19 ?  73  SER B N     1 
ATOM   6145  C  CA    . SER B 1 73  ? 154.550 163.562 162.444 1.00 52.49 ?  73  SER B CA    1 
ATOM   6146  C  C     . SER B 1 73  ? 154.777 162.202 163.093 1.00 51.86 ?  73  SER B C     1 
ATOM   6147  O  O     . SER B 1 73  ? 153.849 161.583 163.620 1.00 54.01 ?  73  SER B O     1 
ATOM   6148  C  CB    . SER B 1 73  ? 154.908 164.684 163.418 1.00 51.38 ?  73  SER B CB    1 
ATOM   6149  O  OG    . SER B 1 73  ? 154.409 164.411 164.715 1.00 50.60 ?  73  SER B OG    1 
ATOM   6150  N  N     . PHE B 1 74  ? 156.024 161.727 163.037 1.00 54.68 ?  74  PHE B N     1 
ATOM   6151  C  CA    . PHE B 1 74  ? 156.304 160.395 163.564 1.00 53.82 ?  74  PHE B CA    1 
ATOM   6152  C  C     . PHE B 1 74  ? 156.018 160.303 165.056 1.00 54.02 ?  74  PHE B C     1 
ATOM   6153  O  O     . PHE B 1 74  ? 155.706 159.219 165.559 1.00 55.52 ?  74  PHE B O     1 
ATOM   6154  C  CB    . PHE B 1 74  ? 157.750 159.988 163.289 1.00 54.59 ?  74  PHE B CB    1 
ATOM   6155  C  CG    . PHE B 1 74  ? 158.135 158.693 163.941 1.00 55.45 ?  74  PHE B CG    1 
ATOM   6156  C  CD1   . PHE B 1 74  ? 157.606 157.496 163.489 1.00 53.33 ?  74  PHE B CD1   1 
ATOM   6157  C  CD2   . PHE B 1 74  ? 159.002 158.672 165.020 1.00 55.41 ?  74  PHE B CD2   1 
ATOM   6158  C  CE1   . PHE B 1 74  ? 157.942 156.301 164.092 1.00 55.48 ?  74  PHE B CE1   1 
ATOM   6159  C  CE2   . PHE B 1 74  ? 159.343 157.479 165.628 1.00 55.10 ?  74  PHE B CE2   1 
ATOM   6160  C  CZ    . PHE B 1 74  ? 158.813 156.292 165.164 1.00 55.55 ?  74  PHE B CZ    1 
ATOM   6161  N  N     . GLU B 1 75  ? 156.118 161.419 165.781 1.00 54.99 ?  75  GLU B N     1 
ATOM   6162  C  CA    . GLU B 1 75  ? 155.761 161.404 167.196 1.00 56.01 ?  75  GLU B CA    1 
ATOM   6163  C  C     . GLU B 1 75  ? 154.288 161.067 167.384 1.00 56.55 ?  75  GLU B C     1 
ATOM   6164  O  O     . GLU B 1 75  ? 153.927 160.299 168.283 1.00 57.06 ?  75  GLU B O     1 
ATOM   6165  C  CB    . GLU B 1 75  ? 156.094 162.751 167.838 1.00 56.12 ?  75  GLU B CB    1 
ATOM   6166  C  CG    . GLU B 1 75  ? 157.489 162.834 168.441 1.00 56.08 ?  75  GLU B CG    1 
ATOM   6167  C  CD    . GLU B 1 75  ? 158.547 162.189 167.568 1.00 59.46 ?  75  GLU B CD    1 
ATOM   6168  O  OE1   . GLU B 1 75  ? 158.871 162.759 166.504 1.00 59.31 ?  75  GLU B OE1   1 
ATOM   6169  O  OE2   . GLU B 1 75  ? 159.057 161.112 167.945 1.00 59.07 -1 75  GLU B OE2   1 
ATOM   6170  N  N     . ASP B 1 76  ? 153.423 161.624 166.534 1.00 52.52 ?  76  ASP B N     1 
ATOM   6171  C  CA    . ASP B 1 76  ? 151.996 161.333 166.624 1.00 51.01 ?  76  ASP B CA    1 
ATOM   6172  C  C     . ASP B 1 76  ? 151.700 159.875 166.291 1.00 49.96 ?  76  ASP B C     1 
ATOM   6173  O  O     . ASP B 1 76  ? 150.872 159.237 166.951 1.00 53.31 ?  76  ASP B O     1 
ATOM   6174  C  CB    . ASP B 1 76  ? 151.221 162.268 165.699 1.00 52.34 ?  76  ASP B CB    1 
ATOM   6175  C  CG    . ASP B 1 76  ? 151.203 163.696 166.205 1.00 54.36 ?  76  ASP B CG    1 
ATOM   6176  O  OD1   . ASP B 1 76  ? 151.641 163.926 167.351 1.00 53.96 ?  76  ASP B OD1   1 
ATOM   6177  O  OD2   . ASP B 1 76  ? 150.752 164.589 165.456 1.00 53.46 -1 76  ASP B OD2   1 
ATOM   6178  N  N     . ILE B 1 77  ? 152.363 159.330 165.268 1.00 47.36 ?  77  ILE B N     1 
ATOM   6179  C  CA    . ILE B 1 77  ? 152.172 157.924 164.922 1.00 47.58 ?  77  ILE B CA    1 
ATOM   6180  C  C     . ILE B 1 77  ? 152.655 157.027 166.052 1.00 48.60 ?  77  ILE B C     1 
ATOM   6181  O  O     . ILE B 1 77  ? 152.023 156.012 166.379 1.00 50.21 ?  77  ILE B O     1 
ATOM   6182  C  CB    . ILE B 1 77  ? 152.886 157.596 163.599 1.00 49.12 ?  77  ILE B CB    1 
ATOM   6183  C  CG1   . ILE B 1 77  ? 152.370 158.496 162.477 1.00 48.20 ?  77  ILE B CG1   1 
ATOM   6184  C  CG2   . ILE B 1 77  ? 152.686 156.136 163.239 1.00 46.74 ?  77  ILE B CG2   1 
ATOM   6185  C  CD1   . ILE B 1 77  ? 153.210 158.448 161.223 1.00 45.94 ?  77  ILE B CD1   1 
ATOM   6186  N  N     . LYS B 1 78  ? 153.792 157.377 166.658 1.00 50.55 ?  78  LYS B N     1 
ATOM   6187  C  CA    . LYS B 1 78  ? 154.290 156.626 167.804 1.00 50.70 ?  78  LYS B CA    1 
ATOM   6188  C  C     . LYS B 1 78  ? 153.302 156.674 168.959 1.00 49.63 ?  78  LYS B C     1 
ATOM   6189  O  O     . LYS B 1 78  ? 153.074 155.663 169.630 1.00 50.68 ?  78  LYS B O     1 
ATOM   6190  C  CB    . LYS B 1 78  ? 155.648 157.177 168.239 1.00 53.57 ?  78  LYS B CB    1 
ATOM   6191  C  CG    . LYS B 1 78  ? 156.516 156.186 168.993 1.00 52.73 ?  78  LYS B CG    1 
ATOM   6192  C  CD    . LYS B 1 78  ? 157.480 156.909 169.918 1.00 53.81 ?  78  LYS B CD    1 
ATOM   6193  C  CE    . LYS B 1 78  ? 158.633 156.014 170.333 1.00 54.50 ?  78  LYS B CE    1 
ATOM   6194  N  NZ    . LYS B 1 78  ? 159.929 156.479 169.765 1.00 52.68 1  78  LYS B NZ    1 
ATOM   6195  N  N     . GLU B 1 79  ? 152.706 157.842 169.205 1.00 51.71 ?  79  GLU B N     1 
ATOM   6196  C  CA    . GLU B 1 79  ? 151.716 157.962 170.270 1.00 51.17 ?  79  GLU B CA    1 
ATOM   6197  C  C     . GLU B 1 79  ? 150.484 157.113 169.976 1.00 49.54 ?  79  GLU B C     1 
ATOM   6198  O  O     . GLU B 1 79  ? 149.926 156.484 170.881 1.00 51.83 ?  79  GLU B O     1 
ATOM   6199  C  CB    . GLU B 1 79  ? 151.336 159.431 170.456 1.00 49.44 ?  79  GLU B CB    1 
ATOM   6200  C  CG    . GLU B 1 79  ? 152.026 160.096 171.637 1.00 52.62 ?  79  GLU B CG    1 
ATOM   6201  C  CD    . GLU B 1 79  ? 151.282 161.315 172.141 1.00 56.12 ?  79  GLU B CD    1 
ATOM   6202  O  OE1   . GLU B 1 79  ? 151.678 161.861 173.193 1.00 54.05 ?  79  GLU B OE1   1 
ATOM   6203  O  OE2   . GLU B 1 79  ? 150.312 161.738 171.480 1.00 56.75 -1 79  GLU B OE2   1 
ATOM   6204  N  N     . VAL B 1 80  ? 150.052 157.077 168.715 1.00 43.97 ?  80  VAL B N     1 
ATOM   6205  C  CA    . VAL B 1 80  ? 148.905 156.253 168.338 1.00 41.94 ?  80  VAL B CA    1 
ATOM   6206  C  C     . VAL B 1 80  ? 149.212 154.772 168.542 1.00 46.28 ?  80  VAL B C     1 
ATOM   6207  O  O     . VAL B 1 80  ? 148.392 154.019 169.085 1.00 48.04 ?  80  VAL B O     1 
ATOM   6208  C  CB    . VAL B 1 80  ? 148.497 156.558 166.885 1.00 43.34 ?  80  VAL B CB    1 
ATOM   6209  C  CG1   . VAL B 1 80  ? 147.558 155.491 166.353 1.00 44.32 ?  80  VAL B CG1   1 
ATOM   6210  C  CG2   . VAL B 1 80  ? 147.852 157.931 166.796 1.00 44.52 ?  80  VAL B CG2   1 
ATOM   6211  N  N     . PHE B 1 81  ? 150.398 154.330 168.116 1.00 46.65 ?  81  PHE B N     1 
ATOM   6212  C  CA    . PHE B 1 81  ? 150.774 152.930 168.296 1.00 43.06 ?  81  PHE B CA    1 
ATOM   6213  C  C     . PHE B 1 81  ? 150.910 152.579 169.774 1.00 45.86 ?  81  PHE B C     1 
ATOM   6214  O  O     . PHE B 1 81  ? 150.537 151.478 170.197 1.00 48.13 ?  81  PHE B O     1 
ATOM   6215  C  CB    . PHE B 1 81  ? 152.074 152.637 167.549 1.00 40.92 ?  81  PHE B CB    1 
ATOM   6216  C  CG    . PHE B 1 81  ? 151.871 152.191 166.129 1.00 40.82 ?  81  PHE B CG    1 
ATOM   6217  C  CD1   . PHE B 1 81  ? 151.653 153.119 165.123 1.00 41.95 ?  81  PHE B CD1   1 
ATOM   6218  C  CD2   . PHE B 1 81  ? 151.896 150.849 165.799 1.00 42.08 ?  81  PHE B CD2   1 
ATOM   6219  C  CE1   . PHE B 1 81  ? 151.467 152.712 163.815 1.00 43.36 ?  81  PHE B CE1   1 
ATOM   6220  C  CE2   . PHE B 1 81  ? 151.710 150.438 164.493 1.00 42.11 ?  81  PHE B CE2   1 
ATOM   6221  C  CZ    . PHE B 1 81  ? 151.495 151.371 163.501 1.00 41.06 ?  81  PHE B CZ    1 
ATOM   6222  N  N     . LYS B 1 82  ? 151.451 153.501 170.573 1.00 47.33 ?  82  LYS B N     1 
ATOM   6223  C  CA    . LYS B 1 82  ? 151.551 153.274 172.010 1.00 46.06 ?  82  LYS B CA    1 
ATOM   6224  C  C     . LYS B 1 82  ? 150.172 153.188 172.649 1.00 44.98 ?  82  LYS B C     1 
ATOM   6225  O  O     . LYS B 1 82  ? 149.953 152.386 173.560 1.00 46.57 ?  82  LYS B O     1 
ATOM   6226  C  CB    . LYS B 1 82  ? 152.378 154.381 172.662 1.00 46.55 ?  82  LYS B CB    1 
ATOM   6227  C  CG    . LYS B 1 82  ? 153.871 154.270 172.411 1.00 47.41 ?  82  LYS B CG    1 
ATOM   6228  C  CD    . LYS B 1 82  ? 154.589 153.692 173.618 1.00 47.76 ?  82  LYS B CD    1 
ATOM   6229  C  CE    . LYS B 1 82  ? 154.322 154.519 174.865 1.00 49.18 ?  82  LYS B CE    1 
ATOM   6230  N  NZ    . LYS B 1 82  ? 155.116 155.778 174.876 1.00 48.24 1  82  LYS B NZ    1 
ATOM   6231  N  N     . THR B 1 83  ? 149.229 154.011 172.186 1.00 42.72 ?  83  THR B N     1 
ATOM   6232  C  CA    . THR B 1 83  ? 147.858 153.910 172.674 1.00 41.20 ?  83  THR B CA    1 
ATOM   6233  C  C     . THR B 1 83  ? 147.253 152.559 172.316 1.00 42.79 ?  83  THR B C     1 
ATOM   6234  O  O     . THR B 1 83  ? 146.528 151.960 173.119 1.00 45.00 ?  83  THR B O     1 
ATOM   6235  C  CB    . THR B 1 83  ? 147.012 155.047 172.101 1.00 41.20 ?  83  THR B CB    1 
ATOM   6236  O  OG1   . THR B 1 83  ? 147.589 156.305 172.474 1.00 46.81 ?  83  THR B OG1   1 
ATOM   6237  C  CG2   . THR B 1 83  ? 145.590 154.977 172.631 1.00 44.21 ?  83  THR B CG2   1 
ATOM   6238  N  N     . ALA B 1 84  ? 147.540 152.066 171.109 1.00 41.52 ?  84  ALA B N     1 
ATOM   6239  C  CA    . ALA B 1 84  ? 147.037 150.754 170.709 1.00 38.00 ?  84  ALA B CA    1 
ATOM   6240  C  C     . ALA B 1 84  ? 147.615 149.644 171.576 1.00 38.28 ?  84  ALA B C     1 
ATOM   6241  O  O     . ALA B 1 84  ? 146.895 148.729 171.989 1.00 43.99 ?  84  ALA B O     1 
ATOM   6242  C  CB    . ALA B 1 84  ? 147.347 150.499 169.237 1.00 39.60 ?  84  ALA B CB    1 
ATOM   6243  N  N     . TYR B 1 85  ? 148.915 149.705 171.860 1.00 45.05 ?  85  TYR B N     1 
ATOM   6244  C  CA    . TYR B 1 85  ? 149.568 148.657 172.637 1.00 43.36 ?  85  TYR B CA    1 
ATOM   6245  C  C     . TYR B 1 85  ? 149.369 148.802 174.142 1.00 44.29 ?  85  TYR B C     1 
ATOM   6246  O  O     . TYR B 1 85  ? 149.655 147.852 174.877 1.00 46.49 ?  85  TYR B O     1 
ATOM   6247  C  CB    . TYR B 1 85  ? 151.063 148.621 172.318 1.00 40.26 ?  85  TYR B CB    1 
ATOM   6248  C  CG    . TYR B 1 85  ? 151.394 147.864 171.053 1.00 41.59 ?  85  TYR B CG    1 
ATOM   6249  C  CD1   . TYR B 1 85  ? 151.622 146.496 171.083 1.00 43.79 ?  85  TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B 1 85  ? 151.472 148.515 169.829 1.00 43.92 ?  85  TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B 1 85  ? 151.924 145.797 169.933 1.00 44.17 ?  85  TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B 1 85  ? 151.773 147.823 168.674 1.00 43.73 ?  85  TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B 1 85  ? 151.998 146.465 168.731 1.00 43.21 ?  85  TYR B CZ    1 
ATOM   6254  O  OH    . TYR B 1 85  ? 152.297 145.771 167.584 1.00 45.29 ?  85  TYR B OH    1 
ATOM   6255  N  N     . ALA B 1 86  ? 148.891 149.954 174.616 1.00 43.66 ?  86  ALA B N     1 
ATOM   6256  C  CA    . ALA B 1 86  ? 148.691 150.135 176.049 1.00 42.01 ?  86  ALA B CA    1 
ATOM   6257  C  C     . ALA B 1 86  ? 147.528 149.304 176.570 1.00 45.48 ?  86  ALA B C     1 
ATOM   6258  O  O     . ALA B 1 86  ? 147.490 148.973 177.760 1.00 47.31 ?  86  ALA B O     1 
ATOM   6259  C  CB    . ALA B 1 86  ? 148.467 151.613 176.365 1.00 42.20 ?  86  ALA B CB    1 
ATOM   6260  N  N     . LYS B 1 87  ? 146.572 148.962 175.704 1.00 44.46 ?  87  LYS B N     1 
ATOM   6261  C  CA    . LYS B 1 87  ? 145.436 148.159 176.135 1.00 45.39 ?  87  LYS B CA    1 
ATOM   6262  C  C     . LYS B 1 87  ? 145.832 146.728 176.474 1.00 44.55 ?  87  LYS B C     1 
ATOM   6263  O  O     . LYS B 1 87  ? 145.088 146.053 177.194 1.00 46.37 ?  87  LYS B O     1 
ATOM   6264  C  CB    . LYS B 1 87  ? 144.355 148.155 175.054 1.00 43.93 ?  87  LYS B CB    1 
ATOM   6265  C  CG    . LYS B 1 87  ? 142.938 148.065 175.594 1.00 43.92 ?  87  LYS B CG    1 
ATOM   6266  C  CD    . LYS B 1 87  ? 142.216 146.845 175.049 1.00 44.50 ?  87  LYS B CD    1 
ATOM   6267  C  CE    . LYS B 1 87  ? 140.981 146.523 175.876 1.00 42.38 ?  87  LYS B CE    1 
ATOM   6268  N  NZ    . LYS B 1 87  ? 140.161 145.445 175.259 1.00 40.62 1  87  LYS B NZ    1 
ATOM   6269  N  N     . LYS B 1 88  ? 146.983 146.263 175.987 1.00 44.68 ?  88  LYS B N     1 
ATOM   6270  C  CA    . LYS B 1 88  ? 147.425 144.882 176.173 1.00 44.57 ?  88  LYS B CA    1 
ATOM   6271  C  C     . LYS B 1 88  ? 146.342 143.903 175.728 1.00 42.41 ?  88  LYS B C     1 
ATOM   6272  O  O     . LYS B 1 88  ? 145.975 142.970 176.445 1.00 43.90 ?  88  LYS B O     1 
ATOM   6273  C  CB    . LYS B 1 88  ? 147.839 144.621 177.623 1.00 45.79 ?  88  LYS B CB    1 
ATOM   6274  C  CG    . LYS B 1 88  ? 149.281 144.981 177.944 1.00 46.36 ?  88  LYS B CG    1 
ATOM   6275  C  CD    . LYS B 1 88  ? 149.424 146.442 178.330 1.00 45.95 ?  88  LYS B CD    1 
ATOM   6276  C  CE    . LYS B 1 88  ? 150.810 146.968 177.989 1.00 46.97 ?  88  LYS B CE    1 
ATOM   6277  N  NZ    . LYS B 1 88  ? 150.857 148.456 177.970 1.00 47.47 1  88  LYS B NZ    1 
ATOM   6278  N  N     . PHE B 1 89  ? 145.817 144.136 174.527 1.00 42.94 ?  89  PHE B N     1 
ATOM   6279  C  CA    . PHE B 1 89  ? 144.723 143.319 174.019 1.00 39.07 ?  89  PHE B CA    1 
ATOM   6280  C  C     . PHE B 1 89  ? 145.164 141.871 173.861 1.00 43.73 ?  89  PHE B C     1 
ATOM   6281  O  O     . PHE B 1 89  ? 146.229 141.587 173.305 1.00 46.25 ?  89  PHE B O     1 
ATOM   6282  C  CB    . PHE B 1 89  ? 144.223 143.866 172.681 1.00 37.31 ?  89  PHE B CB    1 
ATOM   6283  C  CG    . PHE B 1 89  ? 143.186 142.998 172.026 1.00 38.71 ?  89  PHE B CG    1 
ATOM   6284  C  CD1   . PHE B 1 89  ? 141.850 143.124 172.359 1.00 37.31 ?  89  PHE B CD1   1 
ATOM   6285  C  CD2   . PHE B 1 89  ? 143.549 142.050 171.083 1.00 38.40 ?  89  PHE B CD2   1 
ATOM   6286  C  CE1   . PHE B 1 89  ? 140.896 142.325 171.764 1.00 37.73 ?  89  PHE B CE1   1 
ATOM   6287  C  CE2   . PHE B 1 89  ? 142.598 141.247 170.486 1.00 34.60 ?  89  PHE B CE2   1 
ATOM   6288  C  CZ    . PHE B 1 89  ? 141.270 141.387 170.826 1.00 36.67 ?  89  PHE B CZ    1 
ATOM   6289  N  N     . ARG B 1 90  ? 144.333 140.956 174.347 1.00 42.62 ?  90  ARG B N     1 
ATOM   6290  C  CA    . ARG B 1 90  ? 144.572 139.526 174.233 1.00 40.51 ?  90  ARG B CA    1 
ATOM   6291  C  C     . ARG B 1 90  ? 143.384 138.881 173.540 1.00 41.89 ?  90  ARG B C     1 
ATOM   6292  O  O     . ARG B 1 90  ? 142.231 139.166 173.881 1.00 42.84 ?  90  ARG B O     1 
ATOM   6293  C  CB    . ARG B 1 90  ? 144.793 138.893 175.610 1.00 45.34 ?  90  ARG B CB    1 
ATOM   6294  C  CG    . ARG B 1 90  ? 145.986 139.447 176.365 1.00 42.68 ?  90  ARG B CG    1 
ATOM   6295  C  CD    . ARG B 1 90  ? 147.293 139.047 175.704 1.00 45.15 ?  90  ARG B CD    1 
ATOM   6296  N  NE    . ARG B 1 90  ? 148.428 139.776 176.256 1.00 45.79 ?  90  ARG B NE    1 
ATOM   6297  C  CZ    . ARG B 1 90  ? 149.032 140.788 175.650 1.00 44.67 ?  90  ARG B CZ    1 
ATOM   6298  N  NH1   . ARG B 1 90  ? 148.642 141.215 174.461 1.00 46.68 1  90  ARG B NH1   1 
ATOM   6299  N  NH2   . ARG B 1 90  ? 150.056 141.386 176.253 1.00 44.05 ?  90  ARG B NH2   1 
ATOM   6300  N  N     . PHE B 1 91  ? 143.663 138.024 172.571 1.00 39.25 ?  91  PHE B N     1 
ATOM   6301  C  CA    . PHE B 1 91  ? 142.605 137.275 171.912 1.00 38.08 ?  91  PHE B CA    1 
ATOM   6302  C  C     . PHE B 1 91  ? 142.087 136.208 172.866 1.00 43.46 ?  91  PHE B C     1 
ATOM   6303  O  O     . PHE B 1 91  ? 142.866 135.351 173.303 1.00 45.50 ?  91  PHE B O     1 
ATOM   6304  C  CB    . PHE B 1 91  ? 143.122 136.642 170.626 1.00 38.01 ?  91  PHE B CB    1 
ATOM   6305  C  CG    . PHE B 1 91  ? 143.287 137.616 169.494 1.00 39.78 ?  91  PHE B CG    1 
ATOM   6306  C  CD1   . PHE B 1 91  ? 142.191 138.054 168.772 1.00 40.90 ?  91  PHE B CD1   1 
ATOM   6307  C  CD2   . PHE B 1 91  ? 144.541 138.095 169.154 1.00 39.02 ?  91  PHE B CD2   1 
ATOM   6308  C  CE1   . PHE B 1 91  ? 142.342 138.948 167.731 1.00 39.44 ?  91  PHE B CE1   1 
ATOM   6309  C  CE2   . PHE B 1 91  ? 144.697 138.988 168.114 1.00 39.13 ?  91  PHE B CE2   1 
ATOM   6310  C  CZ    . PHE B 1 91  ? 143.595 139.416 167.403 1.00 39.68 ?  91  PHE B CZ    1 
ATOM   6311  N  N     . PRO B 1 92  ? 140.797 136.213 173.218 1.00 42.41 ?  92  PRO B N     1 
ATOM   6312  C  CA    . PRO B 1 92  ? 140.305 135.236 174.199 1.00 42.17 ?  92  PRO B CA    1 
ATOM   6313  C  C     . PRO B 1 92  ? 140.141 133.836 173.640 1.00 42.72 ?  92  PRO B C     1 
ATOM   6314  O  O     . PRO B 1 92  ? 140.030 132.886 174.427 1.00 43.37 ?  92  PRO B O     1 
ATOM   6315  C  CB    . PRO B 1 92  ? 138.953 135.822 174.622 1.00 41.94 ?  92  PRO B CB    1 
ATOM   6316  C  CG    . PRO B 1 92  ? 138.489 136.557 173.414 1.00 41.93 ?  92  PRO B CG    1 
ATOM   6317  C  CD    . PRO B 1 92  ? 139.724 137.098 172.732 1.00 40.90 ?  92  PRO B CD    1 
ATOM   6318  N  N     . SER B 1 93  ? 140.125 133.677 172.320 1.00 42.05 ?  93  SER B N     1 
ATOM   6319  C  CA    . SER B 1 93  ? 139.967 132.378 171.689 1.00 39.78 ?  93  SER B CA    1 
ATOM   6320  C  C     . SER B 1 93  ? 141.044 132.200 170.630 1.00 40.03 ?  93  SER B C     1 
ATOM   6321  O  O     . SER B 1 93  ? 141.536 133.173 170.053 1.00 44.07 ?  93  SER B O     1 
ATOM   6322  C  CB    . SER B 1 93  ? 138.577 132.225 171.057 1.00 42.98 ?  93  SER B CB    1 
ATOM   6323  O  OG    . SER B 1 93  ? 138.544 132.781 169.754 1.00 44.75 ?  93  SER B OG    1 
ATOM   6324  N  N     . PHE B 1 94  ? 141.414 130.941 170.391 1.00 40.58 ?  94  PHE B N     1 
ATOM   6325  C  CA    . PHE B 1 94  ? 142.431 130.651 169.386 1.00 41.09 ?  94  PHE B CA    1 
ATOM   6326  C  C     . PHE B 1 94  ? 141.966 131.064 167.997 1.00 41.10 ?  94  PHE B C     1 
ATOM   6327  O  O     . PHE B 1 94  ? 142.754 131.586 167.200 1.00 43.52 ?  94  PHE B O     1 
ATOM   6328  C  CB    . PHE B 1 94  ? 142.788 129.164 169.410 1.00 42.58 ?  94  PHE B CB    1 
ATOM   6329  C  CG    . PHE B 1 94  ? 143.347 128.657 168.111 1.00 39.39 ?  94  PHE B CG    1 
ATOM   6330  C  CD1   . PHE B 1 94  ? 144.612 129.032 167.692 1.00 41.36 ?  94  PHE B CD1   1 
ATOM   6331  C  CD2   . PHE B 1 94  ? 142.604 127.811 167.304 1.00 41.92 ?  94  PHE B CD2   1 
ATOM   6332  C  CE1   . PHE B 1 94  ? 145.125 128.573 166.496 1.00 41.54 ?  94  PHE B CE1   1 
ATOM   6333  C  CE2   . PHE B 1 94  ? 143.113 127.348 166.108 1.00 44.46 ?  94  PHE B CE2   1 
ATOM   6334  C  CZ    . PHE B 1 94  ? 144.377 127.730 165.703 1.00 41.24 ?  94  PHE B CZ    1 
ATOM   6335  N  N     . MET B 1 95  ? 140.688 130.835 167.688 1.00 38.90 ?  95  MET B N     1 
ATOM   6336  C  CA    . MET B 1 95  ? 140.195 131.102 166.342 1.00 36.29 ?  95  MET B CA    1 
ATOM   6337  C  C     . MET B 1 95  ? 140.198 132.590 166.016 1.00 38.72 ?  95  MET B C     1 
ATOM   6338  O  O     . MET B 1 95  ? 140.395 132.957 164.857 1.00 44.00 ?  95  MET B O     1 
ATOM   6339  C  CB    . MET B 1 95  ? 138.794 130.517 166.169 1.00 39.90 ?  95  MET B CB    1 
ATOM   6340  C  CG    . MET B 1 95  ? 138.203 130.697 164.776 1.00 42.25 ?  95  MET B CG    1 
ATOM   6341  S  SD    . MET B 1 95  ? 138.741 129.501 163.532 1.00 51.03 ?  95  MET B SD    1 
ATOM   6342  C  CE    . MET B 1 95  ? 139.473 128.211 164.537 1.00 43.73 ?  95  MET B CE    1 
ATOM   6343  N  N     . SER B 1 96  ? 139.995 133.457 167.010 1.00 33.31 ?  96  SER B N     1 
ATOM   6344  C  CA    . SER B 1 96  ? 140.052 134.894 166.752 1.00 30.40 ?  96  SER B CA    1 
ATOM   6345  C  C     . SER B 1 96  ? 141.425 135.302 166.230 1.00 32.32 ?  96  SER B C     1 
ATOM   6346  O  O     . SER B 1 96  ? 141.545 135.933 165.170 1.00 34.21 ?  96  SER B O     1 
ATOM   6347  C  CB    . SER B 1 96  ? 139.714 135.660 168.030 1.00 33.47 ?  96  SER B CB    1 
ATOM   6348  O  OG    . SER B 1 96  ? 138.495 135.206 168.589 1.00 38.67 ?  96  SER B OG    1 
ATOM   6349  N  N     . ALA B 1 97  ? 142.476 134.927 166.961 1.00 37.86 ?  97  ALA B N     1 
ATOM   6350  C  CA    . ALA B 1 97  ? 143.834 135.250 166.542 1.00 34.01 ?  97  ALA B CA    1 
ATOM   6351  C  C     . ALA B 1 97  ? 144.188 134.554 165.237 1.00 35.07 ?  97  ALA B C     1 
ATOM   6352  O  O     . ALA B 1 97  ? 144.845 135.143 164.371 1.00 42.03 ?  97  ALA B O     1 
ATOM   6353  C  CB    . ALA B 1 97  ? 144.823 134.867 167.640 1.00 36.35 ?  97  ALA B CB    1 
ATOM   6354  N  N     . PHE B 1 98  ? 143.772 133.296 165.082 1.00 33.42 ?  98  PHE B N     1 
ATOM   6355  C  CA    . PHE B 1 98  ? 144.069 132.566 163.855 1.00 32.89 ?  98  PHE B CA    1 
ATOM   6356  C  C     . PHE B 1 98  ? 143.444 133.255 162.649 1.00 35.95 ?  98  PHE B C     1 
ATOM   6357  O  O     . PHE B 1 98  ? 144.099 133.444 161.619 1.00 43.40 ?  98  PHE B O     1 
ATOM   6358  C  CB    . PHE B 1 98  ? 143.573 131.125 163.973 1.00 37.17 ?  98  PHE B CB    1 
ATOM   6359  C  CG    . PHE B 1 98  ? 143.724 130.327 162.711 1.00 39.18 ?  98  PHE B CG    1 
ATOM   6360  C  CD1   . PHE B 1 98  ? 144.934 129.732 162.396 1.00 39.78 ?  98  PHE B CD1   1 
ATOM   6361  C  CD2   . PHE B 1 98  ? 142.660 130.172 161.840 1.00 41.11 ?  98  PHE B CD2   1 
ATOM   6362  C  CE1   . PHE B 1 98  ? 145.078 128.998 161.238 1.00 37.68 ?  98  PHE B CE1   1 
ATOM   6363  C  CE2   . PHE B 1 98  ? 142.799 129.439 160.677 1.00 43.04 ?  98  PHE B CE2   1 
ATOM   6364  C  CZ    . PHE B 1 98  ? 144.010 128.851 160.377 1.00 40.72 ?  98  PHE B CZ    1 
ATOM   6365  N  N     . LYS B 1 99  ? 142.177 133.652 162.768 1.00 39.14 ?  99  LYS B N     1 
ATOM   6366  C  CA    . LYS B 1 99  ? 141.492 134.312 161.667 1.00 37.77 ?  99  LYS B CA    1 
ATOM   6367  C  C     . LYS B 1 99  ? 142.124 135.658 161.353 1.00 35.59 ?  99  LYS B C     1 
ATOM   6368  O  O     . LYS B 1 99  ? 142.288 136.008 160.179 1.00 41.58 ?  99  LYS B O     1 
ATOM   6369  C  CB    . LYS B 1 99  ? 140.008 134.475 161.992 1.00 36.70 ?  99  LYS B CB    1 
ATOM   6370  C  CG    . LYS B 1 99  ? 139.181 133.228 161.737 1.00 39.01 ?  99  LYS B CG    1 
ATOM   6371  C  CD    . LYS B 1 99  ? 139.489 132.628 160.378 1.00 42.01 ?  99  LYS B CD    1 
ATOM   6372  C  CE    . LYS B 1 99  ? 138.268 131.947 159.786 1.00 40.21 ?  99  LYS B CE    1 
ATOM   6373  N  NZ    . LYS B 1 99  ? 138.162 132.185 158.321 1.00 42.41 1  99  LYS B NZ    1 
ATOM   6374  N  N     . PHE B 1 100 ? 142.493 136.427 162.381 1.00 32.10 ?  100 PHE B N     1 
ATOM   6375  C  CA    . PHE B 1 100 ? 143.144 137.704 162.110 1.00 35.03 ?  100 PHE B CA    1 
ATOM   6376  C  C     . PHE B 1 100 ? 144.477 137.507 161.398 1.00 35.92 ?  100 PHE B C     1 
ATOM   6377  O  O     . PHE B 1 100 ? 144.751 138.153 160.380 1.00 41.09 ?  100 PHE B O     1 
ATOM   6378  C  CB    . PHE B 1 100 ? 143.363 138.503 163.389 1.00 33.33 ?  100 PHE B CB    1 
ATOM   6379  C  CG    . PHE B 1 100 ? 144.197 139.727 163.168 1.00 35.46 ?  100 PHE B CG    1 
ATOM   6380  C  CD1   . PHE B 1 100 ? 143.690 140.801 162.458 1.00 34.60 ?  100 PHE B CD1   1 
ATOM   6381  C  CD2   . PHE B 1 100 ? 145.507 139.779 163.608 1.00 34.53 ?  100 PHE B CD2   1 
ATOM   6382  C  CE1   . PHE B 1 100 ? 144.460 141.921 162.226 1.00 34.60 ?  100 PHE B CE1   1 
ATOM   6383  C  CE2   . PHE B 1 100 ? 146.281 140.893 163.375 1.00 35.28 ?  100 PHE B CE2   1 
ATOM   6384  C  CZ    . PHE B 1 100 ? 145.757 141.967 162.683 1.00 34.72 ?  100 PHE B CZ    1 
ATOM   6385  N  N     . TYR B 1 101 ? 145.320 136.617 161.918 1.00 36.51 ?  101 TYR B N     1 
ATOM   6386  C  CA    . TYR B 1 101 ? 146.666 136.467 161.383 1.00 35.32 ?  101 TYR B CA    1 
ATOM   6387  C  C     . TYR B 1 101 ? 146.709 135.650 160.100 1.00 37.20 ?  101 TYR B C     1 
ATOM   6388  O  O     . TYR B 1 101 ? 147.764 135.593 159.460 1.00 45.47 ?  101 TYR B O     1 
ATOM   6389  C  CB    . TYR B 1 101 ? 147.583 135.849 162.440 1.00 38.28 ?  101 TYR B CB    1 
ATOM   6390  C  CG    . TYR B 1 101 ? 147.948 136.822 163.538 1.00 37.54 ?  101 TYR B CG    1 
ATOM   6391  C  CD1   . TYR B 1 101 ? 148.811 137.881 163.293 1.00 36.80 ?  101 TYR B CD1   1 
ATOM   6392  C  CD2   . TYR B 1 101 ? 147.415 136.696 164.813 1.00 36.97 ?  101 TYR B CD2   1 
ATOM   6393  C  CE1   . TYR B 1 101 ? 149.140 138.779 164.288 1.00 36.63 ?  101 TYR B CE1   1 
ATOM   6394  C  CE2   . TYR B 1 101 ? 147.738 137.589 165.814 1.00 38.05 ?  101 TYR B CE2   1 
ATOM   6395  C  CZ    . TYR B 1 101 ? 148.601 138.629 165.546 1.00 39.59 ?  101 TYR B CZ    1 
ATOM   6396  O  OH    . TYR B 1 101 ? 148.925 139.520 166.542 1.00 42.17 ?  101 TYR B OH    1 
ATOM   6397  N  N     . ASN B 1 102 ? 145.601 135.026 159.706 1.00 40.40 ?  102 ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 102 ? 145.534 134.336 158.428 1.00 41.86 ?  102 ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 102 ? 144.807 135.128 157.352 1.00 43.32 ?  102 ASN B C     1 
ATOM   6400  O  O     . ASN B 1 102 ? 145.123 134.972 156.168 1.00 47.54 ?  102 ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 102 ? 144.849 132.977 158.597 1.00 40.01 ?  102 ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 102 ? 145.765 131.934 159.202 1.00 43.14 ?  102 ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 102 ? 146.367 132.153 160.253 1.00 45.88 ?  102 ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 102 ? 145.877 130.789 158.539 1.00 43.81 ?  102 ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 103 ? 143.847 135.975 157.727 1.00 38.59 ?  103 ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 103 ? 143.045 136.704 156.754 1.00 40.61 ?  103 ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 103 ? 143.294 138.204 156.736 1.00 40.98 ?  103 ASP B C     1 
ATOM   6408  O  O     . ASP B 1 103 ? 143.085 138.831 155.696 1.00 46.47 ?  103 ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 103 ? 141.549 136.469 157.009 1.00 42.23 ?  103 ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 103 ? 141.208 135.004 157.202 1.00 45.37 ?  103 ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 103 ? 142.024 134.139 156.820 1.00 44.78 ?  103 ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 103 ? 140.116 134.718 157.736 1.00 47.06 -1 103 ASP B OD2   1 
ATOM   6413  N  N     . TYR B 1 104 ? 143.729 138.800 157.847 1.00 31.95 ?  104 TYR B N     1 
ATOM   6414  C  CA    . TYR B 1 104 ? 143.798 140.253 157.942 1.00 35.66 ?  104 TYR B CA    1 
ATOM   6415  C  C     . TYR B 1 104 ? 145.161 140.810 158.323 1.00 38.78 ?  104 TYR B C     1 
ATOM   6416  O  O     . TYR B 1 104 ? 145.442 141.963 157.975 1.00 43.88 ?  104 TYR B O     1 
ATOM   6417  C  CB    . TYR B 1 104 ? 142.754 140.774 158.943 1.00 37.44 ?  104 TYR B CB    1 
ATOM   6418  C  CG    . TYR B 1 104 ? 141.356 140.284 158.646 1.00 36.15 ?  104 TYR B CG    1 
ATOM   6419  C  CD1   . TYR B 1 104 ? 140.527 140.980 157.776 1.00 34.65 ?  104 TYR B CD1   1 
ATOM   6420  C  CD2   . TYR B 1 104 ? 140.864 139.127 159.236 1.00 33.99 ?  104 TYR B CD2   1 
ATOM   6421  C  CE1   . TYR B 1 104 ? 139.252 140.533 157.495 1.00 36.14 ?  104 TYR B CE1   1 
ATOM   6422  C  CE2   . TYR B 1 104 ? 139.588 138.674 158.962 1.00 37.33 ?  104 TYR B CE2   1 
ATOM   6423  C  CZ    . TYR B 1 104 ? 138.787 139.380 158.091 1.00 38.90 ?  104 TYR B CZ    1 
ATOM   6424  O  OH    . TYR B 1 104 ? 137.515 138.933 157.819 1.00 38.34 ?  104 TYR B OH    1 
ATOM   6425  N  N     . ALA B 1 105 ? 146.007 140.057 159.020 1.00 40.73 ?  105 ALA B N     1 
ATOM   6426  C  CA    . ALA B 1 105 ? 147.335 140.555 159.347 1.00 40.00 ?  105 ALA B CA    1 
ATOM   6427  C  C     . ALA B 1 105 ? 148.192 140.645 158.091 1.00 43.61 ?  105 ALA B C     1 
ATOM   6428  O  O     . ALA B 1 105 ? 148.175 139.750 157.242 1.00 40.70 ?  105 ALA B O     1 
ATOM   6429  C  CB    . ALA B 1 105 ? 148.009 139.655 160.378 1.00 37.04 ?  105 ALA B CB    1 
ATOM   6430  N  N     . LEU B 1 106 ? 148.940 141.738 157.975 1.00 46.91 ?  106 LEU B N     1 
ATOM   6431  C  CA    . LEU B 1 106 ? 149.792 141.937 156.811 1.00 44.23 ?  106 LEU B CA    1 
ATOM   6432  C  C     . LEU B 1 106 ? 151.003 141.015 156.881 1.00 47.83 ?  106 LEU B C     1 
ATOM   6433  O  O     . LEU B 1 106 ? 151.694 140.952 157.901 1.00 46.99 ?  106 LEU B O     1 
ATOM   6434  C  CB    . LEU B 1 106 ? 150.240 143.394 156.722 1.00 46.87 ?  106 LEU B CB    1 
ATOM   6435  C  CG    . LEU B 1 106 ? 151.209 143.742 155.592 1.00 45.27 ?  106 LEU B CG    1 
ATOM   6436  C  CD1   . LEU B 1 106 ? 150.506 143.682 154.246 1.00 45.59 ?  106 LEU B CD1   1 
ATOM   6437  C  CD2   . LEU B 1 106 ? 151.822 145.114 155.818 1.00 46.37 ?  106 LEU B CD2   1 
ATOM   6438  N  N     . LYS B 1 107 ? 151.254 140.299 155.790 1.00 53.13 ?  107 LYS B N     1 
ATOM   6439  C  CA    . LYS B 1 107 ? 152.391 139.403 155.669 1.00 52.70 ?  107 LYS B CA    1 
ATOM   6440  C  C     . LYS B 1 107 ? 153.333 139.918 154.589 1.00 55.30 ?  107 LYS B C     1 
ATOM   6441  O  O     . LYS B 1 107 ? 153.030 140.871 153.867 1.00 56.79 ?  107 LYS B O     1 
ATOM   6442  C  CB    . LYS B 1 107 ? 151.938 137.973 155.346 1.00 52.84 ?  107 LYS B CB    1 
ATOM   6443  C  CG    . LYS B 1 107 ? 151.185 137.286 156.472 1.00 51.33 ?  107 LYS B CG    1 
ATOM   6444  C  CD    . LYS B 1 107 ? 150.697 135.912 156.042 1.00 54.71 ?  107 LYS B CD    1 
ATOM   6445  C  CE    . LYS B 1 107 ? 149.976 135.202 157.173 1.00 55.56 ?  107 LYS B CE    1 
ATOM   6446  N  NZ    . LYS B 1 107 ? 149.270 133.977 156.701 1.00 52.71 1  107 LYS B NZ    1 
ATOM   6447  N  N     . THR B 1 108 ? 154.489 139.269 154.485 1.00 59.23 ?  108 THR B N     1 
ATOM   6448  C  CA    . THR B 1 108 ? 155.477 139.647 153.488 1.00 59.39 ?  108 THR B CA    1 
ATOM   6449  C  C     . THR B 1 108 ? 154.995 139.250 152.093 1.00 61.88 ?  108 THR B C     1 
ATOM   6450  O  O     . THR B 1 108 ? 153.924 138.663 151.914 1.00 61.58 ?  108 THR B O     1 
ATOM   6451  C  CB    . THR B 1 108 ? 156.824 139.000 153.805 1.00 60.99 ?  108 THR B CB    1 
ATOM   6452  O  OG1   . THR B 1 108 ? 156.621 137.641 154.210 1.00 65.24 ?  108 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 1 108 ? 157.522 139.755 154.926 1.00 58.11 ?  108 THR B CG2   1 
ATOM   6454  N  N     . ASN B 1 109 ? 155.803 139.587 151.084 1.00 63.97 ?  109 ASN B N     1 
ATOM   6455  C  CA    . ASN B 1 109 ? 155.447 139.255 149.708 1.00 61.95 ?  109 ASN B CA    1 
ATOM   6456  C  C     . ASN B 1 109 ? 155.347 137.747 149.510 1.00 64.82 ?  109 ASN B C     1 
ATOM   6457  O  O     . ASN B 1 109 ? 154.439 137.261 148.826 1.00 64.81 ?  109 ASN B O     1 
ATOM   6458  C  CB    . ASN B 1 109 ? 156.469 139.854 148.742 1.00 63.18 ?  109 ASN B CB    1 
ATOM   6459  C  CG    . ASN B 1 109 ? 156.555 141.362 148.849 1.00 63.25 ?  109 ASN B CG    1 
ATOM   6460  O  OD1   . ASN B 1 109 ? 155.731 141.997 149.505 1.00 61.63 ?  109 ASN B OD1   1 
ATOM   6461  N  ND2   . ASN B 1 109 ? 157.556 141.946 148.202 1.00 64.76 ?  109 ASN B ND2   1 
ATOM   6462  N  N     . ASP B 1 110 ? 156.270 136.992 150.102 1.00 66.37 ?  110 ASP B N     1 
ATOM   6463  C  CA    . ASP B 1 110 ? 156.238 135.537 150.030 1.00 66.12 ?  110 ASP B CA    1 
ATOM   6464  C  C     . ASP B 1 110 ? 155.347 134.911 151.095 1.00 66.70 ?  110 ASP B C     1 
ATOM   6465  O  O     . ASP B 1 110 ? 155.225 133.682 151.129 1.00 67.58 ?  110 ASP B O     1 
ATOM   6466  C  CB    . ASP B 1 110 ? 157.659 134.976 150.142 1.00 66.14 ?  110 ASP B CB    1 
ATOM   6467  C  CG    . ASP B 1 110 ? 158.398 135.501 151.355 1.00 67.51 ?  110 ASP B CG    1 
ATOM   6468  O  OD1   . ASP B 1 110 ? 157.898 136.447 151.997 1.00 67.34 ?  110 ASP B OD1   1 
ATOM   6469  O  OD2   . ASP B 1 110 ? 159.487 134.973 151.661 1.00 67.65 -1 110 ASP B OD2   1 
ATOM   6470  N  N     . LYS B 1 111 ? 154.729 135.726 151.954 1.00 62.24 ?  111 LYS B N     1 
ATOM   6471  C  CA    . LYS B 1 111 ? 153.812 135.251 152.993 1.00 63.06 ?  111 LYS B CA    1 
ATOM   6472  C  C     . LYS B 1 111 ? 154.481 134.232 153.913 1.00 64.05 ?  111 LYS B C     1 
ATOM   6473  O  O     . LYS B 1 111 ? 153.876 133.233 154.307 1.00 65.21 ?  111 LYS B O     1 
ATOM   6474  C  CB    . LYS B 1 111 ? 152.531 134.675 152.384 1.00 63.14 ?  111 LYS B CB    1 
ATOM   6475  C  CG    . LYS B 1 111 ? 151.981 135.470 151.209 1.00 63.13 ?  111 LYS B CG    1 
ATOM   6476  C  CD    . LYS B 1 111 ? 151.061 136.586 151.675 1.00 64.53 ?  111 LYS B CD    1 
ATOM   6477  C  CE    . LYS B 1 111 ? 151.023 137.726 150.673 1.00 64.19 ?  111 LYS B CE    1 
ATOM   6478  N  NZ    . LYS B 1 111 ? 151.098 137.234 149.270 1.00 63.59 1  111 LYS B NZ    1 
ATOM   6479  N  N     . LYS B 1 112 ? 155.743 134.485 154.259 1.00 64.60 ?  112 LYS B N     1 
ATOM   6480  C  CA    . LYS B 1 112 ? 156.468 133.626 155.185 1.00 64.95 ?  112 LYS B CA    1 
ATOM   6481  C  C     . LYS B 1 112 ? 156.556 134.201 156.590 1.00 64.12 ?  112 LYS B C     1 
ATOM   6482  O  O     . LYS B 1 112 ? 156.857 133.454 157.529 1.00 64.02 ?  112 LYS B O     1 
ATOM   6483  C  CB    . LYS B 1 112 ? 157.887 133.359 154.669 1.00 64.38 ?  112 LYS B CB    1 
ATOM   6484  C  CG    . LYS B 1 112 ? 158.866 134.491 154.936 1.00 65.17 ?  112 LYS B CG    1 
ATOM   6485  C  CD    . LYS B 1 112 ? 160.293 134.080 154.615 1.00 66.05 ?  112 LYS B CD    1 
ATOM   6486  C  CE    . LYS B 1 112 ? 161.255 135.240 154.812 1.00 64.52 ?  112 LYS B CE    1 
ATOM   6487  N  NZ    . LYS B 1 112 ? 160.646 136.539 154.413 1.00 64.63 1  112 LYS B NZ    1 
ATOM   6488  N  N     . LYS B 1 113 ? 156.302 135.496 156.759 1.00 59.57 ?  113 LYS B N     1 
ATOM   6489  C  CA    . LYS B 1 113 ? 156.424 136.149 158.053 1.00 59.62 ?  113 LYS B CA    1 
ATOM   6490  C  C     . LYS B 1 113 ? 155.262 137.112 158.239 1.00 57.88 ?  113 LYS B C     1 
ATOM   6491  O  O     . LYS B 1 113 ? 154.579 137.488 157.283 1.00 60.09 ?  113 LYS B O     1 
ATOM   6492  C  CB    . LYS B 1 113 ? 157.760 136.893 158.184 1.00 60.10 ?  113 LYS B CB    1 
ATOM   6493  C  CG    . LYS B 1 113 ? 158.972 135.985 158.327 1.00 58.77 ?  113 LYS B CG    1 
ATOM   6494  C  CD    . LYS B 1 113 ? 158.928 135.203 159.627 1.00 60.69 ?  113 LYS B CD    1 
ATOM   6495  C  CE    . LYS B 1 113 ? 160.149 134.314 159.779 1.00 61.41 ?  113 LYS B CE    1 
ATOM   6496  N  NZ    . LYS B 1 113 ? 160.020 133.391 160.940 1.00 60.18 1  113 LYS B NZ    1 
ATOM   6497  N  N     . ILE B 1 114 ? 155.045 137.509 159.489 1.00 52.57 ?  114 ILE B N     1 
ATOM   6498  C  CA    . ILE B 1 114 ? 153.952 138.399 159.862 1.00 52.15 ?  114 ILE B CA    1 
ATOM   6499  C  C     . ILE B 1 114 ? 154.536 139.778 160.128 1.00 53.20 ?  114 ILE B C     1 
ATOM   6500  O  O     . ILE B 1 114 ? 155.386 139.942 161.012 1.00 54.37 ?  114 ILE B O     1 
ATOM   6501  C  CB    . ILE B 1 114 ? 153.190 137.877 161.091 1.00 53.28 ?  114 ILE B CB    1 
ATOM   6502  C  CG1   . ILE B 1 114 ? 152.351 136.654 160.717 1.00 49.72 ?  114 ILE B CG1   1 
ATOM   6503  C  CG2   . ILE B 1 114 ? 152.313 138.969 161.678 1.00 51.69 ?  114 ILE B CG2   1 
ATOM   6504  C  CD1   . ILE B 1 114 ? 151.866 135.868 161.909 1.00 50.40 ?  114 ILE B CD1   1 
ATOM   6505  N  N     . LEU B 1 115 ? 154.081 140.769 159.364 1.00 49.76 ?  115 LEU B N     1 
ATOM   6506  C  CA    . LEU B 1 115 ? 154.544 142.138 159.544 1.00 48.02 ?  115 LEU B CA    1 
ATOM   6507  C  C     . LEU B 1 115 ? 153.631 142.958 160.441 1.00 49.77 ?  115 LEU B C     1 
ATOM   6508  O  O     . LEU B 1 115 ? 154.095 143.914 161.074 1.00 50.66 ?  115 LEU B O     1 
ATOM   6509  C  CB    . LEU B 1 115 ? 154.678 142.836 158.188 1.00 48.78 ?  115 LEU B CB    1 
ATOM   6510  C  CG    . LEU B 1 115 ? 155.878 142.438 157.331 1.00 48.87 ?  115 LEU B CG    1 
ATOM   6511  C  CD1   . LEU B 1 115 ? 155.664 142.872 155.892 1.00 48.97 ?  115 LEU B CD1   1 
ATOM   6512  C  CD2   . LEU B 1 115 ? 157.156 143.040 157.893 1.00 49.55 ?  115 LEU B CD2   1 
ATOM   6513  N  N     . GLU B 1 116 ? 152.348 142.613 160.517 1.00 49.06 ?  116 GLU B N     1 
ATOM   6514  C  CA    . GLU B 1 116 ? 151.367 143.392 161.257 1.00 45.44 ?  116 GLU B CA    1 
ATOM   6515  C  C     . GLU B 1 116 ? 150.804 142.576 162.409 1.00 45.77 ?  116 GLU B C     1 
ATOM   6516  O  O     . GLU B 1 116 ? 150.319 141.458 162.206 1.00 48.91 ?  116 GLU B O     1 
ATOM   6517  C  CB    . GLU B 1 116 ? 150.224 143.846 160.347 1.00 44.67 ?  116 GLU B CB    1 
ATOM   6518  C  CG    . GLU B 1 116 ? 150.295 145.299 159.931 1.00 44.82 ?  116 GLU B CG    1 
ATOM   6519  C  CD    . GLU B 1 116 ? 149.101 145.720 159.102 1.00 45.82 ?  116 GLU B CD    1 
ATOM   6520  O  OE1   . GLU B 1 116 ? 148.245 144.859 158.810 1.00 44.53 ?  116 GLU B OE1   1 
ATOM   6521  O  OE2   . GLU B 1 116 ? 149.014 146.912 158.742 1.00 47.68 -1 116 GLU B OE2   1 
ATOM   6522  N  N     . ARG B 1 117 ? 150.862 143.141 163.611 1.00 40.37 ?  117 ARG B N     1 
ATOM   6523  C  CA    . ARG B 1 117 ? 150.120 142.605 164.738 1.00 41.84 ?  117 ARG B CA    1 
ATOM   6524  C  C     . ARG B 1 117 ? 148.698 143.162 164.712 1.00 42.11 ?  117 ARG B C     1 
ATOM   6525  O  O     . ARG B 1 117 ? 148.333 143.960 163.844 1.00 44.85 ?  117 ARG B O     1 
ATOM   6526  C  CB    . ARG B 1 117 ? 150.827 142.941 166.049 1.00 43.52 ?  117 ARG B CB    1 
ATOM   6527  C  CG    . ARG B 1 117 ? 152.148 142.217 166.248 1.00 43.24 ?  117 ARG B CG    1 
ATOM   6528  C  CD    . ARG B 1 117 ? 151.996 140.720 166.031 1.00 45.76 ?  117 ARG B CD    1 
ATOM   6529  N  NE    . ARG B 1 117 ? 152.828 139.945 166.945 1.00 45.69 ?  117 ARG B NE    1 
ATOM   6530  C  CZ    . ARG B 1 117 ? 152.538 139.724 168.220 1.00 45.62 ?  117 ARG B CZ    1 
ATOM   6531  N  NH1   . ARG B 1 117 ? 151.436 140.204 168.773 1.00 44.83 1  117 ARG B NH1   1 
ATOM   6532  N  NH2   . ARG B 1 117 ? 153.374 139.002 168.960 1.00 48.06 ?  117 ARG B NH2   1 
ATOM   6533  N  N     . TYR B 1 118 ? 147.873 142.732 165.669 1.00 39.73 ?  118 TYR B N     1 
ATOM   6534  C  CA    . TYR B 1 118 ? 146.532 143.297 165.774 1.00 36.21 ?  118 TYR B CA    1 
ATOM   6535  C  C     . TYR B 1 118 ? 146.594 144.780 166.107 1.00 37.83 ?  118 TYR B C     1 
ATOM   6536  O  O     . TYR B 1 118 ? 145.860 145.590 165.526 1.00 41.14 ?  118 TYR B O     1 
ATOM   6537  C  CB    . TYR B 1 118 ? 145.718 142.539 166.820 1.00 34.13 ?  118 TYR B CB    1 
ATOM   6538  C  CG    . TYR B 1 118 ? 144.242 142.861 166.789 1.00 35.58 ?  118 TYR B CG    1 
ATOM   6539  C  CD1   . TYR B 1 118 ? 143.514 142.759 165.612 1.00 34.33 ?  118 TYR B CD1   1 
ATOM   6540  C  CD2   . TYR B 1 118 ? 143.578 143.271 167.935 1.00 35.30 ?  118 TYR B CD2   1 
ATOM   6541  C  CE1   . TYR B 1 118 ? 142.167 143.052 165.579 1.00 34.36 ?  118 TYR B CE1   1 
ATOM   6542  C  CE2   . TYR B 1 118 ? 142.231 143.563 167.914 1.00 30.65 ?  118 TYR B CE2   1 
ATOM   6543  C  CZ    . TYR B 1 118 ? 141.530 143.454 166.733 1.00 36.75 ?  118 TYR B CZ    1 
ATOM   6544  O  OH    . TYR B 1 118 ? 140.187 143.749 166.706 1.00 40.55 ?  118 TYR B OH    1 
ATOM   6545  N  N     . GLU B 1 119 ? 147.480 145.155 167.030 1.00 39.86 ?  119 GLU B N     1 
ATOM   6546  C  CA    . GLU B 1 119 ? 147.636 146.560 167.380 1.00 39.18 ?  119 GLU B CA    1 
ATOM   6547  C  C     . GLU B 1 119 ? 148.185 147.365 166.208 1.00 38.98 ?  119 GLU B C     1 
ATOM   6548  O  O     . GLU B 1 119 ? 147.774 148.508 165.996 1.00 43.90 ?  119 GLU B O     1 
ATOM   6549  C  CB    . GLU B 1 119 ? 148.540 146.698 168.603 1.00 36.58 ?  119 GLU B CB    1 
ATOM   6550  C  CG    . GLU B 1 119 ? 147.864 146.338 169.914 1.00 36.87 ?  119 GLU B CG    1 
ATOM   6551  C  CD    . GLU B 1 119 ? 148.176 144.926 170.363 1.00 44.14 ?  119 GLU B CD    1 
ATOM   6552  O  OE1   . GLU B 1 119 ? 148.419 144.063 169.492 1.00 43.47 ?  119 GLU B OE1   1 
ATOM   6553  O  OE2   . GLU B 1 119 ? 148.176 144.677 171.587 1.00 45.63 -1 119 GLU B OE2   1 
ATOM   6554  N  N     . ASP B 1 120 ? 149.109 146.790 165.436 1.00 40.51 ?  120 ASP B N     1 
ATOM   6555  C  CA    . ASP B 1 120 ? 149.646 147.495 164.275 1.00 37.36 ?  120 ASP B CA    1 
ATOM   6556  C  C     . ASP B 1 120 ? 148.561 147.745 163.235 1.00 35.98 ?  120 ASP B C     1 
ATOM   6557  O  O     . ASP B 1 120 ? 148.443 148.852 162.694 1.00 39.04 ?  120 ASP B O     1 
ATOM   6558  C  CB    . ASP B 1 120 ? 150.797 146.697 163.660 1.00 41.42 ?  120 ASP B CB    1 
ATOM   6559  C  CG    . ASP B 1 120 ? 151.896 146.399 164.655 1.00 45.25 ?  120 ASP B CG    1 
ATOM   6560  O  OD1   . ASP B 1 120 ? 152.090 147.205 165.586 1.00 45.23 ?  120 ASP B OD1   1 
ATOM   6561  O  OD2   . ASP B 1 120 ? 152.566 145.357 164.506 1.00 48.28 -1 120 ASP B OD2   1 
ATOM   6562  N  N     . ARG B 1 121 ? 147.758 146.720 162.943 1.00 33.62 ?  121 ARG B N     1 
ATOM   6563  C  CA    . ARG B 1 121 ? 146.670 146.875 161.984 1.00 33.76 ?  121 ARG B CA    1 
ATOM   6564  C  C     . ARG B 1 121 ? 145.658 147.906 162.464 1.00 36.24 ?  121 ARG B C     1 
ATOM   6565  O  O     . ARG B 1 121 ? 145.207 148.755 161.686 1.00 37.10 ?  121 ARG B O     1 
ATOM   6566  C  CB    . ARG B 1 121 ? 145.997 145.523 161.745 1.00 32.18 ?  121 ARG B CB    1 
ATOM   6567  C  CG    . ARG B 1 121 ? 144.746 145.574 160.889 1.00 30.15 ?  121 ARG B CG    1 
ATOM   6568  C  CD    . ARG B 1 121 ? 145.079 145.518 159.412 1.00 30.70 ?  121 ARG B CD    1 
ATOM   6569  N  NE    . ARG B 1 121 ? 144.808 146.788 158.752 1.00 37.96 ?  121 ARG B NE    1 
ATOM   6570  C  CZ    . ARG B 1 121 ? 145.570 147.322 157.809 1.00 34.88 ?  121 ARG B CZ    1 
ATOM   6571  N  NH1   . ARG B 1 121 ? 146.664 146.717 157.379 1.00 37.95 1  121 ARG B NH1   1 
ATOM   6572  N  NH2   . ARG B 1 121 ? 145.225 148.492 157.283 1.00 31.85 ?  121 ARG B NH2   1 
ATOM   6573  N  N     . ILE B 1 122 ? 145.304 147.856 163.750 1.00 33.71 ?  122 ILE B N     1 
ATOM   6574  C  CA    . ILE B 1 122 ? 144.338 148.805 164.291 1.00 26.54 ?  122 ILE B CA    1 
ATOM   6575  C  C     . ILE B 1 122 ? 144.893 150.223 164.243 1.00 30.87 ?  122 ILE B C     1 
ATOM   6576  O  O     . ILE B 1 122 ? 144.174 151.170 163.912 1.00 37.19 ?  122 ILE B O     1 
ATOM   6577  C  CB    . ILE B 1 122 ? 143.931 148.391 165.716 1.00 33.72 ?  122 ILE B CB    1 
ATOM   6578  C  CG1   . ILE B 1 122 ? 142.894 147.269 165.650 1.00 29.67 ?  122 ILE B CG1   1 
ATOM   6579  C  CG2   . ILE B 1 122 ? 143.387 149.581 166.496 1.00 31.03 ?  122 ILE B CG2   1 
ATOM   6580  C  CD1   . ILE B 1 122 ? 142.297 146.920 166.978 1.00 29.81 ?  122 ILE B CD1   1 
ATOM   6581  N  N     . SER B 1 123 ? 146.178 150.394 164.563 1.00 35.20 ?  123 SER B N     1 
ATOM   6582  C  CA    . SER B 1 123 ? 146.791 151.717 164.505 1.00 30.91 ?  123 SER B CA    1 
ATOM   6583  C  C     . SER B 1 123 ? 146.803 152.258 163.084 1.00 30.80 ?  123 SER B C     1 
ATOM   6584  O  O     . SER B 1 123 ? 146.522 153.439 162.861 1.00 39.32 ?  123 SER B O     1 
ATOM   6585  C  CB    . SER B 1 123 ? 148.214 151.665 165.059 1.00 32.46 ?  123 SER B CB    1 
ATOM   6586  O  OG    . SER B 1 123 ? 148.255 151.001 166.305 1.00 36.41 ?  123 SER B OG    1 
ATOM   6587  N  N     . ILE B 1 124 ? 147.135 151.411 162.107 1.00 30.84 ?  124 ILE B N     1 
ATOM   6588  C  CA    . ILE B 1 124 ? 147.163 151.864 160.720 1.00 31.07 ?  124 ILE B CA    1 
ATOM   6589  C  C     . ILE B 1 124 ? 145.765 152.256 160.258 1.00 34.58 ?  124 ILE B C     1 
ATOM   6590  O  O     . ILE B 1 124 ? 145.577 153.293 159.607 1.00 36.70 ?  124 ILE B O     1 
ATOM   6591  C  CB    . ILE B 1 124 ? 147.785 150.782 159.819 1.00 37.99 ?  124 ILE B CB    1 
ATOM   6592  C  CG1   . ILE B 1 124 ? 149.291 150.695 160.074 1.00 37.08 ?  124 ILE B CG1   1 
ATOM   6593  C  CG2   . ILE B 1 124 ? 147.506 151.073 158.353 1.00 34.09 ?  124 ILE B CG2   1 
ATOM   6594  C  CD1   . ILE B 1 124 ? 149.986 152.039 160.091 1.00 34.28 ?  124 ILE B CD1   1 
ATOM   6595  N  N     . VAL B 1 125 ? 144.761 151.444 160.600 1.00 33.80 ?  125 VAL B N     1 
ATOM   6596  C  CA    . VAL B 1 125 ? 143.390 151.758 160.210 1.00 27.57 ?  125 VAL B CA    1 
ATOM   6597  C  C     . VAL B 1 125 ? 142.927 153.051 160.874 1.00 24.37 ?  125 VAL B C     1 
ATOM   6598  O  O     . VAL B 1 125 ? 142.258 153.882 160.248 1.00 35.89 ?  125 VAL B O     1 
ATOM   6599  C  CB    . VAL B 1 125 ? 142.456 150.578 160.540 1.00 31.00 ?  125 VAL B CB    1 
ATOM   6600  C  CG1   . VAL B 1 125 ? 141.011 150.958 160.304 1.00 31.11 ?  125 VAL B CG1   1 
ATOM   6601  C  CG2   . VAL B 1 125 ? 142.819 149.370 159.696 1.00 28.16 ?  125 VAL B CG2   1 
ATOM   6602  N  N     . ALA B 1 126 ? 143.283 153.249 162.146 1.00 23.02 ?  126 ALA B N     1 
ATOM   6603  C  CA    . ALA B 1 126 ? 142.899 154.467 162.852 1.00 25.33 ?  126 ALA B CA    1 
ATOM   6604  C  C     . ALA B 1 126 ? 143.571 155.697 162.256 1.00 30.57 ?  126 ALA B C     1 
ATOM   6605  O  O     . ALA B 1 126 ? 142.942 156.752 162.124 1.00 35.12 ?  126 ALA B O     1 
ATOM   6606  C  CB    . ALA B 1 126 ? 143.244 154.339 164.331 1.00 31.54 ?  126 ALA B CB    1 
ATOM   6607  N  N     . LEU B 1 127 ? 144.854 155.583 161.907 1.00 33.87 ?  127 LEU B N     1 
ATOM   6608  C  CA    . LEU B 1 127 ? 145.557 156.704 161.295 1.00 29.95 ?  127 LEU B CA    1 
ATOM   6609  C  C     . LEU B 1 127 ? 144.975 157.035 159.930 1.00 30.74 ?  127 LEU B C     1 
ATOM   6610  O  O     . LEU B 1 127 ? 144.892 158.210 159.553 1.00 36.71 ?  127 LEU B O     1 
ATOM   6611  C  CB    . LEU B 1 127 ? 147.048 156.392 161.187 1.00 33.31 ?  127 LEU B CB    1 
ATOM   6612  C  CG    . LEU B 1 127 ? 147.836 156.388 162.499 1.00 32.21 ?  127 LEU B CG    1 
ATOM   6613  C  CD1   . LEU B 1 127 ? 149.148 155.648 162.326 1.00 36.25 ?  127 LEU B CD1   1 
ATOM   6614  C  CD2   . LEU B 1 127 ? 148.076 157.804 162.991 1.00 33.87 ?  127 LEU B CD2   1 
ATOM   6615  N  N     . PHE B 1 128 ? 144.575 156.014 159.169 1.00 29.85 ?  128 PHE B N     1 
ATOM   6616  C  CA    . PHE B 1 128 ? 143.892 156.270 157.906 1.00 29.40 ?  128 PHE B CA    1 
ATOM   6617  C  C     . PHE B 1 128 ? 142.548 156.953 158.137 1.00 28.36 ?  128 PHE B C     1 
ATOM   6618  O  O     . PHE B 1 128 ? 142.175 157.873 157.400 1.00 33.31 ?  128 PHE B O     1 
ATOM   6619  C  CB    . PHE B 1 128 ? 143.704 154.964 157.133 1.00 28.61 ?  128 PHE B CB    1 
ATOM   6620  C  CG    . PHE B 1 128 ? 142.668 155.050 156.051 1.00 33.12 ?  128 PHE B CG    1 
ATOM   6621  C  CD1   . PHE B 1 128 ? 142.960 155.664 154.846 1.00 31.02 ?  128 PHE B CD1   1 
ATOM   6622  C  CD2   . PHE B 1 128 ? 141.401 154.526 156.242 1.00 32.42 ?  128 PHE B CD2   1 
ATOM   6623  C  CE1   . PHE B 1 128 ? 142.011 155.750 153.850 1.00 31.53 ?  128 PHE B CE1   1 
ATOM   6624  C  CE2   . PHE B 1 128 ? 140.447 154.613 155.251 1.00 31.93 ?  128 PHE B CE2   1 
ATOM   6625  C  CZ    . PHE B 1 128 ? 140.753 155.226 154.052 1.00 31.58 ?  128 PHE B CZ    1 
ATOM   6626  N  N     . PHE B 1 129 ? 141.806 156.508 159.153 1.00 29.04 ?  129 PHE B N     1 
ATOM   6627  C  CA    . PHE B 1 129 ? 140.495 157.086 159.437 1.00 26.13 ?  129 PHE B CA    1 
ATOM   6628  C  C     . PHE B 1 129 ? 140.602 158.551 159.840 1.00 28.48 ?  129 PHE B C     1 
ATOM   6629  O  O     . PHE B 1 129 ? 139.808 159.386 159.392 1.00 32.18 ?  129 PHE B O     1 
ATOM   6630  C  CB    . PHE B 1 129 ? 139.802 156.294 160.545 1.00 28.98 ?  129 PHE B CB    1 
ATOM   6631  C  CG    . PHE B 1 129 ? 139.163 155.021 160.082 1.00 26.86 ?  129 PHE B CG    1 
ATOM   6632  C  CD1   . PHE B 1 129 ? 138.975 154.769 158.736 1.00 25.66 ?  129 PHE B CD1   1 
ATOM   6633  C  CD2   . PHE B 1 129 ? 138.736 154.079 161.001 1.00 25.26 ?  129 PHE B CD2   1 
ATOM   6634  C  CE1   . PHE B 1 129 ? 138.382 153.597 158.316 1.00 26.72 ?  129 PHE B CE1   1 
ATOM   6635  C  CE2   . PHE B 1 129 ? 138.140 152.908 160.587 1.00 28.32 ?  129 PHE B CE2   1 
ATOM   6636  C  CZ    . PHE B 1 129 ? 137.962 152.665 159.242 1.00 30.23 ?  129 PHE B CZ    1 
ATOM   6637  N  N     . ALA B 1 130 ? 141.575 158.880 160.691 1.00 33.69 ?  130 ALA B N     1 
ATOM   6638  C  CA    . ALA B 1 130 ? 141.624 160.215 161.279 1.00 35.78 ?  130 ALA B CA    1 
ATOM   6639  C  C     . ALA B 1 130 ? 141.998 161.281 160.258 1.00 40.17 ?  130 ALA B C     1 
ATOM   6640  O  O     . ALA B 1 130 ? 141.587 162.438 160.399 1.00 46.69 ?  130 ALA B O     1 
ATOM   6641  C  CB    . ALA B 1 130 ? 142.603 160.234 162.448 1.00 33.05 ?  130 ALA B CB    1 
ATOM   6642  N  N     . ASN B 1 131 ? 142.777 160.917 159.237 1.00 41.05 ?  131 ASN B N     1 
ATOM   6643  C  CA    . ASN B 1 131 ? 143.173 161.837 158.169 1.00 41.85 ?  131 ASN B CA    1 
ATOM   6644  C  C     . ASN B 1 131 ? 143.925 163.049 158.723 1.00 41.78 ?  131 ASN B C     1 
ATOM   6645  O  O     . ASN B 1 131 ? 143.617 164.200 158.409 1.00 44.86 ?  131 ASN B O     1 
ATOM   6646  C  CB    . ASN B 1 131 ? 141.959 162.274 157.343 1.00 38.10 ?  131 ASN B CB    1 
ATOM   6647  C  CG    . ASN B 1 131 ? 142.320 162.614 155.911 1.00 45.08 ?  131 ASN B CG    1 
ATOM   6648  O  OD1   . ASN B 1 131 ? 143.269 162.068 155.351 1.00 45.24 ?  131 ASN B OD1   1 
ATOM   6649  N  ND2   . ASN B 1 131 ? 141.559 163.521 155.310 1.00 43.88 ?  131 ASN B ND2   1 
ATOM   6650  N  N     . GLY B 1 132 ? 144.924 162.777 159.561 1.00 42.24 ?  132 GLY B N     1 
ATOM   6651  C  CA    . GLY B 1 132 ? 145.795 163.811 160.080 1.00 43.72 ?  132 GLY B CA    1 
ATOM   6652  C  C     . GLY B 1 132 ? 145.491 164.293 161.481 1.00 46.62 ?  132 GLY B C     1 
ATOM   6653  O  O     . GLY B 1 132 ? 146.207 165.169 161.980 1.00 49.36 ?  132 GLY B O     1 
ATOM   6654  N  N     . ASP B 1 133 ? 144.462 163.756 162.133 1.00 42.99 ?  133 ASP B N     1 
ATOM   6655  C  CA    . ASP B 1 133 ? 144.079 164.174 163.479 1.00 43.79 ?  133 ASP B CA    1 
ATOM   6656  C  C     . ASP B 1 133 ? 144.587 163.137 164.477 1.00 46.29 ?  133 ASP B C     1 
ATOM   6657  O  O     . ASP B 1 133 ? 144.090 162.008 164.515 1.00 48.43 ?  133 ASP B O     1 
ATOM   6658  C  CB    . ASP B 1 133 ? 142.565 164.344 163.580 1.00 45.24 ?  133 ASP B CB    1 
ATOM   6659  C  CG    . ASP B 1 133 ? 142.150 165.198 164.763 1.00 48.48 ?  133 ASP B CG    1 
ATOM   6660  O  OD1   . ASP B 1 133 ? 142.961 165.363 165.698 1.00 49.94 ?  133 ASP B OD1   1 
ATOM   6661  O  OD2   . ASP B 1 133 ? 141.008 165.702 164.759 1.00 49.76 -1 133 ASP B OD2   1 
ATOM   6662  N  N     . THR B 1 134 ? 145.576 163.524 165.283 1.00 46.10 ?  134 THR B N     1 
ATOM   6663  C  CA    . THR B 1 134 ? 146.161 162.586 166.237 1.00 45.62 ?  134 THR B CA    1 
ATOM   6664  C  C     . THR B 1 134 ? 145.157 162.175 167.307 1.00 45.11 ?  134 THR B C     1 
ATOM   6665  O  O     . THR B 1 134 ? 145.076 160.995 167.667 1.00 45.77 ?  134 THR B O     1 
ATOM   6666  C  CB    . THR B 1 134 ? 147.404 163.198 166.878 1.00 47.78 ?  134 THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 134 ? 148.257 163.721 165.853 1.00 49.81 ?  134 THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 134 ? 148.161 162.149 167.678 1.00 46.42 ?  134 THR B CG2   1 
ATOM   6669  N  N     . GLU B 1 135 ? 144.388 163.132 167.833 1.00 43.87 ?  135 GLU B N     1 
ATOM   6670  C  CA    . GLU B 1 135 ? 143.392 162.802 168.845 1.00 42.72 ?  135 GLU B CA    1 
ATOM   6671  C  C     . GLU B 1 135 ? 142.297 161.910 168.274 1.00 44.61 ?  135 GLU B C     1 
ATOM   6672  O  O     . GLU B 1 135 ? 141.851 160.964 168.934 1.00 45.08 ?  135 GLU B O     1 
ATOM   6673  C  CB    . GLU B 1 135 ? 142.798 164.081 169.434 1.00 45.96 ?  135 GLU B CB    1 
ATOM   6674  C  CG    . GLU B 1 135 ? 143.793 164.901 170.234 1.00 46.64 ?  135 GLU B CG    1 
ATOM   6675  C  CD    . GLU B 1 135 ? 144.567 164.062 171.232 1.00 50.56 ?  135 GLU B CD    1 
ATOM   6676  O  OE1   . GLU B 1 135 ? 143.931 163.442 172.109 1.00 49.79 ?  135 GLU B OE1   1 
ATOM   6677  O  OE2   . GLU B 1 135 ? 145.812 164.019 171.136 1.00 49.37 -1 135 GLU B OE2   1 
ATOM   6678  N  N     . LYS B 1 136 ? 141.854 162.193 167.048 1.00 40.26 ?  136 LYS B N     1 
ATOM   6679  C  CA    . LYS B 1 136 ? 140.873 161.330 166.400 1.00 37.63 ?  136 LYS B CA    1 
ATOM   6680  C  C     . LYS B 1 136 ? 141.452 159.944 166.141 1.00 37.69 ?  136 LYS B C     1 
ATOM   6681  O  O     . LYS B 1 136 ? 140.747 158.935 166.256 1.00 41.90 ?  136 LYS B O     1 
ATOM   6682  C  CB    . LYS B 1 136 ? 140.392 161.968 165.099 1.00 42.81 ?  136 LYS B CB    1 
ATOM   6683  C  CG    . LYS B 1 136 ? 139.088 161.406 164.567 1.00 41.41 ?  136 LYS B CG    1 
ATOM   6684  C  CD    . LYS B 1 136 ? 137.893 162.160 165.120 1.00 41.96 ?  136 LYS B CD    1 
ATOM   6685  C  CE    . LYS B 1 136 ? 136.655 161.925 164.273 1.00 42.73 ?  136 LYS B CE    1 
ATOM   6686  N  NZ    . LYS B 1 136 ? 135.570 162.889 164.598 1.00 43.51 1  136 LYS B NZ    1 
ATOM   6687  N  N     . ALA B 1 137 ? 142.737 159.877 165.786 1.00 36.90 ?  137 ALA B N     1 
ATOM   6688  C  CA    . ALA B 1 137 ? 143.383 158.583 165.592 1.00 33.48 ?  137 ALA B CA    1 
ATOM   6689  C  C     . ALA B 1 137 ? 143.425 157.789 166.890 1.00 36.36 ?  137 ALA B C     1 
ATOM   6690  O  O     . ALA B 1 137 ? 143.194 156.576 166.892 1.00 39.45 ?  137 ALA B O     1 
ATOM   6691  C  CB    . ALA B 1 137 ? 144.791 158.776 165.031 1.00 33.49 ?  137 ALA B CB    1 
ATOM   6692  N  N     . LYS B 1 138 ? 143.708 158.461 168.008 1.00 38.61 ?  138 LYS B N     1 
ATOM   6693  C  CA    . LYS B 1 138 ? 143.685 157.784 169.302 1.00 36.74 ?  138 LYS B CA    1 
ATOM   6694  C  C     . LYS B 1 138 ? 142.276 157.337 169.668 1.00 37.49 ?  138 LYS B C     1 
ATOM   6695  O  O     . LYS B 1 138 ? 142.093 156.268 170.260 1.00 39.01 ?  138 LYS B O     1 
ATOM   6696  C  CB    . LYS B 1 138 ? 144.255 158.695 170.387 1.00 41.46 ?  138 LYS B CB    1 
ATOM   6697  C  CG    . LYS B 1 138 ? 145.705 159.080 170.175 1.00 41.35 ?  138 LYS B CG    1 
ATOM   6698  C  CD    . LYS B 1 138 ? 146.434 159.185 171.500 1.00 38.39 ?  138 LYS B CD    1 
ATOM   6699  C  CE    . LYS B 1 138 ? 147.576 160.176 171.416 1.00 41.44 ?  138 LYS B CE    1 
ATOM   6700  N  NZ    . LYS B 1 138 ? 147.118 161.508 170.934 1.00 43.43 1  138 LYS B NZ    1 
ATOM   6701  N  N     . GLU B 1 139 ? 141.269 158.148 169.340 1.00 37.44 ?  139 GLU B N     1 
ATOM   6702  C  CA    . GLU B 1 139 ? 139.887 157.746 169.589 1.00 37.33 ?  139 GLU B CA    1 
ATOM   6703  C  C     . GLU B 1 139 ? 139.525 156.498 168.793 1.00 36.11 ?  139 GLU B C     1 
ATOM   6704  O  O     . GLU B 1 139 ? 138.898 155.574 169.321 1.00 41.74 ?  139 GLU B O     1 
ATOM   6705  C  CB    . GLU B 1 139 ? 138.936 158.893 169.252 1.00 34.82 ?  139 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 1 139 ? 139.009 160.065 170.214 1.00 38.00 ?  139 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 1 139 ? 138.076 161.194 169.827 1.00 45.17 ?  139 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 1 139 ? 137.014 160.912 169.233 1.00 43.55 ?  139 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 1 139 ? 138.403 162.364 170.117 1.00 44.22 -1 139 GLU B OE2   1 
ATOM   6710  N  N     . TYR B 1 140 ? 139.925 156.449 167.520 1.00 29.54 ?  140 TYR B N     1 
ATOM   6711  C  CA    . TYR B 1 140 ? 139.679 155.260 166.708 1.00 28.47 ?  140 TYR B CA    1 
ATOM   6712  C  C     . TYR B 1 140 ? 140.437 154.055 167.252 1.00 31.07 ?  140 TYR B C     1 
ATOM   6713  O  O     . TYR B 1 140 ? 139.925 152.929 167.237 1.00 35.49 ?  140 TYR B O     1 
ATOM   6714  C  CB    . TYR B 1 140 ? 140.072 155.521 165.256 1.00 29.36 ?  140 TYR B CB    1 
ATOM   6715  C  CG    . TYR B 1 140 ? 139.100 156.378 164.485 1.00 30.90 ?  140 TYR B CG    1 
ATOM   6716  C  CD1   . TYR B 1 140 ? 137.755 156.043 164.410 1.00 31.12 ?  140 TYR B CD1   1 
ATOM   6717  C  CD2   . TYR B 1 140 ? 139.529 157.519 163.826 1.00 32.00 ?  140 TYR B CD2   1 
ATOM   6718  C  CE1   . TYR B 1 140 ? 136.867 156.825 163.701 1.00 34.65 ?  140 TYR B CE1   1 
ATOM   6719  C  CE2   . TYR B 1 140 ? 138.650 158.306 163.119 1.00 30.75 ?  140 TYR B CE2   1 
ATOM   6720  C  CZ    . TYR B 1 140 ? 137.323 157.956 163.057 1.00 28.98 ?  140 TYR B CZ    1 
ATOM   6721  O  OH    . TYR B 1 140 ? 136.453 158.746 162.348 1.00 37.84 ?  140 TYR B OH    1 
ATOM   6722  N  N     . VAL B 1 141 ? 141.668 154.273 167.719 1.00 32.75 ?  141 VAL B N     1 
ATOM   6723  C  CA    . VAL B 1 141 ? 142.456 153.190 168.301 1.00 32.90 ?  141 VAL B CA    1 
ATOM   6724  C  C     . VAL B 1 141 ? 141.760 152.628 169.531 1.00 32.97 ?  141 VAL B C     1 
ATOM   6725  O  O     . VAL B 1 141 ? 141.666 151.411 169.711 1.00 38.73 ?  141 VAL B O     1 
ATOM   6726  C  CB    . VAL B 1 141 ? 143.878 153.681 168.631 1.00 35.19 ?  141 VAL B CB    1 
ATOM   6727  C  CG1   . VAL B 1 141 ? 144.449 152.899 169.787 1.00 33.55 ?  141 VAL B CG1   1 
ATOM   6728  C  CG2   . VAL B 1 141 ? 144.772 153.531 167.424 1.00 33.99 ?  141 VAL B CG2   1 
ATOM   6729  N  N     . ASN B 1 142 ? 141.266 153.509 170.402 1.00 32.61 ?  142 ASN B N     1 
ATOM   6730  C  CA    . ASN B 1 142 ? 140.558 153.047 171.589 1.00 30.80 ?  142 ASN B CA    1 
ATOM   6731  C  C     . ASN B 1 142 ? 139.249 152.364 171.225 1.00 31.55 ?  142 ASN B C     1 
ATOM   6732  O  O     . ASN B 1 142 ? 138.825 151.429 171.913 1.00 35.97 ?  142 ASN B O     1 
ATOM   6733  C  CB    . ASN B 1 142 ? 140.306 154.217 172.538 1.00 28.16 ?  142 ASN B CB    1 
ATOM   6734  C  CG    . ASN B 1 142 ? 141.565 154.672 173.245 1.00 32.27 ?  142 ASN B CG    1 
ATOM   6735  O  OD1   . ASN B 1 142 ? 142.253 153.877 173.884 1.00 32.50 ?  142 ASN B OD1   1 
ATOM   6736  N  ND2   . ASN B 1 142 ? 141.876 155.957 173.130 1.00 34.28 ?  142 ASN B ND2   1 
ATOM   6737  N  N     . LEU B 1 143 ? 138.598 152.815 170.153 1.00 31.52 ?  143 LEU B N     1 
ATOM   6738  C  CA    . LEU B 1 143 ? 137.340 152.208 169.733 1.00 25.88 ?  143 LEU B CA    1 
ATOM   6739  C  C     . LEU B 1 143 ? 137.553 150.806 169.176 1.00 30.44 ?  143 LEU B C     1 
ATOM   6740  O  O     . LEU B 1 143 ? 136.736 149.908 169.411 1.00 32.84 ?  143 LEU B O     1 
ATOM   6741  C  CB    . LEU B 1 143 ? 136.663 153.102 168.698 1.00 25.23 ?  143 LEU B CB    1 
ATOM   6742  C  CG    . LEU B 1 143 ? 135.150 152.976 168.548 1.00 28.76 ?  143 LEU B CG    1 
ATOM   6743  C  CD1   . LEU B 1 143 ? 134.458 153.680 169.698 1.00 31.58 ?  143 LEU B CD1   1 
ATOM   6744  C  CD2   . LEU B 1 143 ? 134.718 153.568 167.224 1.00 28.42 ?  143 LEU B CD2   1 
ATOM   6745  N  N     . MET B 1 144 ? 138.637 150.599 168.430 1.00 28.96 ?  144 MET B N     1 
ATOM   6746  C  CA    . MET B 1 144 ? 138.881 149.306 167.801 1.00 21.69 ?  144 MET B CA    1 
ATOM   6747  C  C     . MET B 1 144 ? 139.619 148.325 168.701 1.00 26.49 ?  144 MET B C     1 
ATOM   6748  O  O     . MET B 1 144 ? 139.371 147.117 168.616 1.00 30.49 ?  144 MET B O     1 
ATOM   6749  C  CB    . MET B 1 144 ? 139.663 149.493 166.498 1.00 24.86 ?  144 MET B CB    1 
ATOM   6750  C  CG    . MET B 1 144 ? 138.878 150.203 165.409 1.00 25.95 ?  144 MET B CG    1 
ATOM   6751  S  SD    . MET B 1 144 ? 139.738 150.210 163.829 1.00 37.66 ?  144 MET B SD    1 
ATOM   6752  C  CE    . MET B 1 144 ? 140.568 151.792 163.915 1.00 27.90 ?  144 MET B CE    1 
ATOM   6753  N  N     . ILE B 1 145 ? 140.529 148.805 169.550 1.00 29.57 ?  145 ILE B N     1 
ATOM   6754  C  CA    . ILE B 1 145 ? 141.229 147.917 170.473 1.00 30.47 ?  145 ILE B CA    1 
ATOM   6755  C  C     . ILE B 1 145 ? 140.295 147.447 171.584 1.00 31.16 ?  145 ILE B C     1 
ATOM   6756  O  O     . ILE B 1 145 ? 140.426 146.318 172.071 1.00 35.22 ?  145 ILE B O     1 
ATOM   6757  C  CB    . ILE B 1 145 ? 142.497 148.600 171.021 1.00 29.75 ?  145 ILE B CB    1 
ATOM   6758  C  CG1   . ILE B 1 145 ? 143.586 147.563 171.301 1.00 28.07 ?  145 ILE B CG1   1 
ATOM   6759  C  CG2   . ILE B 1 145 ? 142.203 149.427 172.267 1.00 31.72 ?  145 ILE B CG2   1 
ATOM   6760  C  CD1   . ILE B 1 145 ? 144.217 146.987 170.056 1.00 28.63 ?  145 ILE B CD1   1 
ATOM   6761  N  N     . ASN B 1 146 ? 139.343 148.286 172.000 1.00 28.14 ?  146 ASN B N     1 
ATOM   6762  C  CA    . ASN B 1 146 ? 138.261 147.824 172.858 1.00 28.75 ?  146 ASN B CA    1 
ATOM   6763  C  C     . ASN B 1 146 ? 137.277 146.947 172.104 1.00 30.68 ?  146 ASN B C     1 
ATOM   6764  O  O     . ASN B 1 146 ? 136.389 146.357 172.730 1.00 37.17 ?  146 ASN B O     1 
ATOM   6765  C  CB    . ASN B 1 146 ? 137.520 149.010 173.475 1.00 28.50 ?  146 ASN B CB    1 
ATOM   6766  C  CG    . ASN B 1 146 ? 138.372 149.784 174.458 1.00 31.95 ?  146 ASN B CG    1 
ATOM   6767  O  OD1   . ASN B 1 146 ? 139.372 149.277 174.964 1.00 33.23 ?  146 ASN B OD1   1 
ATOM   6768  N  ND2   . ASN B 1 146 ? 137.979 151.022 174.733 1.00 31.99 ?  146 ASN B ND2   1 
ATOM   6769  N  N     . GLN B 1 147 ? 137.412 146.868 170.779 1.00 27.45 ?  147 GLN B N     1 
ATOM   6770  C  CA    . GLN B 1 147 ? 136.544 146.068 169.922 1.00 23.39 ?  147 GLN B CA    1 
ATOM   6771  C  C     . GLN B 1 147 ? 135.089 146.509 170.026 1.00 23.64 ?  147 GLN B C     1 
ATOM   6772  O  O     . GLN B 1 147 ? 134.175 145.696 169.902 1.00 30.53 ?  147 GLN B O     1 
ATOM   6773  C  CB    . GLN B 1 147 ? 136.683 144.575 170.231 1.00 26.93 ?  147 GLN B CB    1 
ATOM   6774  C  CG    . GLN B 1 147 ? 138.064 144.022 169.936 1.00 20.38 ?  147 GLN B CG    1 
ATOM   6775  C  CD    . GLN B 1 147 ? 138.046 142.538 169.647 1.00 27.43 ?  147 GLN B CD    1 
ATOM   6776  O  OE1   . GLN B 1 147 ? 138.726 142.063 168.737 1.00 28.19 ?  147 GLN B OE1   1 
ATOM   6777  N  NE2   . GLN B 1 147 ? 137.268 141.795 170.422 1.00 34.56 ?  147 GLN B NE2   1 
ATOM   6778  N  N     . GLU B 1 148 ? 134.869 147.801 170.270 1.00 26.03 ?  148 GLU B N     1 
ATOM   6779  C  CA    . GLU B 1 148 ? 133.521 148.352 170.212 1.00 23.10 ?  148 GLU B CA    1 
ATOM   6780  C  C     . GLU B 1 148 ? 133.032 148.487 168.778 1.00 26.63 ?  148 GLU B C     1 
ATOM   6781  O  O     . GLU B 1 148 ? 131.846 148.273 168.506 1.00 32.90 ?  148 GLU B O     1 
ATOM   6782  C  CB    . GLU B 1 148 ? 133.479 149.713 170.906 1.00 21.39 ?  148 GLU B CB    1 
ATOM   6783  C  CG    . GLU B 1 148 ? 133.830 149.670 172.379 1.00 26.46 ?  148 GLU B CG    1 
ATOM   6784  C  CD    . GLU B 1 148 ? 134.016 151.051 172.969 1.00 32.26 ?  148 GLU B CD    1 
ATOM   6785  O  OE1   . GLU B 1 148 ? 135.117 151.621 172.818 1.00 33.54 ?  148 GLU B OE1   1 
ATOM   6786  O  OE2   . GLU B 1 148 ? 133.061 151.571 173.580 1.00 37.57 -1 148 GLU B OE2   1 
ATOM   6787  N  N     . TYR B 1 149 ? 133.925 148.834 167.858 1.00 23.60 ?  149 TYR B N     1 
ATOM   6788  C  CA    . TYR B 1 149 ? 133.596 148.995 166.452 1.00 19.15 ?  149 TYR B CA    1 
ATOM   6789  C  C     . TYR B 1 149 ? 134.580 148.207 165.607 1.00 22.53 ?  149 TYR B C     1 
ATOM   6790  O  O     . TYR B 1 149 ? 135.770 148.134 165.924 1.00 28.88 ?  149 TYR B O     1 
ATOM   6791  C  CB    . TYR B 1 149 ? 133.616 150.467 166.039 1.00 21.16 ?  149 TYR B CB    1 
ATOM   6792  C  CG    . TYR B 1 149 ? 133.519 150.685 164.547 1.00 21.61 ?  149 TYR B CG    1 
ATOM   6793  C  CD1   . TYR B 1 149 ? 132.371 150.338 163.847 1.00 13.92 ?  149 TYR B CD1   1 
ATOM   6794  C  CD2   . TYR B 1 149 ? 134.575 151.241 163.840 1.00 19.53 ?  149 TYR B CD2   1 
ATOM   6795  C  CE1   . TYR B 1 149 ? 132.280 150.537 162.485 1.00 17.41 ?  149 TYR B CE1   1 
ATOM   6796  C  CE2   . TYR B 1 149 ? 134.494 151.445 162.480 1.00 20.91 ?  149 TYR B CE2   1 
ATOM   6797  C  CZ    . TYR B 1 149 ? 133.344 151.093 161.806 1.00 20.04 ?  149 TYR B CZ    1 
ATOM   6798  O  OH    . TYR B 1 149 ? 133.263 151.295 160.449 1.00 18.44 ?  149 TYR B OH    1 
ATOM   6799  N  N     . GLN B 1 150 ? 134.074 147.616 164.535 1.00 17.68 ?  150 GLN B N     1 
ATOM   6800  C  CA    . GLN B 1 150 ? 134.883 146.829 163.614 1.00 10.71 ?  150 GLN B CA    1 
ATOM   6801  C  C     . GLN B 1 150 ? 134.631 147.307 162.194 1.00 20.38 ?  150 GLN B C     1 
ATOM   6802  O  O     . GLN B 1 150 ? 133.500 147.169 161.689 1.00 23.27 ?  150 GLN B O     1 
ATOM   6803  C  CB    . GLN B 1 150 ? 134.549 145.345 163.751 1.00 17.41 ?  150 GLN B CB    1 
ATOM   6804  C  CG    . GLN B 1 150 ? 135.307 144.450 162.803 1.00 18.97 ?  150 GLN B CG    1 
ATOM   6805  C  CD    . GLN B 1 150 ? 136.808 144.605 162.925 1.00 17.16 ?  150 GLN B CD    1 
ATOM   6806  O  OE1   . GLN B 1 150 ? 137.391 144.322 163.970 1.00 30.40 ?  150 GLN B OE1   1 
ATOM   6807  N  NE2   . GLN B 1 150 ? 137.443 145.050 161.850 1.00 15.84 ?  150 GLN B NE2   1 
ATOM   6808  N  N     . PRO B 1 151 ? 135.620 147.896 161.526 1.00 26.31 ?  151 PRO B N     1 
ATOM   6809  C  CA    . PRO B 1 151 ? 135.464 148.191 160.100 1.00 16.21 ?  151 PRO B CA    1 
ATOM   6810  C  C     . PRO B 1 151 ? 135.300 146.906 159.306 1.00 16.18 ?  151 PRO B C     1 
ATOM   6811  O  O     . PRO B 1 151 ? 135.772 145.839 159.706 1.00 21.62 ?  151 PRO B O     1 
ATOM   6812  C  CB    . PRO B 1 151 ? 136.766 148.915 159.738 1.00 18.71 ?  151 PRO B CB    1 
ATOM   6813  C  CG    . PRO B 1 151 ? 137.299 149.420 161.039 1.00 18.97 ?  151 PRO B CG    1 
ATOM   6814  C  CD    . PRO B 1 151 ? 136.885 148.420 162.068 1.00 21.62 ?  151 PRO B CD    1 
ATOM   6815  N  N     . SER B 1 152 ? 134.603 147.013 158.179 1.00 21.04 ?  152 SER B N     1 
ATOM   6816  C  CA    . SER B 1 152 ? 134.344 145.850 157.346 1.00 14.61 ?  152 SER B CA    1 
ATOM   6817  C  C     . SER B 1 152 ? 135.650 145.205 156.893 1.00 22.02 ?  152 SER B C     1 
ATOM   6818  O  O     . SER B 1 152 ? 136.731 145.796 156.975 1.00 25.96 ?  152 SER B O     1 
ATOM   6819  C  CB    . SER B 1 152 ? 133.509 146.237 156.128 1.00 20.91 ?  152 SER B CB    1 
ATOM   6820  O  OG    . SER B 1 152 ? 134.244 147.070 155.250 1.00 24.93 ?  152 SER B OG    1 
ATOM   6821  N  N     . THR B 1 153 ? 135.538 143.967 156.415 1.00 28.20 ?  153 THR B N     1 
ATOM   6822  C  CA    . THR B 1 153 ? 136.703 143.241 155.915 1.00 20.89 ?  153 THR B CA    1 
ATOM   6823  C  C     . THR B 1 153 ? 137.483 144.015 154.856 1.00 27.54 ?  153 THR B C     1 
ATOM   6824  O  O     . THR B 1 153 ? 138.717 144.084 154.970 1.00 27.63 ?  153 THR B O     1 
ATOM   6825  C  CB    . THR B 1 153 ? 136.260 141.866 155.394 1.00 25.86 ?  153 THR B CB    1 
ATOM   6826  O  OG1   . THR B 1 153 ? 135.942 141.014 156.500 1.00 29.62 ?  153 THR B OG1   1 
ATOM   6827  C  CG2   . THR B 1 153 ? 137.358 141.222 154.560 1.00 25.78 ?  153 THR B CG2   1 
ATOM   6828  N  N     . PRO B 1 154 ? 136.860 144.624 153.837 1.00 25.81 ?  154 PRO B N     1 
ATOM   6829  C  CA    . PRO B 1 154 ? 137.659 145.449 152.911 1.00 19.80 ?  154 PRO B CA    1 
ATOM   6830  C  C     . PRO B 1 154 ? 138.376 146.595 153.602 1.00 20.96 ?  154 PRO B C     1 
ATOM   6831  O  O     . PRO B 1 154 ? 139.575 146.802 153.377 1.00 26.68 ?  154 PRO B O     1 
ATOM   6832  C  CB    . PRO B 1 154 ? 136.617 145.947 151.902 1.00 21.37 ?  154 PRO B CB    1 
ATOM   6833  C  CG    . PRO B 1 154 ? 135.522 144.959 151.968 1.00 24.97 ?  154 PRO B CG    1 
ATOM   6834  C  CD    . PRO B 1 154 ? 135.457 144.529 153.394 1.00 19.97 ?  154 PRO B CD    1 
ATOM   6835  N  N     . THR B 1 155 ? 137.674 147.340 154.458 1.00 22.65 ?  155 THR B N     1 
ATOM   6836  C  CA    . THR B 1 155 ? 138.287 148.485 155.122 1.00 20.13 ?  155 THR B CA    1 
ATOM   6837  C  C     . THR B 1 155 ? 139.354 148.043 156.117 1.00 24.21 ?  155 THR B C     1 
ATOM   6838  O  O     . THR B 1 155 ? 140.469 148.573 156.121 1.00 29.73 ?  155 THR B O     1 
ATOM   6839  C  CB    . THR B 1 155 ? 137.218 149.323 155.820 1.00 22.59 ?  155 THR B CB    1 
ATOM   6840  O  OG1   . THR B 1 155 ? 136.180 149.652 154.889 1.00 23.45 ?  155 THR B OG1   1 
ATOM   6841  C  CG2   . THR B 1 155 ? 137.823 150.605 156.363 1.00 17.64 ?  155 THR B CG2   1 
ATOM   6842  N  N     . PHE B 1 156 ? 139.030 147.068 156.970 1.00 23.30 ?  156 PHE B N     1 
ATOM   6843  C  CA    . PHE B 1 156 ? 139.991 146.619 157.971 1.00 20.13 ?  156 PHE B CA    1 
ATOM   6844  C  C     . PHE B 1 156 ? 141.228 146.011 157.322 1.00 29.69 ?  156 PHE B C     1 
ATOM   6845  O  O     . PHE B 1 156 ? 142.354 146.244 157.774 1.00 29.95 ?  156 PHE B O     1 
ATOM   6846  C  CB    . PHE B 1 156 ? 139.336 145.614 158.918 1.00 23.60 ?  156 PHE B CB    1 
ATOM   6847  C  CG    . PHE B 1 156 ? 140.091 145.407 160.199 1.00 28.03 ?  156 PHE B CG    1 
ATOM   6848  C  CD1   . PHE B 1 156 ? 140.342 146.471 161.049 1.00 24.88 ?  156 PHE B CD1   1 
ATOM   6849  C  CD2   . PHE B 1 156 ? 140.551 144.151 160.552 1.00 23.77 ?  156 PHE B CD2   1 
ATOM   6850  C  CE1   . PHE B 1 156 ? 141.037 146.284 162.227 1.00 26.16 ?  156 PHE B CE1   1 
ATOM   6851  C  CE2   . PHE B 1 156 ? 141.247 143.959 161.729 1.00 22.91 ?  156 PHE B CE2   1 
ATOM   6852  C  CZ    . PHE B 1 156 ? 141.489 145.026 162.567 1.00 29.01 ?  156 PHE B CZ    1 
ATOM   6853  N  N     . LEU B 1 157 ? 141.037 145.229 156.260 1.00 30.11 ?  157 LEU B N     1 
ATOM   6854  C  CA    . LEU B 1 157 ? 142.153 144.541 155.624 1.00 26.59 ?  157 LEU B CA    1 
ATOM   6855  C  C     . LEU B 1 157 ? 142.993 145.478 154.764 1.00 31.97 ?  157 LEU B C     1 
ATOM   6856  O  O     . LEU B 1 157 ? 144.219 145.333 154.707 1.00 40.37 ?  157 LEU B O     1 
ATOM   6857  C  CB    . LEU B 1 157 ? 141.626 143.375 154.783 1.00 30.79 ?  157 LEU B CB    1 
ATOM   6858  C  CG    . LEU B 1 157 ? 142.606 142.654 153.859 1.00 29.61 ?  157 LEU B CG    1 
ATOM   6859  C  CD1   . LEU B 1 157 ? 143.675 141.938 154.662 1.00 32.68 ?  157 LEU B CD1   1 
ATOM   6860  C  CD2   . LEU B 1 157 ? 141.868 141.679 152.957 1.00 30.30 ?  157 LEU B CD2   1 
ATOM   6861  N  N     . ASN B 1 158 ? 142.367 146.450 154.099 1.00 30.57 ?  158 ASN B N     1 
ATOM   6862  C  CA    . ASN B 1 158 ? 143.033 147.202 153.048 1.00 29.15 ?  158 ASN B CA    1 
ATOM   6863  C  C     . ASN B 1 158 ? 143.365 148.643 153.407 1.00 32.44 ?  158 ASN B C     1 
ATOM   6864  O  O     . ASN B 1 158 ? 144.017 149.319 152.605 1.00 39.63 ?  158 ASN B O     1 
ATOM   6865  C  CB    . ASN B 1 158 ? 142.171 147.193 151.777 1.00 29.82 ?  158 ASN B CB    1 
ATOM   6866  C  CG    . ASN B 1 158 ? 141.951 145.798 151.234 1.00 35.71 ?  158 ASN B CG    1 
ATOM   6867  O  OD1   . ASN B 1 158 ? 142.779 144.908 151.424 1.00 40.03 ?  158 ASN B OD1   1 
ATOM   6868  N  ND2   . ASN B 1 158 ? 140.829 145.598 150.554 1.00 35.98 ?  158 ASN B ND2   1 
ATOM   6869  N  N     . ALA B 1 159 ? 142.942 149.138 154.568 1.00 31.90 ?  159 ALA B N     1 
ATOM   6870  C  CA    . ALA B 1 159 ? 143.196 150.535 154.905 1.00 33.22 ?  159 ALA B CA    1 
ATOM   6871  C  C     . ALA B 1 159 ? 144.692 150.794 155.032 1.00 38.83 ?  159 ALA B C     1 
ATOM   6872  O  O     . ALA B 1 159 ? 145.402 150.080 155.745 1.00 42.87 ?  159 ALA B O     1 
ATOM   6873  C  CB    . ALA B 1 159 ? 142.488 150.911 156.206 1.00 32.12 ?  159 ALA B CB    1 
ATOM   6874  N  N     . GLY B 1 160 ? 145.169 151.820 154.334 1.00 45.42 ?  160 GLY B N     1 
ATOM   6875  C  CA    . GLY B 1 160 ? 146.558 152.211 154.423 1.00 40.42 ?  160 GLY B CA    1 
ATOM   6876  C  C     . GLY B 1 160 ? 147.539 151.305 153.715 1.00 40.71 ?  160 GLY B C     1 
ATOM   6877  O  O     . GLY B 1 160 ? 148.747 151.447 153.928 1.00 45.57 ?  160 GLY B O     1 
ATOM   6878  N  N     . ARG B 1 161 ? 147.067 150.382 152.884 1.00 43.00 ?  161 ARG B N     1 
ATOM   6879  C  CA    . ARG B 1 161 ? 147.933 149.451 152.174 1.00 44.08 ?  161 ARG B CA    1 
ATOM   6880  C  C     . ARG B 1 161 ? 148.131 149.909 150.735 1.00 46.63 ?  161 ARG B C     1 
ATOM   6881  O  O     . ARG B 1 161 ? 147.198 150.398 150.092 1.00 46.53 ?  161 ARG B O     1 
ATOM   6882  C  CB    . ARG B 1 161 ? 147.351 148.037 152.193 1.00 38.66 ?  161 ARG B CB    1 
ATOM   6883  C  CG    . ARG B 1 161 ? 147.419 147.355 153.548 1.00 39.48 ?  161 ARG B CG    1 
ATOM   6884  C  CD    . ARG B 1 161 ? 147.255 145.851 153.418 1.00 40.50 ?  161 ARG B CD    1 
ATOM   6885  N  NE    . ARG B 1 161 ? 147.086 145.207 154.716 1.00 44.00 ?  161 ARG B NE    1 
ATOM   6886  C  CZ    . ARG B 1 161 ? 146.851 143.913 154.887 1.00 44.80 ?  161 ARG B CZ    1 
ATOM   6887  N  NH1   . ARG B 1 161 ? 146.759 143.086 153.859 1.00 44.14 1  161 ARG B NH1   1 
ATOM   6888  N  NH2   . ARG B 1 161 ? 146.703 143.439 156.120 1.00 43.06 ?  161 ARG B NH2   1 
ATOM   6889  N  N     . LYS B 1 162 ? 149.361 149.759 150.236 1.00 53.05 ?  162 LYS B N     1 
ATOM   6890  C  CA    . LYS B 1 162 ? 149.643 150.121 148.851 1.00 52.29 ?  162 LYS B CA    1 
ATOM   6891  C  C     . LYS B 1 162 ? 149.037 149.113 147.882 1.00 52.62 ?  162 LYS B C     1 
ATOM   6892  O  O     . LYS B 1 162 ? 148.433 149.497 146.875 1.00 52.82 ?  162 LYS B O     1 
ATOM   6893  C  CB    . LYS B 1 162 ? 151.152 150.239 148.637 1.00 52.13 ?  162 LYS B CB    1 
ATOM   6894  C  CG    . LYS B 1 162 ? 151.567 150.364 147.181 1.00 52.46 ?  162 LYS B CG    1 
ATOM   6895  C  CD    . LYS B 1 162 ? 151.614 151.819 146.740 1.00 54.30 ?  162 LYS B CD    1 
ATOM   6896  C  CE    . LYS B 1 162 ? 152.528 152.641 147.633 1.00 54.39 ?  162 LYS B CE    1 
ATOM   6897  N  NZ    . LYS B 1 162 ? 152.064 154.052 147.748 1.00 54.64 1  162 LYS B NZ    1 
ATOM   6898  N  N     . ARG B 1 163 ? 149.178 147.819 148.175 1.00 53.33 ?  163 ARG B N     1 
ATOM   6899  C  CA    . ARG B 1 163 ? 148.629 146.753 147.345 1.00 55.14 ?  163 ARG B CA    1 
ATOM   6900  C  C     . ARG B 1 163 ? 147.156 146.486 147.633 1.00 57.86 ?  163 ARG B C     1 
ATOM   6901  O  O     . ARG B 1 163 ? 146.646 145.408 147.306 1.00 56.49 ?  163 ARG B O     1 
ATOM   6902  C  CB    . ARG B 1 163 ? 149.447 145.471 147.530 1.00 56.25 ?  163 ARG B CB    1 
ATOM   6903  C  CG    . ARG B 1 163 ? 149.463 144.551 146.317 1.00 58.12 ?  163 ARG B CG    1 
ATOM   6904  C  CD    . ARG B 1 163 ? 149.614 143.092 146.724 1.00 56.45 ?  163 ARG B CD    1 
ATOM   6905  N  NE    . ARG B 1 163 ? 148.839 142.761 147.914 1.00 59.28 ?  163 ARG B NE    1 
ATOM   6906  C  CZ    . ARG B 1 163 ? 147.538 142.502 147.917 1.00 58.45 ?  163 ARG B CZ    1 
ATOM   6907  N  NH1   . ARG B 1 163 ? 146.825 142.526 146.803 1.00 56.93 1  163 ARG B NH1   1 
ATOM   6908  N  NH2   . ARG B 1 163 ? 146.937 142.210 149.067 1.00 56.83 ?  163 ARG B NH2   1 
ATOM   6909  N  N     . ARG B 1 164 ? 146.468 147.447 148.240 1.00 55.68 ?  164 ARG B N     1 
ATOM   6910  C  CA    . ARG B 1 164 ? 145.082 147.271 148.635 1.00 50.63 ?  164 ARG B CA    1 
ATOM   6911  C  C     . ARG B 1 164 ? 144.157 147.270 147.421 1.00 50.63 ?  164 ARG B C     1 
ATOM   6912  O  O     . ARG B 1 164 ? 144.524 147.685 146.317 1.00 50.44 ?  164 ARG B O     1 
ATOM   6913  C  CB    . ARG B 1 164 ? 144.658 148.382 149.592 1.00 48.84 ?  164 ARG B CB    1 
ATOM   6914  C  CG    . ARG B 1 164 ? 144.322 149.694 148.901 1.00 45.63 ?  164 ARG B CG    1 
ATOM   6915  C  CD    . ARG B 1 164 ? 143.394 150.547 149.748 1.00 48.21 ?  164 ARG B CD    1 
ATOM   6916  N  NE    . ARG B 1 164 ? 142.970 151.755 149.051 1.00 50.38 ?  164 ARG B NE    1 
ATOM   6917  C  CZ    . ARG B 1 164 ? 142.773 152.928 149.638 1.00 53.94 ?  164 ARG B CZ    1 
ATOM   6918  N  NH1   . ARG B 1 164 ? 142.963 153.090 150.936 1.00 51.60 1  164 ARG B NH1   1 
ATOM   6919  N  NH2   . ARG B 1 164 ? 142.379 153.964 148.903 1.00 53.54 ?  164 ARG B NH2   1 
ATOM   6920  N  N     . GLY B 1 165 ? 142.943 146.785 147.642 1.00 49.03 ?  165 GLY B N     1 
ATOM   6921  C  CA    . GLY B 1 165 ? 141.851 146.930 146.701 1.00 45.13 ?  165 GLY B CA    1 
ATOM   6922  C  C     . GLY B 1 165 ? 141.004 148.139 147.030 1.00 48.10 ?  165 GLY B C     1 
ATOM   6923  O  O     . GLY B 1 165 ? 141.514 149.223 147.329 1.00 48.97 ?  165 GLY B O     1 
ATOM   6924  N  N     . GLU B 1 166 ? 139.691 147.955 146.972 1.00 43.00 ?  166 GLU B N     1 
ATOM   6925  C  CA    . GLU B 1 166 ? 138.763 148.997 147.381 1.00 39.82 ?  166 GLU B CA    1 
ATOM   6926  C  C     . GLU B 1 166 ? 138.205 148.697 148.767 1.00 37.59 ?  166 GLU B C     1 
ATOM   6927  O  O     . GLU B 1 166 ? 138.041 147.538 149.157 1.00 33.46 ?  166 GLU B O     1 
ATOM   6928  C  CB    . GLU B 1 166 ? 137.619 149.137 146.376 1.00 36.97 ?  166 GLU B CB    1 
ATOM   6929  C  CG    . GLU B 1 166 ? 137.943 150.049 145.207 1.00 41.28 ?  166 GLU B CG    1 
ATOM   6930  C  CD    . GLU B 1 166 ? 138.187 151.483 145.632 1.00 42.78 ?  166 GLU B CD    1 
ATOM   6931  O  OE1   . GLU B 1 166 ? 137.551 151.932 146.609 1.00 47.42 ?  166 GLU B OE1   1 
ATOM   6932  O  OE2   . GLU B 1 166 ? 139.016 152.160 144.991 1.00 39.22 -1 166 GLU B OE2   1 
ATOM   6933  N  N     . LEU B 1 167 ? 137.918 149.763 149.514 1.00 30.71 ?  167 LEU B N     1 
ATOM   6934  C  CA    . LEU B 1 167 ? 137.370 149.626 150.855 1.00 23.73 ?  167 LEU B CA    1 
ATOM   6935  C  C     . LEU B 1 167 ? 135.869 149.380 150.862 1.00 29.03 ?  167 LEU B C     1 
ATOM   6936  O  O     . LEU B 1 167 ? 135.318 149.047 151.917 1.00 30.76 ?  167 LEU B O     1 
ATOM   6937  C  CB    . LEU B 1 167 ? 137.681 150.874 151.684 1.00 30.06 ?  167 LEU B CB    1 
ATOM   6938  C  CG    . LEU B 1 167 ? 139.149 151.273 151.840 1.00 26.48 ?  167 LEU B CG    1 
ATOM   6939  C  CD1   . LEU B 1 167 ? 139.301 152.210 153.015 1.00 27.89 ?  167 LEU B CD1   1 
ATOM   6940  C  CD2   . LEU B 1 167 ? 140.032 150.055 152.020 1.00 26.02 ?  167 LEU B CD2   1 
ATOM   6941  N  N     . VAL B 1 168 ? 135.198 149.536 149.725 1.00 29.42 ?  168 VAL B N     1 
ATOM   6942  C  CA    . VAL B 1 168 ? 133.760 149.308 149.650 1.00 22.91 ?  168 VAL B CA    1 
ATOM   6943  C  C     . VAL B 1 168 ? 133.504 147.825 149.428 1.00 26.85 ?  168 VAL B C     1 
ATOM   6944  O  O     . VAL B 1 168 ? 134.117 147.199 148.556 1.00 28.67 ?  168 VAL B O     1 
ATOM   6945  C  CB    . VAL B 1 168 ? 133.132 150.156 148.533 1.00 27.41 ?  168 VAL B CB    1 
ATOM   6946  C  CG1   . VAL B 1 168 ? 131.618 150.057 148.589 1.00 28.93 ?  168 VAL B CG1   1 
ATOM   6947  C  CG2   . VAL B 1 168 ? 133.579 151.599 148.654 1.00 27.27 ?  168 VAL B CG2   1 
ATOM   6948  N  N     . SER B 1 169 ? 132.595 147.259 150.222 1.00 35.86 ?  169 SER B N     1 
ATOM   6949  C  CA    . SER B 1 169 ? 132.329 145.828 150.155 1.00 37.59 ?  169 SER B CA    1 
ATOM   6950  C  C     . SER B 1 169 ? 131.389 145.481 149.006 1.00 36.82 ?  169 SER B C     1 
ATOM   6951  O  O     . SER B 1 169 ? 131.673 144.577 148.213 1.00 34.09 ?  169 SER B O     1 
ATOM   6952  C  CB    . SER B 1 169 ? 131.748 145.343 151.485 1.00 31.71 ?  169 SER B CB    1 
ATOM   6953  O  OG    . SER B 1 169 ? 131.556 143.938 151.478 1.00 34.78 ?  169 SER B OG    1 
ATOM   6954  N  N     . CYS B 1 170 ? 130.265 146.185 148.900 1.00 31.77 ?  170 CYS B N     1 
ATOM   6955  C  CA    . CYS B 1 170 ? 129.199 145.822 147.980 1.00 26.64 ?  170 CYS B CA    1 
ATOM   6956  C  C     . CYS B 1 170 ? 128.917 146.957 147.005 1.00 25.35 ?  170 CYS B C     1 
ATOM   6957  O  O     . CYS B 1 170 ? 129.003 148.136 147.363 1.00 24.91 ?  170 CYS B O     1 
ATOM   6958  C  CB    . CYS B 1 170 ? 127.922 145.466 148.745 1.00 34.42 ?  170 CYS B CB    1 
ATOM   6959  S  SG    . CYS B 1 170 ? 127.434 146.695 149.975 1.00 53.61 ?  170 CYS B SG    1 
ATOM   6960  N  N     . PHE B 1 171 ? 128.579 146.586 145.772 1.00 22.77 ?  171 PHE B N     1 
ATOM   6961  C  CA    . PHE B 1 171 ? 128.179 147.526 144.737 1.00 13.83 ?  171 PHE B CA    1 
ATOM   6962  C  C     . PHE B 1 171 ? 126.888 147.043 144.096 1.00 12.90 ?  171 PHE B C     1 
ATOM   6963  O  O     . PHE B 1 171 ? 126.707 145.842 143.878 1.00 24.47 ?  171 PHE B O     1 
ATOM   6964  C  CB    . PHE B 1 171 ? 129.259 147.680 143.665 1.00 16.07 ?  171 PHE B CB    1 
ATOM   6965  C  CG    . PHE B 1 171 ? 130.614 147.999 144.214 1.00 19.04 ?  171 PHE B CG    1 
ATOM   6966  C  CD1   . PHE B 1 171 ? 130.941 149.292 144.576 1.00 15.01 ?  171 PHE B CD1   1 
ATOM   6967  C  CD2   . PHE B 1 171 ? 131.565 147.005 144.362 1.00 18.02 ?  171 PHE B CD2   1 
ATOM   6968  C  CE1   . PHE B 1 171 ? 132.186 149.586 145.081 1.00 13.11 ?  171 PHE B CE1   1 
ATOM   6969  C  CE2   . PHE B 1 171 ? 132.813 147.297 144.864 1.00 15.58 ?  171 PHE B CE2   1 
ATOM   6970  C  CZ    . PHE B 1 171 ? 133.125 148.589 145.224 1.00 15.68 ?  171 PHE B CZ    1 
ATOM   6971  N  N     . LEU B 1 172 ? 125.995 147.981 143.799 1.00 13.06 ?  172 LEU B N     1 
ATOM   6972  C  CA    . LEU B 1 172 ? 124.703 147.678 143.198 1.00 10.19 ?  172 LEU B CA    1 
ATOM   6973  C  C     . LEU B 1 172 ? 124.579 148.457 141.899 1.00 11.41 ?  172 LEU B C     1 
ATOM   6974  O  O     . LEU B 1 172 ? 124.684 149.687 141.900 1.00 17.26 ?  172 LEU B O     1 
ATOM   6975  C  CB    . LEU B 1 172 ? 123.558 148.033 144.148 1.00 13.81 ?  172 LEU B CB    1 
ATOM   6976  C  CG    . LEU B 1 172 ? 123.387 147.211 145.425 1.00 8.92  ?  172 LEU B CG    1 
ATOM   6977  C  CD1   . LEU B 1 172 ? 124.310 147.710 146.525 1.00 10.47 ?  172 LEU B CD1   1 
ATOM   6978  C  CD2   . LEU B 1 172 ? 121.947 147.276 145.874 1.00 10.66 ?  172 LEU B CD2   1 
ATOM   6979  N  N     . LEU B 1 173 ? 124.349 147.745 140.800 1.00 17.95 ?  173 LEU B N     1 
ATOM   6980  C  CA    . LEU B 1 173 ? 124.279 148.345 139.476 1.00 9.04  ?  173 LEU B CA    1 
ATOM   6981  C  C     . LEU B 1 173 ? 122.873 148.226 138.907 1.00 14.71 ?  173 LEU B C     1 
ATOM   6982  O  O     . LEU B 1 173 ? 122.224 147.185 139.037 1.00 20.11 ?  173 LEU B O     1 
ATOM   6983  C  CB    . LEU B 1 173 ? 125.269 147.686 138.515 1.00 13.46 ?  173 LEU B CB    1 
ATOM   6984  C  CG    . LEU B 1 173 ? 126.727 147.553 138.952 1.00 18.36 ?  173 LEU B CG    1 
ATOM   6985  C  CD1   . LEU B 1 173 ? 127.532 146.893 137.848 1.00 21.69 ?  173 LEU B CD1   1 
ATOM   6986  C  CD2   . LEU B 1 173 ? 127.309 148.910 139.311 1.00 20.29 ?  173 LEU B CD2   1 
ATOM   6987  N  N     . GLU B 1 174 ? 122.411 149.302 138.279 1.00 23.41 ?  174 GLU B N     1 
ATOM   6988  C  CA    . GLU B 1 174 ? 121.174 149.286 137.512 1.00 20.21 ?  174 GLU B CA    1 
ATOM   6989  C  C     . GLU B 1 174 ? 121.511 149.096 136.039 1.00 18.27 ?  174 GLU B C     1 
ATOM   6990  O  O     . GLU B 1 174 ? 122.314 149.847 135.480 1.00 27.43 ?  174 GLU B O     1 
ATOM   6991  C  CB    . GLU B 1 174 ? 120.392 150.582 137.717 1.00 23.89 ?  174 GLU B CB    1 
ATOM   6992  C  CG    . GLU B 1 174 ? 119.678 150.680 139.051 1.00 18.30 ?  174 GLU B CG    1 
ATOM   6993  C  CD    . GLU B 1 174 ? 118.173 150.756 138.900 1.00 21.69 ?  174 GLU B CD    1 
ATOM   6994  O  OE1   . GLU B 1 174 ? 117.632 150.097 137.989 1.00 28.18 ?  174 GLU B OE1   1 
ATOM   6995  O  OE2   . GLU B 1 174 ? 117.531 151.475 139.691 1.00 24.53 -1 174 GLU B OE2   1 
ATOM   6996  N  N     . VAL B 1 175 ? 120.898 148.093 135.417 1.00 16.95 ?  175 VAL B N     1 
ATOM   6997  C  CA    . VAL B 1 175 ? 121.162 147.748 134.024 1.00 18.41 ?  175 VAL B CA    1 
ATOM   6998  C  C     . VAL B 1 175 ? 119.966 148.185 133.191 1.00 17.16 ?  175 VAL B C     1 
ATOM   6999  O  O     . VAL B 1 175 ? 118.855 147.672 133.368 1.00 13.81 ?  175 VAL B O     1 
ATOM   7000  C  CB    . VAL B 1 175 ? 121.431 146.246 133.855 1.00 19.90 ?  175 VAL B CB    1 
ATOM   7001  C  CG1   . VAL B 1 175 ? 122.107 145.972 132.519 1.00 14.27 ?  175 VAL B CG1   1 
ATOM   7002  C  CG2   . VAL B 1 175 ? 122.276 145.728 135.004 1.00 14.16 ?  175 VAL B CG2   1 
ATOM   7003  N  N     . ASN B 1 176 ? 120.194 149.129 132.283 1.00 18.38 ?  176 ASN B N     1 
ATOM   7004  C  CA    . ASN B 1 176 ? 119.145 149.575 131.382 1.00 19.52 ?  176 ASN B CA    1 
ATOM   7005  C  C     . ASN B 1 176 ? 118.957 148.573 130.247 1.00 20.93 ?  176 ASN B C     1 
ATOM   7006  O  O     . ASN B 1 176 ? 119.830 147.752 129.954 1.00 19.66 ?  176 ASN B O     1 
ATOM   7007  C  CB    . ASN B 1 176 ? 119.465 150.959 130.819 1.00 18.09 ?  176 ASN B CB    1 
ATOM   7008  C  CG    . ASN B 1 176 ? 118.236 151.829 130.683 1.00 19.52 ?  176 ASN B CG    1 
ATOM   7009  O  OD1   . ASN B 1 176 ? 117.109 151.339 130.710 1.00 27.15 ?  176 ASN B OD1   1 
ATOM   7010  N  ND2   . ASN B 1 176 ? 118.447 153.131 130.535 1.00 21.83 ?  176 ASN B ND2   1 
ATOM   7011  N  N     . ASP B 1 177 ? 117.795 148.658 129.600 1.00 25.27 ?  177 ASP B N     1 
ATOM   7012  C  CA    . ASP B 1 177 ? 117.400 147.698 128.570 1.00 22.19 ?  177 ASP B CA    1 
ATOM   7013  C  C     . ASP B 1 177 ? 118.008 148.114 127.233 1.00 23.70 ?  177 ASP B C     1 
ATOM   7014  O  O     . ASP B 1 177 ? 117.357 148.701 126.364 1.00 26.99 ?  177 ASP B O     1 
ATOM   7015  C  CB    . ASP B 1 177 ? 115.883 147.599 128.494 1.00 18.71 ?  177 ASP B CB    1 
ATOM   7016  C  CG    . ASP B 1 177 ? 115.414 146.610 127.454 1.00 26.22 ?  177 ASP B CG    1 
ATOM   7017  O  OD1   . ASP B 1 177 ? 116.069 145.560 127.291 1.00 30.83 ?  177 ASP B OD1   1 
ATOM   7018  O  OD2   . ASP B 1 177 ? 114.387 146.882 126.798 1.00 29.50 -1 177 ASP B OD2   1 
ATOM   7019  N  N     . SER B 1 178 ? 119.291 147.799 127.070 1.00 19.01 ?  178 SER B N     1 
ATOM   7020  C  CA    . SER B 1 178 ? 119.991 148.057 125.822 1.00 18.37 ?  178 SER B CA    1 
ATOM   7021  C  C     . SER B 1 178 ? 121.271 147.235 125.793 1.00 16.76 ?  178 SER B C     1 
ATOM   7022  O  O     . SER B 1 178 ? 121.810 146.870 126.840 1.00 23.35 ?  178 SER B O     1 
ATOM   7023  C  CB    . SER B 1 178 ? 120.309 149.547 125.646 1.00 14.28 ?  178 SER B CB    1 
ATOM   7024  O  OG    . SER B 1 178 ? 121.580 149.866 126.175 1.00 19.63 ?  178 SER B OG    1 
ATOM   7025  N  N     . LEU B 1 179 ? 121.742 146.941 124.580 1.00 23.99 ?  179 LEU B N     1 
ATOM   7026  C  CA    . LEU B 1 179 ? 122.993 146.202 124.432 1.00 19.15 ?  179 LEU B CA    1 
ATOM   7027  C  C     . LEU B 1 179 ? 124.173 147.008 124.957 1.00 14.42 ?  179 LEU B C     1 
ATOM   7028  O  O     . LEU B 1 179 ? 125.084 146.452 125.582 1.00 18.64 ?  179 LEU B O     1 
ATOM   7029  C  CB    . LEU B 1 179 ? 123.215 145.824 122.968 1.00 20.55 ?  179 LEU B CB    1 
ATOM   7030  C  CG    . LEU B 1 179 ? 124.441 144.951 122.694 1.00 17.53 ?  179 LEU B CG    1 
ATOM   7031  C  CD1   . LEU B 1 179 ? 124.290 143.593 123.366 1.00 14.12 ?  179 LEU B CD1   1 
ATOM   7032  C  CD2   . LEU B 1 179 ? 124.673 144.798 121.203 1.00 15.45 ?  179 LEU B CD2   1 
ATOM   7033  N  N     . ASN B 1 180 ? 124.182 148.318 124.700 1.00 18.45 ?  180 ASN B N     1 
ATOM   7034  C  CA    . ASN B 1 180 ? 125.239 149.169 125.235 1.00 19.17 ?  180 ASN B CA    1 
ATOM   7035  C  C     . ASN B 1 180 ? 125.245 149.137 126.756 1.00 19.71 ?  180 ASN B C     1 
ATOM   7036  O  O     . ASN B 1 180 ? 126.306 149.011 127.380 1.00 23.44 ?  180 ASN B O     1 
ATOM   7037  C  CB    . ASN B 1 180 ? 125.062 150.603 124.734 1.00 18.93 ?  180 ASN B CB    1 
ATOM   7038  C  CG    . ASN B 1 180 ? 125.553 150.790 123.316 1.00 24.64 ?  180 ASN B CG    1 
ATOM   7039  O  OD1   . ASN B 1 180 ? 126.370 150.015 122.821 1.00 31.55 ?  180 ASN B OD1   1 
ATOM   7040  N  ND2   . ASN B 1 180 ? 125.052 151.823 122.650 1.00 25.83 ?  180 ASN B ND2   1 
ATOM   7041  N  N     . ASP B 1 181 ? 124.064 149.231 127.368 1.00 19.83 ?  181 ASP B N     1 
ATOM   7042  C  CA    . ASP B 1 181 ? 123.973 149.202 128.822 1.00 15.41 ?  181 ASP B CA    1 
ATOM   7043  C  C     . ASP B 1 181 ? 124.347 147.834 129.376 1.00 14.51 ?  181 ASP B C     1 
ATOM   7044  O  O     . ASP B 1 181 ? 124.976 147.743 130.433 1.00 25.19 ?  181 ASP B O     1 
ATOM   7045  C  CB    . ASP B 1 181 ? 122.568 149.603 129.263 1.00 21.97 ?  181 ASP B CB    1 
ATOM   7046  C  CG    . ASP B 1 181 ? 122.273 151.066 129.000 1.00 24.91 ?  181 ASP B CG    1 
ATOM   7047  O  OD1   . ASP B 1 181 ? 122.870 151.924 129.683 1.00 24.60 ?  181 ASP B OD1   1 
ATOM   7048  O  OD2   . ASP B 1 181 ? 121.445 151.360 128.114 1.00 29.14 -1 181 ASP B OD2   1 
ATOM   7049  N  N     . ILE B 1 182 ? 123.975 146.759 128.678 1.00 15.82 ?  182 ILE B N     1 
ATOM   7050  C  CA    . ILE B 1 182 ? 124.336 145.417 129.130 1.00 17.64 ?  182 ILE B CA    1 
ATOM   7051  C  C     . ILE B 1 182 ? 125.849 145.227 129.088 1.00 17.43 ?  182 ILE B C     1 
ATOM   7052  O  O     . ILE B 1 182 ? 126.454 144.700 130.030 1.00 21.16 ?  182 ILE B O     1 
ATOM   7053  C  CB    . ILE B 1 182 ? 123.609 144.356 128.283 1.00 18.63 ?  182 ILE B CB    1 
ATOM   7054  C  CG1   . ILE B 1 182 ? 122.159 144.211 128.744 1.00 15.17 ?  182 ILE B CG1   1 
ATOM   7055  C  CG2   . ILE B 1 182 ? 124.325 143.017 128.359 1.00 20.80 ?  182 ILE B CG2   1 
ATOM   7056  C  CD1   . ILE B 1 182 ? 121.291 143.452 127.776 1.00 16.89 ?  182 ILE B CD1   1 
ATOM   7057  N  N     . SER B 1 183 ? 126.482 145.654 127.993 1.00 17.86 ?  183 SER B N     1 
ATOM   7058  C  CA    . SER B 1 183 ? 127.932 145.539 127.884 1.00 18.73 ?  183 SER B CA    1 
ATOM   7059  C  C     . SER B 1 183 ? 128.634 146.400 128.926 1.00 21.57 ?  183 SER B C     1 
ATOM   7060  O  O     . SER B 1 183 ? 129.633 145.975 129.519 1.00 28.03 ?  183 SER B O     1 
ATOM   7061  C  CB    . SER B 1 183 ? 128.380 145.919 126.475 1.00 15.98 ?  183 SER B CB    1 
ATOM   7062  O  OG    . SER B 1 183 ? 127.978 147.237 126.153 1.00 30.83 ?  183 SER B OG    1 
ATOM   7063  N  N     . ARG B 1 184 ? 128.124 147.611 129.167 1.00 18.88 ?  184 ARG B N     1 
ATOM   7064  C  CA    . ARG B 1 184 ? 128.705 148.455 130.203 1.00 16.57 ?  184 ARG B CA    1 
ATOM   7065  C  C     . ARG B 1 184 ? 128.538 147.831 131.582 1.00 25.25 ?  184 ARG B C     1 
ATOM   7066  O  O     . ARG B 1 184 ? 129.433 147.932 132.425 1.00 29.17 ?  184 ARG B O     1 
ATOM   7067  C  CB    . ARG B 1 184 ? 128.078 149.847 130.167 1.00 15.37 ?  184 ARG B CB    1 
ATOM   7068  C  CG    . ARG B 1 184 ? 128.812 150.861 131.025 1.00 24.71 ?  184 ARG B CG    1 
ATOM   7069  C  CD    . ARG B 1 184 ? 130.278 150.944 130.644 1.00 24.41 ?  184 ARG B CD    1 
ATOM   7070  N  NE    . ARG B 1 184 ? 130.489 151.810 129.491 1.00 31.42 ?  184 ARG B NE    1 
ATOM   7071  C  CZ    . ARG B 1 184 ? 131.680 152.164 129.028 1.00 33.23 ?  184 ARG B CZ    1 
ATOM   7072  N  NH1   . ARG B 1 184 ? 132.795 151.724 129.585 1.00 27.36 1  184 ARG B NH1   1 
ATOM   7073  N  NH2   . ARG B 1 184 ? 131.751 152.978 127.979 1.00 28.64 ?  184 ARG B NH2   1 
ATOM   7074  N  N     . ALA B 1 185 ? 127.396 147.189 131.833 1.00 22.10 ?  185 ALA B N     1 
ATOM   7075  C  CA    . ALA B 1 185 ? 127.189 146.515 133.108 1.00 11.35 ?  185 ALA B CA    1 
ATOM   7076  C  C     . ALA B 1 185 ? 128.165 145.361 133.284 1.00 15.81 ?  185 ALA B C     1 
ATOM   7077  O  O     . ALA B 1 185 ? 128.702 145.157 134.376 1.00 20.15 ?  185 ALA B O     1 
ATOM   7078  C  CB    . ALA B 1 185 ? 125.748 146.018 133.214 1.00 15.68 ?  185 ALA B CB    1 
ATOM   7079  N  N     . ILE B 1 186 ? 128.404 144.595 132.217 1.00 24.17 ?  186 ILE B N     1 
ATOM   7080  C  CA    . ILE B 1 186 ? 129.390 143.517 132.285 1.00 21.97 ?  186 ILE B CA    1 
ATOM   7081  C  C     . ILE B 1 186 ? 130.775 144.082 132.580 1.00 20.56 ?  186 ILE B C     1 
ATOM   7082  O  O     . ILE B 1 186 ? 131.516 143.555 133.424 1.00 26.55 ?  186 ILE B O     1 
ATOM   7083  C  CB    . ILE B 1 186 ? 129.379 142.701 130.979 1.00 26.98 ?  186 ILE B CB    1 
ATOM   7084  C  CG1   . ILE B 1 186 ? 128.049 141.968 130.812 1.00 20.24 ?  186 ILE B CG1   1 
ATOM   7085  C  CG2   . ILE B 1 186 ? 130.534 141.715 130.951 1.00 22.94 ?  186 ILE B CG2   1 
ATOM   7086  C  CD1   . ILE B 1 186 ? 127.740 141.605 129.379 1.00 23.18 ?  186 ILE B CD1   1 
ATOM   7087  N  N     . ASP B 1 187 ? 131.143 145.165 131.891 1.00 22.65 ?  187 ASP B N     1 
ATOM   7088  C  CA    . ASP B 1 187 ? 132.446 145.785 132.111 1.00 21.24 ?  187 ASP B CA    1 
ATOM   7089  C  C     . ASP B 1 187 ? 132.589 146.277 133.547 1.00 23.70 ?  187 ASP B C     1 
ATOM   7090  O  O     . ASP B 1 187 ? 133.613 146.043 134.196 1.00 29.52 ?  187 ASP B O     1 
ATOM   7091  C  CB    . ASP B 1 187 ? 132.644 146.937 131.126 1.00 21.82 ?  187 ASP B CB    1 
ATOM   7092  C  CG    . ASP B 1 187 ? 133.762 147.874 131.538 1.00 30.86 ?  187 ASP B CG    1 
ATOM   7093  O  OD1   . ASP B 1 187 ? 134.889 147.392 131.778 1.00 30.90 ?  187 ASP B OD1   1 
ATOM   7094  O  OD2   . ASP B 1 187 ? 133.514 149.094 131.624 1.00 35.86 -1 187 ASP B OD2   1 
ATOM   7095  N  N     . ILE B 1 188 ? 131.563 146.958 134.060 1.00 21.60 ?  188 ILE B N     1 
ATOM   7096  C  CA    . ILE B 1 188 ? 131.622 147.503 135.413 1.00 19.74 ?  188 ILE B CA    1 
ATOM   7097  C  C     . ILE B 1 188 ? 131.641 146.380 136.442 1.00 21.48 ?  188 ILE B C     1 
ATOM   7098  O  O     . ILE B 1 188 ? 132.309 146.483 137.476 1.00 28.68 ?  188 ILE B O     1 
ATOM   7099  C  CB    . ILE B 1 188 ? 130.450 148.475 135.646 1.00 21.13 ?  188 ILE B CB    1 
ATOM   7100  C  CG1   . ILE B 1 188 ? 130.576 149.692 134.729 1.00 22.43 ?  188 ILE B CG1   1 
ATOM   7101  C  CG2   . ILE B 1 188 ? 130.412 148.938 137.087 1.00 23.49 ?  188 ILE B CG2   1 
ATOM   7102  C  CD1   . ILE B 1 188 ? 129.348 150.571 134.713 1.00 18.85 ?  188 ILE B CD1   1 
ATOM   7103  N  N     . SER B 1 189 ? 130.913 145.292 136.180 1.00 17.21 ?  189 SER B N     1 
ATOM   7104  C  CA    . SER B 1 189 ? 130.949 144.147 137.079 1.00 10.40 ?  189 SER B CA    1 
ATOM   7105  C  C     . SER B 1 189 ? 132.344 143.543 137.140 1.00 22.08 ?  189 SER B C     1 
ATOM   7106  O  O     . SER B 1 189 ? 132.842 143.226 138.225 1.00 23.66 ?  189 SER B O     1 
ATOM   7107  C  CB    . SER B 1 189 ? 129.929 143.100 136.633 1.00 18.67 ?  189 SER B CB    1 
ATOM   7108  O  OG    . SER B 1 189 ? 128.633 143.659 136.545 1.00 25.30 ?  189 SER B OG    1 
ATOM   7109  N  N     . MET B 1 190 ? 132.995 143.384 135.984 1.00 27.49 ?  190 MET B N     1 
ATOM   7110  C  CA    . MET B 1 190 ? 134.366 142.881 135.987 1.00 19.93 ?  190 MET B CA    1 
ATOM   7111  C  C     . MET B 1 190 ? 135.307 143.841 136.704 1.00 19.96 ?  190 MET B C     1 
ATOM   7112  O  O     . MET B 1 190 ? 136.194 143.411 137.448 1.00 24.18 ?  190 MET B O     1 
ATOM   7113  C  CB    . MET B 1 190 ? 134.851 142.625 134.561 1.00 20.87 ?  190 MET B CB    1 
ATOM   7114  C  CG    . MET B 1 190 ? 134.116 141.514 133.842 1.00 22.70 ?  190 MET B CG    1 
ATOM   7115  S  SD    . MET B 1 190 ? 134.898 141.074 132.280 1.00 37.29 ?  190 MET B SD    1 
ATOM   7116  C  CE    . MET B 1 190 ? 134.141 142.258 131.171 1.00 24.55 ?  190 MET B CE    1 
ATOM   7117  N  N     . GLN B 1 191 ? 135.128 145.147 136.493 1.00 19.21 ?  191 GLN B N     1 
ATOM   7118  C  CA    . GLN B 1 191 ? 135.996 146.127 137.140 1.00 23.96 ?  191 GLN B CA    1 
ATOM   7119  C  C     . GLN B 1 191 ? 135.840 146.100 138.654 1.00 23.51 ?  191 GLN B C     1 
ATOM   7120  O  O     . GLN B 1 191 ? 136.830 146.183 139.390 1.00 29.80 ?  191 GLN B O     1 
ATOM   7121  C  CB    . GLN B 1 191 ? 135.705 147.528 136.603 1.00 21.47 ?  191 GLN B CB    1 
ATOM   7122  C  CG    . GLN B 1 191 ? 136.045 147.729 135.137 1.00 20.65 ?  191 GLN B CG    1 
ATOM   7123  C  CD    . GLN B 1 191 ? 137.525 147.586 134.851 1.00 26.80 ?  191 GLN B CD    1 
ATOM   7124  O  OE1   . GLN B 1 191 ? 138.362 147.761 135.736 1.00 30.50 ?  191 GLN B OE1   1 
ATOM   7125  N  NE2   . GLN B 1 191 ? 137.856 147.269 133.606 1.00 25.97 ?  191 GLN B NE2   1 
ATOM   7126  N  N     . LEU B 1 192 ? 134.604 145.989 139.141 1.00 23.86 ?  192 LEU B N     1 
ATOM   7127  C  CA    . LEU B 1 192 ? 134.367 146.002 140.579 1.00 18.39 ?  192 LEU B CA    1 
ATOM   7128  C  C     . LEU B 1 192 ? 134.728 144.678 141.237 1.00 22.39 ?  192 LEU B C     1 
ATOM   7129  O  O     . LEU B 1 192 ? 135.137 144.668 142.403 1.00 33.29 ?  192 LEU B O     1 
ATOM   7130  C  CB    . LEU B 1 192 ? 132.910 146.361 140.868 1.00 19.17 ?  192 LEU B CB    1 
ATOM   7131  C  CG    . LEU B 1 192 ? 132.491 147.785 140.498 1.00 20.72 ?  192 LEU B CG    1 
ATOM   7132  C  CD1   . LEU B 1 192 ? 130.981 147.923 140.527 1.00 20.16 ?  192 LEU B CD1   1 
ATOM   7133  C  CD2   . LEU B 1 192 ? 133.146 148.798 141.423 1.00 21.42 ?  192 LEU B CD2   1 
ATOM   7134  N  N     . SER B 1 193 ? 134.581 143.556 140.527 1.00 19.80 ?  193 SER B N     1 
ATOM   7135  C  CA    . SER B 1 193 ? 135.080 142.291 141.051 1.00 22.09 ?  193 SER B CA    1 
ATOM   7136  C  C     . SER B 1 193 ? 136.600 142.265 141.070 1.00 27.73 ?  193 SER B C     1 
ATOM   7137  O  O     . SER B 1 193 ? 137.200 141.632 141.945 1.00 36.62 ?  193 SER B O     1 
ATOM   7138  C  CB    . SER B 1 193 ? 134.537 141.128 140.228 1.00 24.90 ?  193 SER B CB    1 
ATOM   7139  O  OG    . SER B 1 193 ? 133.131 141.054 140.343 1.00 35.01 ?  193 SER B OG    1 
ATOM   7140  N  N     . LYS B 1 194 ? 137.232 142.938 140.108 1.00 29.29 ?  194 LYS B N     1 
ATOM   7141  C  CA    . LYS B 1 194 ? 138.674 143.134 140.157 1.00 29.16 ?  194 LYS B CA    1 
ATOM   7142  C  C     . LYS B 1 194 ? 139.070 143.921 141.399 1.00 35.14 ?  194 LYS B C     1 
ATOM   7143  O  O     . LYS B 1 194 ? 140.081 143.617 142.043 1.00 39.81 ?  194 LYS B O     1 
ATOM   7144  C  CB    . LYS B 1 194 ? 139.136 143.844 138.885 1.00 26.06 ?  194 LYS B CB    1 
ATOM   7145  C  CG    . LYS B 1 194 ? 140.527 144.433 138.945 1.00 33.46 ?  194 LYS B CG    1 
ATOM   7146  C  CD    . LYS B 1 194 ? 140.766 145.351 137.760 1.00 33.37 ?  194 LYS B CD    1 
ATOM   7147  C  CE    . LYS B 1 194 ? 142.220 145.776 137.668 1.00 34.95 ?  194 LYS B CE    1 
ATOM   7148  N  NZ    . LYS B 1 194 ? 142.451 146.712 136.533 1.00 35.12 1  194 LYS B NZ    1 
ATOM   7149  N  N     . LEU B 1 195 ? 138.276 144.933 141.756 1.00 30.45 ?  195 LEU B N     1 
ATOM   7150  C  CA    . LEU B 1 195 ? 138.498 145.689 142.980 1.00 29.84 ?  195 LEU B CA    1 
ATOM   7151  C  C     . LEU B 1 195 ? 138.155 144.897 144.234 1.00 31.64 ?  195 LEU B C     1 
ATOM   7152  O  O     . LEU B 1 195 ? 138.456 145.360 145.340 1.00 35.04 ?  195 LEU B O     1 
ATOM   7153  C  CB    . LEU B 1 195 ? 137.685 146.984 142.944 1.00 31.01 ?  195 LEU B CB    1 
ATOM   7154  C  CG    . LEU B 1 195 ? 138.091 147.976 141.852 1.00 32.60 ?  195 LEU B CG    1 
ATOM   7155  C  CD1   . LEU B 1 195 ? 137.133 149.154 141.802 1.00 32.68 ?  195 LEU B CD1   1 
ATOM   7156  C  CD2   . LEU B 1 195 ? 139.522 148.450 142.065 1.00 30.72 ?  195 LEU B CD2   1 
ATOM   7157  N  N     . GLY B 1 196 ? 137.530 143.727 144.096 1.00 31.68 ?  196 GLY B N     1 
ATOM   7158  C  CA    . GLY B 1 196 ? 137.250 142.856 145.214 1.00 32.64 ?  196 GLY B CA    1 
ATOM   7159  C  C     . GLY B 1 196 ? 135.841 142.938 145.764 1.00 33.71 ?  196 GLY B C     1 
ATOM   7160  O  O     . GLY B 1 196 ? 135.501 142.156 146.661 1.00 35.13 ?  196 GLY B O     1 
ATOM   7161  N  N     . GLY B 1 197 ? 135.015 143.849 145.260 1.00 30.62 ?  197 GLY B N     1 
ATOM   7162  C  CA    . GLY B 1 197 ? 133.689 144.025 145.814 1.00 26.25 ?  197 GLY B CA    1 
ATOM   7163  C  C     . GLY B 1 197 ? 132.652 143.128 145.166 1.00 22.65 ?  197 GLY B C     1 
ATOM   7164  O  O     . GLY B 1 197 ? 132.732 142.782 143.989 1.00 27.65 ?  197 GLY B O     1 
ATOM   7165  N  N     . GLY B 1 198 ? 131.655 142.747 145.964 1.00 19.98 ?  198 GLY B N     1 
ATOM   7166  C  CA    . GLY B 1 198 ? 130.529 141.990 145.448 1.00 16.72 ?  198 GLY B CA    1 
ATOM   7167  C  C     . GLY B 1 198 ? 129.585 142.905 144.692 1.00 17.83 ?  198 GLY B C     1 
ATOM   7168  O  O     . GLY B 1 198 ? 129.217 143.979 145.179 1.00 21.91 ?  198 GLY B O     1 
ATOM   7169  N  N     . VAL B 1 199 ? 129.189 142.481 143.496 1.00 20.11 ?  199 VAL B N     1 
ATOM   7170  C  CA    . VAL B 1 199 ? 128.413 143.306 142.579 1.00 12.78 ?  199 VAL B CA    1 
ATOM   7171  C  C     . VAL B 1 199 ? 127.012 142.726 142.460 1.00 7.15  ?  199 VAL B C     1 
ATOM   7172  O  O     . VAL B 1 199 ? 126.849 141.526 142.219 1.00 15.02 ?  199 VAL B O     1 
ATOM   7173  C  CB    . VAL B 1 199 ? 129.084 143.395 141.198 1.00 13.70 ?  199 VAL B CB    1 
ATOM   7174  C  CG1   . VAL B 1 199 ? 128.340 144.371 140.308 1.00 16.53 ?  199 VAL B CG1   1 
ATOM   7175  C  CG2   . VAL B 1 199 ? 130.539 143.791 141.343 1.00 11.69 ?  199 VAL B CG2   1 
ATOM   7176  N  N     . SER B 1 200 ? 126.006 143.578 142.629 1.00 13.20 ?  200 SER B N     1 
ATOM   7177  C  CA    . SER B 1 200 ? 124.612 143.214 142.435 1.00 3.98  ?  200 SER B CA    1 
ATOM   7178  C  C     . SER B 1 200 ? 124.047 144.019 141.274 1.00 13.16 ?  200 SER B C     1 
ATOM   7179  O  O     . SER B 1 200 ? 124.282 145.226 141.172 1.00 23.38 ?  200 SER B O     1 
ATOM   7180  C  CB    . SER B 1 200 ? 123.791 143.465 143.701 1.00 10.36 ?  200 SER B CB    1 
ATOM   7181  O  OG    . SER B 1 200 ? 122.557 142.774 143.654 1.00 15.93 ?  200 SER B OG    1 
ATOM   7182  N  N     . LEU B 1 201 ? 123.308 143.348 140.396 1.00 15.98 ?  201 LEU B N     1 
ATOM   7183  C  CA    . LEU B 1 201 ? 122.758 143.968 139.200 1.00 8.21  ?  201 LEU B CA    1 
ATOM   7184  C  C     . LEU B 1 201 ? 121.254 143.758 139.154 1.00 7.83  ?  201 LEU B C     1 
ATOM   7185  O  O     . LEU B 1 201 ? 120.775 142.631 139.315 1.00 14.96 ?  201 LEU B O     1 
ATOM   7186  C  CB    . LEU B 1 201 ? 123.408 143.399 137.937 1.00 14.50 ?  201 LEU B CB    1 
ATOM   7187  C  CG    . LEU B 1 201 ? 124.929 143.524 137.864 1.00 19.27 ?  201 LEU B CG    1 
ATOM   7188  C  CD1   . LEU B 1 201 ? 125.590 142.176 138.106 1.00 16.44 ?  201 LEU B CD1   1 
ATOM   7189  C  CD2   . LEU B 1 201 ? 125.353 144.107 136.527 1.00 17.08 ?  201 LEU B CD2   1 
ATOM   7190  N  N     . ASN B 1 202 ? 120.519 144.841 138.924 1.00 13.30 ?  202 ASN B N     1 
ATOM   7191  C  CA    . ASN B 1 202 ? 119.072 144.789 138.758 1.00 4.34  ?  202 ASN B CA    1 
ATOM   7192  C  C     . ASN B 1 202 ? 118.770 144.513 137.290 1.00 19.44 ?  202 ASN B C     1 
ATOM   7193  O  O     . ASN B 1 202 ? 119.042 145.350 136.425 1.00 25.78 ?  202 ASN B O     1 
ATOM   7194  C  CB    . ASN B 1 202 ? 118.428 146.093 139.217 1.00 8.57  ?  202 ASN B CB    1 
ATOM   7195  C  CG    . ASN B 1 202 ? 116.938 145.959 139.445 1.00 9.79  ?  202 ASN B CG    1 
ATOM   7196  O  OD1   . ASN B 1 202 ? 116.429 144.863 139.670 1.00 17.92 ?  202 ASN B OD1   1 
ATOM   7197  N  ND2   . ASN B 1 202 ? 116.227 147.079 139.387 1.00 12.16 ?  202 ASN B ND2   1 
ATOM   7198  N  N     . LEU B 1 203 ? 118.208 143.340 137.011 1.00 12.94 ?  203 LEU B N     1 
ATOM   7199  C  CA    . LEU B 1 203 ? 117.880 142.936 135.652 1.00 9.62  ?  203 LEU B CA    1 
ATOM   7200  C  C     . LEU B 1 203 ? 116.407 143.129 135.324 1.00 12.21 ?  203 LEU B C     1 
ATOM   7201  O  O     . LEU B 1 203 ? 115.943 142.634 134.292 1.00 17.15 ?  203 LEU B O     1 
ATOM   7202  C  CB    . LEU B 1 203 ? 118.281 141.477 135.428 1.00 15.46 ?  203 LEU B CB    1 
ATOM   7203  C  CG    . LEU B 1 203 ? 119.736 141.118 135.739 1.00 15.40 ?  203 LEU B CG    1 
ATOM   7204  C  CD1   . LEU B 1 203 ? 120.055 139.718 135.248 1.00 14.42 ?  203 LEU B CD1   1 
ATOM   7205  C  CD2   . LEU B 1 203 ? 120.690 142.130 135.128 1.00 15.77 ?  203 LEU B CD2   1 
ATOM   7206  N  N     . SER B 1 204 ? 115.663 143.842 136.173 1.00 15.54 ?  204 SER B N     1 
ATOM   7207  C  CA    . SER B 1 204 ? 114.228 143.994 135.976 1.00 10.71 ?  204 SER B CA    1 
ATOM   7208  C  C     . SER B 1 204 ? 113.882 144.920 134.818 1.00 20.34 ?  204 SER B C     1 
ATOM   7209  O  O     . SER B 1 204 ? 112.784 144.807 134.262 1.00 23.52 ?  204 SER B O     1 
ATOM   7210  C  CB    . SER B 1 204 ? 113.576 144.515 137.257 1.00 8.35  ?  204 SER B CB    1 
ATOM   7211  O  OG    . SER B 1 204 ? 113.865 143.666 138.353 1.00 20.64 ?  204 SER B OG    1 
ATOM   7212  N  N     . LYS B 1 205 ? 114.782 145.829 134.446 1.00 22.11 ?  205 LYS B N     1 
ATOM   7213  C  CA    . LYS B 1 205 ? 114.530 146.703 133.309 1.00 16.32 ?  205 LYS B CA    1 
ATOM   7214  C  C     . LYS B 1 205 ? 114.772 146.013 131.976 1.00 15.37 ?  205 LYS B C     1 
ATOM   7215  O  O     . LYS B 1 205 ? 114.184 146.423 130.970 1.00 26.69 ?  205 LYS B O     1 
ATOM   7216  C  CB    . LYS B 1 205 ? 115.396 147.959 133.405 1.00 18.23 ?  205 LYS B CB    1 
ATOM   7217  C  CG    . LYS B 1 205 ? 114.967 148.908 134.506 1.00 15.88 ?  205 LYS B CG    1 
ATOM   7218  C  CD    . LYS B 1 205 ? 115.811 150.165 134.513 1.00 21.18 ?  205 LYS B CD    1 
ATOM   7219  C  CE    . LYS B 1 205 ? 115.198 151.226 135.408 1.00 24.74 ?  205 LYS B CE    1 
ATOM   7220  N  NZ    . LYS B 1 205 ? 115.081 150.765 136.818 1.00 17.90 1  205 LYS B NZ    1 
ATOM   7221  N  N     . LEU B 1 206 ? 115.616 144.986 131.946 1.00 19.58 ?  206 LEU B N     1 
ATOM   7222  C  CA    . LEU B 1 206 ? 115.856 144.244 130.716 1.00 19.72 ?  206 LEU B CA    1 
ATOM   7223  C  C     . LEU B 1 206 ? 114.578 143.563 130.253 1.00 20.06 ?  206 LEU B C     1 
ATOM   7224  O  O     . LEU B 1 206 ? 113.868 142.940 131.049 1.00 24.64 ?  206 LEU B O     1 
ATOM   7225  C  CB    . LEU B 1 206 ? 116.956 143.209 130.932 1.00 19.51 ?  206 LEU B CB    1 
ATOM   7226  C  CG    . LEU B 1 206 ? 118.285 143.737 131.467 1.00 18.70 ?  206 LEU B CG    1 
ATOM   7227  C  CD1   . LEU B 1 206 ? 119.222 142.586 131.766 1.00 19.93 ?  206 LEU B CD1   1 
ATOM   7228  C  CD2   . LEU B 1 206 ? 118.908 144.694 130.473 1.00 22.12 ?  206 LEU B CD2   1 
ATOM   7229  N  N     . ARG B 1 207 ? 114.284 143.679 128.962 1.00 26.04 ?  207 ARG B N     1 
ATOM   7230  C  CA    . ARG B 1 207 ? 113.073 143.077 128.430 1.00 23.84 ?  207 ARG B CA    1 
ATOM   7231  C  C     . ARG B 1 207 ? 113.188 141.557 128.418 1.00 25.07 ?  207 ARG B C     1 
ATOM   7232  O  O     . ARG B 1 207 ? 114.277 140.991 128.294 1.00 30.59 ?  207 ARG B O     1 
ATOM   7233  C  CB    . ARG B 1 207 ? 112.779 143.605 127.026 1.00 22.30 ?  207 ARG B CB    1 
ATOM   7234  C  CG    . ARG B 1 207 ? 113.880 143.405 126.007 1.00 26.52 ?  207 ARG B CG    1 
ATOM   7235  C  CD    . ARG B 1 207 ? 113.562 144.174 124.736 1.00 24.61 ?  207 ARG B CD    1 
ATOM   7236  N  NE    . ARG B 1 207 ? 113.958 145.574 124.827 1.00 25.92 ?  207 ARG B NE    1 
ATOM   7237  C  CZ    . ARG B 1 207 ? 114.218 146.348 123.783 1.00 23.22 ?  207 ARG B CZ    1 
ATOM   7238  N  NH1   . ARG B 1 207 ? 114.117 145.895 122.544 1.00 26.34 1  207 ARG B NH1   1 
ATOM   7239  N  NH2   . ARG B 1 207 ? 114.589 147.608 123.986 1.00 20.80 ?  207 ARG B NH2   1 
ATOM   7240  N  N     . ALA B 1 208 ? 112.041 140.899 128.554 1.00 29.42 ?  208 ALA B N     1 
ATOM   7241  C  CA    . ALA B 1 208 ? 112.004 139.458 128.733 1.00 21.81 ?  208 ALA B CA    1 
ATOM   7242  C  C     . ALA B 1 208 ? 112.322 138.735 127.426 1.00 28.96 ?  208 ALA B C     1 
ATOM   7243  O  O     . ALA B 1 208 ? 112.525 139.341 126.372 1.00 34.82 ?  208 ALA B O     1 
ATOM   7244  C  CB    . ALA B 1 208 ? 110.640 139.024 129.260 1.00 23.95 ?  208 ALA B CB    1 
ATOM   7245  N  N     . LYS B 1 209 ? 112.374 137.409 127.516 1.00 28.19 ?  209 LYS B N     1 
ATOM   7246  C  CA    . LYS B 1 209 ? 112.605 136.582 126.342 1.00 24.45 ?  209 LYS B CA    1 
ATOM   7247  C  C     . LYS B 1 209 ? 111.418 136.670 125.392 1.00 31.93 ?  209 LYS B C     1 
ATOM   7248  O  O     . LYS B 1 209 ? 110.260 136.698 125.817 1.00 34.54 ?  209 LYS B O     1 
ATOM   7249  C  CB    . LYS B 1 209 ? 112.846 135.131 126.754 1.00 27.07 ?  209 LYS B CB    1 
ATOM   7250  C  CG    . LYS B 1 209 ? 113.453 134.268 125.662 1.00 32.28 ?  209 LYS B CG    1 
ATOM   7251  C  CD    . LYS B 1 209 ? 114.078 133.009 126.237 1.00 29.21 ?  209 LYS B CD    1 
ATOM   7252  C  CE    . LYS B 1 209 ? 113.019 132.015 126.684 1.00 32.67 ?  209 LYS B CE    1 
ATOM   7253  N  NZ    . LYS B 1 209 ? 111.825 132.036 125.794 1.00 33.89 1  209 LYS B NZ    1 
ATOM   7254  N  N     . GLY B 1 210 ? 111.713 136.714 124.096 1.00 35.25 ?  210 GLY B N     1 
ATOM   7255  C  CA    . GLY B 1 210 ? 110.667 136.822 123.101 1.00 34.69 ?  210 GLY B CA    1 
ATOM   7256  C  C     . GLY B 1 210 ? 110.161 138.225 122.862 1.00 35.24 ?  210 GLY B C     1 
ATOM   7257  O  O     . GLY B 1 210 ? 109.018 138.396 122.426 1.00 38.95 ?  210 GLY B O     1 
ATOM   7258  N  N     . GLU B 1 211 ? 110.975 139.237 123.137 1.00 33.78 ?  211 GLU B N     1 
ATOM   7259  C  CA    . GLU B 1 211 ? 110.620 140.619 122.861 1.00 33.10 ?  211 GLU B CA    1 
ATOM   7260  C  C     . GLU B 1 211 ? 111.313 141.097 121.588 1.00 37.21 ?  211 GLU B C     1 
ATOM   7261  O  O     . GLU B 1 211 ? 112.193 140.432 121.037 1.00 40.01 ?  211 GLU B O     1 
ATOM   7262  C  CB    . GLU B 1 211 ? 110.978 141.519 124.047 1.00 31.64 ?  211 GLU B CB    1 
ATOM   7263  C  CG    . GLU B 1 211 ? 110.185 141.212 125.302 1.00 33.93 ?  211 GLU B CG    1 
ATOM   7264  C  CD    . GLU B 1 211 ? 109.418 142.412 125.818 1.00 36.00 ?  211 GLU B CD    1 
ATOM   7265  O  OE1   . GLU B 1 211 ? 108.538 142.913 125.089 1.00 39.65 ?  211 GLU B OE1   1 
ATOM   7266  O  OE2   . GLU B 1 211 ? 109.684 142.847 126.957 1.00 32.33 -1 211 GLU B OE2   1 
ATOM   7267  N  N     . ALA B 1 212 ? 110.902 142.272 121.125 1.00 38.34 ?  212 ALA B N     1 
ATOM   7268  C  CA    . ALA B 1 212 ? 111.341 142.793 119.838 1.00 35.63 ?  212 ALA B CA    1 
ATOM   7269  C  C     . ALA B 1 212 ? 112.522 143.740 120.010 1.00 41.57 ?  212 ALA B C     1 
ATOM   7270  O  O     . ALA B 1 212 ? 112.501 144.621 120.874 1.00 44.34 ?  212 ALA B O     1 
ATOM   7271  C  CB    . ALA B 1 212 ? 110.191 143.510 119.132 1.00 38.46 ?  212 ALA B CB    1 
ATOM   7272  N  N     . ILE B 1 213 ? 113.549 143.547 119.187 1.00 40.74 ?  213 ILE B N     1 
ATOM   7273  C  CA    . ILE B 1 213 ? 114.676 144.467 119.090 1.00 43.49 ?  213 ILE B CA    1 
ATOM   7274  C  C     . ILE B 1 213 ? 114.525 145.207 117.766 1.00 41.50 ?  213 ILE B C     1 
ATOM   7275  O  O     . ILE B 1 213 ? 114.984 144.733 116.725 1.00 44.98 ?  213 ILE B O     1 
ATOM   7276  C  CB    . ILE B 1 213 ? 116.019 143.738 119.180 1.00 41.22 ?  213 ILE B CB    1 
ATOM   7277  C  CG1   . ILE B 1 213 ? 116.054 142.830 120.406 1.00 41.47 ?  213 ILE B CG1   1 
ATOM   7278  C  CG2   . ILE B 1 213 ? 117.165 144.737 119.219 1.00 38.15 ?  213 ILE B CG2   1 
ATOM   7279  C  CD1   . ILE B 1 213 ? 117.024 141.682 120.283 1.00 41.34 ?  213 ILE B CD1   1 
ATOM   7280  N  N     . LYS B 1 214 ? 113.890 146.376 117.809 1.00 46.02 ?  214 LYS B N     1 
ATOM   7281  C  CA    . LYS B 1 214 ? 113.615 147.188 116.623 1.00 46.63 ?  214 LYS B CA    1 
ATOM   7282  C  C     . LYS B 1 214 ? 112.774 146.419 115.602 1.00 52.94 ?  214 LYS B C     1 
ATOM   7283  O  O     . LYS B 1 214 ? 113.218 146.093 114.499 1.00 55.44 ?  214 LYS B O     1 
ATOM   7284  C  CB    . LYS B 1 214 ? 114.909 147.706 115.991 1.00 48.06 ?  214 LYS B CB    1 
ATOM   7285  C  CG    . LYS B 1 214 ? 115.223 149.152 116.336 1.00 49.74 ?  214 LYS B CG    1 
ATOM   7286  C  CD    . LYS B 1 214 ? 116.717 149.424 116.324 1.00 49.95 ?  214 LYS B CD    1 
ATOM   7287  C  CE    . LYS B 1 214 ? 117.421 148.654 115.217 1.00 48.13 ?  214 LYS B CE    1 
ATOM   7288  N  NZ    . LYS B 1 214 ? 118.867 148.458 115.508 1.00 51.60 1  214 LYS B NZ    1 
ATOM   7289  N  N     . ASP B 1 215 ? 111.547 146.099 116.022 1.00 54.72 ?  215 ASP B N     1 
ATOM   7290  C  CA    . ASP B 1 215 ? 110.466 145.663 115.141 1.00 56.27 ?  215 ASP B CA    1 
ATOM   7291  C  C     . ASP B 1 215 ? 110.615 144.230 114.635 1.00 55.86 ?  215 ASP B C     1 
ATOM   7292  O  O     . ASP B 1 215 ? 109.732 143.735 113.928 1.00 57.90 ?  215 ASP B O     1 
ATOM   7293  C  CB    . ASP B 1 215 ? 110.330 146.620 113.951 1.00 56.75 ?  215 ASP B CB    1 
ATOM   7294  C  CG    . ASP B 1 215 ? 109.540 147.867 114.295 1.00 58.77 ?  215 ASP B CG    1 
ATOM   7295  O  OD1   . ASP B 1 215 ? 108.312 147.757 114.497 1.00 57.83 ?  215 ASP B OD1   1 
ATOM   7296  O  OD2   . ASP B 1 215 ? 110.147 148.956 114.365 1.00 57.94 -1 215 ASP B OD2   1 
ATOM   7297  N  N     . VAL B 1 216 ? 111.706 143.550 114.982 1.00 49.80 ?  216 VAL B N     1 
ATOM   7298  C  CA    . VAL B 1 216 ? 111.816 142.118 114.707 1.00 49.24 ?  216 VAL B CA    1 
ATOM   7299  C  C     . VAL B 1 216 ? 111.495 141.400 116.016 1.00 51.37 ?  216 VAL B C     1 
ATOM   7300  O  O     . VAL B 1 216 ? 112.164 141.599 117.032 1.00 54.49 ?  216 VAL B O     1 
ATOM   7301  C  CB    . VAL B 1 216 ? 113.191 141.732 114.151 1.00 49.43 ?  216 VAL B CB    1 
ATOM   7302  C  CG1   . VAL B 1 216 ? 114.212 142.818 114.422 1.00 48.26 ?  216 VAL B CG1   1 
ATOM   7303  C  CG2   . VAL B 1 216 ? 113.656 140.377 114.687 1.00 49.08 ?  216 VAL B CG2   1 
ATOM   7304  N  N     . GLU B 1 217 ? 110.444 140.584 116.001 1.00 49.49 ?  217 GLU B N     1 
ATOM   7305  C  CA    . GLU B 1 217 ? 109.879 140.052 117.231 1.00 48.12 ?  217 GLU B CA    1 
ATOM   7306  C  C     . GLU B 1 217 ? 110.542 138.729 117.611 1.00 47.97 ?  217 GLU B C     1 
ATOM   7307  O  O     . GLU B 1 217 ? 111.217 138.080 116.807 1.00 49.55 ?  217 GLU B O     1 
ATOM   7308  C  CB    . GLU B 1 217 ? 108.370 139.867 117.083 1.00 49.89 ?  217 GLU B CB    1 
ATOM   7309  C  CG    . GLU B 1 217 ? 107.660 141.070 116.486 1.00 50.43 ?  217 GLU B CG    1 
ATOM   7310  C  CD    . GLU B 1 217 ? 107.354 142.137 117.516 1.00 53.17 ?  217 GLU B CD    1 
ATOM   7311  O  OE1   . GLU B 1 217 ? 107.334 141.812 118.722 1.00 52.28 ?  217 GLU B OE1   1 
ATOM   7312  O  OE2   . GLU B 1 217 ? 107.137 143.302 117.122 1.00 49.00 -1 217 GLU B OE2   1 
ATOM   7313  N  N     . ASN B 1 218 ? 110.326 138.334 118.865 1.00 43.64 ?  218 ASN B N     1 
ATOM   7314  C  CA    . ASN B 1 218 ? 110.865 137.096 119.427 1.00 41.92 ?  218 ASN B CA    1 
ATOM   7315  C  C     . ASN B 1 218 ? 112.374 137.017 119.225 1.00 45.22 ?  218 ASN B C     1 
ATOM   7316  O  O     . ASN B 1 218 ? 112.930 135.991 118.826 1.00 46.74 ?  218 ASN B O     1 
ATOM   7317  C  CB    . ASN B 1 218 ? 110.164 135.875 118.836 1.00 43.14 ?  218 ASN B CB    1 
ATOM   7318  C  CG    . ASN B 1 218 ? 109.065 135.345 119.733 1.00 46.85 ?  218 ASN B CG    1 
ATOM   7319  O  OD1   . ASN B 1 218 ? 108.109 136.053 120.047 1.00 45.77 ?  218 ASN B OD1   1 
ATOM   7320  N  ND2   . ASN B 1 218 ? 109.200 134.094 120.158 1.00 48.32 ?  218 ASN B ND2   1 
ATOM   7321  N  N     . ALA B 1 219 ? 113.043 138.128 119.517 1.00 37.53 ?  219 ALA B N     1 
ATOM   7322  C  CA    . ALA B 1 219 ? 114.468 138.282 119.259 1.00 35.07 ?  219 ALA B CA    1 
ATOM   7323  C  C     . ALA B 1 219 ? 115.321 138.287 120.516 1.00 37.31 ?  219 ALA B C     1 
ATOM   7324  O  O     . ALA B 1 219 ? 116.468 137.836 120.476 1.00 35.41 ?  219 ALA B O     1 
ATOM   7325  C  CB    . ALA B 1 219 ? 114.716 139.578 118.480 1.00 36.43 ?  219 ALA B CB    1 
ATOM   7326  N  N     . THR B 1 220 ? 114.795 138.783 121.631 1.00 34.97 ?  220 THR B N     1 
ATOM   7327  C  CA    . THR B 1 220 ? 115.585 138.911 122.846 1.00 31.02 ?  220 THR B CA    1 
ATOM   7328  C  C     . THR B 1 220 ? 115.813 137.555 123.500 1.00 34.50 ?  220 THR B C     1 
ATOM   7329  O  O     . THR B 1 220 ? 114.960 136.664 123.455 1.00 35.03 ?  220 THR B O     1 
ATOM   7330  C  CB    . THR B 1 220 ? 114.898 139.847 123.840 1.00 32.28 ?  220 THR B CB    1 
ATOM   7331  O  OG1   . THR B 1 220 ? 113.667 139.260 124.281 1.00 38.26 ?  220 THR B OG1   1 
ATOM   7332  C  CG2   . THR B 1 220 ? 114.604 141.175 123.186 1.00 32.74 ?  220 THR B CG2   1 
ATOM   7333  N  N     . LYS B 1 221 ? 116.987 137.410 124.111 1.00 32.78 ?  221 LYS B N     1 
ATOM   7334  C  CA    . LYS B 1 221 ? 117.304 136.235 124.910 1.00 29.71 ?  221 LYS B CA    1 
ATOM   7335  C  C     . LYS B 1 221 ? 116.772 136.331 126.331 1.00 31.82 ?  221 LYS B C     1 
ATOM   7336  O  O     . LYS B 1 221 ? 116.869 135.352 127.080 1.00 34.84 ?  221 LYS B O     1 
ATOM   7337  C  CB    . LYS B 1 221 ? 118.819 136.016 124.950 1.00 29.40 ?  221 LYS B CB    1 
ATOM   7338  C  CG    . LYS B 1 221 ? 119.402 135.523 123.644 1.00 30.09 ?  221 LYS B CG    1 
ATOM   7339  C  CD    . LYS B 1 221 ? 120.422 134.426 123.884 1.00 32.86 ?  221 LYS B CD    1 
ATOM   7340  C  CE    . LYS B 1 221 ? 120.852 133.791 122.577 1.00 35.04 ?  221 LYS B CE    1 
ATOM   7341  N  NZ    . LYS B 1 221 ? 119.898 134.100 121.477 1.00 32.52 1  221 LYS B NZ    1 
ATOM   7342  N  N     . GLY B 1 222 ? 116.217 137.474 126.716 1.00 31.02 ?  222 GLY B N     1 
ATOM   7343  C  CA    . GLY B 1 222 ? 115.715 137.650 128.056 1.00 27.64 ?  222 GLY B CA    1 
ATOM   7344  C  C     . GLY B 1 222 ? 116.823 137.923 129.054 1.00 28.06 ?  222 GLY B C     1 
ATOM   7345  O  O     . GLY B 1 222 ? 117.979 138.182 128.707 1.00 31.31 ?  222 GLY B O     1 
ATOM   7346  N  N     . VAL B 1 223 ? 116.445 137.864 130.332 1.00 27.28 ?  223 VAL B N     1 
ATOM   7347  C  CA    . VAL B 1 223 ? 117.412 138.106 131.394 1.00 25.17 ?  223 VAL B CA    1 
ATOM   7348  C  C     . VAL B 1 223 ? 118.349 136.924 131.587 1.00 20.16 ?  223 VAL B C     1 
ATOM   7349  O  O     . VAL B 1 223 ? 119.382 137.067 132.243 1.00 26.46 ?  223 VAL B O     1 
ATOM   7350  C  CB    . VAL B 1 223 ? 116.699 138.451 132.715 1.00 21.99 ?  223 VAL B CB    1 
ATOM   7351  C  CG1   . VAL B 1 223 ? 115.597 139.468 132.474 1.00 22.24 ?  223 VAL B CG1   1 
ATOM   7352  C  CG2   . VAL B 1 223 ? 116.146 137.196 133.373 1.00 22.98 ?  223 VAL B CG2   1 
ATOM   7353  N  N     . VAL B 1 224 ? 118.018 135.755 131.036 1.00 24.17 ?  224 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 224 ? 118.878 134.587 131.207 1.00 22.49 ?  224 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 224 ? 120.173 134.723 130.409 1.00 26.27 ?  224 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 224 ? 121.240 134.313 130.878 1.00 30.84 ?  224 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 224 ? 118.109 133.308 130.834 1.00 27.68 ?  224 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 224 ? 119.035 132.103 130.834 1.00 27.23 ?  224 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 224 ? 116.960 133.094 131.801 1.00 26.03 ?  224 VAL B CG2   1 
ATOM   7360  N  N     . GLY B 1 225 ? 120.115 135.291 129.202 1.00 22.82 ?  225 GLY B N     1 
ATOM   7361  C  CA    . GLY B 1 225 ? 121.340 135.523 128.451 1.00 18.39 ?  225 GLY B CA    1 
ATOM   7362  C  C     . GLY B 1 225 ? 122.261 136.515 129.135 1.00 21.88 ?  225 GLY B C     1 
ATOM   7363  O  O     . GLY B 1 225 ? 123.475 136.301 129.218 1.00 34.08 ?  225 GLY B O     1 
ATOM   7364  N  N     . VAL B 1 226 ? 121.695 137.613 129.640 1.00 19.13 ?  226 VAL B N     1 
ATOM   7365  C  CA    . VAL B 1 226 ? 122.480 138.571 130.409 1.00 19.93 ?  226 VAL B CA    1 
ATOM   7366  C  C     . VAL B 1 226 ? 123.013 137.922 131.674 1.00 19.06 ?  226 VAL B C     1 
ATOM   7367  O  O     . VAL B 1 226 ? 124.122 138.231 132.122 1.00 23.03 ?  226 VAL B O     1 
ATOM   7368  C  CB    . VAL B 1 226 ? 121.638 139.821 130.727 1.00 17.08 ?  226 VAL B CB    1 
ATOM   7369  C  CG1   . VAL B 1 226 ? 122.530 140.954 131.212 1.00 22.26 ?  226 VAL B CG1   1 
ATOM   7370  C  CG2   . VAL B 1 226 ? 120.844 140.241 129.509 1.00 16.72 ?  226 VAL B CG2   1 
ATOM   7371  N  N     . MET B 1 227 ? 122.236 137.018 132.272 1.00 22.71 ?  227 MET B N     1 
ATOM   7372  C  CA    . MET B 1 227 ? 122.697 136.286 133.444 1.00 21.23 ?  227 MET B CA    1 
ATOM   7373  C  C     . MET B 1 227 ? 123.910 135.431 133.118 1.00 21.57 ?  227 MET B C     1 
ATOM   7374  O  O     . MET B 1 227 ? 124.863 135.373 133.898 1.00 27.55 ?  227 MET B O     1 
ATOM   7375  C  CB    . MET B 1 227 ? 121.566 135.416 133.986 1.00 20.01 ?  227 MET B CB    1 
ATOM   7376  C  CG    . MET B 1 227 ? 120.671 136.106 134.985 1.00 16.03 ?  227 MET B CG    1 
ATOM   7377  S  SD    . MET B 1 227 ? 119.489 134.950 135.683 1.00 40.04 ?  227 MET B SD    1 
ATOM   7378  C  CE    . MET B 1 227 ? 120.196 134.741 137.306 1.00 24.27 ?  227 MET B CE    1 
ATOM   7379  N  N     . LYS B 1 228 ? 123.884 134.747 131.975 1.00 22.19 ?  228 LYS B N     1 
ATOM   7380  C  CA    . LYS B 1 228 ? 125.033 133.943 131.564 1.00 22.43 ?  228 LYS B CA    1 
ATOM   7381  C  C     . LYS B 1 228 ? 126.250 134.820 131.299 1.00 22.93 ?  228 LYS B C     1 
ATOM   7382  O  O     . LYS B 1 228 ? 127.376 134.472 131.680 1.00 23.93 ?  228 LYS B O     1 
ATOM   7383  C  CB    . LYS B 1 228 ? 124.683 133.124 130.324 1.00 24.69 ?  228 LYS B CB    1 
ATOM   7384  C  CG    . LYS B 1 228 ? 124.227 131.710 130.622 1.00 29.35 ?  228 LYS B CG    1 
ATOM   7385  C  CD    . LYS B 1 228 ? 122.801 131.495 130.150 1.00 29.88 ?  228 LYS B CD    1 
ATOM   7386  C  CE    . LYS B 1 228 ? 122.679 131.735 128.655 1.00 33.12 ?  228 LYS B CE    1 
ATOM   7387  N  NZ    . LYS B 1 228 ? 121.411 131.185 128.104 1.00 34.24 1  228 LYS B NZ    1 
ATOM   7388  N  N     . LEU B 1 229 ? 126.038 135.966 130.646 1.00 22.47 ?  229 LEU B N     1 
ATOM   7389  C  CA    . LEU B 1 229 ? 127.140 136.893 130.402 1.00 20.86 ?  229 LEU B CA    1 
ATOM   7390  C  C     . LEU B 1 229 ? 127.748 137.375 131.713 1.00 19.28 ?  229 LEU B C     1 
ATOM   7391  O  O     . LEU B 1 229 ? 128.974 137.408 131.869 1.00 25.07 ?  229 LEU B O     1 
ATOM   7392  C  CB    . LEU B 1 229 ? 126.654 138.084 129.578 1.00 23.23 ?  229 LEU B CB    1 
ATOM   7393  C  CG    . LEU B 1 229 ? 126.141 137.824 128.167 1.00 19.52 ?  229 LEU B CG    1 
ATOM   7394  C  CD1   . LEU B 1 229 ? 125.153 138.909 127.789 1.00 20.88 ?  229 LEU B CD1   1 
ATOM   7395  C  CD2   . LEU B 1 229 ? 127.296 137.775 127.186 1.00 17.63 ?  229 LEU B CD2   1 
ATOM   7396  N  N     . LEU B 1 230 ? 126.899 137.750 132.671 1.00 21.75 ?  230 LEU B N     1 
ATOM   7397  C  CA    . LEU B 1 230 ? 127.384 138.218 133.963 1.00 17.81 ?  230 LEU B CA    1 
ATOM   7398  C  C     . LEU B 1 230 ? 128.077 137.101 134.730 1.00 17.83 ?  230 LEU B C     1 
ATOM   7399  O  O     . LEU B 1 230 ? 129.071 137.342 135.420 1.00 28.53 ?  230 LEU B O     1 
ATOM   7400  C  CB    . LEU B 1 230 ? 126.228 138.794 134.779 1.00 19.03 ?  230 LEU B CB    1 
ATOM   7401  C  CG    . LEU B 1 230 ? 125.652 140.123 134.293 1.00 23.50 ?  230 LEU B CG    1 
ATOM   7402  C  CD1   . LEU B 1 230 ? 124.337 140.418 134.992 1.00 24.96 ?  230 LEU B CD1   1 
ATOM   7403  C  CD2   . LEU B 1 230 ? 126.647 141.249 134.516 1.00 20.05 ?  230 LEU B CD2   1 
ATOM   7404  N  N     . ASP B 1 231 ? 127.561 135.877 134.631 1.00 21.74 ?  231 ASP B N     1 
ATOM   7405  C  CA    . ASP B 1 231 ? 128.195 134.746 135.294 1.00 24.81 ?  231 ASP B CA    1 
ATOM   7406  C  C     . ASP B 1 231 ? 129.597 134.509 134.750 1.00 26.22 ?  231 ASP B C     1 
ATOM   7407  O  O     . ASP B 1 231 ? 130.542 134.296 135.519 1.00 32.42 ?  231 ASP B O     1 
ATOM   7408  C  CB    . ASP B 1 231 ? 127.332 133.496 135.125 1.00 26.44 ?  231 ASP B CB    1 
ATOM   7409  C  CG    . ASP B 1 231 ? 127.940 132.275 135.777 1.00 35.82 ?  231 ASP B CG    1 
ATOM   7410  O  OD1   . ASP B 1 231 ? 128.329 132.367 136.959 1.00 38.60 ?  231 ASP B OD1   1 
ATOM   7411  O  OD2   . ASP B 1 231 ? 128.030 131.225 135.109 1.00 35.57 -1 231 ASP B OD2   1 
ATOM   7412  N  N     . ASN B 1 232 ? 129.755 134.564 133.427 1.00 29.25 ?  232 ASN B N     1 
ATOM   7413  C  CA    . ASN B 1 232 ? 131.087 134.419 132.847 1.00 26.54 ?  232 ASN B CA    1 
ATOM   7414  C  C     . ASN B 1 232 ? 131.987 135.590 133.216 1.00 23.51 ?  232 ASN B C     1 
ATOM   7415  O  O     . ASN B 1 232 ? 133.191 135.407 133.438 1.00 31.02 ?  232 ASN B O     1 
ATOM   7416  C  CB    . ASN B 1 232 ? 130.991 134.265 131.331 1.00 29.57 ?  232 ASN B CB    1 
ATOM   7417  C  CG    . ASN B 1 232 ? 131.789 133.086 130.820 1.00 31.72 ?  232 ASN B CG    1 
ATOM   7418  O  OD1   . ASN B 1 232 ? 131.235 132.157 130.236 1.00 31.09 ?  232 ASN B OD1   1 
ATOM   7419  N  ND2   . ASN B 1 232 ? 133.099 133.126 131.018 1.00 30.58 ?  232 ASN B ND2   1 
ATOM   7420  N  N     . ALA B 1 233 ? 131.429 136.800 133.283 1.00 22.25 ?  233 ALA B N     1 
ATOM   7421  C  CA    . ALA B 1 233 ? 132.219 137.963 133.672 1.00 19.36 ?  233 ALA B CA    1 
ATOM   7422  C  C     . ALA B 1 233 ? 132.727 137.836 135.103 1.00 30.42 ?  233 ALA B C     1 
ATOM   7423  O  O     . ALA B 1 233 ? 133.885 138.159 135.391 1.00 37.00 ?  233 ALA B O     1 
ATOM   7424  C  CB    . ALA B 1 233 ? 131.391 139.234 133.506 1.00 21.32 ?  233 ALA B CB    1 
ATOM   7425  N  N     . PHE B 1 234 ? 131.871 137.370 136.014 1.00 26.24 ?  234 PHE B N     1 
ATOM   7426  C  CA    . PHE B 1 234 ? 132.282 137.190 137.402 1.00 18.46 ?  234 PHE B CA    1 
ATOM   7427  C  C     . PHE B 1 234 ? 133.245 136.022 137.552 1.00 23.57 ?  234 PHE B C     1 
ATOM   7428  O  O     . PHE B 1 234 ? 134.128 136.057 138.416 1.00 30.29 ?  234 PHE B O     1 
ATOM   7429  C  CB    . PHE B 1 234 ? 131.055 136.997 138.293 1.00 25.09 ?  234 PHE B CB    1 
ATOM   7430  C  CG    . PHE B 1 234 ? 130.306 138.268 138.572 1.00 21.29 ?  234 PHE B CG    1 
ATOM   7431  C  CD1   . PHE B 1 234 ? 130.920 139.316 139.229 1.00 22.20 ?  234 PHE B CD1   1 
ATOM   7432  C  CD2   . PHE B 1 234 ? 128.991 138.416 138.175 1.00 20.87 ?  234 PHE B CD2   1 
ATOM   7433  C  CE1   . PHE B 1 234 ? 130.237 140.487 139.481 1.00 20.21 ?  234 PHE B CE1   1 
ATOM   7434  C  CE2   . PHE B 1 234 ? 128.305 139.588 138.423 1.00 20.94 ?  234 PHE B CE2   1 
ATOM   7435  C  CZ    . PHE B 1 234 ? 128.928 140.621 139.079 1.00 20.90 ?  234 PHE B CZ    1 
ATOM   7436  N  N     . ARG B 1 235 ? 133.088 134.978 136.734 1.00 29.56 ?  235 ARG B N     1 
ATOM   7437  C  CA    . ARG B 1 235 ? 134.064 133.895 136.729 1.00 26.83 ?  235 ARG B CA    1 
ATOM   7438  C  C     . ARG B 1 235 ? 135.430 134.392 136.277 1.00 28.32 ?  235 ARG B C     1 
ATOM   7439  O  O     . ARG B 1 235 ? 136.458 134.012 136.849 1.00 36.66 ?  235 ARG B O     1 
ATOM   7440  C  CB    . ARG B 1 235 ? 133.587 132.759 135.826 1.00 24.84 ?  235 ARG B CB    1 
ATOM   7441  C  CG    . ARG B 1 235 ? 132.996 131.581 136.572 1.00 32.99 ?  235 ARG B CG    1 
ATOM   7442  C  CD    . ARG B 1 235 ? 132.617 130.456 135.626 1.00 30.46 ?  235 ARG B CD    1 
ATOM   7443  N  NE    . ARG B 1 235 ? 131.262 130.605 135.109 1.00 34.53 ?  235 ARG B NE    1 
ATOM   7444  C  CZ    . ARG B 1 235 ? 130.958 130.662 133.819 1.00 36.67 ?  235 ARG B CZ    1 
ATOM   7445  N  NH1   . ARG B 1 235 ? 131.891 130.592 132.885 1.00 35.53 1  235 ARG B NH1   1 
ATOM   7446  N  NH2   . ARG B 1 235 ? 129.684 130.790 133.458 1.00 32.65 ?  235 ARG B NH2   1 
ATOM   7447  N  N     . TYR B 1 236 ? 135.460 135.244 135.251 1.00 24.71 ?  236 TYR B N     1 
ATOM   7448  C  CA    . TYR B 1 236 ? 136.731 135.747 134.742 1.00 25.51 ?  236 TYR B CA    1 
ATOM   7449  C  C     . TYR B 1 236 ? 137.388 136.689 135.743 1.00 27.63 ?  236 TYR B C     1 
ATOM   7450  O  O     . TYR B 1 236 ? 138.586 136.573 136.027 1.00 28.35 ?  236 TYR B O     1 
ATOM   7451  C  CB    . TYR B 1 236 ? 136.513 136.448 133.403 1.00 22.47 ?  236 TYR B CB    1 
ATOM   7452  C  CG    . TYR B 1 236 ? 137.790 136.919 132.754 1.00 23.31 ?  236 TYR B CG    1 
ATOM   7453  C  CD1   . TYR B 1 236 ? 138.656 136.015 132.160 1.00 21.64 ?  236 TYR B CD1   1 
ATOM   7454  C  CD2   . TYR B 1 236 ? 138.131 138.265 132.737 1.00 24.88 ?  236 TYR B CD2   1 
ATOM   7455  C  CE1   . TYR B 1 236 ? 139.823 136.433 131.565 1.00 24.32 ?  236 TYR B CE1   1 
ATOM   7456  C  CE2   . TYR B 1 236 ? 139.299 138.693 132.141 1.00 17.73 ?  236 TYR B CE2   1 
ATOM   7457  C  CZ    . TYR B 1 236 ? 140.139 137.770 131.558 1.00 20.63 ?  236 TYR B CZ    1 
ATOM   7458  O  OH    . TYR B 1 236 ? 141.306 138.180 130.961 1.00 30.59 ?  236 TYR B OH    1 
ATOM   7459  N  N     . ALA B 1 237 ? 136.620 137.634 136.284 1.00 29.98 ?  237 ALA B N     1 
ATOM   7460  C  CA    . ALA B 1 237 ? 137.127 138.583 137.275 1.00 29.43 ?  237 ALA B CA    1 
ATOM   7461  C  C     . ALA B 1 237 ? 136.897 137.982 138.655 1.00 36.88 ?  237 ALA B C     1 
ATOM   7462  O  O     . ALA B 1 237 ? 135.866 138.202 139.291 1.00 39.03 ?  237 ALA B O     1 
ATOM   7463  C  CB    . ALA B 1 237 ? 136.448 139.937 137.123 1.00 30.69 ?  237 ALA B CB    1 
ATOM   7464  N  N     . ASP B 1 238 ? 137.878 137.213 139.125 1.00 50.17 ?  238 ASP B N     1 
ATOM   7465  C  CA    . ASP B 1 238 ? 137.748 136.501 140.390 1.00 53.56 ?  238 ASP B CA    1 
ATOM   7466  C  C     . ASP B 1 238 ? 138.840 136.907 141.373 1.00 57.82 ?  238 ASP B C     1 
ATOM   7467  O  O     . ASP B 1 238 ? 139.489 136.045 141.975 1.00 57.80 ?  238 ASP B O     1 
ATOM   7468  C  CB    . ASP B 1 238 ? 137.776 134.987 140.156 1.00 52.95 ?  238 ASP B CB    1 
ATOM   7469  C  CG    . ASP B 1 238 ? 139.018 134.532 139.415 1.00 57.45 ?  238 ASP B CG    1 
ATOM   7470  O  OD1   . ASP B 1 238 ? 139.654 135.370 138.742 1.00 57.54 ?  238 ASP B OD1   1 
ATOM   7471  O  OD2   . ASP B 1 238 ? 139.362 133.335 139.511 1.00 56.42 -1 238 ASP B OD2   1 
ATOM   7472  N  N     . GLN B 1 239 ? 139.056 138.215 141.528 1.00 63.48 ?  239 GLN B N     1 
ATOM   7473  C  CA    . GLN B 1 239 ? 140.037 138.754 142.473 1.00 64.82 ?  239 GLN B CA    1 
ATOM   7474  C  C     . GLN B 1 239 ? 141.417 138.141 142.251 1.00 67.35 ?  239 GLN B C     1 
ATOM   7475  O  O     . GLN B 1 239 ? 142.096 137.715 143.190 1.00 66.69 ?  239 GLN B O     1 
ATOM   7476  C  CB    . GLN B 1 239 ? 139.581 138.550 143.918 1.00 64.62 ?  239 GLN B CB    1 
ATOM   7477  C  CG    . GLN B 1 239 ? 138.664 139.635 144.448 1.00 63.82 ?  239 GLN B CG    1 
ATOM   7478  C  CD    . GLN B 1 239 ? 138.911 139.932 145.914 1.00 66.05 ?  239 GLN B CD    1 
ATOM   7479  O  OE1   . GLN B 1 239 ? 137.978 140.006 146.713 1.00 65.31 ?  239 GLN B OE1   1 
ATOM   7480  N  NE2   . GLN B 1 239 ? 140.177 140.105 146.276 1.00 65.72 ?  239 GLN B NE2   1 
ATOM   7481  N  N     . MET B 1 240 ? 141.829 138.096 140.982 1.00 69.45 ?  240 MET B N     1 
ATOM   7482  C  CA    . MET B 1 240 ? 143.116 137.525 140.586 1.00 68.65 ?  240 MET B CA    1 
ATOM   7483  C  C     . MET B 1 240 ? 143.254 136.072 141.033 1.00 69.19 ?  240 MET B C     1 
ATOM   7484  O  O     . MET B 1 240 ? 144.350 135.613 141.365 1.00 69.12 ?  240 MET B O     1 
ATOM   7485  C  CB    . MET B 1 240 ? 144.285 138.363 141.114 1.00 68.32 ?  240 MET B CB    1 
ATOM   7486  C  CG    . MET B 1 240 ? 144.368 139.766 140.529 1.00 68.69 ?  240 MET B CG    1 
ATOM   7487  S  SD    . MET B 1 240 ? 142.794 140.645 140.511 1.00 73.09 ?  240 MET B SD    1 
ATOM   7488  C  CE    . MET B 1 240 ? 143.304 142.238 139.875 1.00 67.85 ?  240 MET B CE    1 
ATOM   7489  N  N     . GLY B 1 241 ? 142.144 135.337 141.046 1.00 67.80 ?  241 GLY B N     1 
ATOM   7490  C  CA    . GLY B 1 241 ? 142.164 133.930 141.387 1.00 68.08 ?  241 GLY B CA    1 
ATOM   7491  C  C     . GLY B 1 241 ? 142.232 133.615 142.864 1.00 70.85 ?  241 GLY B C     1 
ATOM   7492  O  O     . GLY B 1 241 ? 142.381 132.441 143.220 1.00 70.98 ?  241 GLY B O     1 
ATOM   7493  N  N     . GLN B 1 242 ? 142.126 134.618 143.736 1.00 75.83 ?  242 GLN B N     1 
ATOM   7494  C  CA    . GLN B 1 242 ? 142.183 134.379 145.174 1.00 75.30 ?  242 GLN B CA    1 
ATOM   7495  C  C     . GLN B 1 242 ? 140.812 134.039 145.748 1.00 76.57 ?  242 GLN B C     1 
ATOM   7496  O  O     . GLN B 1 242 ? 140.640 132.985 146.369 1.00 76.27 ?  242 GLN B O     1 
ATOM   7497  C  CB    . GLN B 1 242 ? 142.767 135.602 145.886 1.00 74.11 ?  242 GLN B CB    1 
ATOM   7498  C  CG    . GLN B 1 242 ? 144.250 135.817 145.627 1.00 76.09 ?  242 GLN B CG    1 
ATOM   7499  C  CD    . GLN B 1 242 ? 144.898 136.719 146.658 1.00 77.11 ?  242 GLN B CD    1 
ATOM   7500  O  OE1   . GLN B 1 242 ? 144.298 137.043 147.684 1.00 76.41 ?  242 GLN B OE1   1 
ATOM   7501  N  NE2   . GLN B 1 242 ? 146.132 137.132 146.390 1.00 75.63 ?  242 GLN B NE2   1 
ATOM   7502  N  N     . ARG B 1 243 ? 139.831 134.915 145.551 1.00 64.77 ?  243 ARG B N     1 
ATOM   7503  C  CA    . ARG B 1 243 ? 138.462 134.690 145.991 1.00 64.67 ?  243 ARG B CA    1 
ATOM   7504  C  C     . ARG B 1 243 ? 137.568 134.597 144.765 1.00 63.62 ?  243 ARG B C     1 
ATOM   7505  O  O     . ARG B 1 243 ? 137.656 135.440 143.867 1.00 62.13 ?  243 ARG B O     1 
ATOM   7506  C  CB    . ARG B 1 243 ? 137.987 135.813 146.921 1.00 63.04 ?  243 ARG B CB    1 
ATOM   7507  C  CG    . ARG B 1 243 ? 136.490 136.092 146.863 1.00 63.91 ?  243 ARG B CG    1 
ATOM   7508  C  CD    . ARG B 1 243 ? 136.191 137.386 146.116 1.00 63.15 ?  243 ARG B CD    1 
ATOM   7509  N  NE    . ARG B 1 243 ? 134.864 137.906 146.427 1.00 65.04 ?  243 ARG B NE    1 
ATOM   7510  C  CZ    . ARG B 1 243 ? 134.294 138.925 145.800 1.00 62.89 ?  243 ARG B CZ    1 
ATOM   7511  N  NH1   . ARG B 1 243 ? 134.906 139.561 144.814 1.00 59.40 1  243 ARG B NH1   1 
ATOM   7512  N  NH2   . ARG B 1 243 ? 133.078 139.316 146.170 1.00 60.40 ?  243 ARG B NH2   1 
ATOM   7513  N  N     . GLN B 1 244 ? 136.716 133.574 144.729 1.00 61.88 ?  244 GLN B N     1 
ATOM   7514  C  CA    . GLN B 1 244 ? 135.825 133.383 143.591 1.00 62.67 ?  244 GLN B CA    1 
ATOM   7515  C  C     . GLN B 1 244 ? 134.952 134.614 143.386 1.00 61.97 ?  244 GLN B C     1 
ATOM   7516  O  O     . GLN B 1 244 ? 134.388 135.157 144.342 1.00 61.07 ?  244 GLN B O     1 
ATOM   7517  C  CB    . GLN B 1 244 ? 134.950 132.148 143.808 1.00 59.38 ?  244 GLN B CB    1 
ATOM   7518  C  CG    . GLN B 1 244 ? 135.702 130.830 143.742 1.00 59.03 ?  244 GLN B CG    1 
ATOM   7519  C  CD    . GLN B 1 244 ? 134.790 129.653 143.458 1.00 60.67 ?  244 GLN B CD    1 
ATOM   7520  O  OE1   . GLN B 1 244 ? 133.690 129.559 144.004 1.00 61.69 ?  244 GLN B OE1   1 
ATOM   7521  N  NE2   . GLN B 1 244 ? 135.241 128.747 142.600 1.00 59.63 ?  244 GLN B NE2   1 
ATOM   7522  N  N     . GLY B 1 245 ? 134.854 135.061 142.136 1.00 50.30 ?  245 GLY B N     1 
ATOM   7523  C  CA    . GLY B 1 245 ? 134.028 136.205 141.810 1.00 47.08 ?  245 GLY B CA    1 
ATOM   7524  C  C     . GLY B 1 245 ? 132.571 135.967 142.142 1.00 46.51 ?  245 GLY B C     1 
ATOM   7525  O  O     . GLY B 1 245 ? 131.960 135.020 141.640 1.00 46.35 ?  245 GLY B O     1 
ATOM   7526  N  N     . SER B 1 246 ? 132.004 136.819 142.990 1.00 41.79 ?  246 SER B N     1 
ATOM   7527  C  CA    . SER B 1 246 ? 130.641 136.659 143.477 1.00 37.18 ?  246 SER B CA    1 
ATOM   7528  C  C     . SER B 1 246 ? 129.777 137.779 142.915 1.00 35.91 ?  246 SER B C     1 
ATOM   7529  O  O     . SER B 1 246 ? 130.086 138.960 143.099 1.00 30.02 ?  246 SER B O     1 
ATOM   7530  C  CB    . SER B 1 246 ? 130.602 136.663 145.004 1.00 37.49 ?  246 SER B CB    1 
ATOM   7531  O  OG    . SER B 1 246 ? 131.210 135.498 145.533 1.00 43.74 ?  246 SER B OG    1 
ATOM   7532  N  N     . GLY B 1 247 ? 128.695 137.400 142.237 1.00 25.68 ?  247 GLY B N     1 
ATOM   7533  C  CA    . GLY B 1 247 ? 127.754 138.363 141.721 1.00 8.74  ?  247 GLY B CA    1 
ATOM   7534  C  C     . GLY B 1 247 ? 126.342 137.997 142.130 1.00 13.22 ?  247 GLY B C     1 
ATOM   7535  O  O     . GLY B 1 247 ? 126.044 136.859 142.489 1.00 20.58 ?  247 GLY B O     1 
ATOM   7536  N  N     . ALA B 1 248 ? 125.473 138.998 142.082 1.00 14.03 ?  248 ALA B N     1 
ATOM   7537  C  CA    . ALA B 1 248 ? 124.062 138.823 142.380 1.00 14.28 ?  248 ALA B CA    1 
ATOM   7538  C  C     . ALA B 1 248 ? 123.238 139.430 141.259 1.00 10.37 ?  248 ALA B C     1 
ATOM   7539  O  O     . ALA B 1 248 ? 123.567 140.501 140.746 1.00 17.81 ?  248 ALA B O     1 
ATOM   7540  C  CB    . ALA B 1 248 ? 123.684 139.461 143.720 1.00 9.00  ?  248 ALA B CB    1 
ATOM   7541  N  N     . ALA B 1 249 ? 122.179 138.732 140.870 1.00 12.61 ?  249 ALA B N     1 
ATOM   7542  C  CA    . ALA B 1 249 ? 121.203 139.242 139.920 1.00 12.36 ?  249 ALA B CA    1 
ATOM   7543  C  C     . ALA B 1 249 ? 119.861 139.345 140.624 1.00 8.88  ?  249 ALA B C     1 
ATOM   7544  O  O     . ALA B 1 249 ? 119.437 138.401 141.298 1.00 16.83 ?  249 ALA B O     1 
ATOM   7545  C  CB    . ALA B 1 249 ? 121.093 138.339 138.689 1.00 14.14 ?  249 ALA B CB    1 
ATOM   7546  N  N     . TYR B 1 250 ? 119.206 140.491 140.486 1.00 8.30  ?  250 TYR B N     1 
ATOM   7547  C  CA    . TYR B 1 250 ? 117.903 140.717 141.089 1.00 8.18  ?  250 TYR B CA    1 
ATOM   7548  C  C     . TYR B 1 250 ? 116.878 140.928 139.988 1.00 7.77  ?  250 TYR B C     1 
ATOM   7549  O  O     . TYR B 1 250 ? 117.119 141.690 139.046 1.00 13.56 ?  250 TYR B O     1 
ATOM   7550  C  CB    . TYR B 1 250 ? 117.930 141.917 142.034 1.00 7.54  ?  250 TYR B CB    1 
ATOM   7551  C  CG    . TYR B 1 250 ? 118.389 141.575 143.429 1.00 15.50 ?  250 TYR B CG    1 
ATOM   7552  C  CD1   . TYR B 1 250 ? 119.730 141.343 143.699 1.00 3.04  ?  250 TYR B CD1   1 
ATOM   7553  C  CD2   . TYR B 1 250 ? 117.485 141.482 144.477 1.00 12.49 ?  250 TYR B CD2   1 
ATOM   7554  C  CE1   . TYR B 1 250 ? 120.158 141.031 144.969 1.00 0.74  ?  250 TYR B CE1   1 
ATOM   7555  C  CE2   . TYR B 1 250 ? 117.904 141.168 145.754 1.00 7.28  ?  250 TYR B CE2   1 
ATOM   7556  C  CZ    . TYR B 1 250 ? 119.243 140.945 145.994 1.00 8.49  ?  250 TYR B CZ    1 
ATOM   7557  O  OH    . TYR B 1 250 ? 119.669 140.632 147.264 1.00 12.85 ?  250 TYR B OH    1 
ATOM   7558  N  N     . LEU B 1 251 ? 115.745 140.249 140.105 1.00 12.99 ?  251 LEU B N     1 
ATOM   7559  C  CA    . LEU B 1 251 ? 114.658 140.373 139.148 1.00 14.29 ?  251 LEU B CA    1 
ATOM   7560  C  C     . LEU B 1 251 ? 113.349 140.559 139.895 1.00 12.54 ?  251 LEU B C     1 
ATOM   7561  O  O     . LEU B 1 251 ? 113.107 139.902 140.911 1.00 15.58 ?  251 LEU B O     1 
ATOM   7562  C  CB    . LEU B 1 251 ? 114.571 139.145 138.240 1.00 15.25 ?  251 LEU B CB    1 
ATOM   7563  C  CG    . LEU B 1 251 ? 113.778 139.349 136.950 1.00 11.75 ?  251 LEU B CG    1 
ATOM   7564  C  CD1   . LEU B 1 251 ? 114.519 140.295 136.027 1.00 12.25 ?  251 LEU B CD1   1 
ATOM   7565  C  CD2   . LEU B 1 251 ? 113.513 138.025 136.264 1.00 7.68  ?  251 LEU B CD2   1 
ATOM   7566  N  N     . ASN B 1 252 ? 112.513 141.460 139.393 1.00 11.64 ?  252 ASN B N     1 
ATOM   7567  C  CA    . ASN B 1 252 ? 111.181 141.623 139.953 1.00 10.65 ?  252 ASN B CA    1 
ATOM   7568  C  C     . ASN B 1 252 ? 110.347 140.380 139.677 1.00 15.17 ?  252 ASN B C     1 
ATOM   7569  O  O     . ASN B 1 252 ? 110.465 139.753 138.620 1.00 23.08 ?  252 ASN B O     1 
ATOM   7570  C  CB    . ASN B 1 252 ? 110.502 142.860 139.369 1.00 12.48 ?  252 ASN B CB    1 
ATOM   7571  C  CG    . ASN B 1 252 ? 109.466 143.446 140.303 1.00 20.70 ?  252 ASN B CG    1 
ATOM   7572  O  OD1   . ASN B 1 252 ? 108.393 142.876 140.494 1.00 30.12 ?  252 ASN B OD1   1 
ATOM   7573  N  ND2   . ASN B 1 252 ? 109.784 144.588 140.898 1.00 20.44 ?  252 ASN B ND2   1 
ATOM   7574  N  N     . ILE B 1 253 ? 109.501 140.017 140.644 1.00 13.68 ?  253 ILE B N     1 
ATOM   7575  C  CA    . ILE B 1 253 ? 108.685 138.819 140.503 1.00 17.48 ?  253 ILE B CA    1 
ATOM   7576  C  C     . ILE B 1 253 ? 107.626 138.975 139.420 1.00 20.96 ?  253 ILE B C     1 
ATOM   7577  O  O     . ILE B 1 253 ? 107.059 137.975 138.963 1.00 23.60 ?  253 ILE B O     1 
ATOM   7578  C  CB    . ILE B 1 253 ? 108.045 138.449 141.855 1.00 16.66 ?  253 ILE B CB    1 
ATOM   7579  C  CG1   . ILE B 1 253 ? 107.704 136.958 141.895 1.00 16.22 ?  253 ILE B CG1   1 
ATOM   7580  C  CG2   . ILE B 1 253 ? 106.814 139.300 142.122 1.00 13.72 ?  253 ILE B CG2   1 
ATOM   7581  C  CD1   . ILE B 1 253 ? 107.755 136.359 143.274 1.00 16.69 ?  253 ILE B CD1   1 
ATOM   7582  N  N     . PHE B 1 254 ? 107.346 140.201 138.986 1.00 19.04 ?  254 PHE B N     1 
ATOM   7583  C  CA    . PHE B 1 254 ? 106.390 140.446 137.917 1.00 16.79 ?  254 PHE B CA    1 
ATOM   7584  C  C     . PHE B 1 254 ? 107.040 140.456 136.540 1.00 18.10 ?  254 PHE B C     1 
ATOM   7585  O  O     . PHE B 1 254 ? 106.340 140.636 135.539 1.00 25.04 ?  254 PHE B O     1 
ATOM   7586  C  CB    . PHE B 1 254 ? 105.657 141.766 138.162 1.00 23.09 ?  254 PHE B CB    1 
ATOM   7587  C  CG    . PHE B 1 254 ? 104.567 141.664 139.188 1.00 22.28 ?  254 PHE B CG    1 
ATOM   7588  C  CD1   . PHE B 1 254 ? 103.417 140.942 138.925 1.00 22.04 ?  254 PHE B CD1   1 
ATOM   7589  C  CD2   . PHE B 1 254 ? 104.701 142.271 140.424 1.00 26.07 ?  254 PHE B CD2   1 
ATOM   7590  C  CE1   . PHE B 1 254 ? 102.415 140.839 139.869 1.00 24.80 ?  254 PHE B CE1   1 
ATOM   7591  C  CE2   . PHE B 1 254 ? 103.704 142.171 141.373 1.00 27.48 ?  254 PHE B CE2   1 
ATOM   7592  C  CZ    . PHE B 1 254 ? 102.559 141.454 141.094 1.00 21.77 ?  254 PHE B CZ    1 
ATOM   7593  N  N     . HIS B 1 255 ? 108.355 140.278 136.470 1.00 25.56 ?  255 HIS B N     1 
ATOM   7594  C  CA    . HIS B 1 255 ? 109.028 140.089 135.194 1.00 14.87 ?  255 HIS B CA    1 
ATOM   7595  C  C     . HIS B 1 255 ? 108.606 138.761 134.578 1.00 18.41 ?  255 HIS B C     1 
ATOM   7596  O  O     . HIS B 1 255 ? 108.414 137.768 135.283 1.00 27.28 ?  255 HIS B O     1 
ATOM   7597  C  CB    . HIS B 1 255 ? 110.542 140.123 135.393 1.00 17.20 ?  255 HIS B CB    1 
ATOM   7598  C  CG    . HIS B 1 255 ? 111.314 140.470 134.161 1.00 19.61 ?  255 HIS B CG    1 
ATOM   7599  N  ND1   . HIS B 1 255 ? 111.451 139.603 133.099 1.00 17.88 ?  255 HIS B ND1   1 
ATOM   7600  C  CD2   . HIS B 1 255 ? 112.008 141.584 133.829 1.00 14.91 ?  255 HIS B CD2   1 
ATOM   7601  C  CE1   . HIS B 1 255 ? 112.188 140.171 132.163 1.00 16.46 ?  255 HIS B CE1   1 
ATOM   7602  N  NE2   . HIS B 1 255 ? 112.541 141.373 132.581 1.00 11.54 ?  255 HIS B NE2   1 
ATOM   7603  N  N     . ARG B 1 256 ? 108.454 138.746 133.252 1.00 21.76 ?  256 ARG B N     1 
ATOM   7604  C  CA    . ARG B 1 256 ? 108.023 137.524 132.581 1.00 22.18 ?  256 ARG B CA    1 
ATOM   7605  C  C     . ARG B 1 256 ? 109.057 136.413 132.717 1.00 23.41 ?  256 ARG B C     1 
ATOM   7606  O  O     . ARG B 1 256 ? 108.697 135.232 132.774 1.00 25.13 ?  256 ARG B O     1 
ATOM   7607  C  CB    . ARG B 1 256 ? 107.737 137.805 131.105 1.00 22.61 ?  256 ARG B CB    1 
ATOM   7608  C  CG    . ARG B 1 256 ? 107.330 136.574 130.314 1.00 23.62 ?  256 ARG B CG    1 
ATOM   7609  C  CD    . ARG B 1 256 ? 108.228 136.361 129.109 1.00 25.89 ?  256 ARG B CD    1 
ATOM   7610  N  NE    . ARG B 1 256 ? 109.361 135.492 129.402 1.00 27.83 ?  256 ARG B NE    1 
ATOM   7611  C  CZ    . ARG B 1 256 ? 109.282 134.176 129.536 1.00 29.95 ?  256 ARG B CZ    1 
ATOM   7612  N  NH1   . ARG B 1 256 ? 108.131 133.535 129.412 1.00 28.67 1  256 ARG B NH1   1 
ATOM   7613  N  NH2   . ARG B 1 256 ? 110.386 133.484 129.802 1.00 27.86 ?  256 ARG B NH2   1 
ATOM   7614  N  N     . ASP B 1 257 ? 110.335 136.770 132.790 1.00 14.82 ?  257 ASP B N     1 
ATOM   7615  C  CA    . ASP B 1 257 ? 111.414 135.796 132.884 1.00 19.17 ?  257 ASP B CA    1 
ATOM   7616  C  C     . ASP B 1 257 ? 111.596 135.236 134.287 1.00 18.74 ?  257 ASP B C     1 
ATOM   7617  O  O     . ASP B 1 257 ? 112.540 134.468 134.504 1.00 24.95 ?  257 ASP B O     1 
ATOM   7618  C  CB    . ASP B 1 257 ? 112.727 136.425 132.417 1.00 23.39 ?  257 ASP B CB    1 
ATOM   7619  C  CG    . ASP B 1 257 ? 112.810 136.549 130.914 1.00 26.85 ?  257 ASP B CG    1 
ATOM   7620  O  OD1   . ASP B 1 257 ? 111.997 135.910 130.215 1.00 27.01 ?  257 ASP B OD1   1 
ATOM   7621  O  OD2   . ASP B 1 257 ? 113.693 137.284 130.432 1.00 31.26 -1 257 ASP B OD2   1 
ATOM   7622  N  N     . ILE B 1 258 ? 110.707 135.576 135.225 1.00 19.61 ?  258 ILE B N     1 
ATOM   7623  C  CA    . ILE B 1 258 ? 110.932 135.246 136.630 1.00 21.87 ?  258 ILE B CA    1 
ATOM   7624  C  C     . ILE B 1 258 ? 111.085 133.741 136.812 1.00 23.00 ?  258 ILE B C     1 
ATOM   7625  O  O     . ILE B 1 258 ? 111.894 133.282 137.626 1.00 32.37 ?  258 ILE B O     1 
ATOM   7626  C  CB    . ILE B 1 258 ? 109.803 135.820 137.509 1.00 23.55 ?  258 ILE B CB    1 
ATOM   7627  C  CG1   . ILE B 1 258 ? 110.119 135.609 138.992 1.00 21.31 ?  258 ILE B CG1   1 
ATOM   7628  C  CG2   . ILE B 1 258 ? 108.455 135.207 137.155 1.00 20.68 ?  258 ILE B CG2   1 
ATOM   7629  C  CD1   . ILE B 1 258 ? 111.383 136.299 139.449 1.00 19.07 ?  258 ILE B CD1   1 
ATOM   7630  N  N     . ASN B 1 259 ? 110.325 132.950 136.054 1.00 26.15 ?  259 ASN B N     1 
ATOM   7631  C  CA    . ASN B 1 259 ? 110.485 131.502 136.126 1.00 24.53 ?  259 ASN B CA    1 
ATOM   7632  C  C     . ASN B 1 259 ? 111.846 131.081 135.589 1.00 23.29 ?  259 ASN B C     1 
ATOM   7633  O  O     . ASN B 1 259 ? 112.596 130.365 136.264 1.00 26.89 ?  259 ASN B O     1 
ATOM   7634  C  CB    . ASN B 1 259 ? 109.357 130.813 135.361 1.00 24.70 ?  259 ASN B CB    1 
ATOM   7635  C  CG    . ASN B 1 259 ? 108.100 130.664 136.191 1.00 24.50 ?  259 ASN B CG    1 
ATOM   7636  O  OD1   . ASN B 1 259 ? 108.060 129.886 137.143 1.00 26.50 ?  259 ASN B OD1   1 
ATOM   7637  N  ND2   . ASN B 1 259 ? 107.065 131.415 135.837 1.00 30.54 ?  259 ASN B ND2   1 
ATOM   7638  N  N     . ASP B 1 260 ? 112.202 131.555 134.391 1.00 27.76 ?  260 ASP B N     1 
ATOM   7639  C  CA    . ASP B 1 260 ? 113.491 131.204 133.807 1.00 24.59 ?  260 ASP B CA    1 
ATOM   7640  C  C     . ASP B 1 260 ? 114.629 131.657 134.710 1.00 19.53 ?  260 ASP B C     1 
ATOM   7641  O  O     . ASP B 1 260 ? 115.585 130.910 134.952 1.00 27.97 ?  260 ASP B O     1 
ATOM   7642  C  CB    . ASP B 1 260 ? 113.624 131.824 132.417 1.00 23.49 ?  260 ASP B CB    1 
ATOM   7643  C  CG    . ASP B 1 260 ? 112.613 131.273 131.433 1.00 32.69 ?  260 ASP B CG    1 
ATOM   7644  O  OD1   . ASP B 1 260 ? 112.224 130.093 131.574 1.00 33.48 ?  260 ASP B OD1   1 
ATOM   7645  O  OD2   . ASP B 1 260 ? 112.208 132.018 130.517 1.00 33.86 -1 260 ASP B OD2   1 
ATOM   7646  N  N     . PHE B 1 261 ? 114.534 132.889 135.216 1.00 26.81 ?  261 PHE B N     1 
ATOM   7647  C  CA    . PHE B 1 261 ? 115.402 133.380 136.277 1.00 22.12 ?  261 PHE B CA    1 
ATOM   7648  C  C     . PHE B 1 261 ? 115.576 132.331 137.370 1.00 16.07 ?  261 PHE B C     1 
ATOM   7649  O  O     . PHE B 1 261 ? 116.693 131.873 137.643 1.00 21.75 ?  261 PHE B O     1 
ATOM   7650  C  CB    . PHE B 1 261 ? 114.797 134.674 136.838 1.00 10.28 ?  261 PHE B CB    1 
ATOM   7651  C  CG    . PHE B 1 261 ? 115.672 135.394 137.822 1.00 22.77 ?  261 PHE B CG    1 
ATOM   7652  C  CD1   . PHE B 1 261 ? 116.735 136.167 137.390 1.00 20.56 ?  261 PHE B CD1   1 
ATOM   7653  C  CD2   . PHE B 1 261 ? 115.405 135.332 139.179 1.00 23.60 ?  261 PHE B CD2   1 
ATOM   7654  C  CE1   . PHE B 1 261 ? 117.530 136.843 138.294 1.00 15.18 ?  261 PHE B CE1   1 
ATOM   7655  C  CE2   . PHE B 1 261 ? 116.195 136.005 140.085 1.00 15.89 ?  261 PHE B CE2   1 
ATOM   7656  C  CZ    . PHE B 1 261 ? 117.260 136.761 139.641 1.00 15.76 ?  261 PHE B CZ    1 
ATOM   7657  N  N     . LEU B 1 262 ? 114.460 131.900 137.963 1.00 23.93 ?  262 LEU B N     1 
ATOM   7658  C  CA    . LEU B 1 262 ? 114.528 130.896 139.018 1.00 23.77 ?  262 LEU B CA    1 
ATOM   7659  C  C     . LEU B 1 262 ? 115.100 129.588 138.491 1.00 28.49 ?  262 LEU B C     1 
ATOM   7660  O  O     . LEU B 1 262 ? 115.843 128.895 139.197 1.00 30.74 ?  262 LEU B O     1 
ATOM   7661  C  CB    . LEU B 1 262 ? 113.145 130.674 139.623 1.00 27.44 ?  262 LEU B CB    1 
ATOM   7662  C  CG    . LEU B 1 262 ? 112.536 131.877 140.340 1.00 24.56 ?  262 LEU B CG    1 
ATOM   7663  C  CD1   . LEU B 1 262 ? 111.121 131.567 140.791 1.00 26.12 ?  262 LEU B CD1   1 
ATOM   7664  C  CD2   . LEU B 1 262 ? 113.404 132.301 141.511 1.00 23.89 ?  262 LEU B CD2   1 
ATOM   7665  N  N     . ASP B 1 263 ? 114.794 129.251 137.238 1.00 34.07 ?  263 ASP B N     1 
ATOM   7666  C  CA    . ASP B 1 263 ? 115.307 128.019 136.659 1.00 25.65 ?  263 ASP B CA    1 
ATOM   7667  C  C     . ASP B 1 263 ? 116.822 128.029 136.529 1.00 29.95 ?  263 ASP B C     1 
ATOM   7668  O  O     . ASP B 1 263 ? 117.411 126.967 136.306 1.00 38.33 ?  263 ASP B O     1 
ATOM   7669  C  CB    . ASP B 1 263 ? 114.666 127.773 135.293 1.00 30.81 ?  263 ASP B CB    1 
ATOM   7670  C  CG    . ASP B 1 263 ? 113.202 127.392 135.398 1.00 37.05 ?  263 ASP B CG    1 
ATOM   7671  O  OD1   . ASP B 1 263 ? 112.777 126.957 136.489 1.00 36.66 ?  263 ASP B OD1   1 
ATOM   7672  O  OD2   . ASP B 1 263 ? 112.478 127.528 134.390 1.00 35.56 -1 263 ASP B OD2   1 
ATOM   7673  N  N     . THR B 1 264 ? 117.463 129.194 136.659 1.00 33.51 ?  264 THR B N     1 
ATOM   7674  C  CA    . THR B 1 264 ? 118.920 129.224 136.670 1.00 32.04 ?  264 THR B CA    1 
ATOM   7675  C  C     . THR B 1 264 ? 119.500 128.543 137.903 1.00 36.16 ?  264 THR B C     1 
ATOM   7676  O  O     . THR B 1 264 ? 120.657 128.112 137.868 1.00 36.90 ?  264 THR B O     1 
ATOM   7677  C  CB    . THR B 1 264 ? 119.423 130.665 136.587 1.00 33.04 ?  264 THR B CB    1 
ATOM   7678  O  OG1   . THR B 1 264 ? 118.923 131.413 137.702 1.00 36.48 ?  264 THR B OG1   1 
ATOM   7679  C  CG2   . THR B 1 264 ? 118.959 131.316 135.294 1.00 30.51 ?  264 THR B CG2   1 
ATOM   7680  N  N     . LYS B 1 265 ? 118.729 128.431 138.985 1.00 32.38 ?  265 LYS B N     1 
ATOM   7681  C  CA    . LYS B 1 265 ? 119.215 127.839 140.224 1.00 34.15 ?  265 LYS B CA    1 
ATOM   7682  C  C     . LYS B 1 265 ? 118.679 126.438 140.481 1.00 36.53 ?  265 LYS B C     1 
ATOM   7683  O  O     . LYS B 1 265 ? 119.041 125.830 141.493 1.00 39.20 ?  265 LYS B O     1 
ATOM   7684  C  CB    . LYS B 1 265 ? 118.876 128.745 141.412 1.00 33.86 ?  265 LYS B CB    1 
ATOM   7685  C  CG    . LYS B 1 265 ? 119.793 129.944 141.547 1.00 32.96 ?  265 LYS B CG    1 
ATOM   7686  C  CD    . LYS B 1 265 ? 121.250 129.524 141.540 1.00 35.96 ?  265 LYS B CD    1 
ATOM   7687  C  CE    . LYS B 1 265 ? 122.166 130.729 141.494 1.00 34.47 ?  265 LYS B CE    1 
ATOM   7688  N  NZ    . LYS B 1 265 ? 123.578 130.343 141.228 1.00 37.38 1  265 LYS B NZ    1 
ATOM   7689  N  N     . LYS B 1 266 ? 117.828 125.912 139.604 1.00 45.03 ?  266 LYS B N     1 
ATOM   7690  C  CA    . LYS B 1 266 ? 117.362 124.542 139.763 1.00 44.08 ?  266 LYS B CA    1 
ATOM   7691  C  C     . LYS B 1 266 ? 118.516 123.569 139.561 1.00 48.90 ?  266 LYS B C     1 
ATOM   7692  O  O     . LYS B 1 266 ? 119.354 123.749 138.672 1.00 50.53 ?  266 LYS B O     1 
ATOM   7693  C  CB    . LYS B 1 266 ? 116.235 124.241 138.777 1.00 44.10 ?  266 LYS B CB    1 
ATOM   7694  C  CG    . LYS B 1 266 ? 114.865 124.696 139.253 1.00 46.71 ?  266 LYS B CG    1 
ATOM   7695  C  CD    . LYS B 1 266 ? 113.765 124.220 138.319 1.00 48.45 ?  266 LYS B CD    1 
ATOM   7696  C  CE    . LYS B 1 266 ? 112.407 124.273 139.002 1.00 47.44 ?  266 LYS B CE    1 
ATOM   7697  N  NZ    . LYS B 1 266 ? 111.292 124.018 138.050 1.00 49.34 1  266 LYS B NZ    1 
ATOM   7698  N  N     . ILE B 1 267 ? 118.561 122.531 140.400 1.00 56.82 ?  267 ILE B N     1 
ATOM   7699  C  CA    . ILE B 1 267 ? 119.660 121.574 140.335 1.00 59.40 ?  267 ILE B CA    1 
ATOM   7700  C  C     . ILE B 1 267 ? 119.583 120.695 139.092 1.00 59.98 ?  267 ILE B C     1 
ATOM   7701  O  O     . ILE B 1 267 ? 120.567 120.035 138.743 1.00 58.71 ?  267 ILE B O     1 
ATOM   7702  C  CB    . ILE B 1 267 ? 119.717 120.739 141.632 1.00 60.41 ?  267 ILE B CB    1 
ATOM   7703  C  CG1   . ILE B 1 267 ? 118.318 120.364 142.153 1.00 59.80 ?  267 ILE B CG1   1 
ATOM   7704  C  CG2   . ILE B 1 267 ? 120.493 121.487 142.708 1.00 58.18 ?  267 ILE B CG2   1 
ATOM   7705  C  CD1   . ILE B 1 267 ? 117.469 119.498 141.240 1.00 57.74 ?  267 ILE B CD1   1 
ATOM   7706  N  N     . SER B 1 268 ? 118.438 120.670 138.412 1.00 62.10 ?  268 SER B N     1 
ATOM   7707  C  CA    . SER B 1 268 ? 118.260 119.901 137.189 1.00 64.31 ?  268 SER B CA    1 
ATOM   7708  C  C     . SER B 1 268 ? 118.390 120.758 135.937 1.00 65.31 ?  268 SER B C     1 
ATOM   7709  O  O     . SER B 1 268 ? 118.120 120.272 134.834 1.00 66.20 ?  268 SER B O     1 
ATOM   7710  C  CB    . SER B 1 268 ? 116.900 119.201 137.202 1.00 67.03 ?  268 SER B CB    1 
ATOM   7711  O  OG    . SER B 1 268 ? 115.853 120.130 137.428 1.00 64.20 ?  268 SER B OG    1 
ATOM   7712  N  N     . ALA B 1 269 ? 118.793 122.018 136.083 1.00 66.97 ?  269 ALA B N     1 
ATOM   7713  C  CA    . ALA B 1 269 ? 118.870 122.924 134.946 1.00 67.58 ?  269 ALA B CA    1 
ATOM   7714  C  C     . ALA B 1 269 ? 119.967 122.499 133.977 1.00 67.63 ?  269 ALA B C     1 
ATOM   7715  O  O     . ALA B 1 269 ? 121.018 121.988 134.372 1.00 65.97 ?  269 ALA B O     1 
ATOM   7716  C  CB    . ALA B 1 269 ? 119.121 124.354 135.422 1.00 65.51 ?  269 ALA B CB    1 
ATOM   7717  N  N     . ASP B 1 270 ? 119.709 122.720 132.690 1.00 73.26 ?  270 ASP B N     1 
ATOM   7718  C  CA    . ASP B 1 270 ? 120.689 122.421 131.661 1.00 73.45 ?  270 ASP B CA    1 
ATOM   7719  C  C     . ASP B 1 270 ? 121.840 123.424 131.715 1.00 73.74 ?  270 ASP B C     1 
ATOM   7720  O  O     . ASP B 1 270 ? 121.727 124.511 132.287 1.00 74.05 ?  270 ASP B O     1 
ATOM   7721  C  CB    . ASP B 1 270 ? 120.035 122.439 130.278 1.00 73.73 ?  270 ASP B CB    1 
ATOM   7722  C  CG    . ASP B 1 270 ? 120.772 121.578 129.272 1.00 75.07 ?  270 ASP B CG    1 
ATOM   7723  O  OD1   . ASP B 1 270 ? 121.963 121.850 129.011 1.00 75.22 ?  270 ASP B OD1   1 
ATOM   7724  O  OD2   . ASP B 1 270 ? 120.160 120.626 128.742 1.00 74.14 -1 270 ASP B OD2   1 
ATOM   7725  N  N     . GLU B 1 271 ? 122.964 123.039 131.105 1.00 73.75 ?  271 GLU B N     1 
ATOM   7726  C  CA    . GLU B 1 271 ? 124.156 123.880 131.153 1.00 73.72 ?  271 GLU B CA    1 
ATOM   7727  C  C     . GLU B 1 271 ? 123.951 125.207 130.429 1.00 72.95 ?  271 GLU B C     1 
ATOM   7728  O  O     . GLU B 1 271 ? 124.567 126.212 130.801 1.00 72.44 ?  271 GLU B O     1 
ATOM   7729  C  CB    . GLU B 1 271 ? 125.350 123.133 130.560 1.00 72.64 ?  271 GLU B CB    1 
ATOM   7730  C  CG    . GLU B 1 271 ? 125.962 122.107 131.499 1.00 73.86 ?  271 GLU B CG    1 
ATOM   7731  C  CD    . GLU B 1 271 ? 126.535 122.736 132.755 1.00 74.42 ?  271 GLU B CD    1 
ATOM   7732  O  OE1   . GLU B 1 271 ? 127.094 123.848 132.664 1.00 73.57 ?  271 GLU B OE1   1 
ATOM   7733  O  OE2   . GLU B 1 271 ? 126.424 122.117 133.835 1.00 73.53 -1 271 GLU B OE2   1 
ATOM   7734  N  N     . ASP B 1 272 ? 123.099 125.234 129.404 1.00 69.22 ?  272 ASP B N     1 
ATOM   7735  C  CA    . ASP B 1 272 ? 122.837 126.478 128.689 1.00 70.00 ?  272 ASP B CA    1 
ATOM   7736  C  C     . ASP B 1 272 ? 121.967 127.443 129.484 1.00 69.56 ?  272 ASP B C     1 
ATOM   7737  O  O     . ASP B 1 272 ? 121.842 128.606 129.087 1.00 68.28 ?  272 ASP B O     1 
ATOM   7738  C  CB    . ASP B 1 272 ? 122.184 126.180 127.337 1.00 69.68 ?  272 ASP B CB    1 
ATOM   7739  C  CG    . ASP B 1 272 ? 120.740 125.734 127.468 1.00 72.04 ?  272 ASP B CG    1 
ATOM   7740  O  OD1   . ASP B 1 272 ? 120.396 125.109 128.494 1.00 71.80 ?  272 ASP B OD1   1 
ATOM   7741  O  OD2   . ASP B 1 272 ? 119.948 126.005 126.542 1.00 69.21 -1 272 ASP B OD2   1 
ATOM   7742  N  N     . VAL B 1 273 ? 121.361 126.991 130.583 1.00 62.08 ?  273 VAL B N     1 
ATOM   7743  C  CA    . VAL B 1 273 ? 120.534 127.832 131.434 1.00 62.78 ?  273 VAL B CA    1 
ATOM   7744  C  C     . VAL B 1 273 ? 121.134 127.993 132.826 1.00 61.16 ?  273 VAL B C     1 
ATOM   7745  O  O     . VAL B 1 273 ? 121.057 129.075 133.418 1.00 60.96 ?  273 VAL B O     1 
ATOM   7746  C  CB    . VAL B 1 273 ? 119.093 127.280 131.524 1.00 63.68 ?  273 VAL B CB    1 
ATOM   7747  C  CG1   . VAL B 1 273 ? 118.258 128.093 132.503 1.00 61.00 ?  273 VAL B CG1   1 
ATOM   7748  C  CG2   . VAL B 1 273 ? 118.445 127.268 130.149 1.00 62.41 ?  273 VAL B CG2   1 
ATOM   7749  N  N     . ARG B 1 274 ? 121.743 126.934 133.359 1.00 61.27 ?  274 ARG B N     1 
ATOM   7750  C  CA    . ARG B 1 274 ? 122.260 126.960 134.720 1.00 60.75 ?  274 ARG B CA    1 
ATOM   7751  C  C     . ARG B 1 274 ? 123.331 128.033 134.883 1.00 59.70 ?  274 ARG B C     1 
ATOM   7752  O  O     . ARG B 1 274 ? 124.220 128.186 134.040 1.00 62.45 ?  274 ARG B O     1 
ATOM   7753  C  CB    . ARG B 1 274 ? 122.829 125.590 135.093 1.00 62.89 ?  274 ARG B CB    1 
ATOM   7754  C  CG    . ARG B 1 274 ? 124.028 125.640 136.029 1.00 58.68 ?  274 ARG B CG    1 
ATOM   7755  C  CD    . ARG B 1 274 ? 124.012 124.493 137.025 1.00 61.77 ?  274 ARG B CD    1 
ATOM   7756  N  NE    . ARG B 1 274 ? 124.157 123.199 136.369 1.00 65.06 ?  274 ARG B NE    1 
ATOM   7757  C  CZ    . ARG B 1 274 ? 123.283 122.208 136.464 1.00 66.11 ?  274 ARG B CZ    1 
ATOM   7758  N  NH1   . ARG B 1 274 ? 122.184 122.322 137.192 1.00 63.75 1  274 ARG B NH1   1 
ATOM   7759  N  NH2   . ARG B 1 274 ? 123.516 121.071 135.815 1.00 63.75 ?  274 ARG B NH2   1 
ATOM   7760  N  N     . VAL B 1 275 ? 123.232 128.782 135.977 1.00 47.00 ?  275 VAL B N     1 
ATOM   7761  C  CA    . VAL B 1 275 ? 124.217 129.782 136.365 1.00 44.89 ?  275 VAL B CA    1 
ATOM   7762  C  C     . VAL B 1 275 ? 124.653 129.465 137.789 1.00 48.71 ?  275 VAL B C     1 
ATOM   7763  O  O     . VAL B 1 275 ? 123.807 129.288 138.673 1.00 51.14 ?  275 VAL B O     1 
ATOM   7764  C  CB    . VAL B 1 275 ? 123.643 131.207 136.266 1.00 45.84 ?  275 VAL B CB    1 
ATOM   7765  C  CG1   . VAL B 1 275 ? 124.521 132.173 137.013 1.00 45.29 ?  275 VAL B CG1   1 
ATOM   7766  C  CG2   . VAL B 1 275 ? 123.501 131.625 134.811 1.00 43.95 ?  275 VAL B CG2   1 
ATOM   7767  N  N     . LYS B 1 276 ? 125.968 129.392 138.014 1.00 46.32 ?  276 LYS B N     1 
ATOM   7768  C  CA    . LYS B 1 276 ? 126.488 128.839 139.257 1.00 47.39 ?  276 LYS B CA    1 
ATOM   7769  C  C     . LYS B 1 276 ? 127.285 129.810 140.120 1.00 45.61 ?  276 LYS B C     1 
ATOM   7770  O  O     . LYS B 1 276 ? 127.385 129.576 141.330 1.00 51.16 ?  276 LYS B O     1 
ATOM   7771  C  CB    . LYS B 1 276 ? 127.357 127.603 138.964 1.00 48.20 ?  276 LYS B CB    1 
ATOM   7772  C  CG    . LYS B 1 276 ? 128.777 127.910 138.532 1.00 47.46 ?  276 LYS B CG    1 
ATOM   7773  C  CD    . LYS B 1 276 ? 129.381 126.750 137.761 1.00 50.60 ?  276 LYS B CD    1 
ATOM   7774  C  CE    . LYS B 1 276 ? 128.629 126.514 136.462 1.00 49.82 ?  276 LYS B CE    1 
ATOM   7775  N  NZ    . LYS B 1 276 ? 128.380 127.789 135.738 1.00 48.35 1  276 LYS B NZ    1 
ATOM   7776  N  N     . THR B 1 277 ? 127.855 130.875 139.558 1.00 37.24 ?  277 THR B N     1 
ATOM   7777  C  CA    . THR B 1 277 ? 128.595 131.850 140.350 1.00 36.87 ?  277 THR B CA    1 
ATOM   7778  C  C     . THR B 1 277 ? 127.846 133.159 140.549 1.00 38.11 ?  277 THR B C     1 
ATOM   7779  O  O     . THR B 1 277 ? 128.423 134.113 141.082 1.00 42.20 ?  277 THR B O     1 
ATOM   7780  C  CB    . THR B 1 277 ? 129.962 132.147 139.715 1.00 39.89 ?  277 THR B CB    1 
ATOM   7781  O  OG1   . THR B 1 277 ? 129.833 133.222 138.775 1.00 37.56 ?  277 THR B OG1   1 
ATOM   7782  C  CG2   . THR B 1 277 ? 130.506 130.922 139.014 1.00 40.45 ?  277 THR B CG2   1 
ATOM   7783  N  N     . LEU B 1 278 ? 126.584 133.234 140.144 1.00 29.21 ?  278 LEU B N     1 
ATOM   7784  C  CA    . LEU B 1 278 ? 125.790 134.452 140.247 1.00 29.10 ?  278 LEU B CA    1 
ATOM   7785  C  C     . LEU B 1 278 ? 124.586 134.172 141.137 1.00 23.31 ?  278 LEU B C     1 
ATOM   7786  O  O     . LEU B 1 278 ? 123.684 133.422 140.750 1.00 29.21 ?  278 LEU B O     1 
ATOM   7787  C  CB    . LEU B 1 278 ? 125.359 134.935 138.864 1.00 26.18 ?  278 LEU B CB    1 
ATOM   7788  C  CG    . LEU B 1 278 ? 124.630 136.267 138.723 1.00 26.72 ?  278 LEU B CG    1 
ATOM   7789  C  CD1   . LEU B 1 278 ? 125.616 137.413 138.710 1.00 23.26 ?  278 LEU B CD1   1 
ATOM   7790  C  CD2   . LEU B 1 278 ? 123.798 136.262 137.452 1.00 23.82 ?  278 LEU B CD2   1 
ATOM   7791  N  N     . SER B 1 279 ? 124.577 134.771 142.323 1.00 23.24 ?  279 SER B N     1 
ATOM   7792  C  CA    . SER B 1 279 ? 123.432 134.654 143.213 1.00 18.49 ?  279 SER B CA    1 
ATOM   7793  C  C     . SER B 1 279 ? 122.217 135.333 142.595 1.00 19.07 ?  279 SER B C     1 
ATOM   7794  O  O     . SER B 1 279 ? 122.337 136.259 141.790 1.00 29.86 ?  279 SER B O     1 
ATOM   7795  C  CB    . SER B 1 279 ? 123.746 135.276 144.571 1.00 17.19 ?  279 SER B CB    1 
ATOM   7796  O  OG    . SER B 1 279 ? 124.858 134.642 145.176 1.00 23.76 ?  279 SER B OG    1 
ATOM   7797  N  N     . ILE B 1 280 ? 121.033 134.860 142.966 1.00 20.84 ?  280 ILE B N     1 
ATOM   7798  C  CA    . ILE B 1 280 ? 119.792 135.377 142.411 1.00 19.36 ?  280 ILE B CA    1 
ATOM   7799  C  C     . ILE B 1 280 ? 118.936 135.926 143.542 1.00 20.82 ?  280 ILE B C     1 
ATOM   7800  O  O     . ILE B 1 280 ? 118.904 135.366 144.644 1.00 24.93 ?  280 ILE B O     1 
ATOM   7801  C  CB    . ILE B 1 280 ? 119.029 134.308 141.599 1.00 16.70 ?  280 ILE B CB    1 
ATOM   7802  C  CG1   . ILE B 1 280 ? 118.447 133.220 142.498 1.00 22.49 ?  280 ILE B CG1   1 
ATOM   7803  C  CG2   . ILE B 1 280 ? 119.950 133.657 140.597 1.00 25.14 ?  280 ILE B CG2   1 
ATOM   7804  C  CD1   . ILE B 1 280 ? 117.306 132.464 141.852 1.00 21.68 ?  280 ILE B CD1   1 
ATOM   7805  N  N     . GLY B 1 281 ? 118.279 137.045 143.276 1.00 11.91 ?  281 GLY B N     1 
ATOM   7806  C  CA    . GLY B 1 281 ? 117.333 137.614 144.211 1.00 6.43  ?  281 GLY B CA    1 
ATOM   7807  C  C     . GLY B 1 281 ? 116.052 137.986 143.499 1.00 8.98  ?  281 GLY B C     1 
ATOM   7808  O  O     . GLY B 1 281 ? 116.053 138.358 142.327 1.00 18.68 ?  281 GLY B O     1 
ATOM   7809  N  N     . VAL B 1 282 ? 114.947 137.872 144.227 1.00 8.40  ?  282 VAL B N     1 
ATOM   7810  C  CA    . VAL B 1 282 ? 113.620 138.151 143.694 1.00 14.89 ?  282 VAL B CA    1 
ATOM   7811  C  C     . VAL B 1 282 ? 113.010 139.289 144.497 1.00 11.81 ?  282 VAL B C     1 
ATOM   7812  O  O     . VAL B 1 282 ? 112.991 139.245 145.732 1.00 18.21 ?  282 VAL B O     1 
ATOM   7813  C  CB    . VAL B 1 282 ? 112.720 136.902 143.730 1.00 13.09 ?  282 VAL B CB    1 
ATOM   7814  C  CG1   . VAL B 1 282 ? 111.271 137.284 143.512 1.00 15.57 ?  282 VAL B CG1   1 
ATOM   7815  C  CG2   . VAL B 1 282 ? 113.164 135.910 142.673 1.00 19.32 ?  282 VAL B CG2   1 
ATOM   7816  N  N     . VAL B 1 283 ? 112.525 140.307 143.796 1.00 7.35  ?  283 VAL B N     1 
ATOM   7817  C  CA    . VAL B 1 283 ? 111.892 141.465 144.412 1.00 10.05 ?  283 VAL B CA    1 
ATOM   7818  C  C     . VAL B 1 283 ? 110.385 141.283 144.309 1.00 12.37 ?  283 VAL B C     1 
ATOM   7819  O  O     . VAL B 1 283 ? 109.830 141.234 143.205 1.00 22.54 ?  283 VAL B O     1 
ATOM   7820  C  CB    . VAL B 1 283 ? 112.346 142.770 143.743 1.00 6.35  ?  283 VAL B CB    1 
ATOM   7821  C  CG1   . VAL B 1 283 ? 111.768 143.966 144.474 1.00 9.67  ?  283 VAL B CG1   1 
ATOM   7822  C  CG2   . VAL B 1 283 ? 113.862 142.836 143.713 1.00 8.67  ?  283 VAL B CG2   1 
ATOM   7823  N  N     . ILE B 1 284 ? 109.724 141.184 145.456 1.00 17.09 ?  284 ILE B N     1 
ATOM   7824  C  CA    . ILE B 1 284 ? 108.304 140.858 145.533 1.00 17.92 ?  284 ILE B CA    1 
ATOM   7825  C  C     . ILE B 1 284 ? 107.561 142.092 146.039 1.00 17.41 ?  284 ILE B C     1 
ATOM   7826  O  O     . ILE B 1 284 ? 107.678 142.444 147.224 1.00 19.60 ?  284 ILE B O     1 
ATOM   7827  C  CB    . ILE B 1 284 ? 108.052 139.649 146.442 1.00 12.85 ?  284 ILE B CB    1 
ATOM   7828  C  CG1   . ILE B 1 284 ? 108.974 138.491 146.057 1.00 13.68 ?  284 ILE B CG1   1 
ATOM   7829  C  CG2   . ILE B 1 284 ? 106.595 139.227 146.371 1.00 17.19 ?  284 ILE B CG2   1 
ATOM   7830  C  CD1   . ILE B 1 284 ? 108.692 137.211 146.805 1.00 15.71 ?  284 ILE B CD1   1 
ATOM   7831  N  N     . PRO B 1 285 ? 106.795 142.777 145.197 1.00 22.30 ?  285 PRO B N     1 
ATOM   7832  C  CA    . PRO B 1 285 ? 105.906 143.828 145.698 1.00 25.67 ?  285 PRO B CA    1 
ATOM   7833  C  C     . PRO B 1 285 ? 104.754 143.237 146.496 1.00 25.21 ?  285 PRO B C     1 
ATOM   7834  O  O     . PRO B 1 285 ? 104.482 142.036 146.456 1.00 24.82 ?  285 PRO B O     1 
ATOM   7835  C  CB    . PRO B 1 285 ? 105.402 144.513 144.422 1.00 23.16 ?  285 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 1 285 ? 106.366 144.108 143.353 1.00 19.61 ?  285 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 1 285 ? 106.830 142.738 143.726 1.00 16.49 ?  285 PRO B CD    1 
ATOM   7838  N  N     . ASP B 1 286 ? 104.076 144.112 147.242 1.00 29.11 ?  286 ASP B N     1 
ATOM   7839  C  CA    . ASP B 1 286 ? 102.912 143.684 148.010 1.00 23.66 ?  286 ASP B CA    1 
ATOM   7840  C  C     . ASP B 1 286 ? 101.789 143.177 147.119 1.00 30.67 ?  286 ASP B C     1 
ATOM   7841  O  O     . ASP B 1 286 ? 100.950 142.396 147.582 1.00 32.81 ?  286 ASP B O     1 
ATOM   7842  C  CB    . ASP B 1 286 ? 102.404 144.833 148.882 1.00 26.22 ?  286 ASP B CB    1 
ATOM   7843  C  CG    . ASP B 1 286 ? 102.829 144.699 150.329 1.00 37.25 ?  286 ASP B CG    1 
ATOM   7844  O  OD1   . ASP B 1 286 ? 103.975 144.267 150.575 1.00 38.58 ?  286 ASP B OD1   1 
ATOM   7845  O  OD2   . ASP B 1 286 ? 102.020 145.030 151.220 1.00 39.34 -1 286 ASP B OD2   1 
ATOM   7846  N  N     . LYS B 1 287 ? 101.754 143.606 145.854 1.00 33.03 ?  287 LYS B N     1 
ATOM   7847  C  CA    . LYS B 1 287 ? 100.722 143.136 144.937 1.00 25.93 ?  287 LYS B CA    1 
ATOM   7848  C  C     . LYS B 1 287 ? 100.812 141.631 144.722 1.00 26.93 ?  287 LYS B C     1 
ATOM   7849  O  O     . LYS B 1 287 ? 99.786  140.943 144.670 1.00 33.99 ?  287 LYS B O     1 
ATOM   7850  C  CB    . LYS B 1 287 ? 100.828 143.874 143.604 1.00 27.63 ?  287 LYS B CB    1 
ATOM   7851  C  CG    . LYS B 1 287 ? 99.646  143.647 142.680 1.00 27.80 ?  287 LYS B CG    1 
ATOM   7852  C  CD    . LYS B 1 287 ? 98.338  143.959 143.386 1.00 32.66 ?  287 LYS B CD    1 
ATOM   7853  C  CE    . LYS B 1 287 ? 97.159  143.865 142.436 1.00 31.91 ?  287 LYS B CE    1 
ATOM   7854  N  NZ    . LYS B 1 287 ? 95.897  144.317 143.081 1.00 33.82 1  287 LYS B NZ    1 
ATOM   7855  N  N     . PHE B 1 288 ? 102.029 141.101 144.582 1.00 26.58 ?  288 PHE B N     1 
ATOM   7856  C  CA    . PHE B 1 288 ? 102.186 139.664 144.379 1.00 23.20 ?  288 PHE B CA    1 
ATOM   7857  C  C     . PHE B 1 288 ? 101.707 138.878 145.592 1.00 22.50 ?  288 PHE B C     1 
ATOM   7858  O  O     . PHE B 1 288 ? 101.038 137.847 145.450 1.00 30.53 ?  288 PHE B O     1 
ATOM   7859  C  CB    . PHE B 1 288 ? 103.643 139.329 144.069 1.00 27.79 ?  288 PHE B CB    1 
ATOM   7860  C  CG    . PHE B 1 288 ? 103.870 137.885 143.731 1.00 26.67 ?  288 PHE B CG    1 
ATOM   7861  C  CD1   . PHE B 1 288 ? 103.654 137.421 142.446 1.00 23.90 ?  288 PHE B CD1   1 
ATOM   7862  C  CD2   . PHE B 1 288 ? 104.290 136.988 144.699 1.00 23.29 ?  288 PHE B CD2   1 
ATOM   7863  C  CE1   . PHE B 1 288 ? 103.856 136.093 142.131 1.00 28.59 ?  288 PHE B CE1   1 
ATOM   7864  C  CE2   . PHE B 1 288 ? 104.492 135.659 144.391 1.00 24.98 ?  288 PHE B CE2   1 
ATOM   7865  C  CZ    . PHE B 1 288 ? 104.278 135.212 143.105 1.00 26.34 ?  288 PHE B CZ    1 
ATOM   7866  N  N     . VAL B 1 289 ? 102.047 139.345 146.794 1.00 25.75 ?  289 VAL B N     1 
ATOM   7867  C  CA    . VAL B 1 289 ? 101.602 138.668 148.007 1.00 26.07 ?  289 VAL B CA    1 
ATOM   7868  C  C     . VAL B 1 289 ? 100.087 138.745 148.133 1.00 26.59 ?  289 VAL B C     1 
ATOM   7869  O  O     . VAL B 1 289 ? 99.438  137.790 148.572 1.00 29.88 ?  289 VAL B O     1 
ATOM   7870  C  CB    . VAL B 1 289 ? 102.306 139.264 149.239 1.00 31.81 ?  289 VAL B CB    1 
ATOM   7871  C  CG1   . VAL B 1 289 ? 101.983 138.452 150.481 1.00 23.07 ?  289 VAL B CG1   1 
ATOM   7872  C  CG2   . VAL B 1 289 ? 103.808 139.327 149.010 1.00 25.12 ?  289 VAL B CG2   1 
ATOM   7873  N  N     . GLU B 1 290 ? 99.499  139.881 147.753 1.00 34.76 ?  290 GLU B N     1 
ATOM   7874  C  CA    . GLU B 1 290 ? 98.046  140.012 147.781 1.00 30.92 ?  290 GLU B CA    1 
ATOM   7875  C  C     . GLU B 1 290 ? 97.384  139.048 146.802 1.00 34.54 ?  290 GLU B C     1 
ATOM   7876  O  O     . GLU B 1 290 ? 96.378  138.409 147.131 1.00 39.59 ?  290 GLU B O     1 
ATOM   7877  C  CB    . GLU B 1 290 ? 97.651  141.456 147.475 1.00 28.23 ?  290 GLU B CB    1 
ATOM   7878  C  CG    . GLU B 1 290 ? 96.312  141.613 146.776 1.00 37.04 ?  290 GLU B CG    1 
ATOM   7879  C  CD    . GLU B 1 290 ? 95.924  143.065 146.588 1.00 41.41 ?  290 GLU B CD    1 
ATOM   7880  O  OE1   . GLU B 1 290 ? 96.010  143.836 147.566 1.00 42.37 ?  290 GLU B OE1   1 
ATOM   7881  O  OE2   . GLU B 1 290 ? 95.535  143.437 145.461 1.00 38.39 -1 290 GLU B OE2   1 
ATOM   7882  N  N     . LEU B 1 291 ? 97.939  138.928 145.593 1.00 27.28 ?  291 LEU B N     1 
ATOM   7883  C  CA    . LEU B 1 291 ? 97.384  138.006 144.606 1.00 25.18 ?  291 LEU B CA    1 
ATOM   7884  C  C     . LEU B 1 291 ? 97.507  136.559 145.067 1.00 32.91 ?  291 LEU B C     1 
ATOM   7885  O  O     . LEU B 1 291 ? 96.574  135.766 144.892 1.00 37.34 ?  291 LEU B O     1 
ATOM   7886  C  CB    . LEU B 1 291 ? 98.079  138.196 143.257 1.00 29.43 ?  291 LEU B CB    1 
ATOM   7887  C  CG    . LEU B 1 291 ? 97.847  139.526 142.539 1.00 29.44 ?  291 LEU B CG    1 
ATOM   7888  C  CD1   . LEU B 1 291 ? 98.958  139.791 141.540 1.00 26.20 ?  291 LEU B CD1   1 
ATOM   7889  C  CD2   . LEU B 1 291 ? 96.493  139.539 141.855 1.00 32.36 ?  291 LEU B CD2   1 
ATOM   7890  N  N     . ALA B 1 292 ? 98.654  136.192 145.643 1.00 32.40 ?  292 ALA B N     1 
ATOM   7891  C  CA    . ALA B 1 292 ? 98.827  134.835 146.150 1.00 27.35 ?  292 ALA B CA    1 
ATOM   7892  C  C     . ALA B 1 292 ? 97.882  134.555 147.313 1.00 29.21 ?  292 ALA B C     1 
ATOM   7893  O  O     . ALA B 1 292 ? 97.340  133.451 147.428 1.00 36.30 ?  292 ALA B O     1 
ATOM   7894  C  CB    . ALA B 1 292 ? 100.278 134.611 146.569 1.00 27.19 ?  292 ALA B CB    1 
ATOM   7895  N  N     . ARG B 1 293 ? 97.679  135.544 148.185 1.00 28.11 ?  293 ARG B N     1 
ATOM   7896  C  CA    . ARG B 1 293 ? 96.783  135.370 149.322 1.00 28.07 ?  293 ARG B CA    1 
ATOM   7897  C  C     . ARG B 1 293 ? 95.350  135.126 148.867 1.00 35.25 ?  293 ARG B C     1 
ATOM   7898  O  O     . ARG B 1 293 ? 94.654  134.265 149.416 1.00 39.63 ?  293 ARG B O     1 
ATOM   7899  C  CB    . ARG B 1 293 ? 96.862  136.598 150.229 1.00 29.39 ?  293 ARG B CB    1 
ATOM   7900  C  CG    . ARG B 1 293 ? 95.731  136.731 151.230 1.00 31.61 ?  293 ARG B CG    1 
ATOM   7901  C  CD    . ARG B 1 293 ? 95.723  138.121 151.838 1.00 32.58 ?  293 ARG B CD    1 
ATOM   7902  N  NE    . ARG B 1 293 ? 97.061  138.535 152.243 1.00 38.76 ?  293 ARG B NE    1 
ATOM   7903  C  CZ    . ARG B 1 293 ? 97.638  139.669 151.871 1.00 37.05 ?  293 ARG B CZ    1 
ATOM   7904  N  NH1   . ARG B 1 293 ? 97.018  140.537 151.090 1.00 36.91 1  293 ARG B NH1   1 
ATOM   7905  N  NH2   . ARG B 1 293 ? 98.872  139.935 152.289 1.00 29.92 ?  293 ARG B NH2   1 
ATOM   7906  N  N     . GLU B 1 294 ? 94.897  135.867 147.859 1.00 44.02 ?  294 GLU B N     1 
ATOM   7907  C  CA    . GLU B 1 294 ? 93.546  135.723 147.336 1.00 41.02 ?  294 GLU B CA    1 
ATOM   7908  C  C     . GLU B 1 294 ? 93.418  134.590 146.327 1.00 42.10 ?  294 GLU B C     1 
ATOM   7909  O  O     . GLU B 1 294 ? 92.310  134.341 145.841 1.00 46.91 ?  294 GLU B O     1 
ATOM   7910  C  CB    . GLU B 1 294 ? 93.093  137.038 146.699 1.00 37.63 ?  294 GLU B CB    1 
ATOM   7911  C  CG    . GLU B 1 294 ? 93.103  138.218 147.656 1.00 42.57 ?  294 GLU B CG    1 
ATOM   7912  C  CD    . GLU B 1 294 ? 92.868  139.542 146.955 1.00 48.77 ?  294 GLU B CD    1 
ATOM   7913  O  OE1   . GLU B 1 294 ? 92.757  139.547 145.712 1.00 48.12 ?  294 GLU B OE1   1 
ATOM   7914  O  OE2   . GLU B 1 294 ? 92.795  140.578 147.649 1.00 45.21 -1 294 GLU B OE2   1 
ATOM   7915  N  N     . ASP B 1 295 ? 94.520  133.915 145.997 1.00 39.29 ?  295 ASP B N     1 
ATOM   7916  C  CA    . ASP B 1 295 ? 94.550  132.799 145.052 1.00 41.69 ?  295 ASP B CA    1 
ATOM   7917  C  C     . ASP B 1 295 ? 94.105  133.209 143.652 1.00 45.58 ?  295 ASP B C     1 
ATOM   7918  O  O     . ASP B 1 295 ? 93.767  132.351 142.829 1.00 46.25 ?  295 ASP B O     1 
ATOM   7919  C  CB    . ASP B 1 295 ? 93.706  131.620 145.550 1.00 45.70 ?  295 ASP B CB    1 
ATOM   7920  C  CG    . ASP B 1 295 ? 94.351  130.279 145.260 1.00 50.22 ?  295 ASP B CG    1 
ATOM   7921  O  OD1   . ASP B 1 295 ? 94.100  129.321 146.019 1.00 47.79 ?  295 ASP B OD1   1 
ATOM   7922  O  OD2   . ASP B 1 295 ? 95.110  130.185 144.272 1.00 47.83 -1 295 ASP B OD2   1 
ATOM   7923  N  N     . LYS B 1 296 ? 94.096  134.508 143.363 1.00 45.81 ?  296 LYS B N     1 
ATOM   7924  C  CA    . LYS B 1 296 ? 93.767  134.989 142.031 1.00 44.99 ?  296 LYS B CA    1 
ATOM   7925  C  C     . LYS B 1 296 ? 94.981  134.849 141.124 1.00 46.34 ?  296 LYS B C     1 
ATOM   7926  O  O     . LYS B 1 296 ? 96.096  135.214 141.508 1.00 48.28 ?  296 LYS B O     1 
ATOM   7927  C  CB    . LYS B 1 296 ? 93.311  136.446 142.089 1.00 45.13 ?  296 LYS B CB    1 
ATOM   7928  C  CG    . LYS B 1 296 ? 92.041  136.666 142.894 1.00 46.13 ?  296 LYS B CG    1 
ATOM   7929  C  CD    . LYS B 1 296 ? 91.676  138.139 142.963 1.00 46.16 ?  296 LYS B CD    1 
ATOM   7930  C  CE    . LYS B 1 296 ? 90.354  138.347 143.684 1.00 47.56 ?  296 LYS B CE    1 
ATOM   7931  N  NZ    . LYS B 1 296 ? 90.113  139.782 144.002 1.00 45.77 1  296 LYS B NZ    1 
ATOM   7932  N  N     . ALA B 1 297 ? 94.766  134.314 139.923 1.00 44.65 ?  297 ALA B N     1 
ATOM   7933  C  CA    . ALA B 1 297 ? 95.863  134.123 138.984 1.00 43.38 ?  297 ALA B CA    1 
ATOM   7934  C  C     . ALA B 1 297 ? 96.501  135.460 138.634 1.00 42.38 ?  297 ALA B C     1 
ATOM   7935  O  O     . ALA B 1 297 ? 95.809  136.428 138.304 1.00 44.72 ?  297 ALA B O     1 
ATOM   7936  C  CB    . ALA B 1 297 ? 95.362  133.426 137.720 1.00 42.71 ?  297 ALA B CB    1 
ATOM   7937  N  N     . ALA B 1 298 ? 97.826  135.511 138.709 1.00 34.57 ?  298 ALA B N     1 
ATOM   7938  C  CA    . ALA B 1 298 ? 98.556  136.745 138.480 1.00 33.18 ?  298 ALA B CA    1 
ATOM   7939  C  C     . ALA B 1 298 ? 99.069  136.802 137.046 1.00 35.87 ?  298 ALA B C     1 
ATOM   7940  O  O     . ALA B 1 298 ? 98.952  135.849 136.274 1.00 40.21 ?  298 ALA B O     1 
ATOM   7941  C  CB    . ALA B 1 298 ? 99.715  136.872 139.469 1.00 34.50 ?  298 ALA B CB    1 
ATOM   7942  N  N     . TYR B 1 299 ? 99.656  137.941 136.693 1.00 36.18 ?  299 TYR B N     1 
ATOM   7943  C  CA    . TYR B 1 299 ? 100.207 138.145 135.362 1.00 25.69 ?  299 TYR B CA    1 
ATOM   7944  C  C     . TYR B 1 299 ? 101.621 138.687 135.480 1.00 27.90 ?  299 TYR B C     1 
ATOM   7945  O  O     . TYR B 1 299 ? 101.849 139.698 136.152 1.00 34.61 ?  299 TYR B O     1 
ATOM   7946  C  CB    . TYR B 1 299 ? 99.340  139.107 134.547 1.00 30.33 ?  299 TYR B CB    1 
ATOM   7947  C  CG    . TYR B 1 299 ? 98.092  138.473 133.975 1.00 31.78 ?  299 TYR B CG    1 
ATOM   7948  C  CD1   . TYR B 1 299 ? 98.157  137.647 132.861 1.00 33.34 ?  299 TYR B CD1   1 
ATOM   7949  C  CD2   . TYR B 1 299 ? 96.848  138.710 134.542 1.00 32.79 ?  299 TYR B CD2   1 
ATOM   7950  C  CE1   . TYR B 1 299 ? 97.021  137.069 132.334 1.00 33.86 ?  299 TYR B CE1   1 
ATOM   7951  C  CE2   . TYR B 1 299 ? 95.704  138.138 134.022 1.00 33.08 ?  299 TYR B CE2   1 
ATOM   7952  C  CZ    . TYR B 1 299 ? 95.797  137.317 132.917 1.00 35.07 ?  299 TYR B CZ    1 
ATOM   7953  O  OH    . TYR B 1 299 ? 94.660  136.744 132.393 1.00 37.22 ?  299 TYR B OH    1 
ATOM   7954  N  N     . VAL B 1 300 ? 102.564 138.015 134.838 1.00 29.64 ?  300 VAL B N     1 
ATOM   7955  C  CA    . VAL B 1 300 ? 103.912 138.543 134.677 1.00 22.32 ?  300 VAL B CA    1 
ATOM   7956  C  C     . VAL B 1 300 ? 103.943 139.331 133.378 1.00 25.64 ?  300 VAL B C     1 
ATOM   7957  O  O     . VAL B 1 300 ? 103.190 139.044 132.446 1.00 30.12 ?  300 VAL B O     1 
ATOM   7958  C  CB    . VAL B 1 300 ? 104.971 137.421 134.694 1.00 24.45 ?  300 VAL B CB    1 
ATOM   7959  C  CG1   . VAL B 1 300 ? 105.168 136.904 136.108 1.00 23.16 ?  300 VAL B CG1   1 
ATOM   7960  C  CG2   . VAL B 1 300 ? 104.568 136.294 133.758 1.00 26.14 ?  300 VAL B CG2   1 
ATOM   7961  N  N     . PHE B 1 301 ? 104.806 140.336 133.307 1.00 25.84 ?  301 PHE B N     1 
ATOM   7962  C  CA    . PHE B 1 301 ? 104.725 141.316 132.239 1.00 20.81 ?  301 PHE B CA    1 
ATOM   7963  C  C     . PHE B 1 301 ? 106.013 141.370 131.432 1.00 28.11 ?  301 PHE B C     1 
ATOM   7964  O  O     . PHE B 1 301 ? 107.099 141.044 131.918 1.00 29.52 ?  301 PHE B O     1 
ATOM   7965  C  CB    . PHE B 1 301 ? 104.404 142.705 132.798 1.00 24.66 ?  301 PHE B CB    1 
ATOM   7966  C  CG    . PHE B 1 301 ? 103.120 142.759 133.567 1.00 27.51 ?  301 PHE B CG    1 
ATOM   7967  C  CD1   . PHE B 1 301 ? 101.904 142.698 132.911 1.00 26.92 ?  301 PHE B CD1   1 
ATOM   7968  C  CD2   . PHE B 1 301 ? 103.127 142.865 134.946 1.00 25.39 ?  301 PHE B CD2   1 
ATOM   7969  C  CE1   . PHE B 1 301 ? 100.721 142.739 133.614 1.00 27.62 ?  301 PHE B CE1   1 
ATOM   7970  C  CE2   . PHE B 1 301 ? 101.948 142.909 135.654 1.00 28.97 ?  301 PHE B CE2   1 
ATOM   7971  C  CZ    . PHE B 1 301 ? 100.742 142.849 134.987 1.00 28.06 ?  301 PHE B CZ    1 
ATOM   7972  N  N     . TYR B 1 302 ? 105.863 141.792 130.176 1.00 25.95 ?  302 TYR B N     1 
ATOM   7973  C  CA    . TYR B 1 302 ? 106.998 142.049 129.304 1.00 26.54 ?  302 TYR B CA    1 
ATOM   7974  C  C     . TYR B 1 302 ? 107.431 143.493 129.513 1.00 29.50 ?  302 TYR B C     1 
ATOM   7975  O  O     . TYR B 1 302 ? 106.650 144.409 129.217 1.00 30.63 ?  302 TYR B O     1 
ATOM   7976  C  CB    . TYR B 1 302 ? 106.624 141.807 127.849 1.00 25.74 ?  302 TYR B CB    1 
ATOM   7977  C  CG    . TYR B 1 302 ? 106.448 140.350 127.492 1.00 27.02 ?  302 TYR B CG    1 
ATOM   7978  C  CD1   . TYR B 1 302 ? 105.322 139.646 127.896 1.00 25.03 ?  302 TYR B CD1   1 
ATOM   7979  C  CD2   . TYR B 1 302 ? 107.407 139.679 126.749 1.00 27.54 ?  302 TYR B CD2   1 
ATOM   7980  C  CE1   . TYR B 1 302 ? 105.158 138.317 127.571 1.00 25.70 ?  302 TYR B CE1   1 
ATOM   7981  C  CE2   . TYR B 1 302 ? 107.251 138.349 126.417 1.00 26.81 ?  302 TYR B CE2   1 
ATOM   7982  C  CZ    . TYR B 1 302 ? 106.124 137.673 126.831 1.00 30.33 ?  302 TYR B CZ    1 
ATOM   7983  O  OH    . TYR B 1 302 ? 105.968 136.347 126.504 1.00 33.17 ?  302 TYR B OH    1 
ATOM   7984  N  N     . PRO B 1 303 ? 108.633 143.747 130.033 1.00 28.05 ?  303 PRO B N     1 
ATOM   7985  C  CA    . PRO B 1 303 ? 109.015 145.130 130.361 1.00 25.48 ?  303 PRO B CA    1 
ATOM   7986  C  C     . PRO B 1 303 ? 109.027 146.071 129.170 1.00 29.88 ?  303 PRO B C     1 
ATOM   7987  O  O     . PRO B 1 303 ? 108.701 147.253 129.330 1.00 30.10 ?  303 PRO B O     1 
ATOM   7988  C  CB    . PRO B 1 303 ? 110.419 144.971 130.960 1.00 23.10 ?  303 PRO B CB    1 
ATOM   7989  C  CG    . PRO B 1 303 ? 110.484 143.563 131.415 1.00 25.78 ?  303 PRO B CG    1 
ATOM   7990  C  CD    . PRO B 1 303 ? 109.657 142.776 130.450 1.00 22.71 ?  303 PRO B CD    1 
ATOM   7991  N  N     . HIS B 1 304 ? 109.396 145.588 127.981 1.00 29.63 ?  304 HIS B N     1 
ATOM   7992  C  CA    . HIS B 1 304 ? 109.545 146.493 126.846 1.00 29.90 ?  304 HIS B CA    1 
ATOM   7993  C  C     . HIS B 1 304 ? 108.197 147.010 126.365 1.00 31.79 ?  304 HIS B C     1 
ATOM   7994  O  O     . HIS B 1 304 ? 108.086 148.169 125.952 1.00 37.64 ?  304 HIS B O     1 
ATOM   7995  C  CB    . HIS B 1 304 ? 110.288 145.806 125.706 1.00 27.70 ?  304 HIS B CB    1 
ATOM   7996  C  CG    . HIS B 1 304 ? 110.626 146.723 124.574 1.00 28.80 ?  304 HIS B CG    1 
ATOM   7997  N  ND1   . HIS B 1 304 ? 111.096 148.003 124.772 1.00 27.07 ?  304 HIS B ND1   1 
ATOM   7998  C  CD2   . HIS B 1 304 ? 110.557 146.550 123.233 1.00 35.59 ?  304 HIS B CD2   1 
ATOM   7999  C  CE1   . HIS B 1 304 ? 111.304 148.578 123.601 1.00 30.15 ?  304 HIS B CE1   1 
ATOM   8000  N  NE2   . HIS B 1 304 ? 110.986 147.718 122.652 1.00 35.61 ?  304 HIS B NE2   1 
ATOM   8001  N  N     . THR B 1 305 ? 107.162 146.169 126.398 1.00 28.56 ?  305 THR B N     1 
ATOM   8002  C  CA    . THR B 1 305 ? 105.829 146.630 126.023 1.00 32.68 ?  305 THR B CA    1 
ATOM   8003  C  C     . THR B 1 305 ? 105.333 147.705 126.980 1.00 29.26 ?  305 THR B C     1 
ATOM   8004  O  O     . THR B 1 305 ? 104.750 148.710 126.555 1.00 34.96 ?  305 THR B O     1 
ATOM   8005  C  CB    . THR B 1 305 ? 104.857 145.452 125.986 1.00 30.45 ?  305 THR B CB    1 
ATOM   8006  O  OG1   . THR B 1 305 ? 104.715 144.907 127.304 1.00 28.12 ?  305 THR B OG1   1 
ATOM   8007  C  CG2   . THR B 1 305 ? 105.370 144.371 125.052 1.00 31.29 ?  305 THR B CG2   1 
ATOM   8008  N  N     . ILE B 1 306 ? 105.568 147.514 128.280 1.00 29.89 ?  306 ILE B N     1 
ATOM   8009  C  CA    . ILE B 1 306 ? 105.177 148.513 129.268 1.00 30.13 ?  306 ILE B CA    1 
ATOM   8010  C  C     . ILE B 1 306 ? 105.947 149.807 129.051 1.00 29.22 ?  306 ILE B C     1 
ATOM   8011  O  O     . ILE B 1 306 ? 105.384 150.905 129.144 1.00 34.03 ?  306 ILE B O     1 
ATOM   8012  C  CB    . ILE B 1 306 ? 105.382 147.958 130.689 1.00 26.76 ?  306 ILE B CB    1 
ATOM   8013  C  CG1   . ILE B 1 306 ? 104.345 146.879 130.990 1.00 26.49 ?  306 ILE B CG1   1 
ATOM   8014  C  CG2   . ILE B 1 306 ? 105.309 149.066 131.716 1.00 29.75 ?  306 ILE B CG2   1 
ATOM   8015  C  CD1   . ILE B 1 306 ? 104.516 146.238 132.336 1.00 28.94 ?  306 ILE B CD1   1 
ATOM   8016  N  N     . TYR B 1 307 ? 107.245 149.703 128.761 1.00 30.63 ?  307 TYR B N     1 
ATOM   8017  C  CA    . TYR B 1 307 ? 108.044 150.899 128.513 1.00 27.67 ?  307 TYR B CA    1 
ATOM   8018  C  C     . TYR B 1 307 ? 107.566 151.631 127.265 1.00 31.63 ?  307 TYR B C     1 
ATOM   8019  O  O     . TYR B 1 307 ? 107.521 152.865 127.241 1.00 35.31 ?  307 TYR B O     1 
ATOM   8020  C  CB    . TYR B 1 307 ? 109.523 150.526 128.401 1.00 24.46 ?  307 TYR B CB    1 
ATOM   8021  C  CG    . TYR B 1 307 ? 110.448 151.700 128.161 1.00 31.21 ?  307 TYR B CG    1 
ATOM   8022  C  CD1   . TYR B 1 307 ? 110.650 152.208 126.882 1.00 31.54 ?  307 TYR B CD1   1 
ATOM   8023  C  CD2   . TYR B 1 307 ? 111.108 152.311 129.218 1.00 26.86 ?  307 TYR B CD2   1 
ATOM   8024  C  CE1   . TYR B 1 307 ? 111.487 153.281 126.667 1.00 31.01 ?  307 TYR B CE1   1 
ATOM   8025  C  CE2   . TYR B 1 307 ? 111.945 153.384 129.012 1.00 29.82 ?  307 TYR B CE2   1 
ATOM   8026  C  CZ    . TYR B 1 307 ? 112.132 153.865 127.734 1.00 34.47 ?  307 TYR B CZ    1 
ATOM   8027  O  OH    . TYR B 1 307 ? 112.969 154.937 127.522 1.00 36.60 ?  307 TYR B OH    1 
ATOM   8028  N  N     . LYS B 1 308 ? 107.217 150.886 126.214 1.00 34.42 ?  308 LYS B N     1 
ATOM   8029  C  CA    . LYS B 1 308 ? 106.699 151.507 125.001 1.00 31.88 ?  308 LYS B CA    1 
ATOM   8030  C  C     . LYS B 1 308 ? 105.376 152.213 125.266 1.00 31.61 ?  308 LYS B C     1 
ATOM   8031  O  O     . LYS B 1 308 ? 105.150 153.328 124.781 1.00 36.40 ?  308 LYS B O     1 
ATOM   8032  C  CB    . LYS B 1 308 ? 106.531 150.453 123.907 1.00 32.36 ?  308 LYS B CB    1 
ATOM   8033  C  CG    . LYS B 1 308 ? 107.807 150.131 123.147 1.00 33.85 ?  308 LYS B CG    1 
ATOM   8034  C  CD    . LYS B 1 308 ? 107.817 148.697 122.626 1.00 35.89 ?  308 LYS B CD    1 
ATOM   8035  C  CE    . LYS B 1 308 ? 106.430 148.068 122.627 1.00 36.98 ?  308 LYS B CE    1 
ATOM   8036  N  NZ    . LYS B 1 308 ? 106.305 146.992 121.607 1.00 35.60 1  308 LYS B NZ    1 
ATOM   8037  N  N     . GLU B 1 309 ? 104.488 151.579 126.034 1.00 29.97 ?  309 GLU B N     1 
ATOM   8038  C  CA    . GLU B 1 309 ? 103.163 152.150 126.248 1.00 34.83 ?  309 GLU B CA    1 
ATOM   8039  C  C     . GLU B 1 309 ? 103.206 153.357 127.178 1.00 35.03 ?  309 GLU B C     1 
ATOM   8040  O  O     . GLU B 1 309 ? 102.548 154.370 126.917 1.00 37.16 ?  309 GLU B O     1 
ATOM   8041  C  CB    . GLU B 1 309 ? 102.218 151.085 126.800 1.00 32.85 ?  309 GLU B CB    1 
ATOM   8042  C  CG    . GLU B 1 309 ? 100.911 151.643 127.334 1.00 35.09 ?  309 GLU B CG    1 
ATOM   8043  C  CD    . GLU B 1 309 ? 100.024 152.219 126.248 1.00 40.22 ?  309 GLU B CD    1 
ATOM   8044  O  OE1   . GLU B 1 309 ? 100.236 151.892 125.062 1.00 40.62 ?  309 GLU B OE1   1 
ATOM   8045  O  OE2   . GLU B 1 309 ? 99.112  153.004 126.583 1.00 39.65 -1 309 GLU B OE2   1 
ATOM   8046  N  N     . TYR B 1 310 ? 103.974 153.274 128.265 1.00 33.44 ?  310 TYR B N     1 
ATOM   8047  C  CA    . TYR B 1 310 ? 103.938 154.291 129.306 1.00 33.04 ?  310 TYR B CA    1 
ATOM   8048  C  C     . TYR B 1 310 ? 105.159 155.199 129.326 1.00 31.90 ?  310 TYR B C     1 
ATOM   8049  O  O     . TYR B 1 310 ? 105.106 156.257 129.963 1.00 31.87 ?  310 TYR B O     1 
ATOM   8050  C  CB    . TYR B 1 310 ? 103.782 153.629 130.682 1.00 31.08 ?  310 TYR B CB    1 
ATOM   8051  C  CG    . TYR B 1 310 ? 102.524 152.803 130.819 1.00 32.59 ?  310 TYR B CG    1 
ATOM   8052  C  CD1   . TYR B 1 310 ? 101.321 153.391 131.188 1.00 31.36 ?  310 TYR B CD1   1 
ATOM   8053  C  CD2   . TYR B 1 310 ? 102.536 151.437 130.573 1.00 32.26 ?  310 TYR B CD2   1 
ATOM   8054  C  CE1   . TYR B 1 310 ? 100.168 152.641 131.312 1.00 33.04 ?  310 TYR B CE1   1 
ATOM   8055  C  CE2   . TYR B 1 310 ? 101.387 150.679 130.692 1.00 32.17 ?  310 TYR B CE2   1 
ATOM   8056  C  CZ    . TYR B 1 310 ? 100.208 151.286 131.064 1.00 33.62 ?  310 TYR B CZ    1 
ATOM   8057  O  OH    . TYR B 1 310 ? 99.062  150.536 131.186 1.00 34.39 ?  310 TYR B OH    1 
ATOM   8058  N  N     . GLY B 1 311 ? 106.244 154.829 128.654 1.00 29.63 ?  311 GLY B N     1 
ATOM   8059  C  CA    . GLY B 1 311 ? 107.457 155.615 128.689 1.00 29.67 ?  311 GLY B CA    1 
ATOM   8060  C  C     . GLY B 1 311 ? 108.333 155.384 129.898 1.00 34.53 ?  311 GLY B C     1 
ATOM   8061  O  O     . GLY B 1 311 ? 109.395 156.008 130.000 1.00 36.90 ?  311 GLY B O     1 
ATOM   8062  N  N     . GLN B 1 312 ? 107.924 154.512 130.816 1.00 31.52 ?  312 GLN B N     1 
ATOM   8063  C  CA    . GLN B 1 312 ? 108.696 154.201 132.007 1.00 29.78 ?  312 GLN B CA    1 
ATOM   8064  C  C     . GLN B 1 312 ? 108.839 152.691 132.136 1.00 32.31 ?  312 GLN B C     1 
ATOM   8065  O  O     . GLN B 1 312 ? 108.031 151.922 131.610 1.00 39.23 ?  312 GLN B O     1 
ATOM   8066  C  CB    . GLN B 1 312 ? 108.045 154.771 133.275 1.00 32.47 ?  312 GLN B CB    1 
ATOM   8067  C  CG    . GLN B 1 312 ? 107.166 155.987 133.039 1.00 31.94 ?  312 GLN B CG    1 
ATOM   8068  C  CD    . GLN B 1 312 ? 106.222 156.254 134.193 1.00 35.90 ?  312 GLN B CD    1 
ATOM   8069  O  OE1   . GLN B 1 312 ? 106.646 156.661 135.275 1.00 38.51 ?  312 GLN B OE1   1 
ATOM   8070  N  NE2   . GLN B 1 312 ? 104.934 156.026 133.969 1.00 33.65 ?  312 GLN B NE2   1 
ATOM   8071  N  N     . HIS B 1 313 ? 109.884 152.276 132.845 1.00 29.23 ?  313 HIS B N     1 
ATOM   8072  C  CA    . HIS B 1 313 ? 110.123 150.861 133.064 1.00 29.45 ?  313 HIS B CA    1 
ATOM   8073  C  C     . HIS B 1 313 ? 109.106 150.290 134.049 1.00 32.07 ?  313 HIS B C     1 
ATOM   8074  O  O     . HIS B 1 313 ? 108.505 151.009 134.853 1.00 32.39 ?  313 HIS B O     1 
ATOM   8075  C  CB    . HIS B 1 313 ? 111.545 150.635 133.575 1.00 26.13 ?  313 HIS B CB    1 
ATOM   8076  C  CG    . HIS B 1 313 ? 112.604 151.141 132.647 1.00 27.87 ?  313 HIS B CG    1 
ATOM   8077  N  ND1   . HIS B 1 313 ? 113.042 150.422 131.555 1.00 30.95 ?  313 HIS B ND1   1 
ATOM   8078  C  CD2   . HIS B 1 313 ? 113.311 152.295 132.644 1.00 29.49 ?  313 HIS B CD2   1 
ATOM   8079  C  CE1   . HIS B 1 313 ? 113.973 151.111 130.921 1.00 28.56 ?  313 HIS B CE1   1 
ATOM   8080  N  NE2   . HIS B 1 313 ? 114.155 152.252 131.561 1.00 30.09 ?  313 HIS B NE2   1 
ATOM   8081  N  N     . MET B 1 314 ? 108.914 148.971 133.971 1.00 35.31 ?  314 MET B N     1 
ATOM   8082  C  CA    . MET B 1 314 ? 107.933 148.313 134.830 1.00 30.43 ?  314 MET B CA    1 
ATOM   8083  C  C     . MET B 1 314 ? 108.305 148.449 136.301 1.00 37.07 ?  314 MET B C     1 
ATOM   8084  O  O     . MET B 1 314 ? 107.435 148.672 137.151 1.00 39.69 ?  314 MET B O     1 
ATOM   8085  C  CB    . MET B 1 314 ? 107.799 146.841 134.446 1.00 28.98 ?  314 MET B CB    1 
ATOM   8086  C  CG    . MET B 1 314 ? 106.706 146.113 135.209 1.00 29.54 ?  314 MET B CG    1 
ATOM   8087  S  SD    . MET B 1 314 ? 106.983 144.343 135.399 1.00 45.32 ?  314 MET B SD    1 
ATOM   8088  C  CE    . MET B 1 314 ? 108.130 144.028 134.065 1.00 30.08 ?  314 MET B CE    1 
ATOM   8089  N  N     . ASP B 1 315 ? 109.590 148.317 136.623 1.00 30.29 ?  315 ASP B N     1 
ATOM   8090  C  CA    . ASP B 1 315 ? 110.047 148.461 137.999 1.00 34.42 ?  315 ASP B CA    1 
ATOM   8091  C  C     . ASP B 1 315 ? 110.257 149.914 138.402 1.00 30.20 ?  315 ASP B C     1 
ATOM   8092  O  O     . ASP B 1 315 ? 110.623 150.174 139.553 1.00 36.93 ?  315 ASP B O     1 
ATOM   8093  C  CB    . ASP B 1 315 ? 111.343 147.672 138.210 1.00 33.18 ?  315 ASP B CB    1 
ATOM   8094  C  CG    . ASP B 1 315 ? 112.490 148.204 137.380 1.00 32.79 ?  315 ASP B CG    1 
ATOM   8095  O  OD1   . ASP B 1 315 ? 112.226 148.793 136.311 1.00 36.65 ?  315 ASP B OD1   1 
ATOM   8096  O  OD2   . ASP B 1 315 ? 113.654 148.036 137.795 1.00 29.78 -1 315 ASP B OD2   1 
ATOM   8097  N  N     . GLU B 1 316 ? 110.037 150.861 137.489 1.00 28.38 ?  316 GLU B N     1 
ATOM   8098  C  CA    . GLU B 1 316 ? 110.174 152.276 137.798 1.00 29.96 ?  316 GLU B CA    1 
ATOM   8099  C  C     . GLU B 1 316 ? 108.928 152.870 138.442 1.00 35.54 ?  316 GLU B C     1 
ATOM   8100  O  O     . GLU B 1 316 ? 108.986 154.004 138.927 1.00 39.07 ?  316 GLU B O     1 
ATOM   8101  C  CB    . GLU B 1 316 ? 110.505 153.061 136.526 1.00 36.44 ?  316 GLU B CB    1 
ATOM   8102  C  CG    . GLU B 1 316 ? 111.989 153.283 136.284 1.00 34.69 ?  316 GLU B CG    1 
ATOM   8103  C  CD    . GLU B 1 316 ? 112.766 153.531 137.560 1.00 36.36 ?  316 GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 1 316 ? 112.427 154.484 138.293 1.00 38.09 ?  316 GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 1 316 ? 113.721 152.774 137.827 1.00 41.39 -1 316 GLU B OE2   1 
ATOM   8106  N  N     . MET B 1 317 ? 107.813 152.145 138.457 1.00 38.06 ?  317 MET B N     1 
ATOM   8107  C  CA    . MET B 1 317 ? 106.565 152.645 139.009 1.00 38.40 ?  317 MET B CA    1 
ATOM   8108  C  C     . MET B 1 317 ? 105.953 151.609 139.942 1.00 37.91 ?  317 MET B C     1 
ATOM   8109  O  O     . MET B 1 317 ? 106.394 150.460 140.013 1.00 37.39 ?  317 MET B O     1 
ATOM   8110  C  CB    . MET B 1 317 ? 105.572 153.027 137.902 1.00 40.05 ?  317 MET B CB    1 
ATOM   8111  C  CG    . MET B 1 317 ? 105.639 152.153 136.665 1.00 34.68 ?  317 MET B CG    1 
ATOM   8112  S  SD    . MET B 1 317 ? 105.180 153.086 135.192 1.00 48.10 ?  317 MET B SD    1 
ATOM   8113  C  CE    . MET B 1 317 ? 105.387 151.845 133.924 1.00 33.99 ?  317 MET B CE    1 
ATOM   8114  N  N     . ASP B 1 318 ? 104.916 152.040 140.658 1.00 40.30 ?  318 ASP B N     1 
ATOM   8115  C  CA    . ASP B 1 318 ? 104.293 151.234 141.703 1.00 38.45 ?  318 ASP B CA    1 
ATOM   8116  C  C     . ASP B 1 318 ? 103.388 150.188 141.067 1.00 38.44 ?  318 ASP B C     1 
ATOM   8117  O  O     . ASP B 1 318 ? 102.419 150.528 140.380 1.00 41.14 ?  318 ASP B O     1 
ATOM   8118  C  CB    . ASP B 1 318 ? 103.511 152.131 142.658 1.00 37.95 ?  318 ASP B CB    1 
ATOM   8119  C  CG    . ASP B 1 318 ? 102.854 151.356 143.781 1.00 46.03 ?  318 ASP B CG    1 
ATOM   8120  O  OD1   . ASP B 1 318 ? 103.577 150.865 144.674 1.00 42.17 ?  318 ASP B OD1   1 
ATOM   8121  O  OD2   . ASP B 1 318 ? 101.612 151.242 143.772 1.00 44.77 -1 318 ASP B OD2   1 
ATOM   8122  N  N     . MET B 1 319 ? 103.703 148.910 141.292 1.00 39.69 ?  319 MET B N     1 
ATOM   8123  C  CA    . MET B 1 319 ? 102.857 147.838 140.780 1.00 35.15 ?  319 MET B CA    1 
ATOM   8124  C  C     . MET B 1 319 ? 101.528 147.763 141.521 1.00 36.04 ?  319 MET B C     1 
ATOM   8125  O  O     . MET B 1 319 ? 100.524 147.345 140.937 1.00 38.25 ?  319 MET B O     1 
ATOM   8126  C  CB    . MET B 1 319 ? 103.586 146.497 140.868 1.00 36.87 ?  319 MET B CB    1 
ATOM   8127  C  CG    . MET B 1 319 ? 102.937 145.382 140.058 1.00 37.09 ?  319 MET B CG    1 
ATOM   8128  S  SD    . MET B 1 319 ? 103.401 145.329 138.313 1.00 44.18 ?  319 MET B SD    1 
ATOM   8129  C  CE    . MET B 1 319 ? 104.890 146.321 138.305 1.00 38.47 ?  319 MET B CE    1 
ATOM   8130  N  N     . ASN B 1 320 ? 101.497 148.171 142.791 1.00 38.47 ?  320 ASN B N     1 
ATOM   8131  C  CA    . ASN B 1 320 ? 100.261 148.090 143.563 1.00 38.98 ?  320 ASN B CA    1 
ATOM   8132  C  C     . ASN B 1 320 ? 99.165  148.962 142.967 1.00 40.89 ?  320 ASN B C     1 
ATOM   8133  O  O     . ASN B 1 320 ? 97.976  148.682 143.159 1.00 41.47 ?  320 ASN B O     1 
ATOM   8134  C  CB    . ASN B 1 320 ? 100.524 148.486 145.015 1.00 37.46 ?  320 ASN B CB    1 
ATOM   8135  C  CG    . ASN B 1 320 ? 101.464 147.530 145.716 1.00 42.30 ?  320 ASN B CG    1 
ATOM   8136  O  OD1   . ASN B 1 320 ? 102.588 147.303 145.266 1.00 37.80 ?  320 ASN B OD1   1 
ATOM   8137  N  ND2   . ASN B 1 320 ? 101.009 146.960 146.824 1.00 41.25 ?  320 ASN B ND2   1 
ATOM   8138  N  N     . GLU B 1 321 ? 99.539  150.017 142.244 1.00 42.19 ?  321 GLU B N     1 
ATOM   8139  C  CA    . GLU B 1 321 ? 98.576  150.907 141.617 1.00 40.34 ?  321 GLU B CA    1 
ATOM   8140  C  C     . GLU B 1 321 ? 98.516  150.770 140.103 1.00 40.01 ?  321 GLU B C     1 
ATOM   8141  O  O     . GLU B 1 321 ? 97.564  151.271 139.493 1.00 46.31 ?  321 GLU B O     1 
ATOM   8142  C  CB    . GLU B 1 321 ? 98.892  152.367 141.978 1.00 42.72 ?  321 GLU B CB    1 
ATOM   8143  C  CG    . GLU B 1 321 ? 99.814  153.065 140.991 1.00 39.85 ?  321 GLU B CG    1 
ATOM   8144  C  CD    . GLU B 1 321 ? 100.645 154.154 141.637 1.00 45.15 ?  321 GLU B CD    1 
ATOM   8145  O  OE1   . GLU B 1 321 ? 100.587 154.290 142.877 1.00 45.47 ?  321 GLU B OE1   1 
ATOM   8146  O  OE2   . GLU B 1 321 ? 101.362 154.869 140.907 1.00 45.61 -1 321 GLU B OE2   1 
ATOM   8147  N  N     . MET B 1 322 ? 99.488  150.106 139.479 1.00 34.71 ?  322 MET B N     1 
ATOM   8148  C  CA    . MET B 1 322 ? 99.550  150.019 138.028 1.00 32.82 ?  322 MET B CA    1 
ATOM   8149  C  C     . MET B 1 322 ? 99.361  148.601 137.505 1.00 33.10 ?  322 MET B C     1 
ATOM   8150  O  O     . MET B 1 322 ? 99.359  148.405 136.286 1.00 39.54 ?  322 MET B O     1 
ATOM   8151  C  CB    . MET B 1 322 ? 100.886 150.576 137.523 1.00 33.39 ?  322 MET B CB    1 
ATOM   8152  C  CG    . MET B 1 322 ? 100.984 152.098 137.551 1.00 35.60 ?  322 MET B CG    1 
ATOM   8153  S  SD    . MET B 1 322 ? 100.272 152.971 136.142 1.00 45.22 ?  322 MET B SD    1 
ATOM   8154  C  CE    . MET B 1 322 ? 100.334 151.721 134.869 1.00 36.56 ?  322 MET B CE    1 
ATOM   8155  N  N     . TYR B 1 323 ? 99.212  147.608 138.387 1.00 32.48 ?  323 TYR B N     1 
ATOM   8156  C  CA    . TYR B 1 323 ? 99.055  146.227 137.938 1.00 28.69 ?  323 TYR B CA    1 
ATOM   8157  C  C     . TYR B 1 323 ? 97.759  146.040 137.159 1.00 29.49 ?  323 TYR B C     1 
ATOM   8158  O  O     . TYR B 1 323 ? 97.745  145.374 136.116 1.00 33.38 ?  323 TYR B O     1 
ATOM   8159  C  CB    . TYR B 1 323 ? 99.103  145.280 139.138 1.00 32.87 ?  323 TYR B CB    1 
ATOM   8160  C  CG    . TYR B 1 323 ? 98.832  143.833 138.793 1.00 30.91 ?  323 TYR B CG    1 
ATOM   8161  C  CD1   . TYR B 1 323 ? 99.853  143.001 138.360 1.00 27.40 ?  323 TYR B CD1   1 
ATOM   8162  C  CD2   . TYR B 1 323 ? 97.555  143.298 138.906 1.00 30.40 ?  323 TYR B CD2   1 
ATOM   8163  C  CE1   . TYR B 1 323 ? 99.610  141.681 138.042 1.00 29.80 ?  323 TYR B CE1   1 
ATOM   8164  C  CE2   . TYR B 1 323 ? 97.303  141.980 138.591 1.00 25.97 ?  323 TYR B CE2   1 
ATOM   8165  C  CZ    . TYR B 1 323 ? 98.334  141.176 138.161 1.00 31.28 ?  323 TYR B CZ    1 
ATOM   8166  O  OH    . TYR B 1 323 ? 98.088  139.863 137.846 1.00 30.96 ?  323 TYR B OH    1 
ATOM   8167  N  N     . ASP B 1 324 ? 96.661  146.610 137.655 1.00 36.10 ?  324 ASP B N     1 
ATOM   8168  C  CA    . ASP B 1 324 ? 95.389  146.492 136.952 1.00 34.38 ?  324 ASP B CA    1 
ATOM   8169  C  C     . ASP B 1 324 ? 95.436  147.205 135.606 1.00 38.34 ?  324 ASP B C     1 
ATOM   8170  O  O     . ASP B 1 324 ? 94.862  146.725 134.622 1.00 41.12 ?  324 ASP B O     1 
ATOM   8171  C  CB    . ASP B 1 324 ? 94.259  147.041 137.820 1.00 38.72 ?  324 ASP B CB    1 
ATOM   8172  C  CG    . ASP B 1 324 ? 93.801  146.048 138.870 1.00 40.69 ?  324 ASP B CG    1 
ATOM   8173  O  OD1   . ASP B 1 324 ? 93.980  144.831 138.654 1.00 40.70 ?  324 ASP B OD1   1 
ATOM   8174  O  OD2   . ASP B 1 324 ? 93.266  146.483 139.911 1.00 42.71 -1 324 ASP B OD2   1 
ATOM   8175  N  N     . LYS B 1 325 ? 96.112  148.355 135.546 1.00 33.53 ?  325 LYS B N     1 
ATOM   8176  C  CA    . LYS B 1 325 ? 96.268  149.054 134.275 1.00 31.34 ?  325 LYS B CA    1 
ATOM   8177  C  C     . LYS B 1 325 ? 97.109  148.242 133.296 1.00 32.90 ?  325 LYS B C     1 
ATOM   8178  O  O     . LYS B 1 325 ? 96.809  148.205 132.098 1.00 40.84 ?  325 LYS B O     1 
ATOM   8179  C  CB    . LYS B 1 325 ? 96.884  150.431 134.508 1.00 36.26 ?  325 LYS B CB    1 
ATOM   8180  C  CG    . LYS B 1 325 ? 95.999  151.359 135.320 1.00 34.78 ?  325 LYS B CG    1 
ATOM   8181  C  CD    . LYS B 1 325 ? 96.771  152.565 135.818 1.00 34.18 ?  325 LYS B CD    1 
ATOM   8182  C  CE    . LYS B 1 325 ? 95.841  153.725 136.122 1.00 36.84 ?  325 LYS B CE    1 
ATOM   8183  N  NZ    . LYS B 1 325 ? 94.432  153.275 136.287 1.00 36.00 1  325 LYS B NZ    1 
ATOM   8184  N  N     . PHE B 1 326 ? 98.165  147.589 133.787 1.00 35.11 ?  326 PHE B N     1 
ATOM   8185  C  CA    . PHE B 1 326 ? 98.945  146.689 132.942 1.00 33.24 ?  326 PHE B CA    1 
ATOM   8186  C  C     . PHE B 1 326 ? 98.087  145.548 132.409 1.00 29.94 ?  326 PHE B C     1 
ATOM   8187  O  O     . PHE B 1 326 ? 98.179  145.190 131.229 1.00 36.57 ?  326 PHE B O     1 
ATOM   8188  C  CB    . PHE B 1 326 ? 100.132 146.123 133.723 1.00 30.23 ?  326 PHE B CB    1 
ATOM   8189  C  CG    . PHE B 1 326 ? 101.197 147.129 134.043 1.00 30.01 ?  326 PHE B CG    1 
ATOM   8190  C  CD1   . PHE B 1 326 ? 101.295 148.312 133.335 1.00 33.25 ?  326 PHE B CD1   1 
ATOM   8191  C  CD2   . PHE B 1 326 ? 102.104 146.886 135.061 1.00 33.29 ?  326 PHE B CD2   1 
ATOM   8192  C  CE1   . PHE B 1 326 ? 102.284 149.229 133.632 1.00 30.86 ?  326 PHE B CE1   1 
ATOM   8193  C  CE2   . PHE B 1 326 ? 103.089 147.801 135.364 1.00 33.97 ?  326 PHE B CE2   1 
ATOM   8194  C  CZ    . PHE B 1 326 ? 103.178 148.975 134.650 1.00 35.34 ?  326 PHE B CZ    1 
ATOM   8195  N  N     . VAL B 1 327 ? 97.256  144.959 133.269 1.00 31.40 ?  327 VAL B N     1 
ATOM   8196  C  CA    . VAL B 1 327 ? 96.464  143.801 132.863 1.00 34.99 ?  327 VAL B CA    1 
ATOM   8197  C  C     . VAL B 1 327 ? 95.394  144.203 131.854 1.00 36.86 ?  327 VAL B C     1 
ATOM   8198  O  O     . VAL B 1 327 ? 95.170  143.507 130.856 1.00 41.34 ?  327 VAL B O     1 
ATOM   8199  C  CB    . VAL B 1 327 ? 95.855  143.114 134.099 1.00 32.98 ?  327 VAL B CB    1 
ATOM   8200  C  CG1   . VAL B 1 327 ? 94.792  142.109 133.685 1.00 35.22 ?  327 VAL B CG1   1 
ATOM   8201  C  CG2   . VAL B 1 327 ? 96.943  142.435 134.914 1.00 29.82 ?  327 VAL B CG2   1 
ATOM   8202  N  N     . ASP B 1 328 ? 94.726  145.332 132.085 1.00 36.62 ?  328 ASP B N     1 
ATOM   8203  C  CA    . ASP B 1 328 ? 93.648  145.774 131.210 1.00 36.77 ?  328 ASP B CA    1 
ATOM   8204  C  C     . ASP B 1 328 ? 94.146  146.449 129.938 1.00 40.53 ?  328 ASP B C     1 
ATOM   8205  O  O     . ASP B 1 328 ? 93.331  146.753 129.062 1.00 43.97 ?  328 ASP B O     1 
ATOM   8206  C  CB    . ASP B 1 328 ? 92.721  146.730 131.966 1.00 38.73 ?  328 ASP B CB    1 
ATOM   8207  C  CG    . ASP B 1 328 ? 92.107  146.092 133.195 1.00 45.21 ?  328 ASP B CG    1 
ATOM   8208  O  OD1   . ASP B 1 328 ? 91.571  146.833 134.045 1.00 46.00 ?  328 ASP B OD1   1 
ATOM   8209  O  OD2   . ASP B 1 328 ? 92.162  144.849 133.312 1.00 44.15 -1 328 ASP B OD2   1 
ATOM   8210  N  N     . ASN B 1 329 ? 95.449  146.688 129.816 1.00 36.19 ?  329 ASN B N     1 
ATOM   8211  C  CA    . ASN B 1 329 ? 95.996  147.363 128.648 1.00 35.52 ?  329 ASN B CA    1 
ATOM   8212  C  C     . ASN B 1 329 ? 96.301  146.331 127.569 1.00 39.38 ?  329 ASN B C     1 
ATOM   8213  O  O     . ASN B 1 329 ? 97.163  145.468 127.783 1.00 39.32 ?  329 ASN B O     1 
ATOM   8214  C  CB    . ASN B 1 329 ? 97.258  148.124 129.020 1.00 35.64 ?  329 ASN B CB    1 
ATOM   8215  C  CG    . ASN B 1 329 ? 97.641  149.183 128.002 1.00 39.66 ?  329 ASN B CG    1 
ATOM   8216  O  OD1   . ASN B 1 329 ? 98.369  150.118 128.322 1.00 37.91 ?  329 ASN B OD1   1 
ATOM   8217  N  ND2   . ASN B 1 329 ? 97.153  149.045 126.777 1.00 42.21 ?  329 ASN B ND2   1 
ATOM   8218  N  N     . PRO B 1 330 ? 95.630  146.374 126.414 1.00 43.55 ?  330 PRO B N     1 
ATOM   8219  C  CA    . PRO B 1 330 ? 95.948  145.401 125.357 1.00 40.99 ?  330 PRO B CA    1 
ATOM   8220  C  C     . PRO B 1 330 ? 97.323  145.603 124.744 1.00 37.31 ?  330 PRO B C     1 
ATOM   8221  O  O     . PRO B 1 330 ? 97.894  144.644 124.210 1.00 39.57 ?  330 PRO B O     1 
ATOM   8222  C  CB    . PRO B 1 330 ? 94.831  145.625 124.329 1.00 41.98 ?  330 PRO B CB    1 
ATOM   8223  C  CG    . PRO B 1 330 ? 94.399  147.035 124.550 1.00 37.44 ?  330 PRO B CG    1 
ATOM   8224  C  CD    . PRO B 1 330 ? 94.534  147.278 126.025 1.00 40.19 ?  330 PRO B CD    1 
ATOM   8225  N  N     . ARG B 1 331 ? 97.875  146.815 124.803 1.00 38.79 ?  331 ARG B N     1 
ATOM   8226  C  CA    . ARG B 1 331 ? 99.197  147.075 124.249 1.00 42.17 ?  331 ARG B CA    1 
ATOM   8227  C  C     . ARG B 1 331 ? 100.322 146.594 125.153 1.00 40.20 ?  331 ARG B C     1 
ATOM   8228  O  O     . ARG B 1 331 ? 101.489 146.660 124.753 1.00 38.14 ?  331 ARG B O     1 
ATOM   8229  C  CB    . ARG B 1 331 ? 99.363  148.569 123.961 1.00 39.65 ?  331 ARG B CB    1 
ATOM   8230  C  CG    . ARG B 1 331 ? 98.530  149.061 122.788 1.00 38.38 ?  331 ARG B CG    1 
ATOM   8231  C  CD    . ARG B 1 331 ? 98.355  150.572 122.812 1.00 40.13 ?  331 ARG B CD    1 
ATOM   8232  N  NE    . ARG B 1 331 ? 97.640  151.035 123.997 1.00 42.43 ?  331 ARG B NE    1 
ATOM   8233  C  CZ    . ARG B 1 331 ? 96.347  150.842 124.221 1.00 42.33 ?  331 ARG B CZ    1 
ATOM   8234  N  NH1   . ARG B 1 331 ? 95.583  150.192 123.358 1.00 41.73 1  331 ARG B NH1   1 
ATOM   8235  N  NH2   . ARG B 1 331 ? 95.806  151.320 125.338 1.00 40.55 ?  331 ARG B NH2   1 
ATOM   8236  N  N     . VAL B 1 332 ? 100.003 146.122 126.354 1.00 38.10 ?  332 VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? 100.977 145.526 127.259 1.00 33.72 ?  332 VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? 100.879 144.014 127.128 1.00 34.64 ?  332 VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? 99.782  143.448 127.204 1.00 37.29 ?  332 VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? 100.734 145.973 128.711 1.00 33.18 ?  332 VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? 101.496 145.082 129.680 1.00 33.55 ?  332 VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? 101.133 147.430 128.889 1.00 33.28 ?  332 VAL B CG2   1 
ATOM   8243  N  N     . LYS B 1 333 ? 102.015 143.361 126.910 1.00 31.25 ?  333 LYS B N     1 
ATOM   8244  C  CA    . LYS B 1 333 ? 102.059 141.912 126.785 1.00 31.37 ?  333 LYS B CA    1 
ATOM   8245  C  C     . LYS B 1 333 ? 102.303 141.281 128.149 1.00 33.26 ?  333 LYS B C     1 
ATOM   8246  O  O     . LYS B 1 333 ? 103.138 141.756 128.925 1.00 34.81 ?  333 LYS B O     1 
ATOM   8247  C  CB    . LYS B 1 333 ? 103.150 141.487 125.802 1.00 26.23 ?  333 LYS B CB    1 
ATOM   8248  C  CG    . LYS B 1 333 ? 102.969 140.091 125.234 1.00 32.17 ?  333 LYS B CG    1 
ATOM   8249  C  CD    . LYS B 1 333 ? 104.140 139.703 124.347 1.00 34.40 ?  333 LYS B CD    1 
ATOM   8250  C  CE    . LYS B 1 333 ? 104.051 138.247 123.919 1.00 35.85 ?  333 LYS B CE    1 
ATOM   8251  N  NZ    . LYS B 1 333 ? 105.194 137.855 123.050 1.00 37.67 1  333 LYS B NZ    1 
ATOM   8252  N  N     . LYS B 1 334 ? 101.570 140.208 128.439 1.00 32.05 ?  334 LYS B N     1 
ATOM   8253  C  CA    . LYS B 1 334 ? 101.665 139.562 129.738 1.00 29.36 ?  334 LYS B CA    1 
ATOM   8254  C  C     . LYS B 1 334 ? 101.383 138.075 129.596 1.00 33.55 ?  334 LYS B C     1 
ATOM   8255  O  O     . LYS B 1 334 ? 100.787 137.622 128.615 1.00 35.10 ?  334 LYS B O     1 
ATOM   8256  C  CB    . LYS B 1 334 ? 100.698 140.187 130.751 1.00 31.14 ?  334 LYS B CB    1 
ATOM   8257  C  CG    . LYS B 1 334 ? 99.236  139.898 130.472 1.00 35.88 ?  334 LYS B CG    1 
ATOM   8258  C  CD    . LYS B 1 334 ? 98.365  141.102 130.769 1.00 32.50 ?  334 LYS B CD    1 
ATOM   8259  C  CE    . LYS B 1 334 ? 98.387  142.087 129.619 1.00 33.97 ?  334 LYS B CE    1 
ATOM   8260  N  NZ    . LYS B 1 334 ? 97.138  142.889 129.543 1.00 34.33 1  334 LYS B NZ    1 
ATOM   8261  N  N     . GLU B 1 335 ? 101.825 137.320 130.599 1.00 33.86 ?  335 GLU B N     1 
ATOM   8262  C  CA    . GLU B 1 335 ? 101.615 135.883 130.679 1.00 33.23 ?  335 GLU B CA    1 
ATOM   8263  C  C     . GLU B 1 335 ? 100.950 135.542 132.003 1.00 34.05 ?  335 GLU B C     1 
ATOM   8264  O  O     . GLU B 1 335 ? 101.267 136.136 133.038 1.00 40.53 ?  335 GLU B O     1 
ATOM   8265  C  CB    . GLU B 1 335 ? 102.935 135.113 130.549 1.00 29.97 ?  335 GLU B CB    1 
ATOM   8266  C  CG    . GLU B 1 335 ? 103.870 135.651 129.485 1.00 37.48 ?  335 GLU B CG    1 
ATOM   8267  C  CD    . GLU B 1 335 ? 104.557 134.551 128.702 1.00 41.55 ?  335 GLU B CD    1 
ATOM   8268  O  OE1   . GLU B 1 335 ? 105.383 133.825 129.295 1.00 36.02 ?  335 GLU B OE1   1 
ATOM   8269  O  OE2   . GLU B 1 335 ? 104.272 134.413 127.494 1.00 36.24 -1 335 GLU B OE2   1 
ATOM   8270  N  N     . LYS B 1 336 ? 100.034 134.580 131.965 1.00 33.34 ?  336 LYS B N     1 
ATOM   8271  C  CA    . LYS B 1 336 ? 99.338  134.148 133.168 1.00 29.33 ?  336 LYS B CA    1 
ATOM   8272  C  C     . LYS B 1 336 ? 100.222 133.223 133.994 1.00 35.73 ?  336 LYS B C     1 
ATOM   8273  O  O     . LYS B 1 336 ? 100.877 132.324 133.461 1.00 37.25 ?  336 LYS B O     1 
ATOM   8274  C  CB    . LYS B 1 336 ? 98.036  133.434 132.804 1.00 37.44 ?  336 LYS B CB    1 
ATOM   8275  C  CG    . LYS B 1 336 ? 96.946  133.555 133.854 1.00 41.25 ?  336 LYS B CG    1 
ATOM   8276  C  CD    . LYS B 1 336 ? 95.691  132.812 133.432 1.00 38.03 ?  336 LYS B CD    1 
ATOM   8277  C  CE    . LYS B 1 336 ? 94.469  133.713 133.481 1.00 39.22 ?  336 LYS B CE    1 
ATOM   8278  N  NZ    . LYS B 1 336 ? 94.460  134.570 134.697 1.00 39.13 1  336 LYS B NZ    1 
ATOM   8279  N  N     . ILE B 1 337 ? 100.240 133.454 135.308 1.00 36.47 ?  337 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 337 ? 100.969 132.620 136.251 1.00 34.68 ?  337 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 337 ? 100.090 132.390 137.471 1.00 35.24 ?  337 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 337 ? 99.116  133.108 137.710 1.00 39.38 ?  337 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 337 ? 102.316 133.242 136.687 1.00 33.50 ?  337 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 337 ? 102.090 134.634 137.284 1.00 33.10 ?  337 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 337 ? 103.289 133.301 135.521 1.00 35.27 ?  337 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 337 ? 102.991 134.947 138.454 1.00 31.75 ?  337 ILE B CD1   1 
ATOM   8287  N  N     . ASN B 1 338 ? 100.443 131.369 138.246 1.00 35.06 ?  338 ASN B N     1 
ATOM   8288  C  CA    . ASN B 1 338 ? 99.803  131.138 139.530 1.00 34.44 ?  338 ASN B CA    1 
ATOM   8289  C  C     . ASN B 1 338 ? 100.707 131.691 140.618 1.00 34.15 ?  338 ASN B C     1 
ATOM   8290  O  O     . ASN B 1 338 ? 101.786 131.128 140.856 1.00 37.77 ?  338 ASN B O     1 
ATOM   8291  C  CB    . ASN B 1 338 ? 99.546  129.650 139.751 1.00 32.16 ?  338 ASN B CB    1 
ATOM   8292  C  CG    . ASN B 1 338 ? 98.522  129.388 140.839 1.00 35.79 ?  338 ASN B CG    1 
ATOM   8293  O  OD1   . ASN B 1 338 ? 98.272  128.242 141.209 1.00 38.49 ?  338 ASN B OD1   1 
ATOM   8294  N  ND2   . ASN B 1 338 ? 97.920  130.453 141.355 1.00 37.38 ?  338 ASN B ND2   1 
ATOM   8295  N  N     . PRO B 1 339 ? 100.335 132.787 141.286 1.00 33.80 ?  339 PRO B N     1 
ATOM   8296  C  CA    . PRO B 1 339 ? 101.224 133.352 142.314 1.00 28.56 ?  339 PRO B CA    1 
ATOM   8297  C  C     . PRO B 1 339 ? 101.520 132.397 143.455 1.00 32.53 ?  339 PRO B C     1 
ATOM   8298  O  O     . PRO B 1 339 ? 102.633 132.422 143.995 1.00 35.56 ?  339 PRO B O     1 
ATOM   8299  C  CB    . PRO B 1 339 ? 100.459 134.593 142.796 1.00 29.85 ?  339 PRO B CB    1 
ATOM   8300  C  CG    . PRO B 1 339 ? 99.042  134.355 142.398 1.00 33.77 ?  339 PRO B CG    1 
ATOM   8301  C  CD    . PRO B 1 339 ? 99.100  133.570 141.129 1.00 33.82 ?  339 PRO B CD    1 
ATOM   8302  N  N     . ARG B 1 340 ? 100.563 131.548 143.839 1.00 31.45 ?  340 ARG B N     1 
ATOM   8303  C  CA    . ARG B 1 340 ? 100.837 130.559 144.876 1.00 28.07 ?  340 ARG B CA    1 
ATOM   8304  C  C     . ARG B 1 340 ? 101.821 129.505 144.385 1.00 31.70 ?  340 ARG B C     1 
ATOM   8305  O  O     . ARG B 1 340 ? 102.697 129.068 145.139 1.00 34.63 ?  340 ARG B O     1 
ATOM   8306  C  CB    . ARG B 1 340 ? 99.536  129.912 145.345 1.00 31.53 ?  340 ARG B CB    1 
ATOM   8307  C  CG    . ARG B 1 340 ? 98.712  130.807 146.247 1.00 29.55 ?  340 ARG B CG    1 
ATOM   8308  C  CD    . ARG B 1 340 ? 97.774  130.017 147.137 1.00 28.13 ?  340 ARG B CD    1 
ATOM   8309  N  NE    . ARG B 1 340 ? 96.904  130.902 147.903 1.00 31.78 ?  340 ARG B NE    1 
ATOM   8310  C  CZ    . ARG B 1 340 ? 95.968  130.491 148.745 1.00 34.23 ?  340 ARG B CZ    1 
ATOM   8311  N  NH1   . ARG B 1 340 ? 95.750  129.205 148.964 1.00 34.73 1  340 ARG B NH1   1 
ATOM   8312  N  NH2   . ARG B 1 340 ? 95.231  131.394 149.385 1.00 34.57 ?  340 ARG B NH2   1 
ATOM   8313  N  N     . LYS B 1 341 ? 101.697 129.090 143.122 1.00 30.60 ?  341 LYS B N     1 
ATOM   8314  C  CA    . LYS B 1 341 ? 102.678 128.168 142.558 1.00 27.34 ?  341 LYS B CA    1 
ATOM   8315  C  C     . LYS B 1 341 ? 104.055 128.810 142.472 1.00 30.08 ?  341 LYS B C     1 
ATOM   8316  O  O     . LYS B 1 341 ? 105.065 128.139 142.698 1.00 29.73 ?  341 LYS B O     1 
ATOM   8317  C  CB    . LYS B 1 341 ? 102.229 127.689 141.177 1.00 35.91 ?  341 LYS B CB    1 
ATOM   8318  C  CG    . LYS B 1 341 ? 101.101 126.661 141.184 1.00 37.10 ?  341 LYS B CG    1 
ATOM   8319  C  CD    . LYS B 1 341 ? 100.950 125.971 142.530 1.00 34.20 ?  341 LYS B CD    1 
ATOM   8320  C  CE    . LYS B 1 341 ? 100.343 124.586 142.375 1.00 36.14 ?  341 LYS B CE    1 
ATOM   8321  N  NZ    . LYS B 1 341 ? 99.016  124.631 141.698 1.00 33.97 1  341 LYS B NZ    1 
ATOM   8322  N  N     . LEU B 1 342 ? 104.117 130.105 142.154 1.00 29.26 ?  342 LEU B N     1 
ATOM   8323  C  CA    . LEU B 1 342 ? 105.401 130.798 142.135 1.00 26.52 ?  342 LEU B CA    1 
ATOM   8324  C  C     . LEU B 1 342 ? 106.000 130.888 143.534 1.00 30.91 ?  342 LEU B C     1 
ATOM   8325  O  O     . LEU B 1 342 ? 107.214 130.732 143.705 1.00 37.75 ?  342 LEU B O     1 
ATOM   8326  C  CB    . LEU B 1 342 ? 105.237 132.188 141.525 1.00 30.07 ?  342 LEU B CB    1 
ATOM   8327  C  CG    . LEU B 1 342 ? 106.521 132.891 141.081 1.00 27.23 ?  342 LEU B CG    1 
ATOM   8328  C  CD1   . LEU B 1 342 ? 107.450 131.918 140.374 1.00 25.62 ?  342 LEU B CD1   1 
ATOM   8329  C  CD2   . LEU B 1 342 ? 106.198 134.073 140.184 1.00 26.81 ?  342 LEU B CD2   1 
ATOM   8330  N  N     . LEU B 1 343 ? 105.167 131.136 144.547 1.00 29.53 ?  343 LEU B N     1 
ATOM   8331  C  CA    . LEU B 1 343 ? 105.651 131.141 145.924 1.00 26.59 ?  343 LEU B CA    1 
ATOM   8332  C  C     . LEU B 1 343 ? 106.176 129.770 146.331 1.00 28.70 ?  343 LEU B C     1 
ATOM   8333  O  O     . LEU B 1 343 ? 107.215 129.663 146.994 1.00 33.74 ?  343 LEU B O     1 
ATOM   8334  C  CB    . LEU B 1 343 ? 104.535 131.584 146.869 1.00 30.61 ?  343 LEU B CB    1 
ATOM   8335  C  CG    . LEU B 1 343 ? 104.506 133.060 147.256 1.00 30.70 ?  343 LEU B CG    1 
ATOM   8336  C  CD1   . LEU B 1 343 ? 103.445 133.305 148.314 1.00 27.27 ?  343 LEU B CD1   1 
ATOM   8337  C  CD2   . LEU B 1 343 ? 105.872 133.512 147.742 1.00 30.33 ?  343 LEU B CD2   1 
ATOM   8338  N  N     . GLU B 1 344 ? 105.462 128.708 145.953 1.00 30.95 ?  344 GLU B N     1 
ATOM   8339  C  CA    . GLU B 1 344 ? 105.925 127.359 146.259 1.00 28.52 ?  344 GLU B CA    1 
ATOM   8340  C  C     . GLU B 1 344 ? 107.227 127.047 145.532 1.00 29.40 ?  344 GLU B C     1 
ATOM   8341  O  O     . GLU B 1 344 ? 108.098 126.363 146.077 1.00 34.84 ?  344 GLU B O     1 
ATOM   8342  C  CB    . GLU B 1 344 ? 104.846 126.338 145.903 1.00 30.80 ?  344 GLU B CB    1 
ATOM   8343  C  CG    . GLU B 1 344 ? 103.610 126.420 146.782 1.00 33.67 ?  344 GLU B CG    1 
ATOM   8344  C  CD    . GLU B 1 344 ? 102.417 125.712 146.176 1.00 38.15 ?  344 GLU B CD    1 
ATOM   8345  O  OE1   . GLU B 1 344 ? 102.597 125.017 145.155 1.00 39.86 ?  344 GLU B OE1   1 
ATOM   8346  O  OE2   . GLU B 1 344 ? 101.300 125.854 146.717 1.00 37.98 -1 344 GLU B OE2   1 
ATOM   8347  N  N     . LYS B 1 345 ? 107.374 127.536 144.299 1.00 29.24 ?  345 LYS B N     1 
ATOM   8348  C  CA    . LYS B 1 345 ? 108.634 127.375 143.580 1.00 27.16 ?  345 LYS B CA    1 
ATOM   8349  C  C     . LYS B 1 345 ? 109.765 128.110 144.286 1.00 30.72 ?  345 LYS B C     1 
ATOM   8350  O  O     . LYS B 1 345 ? 110.887 127.599 144.373 1.00 32.03 ?  345 LYS B O     1 
ATOM   8351  C  CB    . LYS B 1 345 ? 108.487 127.868 142.142 1.00 26.14 ?  345 LYS B CB    1 
ATOM   8352  C  CG    . LYS B 1 345 ? 109.739 127.698 141.302 1.00 29.85 ?  345 LYS B CG    1 
ATOM   8353  C  CD    . LYS B 1 345 ? 109.510 128.127 139.865 1.00 30.37 ?  345 LYS B CD    1 
ATOM   8354  C  CE    . LYS B 1 345 ? 110.757 127.910 139.026 1.00 30.62 ?  345 LYS B CE    1 
ATOM   8355  N  NZ    . LYS B 1 345 ? 110.570 128.351 137.618 1.00 31.25 1  345 LYS B NZ    1 
ATOM   8356  N  N     . LEU B 1 346 ? 109.490 129.314 144.792 1.00 29.75 ?  346 LEU B N     1 
ATOM   8357  C  CA    . LEU B 1 346 ? 110.491 130.046 145.563 1.00 23.48 ?  346 LEU B CA    1 
ATOM   8358  C  C     . LEU B 1 346 ? 110.907 129.258 146.798 1.00 27.62 ?  346 LEU B C     1 
ATOM   8359  O  O     . LEU B 1 346 ? 112.099 129.144 147.106 1.00 30.54 ?  346 LEU B O     1 
ATOM   8360  C  CB    . LEU B 1 346 ? 109.947 131.416 145.973 1.00 24.10 ?  346 LEU B CB    1 
ATOM   8361  C  CG    . LEU B 1 346 ? 109.621 132.455 144.901 1.00 26.77 ?  346 LEU B CG    1 
ATOM   8362  C  CD1   . LEU B 1 346 ? 108.978 133.674 145.535 1.00 28.15 ?  346 LEU B CD1   1 
ATOM   8363  C  CD2   . LEU B 1 346 ? 110.866 132.850 144.142 1.00 26.32 ?  346 LEU B CD2   1 
ATOM   8364  N  N     . ALA B 1 347 ? 109.929 128.705 147.517 1.00 26.89 ?  347 ALA B N     1 
ATOM   8365  C  CA    . ALA B 1 347 ? 110.235 127.937 148.721 1.00 20.29 ?  347 ALA B CA    1 
ATOM   8366  C  C     . ALA B 1 347 ? 111.035 126.682 148.393 1.00 29.91 ?  347 ALA B C     1 
ATOM   8367  O  O     . ALA B 1 347 ? 111.990 126.346 149.103 1.00 35.16 ?  347 ALA B O     1 
ATOM   8368  C  CB    . ALA B 1 347 ? 108.945 127.575 149.455 1.00 22.69 ?  347 ALA B CB    1 
ATOM   8369  N  N     . MET B 1 348 ? 110.664 125.980 147.320 1.00 31.69 ?  348 MET B N     1 
ATOM   8370  C  CA    . MET B 1 348 ? 111.404 124.790 146.915 1.00 29.01 ?  348 MET B CA    1 
ATOM   8371  C  C     . MET B 1 348 ? 112.831 125.137 146.515 1.00 31.20 ?  348 MET B C     1 
ATOM   8372  O  O     . MET B 1 348 ? 113.777 124.432 146.887 1.00 35.64 ?  348 MET B O     1 
ATOM   8373  C  CB    . MET B 1 348 ? 110.677 124.092 145.765 1.00 31.96 ?  348 MET B CB    1 
ATOM   8374  C  CG    . MET B 1 348 ? 111.519 123.073 145.013 1.00 38.36 ?  348 MET B CG    1 
ATOM   8375  S  SD    . MET B 1 348 ? 111.922 123.611 143.340 1.00 53.07 ?  348 MET B SD    1 
ATOM   8376  C  CE    . MET B 1 348 ? 110.286 123.783 142.636 1.00 37.32 ?  348 MET B CE    1 
ATOM   8377  N  N     . LEU B 1 349 ? 113.008 126.223 145.761 1.00 28.67 ?  349 LEU B N     1 
ATOM   8378  C  CA    . LEU B 1 349 ? 114.346 126.640 145.359 1.00 25.58 ?  349 LEU B CA    1 
ATOM   8379  C  C     . LEU B 1 349 ? 115.192 127.015 146.567 1.00 25.72 ?  349 LEU B C     1 
ATOM   8380  O  O     . LEU B 1 349 ? 116.383 126.687 146.624 1.00 30.40 ?  349 LEU B O     1 
ATOM   8381  C  CB    . LEU B 1 349 ? 114.256 127.816 144.387 1.00 30.48 ?  349 LEU B CB    1 
ATOM   8382  C  CG    . LEU B 1 349 ? 114.657 127.562 142.936 1.00 31.43 ?  349 LEU B CG    1 
ATOM   8383  C  CD1   . LEU B 1 349 ? 113.514 126.926 142.163 1.00 31.89 ?  349 LEU B CD1   1 
ATOM   8384  C  CD2   . LEU B 1 349 ? 115.093 128.863 142.290 1.00 28.13 ?  349 LEU B CD2   1 
ATOM   8385  N  N     . ARG B 1 350 ? 114.602 127.717 147.536 1.00 25.07 ?  350 ARG B N     1 
ATOM   8386  C  CA    . ARG B 1 350 ? 115.349 128.083 148.734 1.00 25.84 ?  350 ARG B CA    1 
ATOM   8387  C  C     . ARG B 1 350 ? 115.687 126.864 149.580 1.00 28.68 ?  350 ARG B C     1 
ATOM   8388  O  O     . ARG B 1 350 ? 116.752 126.823 150.205 1.00 33.54 ?  350 ARG B O     1 
ATOM   8389  C  CB    . ARG B 1 350 ? 114.562 129.107 149.550 1.00 22.89 ?  350 ARG B CB    1 
ATOM   8390  C  CG    . ARG B 1 350 ? 114.421 130.458 148.869 1.00 23.30 ?  350 ARG B CG    1 
ATOM   8391  C  CD    . ARG B 1 350 ? 113.439 131.352 149.602 1.00 23.06 ?  350 ARG B CD    1 
ATOM   8392  N  NE    . ARG B 1 350 ? 113.816 131.540 150.997 1.00 34.99 ?  350 ARG B NE    1 
ATOM   8393  C  CZ    . ARG B 1 350 ? 114.789 132.339 151.411 1.00 31.12 ?  350 ARG B CZ    1 
ATOM   8394  N  NH1   . ARG B 1 350 ? 115.506 133.056 150.562 1.00 26.96 1  350 ARG B NH1   1 
ATOM   8395  N  NH2   . ARG B 1 350 ? 115.051 132.420 152.712 1.00 27.93 ?  350 ARG B NH2   1 
ATOM   8396  N  N     . SER B 1 351 ? 114.800 125.870 149.623 1.00 28.79 ?  351 SER B N     1 
ATOM   8397  C  CA    . SER B 1 351 ? 115.124 124.628 150.315 1.00 29.95 ?  351 SER B CA    1 
ATOM   8398  C  C     . SER B 1 351 ? 116.270 123.896 149.631 1.00 33.63 ?  351 SER B C     1 
ATOM   8399  O  O     . SER B 1 351 ? 117.168 123.371 150.300 1.00 40.76 ?  351 SER B O     1 
ATOM   8400  C  CB    . SER B 1 351 ? 113.888 123.733 150.396 1.00 31.21 ?  351 SER B CB    1 
ATOM   8401  O  OG    . SER B 1 351 ? 112.806 124.411 151.010 1.00 36.59 ?  351 SER B OG    1 
ATOM   8402  N  N     . GLU B 1 352 ? 116.261 123.852 148.297 1.00 31.55 ?  352 GLU B N     1 
ATOM   8403  C  CA    . GLU B 1 352 ? 117.281 123.097 147.576 1.00 30.05 ?  352 GLU B CA    1 
ATOM   8404  C  C     . GLU B 1 352 ? 118.639 123.791 147.614 1.00 35.96 ?  352 GLU B C     1 
ATOM   8405  O  O     . GLU B 1 352 ? 119.662 123.141 147.858 1.00 39.68 ?  352 GLU B O     1 
ATOM   8406  C  CB    . GLU B 1 352 ? 116.841 122.864 146.130 1.00 34.33 ?  352 GLU B CB    1 
ATOM   8407  C  CG    . GLU B 1 352 ? 115.571 122.043 145.989 1.00 36.76 ?  352 GLU B CG    1 
ATOM   8408  C  CD    . GLU B 1 352 ? 115.083 121.968 144.557 1.00 41.55 ?  352 GLU B CD    1 
ATOM   8409  O  OE1   . GLU B 1 352 ? 115.335 122.921 143.790 1.00 38.58 ?  352 GLU B OE1   1 
ATOM   8410  O  OE2   . GLU B 1 352 ? 114.445 120.956 144.197 1.00 41.64 -1 352 GLU B OE2   1 
ATOM   8411  N  N     . SER B 1 353 ? 118.675 125.105 147.379 1.00 34.01 ?  353 SER B N     1 
ATOM   8412  C  CA    . SER B 1 353 ? 119.939 125.807 147.202 1.00 35.75 ?  353 SER B CA    1 
ATOM   8413  C  C     . SER B 1 353 ? 120.072 127.095 148.005 1.00 31.83 ?  353 SER B C     1 
ATOM   8414  O  O     . SER B 1 353 ? 121.135 127.722 147.953 1.00 34.71 ?  353 SER B O     1 
ATOM   8415  C  CB    . SER B 1 353 ? 120.162 126.127 145.716 1.00 35.48 ?  353 SER B CB    1 
ATOM   8416  O  OG    . SER B 1 353 ? 119.197 127.050 145.243 1.00 36.62 ?  353 SER B OG    1 
ATOM   8417  N  N     . GLY B 1 354 ? 119.041 127.511 148.736 1.00 22.19 ?  354 GLY B N     1 
ATOM   8418  C  CA    . GLY B 1 354 ? 119.102 128.752 149.478 1.00 23.41 ?  354 GLY B CA    1 
ATOM   8419  C  C     . GLY B 1 354 ? 118.798 129.997 148.675 1.00 21.72 ?  354 GLY B C     1 
ATOM   8420  O  O     . GLY B 1 354 ? 118.820 131.097 149.238 1.00 28.76 ?  354 GLY B O     1 
ATOM   8421  N  N     . TYR B 1 355 ? 118.514 129.860 147.388 1.00 25.60 ?  355 TYR B N     1 
ATOM   8422  C  CA    . TYR B 1 355 ? 118.175 130.952 146.496 1.00 17.85 ?  355 TYR B CA    1 
ATOM   8423  C  C     . TYR B 1 355 ? 116.709 130.863 146.097 1.00 20.21 ?  355 TYR B C     1 
ATOM   8424  O  O     . TYR B 1 355 ? 116.120 129.779 146.116 1.00 28.32 ?  355 TYR B O     1 
ATOM   8425  C  CB    . TYR B 1 355 ? 119.061 130.910 145.244 1.00 22.73 ?  355 TYR B CB    1 
ATOM   8426  C  CG    . TYR B 1 355 ? 120.508 131.238 145.511 1.00 25.91 ?  355 TYR B CG    1 
ATOM   8427  C  CD1   . TYR B 1 355 ? 120.865 132.412 146.158 1.00 23.53 ?  355 TYR B CD1   1 
ATOM   8428  C  CD2   . TYR B 1 355 ? 121.520 130.371 145.121 1.00 26.75 ?  355 TYR B CD2   1 
ATOM   8429  C  CE1   . TYR B 1 355 ? 122.185 132.715 146.407 1.00 26.24 ?  355 TYR B CE1   1 
ATOM   8430  C  CE2   . TYR B 1 355 ? 122.845 130.667 145.365 1.00 28.07 ?  355 TYR B CE2   1 
ATOM   8431  C  CZ    . TYR B 1 355 ? 123.172 131.841 146.009 1.00 29.17 ?  355 TYR B CZ    1 
ATOM   8432  O  OH    . TYR B 1 355 ? 124.490 132.142 146.256 1.00 30.83 ?  355 TYR B OH    1 
ATOM   8433  N  N     . PRO B 1 356 ? 116.080 131.982 145.716 1.00 21.44 ?  356 PRO B N     1 
ATOM   8434  C  CA    . PRO B 1 356 ? 116.599 133.349 145.600 1.00 17.78 ?  356 PRO B CA    1 
ATOM   8435  C  C     . PRO B 1 356 ? 116.602 134.139 146.899 1.00 17.32 ?  356 PRO B C     1 
ATOM   8436  O  O     . PRO B 1 356 ? 115.975 133.759 147.883 1.00 20.04 ?  356 PRO B O     1 
ATOM   8437  C  CB    . PRO B 1 356 ? 115.634 133.980 144.595 1.00 16.77 ?  356 PRO B CB    1 
ATOM   8438  C  CG    . PRO B 1 356 ? 114.328 133.338 144.934 1.00 19.79 ?  356 PRO B CG    1 
ATOM   8439  C  CD    . PRO B 1 356 ? 114.672 131.909 145.285 1.00 17.79 ?  356 PRO B CD    1 
ATOM   8440  N  N     . TYR B 1 357 ? 117.320 135.258 146.915 1.00 23.57 ?  357 TYR B N     1 
ATOM   8441  C  CA    . TYR B 1 357 ? 117.079 136.273 147.925 1.00 11.38 ?  357 TYR B CA    1 
ATOM   8442  C  C     . TYR B 1 357 ? 115.685 136.849 147.724 1.00 17.94 ?  357 TYR B C     1 
ATOM   8443  O  O     . TYR B 1 357 ? 115.228 137.025 146.591 1.00 26.55 ?  357 TYR B O     1 
ATOM   8444  C  CB    . TYR B 1 357 ? 118.122 137.387 147.838 1.00 16.41 ?  357 TYR B CB    1 
ATOM   8445  C  CG    . TYR B 1 357 ? 119.558 136.914 147.809 1.00 21.16 ?  357 TYR B CG    1 
ATOM   8446  C  CD1   . TYR B 1 357 ? 119.946 135.773 148.491 1.00 15.33 ?  357 TYR B CD1   1 
ATOM   8447  C  CD2   . TYR B 1 357 ? 120.525 137.613 147.100 1.00 20.38 ?  357 TYR B CD2   1 
ATOM   8448  C  CE1   . TYR B 1 357 ? 121.253 135.339 148.473 1.00 20.34 ?  357 TYR B CE1   1 
ATOM   8449  C  CE2   . TYR B 1 357 ? 121.836 137.185 147.073 1.00 15.32 ?  357 TYR B CE2   1 
ATOM   8450  C  CZ    . TYR B 1 357 ? 122.195 136.046 147.762 1.00 21.33 ?  357 TYR B CZ    1 
ATOM   8451  O  OH    . TYR B 1 357 ? 123.499 135.613 147.743 1.00 31.57 ?  357 TYR B OH    1 
ATOM   8452  N  N     . ILE B 1 358 ? 115.001 137.137 148.824 1.00 15.26 ?  358 ILE B N     1 
ATOM   8453  C  CA    . ILE B 1 358 ? 113.649 137.678 148.781 1.00 14.09 ?  358 ILE B CA    1 
ATOM   8454  C  C     . ILE B 1 358 ? 113.709 139.119 149.260 1.00 15.26 ?  358 ILE B C     1 
ATOM   8455  O  O     . ILE B 1 358 ? 114.163 139.390 150.377 1.00 24.51 ?  358 ILE B O     1 
ATOM   8456  C  CB    . ILE B 1 358 ? 112.678 136.851 149.636 1.00 23.12 ?  358 ILE B CB    1 
ATOM   8457  C  CG1   . ILE B 1 358 ? 112.575 135.422 149.099 1.00 15.21 ?  358 ILE B CG1   1 
ATOM   8458  C  CG2   . ILE B 1 358 ? 111.308 137.507 149.660 1.00 16.12 ?  358 ILE B CG2   1 
ATOM   8459  C  CD1   . ILE B 1 358 ? 112.093 135.341 147.670 1.00 19.53 ?  358 ILE B CD1   1 
ATOM   8460  N  N     . MET B 1 359 ? 113.257 140.040 148.414 1.00 17.72 ?  359 MET B N     1 
ATOM   8461  C  CA    . MET B 1 359 ? 113.174 141.456 148.754 1.00 7.28  ?  359 MET B CA    1 
ATOM   8462  C  C     . MET B 1 359 ? 111.713 141.874 148.682 1.00 9.30  ?  359 MET B C     1 
ATOM   8463  O  O     . MET B 1 359 ? 111.124 141.908 147.596 1.00 20.49 ?  359 MET B O     1 
ATOM   8464  C  CB    . MET B 1 359 ? 114.030 142.305 147.818 1.00 8.65  ?  359 MET B CB    1 
ATOM   8465  C  CG    . MET B 1 359 ? 114.125 143.762 148.234 1.00 9.10  ?  359 MET B CG    1 
ATOM   8466  S  SD    . MET B 1 359 ? 114.306 144.884 146.841 1.00 32.53 ?  359 MET B SD    1 
ATOM   8467  C  CE    . MET B 1 359 ? 113.483 146.339 147.471 1.00 9.56  ?  359 MET B CE    1 
ATOM   8468  N  N     . PHE B 1 360 ? 111.128 142.185 149.834 1.00 10.36 ?  360 PHE B N     1 
ATOM   8469  C  CA    . PHE B 1 360 ? 109.750 142.665 149.891 1.00 10.65 ?  360 PHE B CA    1 
ATOM   8470  C  C     . PHE B 1 360 ? 109.772 144.156 149.586 1.00 16.04 ?  360 PHE B C     1 
ATOM   8471  O  O     . PHE B 1 360 ? 110.033 144.979 150.465 1.00 19.76 ?  360 PHE B O     1 
ATOM   8472  C  CB    . PHE B 1 360 ? 109.138 142.364 151.251 1.00 12.02 ?  360 PHE B CB    1 
ATOM   8473  C  CG    . PHE B 1 360 ? 109.001 140.896 151.534 1.00 15.34 ?  360 PHE B CG    1 
ATOM   8474  C  CD1   . PHE B 1 360 ? 108.198 140.096 150.740 1.00 15.19 ?  360 PHE B CD1   1 
ATOM   8475  C  CD2   . PHE B 1 360 ? 109.691 140.313 152.583 1.00 14.96 ?  360 PHE B CD2   1 
ATOM   8476  C  CE1   . PHE B 1 360 ? 108.078 138.743 150.994 1.00 13.79 ?  360 PHE B CE1   1 
ATOM   8477  C  CE2   . PHE B 1 360 ? 109.574 138.962 152.841 1.00 14.37 ?  360 PHE B CE2   1 
ATOM   8478  C  CZ    . PHE B 1 360 ? 108.766 138.177 152.046 1.00 17.05 ?  360 PHE B CZ    1 
ATOM   8479  N  N     . GLN B 1 361 ? 109.487 144.499 148.326 1.00 16.85 ?  361 GLN B N     1 
ATOM   8480  C  CA    . GLN B 1 361 ? 109.693 145.862 147.844 1.00 9.93  ?  361 GLN B CA    1 
ATOM   8481  C  C     . GLN B 1 361 ? 108.861 146.871 148.623 1.00 13.61 ?  361 GLN B C     1 
ATOM   8482  O  O     . GLN B 1 361 ? 109.351 147.950 148.978 1.00 15.15 ?  361 GLN B O     1 
ATOM   8483  C  CB    . GLN B 1 361 ? 109.360 145.935 146.354 1.00 15.59 ?  361 GLN B CB    1 
ATOM   8484  C  CG    . GLN B 1 361 ? 109.635 147.279 145.712 1.00 15.46 ?  361 GLN B CG    1 
ATOM   8485  C  CD    . GLN B 1 361 ? 109.843 147.172 144.219 1.00 17.89 ?  361 GLN B CD    1 
ATOM   8486  O  OE1   . GLN B 1 361 ? 109.181 146.386 143.544 1.00 27.70 ?  361 GLN B OE1   1 
ATOM   8487  N  NE2   . GLN B 1 361 ? 110.771 147.961 143.691 1.00 18.34 ?  361 GLN B NE2   1 
ATOM   8488  N  N     . ASP B 1 362 ? 107.595 146.544 148.893 1.00 20.04 ?  362 ASP B N     1 
ATOM   8489  C  CA    . ASP B 1 362 ? 106.738 147.482 149.607 1.00 15.90 ?  362 ASP B CA    1 
ATOM   8490  C  C     . ASP B 1 362 ? 107.172 147.651 151.056 1.00 16.17 ?  362 ASP B C     1 
ATOM   8491  O  O     . ASP B 1 362 ? 107.069 148.752 151.604 1.00 23.66 ?  362 ASP B O     1 
ATOM   8492  C  CB    . ASP B 1 362 ? 105.283 147.029 149.532 1.00 22.13 ?  362 ASP B CB    1 
ATOM   8493  C  CG    . ASP B 1 362 ? 104.632 147.393 148.215 1.00 29.34 ?  362 ASP B CG    1 
ATOM   8494  O  OD1   . ASP B 1 362 ? 104.914 146.717 147.203 1.00 29.39 ?  362 ASP B OD1   1 
ATOM   8495  O  OD2   . ASP B 1 362 ? 103.838 148.356 148.190 1.00 30.44 -1 362 ASP B OD2   1 
ATOM   8496  N  N     . ASN B 1 363 ? 107.667 146.584 151.688 1.00 21.55 ?  363 ASN B N     1 
ATOM   8497  C  CA    . ASN B 1 363 ? 108.215 146.716 153.033 1.00 10.88 ?  363 ASN B CA    1 
ATOM   8498  C  C     . ASN B 1 363 ? 109.424 147.639 153.051 1.00 14.86 ?  363 ASN B C     1 
ATOM   8499  O  O     . ASN B 1 363 ? 109.632 148.374 154.022 1.00 25.42 ?  363 ASN B O     1 
ATOM   8500  C  CB    . ASN B 1 363 ? 108.593 145.341 153.585 1.00 12.50 ?  363 ASN B CB    1 
ATOM   8501  C  CG    . ASN B 1 363 ? 107.386 144.531 154.005 1.00 16.62 ?  363 ASN B CG    1 
ATOM   8502  O  OD1   . ASN B 1 363 ? 106.317 145.079 154.264 1.00 21.40 ?  363 ASN B OD1   1 
ATOM   8503  N  ND2   . ASN B 1 363 ? 107.551 143.217 154.073 1.00 15.52 ?  363 ASN B ND2   1 
ATOM   8504  N  N     . VAL B 1 364 ? 110.236 147.609 151.992 1.00 14.12 ?  364 VAL B N     1 
ATOM   8505  C  CA    . VAL B 1 364 ? 111.385 148.502 151.906 1.00 9.03  ?  364 VAL B CA    1 
ATOM   8506  C  C     . VAL B 1 364 ? 110.934 149.940 151.683 1.00 16.84 ?  364 VAL B C     1 
ATOM   8507  O  O     . VAL B 1 364 ? 111.461 150.871 152.303 1.00 18.99 ?  364 VAL B O     1 
ATOM   8508  C  CB    . VAL B 1 364 ? 112.338 148.035 150.792 1.00 2.44  ?  364 VAL B CB    1 
ATOM   8509  C  CG1   . VAL B 1 364 ? 113.571 148.915 150.750 1.00 6.38  ?  364 VAL B CG1   1 
ATOM   8510  C  CG2   . VAL B 1 364 ? 112.724 146.585 150.999 1.00 9.06  ?  364 VAL B CG2   1 
ATOM   8511  N  N     . ASN B 1 365 ? 109.956 150.147 150.804 1.00 18.91 ?  365 ASN B N     1 
ATOM   8512  C  CA    . ASN B 1 365 ? 109.617 151.489 150.350 1.00 7.74  ?  365 ASN B CA    1 
ATOM   8513  C  C     . ASN B 1 365 ? 108.554 152.180 151.195 1.00 15.37 ?  365 ASN B C     1 
ATOM   8514  O  O     . ASN B 1 365 ? 108.338 153.382 151.012 1.00 22.95 ?  365 ASN B O     1 
ATOM   8515  C  CB    . ASN B 1 365 ? 109.155 151.449 148.891 1.00 11.88 ?  365 ASN B CB    1 
ATOM   8516  C  CG    . ASN B 1 365 ? 110.295 151.196 147.930 1.00 13.44 ?  365 ASN B CG    1 
ATOM   8517  O  OD1   . ASN B 1 365 ? 111.321 151.872 147.976 1.00 15.79 ?  365 ASN B OD1   1 
ATOM   8518  N  ND2   . ASN B 1 365 ? 110.124 150.217 147.055 1.00 19.25 ?  365 ASN B ND2   1 
ATOM   8519  N  N     . LYS B 1 366 ? 107.888 151.471 152.107 1.00 15.39 ?  366 LYS B N     1 
ATOM   8520  C  CA    . LYS B 1 366 ? 106.940 152.135 152.991 1.00 17.04 ?  366 LYS B CA    1 
ATOM   8521  C  C     . LYS B 1 366 ? 107.636 152.934 154.083 1.00 19.24 ?  366 LYS B C     1 
ATOM   8522  O  O     . LYS B 1 366 ? 107.026 153.848 154.649 1.00 26.94 ?  366 LYS B O     1 
ATOM   8523  C  CB    . LYS B 1 366 ? 105.991 151.113 153.621 1.00 18.92 ?  366 LYS B CB    1 
ATOM   8524  C  CG    . LYS B 1 366 ? 106.675 150.064 154.483 1.00 22.26 ?  366 LYS B CG    1 
ATOM   8525  C  CD    . LYS B 1 366 ? 105.700 149.422 155.462 1.00 24.45 ?  366 LYS B CD    1 
ATOM   8526  C  CE    . LYS B 1 366 ? 104.337 149.181 154.829 1.00 24.01 ?  366 LYS B CE    1 
ATOM   8527  N  NZ    . LYS B 1 366 ? 104.351 148.037 153.877 1.00 24.16 1  366 LYS B NZ    1 
ATOM   8528  N  N     . VAL B 1 367 ? 108.891 152.612 154.386 1.00 24.11 ?  367 VAL B N     1 
ATOM   8529  C  CA    . VAL B 1 367 ? 109.697 153.363 155.337 1.00 14.42 ?  367 VAL B CA    1 
ATOM   8530  C  C     . VAL B 1 367 ? 110.947 153.946 154.700 1.00 16.80 ?  367 VAL B C     1 
ATOM   8531  O  O     . VAL B 1 367 ? 111.767 154.540 155.406 1.00 22.49 ?  367 VAL B O     1 
ATOM   8532  C  CB    . VAL B 1 367 ? 110.073 152.500 156.559 1.00 12.46 ?  367 VAL B CB    1 
ATOM   8533  C  CG1   . VAL B 1 367 ? 108.823 152.089 157.318 1.00 19.88 ?  367 VAL B CG1   1 
ATOM   8534  C  CG2   . VAL B 1 367 ? 110.855 151.279 156.119 1.00 9.76  ?  367 VAL B CG2   1 
ATOM   8535  N  N     . HIS B 1 368 ? 111.117 153.787 153.390 1.00 20.92 ?  368 HIS B N     1 
ATOM   8536  C  CA    . HIS B 1 368 ? 112.265 154.353 152.696 1.00 5.32  ?  368 HIS B CA    1 
ATOM   8537  C  C     . HIS B 1 368 ? 112.211 155.874 152.750 1.00 15.48 ?  368 HIS B C     1 
ATOM   8538  O  O     . HIS B 1 368 ? 111.191 156.484 152.414 1.00 25.96 ?  368 HIS B O     1 
ATOM   8539  C  CB    . HIS B 1 368 ? 112.286 153.868 151.249 1.00 13.01 ?  368 HIS B CB    1 
ATOM   8540  C  CG    . HIS B 1 368 ? 113.482 154.320 150.472 1.00 10.56 ?  368 HIS B CG    1 
ATOM   8541  N  ND1   . HIS B 1 368 ? 113.426 154.607 149.126 1.00 14.86 ?  368 HIS B ND1   1 
ATOM   8542  C  CD2   . HIS B 1 368 ? 114.764 154.528 150.849 1.00 7.35  ?  368 HIS B CD2   1 
ATOM   8543  C  CE1   . HIS B 1 368 ? 114.624 154.974 148.708 1.00 14.41 ?  368 HIS B CE1   1 
ATOM   8544  N  NE2   . HIS B 1 368 ? 115.454 154.935 149.734 1.00 10.81 ?  368 HIS B NE2   1 
ATOM   8545  N  N     . ALA B 1 369 ? 113.315 156.487 153.174 1.00 20.22 ?  369 ALA B N     1 
ATOM   8546  C  CA    . ALA B 1 369 ? 113.357 157.927 153.374 1.00 10.07 ?  369 ALA B CA    1 
ATOM   8547  C  C     . ALA B 1 369 ? 113.662 158.707 152.104 1.00 17.57 ?  369 ALA B C     1 
ATOM   8548  O  O     . ALA B 1 369 ? 113.504 159.932 152.101 1.00 26.04 ?  369 ALA B O     1 
ATOM   8549  C  CB    . ALA B 1 369 ? 114.394 158.273 154.443 1.00 10.84 ?  369 ALA B CB    1 
ATOM   8550  N  N     . ASN B 1 370 ? 114.086 158.042 151.033 1.00 16.15 ?  370 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 370 ? 114.511 158.710 149.810 1.00 14.72 ?  370 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 370 ? 113.728 158.210 148.604 1.00 12.00 ?  370 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 370 ? 114.285 157.986 147.527 1.00 18.38 ?  370 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 370 ? 116.011 158.530 149.593 1.00 11.27 ?  370 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 370 ? 116.834 159.093 150.732 1.00 11.90 ?  370 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 370 ? 116.763 160.283 151.034 1.00 26.54 ?  370 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 370 ? 117.618 158.238 151.375 1.00 16.28 ?  370 ASN B ND2   1 
ATOM   8558  N  N     . ASN B 1 371 ? 112.417 158.025 148.772 1.00 20.31 ?  371 ASN B N     1 
ATOM   8559  C  CA    . ASN B 1 371 ? 111.572 157.620 147.657 1.00 10.79 ?  371 ASN B CA    1 
ATOM   8560  C  C     . ASN B 1 371 ? 111.498 158.684 146.571 1.00 16.41 ?  371 ASN B C     1 
ATOM   8561  O  O     . ASN B 1 371 ? 111.232 158.352 145.413 1.00 19.64 ?  371 ASN B O     1 
ATOM   8562  C  CB    . ASN B 1 371 ? 110.164 157.289 148.153 1.00 6.58  ?  371 ASN B CB    1 
ATOM   8563  C  CG    . ASN B 1 371 ? 110.040 155.863 148.641 1.00 16.28 ?  371 ASN B CG    1 
ATOM   8564  O  OD1   . ASN B 1 371 ? 110.808 154.989 148.241 1.00 20.36 ?  371 ASN B OD1   1 
ATOM   8565  N  ND2   . ASN B 1 371 ? 109.067 155.618 149.509 1.00 19.92 ?  371 ASN B ND2   1 
ATOM   8566  N  N     . HIS B 1 372 ? 111.719 159.953 146.925 1.00 21.65 ?  372 HIS B N     1 
ATOM   8567  C  CA    . HIS B 1 372 ? 111.710 161.018 145.928 1.00 17.77 ?  372 HIS B CA    1 
ATOM   8568  C  C     . HIS B 1 372 ? 112.827 160.829 144.909 1.00 20.25 ?  372 HIS B C     1 
ATOM   8569  O  O     . HIS B 1 372 ? 112.619 161.026 143.707 1.00 26.17 ?  372 HIS B O     1 
ATOM   8570  C  CB    . HIS B 1 372 ? 111.835 162.376 146.618 1.00 19.55 ?  372 HIS B CB    1 
ATOM   8571  C  CG    . HIS B 1 372 ? 113.143 162.579 147.314 1.00 19.08 ?  372 HIS B CG    1 
ATOM   8572  N  ND1   . HIS B 1 372 ? 113.568 161.777 148.351 1.00 22.10 ?  372 HIS B ND1   1 
ATOM   8573  C  CD2   . HIS B 1 372 ? 114.127 163.487 147.114 1.00 20.71 ?  372 HIS B CD2   1 
ATOM   8574  C  CE1   . HIS B 1 372 ? 114.756 162.183 148.761 1.00 17.13 ?  372 HIS B CE1   1 
ATOM   8575  N  NE2   . HIS B 1 372 ? 115.115 163.221 148.029 1.00 24.73 ?  372 HIS B NE2   1 
ATOM   8576  N  N     . ILE B 1 373 ? 114.024 160.459 145.373 1.00 16.01 ?  373 ILE B N     1 
ATOM   8577  C  CA    . ILE B 1 373 ? 115.123 160.179 144.455 1.00 18.41 ?  373 ILE B CA    1 
ATOM   8578  C  C     . ILE B 1 373 ? 114.781 158.977 143.587 1.00 18.51 ?  373 ILE B C     1 
ATOM   8579  O  O     . ILE B 1 373 ? 114.860 159.033 142.353 1.00 28.73 ?  373 ILE B O     1 
ATOM   8580  C  CB    . ILE B 1 373 ? 116.428 159.947 145.237 1.00 20.64 ?  373 ILE B CB    1 
ATOM   8581  C  CG1   . ILE B 1 373 ? 116.796 161.194 146.037 1.00 18.92 ?  373 ILE B CG1   1 
ATOM   8582  C  CG2   . ILE B 1 373 ? 117.556 159.555 144.296 1.00 19.25 ?  373 ILE B CG2   1 
ATOM   8583  C  CD1   . ILE B 1 373 ? 117.877 160.967 147.060 1.00 14.77 ?  373 ILE B CD1   1 
ATOM   8584  N  N     . SER B 1 374 ? 114.372 157.883 144.224 1.00 17.14 ?  374 SER B N     1 
ATOM   8585  C  CA    . SER B 1 374 ? 113.993 156.651 143.549 1.00 6.86  ?  374 SER B CA    1 
ATOM   8586  C  C     . SER B 1 374 ? 113.481 155.656 144.577 1.00 13.56 ?  374 SER B C     1 
ATOM   8587  O  O     . SER B 1 374 ? 113.852 155.728 145.752 1.00 16.95 ?  374 SER B O     1 
ATOM   8588  C  CB    . SER B 1 374 ? 115.176 156.059 142.782 1.00 18.97 ?  374 SER B CB    1 
ATOM   8589  O  OG    . SER B 1 374 ? 114.738 155.161 141.782 1.00 32.64 ?  374 SER B OG    1 
ATOM   8590  N  N     . LYS B 1 375 ? 112.625 154.733 144.157 1.00 24.02 ?  375 LYS B N     1 
ATOM   8591  C  CA    . LYS B 1 375 ? 112.258 153.623 145.017 1.00 14.13 ?  375 LYS B CA    1 
ATOM   8592  C  C     . LYS B 1 375 ? 113.357 152.570 144.993 1.00 15.05 ?  375 LYS B C     1 
ATOM   8593  O  O     . LYS B 1 375 ? 114.096 152.436 144.015 1.00 23.95 ?  375 LYS B O     1 
ATOM   8594  C  CB    . LYS B 1 375 ? 110.932 153.005 144.576 1.00 11.94 ?  375 LYS B CB    1 
ATOM   8595  C  CG    . LYS B 1 375 ? 109.760 153.965 144.603 1.00 17.96 ?  375 LYS B CG    1 
ATOM   8596  C  CD    . LYS B 1 375 ? 108.801 153.628 145.728 1.00 17.81 ?  375 LYS B CD    1 
ATOM   8597  C  CE    . LYS B 1 375 ? 107.599 154.553 145.719 1.00 16.98 ?  375 LYS B CE    1 
ATOM   8598  N  NZ    . LYS B 1 375 ? 107.970 155.938 145.322 1.00 23.96 1  375 LYS B NZ    1 
ATOM   8599  N  N     . VAL B 1 376 ? 113.471 151.826 146.088 1.00 9.75  ?  376 VAL B N     1 
ATOM   8600  C  CA    . VAL B 1 376 ? 114.436 150.735 146.153 1.00 13.73 ?  376 VAL B CA    1 
ATOM   8601  C  C     . VAL B 1 376 ? 113.883 149.565 145.351 1.00 16.12 ?  376 VAL B C     1 
ATOM   8602  O  O     . VAL B 1 376 ? 112.842 148.998 145.699 1.00 23.12 ?  376 VAL B O     1 
ATOM   8603  C  CB    . VAL B 1 376 ? 114.723 150.331 147.604 1.00 11.90 ?  376 VAL B CB    1 
ATOM   8604  C  CG1   . VAL B 1 376 ? 115.774 149.237 147.643 1.00 10.55 ?  376 VAL B CG1   1 
ATOM   8605  C  CG2   . VAL B 1 376 ? 115.174 151.534 148.409 1.00 6.92  ?  376 VAL B CG2   1 
ATOM   8606  N  N     . LYS B 1 377 ? 114.574 149.205 144.271 1.00 14.55 ?  377 LYS B N     1 
ATOM   8607  C  CA    . LYS B 1 377 ? 114.093 148.166 143.372 1.00 9.58  ?  377 LYS B CA    1 
ATOM   8608  C  C     . LYS B 1 377 ? 114.829 146.845 143.519 1.00 9.63  ?  377 LYS B C     1 
ATOM   8609  O  O     . LYS B 1 377 ? 114.353 145.835 142.995 1.00 24.47 ?  377 LYS B O     1 
ATOM   8610  C  CB    . LYS B 1 377 ? 114.199 148.626 141.914 1.00 13.22 ?  377 LYS B CB    1 
ATOM   8611  C  CG    . LYS B 1 377 ? 113.664 150.014 141.659 1.00 9.80  ?  377 LYS B CG    1 
ATOM   8612  C  CD    . LYS B 1 377 ? 114.491 150.705 140.599 1.00 18.20 ?  377 LYS B CD    1 
ATOM   8613  C  CE    . LYS B 1 377 ? 114.529 152.198 140.821 1.00 20.76 ?  377 LYS B CE    1 
ATOM   8614  N  NZ    . LYS B 1 377 ? 115.593 152.840 140.003 1.00 19.82 1  377 LYS B NZ    1 
ATOM   8615  N  N     . PHE B 1 378 ? 115.972 146.827 144.197 1.00 11.14 ?  378 PHE B N     1 
ATOM   8616  C  CA    . PHE B 1 378 ? 116.736 145.600 144.380 1.00 8.11  ?  378 PHE B CA    1 
ATOM   8617  C  C     . PHE B 1 378 ? 117.693 145.798 145.548 1.00 7.41  ?  378 PHE B C     1 
ATOM   8618  O  O     . PHE B 1 378 ? 117.818 146.897 146.095 1.00 16.36 ?  378 PHE B O     1 
ATOM   8619  C  CB    . PHE B 1 378 ? 117.464 145.201 143.092 1.00 4.29  ?  378 PHE B CB    1 
ATOM   8620  C  CG    . PHE B 1 378 ? 118.639 146.072 142.749 1.00 4.17  ?  378 PHE B CG    1 
ATOM   8621  C  CD1   . PHE B 1 378 ? 118.474 147.424 142.505 1.00 10.59 ?  378 PHE B CD1   1 
ATOM   8622  C  CD2   . PHE B 1 378 ? 119.907 145.530 142.649 1.00 3.19  ?  378 PHE B CD2   1 
ATOM   8623  C  CE1   . PHE B 1 378 ? 119.550 148.220 142.185 1.00 7.65  ?  378 PHE B CE1   1 
ATOM   8624  C  CE2   . PHE B 1 378 ? 120.986 146.322 142.326 1.00 10.18 ?  378 PHE B CE2   1 
ATOM   8625  C  CZ    . PHE B 1 378 ? 120.807 147.670 142.092 1.00 11.71 ?  378 PHE B CZ    1 
ATOM   8626  N  N     . SER B 1 379 ? 118.363 144.719 145.931 1.00 2.13  ?  379 SER B N     1 
ATOM   8627  C  CA    . SER B 1 379 ? 119.290 144.716 147.054 1.00 0.54  ?  379 SER B CA    1 
ATOM   8628  C  C     . SER B 1 379 ? 120.672 144.284 146.570 1.00 4.59  ?  379 SER B C     1 
ATOM   8629  O  O     . SER B 1 379 ? 120.909 144.104 145.373 1.00 7.64  ?  379 SER B O     1 
ATOM   8630  C  CB    . SER B 1 379 ? 118.773 143.810 148.173 1.00 10.27 ?  379 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 379 ? 119.208 144.275 149.437 1.00 10.56 ?  379 SER B OG    1 
ATOM   8632  N  N     . ASN B 1 380 ? 121.594 144.130 147.515 1.00 11.08 ?  380 ASN B N     1 
ATOM   8633  C  CA    . ASN B 1 380 ? 122.973 143.794 147.214 1.00 7.33  ?  380 ASN B CA    1 
ATOM   8634  C  C     . ASN B 1 380 ? 123.171 142.281 147.276 1.00 13.50 ?  380 ASN B C     1 
ATOM   8635  O  O     . ASN B 1 380 ? 122.216 141.507 147.384 1.00 16.85 ?  380 ASN B O     1 
ATOM   8636  C  CB    . ASN B 1 380 ? 123.914 144.534 148.166 1.00 8.68  ?  380 ASN B CB    1 
ATOM   8637  C  CG    . ASN B 1 380 ? 123.801 144.047 149.593 1.00 6.85  ?  380 ASN B CG    1 
ATOM   8638  O  OD1   . ASN B 1 380 ? 122.703 143.883 150.121 1.00 19.12 ?  380 ASN B OD1   1 
ATOM   8639  N  ND2   . ASN B 1 380 ? 124.942 143.815 150.228 1.00 13.32 ?  380 ASN B ND2   1 
ATOM   8640  N  N     . LEU B 1 381 ? 124.431 141.850 147.196 1.00 18.23 ?  381 LEU B N     1 
ATOM   8641  C  CA    . LEU B 1 381 ? 124.750 140.429 147.223 1.00 11.49 ?  381 LEU B CA    1 
ATOM   8642  C  C     . LEU B 1 381 ? 124.421 139.788 148.566 1.00 7.62  ?  381 LEU B C     1 
ATOM   8643  O  O     . LEU B 1 381 ? 124.161 138.582 148.616 1.00 18.28 ?  381 LEU B O     1 
ATOM   8644  C  CB    . LEU B 1 381 ? 126.229 140.231 146.881 1.00 17.87 ?  381 LEU B CB    1 
ATOM   8645  C  CG    . LEU B 1 381 ? 126.842 138.831 146.948 1.00 19.37 ?  381 LEU B CG    1 
ATOM   8646  C  CD1   . LEU B 1 381 ? 126.289 137.939 145.851 1.00 15.88 ?  381 LEU B CD1   1 
ATOM   8647  C  CD2   . LEU B 1 381 ? 128.354 138.917 146.861 1.00 17.74 ?  381 LEU B CD2   1 
ATOM   8648  N  N     . CYS B 1 382 ? 124.414 140.563 149.647 1.00 11.63 ?  382 CYS B N     1 
ATOM   8649  C  CA    . CYS B 1 382 ? 124.036 140.063 150.960 1.00 5.10  ?  382 CYS B CA    1 
ATOM   8650  C  C     . CYS B 1 382 ? 122.625 140.470 151.359 1.00 8.11  ?  382 CYS B C     1 
ATOM   8651  O  O     . CYS B 1 382 ? 122.205 140.177 152.483 1.00 17.87 ?  382 CYS B O     1 
ATOM   8652  C  CB    . CYS B 1 382 ? 125.037 140.540 152.015 1.00 16.37 ?  382 CYS B CB    1 
ATOM   8653  S  SG    . CYS B 1 382 ? 126.769 140.245 151.588 1.00 31.70 ?  382 CYS B SG    1 
ATOM   8654  N  N     . SER B 1 383 ? 121.889 141.135 150.466 1.00 10.35 ?  383 SER B N     1 
ATOM   8655  C  CA    . SER B 1 383 ? 120.479 141.479 150.668 1.00 9.66  ?  383 SER B CA    1 
ATOM   8656  C  C     . SER B 1 383 ? 120.261 142.278 151.950 1.00 12.91 ?  383 SER B C     1 
ATOM   8657  O  O     . SER B 1 383 ? 119.329 142.025 152.715 1.00 23.55 ?  383 SER B O     1 
ATOM   8658  C  CB    . SER B 1 383 ? 119.597 140.229 150.654 1.00 13.23 ?  383 SER B CB    1 
ATOM   8659  O  OG    . SER B 1 383 ? 119.945 139.342 151.698 1.00 18.79 ?  383 SER B OG    1 
ATOM   8660  N  N     . GLU B 1 384 ? 121.136 143.253 152.196 1.00 7.46  ?  384 GLU B N     1 
ATOM   8661  C  CA    . GLU B 1 384 ? 120.943 144.183 153.299 1.00 8.37  ?  384 GLU B CA    1 
ATOM   8662  C  C     . GLU B 1 384 ? 121.055 145.642 152.886 1.00 13.49 ?  384 GLU B C     1 
ATOM   8663  O  O     . GLU B 1 384 ? 120.653 146.516 153.663 1.00 23.85 ?  384 GLU B O     1 
ATOM   8664  C  CB    . GLU B 1 384 ? 121.938 143.895 154.436 1.00 6.60  ?  384 GLU B CB    1 
ATOM   8665  C  CG    . GLU B 1 384 ? 123.123 144.842 154.541 1.00 10.32 ?  384 GLU B CG    1 
ATOM   8666  C  CD    . GLU B 1 384 ? 124.231 144.506 153.571 1.00 19.47 ?  384 GLU B CD    1 
ATOM   8667  O  OE1   . GLU B 1 384 ? 124.208 143.395 153.008 1.00 13.01 ?  384 GLU B OE1   1 
ATOM   8668  O  OE2   . GLU B 1 384 ? 125.135 145.346 153.387 1.00 26.60 -1 384 GLU B OE2   1 
ATOM   8669  N  N     . VAL B 1 385 ? 121.563 145.935 151.695 1.00 10.47 ?  385 VAL B N     1 
ATOM   8670  C  CA    . VAL B 1 385 ? 121.643 147.301 151.196 1.00 6.73  ?  385 VAL B CA    1 
ATOM   8671  C  C     . VAL B 1 385 ? 120.370 147.601 150.419 1.00 15.55 ?  385 VAL B C     1 
ATOM   8672  O  O     . VAL B 1 385 ? 120.059 146.922 149.434 1.00 24.31 ?  385 VAL B O     1 
ATOM   8673  C  CB    . VAL B 1 385 ? 122.884 147.499 150.317 1.00 6.60  ?  385 VAL B CB    1 
ATOM   8674  C  CG1   . VAL B 1 385 ? 122.852 148.864 149.677 1.00 6.70  ?  385 VAL B CG1   1 
ATOM   8675  C  CG2   . VAL B 1 385 ? 124.137 147.333 151.141 1.00 11.92 ?  385 VAL B CG2   1 
ATOM   8676  N  N     . LEU B 1 386 ? 119.631 148.617 150.861 1.00 12.50 ?  386 LEU B N     1 
ATOM   8677  C  CA    . LEU B 1 386 ? 118.351 148.995 150.261 1.00 2.08  ?  386 LEU B CA    1 
ATOM   8678  C  C     . LEU B 1 386 ? 118.343 150.510 150.095 1.00 5.19  ?  386 LEU B C     1 
ATOM   8679  O  O     . LEU B 1 386 ? 117.966 151.244 151.012 1.00 11.17 ?  386 LEU B O     1 
ATOM   8680  C  CB    . LEU B 1 386 ? 117.190 148.507 151.111 1.00 5.06  ?  386 LEU B CB    1 
ATOM   8681  C  CG    . LEU B 1 386 ? 117.082 146.984 151.188 1.00 5.85  ?  386 LEU B CG    1 
ATOM   8682  C  CD1   . LEU B 1 386 ? 116.143 146.584 152.293 1.00 10.23 ?  386 LEU B CD1   1 
ATOM   8683  C  CD2   . LEU B 1 386 ? 116.622 146.411 149.858 1.00 8.67  ?  386 LEU B CD2   1 
ATOM   8684  N  N     . GLN B 1 387 ? 118.759 150.972 148.920 1.00 11.72 ?  387 GLN B N     1 
ATOM   8685  C  CA    . GLN B 1 387 ? 118.935 152.393 148.664 1.00 9.78  ?  387 GLN B CA    1 
ATOM   8686  C  C     . GLN B 1 387 ? 118.325 152.755 147.318 1.00 11.25 ?  387 GLN B C     1 
ATOM   8687  O  O     . GLN B 1 387 ? 118.105 151.900 146.458 1.00 19.86 ?  387 GLN B O     1 
ATOM   8688  C  CB    . GLN B 1 387 ? 120.416 152.786 148.691 1.00 4.43  ?  387 GLN B CB    1 
ATOM   8689  C  CG    . GLN B 1 387 ? 121.137 152.382 149.960 1.00 6.44  ?  387 GLN B CG    1 
ATOM   8690  C  CD    . GLN B 1 387 ? 122.572 152.840 149.974 1.00 10.27 ?  387 GLN B CD    1 
ATOM   8691  O  OE1   . GLN B 1 387 ? 122.967 153.693 149.181 1.00 21.83 ?  387 GLN B OE1   1 
ATOM   8692  N  NE2   . GLN B 1 387 ? 123.366 152.279 150.874 1.00 10.90 ?  387 GLN B NE2   1 
ATOM   8693  N  N     . ALA B 1 388 ? 118.039 154.044 147.156 1.00 13.59 ?  388 ALA B N     1 
ATOM   8694  C  CA    . ALA B 1 388 ? 117.538 154.550 145.887 1.00 10.79 ?  388 ALA B CA    1 
ATOM   8695  C  C     . ALA B 1 388 ? 118.617 154.463 144.816 1.00 17.73 ?  388 ALA B C     1 
ATOM   8696  O  O     . ALA B 1 388 ? 119.785 154.773 145.060 1.00 23.67 ?  388 ALA B O     1 
ATOM   8697  C  CB    . ALA B 1 388 ? 117.068 155.995 146.040 1.00 9.43  ?  388 ALA B CB    1 
ATOM   8698  N  N     . SER B 1 389 ? 118.219 154.035 143.622 1.00 21.15 ?  389 SER B N     1 
ATOM   8699  C  CA    . SER B 1 389 ? 119.127 153.952 142.490 1.00 8.55  ?  389 SER B CA    1 
ATOM   8700  C  C     . SER B 1 389 ? 118.428 154.466 141.245 1.00 16.13 ?  389 SER B C     1 
ATOM   8701  O  O     . SER B 1 389 ? 117.247 154.187 141.024 1.00 23.96 ?  389 SER B O     1 
ATOM   8702  C  CB    . SER B 1 389 ? 119.614 152.517 142.259 1.00 14.47 ?  389 SER B CB    1 
ATOM   8703  O  OG    . SER B 1 389 ? 118.526 151.613 142.182 1.00 24.83 ?  389 SER B OG    1 
ATOM   8704  N  N     . GLN B 1 390 ? 119.164 155.220 140.435 1.00 17.90 ?  390 GLN B N     1 
ATOM   8705  C  CA    . GLN B 1 390 ? 118.687 155.701 139.148 1.00 11.04 ?  390 GLN B CA    1 
ATOM   8706  C  C     . GLN B 1 390 ? 119.497 155.030 138.051 1.00 12.59 ?  390 GLN B C     1 
ATOM   8707  O  O     . GLN B 1 390 ? 120.731 155.025 138.099 1.00 26.82 ?  390 GLN B O     1 
ATOM   8708  C  CB    . GLN B 1 390 ? 118.802 157.224 139.054 1.00 16.03 ?  390 GLN B CB    1 
ATOM   8709  C  CG    . GLN B 1 390 ? 117.852 157.967 139.981 1.00 18.30 ?  390 GLN B CG    1 
ATOM   8710  C  CD    . GLN B 1 390 ? 118.124 159.456 140.031 1.00 22.91 ?  390 GLN B CD    1 
ATOM   8711  O  OE1   . GLN B 1 390 ? 119.113 159.938 139.480 1.00 25.83 ?  390 GLN B OE1   1 
ATOM   8712  N  NE2   . GLN B 1 390 ? 117.242 160.195 140.694 1.00 18.30 ?  390 GLN B NE2   1 
ATOM   8713  N  N     . VAL B 1 391 ? 118.802 154.452 137.071 1.00 22.98 ?  391 VAL B N     1 
ATOM   8714  C  CA    . VAL B 1 391 ? 119.484 153.727 136.007 1.00 20.87 ?  391 VAL B CA    1 
ATOM   8715  C  C     . VAL B 1 391 ? 120.263 154.705 135.134 1.00 23.00 ?  391 VAL B C     1 
ATOM   8716  O  O     . VAL B 1 391 ? 119.889 155.876 134.976 1.00 21.34 ?  391 VAL B O     1 
ATOM   8717  C  CB    . VAL B 1 391 ? 118.481 152.902 135.179 1.00 15.39 ?  391 VAL B CB    1 
ATOM   8718  C  CG1   . VAL B 1 391 ? 117.719 153.785 134.203 1.00 20.83 ?  391 VAL B CG1   1 
ATOM   8719  C  CG2   . VAL B 1 391 ? 119.190 151.772 134.450 1.00 17.46 ?  391 VAL B CG2   1 
ATOM   8720  N  N     . SER B 1 392 ? 121.371 154.227 134.581 1.00 28.78 ?  392 SER B N     1 
ATOM   8721  C  CA    . SER B 1 392 ? 122.215 155.025 133.706 1.00 21.82 ?  392 SER B CA    1 
ATOM   8722  C  C     . SER B 1 392 ? 121.902 154.713 132.248 1.00 28.18 ?  392 SER B C     1 
ATOM   8723  O  O     . SER B 1 392 ? 121.558 153.583 131.896 1.00 31.29 ?  392 SER B O     1 
ATOM   8724  C  CB    . SER B 1 392 ? 123.697 154.766 133.985 1.00 20.84 ?  392 SER B CB    1 
ATOM   8725  O  OG    . SER B 1 392 ? 124.024 155.065 135.329 1.00 30.03 ?  392 SER B OG    1 
ATOM   8726  N  N     . SER B 1 393 ? 122.024 155.731 131.406 1.00 25.65 ?  393 SER B N     1 
ATOM   8727  C  CA    . SER B 1 393 ? 121.823 155.595 129.966 1.00 23.85 ?  393 SER B CA    1 
ATOM   8728  C  C     . SER B 1 393 ? 123.202 155.619 129.313 1.00 25.99 ?  393 SER B C     1 
ATOM   8729  O  O     . SER B 1 393 ? 123.712 156.676 128.940 1.00 31.14 ?  393 SER B O     1 
ATOM   8730  C  CB    . SER B 1 393 ? 120.924 156.702 129.425 1.00 28.94 ?  393 SER B CB    1 
ATOM   8731  O  OG    . SER B 1 393 ? 119.747 156.829 130.203 1.00 31.30 ?  393 SER B OG    1 
ATOM   8732  N  N     . TYR B 1 394 ? 123.806 154.441 129.186 1.00 28.75 ?  394 TYR B N     1 
ATOM   8733  C  CA    . TYR B 1 394 ? 125.084 154.305 128.497 1.00 26.75 ?  394 TYR B CA    1 
ATOM   8734  C  C     . TYR B 1 394 ? 124.811 154.257 127.000 1.00 26.39 ?  394 TYR B C     1 
ATOM   8735  O  O     . TYR B 1 394 ? 124.245 153.282 126.495 1.00 29.18 ?  394 TYR B O     1 
ATOM   8736  C  CB    . TYR B 1 394 ? 125.820 153.058 128.972 1.00 24.95 ?  394 TYR B CB    1 
ATOM   8737  C  CG    . TYR B 1 394 ? 126.173 153.085 130.442 1.00 23.85 ?  394 TYR B CG    1 
ATOM   8738  C  CD1   . TYR B 1 394 ? 127.101 153.991 130.936 1.00 23.65 ?  394 TYR B CD1   1 
ATOM   8739  C  CD2   . TYR B 1 394 ? 125.572 152.209 131.336 1.00 25.91 ?  394 TYR B CD2   1 
ATOM   8740  C  CE1   . TYR B 1 394 ? 127.425 154.020 132.279 1.00 28.58 ?  394 TYR B CE1   1 
ATOM   8741  C  CE2   . TYR B 1 394 ? 125.889 152.230 132.679 1.00 26.75 ?  394 TYR B CE2   1 
ATOM   8742  C  CZ    . TYR B 1 394 ? 126.816 153.138 133.145 1.00 30.68 ?  394 TYR B CZ    1 
ATOM   8743  O  OH    . TYR B 1 394 ? 127.135 153.163 134.483 1.00 34.71 ?  394 TYR B OH    1 
ATOM   8744  N  N     . THR B 1 395 ? 125.202 155.308 126.293 1.00 31.26 ?  395 THR B N     1 
ATOM   8745  C  CA    . THR B 1 395 ? 124.882 155.470 124.887 1.00 30.91 ?  395 THR B CA    1 
ATOM   8746  C  C     . THR B 1 395 ? 126.001 154.897 124.023 1.00 32.44 ?  395 THR B C     1 
ATOM   8747  O  O     . THR B 1 395 ? 126.928 154.242 124.513 1.00 32.19 ?  395 THR B O     1 
ATOM   8748  C  CB    . THR B 1 395 ? 124.626 156.946 124.584 1.00 30.55 ?  395 THR B CB    1 
ATOM   8749  O  OG1   . THR B 1 395 ? 125.773 157.718 124.959 1.00 32.79 ?  395 THR B OG1   1 
ATOM   8750  C  CG2   . THR B 1 395 ? 123.416 157.444 125.359 1.00 30.29 ?  395 THR B CG2   1 
ATOM   8751  N  N     . ASP B 1 396 ? 125.916 155.138 122.719 1.00 33.29 ?  396 ASP B N     1 
ATOM   8752  C  CA    . ASP B 1 396 ? 126.929 154.658 121.793 1.00 31.68 ?  396 ASP B CA    1 
ATOM   8753  C  C     . ASP B 1 396 ? 128.251 155.383 122.022 1.00 34.49 ?  396 ASP B C     1 
ATOM   8754  O  O     . ASP B 1 396 ? 128.323 156.406 122.708 1.00 40.59 ?  396 ASP B O     1 
ATOM   8755  C  CB    . ASP B 1 396 ? 126.475 154.855 120.347 1.00 33.18 ?  396 ASP B CB    1 
ATOM   8756  C  CG    . ASP B 1 396 ? 125.253 154.032 119.999 1.00 36.09 ?  396 ASP B CG    1 
ATOM   8757  O  OD1   . ASP B 1 396 ? 125.001 153.017 120.680 1.00 39.61 ?  396 ASP B OD1   1 
ATOM   8758  O  OD2   . ASP B 1 396 ? 124.545 154.399 119.038 1.00 36.46 -1 396 ASP B OD2   1 
ATOM   8759  N  N     . TYR B 1 397 ? 129.311 154.829 121.440 1.00 32.92 ?  397 TYR B N     1 
ATOM   8760  C  CA    . TYR B 1 397 ? 130.604 155.494 121.474 1.00 32.88 ?  397 TYR B CA    1 
ATOM   8761  C  C     . TYR B 1 397 ? 130.520 156.829 120.745 1.00 38.23 ?  397 TYR B C     1 
ATOM   8762  O  O     . TYR B 1 397 ? 129.758 156.991 119.786 1.00 43.77 ?  397 TYR B O     1 
ATOM   8763  C  CB    . TYR B 1 397 ? 131.680 154.609 120.845 1.00 31.40 ?  397 TYR B CB    1 
ATOM   8764  C  CG    . TYR B 1 397 ? 133.078 154.915 121.325 1.00 31.29 ?  397 TYR B CG    1 
ATOM   8765  C  CD1   . TYR B 1 397 ? 133.831 155.920 120.732 1.00 34.49 ?  397 TYR B CD1   1 
ATOM   8766  C  CD2   . TYR B 1 397 ? 133.645 154.203 122.372 1.00 32.36 ?  397 TYR B CD2   1 
ATOM   8767  C  CE1   . TYR B 1 397 ? 135.109 156.204 121.168 1.00 33.49 ?  397 TYR B CE1   1 
ATOM   8768  C  CE2   . TYR B 1 397 ? 134.924 154.479 122.813 1.00 29.46 ?  397 TYR B CE2   1 
ATOM   8769  C  CZ    . TYR B 1 397 ? 135.650 155.481 122.208 1.00 31.74 ?  397 TYR B CZ    1 
ATOM   8770  O  OH    . TYR B 1 397 ? 136.923 155.762 122.644 1.00 35.13 ?  397 TYR B OH    1 
ATOM   8771  N  N     . ASP B 1 398 ? 131.297 157.799 121.228 1.00 35.77 ?  398 ASP B N     1 
ATOM   8772  C  CA    . ASP B 1 398 ? 131.297 159.189 120.777 1.00 40.56 ?  398 ASP B CA    1 
ATOM   8773  C  C     . ASP B 1 398 ? 130.011 159.917 121.138 1.00 41.34 ?  398 ASP B C     1 
ATOM   8774  O  O     . ASP B 1 398 ? 129.773 161.026 120.641 1.00 39.21 ?  398 ASP B O     1 
ATOM   8775  C  CB    . ASP B 1 398 ? 131.549 159.310 119.268 1.00 39.07 ?  398 ASP B CB    1 
ATOM   8776  C  CG    . ASP B 1 398 ? 132.956 159.769 118.947 1.00 44.22 ?  398 ASP B CG    1 
ATOM   8777  O  OD1   . ASP B 1 398 ? 133.192 160.211 117.802 1.00 42.46 ?  398 ASP B OD1   1 
ATOM   8778  O  OD2   . ASP B 1 398 ? 133.829 159.687 119.837 1.00 45.23 -1 398 ASP B OD2   1 
ATOM   8779  N  N     . GLU B 1 399 ? 129.174 159.330 121.988 1.00 44.70 ?  399 GLU B N     1 
ATOM   8780  C  CA    . GLU B 1 399 ? 127.968 159.968 122.492 1.00 41.11 ?  399 GLU B CA    1 
ATOM   8781  C  C     . GLU B 1 399 ? 128.053 160.059 124.008 1.00 44.21 ?  399 GLU B C     1 
ATOM   8782  O  O     . GLU B 1 399 ? 128.547 159.139 124.668 1.00 39.66 ?  399 GLU B O     1 
ATOM   8783  C  CB    . GLU B 1 399 ? 126.711 159.192 122.081 1.00 37.86 ?  399 GLU B CB    1 
ATOM   8784  C  CG    . GLU B 1 399 ? 126.474 159.142 120.582 1.00 43.97 ?  399 GLU B CG    1 
ATOM   8785  C  CD    . GLU B 1 399 ? 126.066 160.486 120.011 1.00 47.43 ?  399 GLU B CD    1 
ATOM   8786  O  OE1   . GLU B 1 399 ? 125.253 161.184 120.651 1.00 47.85 ?  399 GLU B OE1   1 
ATOM   8787  O  OE2   . GLU B 1 399 ? 126.560 160.844 118.920 1.00 46.53 -1 399 GLU B OE2   1 
ATOM   8788  N  N     . GLU B 1 400 ? 127.578 161.174 124.557 1.00 45.70 ?  400 GLU B N     1 
ATOM   8789  C  CA    . GLU B 1 400 ? 127.617 161.369 125.999 1.00 39.54 ?  400 GLU B CA    1 
ATOM   8790  C  C     . GLU B 1 400 ? 126.648 160.417 126.688 1.00 40.22 ?  400 GLU B C     1 
ATOM   8791  O  O     . GLU B 1 400 ? 125.508 160.243 126.246 1.00 39.36 ?  400 GLU B O     1 
ATOM   8792  C  CB    . GLU B 1 400 ? 127.277 162.816 126.349 1.00 40.02 ?  400 GLU B CB    1 
ATOM   8793  C  CG    . GLU B 1 400 ? 128.457 163.768 126.253 1.00 44.35 ?  400 GLU B CG    1 
ATOM   8794  C  CD    . GLU B 1 400 ? 129.667 163.274 127.019 1.00 47.31 ?  400 GLU B CD    1 
ATOM   8795  O  OE1   . GLU B 1 400 ? 129.563 163.102 128.251 1.00 46.59 ?  400 GLU B OE1   1 
ATOM   8796  O  OE2   . GLU B 1 400 ? 130.723 163.057 126.389 1.00 45.60 -1 400 GLU B OE2   1 
ATOM   8797  N  N     . ASP B 1 401 ? 127.105 159.799 127.774 1.00 35.64 ?  401 ASP B N     1 
ATOM   8798  C  CA    . ASP B 1 401 ? 126.276 158.893 128.554 1.00 31.88 ?  401 ASP B CA    1 
ATOM   8799  C  C     . ASP B 1 401 ? 125.566 159.653 129.664 1.00 32.92 ?  401 ASP B C     1 
ATOM   8800  O  O     . ASP B 1 401 ? 126.136 160.560 130.276 1.00 38.51 ?  401 ASP B O     1 
ATOM   8801  C  CB    . ASP B 1 401 ? 127.121 157.768 129.155 1.00 31.73 ?  401 ASP B CB    1 
ATOM   8802  C  CG    . ASP B 1 401 ? 127.890 156.990 128.107 1.00 36.42 ?  401 ASP B CG    1 
ATOM   8803  O  OD1   . ASP B 1 401 ? 127.500 157.037 126.921 1.00 38.79 ?  401 ASP B OD1   1 
ATOM   8804  O  OD2   . ASP B 1 401 ? 128.885 156.331 128.470 1.00 38.06 -1 401 ASP B OD2   1 
ATOM   8805  N  N     . GLU B 1 402 ? 124.315 159.279 129.918 1.00 29.52 ?  402 GLU B N     1 
ATOM   8806  C  CA    . GLU B 1 402 ? 123.551 159.828 131.037 1.00 27.64 ?  402 GLU B CA    1 
ATOM   8807  C  C     . GLU B 1 402 ? 123.843 158.962 132.256 1.00 29.15 ?  402 GLU B C     1 
ATOM   8808  O  O     . GLU B 1 402 ? 123.335 157.846 132.377 1.00 30.97 ?  402 GLU B O     1 
ATOM   8809  C  CB    . GLU B 1 402 ? 122.063 159.868 130.715 1.00 29.73 ?  402 GLU B CB    1 
ATOM   8810  C  CG    . GLU B 1 402 ? 121.680 160.908 129.675 1.00 33.82 ?  402 GLU B CG    1 
ATOM   8811  C  CD    . GLU B 1 402 ? 122.372 162.239 129.895 1.00 39.10 ?  402 GLU B CD    1 
ATOM   8812  O  OE1   . GLU B 1 402 ? 122.027 162.935 130.873 1.00 35.36 ?  402 GLU B OE1   1 
ATOM   8813  O  OE2   . GLU B 1 402 ? 123.261 162.589 129.092 1.00 36.60 -1 402 GLU B OE2   1 
ATOM   8814  N  N     . ILE B 1 403 ? 124.666 159.479 133.160 1.00 29.66 ?  403 ILE B N     1 
ATOM   8815  C  CA    . ILE B 1 403 ? 125.132 158.723 134.316 1.00 24.05 ?  403 ILE B CA    1 
ATOM   8816  C  C     . ILE B 1 403 ? 124.092 158.827 135.423 1.00 25.63 ?  403 ILE B C     1 
ATOM   8817  O  O     . ILE B 1 403 ? 123.731 159.929 135.850 1.00 30.61 ?  403 ILE B O     1 
ATOM   8818  C  CB    . ILE B 1 403 ? 126.500 159.230 134.794 1.00 21.38 ?  403 ILE B CB    1 
ATOM   8819  C  CG1   . ILE B 1 403 ? 127.567 158.960 133.731 1.00 23.71 ?  403 ILE B CG1   1 
ATOM   8820  C  CG2   . ILE B 1 403 ? 126.880 158.580 136.110 1.00 20.95 ?  403 ILE B CG2   1 
ATOM   8821  C  CD1   . ILE B 1 403 ? 127.599 157.530 133.247 1.00 27.98 ?  403 ILE B CD1   1 
ATOM   8822  N  N     . GLY B 1 404 ? 123.614 157.681 135.889 1.00 22.24 ?  404 GLY B N     1 
ATOM   8823  C  CA    . GLY B 1 404 ? 122.649 157.613 136.967 1.00 10.85 ?  404 GLY B CA    1 
ATOM   8824  C  C     . GLY B 1 404 ? 123.306 157.412 138.314 1.00 19.17 ?  404 GLY B C     1 
ATOM   8825  O  O     . GLY B 1 404 ? 124.432 157.856 138.558 1.00 26.62 ?  404 GLY B O     1 
ATOM   8826  N  N     . LEU B 1 405 ? 122.593 156.729 139.203 1.00 23.93 ?  405 LEU B N     1 
ATOM   8827  C  CA    . LEU B 1 405 ? 123.068 156.454 140.552 1.00 10.66 ?  405 LEU B CA    1 
ATOM   8828  C  C     . LEU B 1 405 ? 123.108 154.947 140.763 1.00 13.07 ?  405 LEU B C     1 
ATOM   8829  O  O     . LEU B 1 405 ? 122.067 154.284 140.712 1.00 14.56 ?  405 LEU B O     1 
ATOM   8830  C  CB    . LEU B 1 405 ? 122.171 157.119 141.597 1.00 17.18 ?  405 LEU B CB    1 
ATOM   8831  C  CG    . LEU B 1 405 ? 122.047 158.642 141.523 1.00 17.59 ?  405 LEU B CG    1 
ATOM   8832  C  CD1   . LEU B 1 405 ? 120.868 159.118 142.351 1.00 20.83 ?  405 LEU B CD1   1 
ATOM   8833  C  CD2   . LEU B 1 405 ? 123.329 159.315 141.980 1.00 16.71 ?  405 LEU B CD2   1 
ATOM   8834  N  N     . ASP B 1 406 ? 124.301 154.413 141.003 1.00 24.08 ?  406 ASP B N     1 
ATOM   8835  C  CA    . ASP B 1 406 ? 124.487 153.004 141.320 1.00 17.26 ?  406 ASP B CA    1 
ATOM   8836  C  C     . ASP B 1 406 ? 124.908 152.877 142.776 1.00 18.11 ?  406 ASP B C     1 
ATOM   8837  O  O     . ASP B 1 406 ? 125.900 153.480 143.196 1.00 27.75 ?  406 ASP B O     1 
ATOM   8838  C  CB    . ASP B 1 406 ? 125.530 152.361 140.405 1.00 17.89 ?  406 ASP B CB    1 
ATOM   8839  C  CG    . ASP B 1 406 ? 124.936 151.865 139.102 1.00 29.59 ?  406 ASP B CG    1 
ATOM   8840  O  OD1   . ASP B 1 406 ? 123.694 151.780 139.004 1.00 31.46 ?  406 ASP B OD1   1 
ATOM   8841  O  OD2   . ASP B 1 406 ? 125.713 151.556 138.175 1.00 31.03 -1 406 ASP B OD2   1 
ATOM   8842  N  N     . ILE B 1 407 ? 124.163 152.074 143.534 1.00 18.55 ?  407 ILE B N     1 
ATOM   8843  C  CA    . ILE B 1 407 ? 124.314 152.050 144.982 1.00 14.68 ?  407 ILE B CA    1 
ATOM   8844  C  C     . ILE B 1 407 ? 125.682 151.504 145.375 1.00 15.53 ?  407 ILE B C     1 
ATOM   8845  O  O     . ILE B 1 407 ? 126.220 150.578 144.751 1.00 21.25 ?  407 ILE B O     1 
ATOM   8846  C  CB    . ILE B 1 407 ? 123.183 151.221 145.618 1.00 15.58 ?  407 ILE B CB    1 
ATOM   8847  C  CG1   . ILE B 1 407 ? 121.817 151.756 145.189 1.00 3.84  ?  407 ILE B CG1   1 
ATOM   8848  C  CG2   . ILE B 1 407 ? 123.301 151.223 147.118 1.00 13.32 ?  407 ILE B CG2   1 
ATOM   8849  C  CD1   . ILE B 1 407 ? 120.755 150.692 145.130 1.00 11.74 ?  407 ILE B CD1   1 
ATOM   8850  N  N     . SER B 1 408 ? 126.252 152.093 146.424 1.00 26.34 ?  408 SER B N     1 
ATOM   8851  C  CA    . SER B 1 408 ? 127.499 151.631 147.019 1.00 23.56 ?  408 SER B CA    1 
ATOM   8852  C  C     . SER B 1 408 ? 127.610 152.248 148.403 1.00 27.78 ?  408 SER B C     1 
ATOM   8853  O  O     . SER B 1 408 ? 127.503 153.469 148.543 1.00 38.28 ?  408 SER B O     1 
ATOM   8854  C  CB    . SER B 1 408 ? 128.704 152.021 146.156 1.00 29.16 ?  408 SER B CB    1 
ATOM   8855  O  OG    . SER B 1 408 ? 129.844 152.273 146.956 1.00 27.58 ?  408 SER B OG    1 
ATOM   8856  N  N     . CYS B 1 409 ? 127.808 151.412 149.419 1.00 23.83 ?  409 CYS B N     1 
ATOM   8857  C  CA    . CYS B 1 409 ? 127.950 151.892 150.785 1.00 30.39 ?  409 CYS B CA    1 
ATOM   8858  C  C     . CYS B 1 409 ? 129.098 151.164 151.471 1.00 28.90 ?  409 CYS B C     1 
ATOM   8859  O  O     . CYS B 1 409 ? 129.470 150.049 151.098 1.00 26.96 ?  409 CYS B O     1 
ATOM   8860  C  CB    . CYS B 1 409 ? 126.654 151.717 151.592 1.00 25.10 ?  409 CYS B CB    1 
ATOM   8861  S  SG    . CYS B 1 409 ? 126.318 150.034 152.146 1.00 45.46 ?  409 CYS B SG    1 
ATOM   8862  N  N     . ASN B 1 410 ? 129.654 151.822 152.483 1.00 22.93 ?  410 ASN B N     1 
ATOM   8863  C  CA    . ASN B 1 410 ? 130.764 151.290 153.260 1.00 20.91 ?  410 ASN B CA    1 
ATOM   8864  C  C     . ASN B 1 410 ? 130.222 150.638 154.522 1.00 25.91 ?  410 ASN B C     1 
ATOM   8865  O  O     . ASN B 1 410 ? 129.365 151.209 155.203 1.00 28.35 ?  410 ASN B O     1 
ATOM   8866  C  CB    . ASN B 1 410 ? 131.754 152.397 153.617 1.00 24.20 ?  410 ASN B CB    1 
ATOM   8867  C  CG    . ASN B 1 410 ? 131.756 153.513 152.602 1.00 32.33 ?  410 ASN B CG    1 
ATOM   8868  O  OD1   . ASN B 1 410 ? 131.311 154.623 152.887 1.00 34.43 ?  410 ASN B OD1   1 
ATOM   8869  N  ND2   . ASN B 1 410 ? 132.254 153.227 151.405 1.00 34.92 ?  410 ASN B ND2   1 
ATOM   8870  N  N     . LEU B 1 411 ? 130.721 149.449 154.830 1.00 19.65 ?  411 LEU B N     1 
ATOM   8871  C  CA    . LEU B 1 411 ? 130.215 148.656 155.938 1.00 10.94 ?  411 LEU B CA    1 
ATOM   8872  C  C     . LEU B 1 411 ? 131.075 148.848 157.180 1.00 11.69 ?  411 LEU B C     1 
ATOM   8873  O  O     . LEU B 1 411 ? 132.291 149.039 157.099 1.00 22.88 ?  411 LEU B O     1 
ATOM   8874  C  CB    . LEU B 1 411 ? 130.167 147.173 155.569 1.00 19.20 ?  411 LEU B CB    1 
ATOM   8875  C  CG    . LEU B 1 411 ? 128.946 146.626 154.827 1.00 17.67 ?  411 LEU B CG    1 
ATOM   8876  C  CD1   . LEU B 1 411 ? 128.828 147.208 153.431 1.00 18.06 ?  411 LEU B CD1   1 
ATOM   8877  C  CD2   . LEU B 1 411 ? 129.031 145.112 154.763 1.00 23.52 ?  411 LEU B CD2   1 
ATOM   8878  N  N     . GLY B 1 412 ? 130.421 148.805 158.334 1.00 17.26 ?  412 GLY B N     1 
ATOM   8879  C  CA    . GLY B 1 412 ? 131.086 148.841 159.619 1.00 11.56 ?  412 GLY B CA    1 
ATOM   8880  C  C     . GLY B 1 412 ? 130.135 148.359 160.691 1.00 10.58 ?  412 GLY B C     1 
ATOM   8881  O  O     . GLY B 1 412 ? 128.966 148.750 160.692 1.00 27.55 ?  412 GLY B O     1 
ATOM   8882  N  N     . SER B 1 413 ? 130.600 147.509 161.599 1.00 11.05 ?  413 SER B N     1 
ATOM   8883  C  CA    . SER B 1 413 ? 129.719 146.858 162.556 1.00 11.98 ?  413 SER B CA    1 
ATOM   8884  C  C     . SER B 1 413 ? 130.060 147.262 163.982 1.00 19.09 ?  413 SER B C     1 
ATOM   8885  O  O     . SER B 1 413 ? 131.230 147.286 164.370 1.00 20.96 ?  413 SER B O     1 
ATOM   8886  C  CB    . SER B 1 413 ? 129.801 145.337 162.422 1.00 13.26 ?  413 SER B CB    1 
ATOM   8887  O  OG    . SER B 1 413 ? 129.282 144.913 161.175 1.00 31.25 ?  413 SER B OG    1 
ATOM   8888  N  N     . LEU B 1 414 ? 129.031 147.567 164.761 1.00 20.36 ?  414 LEU B N     1 
ATOM   8889  C  CA    . LEU B 1 414 ? 129.185 147.751 166.193 1.00 13.08 ?  414 LEU B CA    1 
ATOM   8890  C  C     . LEU B 1 414 ? 129.161 146.395 166.879 1.00 21.50 ?  414 LEU B C     1 
ATOM   8891  O  O     . LEU B 1 414 ? 128.321 145.546 166.574 1.00 25.61 ?  414 LEU B O     1 
ATOM   8892  C  CB    . LEU B 1 414 ? 128.071 148.634 166.754 1.00 22.88 ?  414 LEU B CB    1 
ATOM   8893  C  CG    . LEU B 1 414 ? 127.779 149.950 166.040 1.00 21.75 ?  414 LEU B CG    1 
ATOM   8894  C  CD1   . LEU B 1 414 ? 126.560 150.604 166.654 1.00 22.36 ?  414 LEU B CD1   1 
ATOM   8895  C  CD2   . LEU B 1 414 ? 128.979 150.876 166.118 1.00 24.62 ?  414 LEU B CD2   1 
ATOM   8896  N  N     . ASN B 1 415 ? 130.094 146.191 167.803 1.00 29.80 ?  415 ASN B N     1 
ATOM   8897  C  CA    . ASN B 1 415 ? 130.070 145.006 168.651 1.00 27.12 ?  415 ASN B CA    1 
ATOM   8898  C  C     . ASN B 1 415 ? 129.165 145.307 169.837 1.00 25.14 ?  415 ASN B C     1 
ATOM   8899  O  O     . ASN B 1 415 ? 129.541 146.065 170.737 1.00 29.23 ?  415 ASN B O     1 
ATOM   8900  C  CB    . ASN B 1 415 ? 131.480 144.636 169.096 1.00 22.71 ?  415 ASN B CB    1 
ATOM   8901  C  CG    . ASN B 1 415 ? 131.568 143.236 169.665 1.00 28.99 ?  415 ASN B CG    1 
ATOM   8902  O  OD1   . ASN B 1 415 ? 130.716 142.810 170.442 1.00 34.87 ?  415 ASN B OD1   1 
ATOM   8903  N  ND2   . ASN B 1 415 ? 132.609 142.509 169.279 1.00 29.53 ?  415 ASN B ND2   1 
ATOM   8904  N  N     . ILE B 1 416 ? 127.969 144.714 169.837 1.00 20.40 ?  416 ILE B N     1 
ATOM   8905  C  CA    . ILE B 1 416 ? 126.944 145.085 170.809 1.00 23.03 ?  416 ILE B CA    1 
ATOM   8906  C  C     . ILE B 1 416 ? 127.418 144.803 172.229 1.00 30.00 ?  416 ILE B C     1 
ATOM   8907  O  O     . ILE B 1 416 ? 127.216 145.617 173.138 1.00 30.28 ?  416 ILE B O     1 
ATOM   8908  C  CB    . ILE B 1 416 ? 125.625 144.359 170.488 1.00 22.35 ?  416 ILE B CB    1 
ATOM   8909  C  CG1   . ILE B 1 416 ? 125.034 144.903 169.186 1.00 22.82 ?  416 ILE B CG1   1 
ATOM   8910  C  CG2   . ILE B 1 416 ? 124.633 144.519 171.623 1.00 17.29 ?  416 ILE B CG2   1 
ATOM   8911  C  CD1   . ILE B 1 416 ? 123.814 144.159 168.701 1.00 21.61 ?  416 ILE B CD1   1 
ATOM   8912  N  N     . LEU B 1 417 ? 128.065 143.655 172.441 1.00 24.98 ?  417 LEU B N     1 
ATOM   8913  C  CA    . LEU B 1 417 ? 128.547 143.315 173.776 1.00 27.55 ?  417 LEU B CA    1 
ATOM   8914  C  C     . LEU B 1 417 ? 129.577 144.323 174.266 1.00 28.75 ?  417 LEU B C     1 
ATOM   8915  O  O     . LEU B 1 417 ? 129.494 144.813 175.398 1.00 34.00 ?  417 LEU B O     1 
ATOM   8916  C  CB    . LEU B 1 417 ? 129.136 141.904 173.774 1.00 28.61 ?  417 LEU B CB    1 
ATOM   8917  C  CG    . LEU B 1 417 ? 129.609 141.383 175.132 1.00 29.91 ?  417 LEU B CG    1 
ATOM   8918  C  CD1   . LEU B 1 417 ? 128.844 140.132 175.511 1.00 27.31 ?  417 LEU B CD1   1 
ATOM   8919  C  CD2   . LEU B 1 417 ? 131.103 141.113 175.108 1.00 32.64 ?  417 LEU B CD2   1 
ATOM   8920  N  N     . ASN B 1 418 ? 130.553 144.657 173.419 1.00 34.08 ?  418 ASN B N     1 
ATOM   8921  C  CA    . ASN B 1 418 ? 131.593 145.593 173.829 1.00 29.41 ?  418 ASN B CA    1 
ATOM   8922  C  C     . ASN B 1 418 ? 131.065 147.019 173.920 1.00 29.20 ?  418 ASN B C     1 
ATOM   8923  O  O     . ASN B 1 418 ? 131.500 147.784 174.788 1.00 35.03 ?  418 ASN B O     1 
ATOM   8924  C  CB    . ASN B 1 418 ? 132.772 145.518 172.862 1.00 27.06 ?  418 ASN B CB    1 
ATOM   8925  C  CG    . ASN B 1 418 ? 133.512 144.201 172.955 1.00 28.65 ?  418 ASN B CG    1 
ATOM   8926  O  OD1   . ASN B 1 418 ? 133.703 143.661 174.043 1.00 36.71 ?  418 ASN B OD1   1 
ATOM   8927  N  ND2   . ASN B 1 418 ? 133.930 143.673 171.811 1.00 30.28 ?  418 ASN B ND2   1 
ATOM   8928  N  N     . VAL B 1 419 ? 130.140 147.396 173.036 1.00 31.16 ?  419 VAL B N     1 
ATOM   8929  C  CA    . VAL B 1 419 ? 129.566 148.737 173.085 1.00 31.46 ?  419 VAL B CA    1 
ATOM   8930  C  C     . VAL B 1 419 ? 128.764 148.931 174.366 1.00 29.36 ?  419 VAL B C     1 
ATOM   8931  O  O     . VAL B 1 419 ? 128.884 149.961 175.041 1.00 36.08 ?  419 VAL B O     1 
ATOM   8932  C  CB    . VAL B 1 419 ? 128.711 148.999 171.831 1.00 26.47 ?  419 VAL B CB    1 
ATOM   8933  C  CG1   . VAL B 1 419 ? 127.777 150.164 172.059 1.00 28.15 ?  419 VAL B CG1   1 
ATOM   8934  C  CG2   . VAL B 1 419 ? 129.601 149.271 170.636 1.00 25.84 ?  419 VAL B CG2   1 
ATOM   8935  N  N     . MET B 1 420 ? 127.941 147.945 174.729 1.00 31.99 ?  420 MET B N     1 
ATOM   8936  C  CA    . MET B 1 420 ? 127.123 148.082 175.927 1.00 34.66 ?  420 MET B CA    1 
ATOM   8937  C  C     . MET B 1 420 ? 127.927 147.879 177.205 1.00 33.26 ?  420 MET B C     1 
ATOM   8938  O  O     . MET B 1 420 ? 127.593 148.469 178.238 1.00 35.93 ?  420 MET B O     1 
ATOM   8939  C  CB    . MET B 1 420 ? 125.944 147.109 175.884 1.00 32.45 ?  420 MET B CB    1 
ATOM   8940  C  CG    . MET B 1 420 ? 124.977 147.378 174.746 1.00 30.51 ?  420 MET B CG    1 
ATOM   8941  S  SD    . MET B 1 420 ? 123.532 148.317 175.273 1.00 43.53 ?  420 MET B SD    1 
ATOM   8942  C  CE    . MET B 1 420 ? 123.147 147.530 176.832 1.00 31.04 ?  420 MET B CE    1 
ATOM   8943  N  N     . GLU B 1 421 ? 128.975 147.053 177.162 1.00 37.77 ?  421 GLU B N     1 
ATOM   8944  C  CA    . GLU B 1 421 ? 129.843 146.906 178.326 1.00 34.78 ?  421 GLU B CA    1 
ATOM   8945  C  C     . GLU B 1 421 ? 130.552 148.215 178.646 1.00 38.51 ?  421 GLU B C     1 
ATOM   8946  O  O     . GLU B 1 421 ? 130.697 148.584 179.816 1.00 41.72 ?  421 GLU B O     1 
ATOM   8947  C  CB    . GLU B 1 421 ? 130.852 145.784 178.086 1.00 34.46 ?  421 GLU B CB    1 
ATOM   8948  C  CG    . GLU B 1 421 ? 132.067 145.828 178.997 1.00 42.35 ?  421 GLU B CG    1 
ATOM   8949  C  CD    . GLU B 1 421 ? 133.360 145.561 178.253 1.00 44.83 ?  421 GLU B CD    1 
ATOM   8950  O  OE1   . GLU B 1 421 ? 133.302 145.318 177.028 1.00 43.17 ?  421 GLU B OE1   1 
ATOM   8951  O  OE2   . GLU B 1 421 ? 134.433 145.595 178.891 1.00 41.27 -1 421 GLU B OE2   1 
ATOM   8952  N  N     . HIS B 1 422 ? 130.989 148.936 177.616 1.00 34.24 ?  422 HIS B N     1 
ATOM   8953  C  CA    . HIS B 1 422 ? 131.630 150.231 177.795 1.00 35.44 ?  422 HIS B CA    1 
ATOM   8954  C  C     . HIS B 1 422 ? 130.631 151.368 177.962 1.00 38.64 ?  422 HIS B C     1 
ATOM   8955  O  O     . HIS B 1 422 ? 131.055 152.504 178.202 1.00 41.12 ?  422 HIS B O     1 
ATOM   8956  C  CB    . HIS B 1 422 ? 132.553 150.525 176.610 1.00 32.69 ?  422 HIS B CB    1 
ATOM   8957  C  CG    . HIS B 1 422 ? 133.753 149.633 176.543 1.00 35.81 ?  422 HIS B CG    1 
ATOM   8958  N  ND1   . HIS B 1 422 ? 133.744 148.423 175.884 1.00 36.57 ?  422 HIS B ND1   1 
ATOM   8959  C  CD2   . HIS B 1 422 ? 134.998 149.773 177.054 1.00 37.01 ?  422 HIS B CD2   1 
ATOM   8960  C  CE1   . HIS B 1 422 ? 134.932 147.856 175.992 1.00 39.80 ?  422 HIS B CE1   1 
ATOM   8961  N  NE2   . HIS B 1 422 ? 135.711 148.654 176.697 1.00 39.81 ?  422 HIS B NE2   1 
ATOM   8962  N  N     . LYS B 1 423 ? 129.331 151.089 177.846 1.00 40.97 ?  423 LYS B N     1 
ATOM   8963  C  CA    . LYS B 1 423 ? 128.283 152.103 177.987 1.00 42.37 ?  423 LYS B CA    1 
ATOM   8964  C  C     . LYS B 1 423 ? 128.531 153.281 177.049 1.00 43.69 ?  423 LYS B C     1 
ATOM   8965  O  O     . LYS B 1 423 ? 128.408 154.446 177.432 1.00 46.33 ?  423 LYS B O     1 
ATOM   8966  C  CB    . LYS B 1 423 ? 128.169 152.575 179.437 1.00 40.41 ?  423 LYS B CB    1 
ATOM   8967  C  CG    . LYS B 1 423 ? 127.458 151.598 180.356 1.00 42.43 ?  423 LYS B CG    1 
ATOM   8968  C  CD    . LYS B 1 423 ? 127.552 152.042 181.806 1.00 43.32 ?  423 LYS B CD    1 
ATOM   8969  C  CE    . LYS B 1 423 ? 128.569 151.210 182.573 1.00 45.85 ?  423 LYS B CE    1 
ATOM   8970  N  NZ    . LYS B 1 423 ? 127.944 150.465 183.701 1.00 43.92 1  423 LYS B NZ    1 
ATOM   8971  N  N     . SER B 1 424 ? 128.882 152.972 175.805 1.00 31.73 ?  424 SER B N     1 
ATOM   8972  C  CA    . SER B 1 424 ? 129.340 153.969 174.845 1.00 33.97 ?  424 SER B CA    1 
ATOM   8973  C  C     . SER B 1 424 ? 128.637 153.799 173.507 1.00 34.09 ?  424 SER B C     1 
ATOM   8974  O  O     . SER B 1 424 ? 129.268 153.769 172.450 1.00 32.55 ?  424 SER B O     1 
ATOM   8975  C  CB    . SER B 1 424 ? 130.851 153.881 174.664 1.00 35.65 ?  424 SER B CB    1 
ATOM   8976  O  OG    . SER B 1 424 ? 131.204 152.696 173.973 1.00 32.02 ?  424 SER B OG    1 
ATOM   8977  N  N     . ILE B 1 425 ? 127.309 153.678 173.533 1.00 33.46 ?  425 ILE B N     1 
ATOM   8978  C  CA    . ILE B 1 425 ? 126.554 153.618 172.283 1.00 26.93 ?  425 ILE B CA    1 
ATOM   8979  C  C     . ILE B 1 425 ? 126.762 154.897 171.483 1.00 32.03 ?  425 ILE B C     1 
ATOM   8980  O  O     . ILE B 1 425 ? 127.065 154.860 170.285 1.00 35.69 ?  425 ILE B O     1 
ATOM   8981  C  CB    . ILE B 1 425 ? 125.061 153.367 172.559 1.00 32.10 ?  425 ILE B CB    1 
ATOM   8982  C  CG1   . ILE B 1 425 ? 124.818 151.908 172.944 1.00 32.37 ?  425 ILE B CG1   1 
ATOM   8983  C  CG2   . ILE B 1 425 ? 124.224 153.726 171.342 1.00 27.48 ?  425 ILE B CG2   1 
ATOM   8984  C  CD1   . ILE B 1 425 ? 123.397 151.625 173.369 1.00 33.35 ?  425 ILE B CD1   1 
ATOM   8985  N  N     . GLU B 1 426 ? 126.629 156.049 172.145 1.00 27.69 ?  426 GLU B N     1 
ATOM   8986  C  CA    . GLU B 1 426 ? 126.721 157.326 171.445 1.00 23.51 ?  426 GLU B CA    1 
ATOM   8987  C  C     . GLU B 1 426 ? 128.103 157.530 170.836 1.00 26.23 ?  426 GLU B C     1 
ATOM   8988  O  O     . GLU B 1 426 ? 128.229 157.814 169.639 1.00 34.59 ?  426 GLU B O     1 
ATOM   8989  C  CB    . GLU B 1 426 ? 126.385 158.468 172.403 1.00 26.59 ?  426 GLU B CB    1 
ATOM   8990  C  CG    . GLU B 1 426 ? 126.820 159.835 171.908 1.00 29.01 ?  426 GLU B CG    1 
ATOM   8991  C  CD    . GLU B 1 426 ? 126.450 160.947 172.867 1.00 33.93 ?  426 GLU B CD    1 
ATOM   8992  O  OE1   . GLU B 1 426 ? 125.987 160.642 173.985 1.00 33.66 ?  426 GLU B OE1   1 
ATOM   8993  O  OE2   . GLU B 1 426 ? 126.623 162.129 172.502 1.00 36.80 -1 426 GLU B OE2   1 
ATOM   8994  N  N     . LYS B 1 427 ? 129.152 157.389 171.649 1.00 33.18 ?  427 LYS B N     1 
ATOM   8995  C  CA    . LYS B 1 427 ? 130.503 157.651 171.164 1.00 27.99 ?  427 LYS B CA    1 
ATOM   8996  C  C     . LYS B 1 427 ? 130.893 156.677 170.061 1.00 28.32 ?  427 LYS B C     1 
ATOM   8997  O  O     . LYS B 1 427 ? 131.462 157.080 169.039 1.00 32.78 ?  427 LYS B O     1 
ATOM   8998  C  CB    . LYS B 1 427 ? 131.497 157.586 172.322 1.00 28.87 ?  427 LYS B CB    1 
ATOM   8999  C  CG    . LYS B 1 427 ? 132.954 157.567 171.892 1.00 32.24 ?  427 LYS B CG    1 
ATOM   9000  C  CD    . LYS B 1 427 ? 133.879 157.316 173.071 1.00 33.02 ?  427 LYS B CD    1 
ATOM   9001  C  CE    . LYS B 1 427 ? 133.647 155.944 173.682 1.00 31.84 ?  427 LYS B CE    1 
ATOM   9002  N  NZ    . LYS B 1 427 ? 133.470 154.890 172.647 1.00 33.99 1  427 LYS B NZ    1 
ATOM   9003  N  N     . THR B 1 428 ? 130.586 155.392 170.245 1.00 30.09 ?  428 THR B N     1 
ATOM   9004  C  CA    . THR B 1 428 ? 130.922 154.402 169.230 1.00 24.75 ?  428 THR B CA    1 
ATOM   9005  C  C     . THR B 1 428 ? 130.171 154.665 167.934 1.00 24.98 ?  428 THR B C     1 
ATOM   9006  O  O     . THR B 1 428 ? 130.754 154.579 166.848 1.00 32.34 ?  428 THR B O     1 
ATOM   9007  C  CB    . THR B 1 428 ? 130.622 152.992 169.738 1.00 24.64 ?  428 THR B CB    1 
ATOM   9008  O  OG1   . THR B 1 428 ? 131.176 152.828 171.049 1.00 26.31 ?  428 THR B OG1   1 
ATOM   9009  C  CG2   . THR B 1 428 ? 131.227 151.959 168.806 1.00 25.22 ?  428 THR B CG2   1 
ATOM   9010  N  N     . VAL B 1 429 ? 128.880 154.992 168.024 1.00 23.05 ?  429 VAL B N     1 
ATOM   9011  C  CA    . VAL B 1 429 ? 128.098 155.248 166.819 1.00 22.40 ?  429 VAL B CA    1 
ATOM   9012  C  C     . VAL B 1 429 ? 128.641 156.462 166.077 1.00 27.00 ?  429 VAL B C     1 
ATOM   9013  O  O     . VAL B 1 429 ? 128.802 156.433 164.851 1.00 28.05 ?  429 VAL B O     1 
ATOM   9014  C  CB    . VAL B 1 429 ? 126.607 155.414 167.166 1.00 25.19 ?  429 VAL B CB    1 
ATOM   9015  C  CG1   . VAL B 1 429 ? 125.872 156.079 166.021 1.00 22.74 ?  429 VAL B CG1   1 
ATOM   9016  C  CG2   . VAL B 1 429 ? 125.982 154.066 167.464 1.00 26.03 ?  429 VAL B CG2   1 
ATOM   9017  N  N     . LYS B 1 430 ? 128.940 157.544 166.801 1.00 25.79 ?  430 LYS B N     1 
ATOM   9018  C  CA    . LYS B 1 430 ? 129.440 158.746 166.138 1.00 20.82 ?  430 LYS B CA    1 
ATOM   9019  C  C     . LYS B 1 430 ? 130.809 158.514 165.508 1.00 23.73 ?  430 LYS B C     1 
ATOM   9020  O  O     . LYS B 1 430 ? 131.057 158.946 164.375 1.00 30.67 ?  430 LYS B O     1 
ATOM   9021  C  CB    . LYS B 1 430 ? 129.488 159.914 167.125 1.00 23.66 ?  430 LYS B CB    1 
ATOM   9022  C  CG    . LYS B 1 430 ? 128.160 160.203 167.801 1.00 25.85 ?  430 LYS B CG    1 
ATOM   9023  C  CD    . LYS B 1 430 ? 127.674 161.613 167.537 1.00 27.12 ?  430 LYS B CD    1 
ATOM   9024  C  CE    . LYS B 1 430 ? 126.522 161.969 168.459 1.00 29.17 ?  430 LYS B CE    1 
ATOM   9025  N  NZ    . LYS B 1 430 ? 126.244 163.430 168.468 1.00 32.65 1  430 LYS B NZ    1 
ATOM   9026  N  N     . LEU B 1 431 ? 131.708 157.826 166.216 1.00 25.57 ?  431 LEU B N     1 
ATOM   9027  C  CA    . LEU B 1 431 ? 133.030 157.561 165.656 1.00 21.63 ?  431 LEU B CA    1 
ATOM   9028  C  C     . LEU B 1 431 ? 132.949 156.626 164.455 1.00 24.56 ?  431 LEU B C     1 
ATOM   9029  O  O     . LEU B 1 431 ? 133.677 156.808 163.471 1.00 28.94 ?  431 LEU B O     1 
ATOM   9030  C  CB    . LEU B 1 431 ? 133.946 156.983 166.731 1.00 26.72 ?  431 LEU B CB    1 
ATOM   9031  C  CG    . LEU B 1 431 ? 134.770 157.992 167.530 1.00 29.74 ?  431 LEU B CG    1 
ATOM   9032  C  CD1   . LEU B 1 431 ? 135.489 157.300 168.673 1.00 27.85 ?  431 LEU B CD1   1 
ATOM   9033  C  CD2   . LEU B 1 431 ? 135.757 158.711 166.626 1.00 28.68 ?  431 LEU B CD2   1 
ATOM   9034  N  N     . ALA B 1 432 ? 132.073 155.620 164.514 1.00 26.78 ?  432 ALA B N     1 
ATOM   9035  C  CA    . ALA B 1 432 ? 131.888 154.728 163.375 1.00 15.82 ?  432 ALA B CA    1 
ATOM   9036  C  C     . ALA B 1 432 ? 131.305 155.472 162.183 1.00 25.44 ?  432 ALA B C     1 
ATOM   9037  O  O     . ALA B 1 432 ? 131.694 155.223 161.037 1.00 27.92 ?  432 ALA B O     1 
ATOM   9038  C  CB    . ALA B 1 432 ? 130.989 153.560 163.771 1.00 17.76 ?  432 ALA B CB    1 
ATOM   9039  N  N     . THR B 1 433 ? 130.364 156.385 162.433 1.00 25.72 ?  433 THR B N     1 
ATOM   9040  C  CA    . THR B 1 433 ? 129.818 157.199 161.355 1.00 19.97 ?  433 THR B CA    1 
ATOM   9041  C  C     . THR B 1 433 ? 130.900 158.064 160.725 1.00 23.21 ?  433 THR B C     1 
ATOM   9042  O  O     . THR B 1 433 ? 130.956 158.204 159.499 1.00 32.64 ?  433 THR B O     1 
ATOM   9043  C  CB    . THR B 1 433 ? 128.673 158.066 161.881 1.00 22.90 ?  433 THR B CB    1 
ATOM   9044  O  OG1   . THR B 1 433 ? 127.672 157.229 162.473 1.00 31.80 ?  433 THR B OG1   1 
ATOM   9045  C  CG2   . THR B 1 433 ? 128.046 158.873 160.754 1.00 22.05 ?  433 THR B CG2   1 
ATOM   9046  N  N     . ASP B 1 434 ? 131.775 158.644 161.549 1.00 23.10 ?  434 ASP B N     1 
ATOM   9047  C  CA    . ASP B 1 434 ? 132.878 159.438 161.015 1.00 23.64 ?  434 ASP B CA    1 
ATOM   9048  C  C     . ASP B 1 434 ? 133.828 158.584 160.182 1.00 20.53 ?  434 ASP B C     1 
ATOM   9049  O  O     . ASP B 1 434 ? 134.281 159.008 159.112 1.00 25.07 ?  434 ASP B O     1 
ATOM   9050  C  CB    . ASP B 1 434 ? 133.631 160.121 162.154 1.00 26.42 ?  434 ASP B CB    1 
ATOM   9051  C  CG    . ASP B 1 434 ? 132.797 161.169 162.855 1.00 32.91 ?  434 ASP B CG    1 
ATOM   9052  O  OD1   . ASP B 1 434 ? 131.993 161.838 162.173 1.00 34.35 ?  434 ASP B OD1   1 
ATOM   9053  O  OD2   . ASP B 1 434 ? 132.943 161.325 164.084 1.00 33.39 -1 434 ASP B OD2   1 
ATOM   9054  N  N     . SER B 1 435 ? 134.145 157.379 160.660 1.00 23.60 ?  435 SER B N     1 
ATOM   9055  C  CA    . SER B 1 435 ? 135.037 156.497 159.912 1.00 18.43 ?  435 SER B CA    1 
ATOM   9056  C  C     . SER B 1 435 ? 134.420 156.078 158.581 1.00 22.69 ?  435 SER B C     1 
ATOM   9057  O  O     . SER B 1 435 ? 135.109 156.040 157.554 1.00 32.06 ?  435 SER B O     1 
ATOM   9058  C  CB    . SER B 1 435 ? 135.385 155.269 160.751 1.00 22.49 ?  435 SER B CB    1 
ATOM   9059  O  OG    . SER B 1 435 ? 134.284 154.383 160.841 1.00 23.75 ?  435 SER B OG    1 
ATOM   9060  N  N     . LEU B 1 436 ? 133.124 155.764 158.577 1.00 21.95 ?  436 LEU B N     1 
ATOM   9061  C  CA    . LEU B 1 436 ? 132.458 155.385 157.334 1.00 13.09 ?  436 LEU B CA    1 
ATOM   9062  C  C     . LEU B 1 436 ? 132.359 156.568 156.380 1.00 18.56 ?  436 LEU B C     1 
ATOM   9063  O  O     . LEU B 1 436 ? 132.477 156.401 155.160 1.00 23.01 ?  436 LEU B O     1 
ATOM   9064  C  CB    . LEU B 1 436 ? 131.075 154.812 157.638 1.00 22.43 ?  436 LEU B CB    1 
ATOM   9065  C  CG    . LEU B 1 436 ? 131.060 153.492 158.412 1.00 21.08 ?  436 LEU B CG    1 
ATOM   9066  C  CD1   . LEU B 1 436 ? 129.682 153.217 158.987 1.00 18.38 ?  436 LEU B CD1   1 
ATOM   9067  C  CD2   . LEU B 1 436 ? 131.513 152.347 157.526 1.00 18.57 ?  436 LEU B CD2   1 
ATOM   9068  N  N     . THR B 1 437 ? 132.148 157.771 156.917 1.00 21.16 ?  437 THR B N     1 
ATOM   9069  C  CA    . THR B 1 437 ? 132.161 158.968 156.085 1.00 20.15 ?  437 THR B CA    1 
ATOM   9070  C  C     . THR B 1 437 ? 133.529 159.175 155.450 1.00 22.83 ?  437 THR B C     1 
ATOM   9071  O  O     . THR B 1 437 ? 133.628 159.530 154.271 1.00 29.74 ?  437 THR B O     1 
ATOM   9072  C  CB    . THR B 1 437 ? 131.768 160.188 156.918 1.00 20.41 ?  437 THR B CB    1 
ATOM   9073  O  OG1   . THR B 1 437 ? 130.524 159.933 157.580 1.00 23.40 ?  437 THR B OG1   1 
ATOM   9074  C  CG2   . THR B 1 437 ? 131.628 161.413 156.039 1.00 20.77 ?  437 THR B CG2   1 
ATOM   9075  N  N     . HIS B 1 438 ? 134.596 158.955 156.220 1.00 21.30 ?  438 HIS B N     1 
ATOM   9076  C  CA    . HIS B 1 438 ? 135.941 159.055 155.663 1.00 21.63 ?  438 HIS B CA    1 
ATOM   9077  C  C     . HIS B 1 438 ? 136.164 158.016 154.572 1.00 23.01 ?  438 HIS B C     1 
ATOM   9078  O  O     . HIS B 1 438 ? 136.744 158.322 153.521 1.00 32.46 ?  438 HIS B O     1 
ATOM   9079  C  CB    . HIS B 1 438 ? 136.980 158.898 156.773 1.00 26.49 ?  438 HIS B CB    1 
ATOM   9080  C  CG    . HIS B 1 438 ? 138.392 158.884 156.277 1.00 27.67 ?  438 HIS B CG    1 
ATOM   9081  N  ND1   . HIS B 1 438 ? 139.082 160.036 155.964 1.00 25.54 ?  438 HIS B ND1   1 
ATOM   9082  C  CD2   . HIS B 1 438 ? 139.240 157.859 156.029 1.00 28.00 ?  438 HIS B CD2   1 
ATOM   9083  C  CE1   . HIS B 1 438 ? 140.297 159.720 155.554 1.00 30.66 ?  438 HIS B CE1   1 
ATOM   9084  N  NE2   . HIS B 1 438 ? 140.418 158.405 155.582 1.00 31.16 ?  438 HIS B NE2   1 
ATOM   9085  N  N     . VAL B 1 439 ? 135.708 156.783 154.800 1.00 21.40 ?  439 VAL B N     1 
ATOM   9086  C  CA    . VAL B 1 439 ? 135.876 155.730 153.799 1.00 19.11 ?  439 VAL B CA    1 
ATOM   9087  C  C     . VAL B 1 439 ? 135.136 156.091 152.519 1.00 28.84 ?  439 VAL B C     1 
ATOM   9088  O  O     . VAL B 1 439 ? 135.641 155.877 151.410 1.00 32.53 ?  439 VAL B O     1 
ATOM   9089  C  CB    . VAL B 1 439 ? 135.408 154.375 154.361 1.00 23.77 ?  439 VAL B CB    1 
ATOM   9090  C  CG1   . VAL B 1 439 ? 135.356 153.327 153.259 1.00 20.70 ?  439 VAL B CG1   1 
ATOM   9091  C  CG2   . VAL B 1 439 ? 136.331 153.922 155.471 1.00 21.77 ?  439 VAL B CG2   1 
ATOM   9092  N  N     . SER B 1 440 ? 133.928 156.645 152.648 1.00 24.41 ?  440 SER B N     1 
ATOM   9093  C  CA    . SER B 1 440 ? 133.191 157.097 151.473 1.00 20.03 ?  440 SER B CA    1 
ATOM   9094  C  C     . SER B 1 440 ? 133.922 158.232 150.764 1.00 25.90 ?  440 SER B C     1 
ATOM   9095  O  O     . SER B 1 440 ? 134.001 158.255 149.531 1.00 31.54 ?  440 SER B O     1 
ATOM   9096  C  CB    . SER B 1 440 ? 131.783 157.536 151.873 1.00 22.41 ?  440 SER B CB    1 
ATOM   9097  O  OG    . SER B 1 440 ? 130.977 157.774 150.732 1.00 31.27 ?  440 SER B OG    1 
ATOM   9098  N  N     . GLU B 1 441 ? 134.461 159.183 151.529 1.00 26.70 ?  441 GLU B N     1 
ATOM   9099  C  CA    . GLU B 1 441 ? 135.104 160.350 150.931 1.00 24.82 ?  441 GLU B CA    1 
ATOM   9100  C  C     . GLU B 1 441 ? 136.370 159.970 150.172 1.00 32.63 ?  441 GLU B C     1 
ATOM   9101  O  O     . GLU B 1 441 ? 136.635 160.511 149.093 1.00 40.05 ?  441 GLU B O     1 
ATOM   9102  C  CB    . GLU B 1 441 ? 135.415 161.386 152.009 1.00 27.11 ?  441 GLU B CB    1 
ATOM   9103  C  CG    . GLU B 1 441 ? 134.230 162.265 152.371 1.00 27.69 ?  441 GLU B CG    1 
ATOM   9104  C  CD    . GLU B 1 441 ? 134.301 162.788 153.792 1.00 35.39 ?  441 GLU B CD    1 
ATOM   9105  O  OE1   . GLU B 1 441 ? 135.247 162.420 154.519 1.00 37.20 ?  441 GLU B OE1   1 
ATOM   9106  O  OE2   . GLU B 1 441 ? 133.406 163.565 154.182 1.00 36.45 -1 441 GLU B OE2   1 
ATOM   9107  N  N     . THR B 1 442 ? 137.165 159.048 150.712 1.00 31.61 ?  442 THR B N     1 
ATOM   9108  C  CA    . THR B 1 442 ? 138.396 158.636 150.050 1.00 30.94 ?  442 THR B CA    1 
ATOM   9109  C  C     . THR B 1 442 ? 138.181 157.548 149.006 1.00 29.64 ?  442 THR B C     1 
ATOM   9110  O  O     . THR B 1 442 ? 139.156 157.089 148.403 1.00 34.42 ?  442 THR B O     1 
ATOM   9111  C  CB    . THR B 1 442 ? 139.434 158.161 151.074 1.00 29.54 ?  442 THR B CB    1 
ATOM   9112  O  OG1   . THR B 1 442 ? 139.143 156.815 151.474 1.00 31.14 ?  442 THR B OG1   1 
ATOM   9113  C  CG2   . THR B 1 442 ? 139.458 159.075 152.283 1.00 31.60 ?  442 THR B CG2   1 
ATOM   9114  N  N     . THR B 1 443 ? 136.942 157.124 148.777 1.00 30.24 ?  443 THR B N     1 
ATOM   9115  C  CA    . THR B 1 443 ? 136.641 156.155 147.734 1.00 34.71 ?  443 THR B CA    1 
ATOM   9116  C  C     . THR B 1 443 ? 136.408 156.877 146.414 1.00 35.60 ?  443 THR B C     1 
ATOM   9117  O  O     . THR B 1 443 ? 135.559 157.770 146.328 1.00 36.53 ?  443 THR B O     1 
ATOM   9118  C  CB    . THR B 1 443 ? 135.413 155.320 148.100 1.00 33.90 ?  443 THR B CB    1 
ATOM   9119  O  OG1   . THR B 1 443 ? 135.727 154.461 149.202 1.00 39.26 ?  443 THR B OG1   1 
ATOM   9120  C  CG2   . THR B 1 443 ? 134.976 154.477 146.914 1.00 27.95 ?  443 THR B CG2   1 
ATOM   9121  N  N     . ASP B 1 444 ? 137.167 156.491 145.391 1.00 39.02 ?  444 ASP B N     1 
ATOM   9122  C  CA    . ASP B 1 444 ? 137.028 157.058 144.052 1.00 38.94 ?  444 ASP B CA    1 
ATOM   9123  C  C     . ASP B 1 444 ? 137.271 155.942 143.046 1.00 39.94 ?  444 ASP B C     1 
ATOM   9124  O  O     . ASP B 1 444 ? 138.413 155.508 142.863 1.00 40.16 ?  444 ASP B O     1 
ATOM   9125  C  CB    . ASP B 1 444 ? 138.001 158.217 143.835 1.00 41.00 ?  444 ASP B CB    1 
ATOM   9126  C  CG    . ASP B 1 444 ? 137.478 159.240 142.847 1.00 46.45 ?  444 ASP B CG    1 
ATOM   9127  O  OD1   . ASP B 1 444 ? 136.400 159.817 143.100 1.00 44.63 ?  444 ASP B OD1   1 
ATOM   9128  O  OD2   . ASP B 1 444 ? 138.147 159.470 141.817 1.00 43.46 -1 444 ASP B OD2   1 
ATOM   9129  N  N     . ILE B 1 445 ? 136.207 155.482 142.399 1.00 37.64 ?  445 ILE B N     1 
ATOM   9130  C  CA    . ILE B 1 445 ? 136.276 154.380 141.446 1.00 36.46 ?  445 ILE B CA    1 
ATOM   9131  C  C     . ILE B 1 445 ? 136.224 154.964 140.042 1.00 37.15 ?  445 ILE B C     1 
ATOM   9132  O  O     . ILE B 1 445 ? 135.248 155.625 139.669 1.00 42.66 ?  445 ILE B O     1 
ATOM   9133  C  CB    . ILE B 1 445 ? 135.140 153.373 141.675 1.00 32.65 ?  445 ILE B CB    1 
ATOM   9134  C  CG1   . ILE B 1 445 ? 135.400 152.578 142.953 1.00 33.55 ?  445 ILE B CG1   1 
ATOM   9135  C  CG2   . ILE B 1 445 ? 135.017 152.432 140.489 1.00 35.35 ?  445 ILE B CG2   1 
ATOM   9136  C  CD1   . ILE B 1 445 ? 134.173 151.924 143.516 1.00 35.02 ?  445 ILE B CD1   1 
ATOM   9137  N  N     . ARG B 1 446 ? 137.273 154.717 139.262 1.00 36.82 ?  446 ARG B N     1 
ATOM   9138  C  CA    . ARG B 1 446 ? 137.457 155.371 137.975 1.00 39.43 ?  446 ARG B CA    1 
ATOM   9139  C  C     . ARG B 1 446 ? 136.864 154.591 136.808 1.00 40.16 ?  446 ARG B C     1 
ATOM   9140  O  O     . ARG B 1 446 ? 136.945 155.061 135.668 1.00 37.10 ?  446 ARG B O     1 
ATOM   9141  C  CB    . ARG B 1 446 ? 138.949 155.614 137.724 1.00 37.35 ?  446 ARG B CB    1 
ATOM   9142  C  CG    . ARG B 1 446 ? 139.770 155.753 138.996 1.00 37.48 ?  446 ARG B CG    1 
ATOM   9143  C  CD    . ARG B 1 446 ? 139.626 157.136 139.612 1.00 39.79 ?  446 ARG B CD    1 
ATOM   9144  N  NE    . ARG B 1 446 ? 139.689 158.197 138.616 1.00 40.67 ?  446 ARG B NE    1 
ATOM   9145  C  CZ    . ARG B 1 446 ? 139.979 159.462 138.889 1.00 40.52 ?  446 ARG B CZ    1 
ATOM   9146  N  NH1   . ARG B 1 446 ? 140.239 159.860 140.124 1.00 37.72 1  446 ARG B NH1   1 
ATOM   9147  N  NH2   . ARG B 1 446 ? 140.008 160.350 137.899 1.00 39.59 ?  446 ARG B NH2   1 
ATOM   9148  N  N     . ASN B 1 447 ? 136.269 153.425 137.054 1.00 33.35 ?  447 ASN B N     1 
ATOM   9149  C  CA    . ASN B 1 447 ? 135.683 152.623 135.992 1.00 25.93 ?  447 ASN B CA    1 
ATOM   9150  C  C     . ASN B 1 447 ? 134.197 152.360 136.185 1.00 30.51 ?  447 ASN B C     1 
ATOM   9151  O  O     . ASN B 1 447 ? 133.579 151.725 135.323 1.00 37.20 ?  447 ASN B O     1 
ATOM   9152  C  CB    . ASN B 1 447 ? 136.425 151.287 135.860 1.00 31.43 ?  447 ASN B CB    1 
ATOM   9153  C  CG    . ASN B 1 447 ? 137.558 151.352 134.860 1.00 30.80 ?  447 ASN B CG    1 
ATOM   9154  O  OD1   . ASN B 1 447 ? 137.339 151.586 133.673 1.00 34.38 ?  447 ASN B OD1   1 
ATOM   9155  N  ND2   . ASN B 1 447 ? 138.780 151.149 135.335 1.00 29.87 ?  447 ASN B ND2   1 
ATOM   9156  N  N     . ALA B 1 448 ? 133.607 152.824 137.285 1.00 31.55 ?  448 ALA B N     1 
ATOM   9157  C  CA    . ALA B 1 448 ? 132.167 152.746 137.523 1.00 26.92 ?  448 ALA B CA    1 
ATOM   9158  C  C     . ALA B 1 448 ? 131.661 154.170 137.706 1.00 27.73 ?  448 ALA B C     1 
ATOM   9159  O  O     . ALA B 1 448 ? 131.746 154.732 138.809 1.00 29.36 ?  448 ALA B O     1 
ATOM   9160  C  CB    . ALA B 1 448 ? 131.849 151.876 138.735 1.00 26.31 ?  448 ALA B CB    1 
ATOM   9161  N  N     . PRO B 1 449 ? 131.139 154.797 136.649 1.00 27.20 ?  449 PRO B N     1 
ATOM   9162  C  CA    . PRO B 1 449 ? 130.756 156.213 136.770 1.00 24.21 ?  449 PRO B CA    1 
ATOM   9163  C  C     . PRO B 1 449 ? 129.533 156.426 137.638 1.00 24.86 ?  449 PRO B C     1 
ATOM   9164  O  O     . PRO B 1 449 ? 129.500 157.376 138.431 1.00 21.81 ?  449 PRO B O     1 
ATOM   9165  C  CB    . PRO B 1 449 ? 130.496 156.637 135.315 1.00 21.18 ?  449 PRO B CB    1 
ATOM   9166  C  CG    . PRO B 1 449 ? 130.893 155.465 134.462 1.00 25.67 ?  449 PRO B CG    1 
ATOM   9167  C  CD    . PRO B 1 449 ? 130.842 154.254 135.316 1.00 25.18 ?  449 PRO B CD    1 
ATOM   9168  N  N     . ALA B 1 450 ? 128.518 155.572 137.505 1.00 28.94 ?  450 ALA B N     1 
ATOM   9169  C  CA    . ALA B 1 450 ? 127.326 155.709 138.332 1.00 19.52 ?  450 ALA B CA    1 
ATOM   9170  C  C     . ALA B 1 450 ? 127.642 155.440 139.797 1.00 23.03 ?  450 ALA B C     1 
ATOM   9171  O  O     . ALA B 1 450 ? 127.112 156.115 140.685 1.00 24.84 ?  450 ALA B O     1 
ATOM   9172  C  CB    . ALA B 1 450 ? 126.229 154.774 137.830 1.00 19.72 ?  450 ALA B CB    1 
ATOM   9173  N  N     . VAL B 1 451 ? 128.513 154.465 140.070 1.00 26.08 ?  451 VAL B N     1 
ATOM   9174  C  CA    . VAL B 1 451 ? 128.929 154.201 141.444 1.00 19.47 ?  451 VAL B CA    1 
ATOM   9175  C  C     . VAL B 1 451 ? 129.659 155.407 142.020 1.00 19.53 ?  451 VAL B C     1 
ATOM   9176  O  O     . VAL B 1 451 ? 129.421 155.805 143.165 1.00 26.05 ?  451 VAL B O     1 
ATOM   9177  C  CB    . VAL B 1 451 ? 129.796 152.929 141.511 1.00 22.52 ?  451 VAL B CB    1 
ATOM   9178  C  CG1   . VAL B 1 451 ? 130.415 152.774 142.890 1.00 25.41 ?  451 VAL B CG1   1 
ATOM   9179  C  CG2   . VAL B 1 451 ? 128.973 151.705 141.159 1.00 19.90 ?  451 VAL B CG2   1 
ATOM   9180  N  N     . ARG B 1 452 ? 130.558 156.007 141.239 1.00 21.20 ?  452 ARG B N     1 
ATOM   9181  C  CA    . ARG B 1 452 ? 131.291 157.179 141.710 1.00 23.42 ?  452 ARG B CA    1 
ATOM   9182  C  C     . ARG B 1 452 ? 130.346 158.344 141.986 1.00 24.60 ?  452 ARG B C     1 
ATOM   9183  O  O     . ARG B 1 452 ? 130.445 159.010 143.026 1.00 30.17 ?  452 ARG B O     1 
ATOM   9184  C  CB    . ARG B 1 452 ? 132.351 157.578 140.682 1.00 20.90 ?  452 ARG B CB    1 
ATOM   9185  C  CG    . ARG B 1 452 ? 133.043 158.892 140.990 1.00 24.84 ?  452 ARG B CG    1 
ATOM   9186  C  CD    . ARG B 1 452 ? 134.496 158.871 140.555 1.00 27.79 ?  452 ARG B CD    1 
ATOM   9187  N  NE    . ARG B 1 452 ? 134.690 159.575 139.293 1.00 33.94 ?  452 ARG B NE    1 
ATOM   9188  C  CZ    . ARG B 1 452 ? 135.726 159.393 138.485 1.00 38.90 ?  452 ARG B CZ    1 
ATOM   9189  N  NH1   . ARG B 1 452 ? 136.686 158.534 138.778 1.00 31.79 1  452 ARG B NH1   1 
ATOM   9190  N  NH2   . ARG B 1 452 ? 135.798 160.093 137.357 1.00 34.38 ?  452 ARG B NH2   1 
ATOM   9191  N  N     . ARG B 1 453 ? 129.417 158.600 141.063 1.00 22.40 ?  453 ARG B N     1 
ATOM   9192  C  CA    . ARG B 1 453 ? 128.481 159.706 141.241 1.00 20.83 ?  453 ARG B CA    1 
ATOM   9193  C  C     . ARG B 1 453 ? 127.579 159.475 142.446 1.00 23.25 ?  453 ARG B C     1 
ATOM   9194  O  O     . ARG B 1 453 ? 127.310 160.406 143.214 1.00 25.88 ?  453 ARG B O     1 
ATOM   9195  C  CB    . ARG B 1 453 ? 127.653 159.899 139.969 1.00 20.64 ?  453 ARG B CB    1 
ATOM   9196  C  CG    . ARG B 1 453 ? 126.395 160.724 140.160 1.00 20.05 ?  453 ARG B CG    1 
ATOM   9197  C  CD    . ARG B 1 453 ? 125.865 161.239 138.834 1.00 20.46 ?  453 ARG B CD    1 
ATOM   9198  N  NE    . ARG B 1 453 ? 124.460 160.906 138.645 1.00 22.82 ?  453 ARG B NE    1 
ATOM   9199  C  CZ    . ARG B 1 453 ? 123.449 161.636 139.095 1.00 26.10 ?  453 ARG B CZ    1 
ATOM   9200  N  NH1   . ARG B 1 453 ? 123.652 162.755 139.770 1.00 28.13 1  453 ARG B NH1   1 
ATOM   9201  N  NH2   . ARG B 1 453 ? 122.203 161.232 138.865 1.00 25.07 ?  453 ARG B NH2   1 
ATOM   9202  N  N     . ALA B 1 454 ? 127.106 158.240 142.634 1.00 23.91 ?  454 ALA B N     1 
ATOM   9203  C  CA    . ALA B 1 454 ? 126.256 157.940 143.780 1.00 17.46 ?  454 ALA B CA    1 
ATOM   9204  C  C     . ALA B 1 454 ? 127.029 158.036 145.088 1.00 21.92 ?  454 ALA B C     1 
ATOM   9205  O  O     . ALA B 1 454 ? 126.483 158.479 146.100 1.00 24.78 ?  454 ALA B O     1 
ATOM   9206  C  CB    . ALA B 1 454 ? 125.633 156.555 143.621 1.00 19.55 ?  454 ALA B CB    1 
ATOM   9207  N  N     . ASN B 1 455 ? 128.294 157.616 145.096 1.00 23.90 ?  455 ASN B N     1 
ATOM   9208  C  CA    . ASN B 1 455 ? 129.108 157.776 146.295 1.00 20.72 ?  455 ASN B CA    1 
ATOM   9209  C  C     . ASN B 1 455 ? 129.304 159.248 146.627 1.00 26.36 ?  455 ASN B C     1 
ATOM   9210  O  O     . ASN B 1 455 ? 129.248 159.644 147.797 1.00 30.59 ?  455 ASN B O     1 
ATOM   9211  C  CB    . ASN B 1 455 ? 130.456 157.082 146.113 1.00 20.52 ?  455 ASN B CB    1 
ATOM   9212  C  CG    . ASN B 1 455 ? 131.274 157.057 147.386 1.00 24.75 ?  455 ASN B CG    1 
ATOM   9213  O  OD1   . ASN B 1 455 ? 130.983 156.299 148.308 1.00 30.97 ?  455 ASN B OD1   1 
ATOM   9214  N  ND2   . ASN B 1 455 ? 132.303 157.893 147.444 1.00 27.07 ?  455 ASN B ND2   1 
ATOM   9215  N  N     . LYS B 1 456 ? 129.532 160.077 145.606 1.00 27.25 ?  456 LYS B N     1 
ATOM   9216  C  CA    . LYS B 1 456 ? 129.745 161.500 145.843 1.00 25.06 ?  456 LYS B CA    1 
ATOM   9217  C  C     . LYS B 1 456 ? 128.466 162.209 146.272 1.00 23.96 ?  456 LYS B C     1 
ATOM   9218  O  O     . LYS B 1 456 ? 128.523 163.157 147.061 1.00 32.65 ?  456 LYS B O     1 
ATOM   9219  C  CB    . LYS B 1 456 ? 130.318 162.159 144.588 1.00 26.81 ?  456 LYS B CB    1 
ATOM   9220  C  CG    . LYS B 1 456 ? 131.572 162.980 144.832 1.00 30.51 ?  456 LYS B CG    1 
ATOM   9221  C  CD    . LYS B 1 456 ? 132.244 163.366 143.525 1.00 33.74 ?  456 LYS B CD    1 
ATOM   9222  C  CE    . LYS B 1 456 ? 132.609 162.138 142.707 1.00 33.23 ?  456 LYS B CE    1 
ATOM   9223  N  NZ    . LYS B 1 456 ? 133.743 161.383 143.307 1.00 28.20 1  456 LYS B NZ    1 
ATOM   9224  N  N     . ALA B 1 457 ? 127.311 161.775 145.767 1.00 24.59 ?  457 ALA B N     1 
ATOM   9225  C  CA    . ALA B 1 457 ? 126.056 162.481 146.008 1.00 18.66 ?  457 ALA B CA    1 
ATOM   9226  C  C     . ALA B 1 457 ? 125.307 161.934 147.220 1.00 26.26 ?  457 ALA B C     1 
ATOM   9227  O  O     . ALA B 1 457 ? 124.992 162.680 148.153 1.00 32.54 ?  457 ALA B O     1 
ATOM   9228  C  CB    . ALA B 1 457 ? 125.175 162.405 144.756 1.00 18.26 ?  457 ALA B CB    1 
ATOM   9229  N  N     . MET B 1 458 ? 125.000 160.636 147.207 1.00 24.94 ?  458 MET B N     1 
ATOM   9230  C  CA    . MET B 1 458 ? 124.255 160.020 148.298 1.00 16.55 ?  458 MET B CA    1 
ATOM   9231  C  C     . MET B 1 458 ? 125.031 160.070 149.607 1.00 21.35 ?  458 MET B C     1 
ATOM   9232  O  O     . MET B 1 458 ? 124.445 160.290 150.673 1.00 30.53 ?  458 MET B O     1 
ATOM   9233  C  CB    . MET B 1 458 ? 123.916 158.572 147.940 1.00 22.58 ?  458 MET B CB    1 
ATOM   9234  C  CG    . MET B 1 458 ? 123.307 158.392 146.561 1.00 21.89 ?  458 MET B CG    1 
ATOM   9235  S  SD    . MET B 1 458 ? 121.917 159.495 146.268 1.00 29.65 ?  458 MET B SD    1 
ATOM   9236  C  CE    . MET B 1 458 ? 120.713 158.791 147.388 1.00 23.61 ?  458 MET B CE    1 
ATOM   9237  N  N     . LYS B 1 459 ? 126.346 159.849 149.549 1.00 19.92 ?  459 LYS B N     1 
ATOM   9238  C  CA    . LYS B 1 459 ? 127.192 159.761 150.743 1.00 17.97 ?  459 LYS B CA    1 
ATOM   9239  C  C     . LYS B 1 459 ? 126.688 158.673 151.688 1.00 20.01 ?  459 LYS B C     1 
ATOM   9240  O  O     . LYS B 1 459 ? 126.776 158.795 152.910 1.00 26.61 ?  459 LYS B O     1 
ATOM   9241  C  CB    . LYS B 1 459 ? 127.284 161.106 151.466 1.00 20.12 ?  459 LYS B CB    1 
ATOM   9242  C  CG    . LYS B 1 459 ? 128.031 162.181 150.702 1.00 24.69 ?  459 LYS B CG    1 
ATOM   9243  C  CD    . LYS B 1 459 ? 127.434 163.551 150.967 1.00 25.09 ?  459 LYS B CD    1 
ATOM   9244  C  CE    . LYS B 1 459 ? 127.802 164.534 149.873 1.00 25.13 ?  459 LYS B CE    1 
ATOM   9245  N  NZ    . LYS B 1 459 ? 129.277 164.670 149.727 1.00 27.84 1  459 LYS B NZ    1 
ATOM   9246  N  N     . SER B 1 460 ? 126.155 157.600 151.114 1.00 24.04 ?  460 SER B N     1 
ATOM   9247  C  CA    . SER B 1 460 ? 125.545 156.540 151.899 1.00 13.89 ?  460 SER B CA    1 
ATOM   9248  C  C     . SER B 1 460 ? 126.604 155.685 152.579 1.00 13.09 ?  460 SER B C     1 
ATOM   9249  O  O     . SER B 1 460 ? 127.626 155.337 151.981 1.00 26.30 ?  460 SER B O     1 
ATOM   9250  C  CB    . SER B 1 460 ? 124.662 155.664 151.013 1.00 15.88 ?  460 SER B CB    1 
ATOM   9251  O  OG    . SER B 1 460 ? 124.647 154.331 151.486 1.00 26.50 ?  460 SER B OG    1 
ATOM   9252  N  N     . ILE B 1 461 ? 126.349 155.345 153.842 1.00 10.69 ?  461 ILE B N     1 
ATOM   9253  C  CA    . ILE B 1 461 ? 127.215 154.470 154.616 1.00 19.56 ?  461 ILE B CA    1 
ATOM   9254  C  C     . ILE B 1 461 ? 126.355 153.379 155.236 1.00 16.81 ?  461 ILE B C     1 
ATOM   9255  O  O     . ILE B 1 461 ? 125.136 153.507 155.356 1.00 20.02 ?  461 ILE B O     1 
ATOM   9256  C  CB    . ILE B 1 461 ? 127.993 155.229 155.711 1.00 14.38 ?  461 ILE B CB    1 
ATOM   9257  C  CG1   . ILE B 1 461 ? 127.026 155.838 156.726 1.00 10.83 ?  461 ILE B CG1   1 
ATOM   9258  C  CG2   . ILE B 1 461 ? 128.878 156.303 155.096 1.00 17.22 ?  461 ILE B CG2   1 
ATOM   9259  C  CD1   . ILE B 1 461 ? 127.702 156.438 157.935 1.00 14.55 ?  461 ILE B CD1   1 
ATOM   9260  N  N     . GLY B 1 462 ? 127.007 152.284 155.612 1.00 15.87 ?  462 GLY B N     1 
ATOM   9261  C  CA    . GLY B 1 462 ? 126.316 151.221 156.312 1.00 6.58  ?  462 GLY B CA    1 
ATOM   9262  C  C     . GLY B 1 462 ? 126.942 150.906 157.652 1.00 11.82 ?  462 GLY B C     1 
ATOM   9263  O  O     . GLY B 1 462 ? 128.049 150.366 157.713 1.00 26.95 ?  462 GLY B O     1 
ATOM   9264  N  N     . LEU B 1 463 ? 126.241 151.230 158.733 1.00 12.36 ?  463 LEU B N     1 
ATOM   9265  C  CA    . LEU B 1 463 ? 126.711 150.951 160.084 1.00 11.25 ?  463 LEU B CA    1 
ATOM   9266  C  C     . LEU B 1 463 ? 125.907 149.778 160.631 1.00 13.98 ?  463 LEU B C     1 
ATOM   9267  O  O     . LEU B 1 463 ? 124.731 149.929 160.974 1.00 25.51 ?  463 LEU B O     1 
ATOM   9268  C  CB    . LEU B 1 463 ? 126.577 152.183 160.976 1.00 19.67 ?  463 LEU B CB    1 
ATOM   9269  C  CG    . LEU B 1 463 ? 126.969 152.009 162.445 1.00 18.45 ?  463 LEU B CG    1 
ATOM   9270  C  CD1   . LEU B 1 463 ? 128.340 151.368 162.559 1.00 6.51  ?  463 LEU B CD1   1 
ATOM   9271  C  CD2   . LEU B 1 463 ? 126.934 153.342 163.171 1.00 14.56 ?  463 LEU B CD2   1 
ATOM   9272  N  N     . GLY B 1 464 ? 126.544 148.611 160.706 1.00 14.85 ?  464 GLY B N     1 
ATOM   9273  C  CA    . GLY B 1 464 ? 125.899 147.405 161.172 1.00 13.86 ?  464 GLY B CA    1 
ATOM   9274  C  C     . GLY B 1 464 ? 126.137 147.148 162.648 1.00 13.07 ?  464 GLY B C     1 
ATOM   9275  O  O     . GLY B 1 464 ? 126.619 148.000 163.397 1.00 15.05 ?  464 GLY B O     1 
ATOM   9276  N  N     . ALA B 1 465 ? 125.785 145.935 163.064 1.00 15.16 ?  465 ALA B N     1 
ATOM   9277  C  CA    . ALA B 1 465 ? 125.966 145.512 164.442 1.00 12.37 ?  465 ALA B CA    1 
ATOM   9278  C  C     . ALA B 1 465 ? 126.242 144.019 164.466 1.00 14.17 ?  465 ALA B C     1 
ATOM   9279  O  O     . ALA B 1 465 ? 125.705 143.268 163.647 1.00 28.53 ?  465 ALA B O     1 
ATOM   9280  C  CB    . ALA B 1 465 ? 124.739 145.841 165.300 1.00 19.00 ?  465 ALA B CB    1 
ATOM   9281  N  N     . MET B 1 466 ? 127.088 143.598 165.402 1.00 20.66 ?  466 MET B N     1 
ATOM   9282  C  CA    . MET B 1 466 ? 127.414 142.197 165.608 1.00 20.75 ?  466 MET B CA    1 
ATOM   9283  C  C     . MET B 1 466 ? 127.275 141.868 167.087 1.00 20.58 ?  466 MET B C     1 
ATOM   9284  O  O     . MET B 1 466 ? 127.142 142.757 167.933 1.00 26.81 ?  466 MET B O     1 
ATOM   9285  C  CB    . MET B 1 466 ? 128.832 141.867 165.119 1.00 27.19 ?  466 MET B CB    1 
ATOM   9286  C  CG    . MET B 1 466 ? 129.905 142.807 165.645 1.00 22.89 ?  466 MET B CG    1 
ATOM   9287  S  SD    . MET B 1 466 ? 131.566 142.400 165.077 1.00 38.02 ?  466 MET B SD    1 
ATOM   9288  C  CE    . MET B 1 466 ? 131.292 142.169 163.324 1.00 29.36 ?  466 MET B CE    1 
ATOM   9289  N  N     . ASN B 1 467 ? 127.291 140.569 167.388 1.00 19.96 ?  467 ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 467 ? 127.279 140.063 168.762 1.00 19.55 ?  467 ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 467 ? 125.980 140.406 169.488 1.00 20.51 ?  467 ASN B C     1 
ATOM   9292  O  O     . ASN B 1 467 ? 125.984 140.685 170.686 1.00 27.46 ?  467 ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 467 ? 128.484 140.571 169.557 1.00 21.54 ?  467 ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 467 ? 129.086 139.506 170.446 1.00 24.57 ?  467 ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 467 ? 128.725 138.333 170.360 1.00 28.94 ?  467 ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 467 ? 130.012 139.907 171.305 1.00 28.00 ?  467 ASN B ND2   1 
ATOM   9297  N  N     . LEU B 1 468 ? 124.861 140.396 168.762 1.00 19.53 ?  468 LEU B N     1 
ATOM   9298  C  CA    . LEU B 1 468 ? 123.568 140.514 169.429 1.00 18.12 ?  468 LEU B CA    1 
ATOM   9299  C  C     . LEU B 1 468 ? 123.266 139.262 170.241 1.00 22.01 ?  468 LEU B C     1 
ATOM   9300  O  O     . LEU B 1 468 ? 122.943 139.341 171.433 1.00 25.58 ?  468 LEU B O     1 
ATOM   9301  C  CB    . LEU B 1 468 ? 122.464 140.765 168.404 1.00 24.55 ?  468 LEU B CB    1 
ATOM   9302  C  CG    . LEU B 1 468 ? 121.042 140.691 168.965 1.00 20.38 ?  468 LEU B CG    1 
ATOM   9303  C  CD1   . LEU B 1 468 ? 120.804 141.805 169.970 1.00 17.94 ?  468 LEU B CD1   1 
ATOM   9304  C  CD2   . LEU B 1 468 ? 120.007 140.733 167.855 1.00 15.41 ?  468 LEU B CD2   1 
ATOM   9305  N  N     . HIS B 1 469 ? 123.398 138.091 169.615 1.00 25.31 ?  469 HIS B N     1 
ATOM   9306  C  CA    . HIS B 1 469 ? 123.139 136.843 170.322 1.00 16.96 ?  469 HIS B CA    1 
ATOM   9307  C  C     . HIS B 1 469 ? 124.185 136.596 171.398 1.00 26.08 ?  469 HIS B C     1 
ATOM   9308  O  O     . HIS B 1 469 ? 123.867 136.059 172.462 1.00 38.87 ?  469 HIS B O     1 
ATOM   9309  C  CB    . HIS B 1 469 ? 123.093 135.674 169.342 1.00 20.40 ?  469 HIS B CB    1 
ATOM   9310  C  CG    . HIS B 1 469 ? 122.454 134.443 169.907 1.00 24.73 ?  469 HIS B CG    1 
ATOM   9311  N  ND1   . HIS B 1 469 ? 122.458 133.233 169.250 1.00 28.72 ?  469 HIS B ND1   1 
ATOM   9312  C  CD2   . HIS B 1 469 ? 121.792 134.238 171.070 1.00 25.30 ?  469 HIS B CD2   1 
ATOM   9313  C  CE1   . HIS B 1 469 ? 121.825 132.335 169.982 1.00 22.84 ?  469 HIS B CE1   1 
ATOM   9314  N  NE2   . HIS B 1 469 ? 121.412 132.918 171.092 1.00 25.44 ?  469 HIS B NE2   1 
ATOM   9315  N  N     . GLY B 1 470 ? 125.437 136.973 171.138 1.00 21.78 ?  470 GLY B N     1 
ATOM   9316  C  CA    . GLY B 1 470 ? 126.459 136.841 172.163 1.00 18.71 ?  470 GLY B CA    1 
ATOM   9317  C  C     . GLY B 1 470 ? 126.151 137.670 173.393 1.00 19.99 ?  470 GLY B C     1 
ATOM   9318  O  O     . GLY B 1 470 ? 126.257 137.191 174.524 1.00 34.01 ?  470 GLY B O     1 
ATOM   9319  N  N     . TYR B 1 471 ? 125.748 138.925 173.185 1.00 22.88 ?  471 TYR B N     1 
ATOM   9320  C  CA    . TYR B 1 471 ? 125.390 139.779 174.312 1.00 25.52 ?  471 TYR B CA    1 
ATOM   9321  C  C     . TYR B 1 471 ? 124.175 139.235 175.050 1.00 27.96 ?  471 TYR B C     1 
ATOM   9322  O  O     . TYR B 1 471 ? 124.141 139.233 176.287 1.00 32.88 ?  471 TYR B O     1 
ATOM   9323  C  CB    . TYR B 1 471 ? 125.124 141.206 173.836 1.00 24.23 ?  471 TYR B CB    1 
ATOM   9324  C  CG    . TYR B 1 471 ? 124.816 142.165 174.963 1.00 26.56 ?  471 TYR B CG    1 
ATOM   9325  C  CD1   . TYR B 1 471 ? 125.813 142.579 175.836 1.00 28.31 ?  471 TYR B CD1   1 
ATOM   9326  C  CD2   . TYR B 1 471 ? 123.527 142.634 175.172 1.00 18.57 ?  471 TYR B CD2   1 
ATOM   9327  C  CE1   . TYR B 1 471 ? 125.540 143.449 176.871 1.00 28.21 ?  471 TYR B CE1   1 
ATOM   9328  C  CE2   . TYR B 1 471 ? 123.245 143.501 176.208 1.00 21.27 ?  471 TYR B CE2   1 
ATOM   9329  C  CZ    . TYR B 1 471 ? 124.254 143.905 177.052 1.00 27.48 ?  471 TYR B CZ    1 
ATOM   9330  O  OH    . TYR B 1 471 ? 123.980 144.767 178.088 1.00 32.99 ?  471 TYR B OH    1 
ATOM   9331  N  N     . LEU B 1 472 ? 123.163 138.772 174.311 1.00 26.27 ?  472 LEU B N     1 
ATOM   9332  C  CA    . LEU B 1 472 ? 121.953 138.272 174.955 1.00 23.87 ?  472 LEU B CA    1 
ATOM   9333  C  C     . LEU B 1 472 ? 122.224 136.998 175.749 1.00 25.52 ?  472 LEU B C     1 
ATOM   9334  O  O     . LEU B 1 472 ? 121.716 136.837 176.864 1.00 31.23 ?  472 LEU B O     1 
ATOM   9335  C  CB    . LEU B 1 472 ? 120.861 138.034 173.913 1.00 28.13 ?  472 LEU B CB    1 
ATOM   9336  C  CG    . LEU B 1 472 ? 120.332 139.266 173.179 1.00 27.42 ?  472 LEU B CG    1 
ATOM   9337  C  CD1   . LEU B 1 472 ? 119.471 138.854 171.995 1.00 24.49 ?  472 LEU B CD1   1 
ATOM   9338  C  CD2   . LEU B 1 472 ? 119.557 140.169 174.124 1.00 19.86 ?  472 LEU B CD2   1 
ATOM   9339  N  N     . ALA B 1 473 ? 123.017 136.080 175.191 1.00 25.93 ?  473 ALA B N     1 
ATOM   9340  C  CA    . ALA B 1 473 ? 123.295 134.823 175.874 1.00 26.31 ?  473 ALA B CA    1 
ATOM   9341  C  C     . ALA B 1 473 ? 124.227 135.028 177.059 1.00 33.22 ?  473 ALA B C     1 
ATOM   9342  O  O     . ALA B 1 473 ? 124.077 134.369 178.094 1.00 38.99 ?  473 ALA B O     1 
ATOM   9343  C  CB    . ALA B 1 473 ? 123.887 133.815 174.890 1.00 26.76 ?  473 ALA B CB    1 
ATOM   9344  N  N     . GLN B 1 474 ? 125.197 135.933 176.932 1.00 27.75 ?  474 GLN B N     1 
ATOM   9345  C  CA    . GLN B 1 474 ? 126.103 136.219 178.036 1.00 28.56 ?  474 GLN B CA    1 
ATOM   9346  C  C     . GLN B 1 474 ? 125.447 137.039 179.137 1.00 29.18 ?  474 GLN B C     1 
ATOM   9347  O  O     . GLN B 1 474 ? 126.039 137.187 180.211 1.00 36.85 ?  474 GLN B O     1 
ATOM   9348  C  CB    . GLN B 1 474 ? 127.348 136.943 177.518 1.00 28.71 ?  474 GLN B CB    1 
ATOM   9349  C  CG    . GLN B 1 474 ? 128.314 136.033 176.779 1.00 28.77 ?  474 GLN B CG    1 
ATOM   9350  C  CD    . GLN B 1 474 ? 129.455 136.792 176.139 1.00 33.70 ?  474 GLN B CD    1 
ATOM   9351  O  OE1   . GLN B 1 474 ? 130.316 137.338 176.828 1.00 36.08 ?  474 GLN B OE1   1 
ATOM   9352  N  NE2   . GLN B 1 474 ? 129.470 136.831 174.812 1.00 33.97 ?  474 GLN B NE2   1 
ATOM   9353  N  N     . ASN B 1 475 ? 124.251 137.573 178.898 1.00 31.43 ?  475 ASN B N     1 
ATOM   9354  C  CA    . ASN B 1 475 ? 123.497 138.305 179.905 1.00 31.52 ?  475 ASN B CA    1 
ATOM   9355  C  C     . ASN B 1 475 ? 122.257 137.548 180.361 1.00 31.77 ?  475 ASN B C     1 
ATOM   9356  O  O     . ASN B 1 475 ? 121.393 138.134 181.021 1.00 34.96 ?  475 ASN B O     1 
ATOM   9357  C  CB    . ASN B 1 475 ? 123.108 139.685 179.371 1.00 30.74 ?  475 ASN B CB    1 
ATOM   9358  C  CG    . ASN B 1 475 ? 124.286 140.633 179.309 1.00 30.26 ?  475 ASN B CG    1 
ATOM   9359  O  OD1   . ASN B 1 475 ? 124.542 141.387 180.247 1.00 38.24 ?  475 ASN B OD1   1 
ATOM   9360  N  ND2   . ASN B 1 475 ? 125.019 140.590 178.205 1.00 28.97 ?  475 ASN B ND2   1 
ATOM   9361  N  N     . GLY B 1 476 ? 122.149 136.267 180.025 1.00 31.06 ?  476 GLY B N     1 
ATOM   9362  C  CA    . GLY B 1 476 ? 121.016 135.462 180.443 1.00 30.18 ?  476 GLY B CA    1 
ATOM   9363  C  C     . GLY B 1 476 ? 119.690 135.868 179.839 1.00 35.17 ?  476 GLY B C     1 
ATOM   9364  O  O     . GLY B 1 476 ? 118.671 135.878 180.541 1.00 37.39 ?  476 GLY B O     1 
ATOM   9365  N  N     . ILE B 1 477 ? 119.674 136.208 178.553 1.00 32.15 ?  477 ILE B N     1 
ATOM   9366  C  CA    . ILE B 1 477 ? 118.453 136.568 177.843 1.00 27.50 ?  477 ILE B CA    1 
ATOM   9367  C  C     . ILE B 1 477 ? 118.318 135.646 176.640 1.00 31.33 ?  477 ILE B C     1 
ATOM   9368  O  O     . ILE B 1 477 ? 119.230 135.568 175.807 1.00 36.33 ?  477 ILE B O     1 
ATOM   9369  C  CB    . ILE B 1 477 ? 118.454 138.040 177.405 1.00 26.02 ?  477 ILE B CB    1 
ATOM   9370  C  CG1   . ILE B 1 477 ? 118.656 138.958 178.611 1.00 29.49 ?  477 ILE B CG1   1 
ATOM   9371  C  CG2   . ILE B 1 477 ? 117.157 138.381 176.695 1.00 30.20 ?  477 ILE B CG2   1 
ATOM   9372  C  CD1   . ILE B 1 477 ? 119.154 140.332 178.243 1.00 32.35 ?  477 ILE B CD1   1 
ATOM   9373  N  N     . ALA B 1 478 ? 117.189 134.948 176.553 1.00 33.41 ?  478 ALA B N     1 
ATOM   9374  C  CA    . ALA B 1 478 ? 116.926 134.093 175.405 1.00 27.28 ?  478 ALA B CA    1 
ATOM   9375  C  C     . ALA B 1 478 ? 116.694 134.946 174.165 1.00 32.74 ?  478 ALA B C     1 
ATOM   9376  O  O     . ALA B 1 478 ? 115.973 135.946 174.216 1.00 34.41 ?  478 ALA B O     1 
ATOM   9377  C  CB    . ALA B 1 478 ? 115.717 133.200 175.673 1.00 27.73 ?  478 ALA B CB    1 
ATOM   9378  N  N     . TYR B 1 479 ? 117.308 134.546 173.048 1.00 30.56 ?  479 TYR B N     1 
ATOM   9379  C  CA    . TYR B 1 479 ? 117.205 135.325 171.818 1.00 23.51 ?  479 TYR B CA    1 
ATOM   9380  C  C     . TYR B 1 479 ? 115.762 135.452 171.348 1.00 26.65 ?  479 TYR B C     1 
ATOM   9381  O  O     . TYR B 1 479 ? 115.387 136.475 170.766 1.00 32.90 ?  479 TYR B O     1 
ATOM   9382  C  CB    . TYR B 1 479 ? 118.075 134.688 170.733 1.00 18.58 ?  479 TYR B CB    1 
ATOM   9383  C  CG    . TYR B 1 479 ? 118.130 135.438 169.417 1.00 26.64 ?  479 TYR B CG    1 
ATOM   9384  C  CD1   . TYR B 1 479 ? 117.184 135.215 168.425 1.00 24.92 ?  479 TYR B CD1   1 
ATOM   9385  C  CD2   . TYR B 1 479 ? 119.142 136.354 169.163 1.00 25.29 ?  479 TYR B CD2   1 
ATOM   9386  C  CE1   . TYR B 1 479 ? 117.236 135.894 167.222 1.00 22.84 ?  479 TYR B CE1   1 
ATOM   9387  C  CE2   . TYR B 1 479 ? 119.203 137.036 167.963 1.00 22.12 ?  479 TYR B CE2   1 
ATOM   9388  C  CZ    . TYR B 1 479 ? 118.249 136.802 166.997 1.00 28.95 ?  479 TYR B CZ    1 
ATOM   9389  O  OH    . TYR B 1 479 ? 118.309 137.481 165.802 1.00 29.93 ?  479 TYR B OH    1 
ATOM   9390  N  N     . GLU B 1 480 ? 114.940 134.432 171.587 1.00 28.98 ?  480 GLU B N     1 
ATOM   9391  C  CA    . GLU B 1 480 ? 113.539 134.472 171.192 1.00 28.27 ?  480 GLU B CA    1 
ATOM   9392  C  C     . GLU B 1 480 ? 112.646 135.150 172.222 1.00 27.46 ?  480 GLU B C     1 
ATOM   9393  O  O     . GLU B 1 480 ? 111.460 135.361 171.945 1.00 33.76 ?  480 GLU B O     1 
ATOM   9394  C  CB    . GLU B 1 480 ? 113.016 133.055 170.942 1.00 30.32 ?  480 GLU B CB    1 
ATOM   9395  C  CG    . GLU B 1 480 ? 113.704 132.314 169.813 1.00 28.24 ?  480 GLU B CG    1 
ATOM   9396  C  CD    . GLU B 1 480 ? 113.318 130.850 169.777 1.00 36.35 ?  480 GLU B CD    1 
ATOM   9397  O  OE1   . GLU B 1 480 ? 112.162 130.548 169.414 1.00 36.92 ?  480 GLU B OE1   1 
ATOM   9398  O  OE2   . GLU B 1 480 ? 114.165 130.000 170.121 1.00 36.74 -1 480 GLU B OE2   1 
ATOM   9399  N  N     . SER B 1 481 ? 113.178 135.493 173.390 1.00 26.14 ?  481 SER B N     1 
ATOM   9400  C  CA    . SER B 1 481 ? 112.356 136.057 174.446 1.00 26.98 ?  481 SER B CA    1 
ATOM   9401  C  C     . SER B 1 481 ? 111.917 137.477 174.091 1.00 28.79 ?  481 SER B C     1 
ATOM   9402  O  O     . SER B 1 481 ? 112.589 138.171 173.323 1.00 29.80 ?  481 SER B O     1 
ATOM   9403  C  CB    . SER B 1 481 ? 113.121 136.067 175.765 1.00 28.32 ?  481 SER B CB    1 
ATOM   9404  O  OG    . SER B 1 481 ? 113.876 137.256 175.905 1.00 32.20 ?  481 SER B OG    1 
ATOM   9405  N  N     . PRO B 1 482 ? 110.778 137.924 174.625 1.00 36.02 ?  482 PRO B N     1 
ATOM   9406  C  CA    . PRO B 1 482 ? 110.394 139.333 174.443 1.00 32.05 ?  482 PRO B CA    1 
ATOM   9407  C  C     . PRO B 1 482 ? 111.392 140.307 175.039 1.00 31.69 ?  482 PRO B C     1 
ATOM   9408  O  O     . PRO B 1 482 ? 111.489 141.445 174.564 1.00 31.35 ?  482 PRO B O     1 
ATOM   9409  C  CB    . PRO B 1 482 ? 109.030 139.417 175.143 1.00 30.81 ?  482 PRO B CB    1 
ATOM   9410  C  CG    . PRO B 1 482 ? 108.524 138.018 175.164 1.00 31.49 ?  482 PRO B CG    1 
ATOM   9411  C  CD    . PRO B 1 482 ? 109.733 137.151 175.316 1.00 33.90 ?  482 PRO B CD    1 
ATOM   9412  N  N     . GLU B 1 483 ? 112.128 139.900 176.076 1.00 34.74 ?  483 GLU B N     1 
ATOM   9413  C  CA    . GLU B 1 483 ? 113.150 140.771 176.648 1.00 33.51 ?  483 GLU B CA    1 
ATOM   9414  C  C     . GLU B 1 483 ? 114.262 141.049 175.645 1.00 33.18 ?  483 GLU B C     1 
ATOM   9415  O  O     . GLU B 1 483 ? 114.781 142.169 175.576 1.00 38.65 ?  483 GLU B O     1 
ATOM   9416  C  CB    . GLU B 1 483 ? 113.720 140.146 177.920 1.00 36.12 ?  483 GLU B CB    1 
ATOM   9417  C  CG    . GLU B 1 483 ? 112.798 140.234 179.120 1.00 37.22 ?  483 GLU B CG    1 
ATOM   9418  C  CD    . GLU B 1 483 ? 111.965 138.982 179.305 1.00 41.25 ?  483 GLU B CD    1 
ATOM   9419  O  OE1   . GLU B 1 483 ? 111.531 138.399 178.290 1.00 39.62 ?  483 GLU B OE1   1 
ATOM   9420  O  OE2   . GLU B 1 483 ? 111.744 138.581 180.468 1.00 40.92 -1 483 GLU B OE2   1 
ATOM   9421  N  N     . ALA B 1 484 ? 114.648 140.035 174.867 1.00 26.92 ?  484 ALA B N     1 
ATOM   9422  C  CA    . ALA B 1 484 ? 115.659 140.236 173.836 1.00 25.36 ?  484 ALA B CA    1 
ATOM   9423  C  C     . ALA B 1 484 ? 115.177 141.212 172.771 1.00 27.63 ?  484 ALA B C     1 
ATOM   9424  O  O     . ALA B 1 484 ? 115.941 142.070 172.313 1.00 27.44 ?  484 ALA B O     1 
ATOM   9425  C  CB    . ALA B 1 484 ? 116.034 138.896 173.210 1.00 24.44 ?  484 ALA B CB    1 
ATOM   9426  N  N     . ARG B 1 485 ? 113.913 141.093 172.357 1.00 29.59 ?  485 ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 485 ? 113.371 142.032 171.381 1.00 22.93 ?  485 ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 485 ? 113.270 143.439 171.956 1.00 23.94 ?  485 ARG B C     1 
ATOM   9429  O  O     . ARG B 1 485 ? 113.492 144.416 171.236 1.00 33.77 ?  485 ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 485 ? 112.006 141.555 170.891 1.00 28.90 ?  485 ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 485 ? 112.066 140.290 170.053 1.00 27.03 ?  485 ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 485 ? 110.729 139.998 169.402 1.00 27.04 ?  485 ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 485 ? 109.656 139.872 170.380 1.00 27.22 ?  485 ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 485 ? 109.321 138.741 170.985 1.00 27.87 ?  485 ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 485 ? 109.967 137.612 170.745 1.00 25.07 1  485 ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 485 ? 108.313 138.743 171.851 1.00 30.16 ?  485 ARG B NH2   1 
ATOM   9437  N  N     . ASP B 1 486 ? 112.944 143.558 173.244 1.00 30.99 ?  486 ASP B N     1 
ATOM   9438  C  CA    . ASP B 1 486 ? 112.944 144.864 173.896 1.00 27.43 ?  486 ASP B CA    1 
ATOM   9439  C  C     . ASP B 1 486 ? 114.339 145.476 173.905 1.00 26.61 ?  486 ASP B C     1 
ATOM   9440  O  O     . ASP B 1 486 ? 114.508 146.673 173.626 1.00 33.37 ?  486 ASP B O     1 
ATOM   9441  C  CB    . ASP B 1 486 ? 112.405 144.724 175.319 1.00 32.56 ?  486 ASP B CB    1 
ATOM   9442  C  CG    . ASP B 1 486 ? 112.230 146.054 176.013 1.00 40.37 ?  486 ASP B CG    1 
ATOM   9443  O  OD1   . ASP B 1 486 ? 111.588 146.953 175.433 1.00 37.86 ?  486 ASP B OD1   1 
ATOM   9444  O  OD2   . ASP B 1 486 ? 112.734 146.193 177.146 1.00 37.16 -1 486 ASP B OD2   1 
ATOM   9445  N  N     . PHE B 1 487 ? 115.352 144.666 174.217 1.00 25.12 ?  487 PHE B N     1 
ATOM   9446  C  CA    . PHE B 1 487 ? 116.724 145.158 174.181 1.00 24.05 ?  487 PHE B CA    1 
ATOM   9447  C  C     . PHE B 1 487 ? 117.109 145.599 172.777 1.00 23.70 ?  487 PHE B C     1 
ATOM   9448  O  O     . PHE B 1 487 ? 117.751 146.637 172.600 1.00 29.55 ?  487 PHE B O     1 
ATOM   9449  C  CB    . PHE B 1 487 ? 117.703 144.094 174.670 1.00 25.33 ?  487 PHE B CB    1 
ATOM   9450  C  CG    . PHE B 1 487 ? 119.119 144.376 174.266 1.00 27.57 ?  487 PHE B CG    1 
ATOM   9451  C  CD1   . PHE B 1 487 ? 119.856 145.340 174.929 1.00 22.50 ?  487 PHE B CD1   1 
ATOM   9452  C  CD2   . PHE B 1 487 ? 119.698 143.715 173.195 1.00 29.01 ?  487 PHE B CD2   1 
ATOM   9453  C  CE1   . PHE B 1 487 ? 121.147 145.624 174.551 1.00 24.30 ?  487 PHE B CE1   1 
ATOM   9454  C  CE2   . PHE B 1 487 ? 120.991 143.998 172.812 1.00 25.24 ?  487 PHE B CE2   1 
ATOM   9455  C  CZ    . PHE B 1 487 ? 121.716 144.954 173.492 1.00 27.43 ?  487 PHE B CZ    1 
ATOM   9456  N  N     . ALA B 1 488 ? 116.758 144.799 171.770 1.00 24.45 ?  488 ALA B N     1 
ATOM   9457  C  CA    . ALA B 1 488 ? 117.086 145.163 170.397 1.00 19.89 ?  488 ALA B CA    1 
ATOM   9458  C  C     . ALA B 1 488 ? 116.399 146.463 170.004 1.00 26.39 ?  488 ALA B C     1 
ATOM   9459  O  O     . ALA B 1 488 ? 117.018 147.341 169.394 1.00 31.88 ?  488 ALA B O     1 
ATOM   9460  C  CB    . ALA B 1 488 ? 116.696 144.036 169.444 1.00 20.17 ?  488 ALA B CB    1 
ATOM   9461  N  N     . ASN B 1 489 ? 115.125 146.609 170.371 1.00 25.22 ?  489 ASN B N     1 
ATOM   9462  C  CA    . ASN B 1 489 ? 114.394 147.838 170.092 1.00 24.36 ?  489 ASN B CA    1 
ATOM   9463  C  C     . ASN B 1 489 ? 115.107 149.043 170.686 1.00 23.95 ?  489 ASN B C     1 
ATOM   9464  O  O     . ASN B 1 489 ? 115.399 150.016 169.981 1.00 24.39 ?  489 ASN B O     1 
ATOM   9465  C  CB    . ASN B 1 489 ? 112.973 147.727 170.644 1.00 21.91 ?  489 ASN B CB    1 
ATOM   9466  C  CG    . ASN B 1 489 ? 112.079 148.856 170.189 1.00 27.14 ?  489 ASN B CG    1 
ATOM   9467  O  OD1   . ASN B 1 489 ? 112.067 149.218 169.015 1.00 33.77 ?  489 ASN B OD1   1 
ATOM   9468  N  ND2   . ASN B 1 489 ? 111.318 149.416 171.119 1.00 30.58 ?  489 ASN B ND2   1 
ATOM   9469  N  N     . THR B 1 490 ? 115.425 148.982 171.980 1.00 27.27 ?  490 THR B N     1 
ATOM   9470  C  CA    . THR B 1 490 ? 116.054 150.127 172.633 1.00 22.97 ?  490 THR B CA    1 
ATOM   9471  C  C     . THR B 1 490 ? 117.442 150.400 172.064 1.00 24.75 ?  490 THR B C     1 
ATOM   9472  O  O     . THR B 1 490 ? 117.779 151.548 171.746 1.00 25.78 ?  490 THR B O     1 
ATOM   9473  C  CB    . THR B 1 490 ? 116.129 149.899 174.142 1.00 28.98 ?  490 THR B CB    1 
ATOM   9474  O  OG1   . THR B 1 490 ? 114.821 149.609 174.648 1.00 32.64 ?  490 THR B OG1   1 
ATOM   9475  C  CG2   . THR B 1 490 ? 116.678 151.136 174.833 1.00 26.06 ?  490 THR B CG2   1 
ATOM   9476  N  N     . PHE B 1 491 ? 118.260 149.354 171.921 1.00 24.63 ?  491 PHE B N     1 
ATOM   9477  C  CA    . PHE B 1 491 ? 119.635 149.532 171.469 1.00 19.07 ?  491 PHE B CA    1 
ATOM   9478  C  C     . PHE B 1 491 ? 119.685 150.102 170.060 1.00 19.39 ?  491 PHE B C     1 
ATOM   9479  O  O     . PHE B 1 491 ? 120.466 151.018 169.782 1.00 28.67 ?  491 PHE B O     1 
ATOM   9480  C  CB    . PHE B 1 491 ? 120.380 148.198 171.535 1.00 25.23 ?  491 PHE B CB    1 
ATOM   9481  C  CG    . PHE B 1 491 ? 121.756 148.239 170.931 1.00 23.98 ?  491 PHE B CG    1 
ATOM   9482  C  CD1   . PHE B 1 491 ? 122.842 148.641 171.686 1.00 19.94 ?  491 PHE B CD1   1 
ATOM   9483  C  CD2   . PHE B 1 491 ? 121.965 147.869 169.611 1.00 19.44 ?  491 PHE B CD2   1 
ATOM   9484  C  CE1   . PHE B 1 491 ? 124.108 148.682 171.139 1.00 16.87 ?  491 PHE B CE1   1 
ATOM   9485  C  CE2   . PHE B 1 491 ? 123.226 147.912 169.059 1.00 17.20 ?  491 PHE B CE2   1 
ATOM   9486  C  CZ    . PHE B 1 491 ? 124.300 148.318 169.825 1.00 23.78 ?  491 PHE B CZ    1 
ATOM   9487  N  N     . PHE B 1 492 ? 118.861 149.580 169.154 1.00 17.42 ?  492 PHE B N     1 
ATOM   9488  C  CA    . PHE B 1 492 ? 118.904 150.062 167.785 1.00 12.24 ?  492 PHE B CA    1 
ATOM   9489  C  C     . PHE B 1 492 ? 118.183 151.389 167.609 1.00 13.03 ?  492 PHE B C     1 
ATOM   9490  O  O     . PHE B 1 492 ? 118.536 152.145 166.703 1.00 24.31 ?  492 PHE B O     1 
ATOM   9491  C  CB    . PHE B 1 492 ? 118.348 148.993 166.847 1.00 17.91 ?  492 PHE B CB    1 
ATOM   9492  C  CG    . PHE B 1 492 ? 119.293 147.844 166.641 1.00 20.42 ?  492 PHE B CG    1 
ATOM   9493  C  CD1   . PHE B 1 492 ? 120.401 147.982 165.825 1.00 14.94 ?  492 PHE B CD1   1 
ATOM   9494  C  CD2   . PHE B 1 492 ? 119.096 146.641 167.295 1.00 19.18 ?  492 PHE B CD2   1 
ATOM   9495  C  CE1   . PHE B 1 492 ? 121.281 146.934 165.647 1.00 10.03 ?  492 PHE B CE1   1 
ATOM   9496  C  CE2   . PHE B 1 492 ? 119.972 145.590 167.122 1.00 15.06 ?  492 PHE B CE2   1 
ATOM   9497  C  CZ    . PHE B 1 492 ? 121.065 145.737 166.295 1.00 15.00 ?  492 PHE B CZ    1 
ATOM   9498  N  N     . MET B 1 493 ? 117.224 151.724 168.479 1.00 16.96 ?  493 MET B N     1 
ATOM   9499  C  CA    . MET B 1 493 ? 116.721 153.092 168.493 1.00 17.53 ?  493 MET B CA    1 
ATOM   9500  C  C     . MET B 1 493 ? 117.815 154.062 168.922 1.00 17.63 ?  493 MET B C     1 
ATOM   9501  O  O     . MET B 1 493 ? 117.945 155.146 168.349 1.00 26.01 ?  493 MET B O     1 
ATOM   9502  C  CB    . MET B 1 493 ? 115.494 153.193 169.404 1.00 17.60 ?  493 MET B CB    1 
ATOM   9503  C  CG    . MET B 1 493 ? 115.044 154.613 169.763 1.00 20.72 ?  493 MET B CG    1 
ATOM   9504  S  SD    . MET B 1 493 ? 115.939 155.395 171.123 1.00 30.63 ?  493 MET B SD    1 
ATOM   9505  C  CE    . MET B 1 493 ? 115.675 154.195 172.421 1.00 24.03 ?  493 MET B CE    1 
ATOM   9506  N  N     . MET B 1 494 ? 118.612 153.685 169.927 1.00 21.86 ?  494 MET B N     1 
ATOM   9507  C  CA    . MET B 1 494 ? 119.753 154.512 170.319 1.00 16.39 ?  494 MET B CA    1 
ATOM   9508  C  C     . MET B 1 494 ? 120.755 154.651 169.180 1.00 19.03 ?  494 MET B C     1 
ATOM   9509  O  O     . MET B 1 494 ? 121.275 155.747 168.926 1.00 22.87 ?  494 MET B O     1 
ATOM   9510  C  CB    . MET B 1 494 ? 120.437 153.914 171.550 1.00 20.19 ?  494 MET B CB    1 
ATOM   9511  C  CG    . MET B 1 494 ? 119.589 153.880 172.806 1.00 20.19 ?  494 MET B CG    1 
ATOM   9512  S  SD    . MET B 1 494 ? 120.607 153.748 174.288 1.00 37.53 ?  494 MET B SD    1 
ATOM   9513  C  CE    . MET B 1 494 ? 121.267 155.405 174.403 1.00 30.33 ?  494 MET B CE    1 
ATOM   9514  N  N     . VAL B 1 495 ? 121.047 153.546 168.494 1.00 19.01 ?  495 VAL B N     1 
ATOM   9515  C  CA    . VAL B 1 495 ? 121.985 153.581 167.377 1.00 17.66 ?  495 VAL B CA    1 
ATOM   9516  C  C     . VAL B 1 495 ? 121.468 154.494 166.274 1.00 17.55 ?  495 VAL B C     1 
ATOM   9517  O  O     . VAL B 1 495 ? 122.217 155.308 165.726 1.00 28.72 ?  495 VAL B O     1 
ATOM   9518  C  CB    . VAL B 1 495 ? 122.253 152.156 166.857 1.00 15.28 ?  495 VAL B CB    1 
ATOM   9519  C  CG1   . VAL B 1 495 ? 123.001 152.203 165.535 1.00 10.14 ?  495 VAL B CG1   1 
ATOM   9520  C  CG2   . VAL B 1 495 ? 123.037 151.359 167.880 1.00 19.24 ?  495 VAL B CG2   1 
ATOM   9521  N  N     . ASN B 1 496 ? 120.182 154.378 165.936 1.00 19.18 ?  496 ASN B N     1 
ATOM   9522  C  CA    . ASN B 1 496 ? 119.599 155.243 164.915 1.00 12.13 ?  496 ASN B CA    1 
ATOM   9523  C  C     . ASN B 1 496 ? 119.625 156.702 165.345 1.00 19.26 ?  496 ASN B C     1 
ATOM   9524  O  O     . ASN B 1 496 ? 119.936 157.588 164.540 1.00 30.91 ?  496 ASN B O     1 
ATOM   9525  C  CB    . ASN B 1 496 ? 118.168 154.802 164.610 1.00 16.23 ?  496 ASN B CB    1 
ATOM   9526  C  CG    . ASN B 1 496 ? 117.655 155.357 163.301 1.00 16.08 ?  496 ASN B CG    1 
ATOM   9527  O  OD1   . ASN B 1 496 ? 118.425 155.600 162.373 1.00 24.74 ?  496 ASN B OD1   1 
ATOM   9528  N  ND2   . ASN B 1 496 ? 116.348 155.566 163.217 1.00 15.35 ?  496 ASN B ND2   1 
ATOM   9529  N  N     . PHE B 1 497 ? 119.303 156.973 166.611 1.00 20.27 ?  497 PHE B N     1 
ATOM   9530  C  CA    . PHE B 1 497 ? 119.305 158.343 167.111 1.00 15.60 ?  497 PHE B CA    1 
ATOM   9531  C  C     . PHE B 1 497 ? 120.687 158.963 166.984 1.00 19.24 ?  497 PHE B C     1 
ATOM   9532  O  O     . PHE B 1 497 ? 120.838 160.074 166.465 1.00 26.32 ?  497 PHE B O     1 
ATOM   9533  C  CB    . PHE B 1 497 ? 118.836 158.361 168.567 1.00 17.84 ?  497 PHE B CB    1 
ATOM   9534  C  CG    . PHE B 1 497 ? 118.851 159.723 169.200 1.00 20.97 ?  497 PHE B CG    1 
ATOM   9535  C  CD1   . PHE B 1 497 ? 119.981 160.189 169.853 1.00 21.66 ?  497 PHE B CD1   1 
ATOM   9536  C  CD2   . PHE B 1 497 ? 117.731 160.534 169.153 1.00 21.23 ?  497 PHE B CD2   1 
ATOM   9537  C  CE1   . PHE B 1 497 ? 119.994 161.440 170.435 1.00 22.63 ?  497 PHE B CE1   1 
ATOM   9538  C  CE2   . PHE B 1 497 ? 117.739 161.785 169.734 1.00 20.87 ?  497 PHE B CE2   1 
ATOM   9539  C  CZ    . PHE B 1 497 ? 118.872 162.237 170.377 1.00 23.33 ?  497 PHE B CZ    1 
ATOM   9540  N  N     . TYR B 1 498 ? 121.714 158.249 167.441 1.00 26.89 ?  498 TYR B N     1 
ATOM   9541  C  CA    . TYR B 1 498 ? 123.052 158.823 167.418 1.00 18.43 ?  498 TYR B CA    1 
ATOM   9542  C  C     . TYR B 1 498 ? 123.639 158.846 166.013 1.00 18.27 ?  498 TYR B C     1 
ATOM   9543  O  O     . TYR B 1 498 ? 124.433 159.737 165.700 1.00 26.71 ?  498 TYR B O     1 
ATOM   9544  C  CB    . TYR B 1 498 ? 123.955 158.073 168.394 1.00 18.97 ?  498 TYR B CB    1 
ATOM   9545  C  CG    . TYR B 1 498 ? 123.598 158.373 169.831 1.00 22.61 ?  498 TYR B CG    1 
ATOM   9546  C  CD1   . TYR B 1 498 ? 123.605 159.678 170.304 1.00 23.34 ?  498 TYR B CD1   1 
ATOM   9547  C  CD2   . TYR B 1 498 ? 123.229 157.360 170.706 1.00 26.29 ?  498 TYR B CD2   1 
ATOM   9548  C  CE1   . TYR B 1 498 ? 123.267 159.965 171.610 1.00 24.09 ?  498 TYR B CE1   1 
ATOM   9549  C  CE2   . TYR B 1 498 ? 122.891 157.639 172.015 1.00 25.24 ?  498 TYR B CE2   1 
ATOM   9550  C  CZ    . TYR B 1 498 ? 122.912 158.943 172.461 1.00 29.24 ?  498 TYR B CZ    1 
ATOM   9551  O  OH    . TYR B 1 498 ? 122.578 159.228 173.765 1.00 35.73 ?  498 TYR B OH    1 
ATOM   9552  N  N     . SER B 1 499 ? 123.235 157.918 165.142 1.00 19.26 ?  499 SER B N     1 
ATOM   9553  C  CA    . SER B 1 499 ? 123.660 157.984 163.749 1.00 13.36 ?  499 SER B CA    1 
ATOM   9554  C  C     . SER B 1 499 ? 123.051 159.189 163.044 1.00 18.33 ?  499 SER B C     1 
ATOM   9555  O  O     . SER B 1 499 ? 123.740 159.888 162.295 1.00 20.27 ?  499 SER B O     1 
ATOM   9556  C  CB    . SER B 1 499 ? 123.289 156.690 163.026 1.00 14.93 ?  499 SER B CB    1 
ATOM   9557  O  OG    . SER B 1 499 ? 124.020 156.552 161.822 1.00 19.27 ?  499 SER B OG    1 
ATOM   9558  N  N     . ILE B 1 500 ? 121.763 159.453 163.280 1.00 18.14 ?  500 ILE B N     1 
ATOM   9559  C  CA    . ILE B 1 500 ? 121.127 160.638 162.710 1.00 20.90 ?  500 ILE B CA    1 
ATOM   9560  C  C     . ILE B 1 500 ? 121.766 161.900 163.270 1.00 19.50 ?  500 ILE B C     1 
ATOM   9561  O  O     . ILE B 1 500 ? 121.994 162.874 162.542 1.00 26.97 ?  500 ILE B O     1 
ATOM   9562  C  CB    . ILE B 1 500 ? 119.610 160.609 162.969 1.00 23.62 ?  500 ILE B CB    1 
ATOM   9563  C  CG1   . ILE B 1 500 ? 118.953 159.473 162.190 1.00 18.38 ?  500 ILE B CG1   1 
ATOM   9564  C  CG2   . ILE B 1 500 ? 118.971 161.932 162.591 1.00 18.21 ?  500 ILE B CG2   1 
ATOM   9565  C  CD1   . ILE B 1 500 ? 117.559 159.166 162.653 1.00 22.35 ?  500 ILE B CD1   1 
ATOM   9566  N  N     . GLN B 1 501 ? 122.062 161.906 164.572 1.00 20.82 ?  501 GLN B N     1 
ATOM   9567  C  CA    . GLN B 1 501 ? 122.703 163.066 165.178 1.00 22.83 ?  501 GLN B CA    1 
ATOM   9568  C  C     . GLN B 1 501 ? 124.076 163.319 164.570 1.00 24.83 ?  501 GLN B C     1 
ATOM   9569  O  O     . GLN B 1 501 ? 124.416 164.463 164.252 1.00 30.68 ?  501 GLN B O     1 
ATOM   9570  C  CB    . GLN B 1 501 ? 122.809 162.874 166.689 1.00 27.35 ?  501 GLN B CB    1 
ATOM   9571  C  CG    . GLN B 1 501 ? 122.879 164.173 167.471 1.00 24.19 ?  501 GLN B CG    1 
ATOM   9572  C  CD    . GLN B 1 501 ? 122.705 163.963 168.959 1.00 28.90 ?  501 GLN B CD    1 
ATOM   9573  O  OE1   . GLN B 1 501 ? 123.363 163.115 169.560 1.00 34.53 ?  501 GLN B OE1   1 
ATOM   9574  N  NE2   . GLN B 1 501 ? 121.813 164.736 169.565 1.00 31.97 ?  501 GLN B NE2   1 
ATOM   9575  N  N     . ARG B 1 502 ? 124.875 162.265 164.391 1.00 23.90 ?  502 ARG B N     1 
ATOM   9576  C  CA    . ARG B 1 502 ? 126.190 162.432 163.783 1.00 20.10 ?  502 ARG B CA    1 
ATOM   9577  C  C     . ARG B 1 502 ? 126.080 162.872 162.328 1.00 22.90 ?  502 ARG B C     1 
ATOM   9578  O  O     . ARG B 1 502 ? 126.872 163.697 161.868 1.00 30.30 ?  502 ARG B O     1 
ATOM   9579  C  CB    . ARG B 1 502 ? 126.995 161.139 163.890 1.00 23.30 ?  502 ARG B CB    1 
ATOM   9580  C  CG    . ARG B 1 502 ? 128.471 161.328 163.585 1.00 26.41 ?  502 ARG B CG    1 
ATOM   9581  C  CD    . ARG B 1 502 ? 129.039 162.506 164.354 1.00 26.01 ?  502 ARG B CD    1 
ATOM   9582  N  NE    . ARG B 1 502 ? 130.361 162.887 163.873 1.00 24.91 ?  502 ARG B NE    1 
ATOM   9583  C  CZ    . ARG B 1 502 ? 130.807 164.134 163.816 1.00 23.93 ?  502 ARG B CZ    1 
ATOM   9584  N  NH1   . ARG B 1 502 ? 130.063 165.152 164.213 1.00 30.63 1  502 ARG B NH1   1 
ATOM   9585  N  NH2   . ARG B 1 502 ? 132.030 164.364 163.348 1.00 28.82 ?  502 ARG B NH2   1 
ATOM   9586  N  N     . SER B 1 503 ? 125.115 162.324 161.586 1.00 23.38 ?  503 SER B N     1 
ATOM   9587  C  CA    . SER B 1 503 ? 124.932 162.737 160.199 1.00 22.11 ?  503 SER B CA    1 
ATOM   9588  C  C     . SER B 1 503 ? 124.566 164.213 160.112 1.00 23.05 ?  503 SER B C     1 
ATOM   9589  O  O     . SER B 1 503 ? 125.106 164.951 159.279 1.00 28.92 ?  503 SER B O     1 
ATOM   9590  C  CB    . SER B 1 503 ? 123.860 161.873 159.536 1.00 18.74 ?  503 SER B CB    1 
ATOM   9591  O  OG    . SER B 1 503 ? 124.030 161.827 158.132 1.00 24.69 ?  503 SER B OG    1 
ATOM   9592  N  N     . ALA B 1 504 ? 123.665 164.667 160.986 1.00 23.24 ?  504 ALA B N     1 
ATOM   9593  C  CA    . ALA B 1 504 ? 123.290 166.076 161.003 1.00 25.89 ?  504 ALA B CA    1 
ATOM   9594  C  C     . ALA B 1 504 ? 124.454 166.957 161.440 1.00 27.48 ?  504 ALA B C     1 
ATOM   9595  O  O     . ALA B 1 504 ? 124.632 168.061 160.915 1.00 34.08 ?  504 ALA B O     1 
ATOM   9596  C  CB    . ALA B 1 504 ? 122.081 166.282 161.912 1.00 26.38 ?  504 ALA B CB    1 
ATOM   9597  N  N     . GLU B 1 505 ? 125.261 166.486 162.393 1.00 25.13 ?  505 GLU B N     1 
ATOM   9598  C  CA    . GLU B 1 505 ? 126.421 167.257 162.830 1.00 25.65 ?  505 GLU B CA    1 
ATOM   9599  C  C     . GLU B 1 505 ? 127.459 167.374 161.722 1.00 26.97 ?  505 GLU B C     1 
ATOM   9600  O  O     . GLU B 1 505 ? 128.075 168.432 161.552 1.00 31.65 ?  505 GLU B O     1 
ATOM   9601  C  CB    . GLU B 1 505 ? 127.034 166.619 164.075 1.00 26.13 ?  505 GLU B CB    1 
ATOM   9602  C  CG    . GLU B 1 505 ? 126.237 166.851 165.346 1.00 27.47 ?  505 GLU B CG    1 
ATOM   9603  C  CD    . GLU B 1 505 ? 126.563 165.843 166.427 1.00 32.39 ?  505 GLU B CD    1 
ATOM   9604  O  OE1   . GLU B 1 505 ? 127.465 165.009 166.208 1.00 31.08 ?  505 GLU B OE1   1 
ATOM   9605  O  OE2   . GLU B 1 505 ? 125.919 165.885 167.495 1.00 34.66 -1 505 GLU B OE2   1 
ATOM   9606  N  N     . ILE B 1 506 ? 127.674 166.298 160.964 1.00 26.20 ?  506 ILE B N     1 
ATOM   9607  C  CA    . ILE B 1 506 ? 128.585 166.356 159.825 1.00 26.19 ?  506 ILE B CA    1 
ATOM   9608  C  C     . ILE B 1 506 ? 128.046 167.302 158.760 1.00 26.67 ?  506 ILE B C     1 
ATOM   9609  O  O     . ILE B 1 506 ? 128.799 168.079 158.161 1.00 33.16 ?  506 ILE B O     1 
ATOM   9610  C  CB    . ILE B 1 506 ? 128.832 164.945 159.262 1.00 25.49 ?  506 ILE B CB    1 
ATOM   9611  C  CG1   . ILE B 1 506 ? 129.543 164.073 160.296 1.00 28.34 ?  506 ILE B CG1   1 
ATOM   9612  C  CG2   . ILE B 1 506 ? 129.652 165.009 157.988 1.00 24.77 ?  506 ILE B CG2   1 
ATOM   9613  C  CD1   . ILE B 1 506 ? 129.564 162.604 159.944 1.00 21.69 ?  506 ILE B CD1   1 
ATOM   9614  N  N     . ALA B 1 507 ? 126.735 167.258 158.508 1.00 26.64 ?  507 ALA B N     1 
ATOM   9615  C  CA    . ALA B 1 507 ? 126.136 168.183 157.552 1.00 28.48 ?  507 ALA B CA    1 
ATOM   9616  C  C     . ALA B 1 507 ? 126.309 169.629 158.001 1.00 32.25 ?  507 ALA B C     1 
ATOM   9617  O  O     . ALA B 1 507 ? 126.559 170.518 157.180 1.00 36.65 ?  507 ALA B O     1 
ATOM   9618  C  CB    . ALA B 1 507 ? 124.656 167.854 157.361 1.00 24.25 ?  507 ALA B CB    1 
ATOM   9619  N  N     . LYS B 1 508 ? 126.171 169.881 159.304 1.00 32.69 ?  508 LYS B N     1 
ATOM   9620  C  CA    . LYS B 1 508 ? 126.364 171.227 159.834 1.00 30.69 ?  508 LYS B CA    1 
ATOM   9621  C  C     . LYS B 1 508 ? 127.817 171.672 159.716 1.00 36.95 ?  508 LYS B C     1 
ATOM   9622  O  O     . LYS B 1 508 ? 128.093 172.812 159.323 1.00 43.58 ?  508 LYS B O     1 
ATOM   9623  C  CB    . LYS B 1 508 ? 125.904 171.275 161.291 1.00 34.62 ?  508 LYS B CB    1 
ATOM   9624  C  CG    . LYS B 1 508 ? 126.173 172.591 161.996 1.00 35.60 ?  508 LYS B CG    1 
ATOM   9625  C  CD    . LYS B 1 508 ? 125.947 172.456 163.493 1.00 34.74 ?  508 LYS B CD    1 
ATOM   9626  C  CE    . LYS B 1 508 ? 125.914 173.811 164.177 1.00 36.44 ?  508 LYS B CE    1 
ATOM   9627  N  NZ    . LYS B 1 508 ? 125.042 173.799 165.384 1.00 38.05 1  508 LYS B NZ    1 
ATOM   9628  N  N     . GLU B 1 509 ? 128.758 170.787 160.050 1.00 34.40 ?  509 GLU B N     1 
ATOM   9629  C  CA    . GLU B 1 509 ? 130.168 171.161 160.048 1.00 35.15 ?  509 GLU B CA    1 
ATOM   9630  C  C     . GLU B 1 509 ? 130.714 171.309 158.633 1.00 36.28 ?  509 GLU B C     1 
ATOM   9631  O  O     . GLU B 1 509 ? 131.672 172.059 158.418 1.00 39.64 ?  509 GLU B O     1 
ATOM   9632  C  CB    . GLU B 1 509 ? 130.981 170.133 160.839 1.00 35.08 ?  509 GLU B CB    1 
ATOM   9633  C  CG    . GLU B 1 509 ? 131.682 169.084 159.993 1.00 32.91 ?  509 GLU B CG    1 
ATOM   9634  C  CD    . GLU B 1 509 ? 132.056 167.848 160.789 1.00 41.57 ?  509 GLU B CD    1 
ATOM   9635  O  OE1   . GLU B 1 509 ? 131.930 167.878 162.032 1.00 40.77 ?  509 GLU B OE1   1 
ATOM   9636  O  OE2   . GLU B 1 509 ? 132.473 166.846 160.172 1.00 40.46 -1 509 GLU B OE2   1 
ATOM   9637  N  N     . LYS B 1 510 ? 130.125 170.612 157.662 1.00 32.33 ?  510 LYS B N     1 
ATOM   9638  C  CA    . LYS B 1 510 ? 130.547 170.721 156.273 1.00 31.26 ?  510 LYS B CA    1 
ATOM   9639  C  C     . LYS B 1 510 ? 129.649 171.630 155.447 1.00 35.37 ?  510 LYS B C     1 
ATOM   9640  O  O     . LYS B 1 510 ? 129.997 171.941 154.303 1.00 39.87 ?  510 LYS B O     1 
ATOM   9641  C  CB    . LYS B 1 510 ? 130.600 169.331 155.626 1.00 30.84 ?  510 LYS B CB    1 
ATOM   9642  C  CG    . LYS B 1 510 ? 131.484 168.345 156.364 1.00 32.21 ?  510 LYS B CG    1 
ATOM   9643  C  CD    . LYS B 1 510 ? 131.812 167.140 155.504 1.00 31.73 ?  510 LYS B CD    1 
ATOM   9644  C  CE    . LYS B 1 510 ? 132.795 166.218 156.206 1.00 33.69 ?  510 LYS B CE    1 
ATOM   9645  N  NZ    . LYS B 1 510 ? 133.742 165.586 155.248 1.00 32.53 1  510 LYS B NZ    1 
ATOM   9646  N  N     . GLY B 1 511 ? 128.513 172.060 155.992 1.00 32.71 ?  511 GLY B N     1 
ATOM   9647  C  CA    . GLY B 1 511 ? 127.607 172.920 155.261 1.00 32.43 ?  511 GLY B CA    1 
ATOM   9648  C  C     . GLY B 1 511 ? 126.931 172.278 154.073 1.00 36.03 ?  511 GLY B C     1 
ATOM   9649  O  O     . GLY B 1 511 ? 126.340 172.991 153.257 1.00 39.42 ?  511 GLY B O     1 
ATOM   9650  N  N     . GLU B 1 512 ? 126.998 170.955 153.947 1.00 33.04 ?  512 GLU B N     1 
ATOM   9651  C  CA    . GLU B 1 512 ? 126.421 170.249 152.814 1.00 29.38 ?  512 GLU B CA    1 
ATOM   9652  C  C     . GLU B 1 512 ? 125.675 169.014 153.293 1.00 31.47 ?  512 GLU B C     1 
ATOM   9653  O  O     . GLU B 1 512 ? 126.098 168.348 154.242 1.00 32.91 ?  512 GLU B O     1 
ATOM   9654  C  CB    . GLU B 1 512 ? 127.501 169.844 151.800 1.00 31.29 ?  512 GLU B CB    1 
ATOM   9655  C  CG    . GLU B 1 512 ? 128.661 169.070 152.400 1.00 31.45 ?  512 GLU B CG    1 
ATOM   9656  C  CD    . GLU B 1 512 ? 129.368 168.198 151.381 1.00 36.04 ?  512 GLU B CD    1 
ATOM   9657  O  OE1   . GLU B 1 512 ? 128.695 167.699 150.456 1.00 32.30 ?  512 GLU B OE1   1 
ATOM   9658  O  OE2   . GLU B 1 512 ? 130.597 168.010 151.505 1.00 36.73 -1 512 GLU B OE2   1 
ATOM   9659  N  N     . THR B 1 513 ? 124.562 168.721 152.634 1.00 31.96 ?  513 THR B N     1 
ATOM   9660  C  CA    . THR B 1 513 ? 123.787 167.510 152.847 1.00 26.26 ?  513 THR B CA    1 
ATOM   9661  C  C     . THR B 1 513 ? 123.979 166.580 151.654 1.00 27.02 ?  513 THR B C     1 
ATOM   9662  O  O     . THR B 1 513 ? 124.694 166.897 150.700 1.00 34.08 ?  513 THR B O     1 
ATOM   9663  C  CB    . THR B 1 513 ? 122.309 167.847 153.055 1.00 27.27 ?  513 THR B CB    1 
ATOM   9664  O  OG1   . THR B 1 513 ? 121.783 168.446 151.865 1.00 29.20 ?  513 THR B OG1   1 
ATOM   9665  C  CG2   . THR B 1 513 ? 122.145 168.816 154.212 1.00 24.46 ?  513 THR B CG2   1 
ATOM   9666  N  N     . PHE B 1 514 ? 123.335 165.418 151.709 1.00 21.67 ?  514 PHE B N     1 
ATOM   9667  C  CA    . PHE B 1 514 ? 123.376 164.546 150.549 1.00 22.78 ?  514 PHE B CA    1 
ATOM   9668  C  C     . PHE B 1 514 ? 122.445 165.078 149.465 1.00 22.05 ?  514 PHE B C     1 
ATOM   9669  O  O     . PHE B 1 514 ? 121.517 165.846 149.730 1.00 26.25 ?  514 PHE B O     1 
ATOM   9670  C  CB    . PHE B 1 514 ? 123.016 163.104 150.923 1.00 19.13 ?  514 PHE B CB    1 
ATOM   9671  C  CG    . PHE B 1 514 ? 121.604 162.920 151.408 1.00 19.25 ?  514 PHE B CG    1 
ATOM   9672  C  CD1   . PHE B 1 514 ? 121.293 163.061 152.748 1.00 17.52 ?  514 PHE B CD1   1 
ATOM   9673  C  CD2   . PHE B 1 514 ? 120.594 162.571 150.525 1.00 19.76 ?  514 PHE B CD2   1 
ATOM   9674  C  CE1   . PHE B 1 514 ? 120.002 162.876 153.196 1.00 20.16 ?  514 PHE B CE1   1 
ATOM   9675  C  CE2   . PHE B 1 514 ? 119.302 162.386 150.968 1.00 14.93 ?  514 PHE B CE2   1 
ATOM   9676  C  CZ    . PHE B 1 514 ? 119.005 162.539 152.306 1.00 21.93 ?  514 PHE B CZ    1 
ATOM   9677  N  N     . ASP B 1 515 ? 122.715 164.672 148.228 1.00 25.10 ?  515 ASP B N     1 
ATOM   9678  C  CA    . ASP B 1 515 ? 121.969 165.198 147.095 1.00 26.53 ?  515 ASP B CA    1 
ATOM   9679  C  C     . ASP B 1 515 ? 120.494 164.839 147.204 1.00 31.04 ?  515 ASP B C     1 
ATOM   9680  O  O     . ASP B 1 515 ? 120.134 163.714 147.564 1.00 40.44 ?  515 ASP B O     1 
ATOM   9681  C  CB    . ASP B 1 515 ? 122.546 164.664 145.786 1.00 29.27 ?  515 ASP B CB    1 
ATOM   9682  C  CG    . ASP B 1 515 ? 123.664 165.533 145.247 1.00 33.63 ?  515 ASP B CG    1 
ATOM   9683  O  OD1   . ASP B 1 515 ? 124.208 166.350 146.019 1.00 32.53 ?  515 ASP B OD1   1 
ATOM   9684  O  OD2   . ASP B 1 515 ? 123.999 165.400 144.052 1.00 38.46 -1 515 ASP B OD2   1 
ATOM   9685  N  N     . GLN B 1 516 ? 119.639 165.816 146.895 1.00 28.92 ?  516 GLN B N     1 
ATOM   9686  C  CA    . GLN B 1 516 ? 118.186 165.665 146.956 1.00 26.49 ?  516 GLN B CA    1 
ATOM   9687  C  C     . GLN B 1 516 ? 117.706 165.338 148.367 1.00 27.05 ?  516 GLN B C     1 
ATOM   9688  O  O     . GLN B 1 516 ? 116.718 164.624 148.546 1.00 32.99 ?  516 GLN B O     1 
ATOM   9689  C  CB    . GLN B 1 516 ? 117.692 164.604 145.969 1.00 26.22 ?  516 GLN B CB    1 
ATOM   9690  C  CG    . GLN B 1 516 ? 118.054 164.870 144.521 1.00 29.62 ?  516 GLN B CG    1 
ATOM   9691  C  CD    . GLN B 1 516 ? 117.763 163.682 143.628 1.00 32.34 ?  516 GLN B CD    1 
ATOM   9692  O  OE1   . GLN B 1 516 ? 116.607 163.393 143.319 1.00 29.80 ?  516 GLN B OE1   1 
ATOM   9693  N  NE2   . GLN B 1 516 ? 118.812 162.984 143.210 1.00 32.48 ?  516 GLN B NE2   1 
ATOM   9694  N  N     . TYR B 1 517 ? 118.398 165.854 149.385 1.00 24.80 ?  517 TYR B N     1 
ATOM   9695  C  CA    . TYR B 1 517 ? 117.943 165.643 150.754 1.00 22.80 ?  517 TYR B CA    1 
ATOM   9696  C  C     . TYR B 1 517 ? 116.634 166.372 151.028 1.00 29.59 ?  517 TYR B C     1 
ATOM   9697  O  O     . TYR B 1 517 ? 115.839 165.925 151.863 1.00 35.82 ?  517 TYR B O     1 
ATOM   9698  C  CB    . TYR B 1 517 ? 119.016 166.090 151.748 1.00 18.52 ?  517 TYR B CB    1 
ATOM   9699  C  CG    . TYR B 1 517 ? 118.456 166.579 153.066 1.00 28.00 ?  517 TYR B CG    1 
ATOM   9700  C  CD1   . TYR B 1 517 ? 118.098 165.684 154.066 1.00 23.79 ?  517 TYR B CD1   1 
ATOM   9701  C  CD2   . TYR B 1 517 ? 118.276 167.936 153.306 1.00 29.52 ?  517 TYR B CD2   1 
ATOM   9702  C  CE1   . TYR B 1 517 ? 117.579 166.125 155.266 1.00 27.50 ?  517 TYR B CE1   1 
ATOM   9703  C  CE2   . TYR B 1 517 ? 117.757 168.384 154.501 1.00 24.93 ?  517 TYR B CE2   1 
ATOM   9704  C  CZ    . TYR B 1 517 ? 117.409 167.475 155.477 1.00 27.75 ?  517 TYR B CZ    1 
ATOM   9705  O  OH    . TYR B 1 517 ? 116.894 167.922 156.671 1.00 36.93 ?  517 TYR B OH    1 
ATOM   9706  N  N     . GLU B 1 518 ? 116.388 167.485 150.333 1.00 28.16 ?  518 GLU B N     1 
ATOM   9707  C  CA    . GLU B 1 518 ? 115.239 168.329 150.642 1.00 30.08 ?  518 GLU B CA    1 
ATOM   9708  C  C     . GLU B 1 518 ? 113.919 167.601 150.421 1.00 34.42 ?  518 GLU B C     1 
ATOM   9709  O  O     . GLU B 1 518 ? 112.937 167.879 151.120 1.00 35.10 ?  518 GLU B O     1 
ATOM   9710  C  CB    . GLU B 1 518 ? 115.284 169.608 149.806 1.00 29.58 ?  518 GLU B CB    1 
ATOM   9711  C  CG    . GLU B 1 518 ? 116.495 170.495 150.070 1.00 34.09 ?  518 GLU B CG    1 
ATOM   9712  C  CD    . GLU B 1 518 ? 117.755 169.994 149.386 1.00 41.01 ?  518 GLU B CD    1 
ATOM   9713  O  OE1   . GLU B 1 518 ? 117.642 169.390 148.299 1.00 38.63 ?  518 GLU B OE1   1 
ATOM   9714  O  OE2   . GLU B 1 518 ? 118.857 170.204 149.937 1.00 38.53 -1 518 GLU B OE2   1 
ATOM   9715  N  N     . GLY B 1 519 ? 113.869 166.681 149.465 1.00 23.98 ?  519 GLY B N     1 
ATOM   9716  C  CA    . GLY B 1 519 ? 112.681 165.891 149.232 1.00 20.26 ?  519 GLY B CA    1 
ATOM   9717  C  C     . GLY B 1 519 ? 112.545 164.663 150.098 1.00 19.74 ?  519 GLY B C     1 
ATOM   9718  O  O     . GLY B 1 519 ? 111.522 163.975 150.026 1.00 28.28 ?  519 GLY B O     1 
ATOM   9719  N  N     . SER B 1 520 ? 113.545 164.365 150.921 1.00 21.17 ?  520 SER B N     1 
ATOM   9720  C  CA    . SER B 1 520 ? 113.528 163.170 151.747 1.00 22.77 ?  520 SER B CA    1 
ATOM   9721  C  C     . SER B 1 520 ? 112.617 163.357 152.956 1.00 22.36 ?  520 SER B C     1 
ATOM   9722  O  O     . SER B 1 520 ? 112.233 164.473 153.317 1.00 24.18 ?  520 SER B O     1 
ATOM   9723  C  CB    . SER B 1 520 ? 114.941 162.815 152.208 1.00 18.69 ?  520 SER B CB    1 
ATOM   9724  O  OG    . SER B 1 520 ? 115.483 163.837 153.023 1.00 23.96 ?  520 SER B OG    1 
ATOM   9725  N  N     . THR B 1 521 ? 112.266 162.231 153.583 1.00 21.97 ?  521 THR B N     1 
ATOM   9726  C  CA    . THR B 1 521 ? 111.458 162.277 154.794 1.00 18.95 ?  521 THR B CA    1 
ATOM   9727  C  C     . THR B 1 521 ? 112.235 162.828 155.981 1.00 25.21 ?  521 THR B C     1 
ATOM   9728  O  O     . THR B 1 521 ? 111.621 163.218 156.979 1.00 26.86 ?  521 THR B O     1 
ATOM   9729  C  CB    . THR B 1 521 ? 110.918 160.885 155.122 1.00 24.09 ?  521 THR B CB    1 
ATOM   9730  O  OG1   . THR B 1 521 ? 111.980 160.059 155.614 1.00 29.44 ?  521 THR B OG1   1 
ATOM   9731  C  CG2   . THR B 1 521 ? 110.322 160.243 153.883 1.00 15.63 ?  521 THR B CG2   1 
ATOM   9732  N  N     . TYR B 1 522 ? 113.567 162.859 155.901 1.00 25.01 ?  522 TYR B N     1 
ATOM   9733  C  CA    . TYR B 1 522 ? 114.352 163.534 156.929 1.00 20.83 ?  522 TYR B CA    1 
ATOM   9734  C  C     . TYR B 1 522 ? 114.092 165.034 156.917 1.00 25.33 ?  522 TYR B C     1 
ATOM   9735  O  O     . TYR B 1 522 ? 113.966 165.659 157.976 1.00 24.25 ?  522 TYR B O     1 
ATOM   9736  C  CB    . TYR B 1 522 ? 115.841 163.254 156.729 1.00 18.01 ?  522 TYR B CB    1 
ATOM   9737  C  CG    . TYR B 1 522 ? 116.240 161.808 156.902 1.00 24.21 ?  522 TYR B CG    1 
ATOM   9738  C  CD1   . TYR B 1 522 ? 116.132 161.178 158.134 1.00 24.70 ?  522 TYR B CD1   1 
ATOM   9739  C  CD2   . TYR B 1 522 ? 116.743 161.077 155.835 1.00 22.12 ?  522 TYR B CD2   1 
ATOM   9740  C  CE1   . TYR B 1 522 ? 116.504 159.859 158.294 1.00 24.61 ?  522 TYR B CE1   1 
ATOM   9741  C  CE2   . TYR B 1 522 ? 117.118 159.759 155.987 1.00 20.99 ?  522 TYR B CE2   1 
ATOM   9742  C  CZ    . TYR B 1 522 ? 116.995 159.155 157.218 1.00 22.49 ?  522 TYR B CZ    1 
ATOM   9743  O  OH    . TYR B 1 522 ? 117.366 157.840 157.371 1.00 28.05 ?  522 TYR B OH    1 
ATOM   9744  N  N     . ALA B 1 523 ? 114.011 165.628 155.724 1.00 27.79 ?  523 ALA B N     1 
ATOM   9745  C  CA    . ALA B 1 523 ? 113.802 167.068 155.619 1.00 30.41 ?  523 ALA B CA    1 
ATOM   9746  C  C     . ALA B 1 523 ? 112.384 167.456 156.016 1.00 29.48 ?  523 ALA B C     1 
ATOM   9747  O  O     . ALA B 1 523 ? 112.176 168.486 156.668 1.00 28.29 ?  523 ALA B O     1 
ATOM   9748  C  CB    . ALA B 1 523 ? 114.110 167.539 154.200 1.00 27.66 ?  523 ALA B CB    1 
ATOM   9749  N  N     . THR B 1 524 ? 111.397 166.648 155.631 1.00 26.48 ?  524 THR B N     1 
ATOM   9750  C  CA    . THR B 1 524 ? 110.006 166.946 155.936 1.00 27.99 ?  524 THR B CA    1 
ATOM   9751  C  C     . THR B 1 524 ? 109.616 166.585 157.364 1.00 33.26 ?  524 THR B C     1 
ATOM   9752  O  O     . THR B 1 524 ? 108.533 166.979 157.809 1.00 38.05 ?  524 THR B O     1 
ATOM   9753  C  CB    . THR B 1 524 ? 109.082 166.213 154.959 1.00 28.49 ?  524 THR B CB    1 
ATOM   9754  O  OG1   . THR B 1 524 ? 109.140 164.804 155.208 1.00 32.57 ?  524 THR B OG1   1 
ATOM   9755  C  CG2   . THR B 1 524 ? 109.501 166.488 153.524 1.00 27.48 ?  524 THR B CG2   1 
ATOM   9756  N  N     . GLY B 1 525 ? 110.462 165.855 158.087 1.00 25.50 ?  525 GLY B N     1 
ATOM   9757  C  CA    . GLY B 1 525 ? 110.163 165.452 159.443 1.00 23.63 ?  525 GLY B CA    1 
ATOM   9758  C  C     . GLY B 1 525 ? 109.298 164.220 159.571 1.00 26.91 ?  525 GLY B C     1 
ATOM   9759  O  O     . GLY B 1 525 ? 109.012 163.800 160.699 1.00 31.03 ?  525 GLY B O     1 
ATOM   9760  N  N     . GLU B 1 526 ? 108.871 163.626 158.454 1.00 31.40 ?  526 GLU B N     1 
ATOM   9761  C  CA    . GLU B 1 526 ? 108.037 162.430 158.520 1.00 30.90 ?  526 GLU B CA    1 
ATOM   9762  C  C     . GLU B 1 526 ? 108.801 161.257 159.122 1.00 31.91 ?  526 GLU B C     1 
ATOM   9763  O  O     . GLU B 1 526 ? 108.232 160.458 159.877 1.00 36.63 ?  526 GLU B O     1 
ATOM   9764  C  CB    . GLU B 1 526 ? 107.519 162.085 157.123 1.00 29.22 ?  526 GLU B CB    1 
ATOM   9765  C  CG    . GLU B 1 526 ? 106.918 160.696 156.995 1.00 33.58 ?  526 GLU B CG    1 
ATOM   9766  C  CD    . GLU B 1 526 ? 106.790 160.250 155.553 1.00 39.33 ?  526 GLU B CD    1 
ATOM   9767  O  OE1   . GLU B 1 526 ? 106.418 161.084 154.701 1.00 39.85 ?  526 GLU B OE1   1 
ATOM   9768  O  OE2   . GLU B 1 526 ? 107.065 159.065 155.269 1.00 35.42 -1 526 GLU B OE2   1 
ATOM   9769  N  N     . TYR B 1 527 ? 110.097 161.150 158.812 1.00 33.11 ?  527 TYR B N     1 
ATOM   9770  C  CA    . TYR B 1 527 ? 110.901 160.029 159.290 1.00 22.71 ?  527 TYR B CA    1 
ATOM   9771  C  C     . TYR B 1 527 ? 110.864 159.915 160.808 1.00 25.58 ?  527 TYR B C     1 
ATOM   9772  O  O     . TYR B 1 527 ? 110.896 158.809 161.358 1.00 30.15 ?  527 TYR B O     1 
ATOM   9773  C  CB    . TYR B 1 527 ? 112.345 160.182 158.809 1.00 18.10 ?  527 TYR B CB    1 
ATOM   9774  C  CG    . TYR B 1 527 ? 113.259 159.064 159.254 1.00 26.66 ?  527 TYR B CG    1 
ATOM   9775  C  CD1   . TYR B 1 527 ? 113.401 157.917 158.487 1.00 26.45 ?  527 TYR B CD1   1 
ATOM   9776  C  CD2   . TYR B 1 527 ? 113.974 159.151 160.441 1.00 24.18 ?  527 TYR B CD2   1 
ATOM   9777  C  CE1   . TYR B 1 527 ? 114.230 156.892 158.885 1.00 23.64 ?  527 TYR B CE1   1 
ATOM   9778  C  CE2   . TYR B 1 527 ? 114.802 158.128 160.849 1.00 19.65 ?  527 TYR B CE2   1 
ATOM   9779  C  CZ    . TYR B 1 527 ? 114.928 157.003 160.066 1.00 20.98 ?  527 TYR B CZ    1 
ATOM   9780  O  OH    . TYR B 1 527 ? 115.756 155.980 160.467 1.00 30.81 ?  527 TYR B OH    1 
ATOM   9781  N  N     . PHE B 1 528 ? 110.798 161.047 161.500 1.00 29.04 ?  528 PHE B N     1 
ATOM   9782  C  CA    . PHE B 1 528 ? 110.835 161.075 162.954 1.00 26.61 ?  528 PHE B CA    1 
ATOM   9783  C  C     . PHE B 1 528 ? 109.470 160.863 163.592 1.00 33.94 ?  528 PHE B C     1 
ATOM   9784  O  O     . PHE B 1 528 ? 109.373 160.899 164.822 1.00 38.82 ?  528 PHE B O     1 
ATOM   9785  C  CB    . PHE B 1 528 ? 111.422 162.405 163.437 1.00 27.80 ?  528 PHE B CB    1 
ATOM   9786  C  CG    . PHE B 1 528 ? 112.775 162.714 162.865 1.00 29.99 ?  528 PHE B CG    1 
ATOM   9787  C  CD1   . PHE B 1 528 ? 113.925 162.282 163.500 1.00 26.60 ?  528 PHE B CD1   1 
ATOM   9788  C  CD2   . PHE B 1 528 ? 112.896 163.441 161.692 1.00 25.41 ?  528 PHE B CD2   1 
ATOM   9789  C  CE1   . PHE B 1 528 ? 115.170 162.565 162.977 1.00 28.91 ?  528 PHE B CE1   1 
ATOM   9790  C  CE2   . PHE B 1 528 ? 114.138 163.727 161.165 1.00 27.68 ?  528 PHE B CE2   1 
ATOM   9791  C  CZ    . PHE B 1 528 ? 115.276 163.288 161.807 1.00 27.60 ?  528 PHE B CZ    1 
ATOM   9792  N  N     . ASP B 1 529 ? 108.424 160.640 162.791 1.00 31.57 ?  529 ASP B N     1 
ATOM   9793  C  CA    . ASP B 1 529 ? 107.068 160.533 163.324 1.00 31.29 ?  529 ASP B CA    1 
ATOM   9794  C  C     . ASP B 1 529 ? 106.986 159.500 164.444 1.00 32.79 ?  529 ASP B C     1 
ATOM   9795  O  O     . ASP B 1 529 ? 106.690 159.834 165.598 1.00 37.04 ?  529 ASP B O     1 
ATOM   9796  C  CB    . ASP B 1 529 ? 106.096 160.181 162.197 1.00 31.85 ?  529 ASP B CB    1 
ATOM   9797  C  CG    . ASP B 1 529 ? 105.704 161.389 161.371 1.00 33.93 ?  529 ASP B CG    1 
ATOM   9798  O  OD1   . ASP B 1 529 ? 106.078 162.517 161.752 1.00 36.54 ?  529 ASP B OD1   1 
ATOM   9799  O  OD2   . ASP B 1 529 ? 105.024 161.208 160.339 1.00 36.46 -1 529 ASP B OD2   1 
ATOM   9800  N  N     . LYS B 1 530 ? 107.285 158.238 164.125 1.00 34.54 ?  530 LYS B N     1 
ATOM   9801  C  CA    . LYS B 1 530 ? 107.224 157.185 165.131 1.00 34.43 ?  530 LYS B CA    1 
ATOM   9802  C  C     . LYS B 1 530 ? 108.196 157.428 166.276 1.00 36.06 ?  530 LYS B C     1 
ATOM   9803  O  O     . LYS B 1 530 ? 108.025 156.851 167.354 1.00 36.80 ?  530 LYS B O     1 
ATOM   9804  C  CB    . LYS B 1 530 ? 107.508 155.825 164.492 1.00 33.22 ?  530 LYS B CB    1 
ATOM   9805  C  CG    . LYS B 1 530 ? 108.962 155.395 164.572 1.00 31.06 ?  530 LYS B CG    1 
ATOM   9806  C  CD    . LYS B 1 530 ? 109.261 154.264 163.612 1.00 32.94 ?  530 LYS B CD    1 
ATOM   9807  C  CE    . LYS B 1 530 ? 110.684 153.778 163.778 1.00 31.12 ?  530 LYS B CE    1 
ATOM   9808  N  NZ    . LYS B 1 530 ? 111.391 153.691 162.471 1.00 37.43 1  530 LYS B NZ    1 
ATOM   9809  N  N     . TYR B 1 531 ? 109.208 158.268 166.070 1.00 35.29 ?  531 TYR B N     1 
ATOM   9810  C  CA    . TYR B 1 531 ? 110.160 158.573 167.124 1.00 28.42 ?  531 TYR B CA    1 
ATOM   9811  C  C     . TYR B 1 531 ? 109.727 159.738 167.998 1.00 29.68 ?  531 TYR B C     1 
ATOM   9812  O  O     . TYR B 1 531 ? 110.251 159.887 169.108 1.00 33.16 ?  531 TYR B O     1 
ATOM   9813  C  CB    . TYR B 1 531 ? 111.533 158.869 166.519 1.00 27.04 ?  531 TYR B CB    1 
ATOM   9814  C  CG    . TYR B 1 531 ? 112.254 157.638 166.023 1.00 28.11 ?  531 TYR B CG    1 
ATOM   9815  C  CD1   . TYR B 1 531 ? 112.510 156.573 166.873 1.00 25.95 ?  531 TYR B CD1   1 
ATOM   9816  C  CD2   . TYR B 1 531 ? 112.677 157.542 164.705 1.00 27.49 ?  531 TYR B CD2   1 
ATOM   9817  C  CE1   . TYR B 1 531 ? 113.170 155.447 166.428 1.00 28.69 ?  531 TYR B CE1   1 
ATOM   9818  C  CE2   . TYR B 1 531 ? 113.338 156.419 164.250 1.00 23.66 ?  531 TYR B CE2   1 
ATOM   9819  C  CZ    . TYR B 1 531 ? 113.581 155.375 165.115 1.00 28.29 ?  531 TYR B CZ    1 
ATOM   9820  O  OH    . TYR B 1 531 ? 114.237 154.254 164.667 1.00 32.32 ?  531 TYR B OH    1 
ATOM   9821  N  N     . VAL B 1 532 ? 108.784 160.564 167.536 1.00 33.72 ?  532 VAL B N     1 
ATOM   9822  C  CA    . VAL B 1 532 ? 108.297 161.682 168.336 1.00 31.71 ?  532 VAL B CA    1 
ATOM   9823  C  C     . VAL B 1 532 ? 106.942 161.397 168.962 1.00 34.87 ?  532 VAL B C     1 
ATOM   9824  O  O     . VAL B 1 532 ? 106.354 162.295 169.581 1.00 40.13 ?  532 VAL B O     1 
ATOM   9825  C  CB    . VAL B 1 532 ? 108.239 162.981 167.505 1.00 34.38 ?  532 VAL B CB    1 
ATOM   9826  C  CG1   . VAL B 1 532 ? 109.618 163.336 166.976 1.00 32.64 ?  532 VAL B CG1   1 
ATOM   9827  C  CG2   . VAL B 1 532 ? 107.239 162.851 166.368 1.00 34.61 ?  532 VAL B CG2   1 
ATOM   9828  N  N     . SER B 1 533 ? 106.429 160.176 168.824 1.00 40.20 ?  533 SER B N     1 
ATOM   9829  C  CA    . SER B 1 533 ? 105.127 159.825 169.376 1.00 39.75 ?  533 SER B CA    1 
ATOM   9830  C  C     . SER B 1 533 ? 105.208 158.542 170.191 1.00 40.09 ?  533 SER B C     1 
ATOM   9831  O  O     . SER B 1 533 ? 104.401 158.326 171.102 1.00 44.55 ?  533 SER B O     1 
ATOM   9832  C  CB    . SER B 1 533 ? 104.098 159.679 168.254 1.00 41.09 ?  533 SER B CB    1 
ATOM   9833  O  OG    . SER B 1 533 ? 104.339 158.507 167.495 1.00 42.45 ?  533 SER B OG    1 
ATOM   9834  N  N     . THR B 1 534 ? 106.174 157.686 169.873 1.00 39.24 ?  534 THR B N     1 
ATOM   9835  C  CA    . THR B 1 534 ? 106.350 156.408 170.547 1.00 38.89 ?  534 THR B CA    1 
ATOM   9836  C  C     . THR B 1 534 ? 107.651 156.411 171.336 1.00 37.46 ?  534 THR B C     1 
ATOM   9837  O  O     . THR B 1 534 ? 108.686 156.871 170.844 1.00 43.15 ?  534 THR B O     1 
ATOM   9838  C  CB    . THR B 1 534 ? 106.352 155.249 169.546 1.00 39.21 ?  534 THR B CB    1 
ATOM   9839  O  OG1   . THR B 1 534 ? 105.225 155.371 168.668 1.00 40.92 ?  534 THR B OG1   1 
ATOM   9840  C  CG2   . THR B 1 534 ? 106.284 153.912 170.268 1.00 40.55 ?  534 THR B CG2   1 
ATOM   9841  N  N     . ASP B 1 535 ? 107.590 155.896 172.560 1.00 42.63 ?  535 ASP B N     1 
ATOM   9842  C  CA    . ASP B 1 535 ? 108.761 155.788 173.418 1.00 41.49 ?  535 ASP B CA    1 
ATOM   9843  C  C     . ASP B 1 535 ? 109.377 154.404 173.268 1.00 41.07 ?  535 ASP B C     1 
ATOM   9844  O  O     . ASP B 1 535 ? 108.679 153.391 173.383 1.00 42.97 ?  535 ASP B O     1 
ATOM   9845  C  CB    . ASP B 1 535 ? 108.382 156.051 174.876 1.00 38.42 ?  535 ASP B CB    1 
ATOM   9846  C  CG    . ASP B 1 535 ? 109.525 155.788 175.831 1.00 44.29 ?  535 ASP B CG    1 
ATOM   9847  O  OD1   . ASP B 1 535 ? 110.360 156.695 176.029 1.00 47.58 ?  535 ASP B OD1   1 
ATOM   9848  O  OD2   . ASP B 1 535 ? 109.583 154.672 176.387 1.00 46.27 -1 535 ASP B OD2   1 
ATOM   9849  N  N     . PHE B 1 536 ? 110.684 154.364 173.010 1.00 32.24 ?  536 PHE B N     1 
ATOM   9850  C  CA    . PHE B 1 536 ? 111.397 153.115 172.787 1.00 32.66 ?  536 PHE B CA    1 
ATOM   9851  C  C     . PHE B 1 536 ? 112.309 152.754 173.954 1.00 33.90 ?  536 PHE B C     1 
ATOM   9852  O  O     . PHE B 1 536 ? 113.261 151.986 173.780 1.00 35.05 ?  536 PHE B O     1 
ATOM   9853  C  CB    . PHE B 1 536 ? 112.192 153.186 171.483 1.00 29.99 ?  536 PHE B CB    1 
ATOM   9854  C  CG    . PHE B 1 536 ? 111.331 153.313 170.260 1.00 27.01 ?  536 PHE B CG    1 
ATOM   9855  C  CD1   . PHE B 1 536 ? 110.871 152.187 169.600 1.00 28.60 ?  536 PHE B CD1   1 
ATOM   9856  C  CD2   . PHE B 1 536 ? 110.972 154.559 169.775 1.00 30.83 ?  536 PHE B CD2   1 
ATOM   9857  C  CE1   . PHE B 1 536 ? 110.076 152.299 168.477 1.00 30.63 ?  536 PHE B CE1   1 
ATOM   9858  C  CE2   . PHE B 1 536 ? 110.176 154.678 168.653 1.00 35.58 ?  536 PHE B CE2   1 
ATOM   9859  C  CZ    . PHE B 1 536 ? 109.729 153.547 168.003 1.00 32.38 ?  536 PHE B CZ    1 
ATOM   9860  N  N     . SER B 1 537 ? 112.037 153.294 175.138 1.00 35.74 ?  537 SER B N     1 
ATOM   9861  C  CA    . SER B 1 537 ? 112.759 152.881 176.327 1.00 33.49 ?  537 SER B CA    1 
ATOM   9862  C  C     . SER B 1 537 ? 112.384 151.445 176.684 1.00 37.92 ?  537 SER B C     1 
ATOM   9863  O  O     . SER B 1 537 ? 111.291 150.981 176.350 1.00 39.77 ?  537 SER B O     1 
ATOM   9864  C  CB    . SER B 1 537 ? 112.443 153.813 177.494 1.00 35.62 ?  537 SER B CB    1 
ATOM   9865  O  OG    . SER B 1 537 ? 112.719 155.161 177.157 1.00 41.80 ?  537 SER B OG    1 
ATOM   9866  N  N     . PRO B 1 538 ? 113.280 150.712 177.346 1.00 35.53 ?  538 PRO B N     1 
ATOM   9867  C  CA    . PRO B 1 538 ? 112.992 149.306 177.655 1.00 34.54 ?  538 PRO B CA    1 
ATOM   9868  C  C     . PRO B 1 538 ? 111.752 149.156 178.523 1.00 38.77 ?  538 PRO B C     1 
ATOM   9869  O  O     . PRO B 1 538 ? 111.537 149.911 179.474 1.00 41.83 ?  538 PRO B O     1 
ATOM   9870  C  CB    . PRO B 1 538 ? 114.254 148.840 178.391 1.00 36.06 ?  538 PRO B CB    1 
ATOM   9871  C  CG    . PRO B 1 538 ? 115.313 149.805 177.987 1.00 37.65 ?  538 PRO B CG    1 
ATOM   9872  C  CD    . PRO B 1 538 ? 114.616 151.113 177.814 1.00 35.67 ?  538 PRO B CD    1 
ATOM   9873  N  N     . LYS B 1 539 ? 110.935 148.160 178.184 1.00 41.02 ?  539 LYS B N     1 
ATOM   9874  C  CA    . LYS B 1 539 ? 109.735 147.844 178.945 1.00 41.05 ?  539 LYS B CA    1 
ATOM   9875  C  C     . LYS B 1 539 ? 109.987 146.843 180.063 1.00 44.29 ?  539 LYS B C     1 
ATOM   9876  O  O     . LYS B 1 539 ? 109.098 146.628 180.893 1.00 47.25 ?  539 LYS B O     1 
ATOM   9877  C  CB    . LYS B 1 539 ? 108.647 147.300 178.014 1.00 42.03 ?  539 LYS B CB    1 
ATOM   9878  C  CG    . LYS B 1 539 ? 108.609 147.967 176.651 1.00 42.44 ?  539 LYS B CG    1 
ATOM   9879  C  CD    . LYS B 1 539 ? 107.549 149.053 176.599 1.00 42.09 ?  539 LYS B CD    1 
ATOM   9880  C  CE    . LYS B 1 539 ? 107.495 149.705 175.228 1.00 44.54 ?  539 LYS B CE    1 
ATOM   9881  N  NZ    . LYS B 1 539 ? 108.854 150.064 174.732 1.00 45.96 1  539 LYS B NZ    1 
ATOM   9882  N  N     . TYR B 1 540 ? 111.167 146.232 180.104 1.00 42.27 ?  540 TYR B N     1 
ATOM   9883  C  CA    . TYR B 1 540 ? 111.521 145.258 181.124 1.00 39.72 ?  540 TYR B CA    1 
ATOM   9884  C  C     . TYR B 1 540 ? 112.605 145.831 182.025 1.00 46.19 ?  540 TYR B C     1 
ATOM   9885  O  O     . TYR B 1 540 ? 113.491 146.557 181.563 1.00 47.07 ?  540 TYR B O     1 
ATOM   9886  C  CB    . TYR B 1 540 ? 111.995 143.948 180.490 1.00 41.89 ?  540 TYR B CB    1 
ATOM   9887  C  CG    . TYR B 1 540 ? 110.913 143.217 179.729 1.00 45.05 ?  540 TYR B CG    1 
ATOM   9888  C  CD1   . TYR B 1 540 ? 110.675 143.491 178.388 1.00 42.64 ?  540 TYR B CD1   1 
ATOM   9889  C  CD2   . TYR B 1 540 ? 110.124 142.261 180.353 1.00 45.24 ?  540 TYR B CD2   1 
ATOM   9890  C  CE1   . TYR B 1 540 ? 109.684 142.828 177.689 1.00 42.42 ?  540 TYR B CE1   1 
ATOM   9891  C  CE2   . TYR B 1 540 ? 109.131 141.594 179.662 1.00 42.26 ?  540 TYR B CE2   1 
ATOM   9892  C  CZ    . TYR B 1 540 ? 108.916 141.880 178.332 1.00 43.92 ?  540 TYR B CZ    1 
ATOM   9893  O  OH    . TYR B 1 540 ? 107.927 141.217 177.643 1.00 46.28 ?  540 TYR B OH    1 
ATOM   9894  N  N     . GLU B 1 541 ? 112.524 145.506 183.317 1.00 49.66 ?  541 GLU B N     1 
ATOM   9895  C  CA    . GLU B 1 541 ? 113.481 146.043 184.278 1.00 45.98 ?  541 GLU B CA    1 
ATOM   9896  C  C     . GLU B 1 541 ? 114.892 145.542 183.997 1.00 46.37 ?  541 GLU B C     1 
ATOM   9897  O  O     . GLU B 1 541 ? 115.867 146.281 184.178 1.00 45.04 ?  541 GLU B O     1 
ATOM   9898  C  CB    . GLU B 1 541 ? 113.058 145.680 185.702 1.00 46.69 ?  541 GLU B CB    1 
ATOM   9899  C  CG    . GLU B 1 541 ? 113.796 146.457 186.778 1.00 48.66 ?  541 GLU B CG    1 
ATOM   9900  C  CD    . GLU B 1 541 ? 113.850 147.944 186.491 1.00 50.84 ?  541 GLU B CD    1 
ATOM   9901  O  OE1   . GLU B 1 541 ? 112.776 148.557 186.318 1.00 50.80 ?  541 GLU B OE1   1 
ATOM   9902  O  OE2   . GLU B 1 541 ? 114.967 148.501 186.433 1.00 52.89 -1 541 GLU B OE2   1 
ATOM   9903  N  N     . LYS B 1 542 ? 115.024 144.285 183.568 1.00 42.48 ?  542 LYS B N     1 
ATOM   9904  C  CA    . LYS B 1 542 ? 116.346 143.737 183.275 1.00 39.80 ?  542 LYS B CA    1 
ATOM   9905  C  C     . LYS B 1 542 ? 117.019 144.494 182.137 1.00 42.82 ?  542 LYS B C     1 
ATOM   9906  O  O     . LYS B 1 542 ? 118.212 144.813 182.211 1.00 44.21 ?  542 LYS B O     1 
ATOM   9907  C  CB    . LYS B 1 542 ? 116.231 142.250 182.940 1.00 38.45 ?  542 LYS B CB    1 
ATOM   9908  C  CG    . LYS B 1 542 ? 117.561 141.560 182.695 1.00 43.63 ?  542 LYS B CG    1 
ATOM   9909  C  CD    . LYS B 1 542 ? 117.373 140.070 182.473 1.00 42.93 ?  542 LYS B CD    1 
ATOM   9910  C  CE    . LYS B 1 542 ? 118.710 139.354 182.383 1.00 43.45 ?  542 LYS B CE    1 
ATOM   9911  N  NZ    . LYS B 1 542 ? 118.551 137.874 182.379 1.00 41.95 1  542 LYS B NZ    1 
ATOM   9912  N  N     . ILE B 1 543 ? 116.267 144.805 181.081 1.00 39.40 ?  543 ILE B N     1 
ATOM   9913  C  CA    . ILE B 1 543 ? 116.834 145.549 179.960 1.00 37.20 ?  543 ILE B CA    1 
ATOM   9914  C  C     . ILE B 1 543 ? 117.186 146.970 180.381 1.00 36.34 ?  543 ILE B C     1 
ATOM   9915  O  O     . ILE B 1 543 ? 118.223 147.513 179.979 1.00 39.33 ?  543 ILE B O     1 
ATOM   9916  C  CB    . ILE B 1 543 ? 115.861 145.530 178.768 1.00 36.93 ?  543 ILE B CB    1 
ATOM   9917  C  CG1   . ILE B 1 543 ? 115.425 144.096 178.457 1.00 36.34 ?  543 ILE B CG1   1 
ATOM   9918  C  CG2   . ILE B 1 543 ? 116.504 146.166 177.556 1.00 35.21 ?  543 ILE B CG2   1 
ATOM   9919  C  CD1   . ILE B 1 543 ? 116.577 143.138 178.233 1.00 34.56 ?  543 ILE B CD1   1 
ATOM   9920  N  N     . ALA B 1 544 ? 116.330 147.599 181.191 1.00 37.78 ?  544 ALA B N     1 
ATOM   9921  C  CA    . ALA B 1 544 ? 116.628 148.939 181.684 1.00 40.15 ?  544 ALA B CA    1 
ATOM   9922  C  C     . ALA B 1 544 ? 117.904 148.948 182.516 1.00 39.96 ?  544 ALA B C     1 
ATOM   9923  O  O     . ALA B 1 544 ? 118.718 149.872 182.409 1.00 42.67 ?  544 ALA B O     1 
ATOM   9924  C  CB    . ALA B 1 544 ? 115.450 149.473 182.499 1.00 41.98 ?  544 ALA B CB    1 
ATOM   9925  N  N     . ASN B 1 545 ? 118.094 147.926 183.354 1.00 43.77 ?  545 ASN B N     1 
ATOM   9926  C  CA    . ASN B 1 545 ? 119.341 147.799 184.099 1.00 47.64 ?  545 ASN B CA    1 
ATOM   9927  C  C     . ASN B 1 545 ? 120.521 147.590 183.159 1.00 45.05 ?  545 ASN B C     1 
ATOM   9928  O  O     . ASN B 1 545 ? 121.615 148.116 183.396 1.00 46.84 ?  545 ASN B O     1 
ATOM   9929  C  CB    . ASN B 1 545 ? 119.241 146.648 185.101 1.00 44.49 ?  545 ASN B CB    1 
ATOM   9930  C  CG    . ASN B 1 545 ? 118.227 146.916 186.192 1.00 47.52 ?  545 ASN B CG    1 
ATOM   9931  O  OD1   . ASN B 1 545 ? 117.896 148.066 186.479 1.00 49.39 ?  545 ASN B OD1   1 
ATOM   9932  N  ND2   . ASN B 1 545 ? 117.725 145.852 186.808 1.00 44.45 ?  545 ASN B ND2   1 
ATOM   9933  N  N     . LEU B 1 546 ? 120.321 146.809 182.095 1.00 38.60 ?  546 LEU B N     1 
ATOM   9934  C  CA    . LEU B 1 546 ? 121.360 146.646 181.085 1.00 39.55 ?  546 LEU B CA    1 
ATOM   9935  C  C     . LEU B 1 546 ? 121.747 147.980 180.461 1.00 39.47 ?  546 LEU B C     1 
ATOM   9936  O  O     . LEU B 1 546 ? 122.917 148.193 180.125 1.00 39.00 ?  546 LEU B O     1 
ATOM   9937  C  CB    . LEU B 1 546 ? 120.892 145.673 180.003 1.00 36.75 ?  546 LEU B CB    1 
ATOM   9938  C  CG    . LEU B 1 546 ? 121.067 144.183 180.289 1.00 39.09 ?  546 LEU B CG    1 
ATOM   9939  C  CD1   . LEU B 1 546 ? 120.984 143.391 178.999 1.00 37.33 ?  546 LEU B CD1   1 
ATOM   9940  C  CD2   . LEU B 1 546 ? 122.387 143.921 180.999 1.00 38.77 ?  546 LEU B CD2   1 
ATOM   9941  N  N     . PHE B 1 547 ? 120.786 148.887 180.305 1.00 40.07 ?  547 PHE B N     1 
ATOM   9942  C  CA    . PHE B 1 547 ? 121.034 150.198 179.722 1.00 37.64 ?  547 PHE B CA    1 
ATOM   9943  C  C     . PHE B 1 547 ? 121.373 151.261 180.760 1.00 39.81 ?  547 PHE B C     1 
ATOM   9944  O  O     . PHE B 1 547 ? 121.375 152.450 180.427 1.00 43.53 ?  547 PHE B O     1 
ATOM   9945  C  CB    . PHE B 1 547 ? 119.823 150.649 178.903 1.00 35.49 ?  547 PHE B CB    1 
ATOM   9946  C  CG    . PHE B 1 547 ? 119.744 150.024 177.544 1.00 36.65 ?  547 PHE B CG    1 
ATOM   9947  C  CD1   . PHE B 1 547 ? 120.529 150.493 176.507 1.00 35.91 ?  547 PHE B CD1   1 
ATOM   9948  C  CD2   . PHE B 1 547 ? 118.884 148.967 177.301 1.00 35.72 ?  547 PHE B CD2   1 
ATOM   9949  C  CE1   . PHE B 1 547 ? 120.458 149.922 175.254 1.00 34.64 ?  547 PHE B CE1   1 
ATOM   9950  C  CE2   . PHE B 1 547 ? 118.811 148.393 176.050 1.00 36.03 ?  547 PHE B CE2   1 
ATOM   9951  C  CZ    . PHE B 1 547 ? 119.600 148.869 175.026 1.00 35.01 ?  547 PHE B CZ    1 
ATOM   9952  N  N     . GLU B 1 548 ? 121.653 150.868 182.000 1.00 47.04 ?  548 GLU B N     1 
ATOM   9953  C  CA    . GLU B 1 548 ? 121.997 151.840 183.028 1.00 47.44 ?  548 GLU B CA    1 
ATOM   9954  C  C     . GLU B 1 548 ? 123.342 152.493 182.730 1.00 47.26 ?  548 GLU B C     1 
ATOM   9955  O  O     . GLU B 1 548 ? 124.234 151.888 182.129 1.00 50.56 ?  548 GLU B O     1 
ATOM   9956  C  CB    . GLU B 1 548 ? 122.032 151.181 184.407 1.00 46.82 ?  548 GLU B CB    1 
ATOM   9957  C  CG    . GLU B 1 548 ? 120.666 151.007 185.049 1.00 48.12 ?  548 GLU B CG    1 
ATOM   9958  C  CD    . GLU B 1 548 ? 119.936 152.323 185.258 1.00 50.79 ?  548 GLU B CD    1 
ATOM   9959  O  OE1   . GLU B 1 548 ? 120.605 153.370 185.387 1.00 48.80 ?  548 GLU B OE1   1 
ATOM   9960  O  OE2   . GLU B 1 548 ? 118.688 152.308 185.295 1.00 50.91 -1 548 GLU B OE2   1 
ATOM   9961  N  N     . GLY B 1 549 ? 123.478 153.744 183.160 1.00 45.31 ?  549 GLY B N     1 
ATOM   9962  C  CA    . GLY B 1 549 ? 124.654 154.529 182.863 1.00 44.97 ?  549 GLY B CA    1 
ATOM   9963  C  C     . GLY B 1 549 ? 124.665 155.153 181.488 1.00 46.10 ?  549 GLY B C     1 
ATOM   9964  O  O     . GLY B 1 549 ? 125.669 155.773 181.114 1.00 47.53 ?  549 GLY B O     1 
ATOM   9965  N  N     . MET B 1 550 ? 123.585 155.008 180.724 1.00 45.44 ?  550 MET B N     1 
ATOM   9966  C  CA    . MET B 1 550 ? 123.490 155.538 179.372 1.00 44.20 ?  550 MET B CA    1 
ATOM   9967  C  C     . MET B 1 550 ? 122.156 156.249 179.217 1.00 44.33 ?  550 MET B C     1 
ATOM   9968  O  O     . MET B 1 550 ? 121.121 155.731 179.648 1.00 46.15 ?  550 MET B O     1 
ATOM   9969  C  CB    . MET B 1 550 ? 123.623 154.417 178.337 1.00 43.15 ?  550 MET B CB    1 
ATOM   9970  C  CG    . MET B 1 550 ? 124.930 154.438 177.574 1.00 48.10 ?  550 MET B CG    1 
ATOM   9971  S  SD    . MET B 1 550 ? 124.903 153.341 176.149 1.00 54.89 ?  550 MET B SD    1 
ATOM   9972  C  CE    . MET B 1 550 ? 124.605 151.761 176.936 1.00 44.40 ?  550 MET B CE    1 
ATOM   9973  N  N     . HIS B 1 551 ? 122.179 157.429 178.603 1.00 40.63 ?  551 HIS B N     1 
ATOM   9974  C  CA    . HIS B 1 551 ? 120.972 158.232 178.437 1.00 40.60 ?  551 HIS B CA    1 
ATOM   9975  C  C     . HIS B 1 551 ? 120.177 157.713 177.245 1.00 40.33 ?  551 HIS B C     1 
ATOM   9976  O  O     . HIS B 1 551 ? 120.532 157.978 176.092 1.00 41.37 ?  551 HIS B O     1 
ATOM   9977  C  CB    . HIS B 1 551 ? 121.324 159.704 178.252 1.00 39.84 ?  551 HIS B CB    1 
ATOM   9978  C  CG    . HIS B 1 551 ? 120.175 160.539 177.783 1.00 41.55 ?  551 HIS B CG    1 
ATOM   9979  N  ND1   . HIS B 1 551 ? 119.086 160.820 178.578 1.00 44.88 ?  551 HIS B ND1   1 
ATOM   9980  C  CD2   . HIS B 1 551 ? 119.940 161.144 176.595 1.00 41.27 ?  551 HIS B CD2   1 
ATOM   9981  C  CE1   . HIS B 1 551 ? 118.231 161.566 177.903 1.00 43.33 ?  551 HIS B CE1   1 
ATOM   9982  N  NE2   . HIS B 1 551 ? 118.725 161.778 176.697 1.00 40.71 ?  551 HIS B NE2   1 
ATOM   9983  N  N     . ILE B 1 552 ? 119.097 156.990 177.520 1.00 35.98 ?  552 ILE B N     1 
ATOM   9984  C  CA    . ILE B 1 552 ? 118.218 156.474 176.475 1.00 32.38 ?  552 ILE B CA    1 
ATOM   9985  C  C     . ILE B 1 552 ? 117.396 157.632 175.921 1.00 33.83 ?  552 ILE B C     1 
ATOM   9986  O  O     . ILE B 1 552 ? 116.682 158.301 176.681 1.00 38.54 ?  552 ILE B O     1 
ATOM   9987  C  CB    . ILE B 1 552 ? 117.314 155.355 177.012 1.00 35.25 ?  552 ILE B CB    1 
ATOM   9988  C  CG1   . ILE B 1 552 ? 118.161 154.231 177.608 1.00 34.38 ?  552 ILE B CG1   1 
ATOM   9989  C  CG2   . ILE B 1 552 ? 116.415 154.822 175.911 1.00 35.00 ?  552 ILE B CG2   1 
ATOM   9990  C  CD1   . ILE B 1 552 ? 117.394 153.321 178.533 1.00 33.66 ?  552 ILE B CD1   1 
ATOM   9991  N  N     . PRO B 1 553 ? 117.472 157.912 174.620 1.00 37.53 ?  553 PRO B N     1 
ATOM   9992  C  CA    . PRO B 1 553 ? 116.714 159.039 174.064 1.00 34.70 ?  553 PRO B CA    1 
ATOM   9993  C  C     . PRO B 1 553 ? 115.214 158.838 174.222 1.00 35.12 ?  553 PRO B C     1 
ATOM   9994  O  O     . PRO B 1 553 ? 114.687 157.744 174.010 1.00 37.86 ?  553 PRO B O     1 
ATOM   9995  C  CB    . PRO B 1 553 ? 117.126 159.052 172.588 1.00 32.01 ?  553 PRO B CB    1 
ATOM   9996  C  CG    . PRO B 1 553 ? 118.422 158.312 172.543 1.00 30.36 ?  553 PRO B CG    1 
ATOM   9997  C  CD    . PRO B 1 553 ? 118.327 157.270 173.609 1.00 32.54 ?  553 PRO B CD    1 
ATOM   9998  N  N     . THR B 1 554 ? 114.530 159.911 174.595 1.00 39.81 ?  554 THR B N     1 
ATOM   9999  C  CA    . THR B 1 554 ? 113.088 159.913 174.747 1.00 38.48 ?  554 THR B CA    1 
ATOM   10000 C  C     . THR B 1 554 ? 112.455 160.629 173.557 1.00 36.43 ?  554 THR B C     1 
ATOM   10001 O  O     . THR B 1 554 ? 113.131 160.986 172.586 1.00 36.73 ?  554 THR B O     1 
ATOM   10002 C  CB    . THR B 1 554 ? 112.698 160.561 176.077 1.00 38.13 ?  554 THR B CB    1 
ATOM   10003 O  OG1   . THR B 1 554 ? 113.127 161.928 176.088 1.00 37.11 ?  554 THR B OG1   1 
ATOM   10004 C  CG2   . THR B 1 554 ? 113.348 159.823 177.238 1.00 36.24 ?  554 THR B CG2   1 
ATOM   10005 N  N     . THR B 1 555 ? 111.139 160.842 173.622 1.00 39.09 ?  555 THR B N     1 
ATOM   10006 C  CA    . THR B 1 555 ? 110.465 161.568 172.552 1.00 36.65 ?  555 THR B CA    1 
ATOM   10007 C  C     . THR B 1 555 ? 110.925 163.018 172.481 1.00 39.53 ?  555 THR B C     1 
ATOM   10008 O  O     . THR B 1 555 ? 110.928 163.610 171.396 1.00 40.35 ?  555 THR B O     1 
ATOM   10009 C  CB    . THR B 1 555 ? 108.948 161.505 172.739 1.00 38.95 ?  555 THR B CB    1 
ATOM   10010 O  OG1   . THR B 1 555 ? 108.604 161.997 174.040 1.00 44.10 ?  555 THR B OG1   1 
ATOM   10011 C  CG2   . THR B 1 555 ? 108.456 160.073 172.594 1.00 39.39 ?  555 THR B CG2   1 
ATOM   10012 N  N     . GLU B 1 556 ? 111.320 163.605 173.614 1.00 37.71 ?  556 GLU B N     1 
ATOM   10013 C  CA    . GLU B 1 556 ? 111.818 164.977 173.601 1.00 37.73 ?  556 GLU B CA    1 
ATOM   10014 C  C     . GLU B 1 556 ? 113.179 165.066 172.920 1.00 40.49 ?  556 GLU B C     1 
ATOM   10015 O  O     . GLU B 1 556 ? 113.429 165.992 172.137 1.00 41.86 ?  556 GLU B O     1 
ATOM   10016 C  CB    . GLU B 1 556 ? 111.896 165.519 175.027 1.00 39.97 ?  556 GLU B CB    1 
ATOM   10017 C  CG    . GLU B 1 556 ? 110.543 165.817 175.652 1.00 41.23 ?  556 GLU B CG    1 
ATOM   10018 C  CD    . GLU B 1 556 ? 109.580 166.465 174.677 1.00 44.19 ?  556 GLU B CD    1 
ATOM   10019 O  OE1   . GLU B 1 556 ? 109.816 167.630 174.291 1.00 42.40 ?  556 GLU B OE1   1 
ATOM   10020 O  OE2   . GLU B 1 556 ? 108.586 165.811 174.297 1.00 44.24 -1 556 GLU B OE2   1 
ATOM   10021 N  N     . ASP B 1 557 ? 114.073 164.118 173.208 1.00 40.06 ?  557 ASP B N     1 
ATOM   10022 C  CA    . ASP B 1 557 ? 115.361 164.085 172.522 1.00 34.63 ?  557 ASP B CA    1 
ATOM   10023 C  C     . ASP B 1 557 ? 115.176 163.866 171.028 1.00 36.07 ?  557 ASP B C     1 
ATOM   10024 O  O     . ASP B 1 557 ? 115.887 164.460 170.211 1.00 38.98 ?  557 ASP B O     1 
ATOM   10025 C  CB    . ASP B 1 557 ? 116.251 162.994 173.119 1.00 32.74 ?  557 ASP B CB    1 
ATOM   10026 C  CG    . ASP B 1 557 ? 116.154 162.924 174.628 1.00 41.14 ?  557 ASP B CG    1 
ATOM   10027 O  OD1   . ASP B 1 557 ? 115.034 162.722 175.143 1.00 44.16 ?  557 ASP B OD1   1 
ATOM   10028 O  OD2   . ASP B 1 557 ? 117.197 163.069 175.300 1.00 42.26 -1 557 ASP B OD2   1 
ATOM   10029 N  N     . TRP B 1 558 ? 114.218 163.016 170.652 1.00 32.21 ?  558 TRP B N     1 
ATOM   10030 C  CA    . TRP B 1 558 ? 113.944 162.794 169.238 1.00 26.34 ?  558 TRP B CA    1 
ATOM   10031 C  C     . TRP B 1 558 ? 113.352 164.035 168.580 1.00 31.81 ?  558 TRP B C     1 
ATOM   10032 O  O     . TRP B 1 558 ? 113.644 164.320 167.416 1.00 38.07 ?  558 TRP B O     1 
ATOM   10033 C  CB    . TRP B 1 558 ? 113.016 161.595 169.070 1.00 27.19 ?  558 TRP B CB    1 
ATOM   10034 C  CG    . TRP B 1 558 ? 113.746 160.302 168.906 1.00 27.01 ?  558 TRP B CG    1 
ATOM   10035 C  CD1   . TRP B 1 558 ? 113.848 159.296 169.820 1.00 26.33 ?  558 TRP B CD1   1 
ATOM   10036 C  CD2   . TRP B 1 558 ? 114.474 159.871 167.751 1.00 27.89 ?  558 TRP B CD2   1 
ATOM   10037 N  NE1   . TRP B 1 558 ? 114.595 158.265 169.306 1.00 30.65 ?  558 TRP B NE1   1 
ATOM   10038 C  CE2   . TRP B 1 558 ? 114.990 158.592 168.036 1.00 28.06 ?  558 TRP B CE2   1 
ATOM   10039 C  CE3   . TRP B 1 558 ? 114.736 160.439 166.501 1.00 31.92 ?  558 TRP B CE3   1 
ATOM   10040 C  CZ2   . TRP B 1 558 ? 115.753 157.875 167.119 1.00 25.09 ?  558 TRP B CZ2   1 
ATOM   10041 C  CZ3   . TRP B 1 558 ? 115.495 159.727 165.593 1.00 26.96 ?  558 TRP B CZ3   1 
ATOM   10042 C  CH2   . TRP B 1 558 ? 115.994 158.458 165.907 1.00 21.83 ?  558 TRP B CH2   1 
ATOM   10043 N  N     . LYS B 1 559 ? 112.518 164.786 169.304 1.00 36.75 ?  559 LYS B N     1 
ATOM   10044 C  CA    . LYS B 1 559 ? 112.004 166.043 168.767 1.00 31.12 ?  559 LYS B CA    1 
ATOM   10045 C  C     . LYS B 1 559 ? 113.126 167.056 168.566 1.00 34.26 ?  559 LYS B C     1 
ATOM   10046 O  O     . LYS B 1 559 ? 113.164 167.762 167.549 1.00 34.78 ?  559 LYS B O     1 
ATOM   10047 C  CB    . LYS B 1 559 ? 110.933 166.611 169.697 1.00 35.39 ?  559 LYS B CB    1 
ATOM   10048 C  CG    . LYS B 1 559 ? 109.569 165.958 169.552 1.00 37.52 ?  559 LYS B CG    1 
ATOM   10049 C  CD    . LYS B 1 559 ? 108.666 166.307 170.721 1.00 36.46 ?  559 LYS B CD    1 
ATOM   10050 C  CE    . LYS B 1 559 ? 107.539 165.299 170.870 1.00 37.55 ?  559 LYS B CE    1 
ATOM   10051 N  NZ    . LYS B 1 559 ? 106.989 165.284 172.254 1.00 36.41 1  559 LYS B NZ    1 
ATOM   10052 N  N     . LYS B 1 560 ? 114.048 167.138 169.526 1.00 31.68 ?  560 LYS B N     1 
ATOM   10053 C  CA    . LYS B 1 560 ? 115.197 168.025 169.376 1.00 30.42 ?  560 LYS B CA    1 
ATOM   10054 C  C     . LYS B 1 560 ? 116.060 167.606 168.193 1.00 34.62 ?  560 LYS B C     1 
ATOM   10055 O  O     . LYS B 1 560 ? 116.547 168.455 167.438 1.00 36.67 ?  560 LYS B O     1 
ATOM   10056 C  CB    . LYS B 1 560 ? 116.019 168.044 170.664 1.00 30.64 ?  560 LYS B CB    1 
ATOM   10057 C  CG    . LYS B 1 560 ? 115.388 168.843 171.791 1.00 35.01 ?  560 LYS B CG    1 
ATOM   10058 C  CD    . LYS B 1 560 ? 116.299 168.889 173.006 1.00 37.36 ?  560 LYS B CD    1 
ATOM   10059 C  CE    . LYS B 1 560 ? 115.523 169.232 174.267 1.00 35.42 ?  560 LYS B CE    1 
ATOM   10060 N  NZ    . LYS B 1 560 ? 114.680 168.094 174.728 1.00 37.29 1  560 LYS B NZ    1 
ATOM   10061 N  N     . LEU B 1 561 ? 116.259 166.299 168.015 1.00 31.74 ?  561 LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 561 ? 117.026 165.811 166.874 1.00 27.68 ?  561 LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 561 ? 116.314 166.106 165.560 1.00 31.16 ?  561 LEU B C     1 
ATOM   10064 O  O     . LEU B 1 561 ? 116.959 166.427 164.557 1.00 33.36 ?  561 LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 561 ? 117.288 164.313 167.018 1.00 29.77 ?  561 LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 561 ? 118.075 163.669 165.876 1.00 28.99 ?  561 LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 561 ? 119.383 164.408 165.654 1.00 25.20 ?  561 LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 561 ? 118.328 162.202 166.155 1.00 26.50 ?  561 LEU B CD2   1 
ATOM   10069 N  N     . LYS B 1 562 ? 114.985 165.989 165.542 1.00 31.63 ?  562 LYS B N     1 
ATOM   10070 C  CA    . LYS B 1 562 ? 114.221 166.324 164.346 1.00 29.39 ?  562 LYS B CA    1 
ATOM   10071 C  C     . LYS B 1 562 ? 114.371 167.797 163.995 1.00 31.00 ?  562 LYS B C     1 
ATOM   10072 O  O     . LYS B 1 562 ? 114.549 168.151 162.824 1.00 35.93 ?  562 LYS B O     1 
ATOM   10073 C  CB    . LYS B 1 562 ? 112.751 165.961 164.555 1.00 27.01 ?  562 LYS B CB    1 
ATOM   10074 C  CG    . LYS B 1 562 ? 111.809 166.486 163.488 1.00 29.64 ?  562 LYS B CG    1 
ATOM   10075 C  CD    . LYS B 1 562 ? 110.364 166.178 163.844 1.00 30.78 ?  562 LYS B CD    1 
ATOM   10076 C  CE    . LYS B 1 562 ? 109.402 166.733 162.808 1.00 32.17 ?  562 LYS B CE    1 
ATOM   10077 N  NZ    . LYS B 1 562 ? 108.056 166.106 162.912 1.00 32.25 1  562 LYS B NZ    1 
ATOM   10078 N  N     . ALA B 1 563 ? 114.308 168.673 165.000 1.00 31.70 ?  563 ALA B N     1 
ATOM   10079 C  CA    . ALA B 1 563 ? 114.522 170.097 164.754 1.00 32.22 ?  563 ALA B CA    1 
ATOM   10080 C  C     . ALA B 1 563 ? 115.941 170.363 164.264 1.00 32.55 ?  563 ALA B C     1 
ATOM   10081 O  O     . ALA B 1 563 ? 116.153 171.180 163.360 1.00 36.45 ?  563 ALA B O     1 
ATOM   10082 C  CB    . ALA B 1 563 ? 114.232 170.899 166.023 1.00 32.53 ?  563 ALA B CB    1 
ATOM   10083 N  N     . PHE B 1 564 ? 116.925 169.677 164.849 1.00 32.33 ?  564 PHE B N     1 
ATOM   10084 C  CA    . PHE B 1 564 ? 118.313 169.843 164.430 1.00 27.46 ?  564 PHE B CA    1 
ATOM   10085 C  C     . PHE B 1 564 ? 118.506 169.408 162.981 1.00 30.75 ?  564 PHE B C     1 
ATOM   10086 O  O     . PHE B 1 564 ? 119.220 170.067 162.217 1.00 33.53 ?  564 PHE B O     1 
ATOM   10087 C  CB    . PHE B 1 564 ? 119.226 169.047 165.362 1.00 28.79 ?  564 PHE B CB    1 
ATOM   10088 C  CG    . PHE B 1 564 ? 120.681 169.381 165.223 1.00 32.18 ?  564 PHE B CG    1 
ATOM   10089 C  CD1   . PHE B 1 564 ? 121.220 170.475 165.877 1.00 31.86 ?  564 PHE B CD1   1 
ATOM   10090 C  CD2   . PHE B 1 564 ? 121.515 168.592 164.450 1.00 33.00 ?  564 PHE B CD2   1 
ATOM   10091 C  CE1   . PHE B 1 564 ? 122.562 170.779 165.755 1.00 34.64 ?  564 PHE B CE1   1 
ATOM   10092 C  CE2   . PHE B 1 564 ? 122.856 168.892 164.324 1.00 32.71 ?  564 PHE B CE2   1 
ATOM   10093 C  CZ    . PHE B 1 564 ? 123.380 169.986 164.977 1.00 34.29 ?  564 PHE B CZ    1 
ATOM   10094 N  N     . VAL B 1 565 ? 117.880 168.298 162.590 1.00 31.07 ?  565 VAL B N     1 
ATOM   10095 C  CA    . VAL B 1 565 ? 117.963 167.831 161.210 1.00 27.20 ?  565 VAL B CA    1 
ATOM   10096 C  C     . VAL B 1 565 ? 117.273 168.812 160.271 1.00 32.84 ?  565 VAL B C     1 
ATOM   10097 O  O     . VAL B 1 565 ? 117.782 169.116 159.187 1.00 34.16 ?  565 VAL B O     1 
ATOM   10098 C  CB    . VAL B 1 565 ? 117.371 166.416 161.089 1.00 27.17 ?  565 VAL B CB    1 
ATOM   10099 C  CG1   . VAL B 1 565 ? 117.209 166.027 159.630 1.00 27.37 ?  565 VAL B CG1   1 
ATOM   10100 C  CG2   . VAL B 1 565 ? 118.258 165.414 161.804 1.00 29.85 ?  565 VAL B CG2   1 
ATOM   10101 N  N     . ALA B 1 566 ? 116.106 169.324 160.669 1.00 34.96 ?  566 ALA B N     1 
ATOM   10102 C  CA    . ALA B 1 566 ? 115.413 170.302 159.839 1.00 34.18 ?  566 ALA B CA    1 
ATOM   10103 C  C     . ALA B 1 566 ? 116.259 171.552 159.641 1.00 36.19 ?  566 ALA B C     1 
ATOM   10104 O  O     . ALA B 1 566 ? 116.254 172.153 158.560 1.00 38.31 ?  566 ALA B O     1 
ATOM   10105 C  CB    . ALA B 1 566 ? 114.063 170.658 160.462 1.00 33.11 ?  566 ALA B CB    1 
ATOM   10106 N  N     . GLU B 1 567 ? 116.995 171.961 160.677 1.00 36.81 ?  567 GLU B N     1 
ATOM   10107 C  CA    . GLU B 1 567 ? 117.824 173.157 160.565 1.00 35.87 ?  567 GLU B CA    1 
ATOM   10108 C  C     . GLU B 1 567 ? 119.074 172.901 159.726 1.00 38.64 ?  567 GLU B C     1 
ATOM   10109 O  O     . GLU B 1 567 ? 119.444 173.733 158.888 1.00 44.38 ?  567 GLU B O     1 
ATOM   10110 C  CB    . GLU B 1 567 ? 118.202 173.661 161.957 1.00 34.73 ?  567 GLU B CB    1 
ATOM   10111 C  CG    . GLU B 1 567 ? 119.546 174.363 162.027 1.00 37.84 ?  567 GLU B CG    1 
ATOM   10112 C  CD    . GLU B 1 567 ? 119.567 175.482 163.048 1.00 42.89 ?  567 GLU B CD    1 
ATOM   10113 O  OE1   . GLU B 1 567 ? 120.611 176.153 163.174 1.00 42.59 ?  567 GLU B OE1   1 
ATOM   10114 O  OE2   . GLU B 1 567 ? 118.537 175.691 163.722 1.00 42.45 -1 567 GLU B OE2   1 
ATOM   10115 N  N     . HIS B 1 568 ? 119.732 171.755 159.923 1.00 34.94 ?  568 HIS B N     1 
ATOM   10116 C  CA    . HIS B 1 568 ? 121.038 171.511 159.326 1.00 31.70 ?  568 HIS B CA    1 
ATOM   10117 C  C     . HIS B 1 568 ? 121.048 170.454 158.233 1.00 32.49 ?  568 HIS B C     1 
ATOM   10118 O  O     . HIS B 1 568 ? 121.978 170.444 157.421 1.00 37.18 ?  568 HIS B O     1 
ATOM   10119 C  CB    . HIS B 1 568 ? 122.046 171.100 160.408 1.00 31.46 ?  568 HIS B CB    1 
ATOM   10120 C  CG    . HIS B 1 568 ? 122.347 172.182 161.395 1.00 35.80 ?  568 HIS B CG    1 
ATOM   10121 N  ND1   . HIS B 1 568 ? 122.129 172.038 162.747 1.00 36.83 ?  568 HIS B ND1   1 
ATOM   10122 C  CD2   . HIS B 1 568 ? 122.848 173.429 161.224 1.00 34.09 ?  568 HIS B CD2   1 
ATOM   10123 C  CE1   . HIS B 1 568 ? 122.484 173.148 163.368 1.00 32.59 ?  568 HIS B CE1   1 
ATOM   10124 N  NE2   . HIS B 1 568 ? 122.923 174.008 162.468 1.00 39.37 ?  568 HIS B NE2   1 
ATOM   10125 N  N     . GLY B 1 569 ? 120.057 169.574 158.184 1.00 28.65 ?  569 GLY B N     1 
ATOM   10126 C  CA    . GLY B 1 569 ? 120.061 168.511 157.202 1.00 27.61 ?  569 GLY B CA    1 
ATOM   10127 C  C     . GLY B 1 569 ? 120.850 167.301 157.663 1.00 29.72 ?  569 GLY B C     1 
ATOM   10128 O  O     . GLY B 1 569 ? 121.339 167.223 158.791 1.00 33.19 ?  569 GLY B O     1 
ATOM   10129 N  N     . MET B 1 570 ? 120.965 166.331 156.757 1.00 26.84 ?  570 MET B N     1 
ATOM   10130 C  CA    . MET B 1 570 ? 121.710 165.107 157.013 1.00 24.33 ?  570 MET B CA    1 
ATOM   10131 C  C     . MET B 1 570 ? 122.771 164.921 155.942 1.00 26.64 ?  570 MET B C     1 
ATOM   10132 O  O     . MET B 1 570 ? 122.507 165.116 154.753 1.00 30.44 ?  570 MET B O     1 
ATOM   10133 C  CB    . MET B 1 570 ? 120.792 163.882 157.046 1.00 25.96 ?  570 MET B CB    1 
ATOM   10134 C  CG    . MET B 1 570 ? 119.771 163.895 158.165 1.00 23.78 ?  570 MET B CG    1 
ATOM   10135 S  SD    . MET B 1 570 ? 119.860 162.404 159.166 1.00 38.72 ?  570 MET B SD    1 
ATOM   10136 C  CE    . MET B 1 570 ? 119.785 161.145 157.899 1.00 28.81 ?  570 MET B CE    1 
ATOM   10137 N  N     . TYR B 1 571 ? 123.973 164.541 156.372 1.00 19.73 ?  571 TYR B N     1 
ATOM   10138 C  CA    . TYR B 1 571 ? 125.064 164.326 155.430 1.00 11.33 ?  571 TYR B CA    1 
ATOM   10139 C  C     . TYR B 1 571 ? 124.918 163.020 154.661 1.00 18.37 ?  571 TYR B C     1 
ATOM   10140 O  O     . TYR B 1 571 ? 125.360 162.932 153.511 1.00 22.60 ?  571 TYR B O     1 
ATOM   10141 C  CB    . TYR B 1 571 ? 126.405 164.344 156.161 1.00 19.31 ?  571 TYR B CB    1 
ATOM   10142 C  CG    . TYR B 1 571 ? 127.594 164.445 155.236 1.00 20.16 ?  571 TYR B CG    1 
ATOM   10143 C  CD1   . TYR B 1 571 ? 127.885 165.632 154.580 1.00 23.18 ?  571 TYR B CD1   1 
ATOM   10144 C  CD2   . TYR B 1 571 ? 128.420 163.352 155.013 1.00 18.13 ?  571 TYR B CD2   1 
ATOM   10145 C  CE1   . TYR B 1 571 ? 128.968 165.730 153.732 1.00 23.37 ?  571 TYR B CE1   1 
ATOM   10146 C  CE2   . TYR B 1 571 ? 129.505 163.442 154.165 1.00 22.50 ?  571 TYR B CE2   1 
ATOM   10147 C  CZ    . TYR B 1 571 ? 129.774 164.633 153.527 1.00 27.73 ?  571 TYR B CZ    1 
ATOM   10148 O  OH    . TYR B 1 571 ? 130.856 164.726 152.683 1.00 26.73 ?  571 TYR B OH    1 
ATOM   10149 N  N     . HIS B 1 572 ? 124.312 162.004 155.267 1.00 20.02 ?  572 HIS B N     1 
ATOM   10150 C  CA    . HIS B 1 572 ? 124.231 160.674 154.681 1.00 13.85 ?  572 HIS B CA    1 
ATOM   10151 C  C     . HIS B 1 572 ? 122.791 160.355 154.312 1.00 22.03 ?  572 HIS B C     1 
ATOM   10152 O  O     . HIS B 1 572 ? 121.887 160.497 155.142 1.00 26.66 ?  572 HIS B O     1 
ATOM   10153 C  CB    . HIS B 1 572 ? 124.767 159.616 155.648 1.00 13.30 ?  572 HIS B CB    1 
ATOM   10154 C  CG    . HIS B 1 572 ? 126.088 159.967 156.256 1.00 14.70 ?  572 HIS B CG    1 
ATOM   10155 N  ND1   . HIS B 1 572 ? 126.200 160.610 157.470 1.00 18.30 ?  572 HIS B ND1   1 
ATOM   10156 C  CD2   . HIS B 1 572 ? 127.353 159.766 155.820 1.00 16.96 ?  572 HIS B CD2   1 
ATOM   10157 C  CE1   . HIS B 1 572 ? 127.477 160.789 157.755 1.00 19.14 ?  572 HIS B CE1   1 
ATOM   10158 N  NE2   . HIS B 1 572 ? 128.198 160.286 156.770 1.00 26.58 ?  572 HIS B NE2   1 
ATOM   10159 N  N     . SER B 1 573 ? 122.583 159.930 153.065 1.00 13.21 ?  573 SER B N     1 
ATOM   10160 C  CA    . SER B 1 573 ? 121.266 159.457 152.656 1.00 7.91  ?  573 SER B CA    1 
ATOM   10161 C  C     . SER B 1 573 ? 120.890 158.180 153.395 1.00 14.44 ?  573 SER B C     1 
ATOM   10162 O  O     . SER B 1 573 ? 119.727 157.991 153.770 1.00 21.39 ?  573 SER B O     1 
ATOM   10163 C  CB    . SER B 1 573 ? 121.236 159.232 151.146 1.00 14.15 ?  573 SER B CB    1 
ATOM   10164 O  OG    . SER B 1 573 ? 122.365 158.491 150.725 1.00 22.11 ?  573 SER B OG    1 
ATOM   10165 N  N     . TYR B 1 574 ? 121.859 157.294 153.606 1.00 14.03 ?  574 TYR B N     1 
ATOM   10166 C  CA    . TYR B 1 574 ? 121.648 156.043 154.314 1.00 7.35  ?  574 TYR B CA    1 
ATOM   10167 C  C     . TYR B 1 574 ? 122.792 155.847 155.294 1.00 8.48  ?  574 TYR B C     1 
ATOM   10168 O  O     . TYR B 1 574 ? 123.947 156.139 154.973 1.00 18.38 ?  574 TYR B O     1 
ATOM   10169 C  CB    . TYR B 1 574 ? 121.557 154.860 153.344 1.00 10.15 ?  574 TYR B CB    1 
ATOM   10170 C  CG    . TYR B 1 574 ? 120.518 155.050 152.266 1.00 7.41  ?  574 TYR B CG    1 
ATOM   10171 C  CD1   . TYR B 1 574 ? 120.829 155.711 151.085 1.00 9.48  ?  574 TYR B CD1   1 
ATOM   10172 C  CD2   . TYR B 1 574 ? 119.223 154.577 152.429 1.00 7.15  ?  574 TYR B CD2   1 
ATOM   10173 C  CE1   . TYR B 1 574 ? 119.883 155.898 150.101 1.00 9.78  ?  574 TYR B CE1   1 
ATOM   10174 C  CE2   . TYR B 1 574 ? 118.272 154.757 151.447 1.00 9.31  ?  574 TYR B CE2   1 
ATOM   10175 C  CZ    . TYR B 1 574 ? 118.607 155.418 150.287 1.00 4.50  ?  574 TYR B CZ    1 
ATOM   10176 O  OH    . TYR B 1 574 ? 117.664 155.597 149.304 1.00 17.16 ?  574 TYR B OH    1 
ATOM   10177 N  N     . ARG B 1 575 ? 122.468 155.363 156.486 1.00 10.32 ?  575 ARG B N     1 
ATOM   10178 C  CA    . ARG B 1 575 ? 123.444 155.273 157.565 1.00 4.99  ?  575 ARG B CA    1 
ATOM   10179 C  C     . ARG B 1 575 ? 123.618 153.872 158.123 1.00 12.76 ?  575 ARG B C     1 
ATOM   10180 O  O     . ARG B 1 575 ? 124.749 153.461 158.389 1.00 18.56 ?  575 ARG B O     1 
ATOM   10181 C  CB    . ARG B 1 575 ? 123.046 156.218 158.704 1.00 13.95 ?  575 ARG B CB    1 
ATOM   10182 C  CG    . ARG B 1 575 ? 122.965 157.678 158.304 1.00 6.32  ?  575 ARG B CG    1 
ATOM   10183 C  CD    . ARG B 1 575 ? 122.018 158.436 159.214 1.00 13.67 ?  575 ARG B CD    1 
ATOM   10184 N  NE    . ARG B 1 575 ? 120.633 158.020 159.028 1.00 18.22 ?  575 ARG B NE    1 
ATOM   10185 C  CZ    . ARG B 1 575 ? 119.978 157.205 159.843 1.00 13.40 ?  575 ARG B CZ    1 
ATOM   10186 N  NH1   . ARG B 1 575 ? 120.557 156.689 160.914 1.00 12.95 1  575 ARG B NH1   1 
ATOM   10187 N  NH2   . ARG B 1 575 ? 118.711 156.901 159.578 1.00 11.24 ?  575 ARG B NH2   1 
ATOM   10188 N  N     . LEU B 1 576 ? 122.536 153.123 158.306 1.00 20.40 ?  576 LEU B N     1 
ATOM   10189 C  CA    . LEU B 1 576 ? 122.576 151.846 159.003 1.00 10.53 ?  576 LEU B CA    1 
ATOM   10190 C  C     . LEU B 1 576 ? 122.190 150.721 158.057 1.00 5.36  ?  576 LEU B C     1 
ATOM   10191 O  O     . LEU B 1 576 ? 121.121 150.760 157.442 1.00 15.05 ?  576 LEU B O     1 
ATOM   10192 C  CB    . LEU B 1 576 ? 121.639 151.855 160.214 1.00 6.04  ?  576 LEU B CB    1 
ATOM   10193 C  CG    . LEU B 1 576 ? 121.795 153.011 161.201 1.00 7.13  ?  576 LEU B CG    1 
ATOM   10194 C  CD1   . LEU B 1 576 ? 120.705 152.954 162.256 1.00 13.51 ?  576 LEU B CD1   1 
ATOM   10195 C  CD2   . LEU B 1 576 ? 123.166 152.984 161.845 1.00 10.43 ?  576 LEU B CD2   1 
ATOM   10196 N  N     . CYS B 1 577 ? 123.065 149.725 157.942 1.00 14.04 ?  577 CYS B N     1 
ATOM   10197 C  CA    . CYS B 1 577 ? 122.753 148.482 157.251 1.00 8.07  ?  577 CYS B CA    1 
ATOM   10198 C  C     . CYS B 1 577 ? 123.510 147.367 157.954 1.00 14.92 ?  577 CYS B C     1 
ATOM   10199 O  O     . CYS B 1 577 ? 124.702 147.509 158.240 1.00 21.80 ?  577 CYS B O     1 
ATOM   10200 C  CB    . CYS B 1 577 ? 123.113 148.553 155.759 1.00 5.93  ?  577 CYS B CB    1 
ATOM   10201 S  SG    . CYS B 1 577 ? 124.797 148.080 155.295 1.00 35.18 ?  577 CYS B SG    1 
ATOM   10202 N  N     . ILE B 1 578 ? 122.813 146.278 158.258 1.00 16.01 ?  578 ILE B N     1 
ATOM   10203 C  CA    . ILE B 1 578 ? 123.364 145.192 159.059 1.00 12.46 ?  578 ILE B CA    1 
ATOM   10204 C  C     . ILE B 1 578 ? 123.809 144.092 158.100 1.00 9.65  ?  578 ILE B C     1 
ATOM   10205 O  O     . ILE B 1 578 ? 123.001 143.288 157.630 1.00 18.17 ?  578 ILE B O     1 
ATOM   10206 C  CB    . ILE B 1 578 ? 122.357 144.684 160.093 1.00 9.77  ?  578 ILE B CB    1 
ATOM   10207 C  CG1   . ILE B 1 578 ? 121.937 145.828 161.016 1.00 8.00  ?  578 ILE B CG1   1 
ATOM   10208 C  CG2   . ILE B 1 578 ? 122.954 143.557 160.909 1.00 9.50  ?  578 ILE B CG2   1 
ATOM   10209 C  CD1   . ILE B 1 578 ? 121.096 145.391 162.183 1.00 8.95  ?  578 ILE B CD1   1 
ATOM   10210 N  N     . ALA B 1 579 ? 125.106 144.065 157.812 1.00 17.09 ?  579 ALA B N     1 
ATOM   10211 C  CA    . ALA B 1 579 ? 125.715 143.071 156.947 1.00 7.33  ?  579 ALA B CA    1 
ATOM   10212 C  C     . ALA B 1 579 ? 125.874 141.741 157.680 1.00 21.03 ?  579 ALA B C     1 
ATOM   10213 O  O     . ALA B 1 579 ? 125.789 141.686 158.908 1.00 28.62 ?  579 ALA B O     1 
ATOM   10214 C  CB    . ALA B 1 579 ? 127.068 143.574 156.458 1.00 11.73 ?  579 ALA B CB    1 
ATOM   10215 N  N     . PRO B 1 580 ? 126.078 140.643 156.944 1.00 25.04 ?  580 PRO B N     1 
ATOM   10216 C  CA    . PRO B 1 580 ? 126.293 139.348 157.612 1.00 22.61 ?  580 PRO B CA    1 
ATOM   10217 C  C     . PRO B 1 580 ? 127.516 139.309 158.516 1.00 25.92 ?  580 PRO B C     1 
ATOM   10218 O  O     . PRO B 1 580 ? 127.492 138.593 159.526 1.00 32.85 ?  580 PRO B O     1 
ATOM   10219 C  CB    . PRO B 1 580 ? 126.423 138.361 156.442 1.00 22.52 ?  580 PRO B CB    1 
ATOM   10220 C  CG    . PRO B 1 580 ? 126.626 139.200 155.224 1.00 21.75 ?  580 PRO B CG    1 
ATOM   10221 C  CD    . PRO B 1 580 ? 125.934 140.489 155.487 1.00 19.76 ?  580 PRO B CD    1 
ATOM   10222 N  N     . THR B 1 581 ? 128.577 140.051 158.191 1.00 21.55 ?  581 THR B N     1 
ATOM   10223 C  CA    . THR B 1 581 ? 129.820 140.078 158.972 1.00 29.18 ?  581 THR B CA    1 
ATOM   10224 C  C     . THR B 1 581 ? 130.350 138.659 159.212 1.00 28.51 ?  581 THR B C     1 
ATOM   10225 O  O     . THR B 1 581 ? 130.423 138.165 160.335 1.00 27.81 ?  581 THR B O     1 
ATOM   10226 C  CB    . THR B 1 581 ? 129.639 140.817 160.304 1.00 28.11 ?  581 THR B CB    1 
ATOM   10227 O  OG1   . THR B 1 581 ? 129.193 139.899 161.310 1.00 27.66 ?  581 THR B OG1   1 
ATOM   10228 C  CG2   . THR B 1 581 ? 128.649 141.962 160.173 1.00 30.44 ?  581 THR B CG2   1 
ATOM   10229 N  N     . GLY B 1 582 ? 130.725 138.020 158.107 1.00 31.48 ?  582 GLY B N     1 
ATOM   10230 C  CA    . GLY B 1 582 ? 131.090 136.618 158.133 1.00 33.44 ?  582 GLY B CA    1 
ATOM   10231 C  C     . GLY B 1 582 ? 132.352 136.277 158.900 1.00 37.00 ?  582 GLY B C     1 
ATOM   10232 O  O     . GLY B 1 582 ? 132.285 135.622 159.945 1.00 38.24 ?  582 GLY B O     1 
ATOM   10233 N  N     . SER B 1 583 ? 133.510 136.713 158.402 1.00 31.25 ?  583 SER B N     1 
ATOM   10234 C  CA    . SER B 1 583 ? 134.783 136.283 158.968 1.00 33.74 ?  583 SER B CA    1 
ATOM   10235 C  C     . SER B 1 583 ? 135.389 137.279 159.945 1.00 35.09 ?  583 SER B C     1 
ATOM   10236 O  O     . SER B 1 583 ? 136.186 136.874 160.798 1.00 37.38 ?  583 SER B O     1 
ATOM   10237 C  CB    . SER B 1 583 ? 135.793 136.007 157.847 1.00 37.87 ?  583 SER B CB    1 
ATOM   10238 O  OG    . SER B 1 583 ? 135.642 134.691 157.345 1.00 41.00 ?  583 SER B OG    1 
ATOM   10239 N  N     . ILE B 1 584 ? 135.036 138.563 159.849 1.00 33.94 ?  584 ILE B N     1 
ATOM   10240 C  CA    . ILE B 1 584 ? 135.567 139.541 160.788 1.00 27.57 ?  584 ILE B CA    1 
ATOM   10241 C  C     . ILE B 1 584 ? 134.919 139.410 162.160 1.00 26.21 ?  584 ILE B C     1 
ATOM   10242 O  O     . ILE B 1 584 ? 135.422 139.980 163.136 1.00 29.85 ?  584 ILE B O     1 
ATOM   10243 C  CB    . ILE B 1 584 ? 135.400 140.964 160.225 1.00 31.69 ?  584 ILE B CB    1 
ATOM   10244 C  CG1   . ILE B 1 584 ? 136.464 141.895 160.808 1.00 28.37 ?  584 ILE B CG1   1 
ATOM   10245 C  CG2   . ILE B 1 584 ? 134.003 141.496 160.509 1.00 29.13 ?  584 ILE B CG2   1 
ATOM   10246 C  CD1   . ILE B 1 584 ? 137.877 141.429 160.607 1.00 31.61 ?  584 ILE B CD1   1 
ATOM   10247 N  N     . SER B 1 585 ? 133.814 138.669 162.265 1.00 31.58 ?  585 SER B N     1 
ATOM   10248 C  CA    . SER B 1 585 ? 133.218 138.420 163.572 1.00 30.22 ?  585 SER B CA    1 
ATOM   10249 C  C     . SER B 1 585 ? 134.088 137.493 164.409 1.00 28.05 ?  585 SER B C     1 
ATOM   10250 O  O     . SER B 1 585 ? 134.010 137.519 165.643 1.00 26.72 ?  585 SER B O     1 
ATOM   10251 C  CB    . SER B 1 585 ? 131.815 137.834 163.411 1.00 25.61 ?  585 SER B CB    1 
ATOM   10252 O  OG    . SER B 1 585 ? 131.856 136.595 162.726 1.00 30.23 ?  585 SER B OG    1 
ATOM   10253 N  N     . TYR B 1 586 ? 134.909 136.666 163.760 1.00 31.10 ?  586 TYR B N     1 
ATOM   10254 C  CA    . TYR B 1 586 ? 135.840 135.811 164.486 1.00 32.10 ?  586 TYR B CA    1 
ATOM   10255 C  C     . TYR B 1 586 ? 136.861 136.642 165.252 1.00 31.26 ?  586 TYR B C     1 
ATOM   10256 O  O     . TYR B 1 586 ? 137.127 136.389 166.432 1.00 34.53 ?  586 TYR B O     1 
ATOM   10257 C  CB    . TYR B 1 586 ? 136.547 134.871 163.511 1.00 28.08 ?  586 TYR B CB    1 
ATOM   10258 C  CG    . TYR B 1 586 ? 135.704 133.710 163.046 1.00 31.07 ?  586 TYR B CG    1 
ATOM   10259 C  CD1   . TYR B 1 586 ? 135.220 132.772 163.945 1.00 31.09 ?  586 TYR B CD1   1 
ATOM   10260 C  CD2   . TYR B 1 586 ? 135.391 133.555 161.703 1.00 31.81 ?  586 TYR B CD2   1 
ATOM   10261 C  CE1   . TYR B 1 586 ? 134.449 131.711 163.519 1.00 33.96 ?  586 TYR B CE1   1 
ATOM   10262 C  CE2   . TYR B 1 586 ? 134.620 132.498 161.268 1.00 30.57 ?  586 TYR B CE2   1 
ATOM   10263 C  CZ    . TYR B 1 586 ? 134.152 131.579 162.180 1.00 34.73 ?  586 TYR B CZ    1 
ATOM   10264 O  OH    . TYR B 1 586 ? 133.383 130.524 161.748 1.00 37.76 ?  586 TYR B OH    1 
ATOM   10265 N  N     . VAL B 1 587 ? 137.436 137.650 164.590 1.00 28.11 ?  587 VAL B N     1 
ATOM   10266 C  CA    . VAL B 1 587 ? 138.487 138.457 165.204 1.00 24.65 ?  587 VAL B CA    1 
ATOM   10267 C  C     . VAL B 1 587 ? 137.944 139.228 166.399 1.00 29.14 ?  587 VAL B C     1 
ATOM   10268 O  O     . VAL B 1 587 ? 138.633 139.400 167.412 1.00 35.72 ?  587 VAL B O     1 
ATOM   10269 C  CB    . VAL B 1 587 ? 139.108 139.402 164.158 1.00 30.15 ?  587 VAL B CB    1 
ATOM   10270 C  CG1   . VAL B 1 587 ? 140.328 140.102 164.731 1.00 30.11 ?  587 VAL B CG1   1 
ATOM   10271 C  CG2   . VAL B 1 587 ? 139.466 138.635 162.896 1.00 28.67 ?  587 VAL B CG2   1 
ATOM   10272 N  N     . GLN B 1 588 ? 136.704 139.698 166.305 1.00 31.14 ?  588 GLN B N     1 
ATOM   10273 C  CA    . GLN B 1 588 ? 136.094 140.478 167.371 1.00 24.26 ?  588 GLN B CA    1 
ATOM   10274 C  C     . GLN B 1 588 ? 135.536 139.617 168.495 1.00 25.55 ?  588 GLN B C     1 
ATOM   10275 O  O     . GLN B 1 588 ? 135.023 140.170 169.473 1.00 32.76 ?  588 GLN B O     1 
ATOM   10276 C  CB    . GLN B 1 588 ? 134.980 141.360 166.804 1.00 25.03 ?  588 GLN B CB    1 
ATOM   10277 C  CG    . GLN B 1 588 ? 135.479 142.554 166.014 1.00 28.82 ?  588 GLN B CG    1 
ATOM   10278 C  CD    . GLN B 1 588 ? 135.518 143.820 166.845 1.00 24.32 ?  588 GLN B CD    1 
ATOM   10279 O  OE1   . GLN B 1 588 ? 134.560 144.147 167.543 1.00 29.94 ?  588 GLN B OE1   1 
ATOM   10280 N  NE2   . GLN B 1 588 ? 136.629 144.541 166.773 1.00 26.90 ?  588 GLN B NE2   1 
ATOM   10281 N  N     . SER B 1 589 ? 135.635 138.293 168.381 1.00 30.06 ?  589 SER B N     1 
ATOM   10282 C  CA    . SER B 1 589 ? 135.048 137.362 169.341 1.00 27.12 ?  589 SER B CA    1 
ATOM   10283 C  C     . SER B 1 589 ? 133.564 137.667 169.529 1.00 26.93 ?  589 SER B C     1 
ATOM   10284 O  O     . SER B 1 589 ? 133.079 137.931 170.630 1.00 28.72 ?  589 SER B O     1 
ATOM   10285 C  CB    . SER B 1 589 ? 135.799 137.396 170.674 1.00 32.57 ?  589 SER B CB    1 
ATOM   10286 O  OG    . SER B 1 589 ? 137.133 136.953 170.514 1.00 36.64 ?  589 SER B OG    1 
ATOM   10287 N  N     . SER B 1 590 ? 132.848 137.637 168.409 1.00 25.89 ?  590 SER B N     1 
ATOM   10288 C  CA    . SER B 1 590 ? 131.455 138.046 168.365 1.00 22.92 ?  590 SER B CA    1 
ATOM   10289 C  C     . SER B 1 590 ? 130.667 137.081 167.496 1.00 25.94 ?  590 SER B C     1 
ATOM   10290 O  O     . SER B 1 590 ? 131.206 136.470 166.570 1.00 29.51 ?  590 SER B O     1 
ATOM   10291 C  CB    . SER B 1 590 ? 131.315 139.473 167.822 1.00 21.98 ?  590 SER B CB    1 
ATOM   10292 O  OG    . SER B 1 590 ? 131.134 139.468 166.419 1.00 31.28 ?  590 SER B OG    1 
ATOM   10293 N  N     . THR B 1 591 ? 129.382 136.943 167.810 1.00 25.52 ?  591 THR B N     1 
ATOM   10294 C  CA    . THR B 1 591 ? 128.486 136.187 166.950 1.00 21.76 ?  591 THR B CA    1 
ATOM   10295 C  C     . THR B 1 591 ? 128.194 136.975 165.678 1.00 24.15 ?  591 THR B C     1 
ATOM   10296 O  O     . THR B 1 591 ? 128.156 138.208 165.679 1.00 22.75 ?  591 THR B O     1 
ATOM   10297 C  CB    . THR B 1 591 ? 127.186 135.858 167.679 1.00 22.02 ?  591 THR B CB    1 
ATOM   10298 O  OG1   . THR B 1 591 ? 126.391 137.043 167.804 1.00 29.69 ?  591 THR B OG1   1 
ATOM   10299 C  CG2   . THR B 1 591 ? 127.484 135.305 169.060 1.00 20.22 ?  591 THR B CG2   1 
ATOM   10300 N  N     . ALA B 1 592 ? 127.992 136.246 164.584 1.00 22.71 ?  592 ALA B N     1 
ATOM   10301 C  CA    . ALA B 1 592 ? 127.859 136.869 163.274 1.00 20.11 ?  592 ALA B CA    1 
ATOM   10302 C  C     . ALA B 1 592 ? 126.586 137.703 163.202 1.00 19.32 ?  592 ALA B C     1 
ATOM   10303 O  O     . ALA B 1 592 ? 125.478 137.165 163.281 1.00 27.49 ?  592 ALA B O     1 
ATOM   10304 C  CB    . ALA B 1 592 ? 127.859 135.800 162.184 1.00 24.99 ?  592 ALA B CB    1 
ATOM   10305 N  N     . SER B 1 593 ? 126.754 139.014 163.062 1.00 25.09 ?  593 SER B N     1 
ATOM   10306 C  CA    . SER B 1 593 ? 125.657 139.953 162.788 1.00 14.55 ?  593 SER B CA    1 
ATOM   10307 C  C     . SER B 1 593 ? 124.645 139.889 163.933 1.00 16.18 ?  593 SER B C     1 
ATOM   10308 O  O     . SER B 1 593 ? 124.993 139.541 165.070 1.00 27.98 ?  593 SER B O     1 
ATOM   10309 C  CB    . SER B 1 593 ? 125.080 139.656 161.415 1.00 27.06 ?  593 SER B CB    1 
ATOM   10310 O  OG    . SER B 1 593 ? 124.186 140.670 161.001 1.00 23.36 ?  593 SER B OG    1 
ATOM   10311 N  N     . VAL B 1 594 ? 123.389 140.230 163.646 1.00 19.65 ?  594 VAL B N     1 
ATOM   10312 C  CA    . VAL B 1 594 ? 122.303 140.091 164.606 1.00 19.52 ?  594 VAL B CA    1 
ATOM   10313 C  C     . VAL B 1 594 ? 121.612 138.737 164.480 1.00 18.59 ?  594 VAL B C     1 
ATOM   10314 O  O     . VAL B 1 594 ? 120.600 138.495 165.142 1.00 18.18 ?  594 VAL B O     1 
ATOM   10315 C  CB    . VAL B 1 594 ? 121.289 141.238 164.465 1.00 17.07 ?  594 VAL B CB    1 
ATOM   10316 C  CG1   . VAL B 1 594 ? 121.953 142.570 164.768 1.00 12.24 ?  594 VAL B CG1   1 
ATOM   10317 C  CG2   . VAL B 1 594 ? 120.684 141.245 163.072 1.00 19.04 ?  594 VAL B CG2   1 
ATOM   10318 N  N     . MET B 1 595 ? 122.138 137.851 163.640 1.00 23.61 ?  595 MET B N     1 
ATOM   10319 C  CA    . MET B 1 595 ? 121.575 136.522 163.497 1.00 19.01 ?  595 MET B CA    1 
ATOM   10320 C  C     . MET B 1 595 ? 121.896 135.674 164.726 1.00 26.69 ?  595 MET B C     1 
ATOM   10321 O  O     . MET B 1 595 ? 122.924 135.875 165.380 1.00 29.65 ?  595 MET B O     1 
ATOM   10322 C  CB    . MET B 1 595 ? 122.126 135.836 162.250 1.00 18.08 ?  595 MET B CB    1 
ATOM   10323 C  CG    . MET B 1 595 ? 121.421 136.186 160.947 1.00 24.07 ?  595 MET B CG    1 
ATOM   10324 S  SD    . MET B 1 595 ? 119.687 136.632 161.143 1.00 29.78 ?  595 MET B SD    1 
ATOM   10325 C  CE    . MET B 1 595 ? 119.787 138.405 160.929 1.00 22.55 ?  595 MET B CE    1 
ATOM   10326 N  N     . PRO B 1 596 ? 121.031 134.723 165.066 1.00 29.56 ?  596 PRO B N     1 
ATOM   10327 C  CA    . PRO B 1 596 ? 121.377 133.756 166.110 1.00 19.09 ?  596 PRO B CA    1 
ATOM   10328 C  C     . PRO B 1 596 ? 122.443 132.784 165.626 1.00 25.93 ?  596 PRO B C     1 
ATOM   10329 O  O     . PRO B 1 596 ? 122.613 132.545 164.429 1.00 30.62 ?  596 PRO B O     1 
ATOM   10330 C  CB    . PRO B 1 596 ? 120.052 133.042 166.389 1.00 20.74 ?  596 PRO B CB    1 
ATOM   10331 C  CG    . PRO B 1 596 ? 119.276 133.185 165.129 1.00 23.25 ?  596 PRO B CG    1 
ATOM   10332 C  CD    . PRO B 1 596 ? 119.682 134.496 164.518 1.00 25.77 ?  596 PRO B CD    1 
ATOM   10333 N  N     . ILE B 1 597 ? 123.174 132.224 166.591 1.00 28.44 ?  597 ILE B N     1 
ATOM   10334 C  CA    . ILE B 1 597 ? 124.305 131.362 166.273 1.00 31.03 ?  597 ILE B CA    1 
ATOM   10335 C  C     . ILE B 1 597 ? 123.820 130.093 165.585 1.00 34.42 ?  597 ILE B C     1 
ATOM   10336 O  O     . ILE B 1 597 ? 122.780 129.523 165.943 1.00 37.08 ?  597 ILE B O     1 
ATOM   10337 C  CB    . ILE B 1 597 ? 125.108 131.034 167.543 1.00 32.17 ?  597 ILE B CB    1 
ATOM   10338 C  CG1   . ILE B 1 597 ? 124.243 130.267 168.544 1.00 30.45 ?  597 ILE B CG1   1 
ATOM   10339 C  CG2   . ILE B 1 597 ? 125.647 132.305 168.169 1.00 29.22 ?  597 ILE B CG2   1 
ATOM   10340 C  CD1   . ILE B 1 597 ? 125.015 129.303 169.406 1.00 29.18 ?  597 ILE B CD1   1 
ATOM   10341 N  N     . MET B 1 598 ? 124.570 129.654 164.573 1.00 40.22 ?  598 MET B N     1 
ATOM   10342 C  CA    . MET B 1 598 ? 124.241 128.403 163.901 1.00 38.65 ?  598 MET B CA    1 
ATOM   10343 C  C     . MET B 1 598 ? 124.528 127.206 164.797 1.00 36.48 ?  598 MET B C     1 
ATOM   10344 O  O     . MET B 1 598 ? 123.728 126.265 164.864 1.00 42.09 ?  598 MET B O     1 
ATOM   10345 C  CB    . MET B 1 598 ? 125.021 128.291 162.592 1.00 38.14 ?  598 MET B CB    1 
ATOM   10346 C  CG    . MET B 1 598 ? 124.384 129.027 161.429 1.00 35.63 ?  598 MET B CG    1 
ATOM   10347 S  SD    . MET B 1 598 ? 125.567 129.457 160.139 1.00 53.34 ?  598 MET B SD    1 
ATOM   10348 C  CE    . MET B 1 598 ? 126.805 130.332 161.091 1.00 40.76 ?  598 MET B CE    1 
ATOM   10349 N  N     . GLU B 1 599 ? 125.661 127.224 165.495 1.00 37.86 ?  599 GLU B N     1 
ATOM   10350 C  CA    . GLU B 1 599 ? 126.044 126.135 166.378 1.00 37.80 ?  599 GLU B CA    1 
ATOM   10351 C  C     . GLU B 1 599 ? 126.812 126.707 167.559 1.00 34.97 ?  599 GLU B C     1 
ATOM   10352 O  O     . GLU B 1 599 ? 127.447 127.759 167.452 1.00 40.23 ?  599 GLU B O     1 
ATOM   10353 C  CB    . GLU B 1 599 ? 126.895 125.091 165.646 1.00 39.85 ?  599 GLU B CB    1 
ATOM   10354 C  CG    . GLU B 1 599 ? 128.037 125.688 164.845 1.00 37.81 ?  599 GLU B CG    1 
ATOM   10355 C  CD    . GLU B 1 599 ? 128.273 124.964 163.535 1.00 43.29 ?  599 GLU B CD    1 
ATOM   10356 O  OE1   . GLU B 1 599 ? 127.965 123.757 163.459 1.00 44.64 ?  599 GLU B OE1   1 
ATOM   10357 O  OE2   . GLU B 1 599 ? 128.770 125.603 162.584 1.00 43.83 -1 599 GLU B OE2   1 
ATOM   10358 N  N     . ARG B 1 600 ? 126.744 126.004 168.690 1.00 36.52 ?  600 ARG B N     1 
ATOM   10359 C  CA    . ARG B 1 600 ? 127.461 126.451 169.879 1.00 32.88 ?  600 ARG B CA    1 
ATOM   10360 C  C     . ARG B 1 600 ? 128.966 126.325 169.693 1.00 33.71 ?  600 ARG B C     1 
ATOM   10361 O  O     . ARG B 1 600 ? 129.719 127.264 169.975 1.00 39.87 ?  600 ARG B O     1 
ATOM   10362 C  CB    . ARG B 1 600 ? 126.996 125.655 171.097 1.00 35.62 ?  600 ARG B CB    1 
ATOM   10363 C  CG    . ARG B 1 600 ? 125.632 126.068 171.605 1.00 33.67 ?  600 ARG B CG    1 
ATOM   10364 C  CD    . ARG B 1 600 ? 125.335 125.436 172.944 1.00 31.09 ?  600 ARG B CD    1 
ATOM   10365 N  NE    . ARG B 1 600 ? 123.976 125.715 173.390 1.00 32.40 ?  600 ARG B NE    1 
ATOM   10366 C  CZ    . ARG B 1 600 ? 122.902 125.061 172.972 1.00 34.59 ?  600 ARG B CZ    1 
ATOM   10367 N  NH1   . ARG B 1 600 ? 122.989 124.087 172.082 1.00 33.92 1  600 ARG B NH1   1 
ATOM   10368 N  NH2   . ARG B 1 600 ? 121.710 125.393 173.460 1.00 35.08 ?  600 ARG B NH2   1 
ATOM   10369 N  N     . ILE B 1 601 ? 129.423 125.169 169.222 1.00 38.78 ?  601 ILE B N     1 
ATOM   10370 C  CA    . ILE B 1 601 ? 130.823 124.940 168.887 1.00 37.26 ?  601 ILE B CA    1 
ATOM   10371 C  C     . ILE B 1 601 ? 130.876 124.502 167.433 1.00 37.70 ?  601 ILE B C     1 
ATOM   10372 O  O     . ILE B 1 601 ? 130.239 123.511 167.055 1.00 42.98 ?  601 ILE B O     1 
ATOM   10373 C  CB    . ILE B 1 601 ? 131.471 123.888 169.801 1.00 39.69 ?  601 ILE B CB    1 
ATOM   10374 C  CG1   . ILE B 1 601 ? 131.136 124.169 171.266 1.00 40.45 ?  601 ILE B CG1   1 
ATOM   10375 C  CG2   . ILE B 1 601 ? 132.975 123.859 169.595 1.00 37.99 ?  601 ILE B CG2   1 
ATOM   10376 C  CD1   . ILE B 1 601 ? 131.553 123.066 172.211 1.00 39.25 ?  601 ILE B CD1   1 
ATOM   10377 N  N     . GLU B 1 602 ? 131.630 125.233 166.620 1.00 45.48 ?  602 GLU B N     1 
ATOM   10378 C  CA    . GLU B 1 602 ? 131.739 124.940 165.198 1.00 46.01 ?  602 GLU B CA    1 
ATOM   10379 C  C     . GLU B 1 602 ? 133.070 124.266 164.900 1.00 47.78 ?  602 GLU B C     1 
ATOM   10380 O  O     . GLU B 1 602 ? 134.129 124.740 165.321 1.00 47.96 ?  602 GLU B O     1 
ATOM   10381 C  CB    . GLU B 1 602 ? 131.602 126.213 164.362 1.00 44.80 ?  602 GLU B CB    1 
ATOM   10382 C  CG    . GLU B 1 602 ? 132.313 127.418 164.938 1.00 47.22 ?  602 GLU B CG    1 
ATOM   10383 C  CD    . GLU B 1 602 ? 132.544 128.499 163.906 1.00 50.05 ?  602 GLU B CD    1 
ATOM   10384 O  OE1   . GLU B 1 602 ? 131.565 129.161 163.504 1.00 48.81 ?  602 GLU B OE1   1 
ATOM   10385 O  OE2   . GLU B 1 602 ? 133.707 128.684 163.492 1.00 49.61 -1 602 GLU B OE2   1 
ATOM   10386 N  N     . GLU B 1 603 ? 133.011 123.156 164.170 1.00 53.84 ?  603 GLU B N     1 
ATOM   10387 C  CA    . GLU B 1 603 ? 134.196 122.401 163.781 1.00 54.70 ?  603 GLU B CA    1 
ATOM   10388 C  C     . GLU B 1 603 ? 134.557 122.782 162.350 1.00 53.81 ?  603 GLU B C     1 
ATOM   10389 O  O     . GLU B 1 603 ? 133.805 122.491 161.413 1.00 54.77 ?  603 GLU B O     1 
ATOM   10390 C  CB    . GLU B 1 603 ? 133.953 120.899 163.911 1.00 54.03 ?  603 GLU B CB    1 
ATOM   10391 C  CG    . GLU B 1 603 ? 135.133 120.039 163.495 1.00 56.11 ?  603 GLU B CG    1 
ATOM   10392 C  CD    . GLU B 1 603 ? 134.744 118.593 163.257 1.00 58.17 ?  603 GLU B CD    1 
ATOM   10393 O  OE1   . GLU B 1 603 ? 134.529 117.862 164.247 1.00 57.94 ?  603 GLU B OE1   1 
ATOM   10394 O  OE2   . GLU B 1 603 ? 134.652 118.186 162.079 1.00 56.54 -1 603 GLU B OE2   1 
ATOM   10395 N  N     . ARG B 1 604 ? 135.707 123.430 162.185 1.00 55.14 ?  604 ARG B N     1 
ATOM   10396 C  CA    . ARG B 1 604 ? 136.177 123.890 160.888 1.00 55.62 ?  604 ARG B CA    1 
ATOM   10397 C  C     . ARG B 1 604 ? 137.508 123.227 160.566 1.00 56.99 ?  604 ARG B C     1 
ATOM   10398 O  O     . ARG B 1 604 ? 138.390 123.135 161.425 1.00 58.94 ?  604 ARG B O     1 
ATOM   10399 C  CB    . ARG B 1 604 ? 136.334 125.415 160.867 1.00 57.20 ?  604 ARG B CB    1 
ATOM   10400 C  CG    . ARG B 1 604 ? 135.027 126.183 160.735 1.00 57.77 ?  604 ARG B CG    1 
ATOM   10401 C  CD    . ARG B 1 604 ? 134.087 125.527 159.739 1.00 56.81 ?  604 ARG B CD    1 
ATOM   10402 N  NE    . ARG B 1 604 ? 132.921 124.942 160.392 1.00 59.20 ?  604 ARG B NE    1 
ATOM   10403 C  CZ    . ARG B 1 604 ? 131.836 125.620 160.735 1.00 59.01 ?  604 ARG B CZ    1 
ATOM   10404 N  NH1   . ARG B 1 604 ? 131.731 126.919 160.507 1.00 56.40 1  604 ARG B NH1   1 
ATOM   10405 N  NH2   . ARG B 1 604 ? 130.828 124.977 161.319 1.00 56.67 ?  604 ARG B NH2   1 
ATOM   10406 N  N     . THR B 1 605 ? 137.656 122.774 159.326 1.00 63.74 ?  605 THR B N     1 
ATOM   10407 C  CA    . THR B 1 605 ? 138.865 122.092 158.887 1.00 64.57 ?  605 THR B CA    1 
ATOM   10408 C  C     . THR B 1 605 ? 139.775 123.089 158.178 1.00 64.75 ?  605 THR B C     1 
ATOM   10409 O  O     . THR B 1 605 ? 139.384 123.684 157.168 1.00 64.19 ?  605 THR B O     1 
ATOM   10410 C  CB    . THR B 1 605 ? 138.530 120.923 157.962 1.00 64.44 ?  605 THR B CB    1 
ATOM   10411 O  OG1   . THR B 1 605 ? 137.712 119.978 158.662 1.00 64.01 ?  605 THR B OG1   1 
ATOM   10412 C  CG2   . THR B 1 605 ? 139.802 120.236 157.494 1.00 64.39 ?  605 THR B CG2   1 
ATOM   10413 N  N     . TYR B 1 606 ? 140.981 123.267 158.710 1.00 64.82 ?  606 TYR B N     1 
ATOM   10414 C  CA    . TYR B 1 606 ? 141.998 124.116 158.105 1.00 66.48 ?  606 TYR B CA    1 
ATOM   10415 C  C     . TYR B 1 606 ? 143.229 123.269 157.820 1.00 67.41 ?  606 TYR B C     1 
ATOM   10416 O  O     . TYR B 1 606 ? 143.742 122.591 158.719 1.00 65.23 ?  606 TYR B O     1 
ATOM   10417 C  CB    . TYR B 1 606 ? 142.351 125.296 159.015 1.00 64.43 ?  606 TYR B CB    1 
ATOM   10418 C  CG    . TYR B 1 606 ? 141.174 126.192 159.327 1.00 65.10 ?  606 TYR B CG    1 
ATOM   10419 C  CD1   . TYR B 1 606 ? 140.646 127.038 158.360 1.00 64.08 ?  606 TYR B CD1   1 
ATOM   10420 C  CD2   . TYR B 1 606 ? 140.589 126.193 160.586 1.00 63.67 ?  606 TYR B CD2   1 
ATOM   10421 C  CE1   . TYR B 1 606 ? 139.571 127.858 158.638 1.00 64.22 ?  606 TYR B CE1   1 
ATOM   10422 C  CE2   . TYR B 1 606 ? 139.513 127.010 160.874 1.00 62.41 ?  606 TYR B CE2   1 
ATOM   10423 C  CZ    . TYR B 1 606 ? 139.008 127.840 159.896 1.00 65.40 ?  606 TYR B CZ    1 
ATOM   10424 O  OH    . TYR B 1 606 ? 137.936 128.656 160.177 1.00 66.17 ?  606 TYR B OH    1 
ATOM   10425 N  N     . GLY B 1 607 ? 143.698 123.311 156.577 1.00 74.58 ?  607 GLY B N     1 
ATOM   10426 C  CA    . GLY B 1 607 ? 144.781 122.430 156.176 1.00 74.32 ?  607 GLY B CA    1 
ATOM   10427 C  C     . GLY B 1 607 ? 144.374 120.982 156.363 1.00 75.00 ?  607 GLY B C     1 
ATOM   10428 O  O     . GLY B 1 607 ? 143.292 120.557 155.944 1.00 73.95 ?  607 GLY B O     1 
ATOM   10429 N  N     . ASN B 1 608 ? 145.247 120.209 157.002 1.00 78.45 ?  608 ASN B N     1 
ATOM   10430 C  CA    . ASN B 1 608 ? 144.944 118.836 157.378 1.00 78.79 ?  608 ASN B CA    1 
ATOM   10431 C  C     . ASN B 1 608 ? 144.475 118.721 158.821 1.00 78.89 ?  608 ASN B C     1 
ATOM   10432 O  O     . ASN B 1 608 ? 144.248 117.607 159.303 1.00 79.13 ?  608 ASN B O     1 
ATOM   10433 C  CB    . ASN B 1 608 ? 146.165 117.944 157.149 1.00 78.58 ?  608 ASN B CB    1 
ATOM   10434 C  CG    . ASN B 1 608 ? 146.409 117.657 155.681 1.00 79.08 ?  608 ASN B CG    1 
ATOM   10435 O  OD1   . ASN B 1 608 ? 145.532 117.863 154.843 1.00 78.71 ?  608 ASN B OD1   1 
ATOM   10436 N  ND2   . ASN B 1 608 ? 147.606 117.176 155.362 1.00 78.97 ?  608 ASN B ND2   1 
ATOM   10437 N  N     . SER B 1 609 ? 144.321 119.843 159.518 1.00 72.52 ?  609 SER B N     1 
ATOM   10438 C  CA    . SER B 1 609 ? 143.914 119.855 160.913 1.00 71.89 ?  609 SER B CA    1 
ATOM   10439 C  C     . SER B 1 609 ? 142.467 120.314 161.039 1.00 70.62 ?  609 SER B C     1 
ATOM   10440 O  O     . SER B 1 609 ? 141.898 120.917 160.126 1.00 71.68 ?  609 SER B O     1 
ATOM   10441 C  CB    . SER B 1 609 ? 144.824 120.766 161.742 1.00 69.93 ?  609 SER B CB    1 
ATOM   10442 O  OG    . SER B 1 609 ? 144.657 122.124 161.370 1.00 69.72 ?  609 SER B OG    1 
ATOM   10443 N  N     . LYS B 1 610 ? 141.874 120.010 162.188 1.00 61.32 ?  610 LYS B N     1 
ATOM   10444 C  CA    . LYS B 1 610 ? 140.521 120.435 162.511 1.00 61.43 ?  610 LYS B CA    1 
ATOM   10445 C  C     . LYS B 1 610 ? 140.543 121.243 163.801 1.00 61.84 ?  610 LYS B C     1 
ATOM   10446 O  O     . LYS B 1 610 ? 141.286 120.922 164.735 1.00 59.72 ?  610 LYS B O     1 
ATOM   10447 C  CB    . LYS B 1 610 ? 139.576 119.233 162.638 1.00 62.88 ?  610 LYS B CB    1 
ATOM   10448 C  CG    . LYS B 1 610 ? 139.864 118.311 163.811 1.00 61.41 ?  610 LYS B CG    1 
ATOM   10449 C  CD    . LYS B 1 610 ? 138.735 117.314 164.034 1.00 61.32 ?  610 LYS B CD    1 
ATOM   10450 C  CE    . LYS B 1 610 ? 137.997 116.991 162.742 1.00 61.36 ?  610 LYS B CE    1 
ATOM   10451 N  NZ    . LYS B 1 610 ? 136.850 116.071 162.970 1.00 60.10 1  610 LYS B NZ    1 
ATOM   10452 N  N     . THR B 1 611 ? 139.749 122.310 163.836 1.00 60.71 ?  611 THR B N     1 
ATOM   10453 C  CA    . THR B 1 611 ? 139.686 123.209 164.975 1.00 57.67 ?  611 THR B CA    1 
ATOM   10454 C  C     . THR B 1 611 ? 138.238 123.377 165.404 1.00 54.85 ?  611 THR B C     1 
ATOM   10455 O  O     . THR B 1 611 ? 137.317 123.275 164.589 1.00 57.03 ?  611 THR B O     1 
ATOM   10456 C  CB    . THR B 1 611 ? 140.284 124.583 164.648 1.00 58.17 ?  611 THR B CB    1 
ATOM   10457 O  OG1   . THR B 1 611 ? 139.572 125.161 163.548 1.00 58.82 ?  611 THR B OG1   1 
ATOM   10458 C  CG2   . THR B 1 611 ? 141.750 124.456 164.279 1.00 55.74 ?  611 THR B CG2   1 
ATOM   10459 N  N     . TYR B 1 612 ? 138.040 123.623 166.695 1.00 49.86 ?  612 TYR B N     1 
ATOM   10460 C  CA    . TYR B 1 612 ? 136.714 123.857 167.249 1.00 50.17 ?  612 TYR B CA    1 
ATOM   10461 C  C     . TYR B 1 612 ? 136.661 125.262 167.826 1.00 50.25 ?  612 TYR B C     1 
ATOM   10462 O  O     . TYR B 1 612 ? 137.462 125.612 168.699 1.00 51.80 ?  612 TYR B O     1 
ATOM   10463 C  CB    . TYR B 1 612 ? 136.353 122.820 168.315 1.00 52.03 ?  612 TYR B CB    1 
ATOM   10464 C  CG    . TYR B 1 612 ? 136.512 121.381 167.872 1.00 54.51 ?  612 TYR B CG    1 
ATOM   10465 C  CD1   . TYR B 1 612 ? 137.767 120.793 167.767 1.00 53.62 ?  612 TYR B CD1   1 
ATOM   10466 C  CD2   . TYR B 1 612 ? 135.404 120.623 167.523 1.00 54.03 ?  612 TYR B CD2   1 
ATOM   10467 C  CE1   . TYR B 1 612 ? 137.908 119.482 167.356 1.00 55.62 ?  612 TYR B CE1   1 
ATOM   10468 C  CE2   . TYR B 1 612 ? 135.535 119.313 167.112 1.00 54.22 ?  612 TYR B CE2   1 
ATOM   10469 C  CZ    . TYR B 1 612 ? 136.788 118.748 167.029 1.00 55.61 ?  612 TYR B CZ    1 
ATOM   10470 O  OH    . TYR B 1 612 ? 136.919 117.443 166.617 1.00 55.81 ?  612 TYR B OH    1 
ATOM   10471 N  N     . TYR B 1 613 ? 135.719 126.059 167.336 1.00 42.10 ?  613 TYR B N     1 
ATOM   10472 C  CA    . TYR B 1 613 ? 135.489 127.407 167.835 1.00 38.05 ?  613 TYR B CA    1 
ATOM   10473 C  C     . TYR B 1 613 ? 134.208 127.429 168.652 1.00 38.01 ?  613 TYR B C     1 
ATOM   10474 O  O     . TYR B 1 613 ? 133.115 127.275 168.081 1.00 36.70 ?  613 TYR B O     1 
ATOM   10475 C  CB    . TYR B 1 613 ? 135.403 128.407 166.682 1.00 38.76 ?  613 TYR B CB    1 
ATOM   10476 C  CG    . TYR B 1 613 ? 135.078 129.818 167.117 1.00 35.14 ?  613 TYR B CG    1 
ATOM   10477 C  CD1   . TYR B 1 613 ? 135.908 130.505 167.990 1.00 36.58 ?  613 TYR B CD1   1 
ATOM   10478 C  CD2   . TYR B 1 613 ? 133.942 130.465 166.650 1.00 36.96 ?  613 TYR B CD2   1 
ATOM   10479 C  CE1   . TYR B 1 613 ? 135.619 131.793 168.388 1.00 38.78 ?  613 TYR B CE1   1 
ATOM   10480 C  CE2   . TYR B 1 613 ? 133.643 131.754 167.042 1.00 39.76 ?  613 TYR B CE2   1 
ATOM   10481 C  CZ    . TYR B 1 613 ? 134.485 132.413 167.912 1.00 41.14 ?  613 TYR B CZ    1 
ATOM   10482 O  OH    . TYR B 1 613 ? 134.195 133.698 168.306 1.00 40.64 ?  613 TYR B OH    1 
ATOM   10483 N  N     . PRO B 1 614 ? 134.285 127.552 169.973 1.00 35.86 ?  614 PRO B N     1 
ATOM   10484 C  CA    . PRO B 1 614 ? 133.072 127.793 170.758 1.00 34.87 ?  614 PRO B CA    1 
ATOM   10485 C  C     . PRO B 1 614 ? 132.571 129.212 170.551 1.00 38.36 ?  614 PRO B C     1 
ATOM   10486 O  O     . PRO B 1 614 ? 133.338 130.126 170.238 1.00 39.87 ?  614 PRO B O     1 
ATOM   10487 C  CB    . PRO B 1 614 ? 133.528 127.569 172.206 1.00 33.93 ?  614 PRO B CB    1 
ATOM   10488 C  CG    . PRO B 1 614 ? 134.876 126.911 172.109 1.00 36.88 ?  614 PRO B CG    1 
ATOM   10489 C  CD    . PRO B 1 614 ? 135.470 127.384 170.827 1.00 35.12 ?  614 PRO B CD    1 
ATOM   10490 N  N     . MET B 1 615 ? 131.268 129.387 170.725 1.00 32.85 ?  615 MET B N     1 
ATOM   10491 C  CA    . MET B 1 615 ? 130.694 130.718 170.630 1.00 29.77 ?  615 MET B CA    1 
ATOM   10492 C  C     . MET B 1 615 ? 131.258 131.603 171.739 1.00 36.44 ?  615 MET B C     1 
ATOM   10493 O  O     . MET B 1 615 ? 131.554 131.112 172.834 1.00 40.66 ?  615 MET B O     1 
ATOM   10494 C  CB    . MET B 1 615 ? 129.169 130.653 170.715 1.00 30.91 ?  615 MET B CB    1 
ATOM   10495 C  CG    . MET B 1 615 ? 128.477 130.259 169.413 1.00 35.52 ?  615 MET B CG    1 
ATOM   10496 S  SD    . MET B 1 615 ? 129.298 130.832 167.907 1.00 41.17 ?  615 MET B SD    1 
ATOM   10497 C  CE    . MET B 1 615 ? 130.254 129.393 167.427 1.00 34.86 ?  615 MET B CE    1 
ATOM   10498 N  N     . PRO B 1 616 ? 131.437 132.900 171.486 1.00 37.15 ?  616 PRO B N     1 
ATOM   10499 C  CA    . PRO B 1 616 ? 132.090 133.772 172.477 1.00 33.00 ?  616 PRO B CA    1 
ATOM   10500 C  C     . PRO B 1 616 ? 131.318 133.813 173.786 1.00 35.01 ?  616 PRO B C     1 
ATOM   10501 O  O     . PRO B 1 616 ? 130.140 134.170 173.824 1.00 37.07 ?  616 PRO B O     1 
ATOM   10502 C  CB    . PRO B 1 616 ? 132.104 135.138 171.784 1.00 34.26 ?  616 PRO B CB    1 
ATOM   10503 C  CG    . PRO B 1 616 ? 131.960 134.832 170.331 1.00 33.99 ?  616 PRO B CG    1 
ATOM   10504 C  CD    . PRO B 1 616 ? 131.096 133.624 170.252 1.00 33.29 ?  616 PRO B CD    1 
ATOM   10505 N  N     . GLY B 1 617 ? 132.001 133.454 174.870 1.00 35.39 ?  617 GLY B N     1 
ATOM   10506 C  CA    . GLY B 1 617 ? 131.380 133.424 176.175 1.00 33.60 ?  617 GLY B CA    1 
ATOM   10507 C  C     . GLY B 1 617 ? 130.597 132.171 176.486 1.00 38.16 ?  617 GLY B C     1 
ATOM   10508 O  O     . GLY B 1 617 ? 129.925 132.125 177.523 1.00 41.04 ?  617 GLY B O     1 
ATOM   10509 N  N     . LEU B 1 618 ? 130.653 131.159 175.624 1.00 38.93 ?  618 LEU B N     1 
ATOM   10510 C  CA    . LEU B 1 618 ? 129.947 129.914 175.889 1.00 33.74 ?  618 LEU B CA    1 
ATOM   10511 C  C     . LEU B 1 618 ? 130.532 129.225 177.115 1.00 36.51 ?  618 LEU B C     1 
ATOM   10512 O  O     . LEU B 1 618 ? 131.752 129.138 177.278 1.00 38.95 ?  618 LEU B O     1 
ATOM   10513 C  CB    . LEU B 1 618 ? 130.024 128.990 174.673 1.00 30.87 ?  618 LEU B CB    1 
ATOM   10514 C  CG    . LEU B 1 618 ? 129.310 127.641 174.779 1.00 35.47 ?  618 LEU B CG    1 
ATOM   10515 C  CD1   . LEU B 1 618 ? 127.812 127.832 174.955 1.00 36.01 ?  618 LEU B CD1   1 
ATOM   10516 C  CD2   . LEU B 1 618 ? 129.605 126.784 173.560 1.00 35.81 ?  618 LEU B CD2   1 
ATOM   10517 N  N     . ALA B 1 619 ? 129.652 128.734 177.978 1.00 42.84 ?  619 ALA B N     1 
ATOM   10518 C  CA    . ALA B 1 619 ? 130.054 128.080 179.216 1.00 42.21 ?  619 ALA B CA    1 
ATOM   10519 C  C     . ALA B 1 619 ? 128.897 127.204 179.684 1.00 43.92 ?  619 ALA B C     1 
ATOM   10520 O  O     . ALA B 1 619 ? 127.898 127.038 178.977 1.00 49.67 ?  619 ALA B O     1 
ATOM   10521 C  CB    . ALA B 1 619 ? 130.465 129.111 180.272 1.00 41.95 ?  619 ALA B CB    1 
ATOM   10522 N  N     . SER B 1 620 ? 129.037 126.635 180.883 1.00 47.85 ?  620 SER B N     1 
ATOM   10523 C  CA    . SER B 1 620 ? 127.988 125.774 181.418 1.00 49.40 ?  620 SER B CA    1 
ATOM   10524 C  C     . SER B 1 620 ? 126.750 126.574 181.803 1.00 49.40 ?  620 SER B C     1 
ATOM   10525 O  O     . SER B 1 620 ? 125.620 126.131 181.568 1.00 51.23 ?  620 SER B O     1 
ATOM   10526 C  CB    . SER B 1 620 ? 128.515 124.994 182.621 1.00 50.49 ?  620 SER B CB    1 
ATOM   10527 O  OG    . SER B 1 620 ? 129.880 124.654 182.450 1.00 53.13 ?  620 SER B OG    1 
ATOM   10528 N  N     . ASN B 1 621 ? 126.938 127.756 182.393 1.00 47.53 ?  621 ASN B N     1 
ATOM   10529 C  CA    . ASN B 1 621 ? 125.805 128.532 182.881 1.00 49.06 ?  621 ASN B CA    1 
ATOM   10530 C  C     . ASN B 1 621 ? 125.006 129.179 181.757 1.00 50.49 ?  621 ASN B C     1 
ATOM   10531 O  O     . ASN B 1 621 ? 123.818 129.461 181.946 1.00 51.11 ?  621 ASN B O     1 
ATOM   10532 C  CB    . ASN B 1 621 ? 126.284 129.606 183.859 1.00 48.58 ?  621 ASN B CB    1 
ATOM   10533 C  CG    . ASN B 1 621 ? 127.376 130.479 183.278 1.00 51.79 ?  621 ASN B CG    1 
ATOM   10534 O  OD1   . ASN B 1 621 ? 128.161 130.034 182.441 1.00 54.59 ?  621 ASN B OD1   1 
ATOM   10535 N  ND2   . ASN B 1 621 ? 127.433 131.729 183.719 1.00 50.11 ?  621 ASN B ND2   1 
ATOM   10536 N  N     . ASN B 1 622 ? 125.619 129.417 180.599 1.00 42.43 ?  622 ASN B N     1 
ATOM   10537 C  CA    . ASN B 1 622 ? 124.935 130.034 179.469 1.00 42.64 ?  622 ASN B CA    1 
ATOM   10538 C  C     . ASN B 1 622 ? 124.900 129.107 178.258 1.00 45.50 ?  622 ASN B C     1 
ATOM   10539 O  O     . ASN B 1 622 ? 124.830 129.569 177.117 1.00 48.48 ?  622 ASN B O     1 
ATOM   10540 C  CB    . ASN B 1 622 ? 125.579 131.375 179.108 1.00 42.25 ?  622 ASN B CB    1 
ATOM   10541 C  CG    . ASN B 1 622 ? 127.053 131.249 178.757 1.00 43.85 ?  622 ASN B CG    1 
ATOM   10542 O  OD1   . ASN B 1 622 ? 127.583 130.148 178.615 1.00 45.91 ?  622 ASN B OD1   1 
ATOM   10543 N  ND2   . ASN B 1 622 ? 127.721 132.387 178.616 1.00 41.49 ?  622 ASN B ND2   1 
ATOM   10544 N  N     . TRP B 1 623 ? 124.961 127.794 178.494 1.00 40.13 ?  623 TRP B N     1 
ATOM   10545 C  CA    . TRP B 1 623 ? 124.908 126.845 177.386 1.00 38.16 ?  623 TRP B CA    1 
ATOM   10546 C  C     . TRP B 1 623 ? 123.558 126.890 176.683 1.00 39.87 ?  623 TRP B C     1 
ATOM   10547 O  O     . TRP B 1 623 ? 123.494 126.911 175.448 1.00 42.48 ?  623 TRP B O     1 
ATOM   10548 C  CB    . TRP B 1 623 ? 125.207 125.433 177.889 1.00 42.24 ?  623 TRP B CB    1 
ATOM   10549 C  CG    . TRP B 1 623 ? 125.032 124.369 176.845 1.00 40.48 ?  623 TRP B CG    1 
ATOM   10550 C  CD1   . TRP B 1 623 ? 123.881 123.706 176.534 1.00 39.05 ?  623 TRP B CD1   1 
ATOM   10551 C  CD2   . TRP B 1 623 ? 126.043 123.845 175.975 1.00 39.60 ?  623 TRP B CD2   1 
ATOM   10552 N  NE1   . TRP B 1 623 ? 124.111 122.804 175.526 1.00 40.20 ?  623 TRP B NE1   1 
ATOM   10553 C  CE2   . TRP B 1 623 ? 125.431 122.868 175.166 1.00 39.80 ?  623 TRP B CE2   1 
ATOM   10554 C  CE3   . TRP B 1 623 ? 127.405 124.106 175.802 1.00 40.04 ?  623 TRP B CE3   1 
ATOM   10555 C  CZ2   . TRP B 1 623 ? 126.132 122.155 174.197 1.00 39.15 ?  623 TRP B CZ2   1 
ATOM   10556 C  CZ3   . TRP B 1 623 ? 128.100 123.396 174.841 1.00 39.84 ?  623 TRP B CZ3   1 
ATOM   10557 C  CH2   . TRP B 1 623 ? 127.463 122.432 174.051 1.00 39.02 ?  623 TRP B CH2   1 
ATOM   10558 N  N     . PHE B 1 624 ? 122.467 126.906 177.448 1.00 44.42 ?  624 PHE B N     1 
ATOM   10559 C  CA    . PHE B 1 624 ? 121.135 126.899 176.859 1.00 44.06 ?  624 PHE B CA    1 
ATOM   10560 C  C     . PHE B 1 624 ? 120.663 128.279 176.427 1.00 41.51 ?  624 PHE B C     1 
ATOM   10561 O  O     . PHE B 1 624 ? 119.696 128.371 175.663 1.00 46.26 ?  624 PHE B O     1 
ATOM   10562 C  CB    . PHE B 1 624 ? 120.133 126.284 177.836 1.00 42.66 ?  624 PHE B CB    1 
ATOM   10563 C  CG    . PHE B 1 624 ? 120.322 124.809 178.040 1.00 44.84 ?  624 PHE B CG    1 
ATOM   10564 C  CD1   . PHE B 1 624 ? 119.823 123.903 177.120 1.00 42.91 ?  624 PHE B CD1   1 
ATOM   10565 C  CD2   . PHE B 1 624 ? 121.008 124.329 179.142 1.00 45.60 ?  624 PHE B CD2   1 
ATOM   10566 C  CE1   . PHE B 1 624 ? 119.998 122.545 177.300 1.00 42.49 ?  624 PHE B CE1   1 
ATOM   10567 C  CE2   . PHE B 1 624 ? 121.187 122.972 179.327 1.00 45.60 ?  624 PHE B CE2   1 
ATOM   10568 C  CZ    . PHE B 1 624 ? 120.681 122.079 178.404 1.00 45.64 ?  624 PHE B CZ    1 
ATOM   10569 N  N     . PHE B 1 625 ? 121.311 129.349 176.891 1.00 37.19 ?  625 PHE B N     1 
ATOM   10570 C  CA    . PHE B 1 625 ? 121.041 130.666 176.329 1.00 32.73 ?  625 PHE B CA    1 
ATOM   10571 C  C     . PHE B 1 625 ? 121.668 130.828 174.954 1.00 30.95 ?  625 PHE B C     1 
ATOM   10572 O  O     . PHE B 1 625 ? 121.198 131.652 174.162 1.00 33.43 ?  625 PHE B O     1 
ATOM   10573 C  CB    . PHE B 1 625 ? 121.539 131.759 177.274 1.00 29.88 ?  625 PHE B CB    1 
ATOM   10574 C  CG    . PHE B 1 625 ? 120.648 131.983 178.459 1.00 32.89 ?  625 PHE B CG    1 
ATOM   10575 C  CD1   . PHE B 1 625 ? 119.362 132.468 178.292 1.00 33.41 ?  625 PHE B CD1   1 
ATOM   10576 C  CD2   . PHE B 1 625 ? 121.092 131.706 179.741 1.00 33.39 ?  625 PHE B CD2   1 
ATOM   10577 C  CE1   . PHE B 1 625 ? 118.538 132.675 179.380 1.00 33.55 ?  625 PHE B CE1   1 
ATOM   10578 C  CE2   . PHE B 1 625 ? 120.272 131.911 180.832 1.00 35.07 ?  625 PHE B CE2   1 
ATOM   10579 C  CZ    . PHE B 1 625 ? 118.993 132.397 180.651 1.00 35.94 ?  625 PHE B CZ    1 
ATOM   10580 N  N     . TYR B 1 626 ? 122.711 130.061 174.654 1.00 29.75 ?  626 TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 626 ? 123.293 130.013 173.315 1.00 29.27 ?  626 TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 626 ? 122.559 129.005 172.438 1.00 32.33 ?  626 TYR B C     1 
ATOM   10583 O  O     . TYR B 1 626 ? 123.156 128.116 171.835 1.00 35.80 ?  626 TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 626 ? 124.778 129.686 173.403 1.00 31.54 ?  626 TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 626 ? 125.668 130.901 173.337 1.00 29.75 ?  626 TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 626 ? 125.777 131.640 172.168 1.00 33.90 ?  626 TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 626 ? 126.401 131.309 174.443 1.00 28.57 ?  626 TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 626 ? 126.588 132.752 172.101 1.00 30.73 ?  626 TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 626 ? 127.215 132.420 174.386 1.00 31.89 ?  626 TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 626 ? 127.305 133.137 173.211 1.00 33.56 ?  626 TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 626 ? 128.113 134.245 173.145 1.00 36.80 ?  626 TYR B OH    1 
ATOM   10592 N  N     . LYS B 1 627 ? 121.238 129.148 172.376 1.00 33.36 ?  627 LYS B N     1 
ATOM   10593 C  CA    . LYS B 1 627 ? 120.416 128.237 171.593 1.00 31.32 ?  627 LYS B CA    1 
ATOM   10594 C  C     . LYS B 1 627 ? 120.775 128.333 170.116 1.00 31.42 ?  627 LYS B C     1 
ATOM   10595 O  O     . LYS B 1 627 ? 120.946 129.426 169.571 1.00 34.42 ?  627 LYS B O     1 
ATOM   10596 C  CB    . LYS B 1 627 ? 118.939 128.560 171.805 1.00 32.93 ?  627 LYS B CB    1 
ATOM   10597 C  CG    . LYS B 1 627 ? 117.973 127.586 171.161 1.00 33.39 ?  627 LYS B CG    1 
ATOM   10598 C  CD    . LYS B 1 627 ? 116.545 127.912 171.558 1.00 30.93 ?  627 LYS B CD    1 
ATOM   10599 C  CE    . LYS B 1 627 ? 115.552 126.993 170.873 1.00 36.51 ?  627 LYS B CE    1 
ATOM   10600 N  NZ    . LYS B 1 627 ? 114.148 127.380 171.182 1.00 36.73 1  627 LYS B NZ    1 
ATOM   10601 N  N     . GLU B 1 628 ? 120.896 127.177 169.471 1.00 33.49 ?  628 GLU B N     1 
ATOM   10602 C  CA    . GLU B 1 628 ? 121.235 127.153 168.057 1.00 33.47 ?  628 GLU B CA    1 
ATOM   10603 C  C     . GLU B 1 628 ? 120.073 127.675 167.222 1.00 35.41 ?  628 GLU B C     1 
ATOM   10604 O  O     . GLU B 1 628 ? 118.900 127.500 167.564 1.00 39.24 ?  628 GLU B O     1 
ATOM   10605 C  CB    . GLU B 1 628 ? 121.614 125.739 167.621 1.00 35.21 ?  628 GLU B CB    1 
ATOM   10606 C  CG    . GLU B 1 628 ? 122.955 125.278 168.165 1.00 33.53 ?  628 GLU B CG    1 
ATOM   10607 C  CD    . GLU B 1 628 ? 123.364 123.918 167.641 1.00 41.02 ?  628 GLU B CD    1 
ATOM   10608 O  OE1   . GLU B 1 628 ? 122.724 123.430 166.685 1.00 41.66 ?  628 GLU B OE1   1 
ATOM   10609 O  OE2   . GLU B 1 628 ? 124.327 123.337 168.183 1.00 38.10 -1 628 GLU B OE2   1 
ATOM   10610 N  N     . ALA B 1 629 ? 120.417 128.331 166.111 1.00 33.48 ?  629 ALA B N     1 
ATOM   10611 C  CA    . ALA B 1 629 ? 119.408 128.987 165.286 1.00 28.50 ?  629 ALA B CA    1 
ATOM   10612 C  C     . ALA B 1 629 ? 118.424 127.985 164.697 1.00 33.82 ?  629 ALA B C     1 
ATOM   10613 O  O     . ALA B 1 629 ? 117.224 128.267 164.603 1.00 41.85 ?  629 ALA B O     1 
ATOM   10614 C  CB    . ALA B 1 629 ? 120.085 129.787 164.176 1.00 29.76 ?  629 ALA B CB    1 
ATOM   10615 N  N     . TYR B 1 630 ? 118.912 126.813 164.284 1.00 39.39 ?  630 TYR B N     1 
ATOM   10616 C  CA    . TYR B 1 630 ? 118.033 125.818 163.682 1.00 37.06 ?  630 TYR B CA    1 
ATOM   10617 C  C     . TYR B 1 630 ? 116.997 125.305 164.672 1.00 39.49 ?  630 TYR B C     1 
ATOM   10618 O  O     . TYR B 1 630 ? 115.882 124.954 164.272 1.00 42.63 ?  630 TYR B O     1 
ATOM   10619 C  CB    . TYR B 1 630 ? 118.858 124.659 163.124 1.00 34.90 ?  630 TYR B CB    1 
ATOM   10620 C  CG    . TYR B 1 630 ? 119.880 125.086 162.099 1.00 37.14 ?  630 TYR B CG    1 
ATOM   10621 C  CD1   . TYR B 1 630 ? 119.507 125.352 160.788 1.00 33.86 ?  630 TYR B CD1   1 
ATOM   10622 C  CD2   . TYR B 1 630 ? 121.218 125.226 162.440 1.00 37.66 ?  630 TYR B CD2   1 
ATOM   10623 C  CE1   . TYR B 1 630 ? 120.436 125.744 159.847 1.00 37.39 ?  630 TYR B CE1   1 
ATOM   10624 C  CE2   . TYR B 1 630 ? 122.156 125.617 161.505 1.00 36.27 ?  630 TYR B CE2   1 
ATOM   10625 C  CZ    . TYR B 1 630 ? 121.759 125.874 160.210 1.00 39.87 ?  630 TYR B CZ    1 
ATOM   10626 O  OH    . TYR B 1 630 ? 122.688 126.264 159.274 1.00 43.03 ?  630 TYR B OH    1 
ATOM   10627 N  N     . ASP B 1 631 ? 117.337 125.261 165.959 1.00 36.75 ?  631 ASP B N     1 
ATOM   10628 C  CA    . ASP B 1 631 ? 116.393 124.834 166.983 1.00 32.70 ?  631 ASP B CA    1 
ATOM   10629 C  C     . ASP B 1 631 ? 115.395 125.920 167.359 1.00 37.19 ?  631 ASP B C     1 
ATOM   10630 O  O     . ASP B 1 631 ? 114.453 125.642 168.109 1.00 39.80 ?  631 ASP B O     1 
ATOM   10631 C  CB    . ASP B 1 631 ? 117.147 124.382 168.235 1.00 34.41 ?  631 ASP B CB    1 
ATOM   10632 C  CG    . ASP B 1 631 ? 118.110 123.245 167.957 1.00 41.11 ?  631 ASP B CG    1 
ATOM   10633 O  OD1   . ASP B 1 631 ? 117.740 122.318 167.207 1.00 43.19 ?  631 ASP B OD1   1 
ATOM   10634 O  OD2   . ASP B 1 631 ? 119.241 123.280 168.487 1.00 42.19 -1 631 ASP B OD2   1 
ATOM   10635 N  N     . MET B 1 632 ? 115.572 127.138 166.856 1.00 36.47 ?  632 MET B N     1 
ATOM   10636 C  CA    . MET B 1 632 ? 114.735 128.265 167.233 1.00 32.57 ?  632 MET B CA    1 
ATOM   10637 C  C     . MET B 1 632 ? 113.503 128.354 166.344 1.00 34.91 ?  632 MET B C     1 
ATOM   10638 O  O     . MET B 1 632 ? 113.495 127.880 165.204 1.00 34.50 ?  632 MET B O     1 
ATOM   10639 C  CB    . MET B 1 632 ? 115.520 129.573 167.138 1.00 31.54 ?  632 MET B CB    1 
ATOM   10640 C  CG    . MET B 1 632 ? 116.638 129.700 168.146 1.00 36.57 ?  632 MET B CG    1 
ATOM   10641 S  SD    . MET B 1 632 ? 117.511 131.264 167.997 1.00 39.71 ?  632 MET B SD    1 
ATOM   10642 C  CE    . MET B 1 632 ? 118.279 131.361 169.606 1.00 30.53 ?  632 MET B CE    1 
ATOM   10643 N  N     . ASP B 1 633 ? 112.456 128.973 166.881 1.00 33.36 ?  633 ASP B N     1 
ATOM   10644 C  CA    . ASP B 1 633 ? 111.276 129.289 166.089 1.00 26.12 ?  633 ASP B CA    1 
ATOM   10645 C  C     . ASP B 1 633 ? 111.603 130.430 165.136 1.00 31.27 ?  633 ASP B C     1 
ATOM   10646 O  O     . ASP B 1 633 ? 111.971 131.525 165.574 1.00 37.33 ?  633 ASP B O     1 
ATOM   10647 C  CB    . ASP B 1 633 ? 110.113 129.665 167.002 1.00 28.86 ?  633 ASP B CB    1 
ATOM   10648 C  CG    . ASP B 1 633 ? 108.797 129.771 166.259 1.00 36.59 ?  633 ASP B CG    1 
ATOM   10649 O  OD1   . ASP B 1 633 ? 108.751 129.408 165.066 1.00 39.85 ?  633 ASP B OD1   1 
ATOM   10650 O  OD2   . ASP B 1 633 ? 107.805 130.220 166.870 1.00 35.97 -1 633 ASP B OD2   1 
ATOM   10651 N  N     . MET B 1 634 ? 111.476 130.177 163.833 1.00 28.97 ?  634 MET B N     1 
ATOM   10652 C  CA    . MET B 1 634 ? 111.783 131.207 162.850 1.00 19.79 ?  634 MET B CA    1 
ATOM   10653 C  C     . MET B 1 634 ? 110.833 132.393 162.938 1.00 23.83 ?  634 MET B C     1 
ATOM   10654 O  O     . MET B 1 634 ? 111.194 133.489 162.501 1.00 30.66 ?  634 MET B O     1 
ATOM   10655 C  CB    . MET B 1 634 ? 111.752 130.621 161.439 1.00 24.77 ?  634 MET B CB    1 
ATOM   10656 C  CG    . MET B 1 634 ? 113.114 130.210 160.892 1.00 26.45 ?  634 MET B CG    1 
ATOM   10657 S  SD    . MET B 1 634 ? 114.446 131.346 161.328 1.00 40.68 ?  634 MET B SD    1 
ATOM   10658 C  CE    . MET B 1 634 ? 115.308 130.403 162.584 1.00 27.98 ?  634 MET B CE    1 
ATOM   10659 N  N     . PHE B 1 635 ? 109.635 132.203 163.493 1.00 22.81 ?  635 PHE B N     1 
ATOM   10660 C  CA    . PHE B 1 635 ? 108.709 133.321 163.648 1.00 23.82 ?  635 PHE B CA    1 
ATOM   10661 C  C     . PHE B 1 635 ? 109.225 134.326 164.672 1.00 20.23 ?  635 PHE B C     1 
ATOM   10662 O  O     . PHE B 1 635 ? 109.118 135.540 164.468 1.00 23.00 ?  635 PHE B O     1 
ATOM   10663 C  CB    . PHE B 1 635 ? 107.328 132.804 164.046 1.00 22.81 ?  635 PHE B CB    1 
ATOM   10664 C  CG    . PHE B 1 635 ? 106.443 132.482 162.877 1.00 23.55 ?  635 PHE B CG    1 
ATOM   10665 C  CD1   . PHE B 1 635 ? 106.951 131.817 161.773 1.00 25.61 ?  635 PHE B CD1   1 
ATOM   10666 C  CD2   . PHE B 1 635 ? 105.107 132.841 162.881 1.00 24.32 ?  635 PHE B CD2   1 
ATOM   10667 C  CE1   . PHE B 1 635 ? 106.142 131.518 160.694 1.00 22.74 ?  635 PHE B CE1   1 
ATOM   10668 C  CE2   . PHE B 1 635 ? 104.294 132.545 161.804 1.00 25.49 ?  635 PHE B CE2   1 
ATOM   10669 C  CZ    . PHE B 1 635 ? 104.813 131.882 160.709 1.00 23.57 ?  635 PHE B CZ    1 
ATOM   10670 N  N     . LYS B 1 636 ? 109.807 133.842 165.770 1.00 26.75 ?  636 LYS B N     1 
ATOM   10671 C  CA    . LYS B 1 636 ? 110.366 134.747 166.766 1.00 29.79 ?  636 LYS B CA    1 
ATOM   10672 C  C     . LYS B 1 636 ? 111.654 135.401 166.278 1.00 26.40 ?  636 LYS B C     1 
ATOM   10673 O  O     . LYS B 1 636 ? 111.933 136.554 166.629 1.00 29.33 ?  636 LYS B O     1 
ATOM   10674 C  CB    . LYS B 1 636 ? 110.601 133.995 168.075 1.00 27.22 ?  636 LYS B CB    1 
ATOM   10675 C  CG    . LYS B 1 636 ? 109.321 133.445 168.685 1.00 27.67 ?  636 LYS B CG    1 
ATOM   10676 C  CD    . LYS B 1 636 ? 109.552 132.890 170.077 1.00 33.78 ?  636 LYS B CD    1 
ATOM   10677 C  CE    . LYS B 1 636 ? 108.296 132.235 170.624 1.00 33.82 ?  636 LYS B CE    1 
ATOM   10678 N  NZ    . LYS B 1 636 ? 108.551 131.539 171.914 1.00 35.15 1  636 LYS B NZ    1 
ATOM   10679 N  N     . VAL B 1 637 ? 112.434 134.699 165.455 1.00 22.60 ?  637 VAL B N     1 
ATOM   10680 C  CA    . VAL B 1 637 ? 113.580 135.334 164.814 1.00 19.51 ?  637 VAL B CA    1 
ATOM   10681 C  C     . VAL B 1 637 ? 113.112 136.424 163.857 1.00 25.77 ?  637 VAL B C     1 
ATOM   10682 O  O     . VAL B 1 637 ? 113.731 137.490 163.761 1.00 26.46 ?  637 VAL B O     1 
ATOM   10683 C  CB    . VAL B 1 637 ? 114.447 134.281 164.102 1.00 19.65 ?  637 VAL B CB    1 
ATOM   10684 C  CG1   . VAL B 1 637 ? 115.731 134.908 163.589 1.00 20.23 ?  637 VAL B CG1   1 
ATOM   10685 C  CG2   . VAL B 1 637 ? 114.758 133.129 165.043 1.00 24.93 ?  637 VAL B CG2   1 
ATOM   10686 N  N     . VAL B 1 638 ? 112.013 136.179 163.141 1.00 20.68 ?  638 VAL B N     1 
ATOM   10687 C  CA    . VAL B 1 638 ? 111.428 137.209 162.286 1.00 20.02 ?  638 VAL B CA    1 
ATOM   10688 C  C     . VAL B 1 638 ? 110.980 138.400 163.121 1.00 20.80 ?  638 VAL B C     1 
ATOM   10689 O  O     . VAL B 1 638 ? 111.150 139.557 162.722 1.00 28.07 ?  638 VAL B O     1 
ATOM   10690 C  CB    . VAL B 1 638 ? 110.259 136.626 161.465 1.00 22.27 ?  638 VAL B CB    1 
ATOM   10691 C  CG1   . VAL B 1 638 ? 109.387 137.738 160.910 1.00 16.86 ?  638 VAL B CG1   1 
ATOM   10692 C  CG2   . VAL B 1 638 ? 110.776 135.750 160.340 1.00 18.92 ?  638 VAL B CG2   1 
ATOM   10693 N  N     . ASP B 1 639 ? 110.389 138.134 164.287 1.00 21.40 ?  639 ASP B N     1 
ATOM   10694 C  CA    . ASP B 1 639 ? 109.985 139.215 165.181 1.00 16.39 ?  639 ASP B CA    1 
ATOM   10695 C  C     . ASP B 1 639 ? 111.184 140.047 165.619 1.00 22.64 ?  639 ASP B C     1 
ATOM   10696 O  O     . ASP B 1 639 ? 111.127 141.282 165.620 1.00 31.87 ?  639 ASP B O     1 
ATOM   10697 C  CB    . ASP B 1 639 ? 109.260 138.644 166.399 1.00 20.16 ?  639 ASP B CB    1 
ATOM   10698 C  CG    . ASP B 1 639 ? 107.832 138.255 166.096 1.00 30.99 ?  639 ASP B CG    1 
ATOM   10699 O  OD1   . ASP B 1 639 ? 107.179 138.961 165.299 1.00 30.17 ?  639 ASP B OD1   1 
ATOM   10700 O  OD2   . ASP B 1 639 ? 107.358 137.245 166.657 1.00 33.70 -1 639 ASP B OD2   1 
ATOM   10701 N  N     . MET B 1 640 ? 112.282 139.383 165.990 1.00 20.10 ?  640 MET B N     1 
ATOM   10702 C  CA    . MET B 1 640 ? 113.502 140.101 166.352 1.00 16.85 ?  640 MET B CA    1 
ATOM   10703 C  C     . MET B 1 640 ? 114.017 140.943 165.193 1.00 18.80 ?  640 MET B C     1 
ATOM   10704 O  O     . MET B 1 640 ? 114.399 142.107 165.372 1.00 24.56 ?  640 MET B O     1 
ATOM   10705 C  CB    . MET B 1 640 ? 114.580 139.119 166.804 1.00 18.97 ?  640 MET B CB    1 
ATOM   10706 C  CG    . MET B 1 640 ? 115.886 139.802 167.169 1.00 23.29 ?  640 MET B CG    1 
ATOM   10707 S  SD    . MET B 1 640 ? 115.883 140.578 168.789 1.00 26.94 ?  640 MET B SD    1 
ATOM   10708 C  CE    . MET B 1 640 ? 116.547 139.244 169.768 1.00 20.08 ?  640 MET B CE    1 
ATOM   10709 N  N     . ILE B 1 641 ? 114.052 140.362 163.994 1.00 22.96 ?  641 ILE B N     1 
ATOM   10710 C  CA    . ILE B 1 641 ? 114.616 141.075 162.855 1.00 18.61 ?  641 ILE B CA    1 
ATOM   10711 C  C     . ILE B 1 641 ? 113.740 142.261 162.481 1.00 17.77 ?  641 ILE B C     1 
ATOM   10712 O  O     . ILE B 1 641 ? 114.245 143.316 162.099 1.00 25.68 ?  641 ILE B O     1 
ATOM   10713 C  CB    . ILE B 1 641 ? 114.836 140.118 161.668 1.00 23.86 ?  641 ILE B CB    1 
ATOM   10714 C  CG1   . ILE B 1 641 ? 115.819 139.013 162.056 1.00 22.05 ?  641 ILE B CG1   1 
ATOM   10715 C  CG2   . ILE B 1 641 ? 115.389 140.869 160.472 1.00 13.33 ?  641 ILE B CG2   1 
ATOM   10716 C  CD1   . ILE B 1 641 ? 117.003 139.502 162.859 1.00 20.77 ?  641 ILE B CD1   1 
ATOM   10717 N  N     . ALA B 1 642 ? 112.418 142.120 162.607 1.00 9.77  ?  642 ALA B N     1 
ATOM   10718 C  CA    . ALA B 1 642 ? 111.524 143.247 162.354 1.00 17.35 ?  642 ALA B CA    1 
ATOM   10719 C  C     . ALA B 1 642 ? 111.692 144.336 163.407 1.00 19.47 ?  642 ALA B C     1 
ATOM   10720 O  O     . ALA B 1 642 ? 111.663 145.535 163.087 1.00 29.13 ?  642 ALA B O     1 
ATOM   10721 C  CB    . ALA B 1 642 ? 110.075 142.766 162.307 1.00 23.44 ?  642 ALA B CB    1 
ATOM   10722 N  N     . THR B 1 643 ? 111.870 143.938 164.670 1.00 13.83 ?  643 THR B N     1 
ATOM   10723 C  CA    . THR B 1 643 ? 112.109 144.911 165.730 1.00 15.50 ?  643 THR B CA    1 
ATOM   10724 C  C     . THR B 1 643 ? 113.380 145.705 165.468 1.00 18.38 ?  643 THR B C     1 
ATOM   10725 O  O     . THR B 1 643 ? 113.412 146.925 165.664 1.00 22.78 ?  643 THR B O     1 
ATOM   10726 C  CB    . THR B 1 643 ? 112.189 144.199 167.080 1.00 18.85 ?  643 THR B CB    1 
ATOM   10727 O  OG1   . THR B 1 643 ? 110.970 143.485 167.320 1.00 23.42 ?  643 THR B OG1   1 
ATOM   10728 C  CG2   . THR B 1 643 ? 112.410 145.197 168.199 1.00 17.01 ?  643 THR B CG2   1 
ATOM   10729 N  N     . ILE B 1 644 ? 114.441 145.031 165.029 1.00 16.84 ?  644 ILE B N     1 
ATOM   10730 C  CA    . ILE B 1 644 ? 115.666 145.740 164.673 1.00 12.86 ?  644 ILE B CA    1 
ATOM   10731 C  C     . ILE B 1 644 ? 115.454 146.584 163.420 1.00 16.93 ?  644 ILE B C     1 
ATOM   10732 O  O     . ILE B 1 644 ? 115.941 147.717 163.326 1.00 23.05 ?  644 ILE B O     1 
ATOM   10733 C  CB    . ILE B 1 644 ? 116.828 144.748 164.498 1.00 14.99 ?  644 ILE B CB    1 
ATOM   10734 C  CG1   . ILE B 1 644 ? 117.035 143.936 165.775 1.00 15.83 ?  644 ILE B CG1   1 
ATOM   10735 C  CG2   . ILE B 1 644 ? 118.097 145.483 164.123 1.00 10.19 ?  644 ILE B CG2   1 
ATOM   10736 C  CD1   . ILE B 1 644 ? 117.931 142.737 165.589 1.00 18.65 ?  644 ILE B CD1   1 
ATOM   10737 N  N     . GLN B 1 645 ? 114.712 146.049 162.447 1.00 7.72  ?  645 GLN B N     1 
ATOM   10738 C  CA    . GLN B 1 645 ? 114.550 146.689 161.149 1.00 14.27 ?  645 GLN B CA    1 
ATOM   10739 C  C     . GLN B 1 645 ? 113.781 147.995 161.254 1.00 20.95 ?  645 GLN B C     1 
ATOM   10740 O  O     . GLN B 1 645 ? 113.998 148.906 160.447 1.00 28.01 ?  645 GLN B O     1 
ATOM   10741 C  CB    . GLN B 1 645 ? 113.837 145.730 160.197 1.00 12.79 ?  645 GLN B CB    1 
ATOM   10742 C  CG    . GLN B 1 645 ? 113.657 146.251 158.789 1.00 10.57 ?  645 GLN B CG    1 
ATOM   10743 C  CD    . GLN B 1 645 ? 114.903 146.074 157.954 1.00 15.11 ?  645 GLN B CD    1 
ATOM   10744 O  OE1   . GLN B 1 645 ? 115.744 146.963 157.886 1.00 8.69  ?  645 GLN B OE1   1 
ATOM   10745 N  NE2   . GLN B 1 645 ? 115.027 144.919 157.312 1.00 17.69 ?  645 GLN B NE2   1 
ATOM   10746 N  N     . GLN B 1 646 ? 112.882 148.102 162.232 1.00 18.85 ?  646 GLN B N     1 
ATOM   10747 C  CA    . GLN B 1 646 ? 112.142 149.348 162.397 1.00 16.53 ?  646 GLN B CA    1 
ATOM   10748 C  C     . GLN B 1 646 ? 113.060 150.529 162.701 1.00 13.75 ?  646 GLN B C     1 
ATOM   10749 O  O     . GLN B 1 646 ? 112.656 151.677 162.496 1.00 21.39 ?  646 GLN B O     1 
ATOM   10750 C  CB    . GLN B 1 646 ? 111.088 149.189 163.493 1.00 19.98 ?  646 GLN B CB    1 
ATOM   10751 C  CG    . GLN B 1 646 ? 111.604 149.388 164.897 1.00 21.39 ?  646 GLN B CG    1 
ATOM   10752 C  CD    . GLN B 1 646 ? 110.543 149.125 165.944 1.00 27.82 ?  646 GLN B CD    1 
ATOM   10753 O  OE1   . GLN B 1 646 ? 110.659 148.197 166.743 1.00 25.23 ?  646 GLN B OE1   1 
ATOM   10754 N  NE2   . GLN B 1 646 ? 109.498 149.943 165.944 1.00 27.04 ?  646 GLN B NE2   1 
ATOM   10755 N  N     . HIS B 1 647 ? 114.286 150.277 163.159 1.00 22.19 ?  647 HIS B N     1 
ATOM   10756 C  CA    . HIS B 1 647 ? 115.251 151.332 163.440 1.00 19.27 ?  647 HIS B CA    1 
ATOM   10757 C  C     . HIS B 1 647 ? 116.398 151.382 162.440 1.00 16.97 ?  647 HIS B C     1 
ATOM   10758 O  O     . HIS B 1 647 ? 117.291 152.222 162.587 1.00 22.98 ?  647 HIS B O     1 
ATOM   10759 C  CB    . HIS B 1 647 ? 115.817 151.167 164.854 1.00 13.76 ?  647 HIS B CB    1 
ATOM   10760 C  CG    . HIS B 1 647 ? 114.769 151.081 165.917 1.00 17.51 ?  647 HIS B CG    1 
ATOM   10761 N  ND1   . HIS B 1 647 ? 113.931 152.132 166.220 1.00 13.19 ?  647 HIS B ND1   1 
ATOM   10762 C  CD2   . HIS B 1 647 ? 114.424 150.071 166.749 1.00 16.95 ?  647 HIS B CD2   1 
ATOM   10763 C  CE1   . HIS B 1 647 ? 113.113 151.772 167.192 1.00 19.01 ?  647 HIS B CE1   1 
ATOM   10764 N  NE2   . HIS B 1 647 ? 113.391 150.527 167.531 1.00 21.98 ?  647 HIS B NE2   1 
ATOM   10765 N  N     . ILE B 1 648 ? 116.402 150.515 161.432 1.00 12.68 ?  648 ILE B N     1 
ATOM   10766 C  CA    . ILE B 1 648 ? 117.453 150.468 160.422 1.00 11.44 ?  648 ILE B CA    1 
ATOM   10767 C  C     . ILE B 1 648 ? 116.874 150.986 159.113 1.00 16.81 ?  648 ILE B C     1 
ATOM   10768 O  O     . ILE B 1 648 ? 115.852 150.476 158.637 1.00 27.46 ?  648 ILE B O     1 
ATOM   10769 C  CB    . ILE B 1 648 ? 118.012 149.043 160.259 1.00 13.28 ?  648 ILE B CB    1 
ATOM   10770 C  CG1   . ILE B 1 648 ? 118.517 148.507 161.599 1.00 16.65 ?  648 ILE B CG1   1 
ATOM   10771 C  CG2   . ILE B 1 648 ? 119.126 149.018 159.231 1.00 5.40  ?  648 ILE B CG2   1 
ATOM   10772 C  CD1   . ILE B 1 648 ? 119.664 149.296 162.182 1.00 8.73  ?  648 ILE B CD1   1 
ATOM   10773 N  N     . ASP B 1 649 ? 117.521 152.001 158.537 1.00 12.87 ?  649 ASP B N     1 
ATOM   10774 C  CA    . ASP B 1 649 ? 116.999 152.611 157.316 1.00 7.33  ?  649 ASP B CA    1 
ATOM   10775 C  C     . ASP B 1 649 ? 117.203 151.711 156.103 1.00 10.36 ?  649 ASP B C     1 
ATOM   10776 O  O     . ASP B 1 649 ? 116.341 151.654 155.221 1.00 29.65 ?  649 ASP B O     1 
ATOM   10777 C  CB    . ASP B 1 649 ? 117.647 153.977 157.090 1.00 16.59 ?  649 ASP B CB    1 
ATOM   10778 C  CG    . ASP B 1 649 ? 119.134 153.969 157.358 1.00 16.75 ?  649 ASP B CG    1 
ATOM   10779 O  OD1   . ASP B 1 649 ? 119.539 153.451 158.417 1.00 20.57 ?  649 ASP B OD1   1 
ATOM   10780 O  OD2   . ASP B 1 649 ? 119.895 154.486 156.519 1.00 15.48 -1 649 ASP B OD2   1 
ATOM   10781 N  N     . GLN B 1 650 ? 118.330 151.014 156.036 1.00 12.34 ?  650 GLN B N     1 
ATOM   10782 C  CA    . GLN B 1 650 ? 118.548 150.002 155.013 1.00 3.46  ?  650 GLN B CA    1 
ATOM   10783 C  C     . GLN B 1 650 ? 118.073 148.656 155.560 1.00 7.97  ?  650 GLN B C     1 
ATOM   10784 O  O     . GLN B 1 650 ? 117.374 148.601 156.573 1.00 18.13 ?  650 GLN B O     1 
ATOM   10785 C  CB    . GLN B 1 650 ? 120.015 149.995 154.581 1.00 7.16  ?  650 GLN B CB    1 
ATOM   10786 C  CG    . GLN B 1 650 ? 120.501 151.317 154.031 1.00 8.51  ?  650 GLN B CG    1 
ATOM   10787 C  CD    . GLN B 1 650 ? 121.944 151.257 153.584 1.00 13.48 ?  650 GLN B CD    1 
ATOM   10788 O  OE1   . GLN B 1 650 ? 122.260 150.669 152.552 1.00 18.42 ?  650 GLN B OE1   1 
ATOM   10789 N  NE2   . GLN B 1 650 ? 122.829 151.870 154.359 1.00 6.77  ?  650 GLN B NE2   1 
ATOM   10790 N  N     . GLY B 1 651 ? 118.428 147.560 154.894 1.00 7.27  ?  651 GLY B N     1 
ATOM   10791 C  CA    . GLY B 1 651 ? 117.965 146.251 155.295 1.00 8.37  ?  651 GLY B CA    1 
ATOM   10792 C  C     . GLY B 1 651 ? 118.923 145.534 156.227 1.00 7.98  ?  651 GLY B C     1 
ATOM   10793 O  O     . GLY B 1 651 ? 119.963 146.048 156.636 1.00 12.97 ?  651 GLY B O     1 
ATOM   10794 N  N     . ILE B 1 652 ? 118.538 144.309 156.571 1.00 12.55 ?  652 ILE B N     1 
ATOM   10795 C  CA    . ILE B 1 652 ? 119.318 143.421 157.422 1.00 11.63 ?  652 ILE B CA    1 
ATOM   10796 C  C     . ILE B 1 652 ? 119.457 142.093 156.697 1.00 14.25 ?  652 ILE B C     1 
ATOM   10797 O  O     . ILE B 1 652 ? 118.468 141.558 156.186 1.00 25.45 ?  652 ILE B O     1 
ATOM   10798 C  CB    . ILE B 1 652 ? 118.654 143.213 158.796 1.00 6.36  ?  652 ILE B CB    1 
ATOM   10799 C  CG1   . ILE B 1 652 ? 118.375 144.555 159.473 1.00 6.35  ?  652 ILE B CG1   1 
ATOM   10800 C  CG2   . ILE B 1 652 ? 119.515 142.329 159.680 1.00 10.09 ?  652 ILE B CG2   1 
ATOM   10801 C  CD1   . ILE B 1 652 ? 117.473 144.443 160.675 1.00 9.76  ?  652 ILE B CD1   1 
ATOM   10802 N  N     . SER B 1 653 ? 120.674 141.563 156.650 1.00 5.70  ?  653 SER B N     1 
ATOM   10803 C  CA    . SER B 1 653 ? 120.902 140.267 156.017 1.00 12.44 ?  653 SER B CA    1 
ATOM   10804 C  C     . SER B 1 653 ? 120.292 139.194 156.907 1.00 19.34 ?  653 SER B C     1 
ATOM   10805 O  O     . SER B 1 653 ? 120.916 138.725 157.861 1.00 23.48 ?  653 SER B O     1 
ATOM   10806 C  CB    . SER B 1 653 ? 122.389 140.029 155.797 1.00 12.43 ?  653 SER B CB    1 
ATOM   10807 O  OG    . SER B 1 653 ? 122.819 140.621 154.585 1.00 21.12 ?  653 SER B OG    1 
ATOM   10808 N  N     . PHE B 1 654 ? 119.061 138.805 156.593 1.00 19.33 ?  654 PHE B N     1 
ATOM   10809 C  CA    . PHE B 1 654 ? 118.277 137.895 157.420 1.00 12.91 ?  654 PHE B CA    1 
ATOM   10810 C  C     . PHE B 1 654 ? 118.350 136.503 156.803 1.00 16.26 ?  654 PHE B C     1 
ATOM   10811 O  O     . PHE B 1 654 ? 117.692 136.218 155.800 1.00 25.36 ?  654 PHE B O     1 
ATOM   10812 C  CB    . PHE B 1 654 ? 116.840 138.392 157.533 1.00 13.27 ?  654 PHE B CB    1 
ATOM   10813 C  CG    . PHE B 1 654 ? 115.974 137.562 158.433 1.00 16.91 ?  654 PHE B CG    1 
ATOM   10814 C  CD1   . PHE B 1 654 ? 116.528 136.734 159.393 1.00 18.96 ?  654 PHE B CD1   1 
ATOM   10815 C  CD2   . PHE B 1 654 ? 114.598 137.615 158.318 1.00 17.86 ?  654 PHE B CD2   1 
ATOM   10816 C  CE1   . PHE B 1 654 ? 115.726 135.973 160.215 1.00 19.71 ?  654 PHE B CE1   1 
ATOM   10817 C  CE2   . PHE B 1 654 ? 113.793 136.859 159.138 1.00 17.55 ?  654 PHE B CE2   1 
ATOM   10818 C  CZ    . PHE B 1 654 ? 114.357 136.038 160.089 1.00 16.60 ?  654 PHE B CZ    1 
ATOM   10819 N  N     . THR B 1 655 ? 119.147 135.635 157.415 1.00 21.60 ?  655 THR B N     1 
ATOM   10820 C  CA    . THR B 1 655 ? 119.249 134.246 156.998 1.00 22.15 ?  655 THR B CA    1 
ATOM   10821 C  C     . THR B 1 655 ? 118.219 133.415 157.752 1.00 22.47 ?  655 THR B C     1 
ATOM   10822 O  O     . THR B 1 655 ? 118.119 133.505 158.979 1.00 27.99 ?  655 THR B O     1 
ATOM   10823 C  CB    . THR B 1 655 ? 120.657 133.707 157.255 1.00 24.56 ?  655 THR B CB    1 
ATOM   10824 O  OG1   . THR B 1 655 ? 121.593 134.389 156.412 1.00 31.42 ?  655 THR B OG1   1 
ATOM   10825 C  CG2   . THR B 1 655 ? 120.723 132.215 156.971 1.00 24.12 ?  655 THR B CG2   1 
ATOM   10826 N  N     . LEU B 1 656 ? 117.449 132.622 157.016 1.00 28.74 ?  656 LEU B N     1 
ATOM   10827 C  CA    . LEU B 1 656 ? 116.507 131.690 157.618 1.00 31.33 ?  656 LEU B CA    1 
ATOM   10828 C  C     . LEU B 1 656 ? 117.229 130.389 157.935 1.00 24.98 ?  656 LEU B C     1 
ATOM   10829 O  O     . LEU B 1 656 ? 118.002 129.887 157.114 1.00 30.77 ?  656 LEU B O     1 
ATOM   10830 C  CB    . LEU B 1 656 ? 115.323 131.431 156.688 1.00 28.54 ?  656 LEU B CB    1 
ATOM   10831 C  CG    . LEU B 1 656 ? 114.413 132.633 156.434 1.00 29.96 ?  656 LEU B CG    1 
ATOM   10832 C  CD1   . LEU B 1 656 ? 113.220 132.233 155.585 1.00 27.74 ?  656 LEU B CD1   1 
ATOM   10833 C  CD2   . LEU B 1 656 ? 113.960 133.255 157.746 1.00 26.15 ?  656 LEU B CD2   1 
ATOM   10834 N  N     . PHE B 1 657 ? 116.998 129.864 159.132 1.00 25.49 ?  657 PHE B N     1 
ATOM   10835 C  CA    . PHE B 1 657 ? 117.643 128.642 159.600 1.00 29.93 ?  657 PHE B CA    1 
ATOM   10836 C  C     . PHE B 1 657 ? 116.565 127.579 159.749 1.00 34.81 ?  657 PHE B C     1 
ATOM   10837 O  O     . PHE B 1 657 ? 115.735 127.651 160.661 1.00 38.68 ?  657 PHE B O     1 
ATOM   10838 C  CB    . PHE B 1 657 ? 118.379 128.892 160.912 1.00 28.95 ?  657 PHE B CB    1 
ATOM   10839 C  CG    . PHE B 1 657 ? 119.389 129.998 160.831 1.00 33.74 ?  657 PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 1 657 ? 120.666 129.754 160.357 1.00 32.30 ?  657 PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 1 657 ? 119.059 131.287 161.216 1.00 33.75 ?  657 PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 1 657 ? 121.595 130.773 160.275 1.00 32.19 ?  657 PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 1 657 ? 119.984 132.307 161.140 1.00 31.68 ?  657 PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 1 657 ? 121.254 132.050 160.668 1.00 31.73 ?  657 PHE B CZ    1 
ATOM   10845 N  N     . LEU B 1 658 ? 116.581 126.595 158.857 1.00 35.52 ?  658 LEU B N     1 
ATOM   10846 C  CA    . LEU B 1 658 ? 115.490 125.646 158.720 1.00 38.84 ?  658 LEU B CA    1 
ATOM   10847 C  C     . LEU B 1 658 ? 115.961 124.245 159.084 1.00 42.86 ?  658 LEU B C     1 
ATOM   10848 O  O     . LEU B 1 658 ? 117.144 123.916 158.960 1.00 42.45 ?  658 LEU B O     1 
ATOM   10849 C  CB    . LEU B 1 658 ? 114.952 125.650 157.288 1.00 38.92 ?  658 LEU B CB    1 
ATOM   10850 C  CG    . LEU B 1 658 ? 114.631 127.025 156.697 1.00 36.73 ?  658 LEU B CG    1 
ATOM   10851 C  CD1   . LEU B 1 658 ? 114.786 126.981 155.187 1.00 36.74 ?  658 LEU B CD1   1 
ATOM   10852 C  CD2   . LEU B 1 658 ? 113.254 127.526 157.088 1.00 34.53 ?  658 LEU B CD2   1 
ATOM   10853 N  N     . LYS B 1 659 ? 115.024 123.428 159.552 1.00 46.82 ?  659 LYS B N     1 
ATOM   10854 C  CA    . LYS B 1 659 ? 115.277 122.015 159.776 1.00 45.01 ?  659 LYS B CA    1 
ATOM   10855 C  C     . LYS B 1 659 ? 114.896 121.215 158.538 1.00 47.48 ?  659 LYS B C     1 
ATOM   10856 O  O     . LYS B 1 659 ? 114.060 121.636 157.733 1.00 49.57 ?  659 LYS B O     1 
ATOM   10857 C  CB    . LYS B 1 659 ? 114.499 121.505 160.988 1.00 45.65 ?  659 LYS B CB    1 
ATOM   10858 C  CG    . LYS B 1 659 ? 114.914 122.134 162.306 1.00 46.86 ?  659 LYS B CG    1 
ATOM   10859 C  CD    . LYS B 1 659 ? 114.229 121.450 163.478 1.00 49.12 ?  659 LYS B CD    1 
ATOM   10860 C  CE    . LYS B 1 659 ? 114.682 122.037 164.804 1.00 46.79 ?  659 LYS B CE    1 
ATOM   10861 N  NZ    . LYS B 1 659 ? 114.288 121.183 165.959 1.00 49.98 1  659 LYS B NZ    1 
ATOM   10862 N  N     . ASP B 1 660 ? 115.529 120.049 158.387 1.00 53.65 ?  660 ASP B N     1 
ATOM   10863 C  CA    . ASP B 1 660 ? 115.233 119.183 157.251 1.00 52.62 ?  660 ASP B CA    1 
ATOM   10864 C  C     . ASP B 1 660 ? 113.816 118.627 157.299 1.00 51.96 ?  660 ASP B C     1 
ATOM   10865 O  O     . ASP B 1 660 ? 113.252 118.310 156.246 1.00 51.23 ?  660 ASP B O     1 
ATOM   10866 C  CB    . ASP B 1 660 ? 116.241 118.033 157.195 1.00 53.34 ?  660 ASP B CB    1 
ATOM   10867 C  CG    . ASP B 1 660 ? 117.297 118.234 156.127 1.00 55.56 ?  660 ASP B CG    1 
ATOM   10868 O  OD1   . ASP B 1 660 ? 117.009 118.924 155.127 1.00 54.48 ?  660 ASP B OD1   1 
ATOM   10869 O  OD2   . ASP B 1 660 ? 118.416 117.703 156.287 1.00 53.90 -1 660 ASP B OD2   1 
ATOM   10870 N  N     . THR B 1 661 ? 113.231 118.504 158.492 1.00 52.85 ?  661 THR B N     1 
ATOM   10871 C  CA    . THR B 1 661 ? 111.907 117.903 158.614 1.00 52.27 ?  661 THR B CA    1 
ATOM   10872 C  C     . THR B 1 661 ? 110.825 118.800 158.024 1.00 52.80 ?  661 THR B C     1 
ATOM   10873 O  O     . THR B 1 661 ? 109.852 118.307 157.443 1.00 55.96 ?  661 THR B O     1 
ATOM   10874 C  CB    . THR B 1 661 ? 111.602 117.598 160.080 1.00 53.12 ?  661 THR B CB    1 
ATOM   10875 O  OG1   . THR B 1 661 ? 111.778 118.785 160.863 1.00 54.39 ?  661 THR B OG1   1 
ATOM   10876 C  CG2   . THR B 1 661 ? 112.528 116.511 160.601 1.00 52.13 ?  661 THR B CG2   1 
ATOM   10877 N  N     . MET B 1 662 ? 110.973 120.114 158.165 1.00 51.33 ?  662 MET B N     1 
ATOM   10878 C  CA    . MET B 1 662 ? 109.932 121.032 157.728 1.00 52.61 ?  662 MET B CA    1 
ATOM   10879 C  C     . MET B 1 662 ? 109.853 121.088 156.205 1.00 51.05 ?  662 MET B C     1 
ATOM   10880 O  O     . MET B 1 662 ? 110.825 120.819 155.495 1.00 52.14 ?  662 MET B O     1 
ATOM   10881 C  CB    . MET B 1 662 ? 110.178 122.425 158.306 1.00 51.42 ?  662 MET B CB    1 
ATOM   10882 C  CG    . MET B 1 662 ? 111.158 123.276 157.526 1.00 49.54 ?  662 MET B CG    1 
ATOM   10883 S  SD    . MET B 1 662 ? 111.376 124.886 158.301 1.00 59.95 ?  662 MET B SD    1 
ATOM   10884 C  CE    . MET B 1 662 ? 111.206 124.463 160.034 1.00 49.08 ?  662 MET B CE    1 
ATOM   10885 N  N     . THR B 1 663 ? 108.669 121.437 155.709 1.00 43.99 ?  663 THR B N     1 
ATOM   10886 C  CA    . THR B 1 663 ? 108.354 121.387 154.292 1.00 44.61 ?  663 THR B CA    1 
ATOM   10887 C  C     . THR B 1 663 ? 108.503 122.771 153.662 1.00 44.35 ?  663 THR B C     1 
ATOM   10888 O  O     . THR B 1 663 ? 108.812 123.760 154.329 1.00 47.40 ?  663 THR B O     1 
ATOM   10889 C  CB    . THR B 1 663 ? 106.938 120.847 154.084 1.00 44.65 ?  663 THR B CB    1 
ATOM   10890 O  OG1   . THR B 1 663 ? 105.996 121.730 154.705 1.00 46.81 ?  663 THR B OG1   1 
ATOM   10891 C  CG2   . THR B 1 663 ? 106.803 119.467 154.703 1.00 45.09 ?  663 THR B CG2   1 
ATOM   10892 N  N     . THR B 1 664 ? 108.282 122.833 152.345 1.00 36.56 ?  664 THR B N     1 
ATOM   10893 C  CA    . THR B 1 664 ? 108.293 124.120 151.657 1.00 37.93 ?  664 THR B CA    1 
ATOM   10894 C  C     . THR B 1 664 ? 107.139 125.002 152.110 1.00 36.91 ?  664 THR B C     1 
ATOM   10895 O  O     . THR B 1 664 ? 107.215 126.230 152.000 1.00 39.76 ?  664 THR B O     1 
ATOM   10896 C  CB    . THR B 1 664 ? 108.235 123.918 150.142 1.00 37.84 ?  664 THR B CB    1 
ATOM   10897 O  OG1   . THR B 1 664 ? 106.963 123.364 149.780 1.00 38.33 ?  664 THR B OG1   1 
ATOM   10898 C  CG2   . THR B 1 664 ? 109.342 122.983 149.684 1.00 37.08 ?  664 THR B CG2   1 
ATOM   10899 N  N     . ARG B 1 665 ? 106.061 124.396 152.612 1.00 39.50 ?  665 ARG B N     1 
ATOM   10900 C  CA    . ARG B 1 665 ? 104.955 125.177 153.157 1.00 37.27 ?  665 ARG B CA    1 
ATOM   10901 C  C     . ARG B 1 665 ? 105.384 125.941 154.402 1.00 40.60 ?  665 ARG B C     1 
ATOM   10902 O  O     . ARG B 1 665 ? 104.970 127.086 154.605 1.00 42.67 ?  665 ARG B O     1 
ATOM   10903 C  CB    . ARG B 1 665 ? 103.774 124.256 153.459 1.00 39.03 ?  665 ARG B CB    1 
ATOM   10904 C  CG    . ARG B 1 665 ? 102.508 124.952 153.931 1.00 36.25 ?  665 ARG B CG    1 
ATOM   10905 C  CD    . ARG B 1 665 ? 102.184 124.562 155.363 1.00 39.06 ?  665 ARG B CD    1 
ATOM   10906 N  NE    . ARG B 1 665 ? 100.747 124.539 155.610 1.00 42.59 ?  665 ARG B NE    1 
ATOM   10907 C  CZ    . ARG B 1 665 ? 100.151 125.126 156.638 1.00 42.49 ?  665 ARG B CZ    1 
ATOM   10908 N  NH1   . ARG B 1 665 ? 100.840 125.791 157.550 1.00 43.20 1  665 ARG B NH1   1 
ATOM   10909 N  NH2   . ARG B 1 665 ? 98.829  125.044 156.755 1.00 41.16 ?  665 ARG B NH2   1 
ATOM   10910 N  N     . ASP B 1 666 ? 106.220 125.329 155.244 1.00 40.52 ?  666 ASP B N     1 
ATOM   10911 C  CA    . ASP B 1 666 ? 106.751 126.039 156.403 1.00 36.31 ?  666 ASP B CA    1 
ATOM   10912 C  C     . ASP B 1 666 ? 107.640 127.202 155.978 1.00 40.69 ?  666 ASP B C     1 
ATOM   10913 O  O     . ASP B 1 666 ? 107.587 128.283 156.577 1.00 43.81 ?  666 ASP B O     1 
ATOM   10914 C  CB    . ASP B 1 666 ? 107.522 125.071 157.301 1.00 39.39 ?  666 ASP B CB    1 
ATOM   10915 C  CG    . ASP B 1 666 ? 106.628 124.015 157.919 1.00 46.56 ?  666 ASP B CG    1 
ATOM   10916 O  OD1   . ASP B 1 666 ? 105.579 124.383 158.489 1.00 46.49 ?  666 ASP B OD1   1 
ATOM   10917 O  OD2   . ASP B 1 666 ? 106.972 122.818 157.834 1.00 46.36 -1 666 ASP B OD2   1 
ATOM   10918 N  N     . LEU B 1 667 ? 108.464 126.998 154.949 1.00 34.44 ?  667 LEU B N     1 
ATOM   10919 C  CA    . LEU B 1 667 ? 109.296 128.082 154.436 1.00 29.98 ?  667 LEU B CA    1 
ATOM   10920 C  C     . LEU B 1 667 ? 108.442 129.215 153.881 1.00 28.63 ?  667 LEU B C     1 
ATOM   10921 O  O     . LEU B 1 667 ? 108.736 130.396 154.109 1.00 35.33 ?  667 LEU B O     1 
ATOM   10922 C  CB    . LEU B 1 667 ? 110.244 127.543 153.364 1.00 33.52 ?  667 LEU B CB    1 
ATOM   10923 C  CG    . LEU B 1 667 ? 111.353 128.469 152.869 1.00 32.74 ?  667 LEU B CG    1 
ATOM   10924 C  CD1   . LEU B 1 667 ? 111.994 129.204 154.030 1.00 34.04 ?  667 LEU B CD1   1 
ATOM   10925 C  CD2   . LEU B 1 667 ? 112.392 127.677 152.098 1.00 31.27 ?  667 LEU B CD2   1 
ATOM   10926 N  N     . ASN B 1 668 ? 107.376 128.875 153.154 1.00 29.56 ?  668 ASN B N     1 
ATOM   10927 C  CA    . ASN B 1 668 ? 106.473 129.898 152.638 1.00 24.89 ?  668 ASN B CA    1 
ATOM   10928 C  C     . ASN B 1 668 ? 105.774 130.638 153.769 1.00 26.58 ?  668 ASN B C     1 
ATOM   10929 O  O     . ASN B 1 668 ? 105.583 131.856 153.694 1.00 28.91 ?  668 ASN B O     1 
ATOM   10930 C  CB    . ASN B 1 668 ? 105.450 129.270 151.693 1.00 28.31 ?  668 ASN B CB    1 
ATOM   10931 C  CG    . ASN B 1 668 ? 105.926 129.241 150.256 1.00 32.47 ?  668 ASN B CG    1 
ATOM   10932 O  OD1   . ASN B 1 668 ? 106.714 130.086 149.834 1.00 33.33 ?  668 ASN B OD1   1 
ATOM   10933 N  ND2   . ASN B 1 668 ? 105.449 128.263 149.497 1.00 33.17 ?  668 ASN B ND2   1 
ATOM   10934 N  N     . ARG B 1 669 ? 105.378 129.920 154.823 1.00 30.84 ?  669 ARG B N     1 
ATOM   10935 C  CA    . ARG B 1 669 ? 104.761 130.571 155.973 1.00 33.19 ?  669 ARG B CA    1 
ATOM   10936 C  C     . ARG B 1 669 ? 105.730 131.527 156.651 1.00 27.48 ?  669 ARG B C     1 
ATOM   10937 O  O     . ARG B 1 669 ? 105.342 132.625 157.063 1.00 28.14 ?  669 ARG B O     1 
ATOM   10938 C  CB    . ARG B 1 669 ? 104.266 129.525 156.970 1.00 31.40 ?  669 ARG B CB    1 
ATOM   10939 C  CG    . ARG B 1 669 ? 102.758 129.403 157.045 1.00 30.10 ?  669 ARG B CG    1 
ATOM   10940 C  CD    . ARG B 1 669 ? 102.336 128.575 158.248 1.00 32.17 ?  669 ARG B CD    1 
ATOM   10941 N  NE    . ARG B 1 669 ? 102.317 129.351 159.484 1.00 31.03 ?  669 ARG B NE    1 
ATOM   10942 C  CZ    . ARG B 1 669 ? 101.412 130.275 159.780 1.00 34.14 ?  669 ARG B CZ    1 
ATOM   10943 N  NH1   . ARG B 1 669 ? 100.425 130.569 158.950 1.00 33.10 1  669 ARG B NH1   1 
ATOM   10944 N  NH2   . ARG B 1 669 ? 101.498 130.917 160.941 1.00 34.56 ?  669 ARG B NH2   1 
ATOM   10945 N  N     . ILE B 1 670 ? 106.994 131.124 156.785 1.00 24.89 ?  670 ILE B N     1 
ATOM   10946 C  CA    . ILE B 1 670 ? 107.996 132.011 157.372 1.00 28.67 ?  670 ILE B CA    1 
ATOM   10947 C  C     . ILE B 1 670 ? 108.183 133.249 156.506 1.00 27.42 ?  670 ILE B C     1 
ATOM   10948 O  O     . ILE B 1 670 ? 108.268 134.373 157.014 1.00 27.35 ?  670 ILE B O     1 
ATOM   10949 C  CB    . ILE B 1 670 ? 109.323 131.259 157.587 1.00 28.82 ?  670 ILE B CB    1 
ATOM   10950 C  CG1   . ILE B 1 670 ? 109.152 130.167 158.645 1.00 28.87 ?  670 ILE B CG1   1 
ATOM   10951 C  CG2   . ILE B 1 670 ? 110.419 132.221 158.005 1.00 26.47 ?  670 ILE B CG2   1 
ATOM   10952 C  CD1   . ILE B 1 670 ? 110.183 129.065 158.553 1.00 28.03 ?  670 ILE B CD1   1 
ATOM   10953 N  N     . ASP B 1 671 ? 108.242 133.065 155.184 1.00 27.88 ?  671 ASP B N     1 
ATOM   10954 C  CA    . ASP B 1 671 ? 108.392 134.202 154.280 1.00 21.61 ?  671 ASP B CA    1 
ATOM   10955 C  C     . ASP B 1 671 ? 107.204 135.153 154.380 1.00 22.57 ?  671 ASP B C     1 
ATOM   10956 O  O     . ASP B 1 671 ? 107.375 136.377 154.406 1.00 26.72 ?  671 ASP B O     1 
ATOM   10957 C  CB    . ASP B 1 671 ? 108.556 133.707 152.842 1.00 22.56 ?  671 ASP B CB    1 
ATOM   10958 C  CG    . ASP B 1 671 ? 109.887 133.024 152.606 1.00 32.56 ?  671 ASP B CG    1 
ATOM   10959 O  OD1   . ASP B 1 671 ? 110.846 133.307 153.353 1.00 35.53 ?  671 ASP B OD1   1 
ATOM   10960 O  OD2   . ASP B 1 671 ? 109.975 132.199 151.672 1.00 33.40 -1 671 ASP B OD2   1 
ATOM   10961 N  N     . LEU B 1 672 ? 105.989 134.605 154.438 1.00 22.25 ?  672 LEU B N     1 
ATOM   10962 C  CA    . LEU B 1 672 ? 104.800 135.444 154.516 1.00 20.71 ?  672 LEU B CA    1 
ATOM   10963 C  C     . LEU B 1 672 ? 104.689 136.144 155.862 1.00 21.52 ?  672 LEU B C     1 
ATOM   10964 O  O     . LEU B 1 672 ? 104.196 137.274 155.930 1.00 26.69 ?  672 LEU B O     1 
ATOM   10965 C  CB    . LEU B 1 672 ? 103.550 134.610 154.242 1.00 24.45 ?  672 LEU B CB    1 
ATOM   10966 C  CG    . LEU B 1 672 ? 103.456 134.032 152.829 1.00 23.66 ?  672 LEU B CG    1 
ATOM   10967 C  CD1   . LEU B 1 672 ? 102.461 132.885 152.784 1.00 22.52 ?  672 LEU B CD1   1 
ATOM   10968 C  CD2   . LEU B 1 672 ? 103.096 135.116 151.826 1.00 20.82 ?  672 LEU B CD2   1 
ATOM   10969 N  N     . TYR B 1 673 ? 105.130 135.496 156.941 1.00 21.13 ?  673 TYR B N     1 
ATOM   10970 C  CA    . TYR B 1 673 ? 105.159 136.162 158.238 1.00 18.26 ?  673 TYR B CA    1 
ATOM   10971 C  C     . TYR B 1 673 ? 106.201 137.272 158.257 1.00 19.58 ?  673 TYR B C     1 
ATOM   10972 O  O     . TYR B 1 673 ? 105.982 138.325 158.865 1.00 27.13 ?  673 TYR B O     1 
ATOM   10973 C  CB    . TYR B 1 673 ? 105.436 135.147 159.346 1.00 18.99 ?  673 TYR B CB    1 
ATOM   10974 C  CG    . TYR B 1 673 ? 105.380 135.740 160.734 1.00 23.24 ?  673 TYR B CG    1 
ATOM   10975 C  CD1   . TYR B 1 673 ? 104.202 136.277 161.232 1.00 22.65 ?  673 TYR B CD1   1 
ATOM   10976 C  CD2   . TYR B 1 673 ? 106.505 135.764 161.545 1.00 16.57 ?  673 TYR B CD2   1 
ATOM   10977 C  CE1   . TYR B 1 673 ? 104.145 136.819 162.498 1.00 18.82 ?  673 TYR B CE1   1 
ATOM   10978 C  CE2   . TYR B 1 673 ? 106.459 136.306 162.813 1.00 19.29 ?  673 TYR B CE2   1 
ATOM   10979 C  CZ    . TYR B 1 673 ? 105.276 136.831 163.284 1.00 20.46 ?  673 TYR B CZ    1 
ATOM   10980 O  OH    . TYR B 1 673 ? 105.223 137.372 164.548 1.00 28.40 ?  673 TYR B OH    1 
ATOM   10981 N  N     . ALA B 1 674 ? 107.343 137.047 157.607 1.00 18.23 ?  674 ALA B N     1 
ATOM   10982 C  CA    . ALA B 1 674 ? 108.346 138.097 157.478 1.00 14.78 ?  674 ALA B CA    1 
ATOM   10983 C  C     . ALA B 1 674 ? 107.788 139.289 156.714 1.00 19.33 ?  674 ALA B C     1 
ATOM   10984 O  O     . ALA B 1 674 ? 107.973 140.443 157.114 1.00 23.74 ?  674 ALA B O     1 
ATOM   10985 C  CB    . ALA B 1 674 ? 109.592 137.543 156.786 1.00 13.81 ?  674 ALA B CB    1 
ATOM   10986 N  N     . HIS B 1 675 ? 107.086 139.022 155.612 1.00 18.20 ?  675 HIS B N     1 
ATOM   10987 C  CA    . HIS B 1 675 ? 106.453 140.102 154.861 1.00 19.37 ?  675 HIS B CA    1 
ATOM   10988 C  C     . HIS B 1 675 ? 105.408 140.820 155.707 1.00 18.72 ?  675 HIS B C     1 
ATOM   10989 O  O     . HIS B 1 675 ? 105.294 142.050 155.657 1.00 26.02 ?  675 HIS B O     1 
ATOM   10990 C  CB    . HIS B 1 675 ? 105.823 139.551 153.584 1.00 19.31 ?  675 HIS B CB    1 
ATOM   10991 C  CG    . HIS B 1 675 ? 104.947 140.533 152.873 1.00 17.26 ?  675 HIS B CG    1 
ATOM   10992 N  ND1   . HIS B 1 675 ? 103.578 140.557 153.027 1.00 24.61 ?  675 HIS B ND1   1 
ATOM   10993 C  CD2   . HIS B 1 675 ? 105.246 141.530 152.009 1.00 13.15 ?  675 HIS B CD2   1 
ATOM   10994 C  CE1   . HIS B 1 675 ? 103.071 141.524 152.285 1.00 22.93 ?  675 HIS B CE1   1 
ATOM   10995 N  NE2   . HIS B 1 675 ? 104.062 142.131 151.658 1.00 27.16 ?  675 HIS B NE2   1 
ATOM   10996 N  N     . HIS B 1 676 ? 104.632 140.064 156.487 1.00 18.21 ?  676 HIS B N     1 
ATOM   10997 C  CA    . HIS B 1 676 ? 103.614 140.660 157.345 1.00 18.52 ?  676 HIS B CA    1 
ATOM   10998 C  C     . HIS B 1 676 ? 104.238 141.521 158.435 1.00 23.94 ?  676 HIS B C     1 
ATOM   10999 O  O     . HIS B 1 676 ? 103.706 142.583 158.779 1.00 25.31 ?  676 HIS B O     1 
ATOM   11000 C  CB    . HIS B 1 676 ? 102.747 139.560 157.956 1.00 19.23 ?  676 HIS B CB    1 
ATOM   11001 C  CG    . HIS B 1 676 ? 101.903 140.020 159.103 1.00 20.47 ?  676 HIS B CG    1 
ATOM   11002 N  ND1   . HIS B 1 676 ? 100.815 140.851 158.943 1.00 25.04 ?  676 HIS B ND1   1 
ATOM   11003 C  CD2   . HIS B 1 676 ? 101.988 139.765 160.430 1.00 21.47 ?  676 HIS B CD2   1 
ATOM   11004 C  CE1   . HIS B 1 676 ? 100.266 141.087 160.120 1.00 26.61 ?  676 HIS B CE1   1 
ATOM   11005 N  NE2   . HIS B 1 676 ? 100.959 140.440 161.040 1.00 26.42 ?  676 HIS B NE2   1 
ATOM   11006 N  N     . ARG B 1 677 ? 105.365 141.083 158.990 1.00 22.89 ?  677 ARG B N     1 
ATOM   11007 C  CA    . ARG B 1 677 ? 106.004 141.785 160.096 1.00 19.61 ?  677 ARG B CA    1 
ATOM   11008 C  C     . ARG B 1 677 ? 106.865 142.956 159.645 1.00 21.29 ?  677 ARG B C     1 
ATOM   11009 O  O     . ARG B 1 677 ? 107.441 143.641 160.496 1.00 29.33 ?  677 ARG B O     1 
ATOM   11010 C  CB    . ARG B 1 677 ? 106.853 140.810 160.914 1.00 19.71 ?  677 ARG B CB    1 
ATOM   11011 C  CG    . ARG B 1 677 ? 106.041 139.851 161.759 1.00 23.45 ?  677 ARG B CG    1 
ATOM   11012 C  CD    . ARG B 1 677 ? 105.473 140.541 162.985 1.00 21.42 ?  677 ARG B CD    1 
ATOM   11013 N  NE    . ARG B 1 677 ? 106.518 140.943 163.919 1.00 28.85 ?  677 ARG B NE    1 
ATOM   11014 C  CZ    . ARG B 1 677 ? 106.857 142.200 164.170 1.00 35.20 ?  677 ARG B CZ    1 
ATOM   11015 N  NH1   . ARG B 1 677 ? 106.248 143.213 163.575 1.00 30.86 1  677 ARG B NH1   1 
ATOM   11016 N  NH2   . ARG B 1 677 ? 107.833 142.448 165.039 1.00 26.43 ?  677 ARG B NH2   1 
ATOM   11017 N  N     . GLY B 1 678 ? 106.967 143.204 158.344 1.00 20.57 ?  678 GLY B N     1 
ATOM   11018 C  CA    . GLY B 1 678 ? 107.749 144.312 157.847 1.00 13.88 ?  678 GLY B CA    1 
ATOM   11019 C  C     . GLY B 1 678 ? 109.179 143.988 157.489 1.00 12.96 ?  678 GLY B C     1 
ATOM   11020 O  O     . GLY B 1 678 ? 109.978 144.916 157.311 1.00 18.02 ?  678 GLY B O     1 
ATOM   11021 N  N     . ILE B 1 679 ? 109.535 142.706 157.386 1.00 15.56 ?  679 ILE B N     1 
ATOM   11022 C  CA    . ILE B 1 679 ? 110.890 142.341 156.999 1.00 15.82 ?  679 ILE B CA    1 
ATOM   11023 C  C     . ILE B 1 679 ? 111.148 142.821 155.581 1.00 13.14 ?  679 ILE B C     1 
ATOM   11024 O  O     . ILE B 1 679 ? 110.346 142.582 154.669 1.00 26.35 ?  679 ILE B O     1 
ATOM   11025 C  CB    . ILE B 1 679 ? 111.099 140.825 157.124 1.00 16.76 ?  679 ILE B CB    1 
ATOM   11026 C  CG1   . ILE B 1 679 ? 110.982 140.391 158.585 1.00 11.88 ?  679 ILE B CG1   1 
ATOM   11027 C  CG2   . ILE B 1 679 ? 112.442 140.419 156.544 1.00 14.34 ?  679 ILE B CG2   1 
ATOM   11028 C  CD1   . ILE B 1 679 ? 111.978 141.043 159.486 1.00 13.38 ?  679 ILE B CD1   1 
ATOM   11029 N  N     . LYS B 1 680 ? 112.269 143.512 155.389 1.00 9.64  ?  680 LYS B N     1 
ATOM   11030 C  CA    . LYS B 1 680 ? 112.568 144.077 154.081 1.00 9.10  ?  680 LYS B CA    1 
ATOM   11031 C  C     . LYS B 1 680 ? 113.155 143.031 153.142 1.00 6.32  ?  680 LYS B C     1 
ATOM   11032 O  O     . LYS B 1 680 ? 112.708 142.892 151.999 1.00 19.51 ?  680 LYS B O     1 
ATOM   11033 C  CB    . LYS B 1 680 ? 113.521 145.261 154.234 1.00 6.44  ?  680 LYS B CB    1 
ATOM   11034 C  CG    . LYS B 1 680 ? 112.891 146.482 154.871 1.00 0.00  ?  680 LYS B CG    1 
ATOM   11035 C  CD    . LYS B 1 680 ? 113.877 147.629 154.951 1.00 8.90  ?  680 LYS B CD    1 
ATOM   11036 C  CE    . LYS B 1 680 ? 113.377 148.719 155.874 1.00 9.68  ?  680 LYS B CE    1 
ATOM   11037 N  NZ    . LYS B 1 680 ? 114.332 149.853 155.965 1.00 17.63 1  680 LYS B NZ    1 
ATOM   11038 N  N     . THR B 1 681 ? 114.152 142.283 153.606 1.00 14.09 ?  681 THR B N     1 
ATOM   11039 C  CA    . THR B 1 681 ? 114.829 141.300 152.776 1.00 7.46  ?  681 THR B CA    1 
ATOM   11040 C  C     . THR B 1 681 ? 115.069 140.028 153.572 1.00 12.18 ?  681 THR B C     1 
ATOM   11041 O  O     . THR B 1 681 ? 115.195 140.056 154.799 1.00 19.65 ?  681 THR B O     1 
ATOM   11042 C  CB    . THR B 1 681 ? 116.172 141.825 152.243 1.00 12.38 ?  681 THR B CB    1 
ATOM   11043 O  OG1   . THR B 1 681 ? 116.937 142.376 153.323 1.00 23.17 ?  681 THR B OG1   1 
ATOM   11044 C  CG2   . THR B 1 681 ? 115.954 142.894 151.188 1.00 8.64  ?  681 THR B CG2   1 
ATOM   11045 N  N     . ILE B 1 682 ? 115.133 138.908 152.856 1.00 12.38 ?  682 ILE B N     1 
ATOM   11046 C  CA    . ILE B 1 682 ? 115.496 137.615 153.419 1.00 9.09  ?  682 ILE B CA    1 
ATOM   11047 C  C     . ILE B 1 682 ? 116.729 137.119 152.678 1.00 15.98 ?  682 ILE B C     1 
ATOM   11048 O  O     . ILE B 1 682 ? 116.730 137.053 151.444 1.00 19.54 ?  682 ILE B O     1 
ATOM   11049 C  CB    . ILE B 1 682 ? 114.344 136.601 153.314 1.00 11.04 ?  682 ILE B CB    1 
ATOM   11050 C  CG1   . ILE B 1 682 ? 113.046 137.219 153.835 1.00 17.16 ?  682 ILE B CG1   1 
ATOM   11051 C  CG2   . ILE B 1 682 ? 114.677 135.351 154.090 1.00 19.66 ?  682 ILE B CG2   1 
ATOM   11052 C  CD1   . ILE B 1 682 ? 111.851 136.308 153.732 1.00 18.91 ?  682 ILE B CD1   1 
ATOM   11053 N  N     . TYR B 1 683 ? 117.780 136.783 153.428 1.00 13.01 ?  683 TYR B N     1 
ATOM   11054 C  CA    . TYR B 1 683 ? 119.066 136.479 152.802 1.00 12.37 ?  683 TYR B CA    1 
ATOM   11055 C  C     . TYR B 1 683 ? 119.141 135.032 152.320 1.00 20.43 ?  683 TYR B C     1 
ATOM   11056 O  O     . TYR B 1 683 ? 119.206 134.769 151.117 1.00 33.65 ?  683 TYR B O     1 
ATOM   11057 C  CB    . TYR B 1 683 ? 120.201 136.782 153.785 1.00 19.94 ?  683 TYR B CB    1 
ATOM   11058 C  CG    . TYR B 1 683 ? 121.589 136.676 153.195 1.00 16.76 ?  683 TYR B CG    1 
ATOM   11059 C  CD1   . TYR B 1 683 ? 121.796 136.786 151.825 1.00 10.05 ?  683 TYR B CD1   1 
ATOM   11060 C  CD2   . TYR B 1 683 ? 122.694 136.478 154.009 1.00 14.57 ?  683 TYR B CD2   1 
ATOM   11061 C  CE1   . TYR B 1 683 ? 123.059 136.693 151.286 1.00 17.35 ?  683 TYR B CE1   1 
ATOM   11062 C  CE2   . TYR B 1 683 ? 123.964 136.386 153.477 1.00 20.79 ?  683 TYR B CE2   1 
ATOM   11063 C  CZ    . TYR B 1 683 ? 124.141 136.494 152.115 1.00 21.07 ?  683 TYR B CZ    1 
ATOM   11064 O  OH    . TYR B 1 683 ? 125.404 136.403 151.582 1.00 18.47 ?  683 TYR B OH    1 
ATOM   11065 N  N     . TYR B 1 684 ? 119.108 134.080 153.243 1.00 28.72 ?  684 TYR B N     1 
ATOM   11066 C  CA    . TYR B 1 684 ? 119.394 132.698 152.897 1.00 22.47 ?  684 TYR B CA    1 
ATOM   11067 C  C     . TYR B 1 684 ? 118.420 131.773 153.604 1.00 33.54 ?  684 TYR B C     1 
ATOM   11068 O  O     . TYR B 1 684 ? 117.884 132.098 154.667 1.00 33.94 ?  684 TYR B O     1 
ATOM   11069 C  CB    . TYR B 1 684 ? 120.830 132.305 153.268 1.00 23.90 ?  684 TYR B CB    1 
ATOM   11070 C  CG    . TYR B 1 684 ? 121.808 132.380 152.120 1.00 25.15 ?  684 TYR B CG    1 
ATOM   11071 C  CD1   . TYR B 1 684 ? 121.568 131.706 150.932 1.00 28.20 ?  684 TYR B CD1   1 
ATOM   11072 C  CD2   . TYR B 1 684 ? 122.978 133.120 152.230 1.00 27.14 ?  684 TYR B CD2   1 
ATOM   11073 C  CE1   . TYR B 1 684 ? 122.464 131.771 149.881 1.00 30.33 ?  684 TYR B CE1   1 
ATOM   11074 C  CE2   . TYR B 1 684 ? 123.877 133.192 151.186 1.00 27.12 ?  684 TYR B CE2   1 
ATOM   11075 C  CZ    . TYR B 1 684 ? 123.617 132.516 150.014 1.00 30.90 ?  684 TYR B CZ    1 
ATOM   11076 O  OH    . TYR B 1 684 ? 124.514 132.587 148.974 1.00 33.34 ?  684 TYR B OH    1 
ATOM   11077 N  N     . ALA B 1 685 ? 118.201 130.616 152.997 1.00 32.23 ?  685 ALA B N     1 
ATOM   11078 C  CA    . ALA B 1 685 ? 117.458 129.521 153.605 1.00 31.89 ?  685 ALA B CA    1 
ATOM   11079 C  C     . ALA B 1 685 ? 118.453 128.381 153.803 1.00 34.11 ?  685 ALA B C     1 
ATOM   11080 O  O     . ALA B 1 685 ? 118.585 127.497 152.955 1.00 41.93 ?  685 ALA B O     1 
ATOM   11081 C  CB    . ALA B 1 685 ? 116.278 129.107 152.737 1.00 30.04 ?  685 ALA B CB    1 
ATOM   11082 N  N     . ARG B 1 686 ? 119.163 128.415 154.927 1.00 31.14 ?  686 ARG B N     1 
ATOM   11083 C  CA    . ARG B 1 686 ? 120.136 127.383 155.254 1.00 35.59 ?  686 ARG B CA    1 
ATOM   11084 C  C     . ARG B 1 686 ? 119.437 126.260 156.006 1.00 40.36 ?  686 ARG B C     1 
ATOM   11085 O  O     . ARG B 1 686 ? 118.853 126.488 157.069 1.00 39.37 ?  686 ARG B O     1 
ATOM   11086 C  CB    . ARG B 1 686 ? 121.268 127.967 156.095 1.00 35.54 ?  686 ARG B CB    1 
ATOM   11087 C  CG    . ARG B 1 686 ? 122.140 128.968 155.362 1.00 39.12 ?  686 ARG B CG    1 
ATOM   11088 C  CD    . ARG B 1 686 ? 123.314 129.405 156.222 1.00 40.12 ?  686 ARG B CD    1 
ATOM   11089 N  NE    . ARG B 1 686 ? 123.733 128.358 157.146 1.00 42.56 ?  686 ARG B NE    1 
ATOM   11090 C  CZ    . ARG B 1 686 ? 124.869 127.681 157.042 1.00 41.73 ?  686 ARG B CZ    1 
ATOM   11091 N  NH1   . ARG B 1 686 ? 125.726 127.915 156.063 1.00 40.57 1  686 ARG B NH1   1 
ATOM   11092 N  NH2   . ARG B 1 686 ? 125.151 126.745 157.944 1.00 38.17 ?  686 ARG B NH2   1 
ATOM   11093 N  N     . THR B 1 687 ? 119.501 125.050 155.461 1.00 42.20 ?  687 THR B N     1 
ATOM   11094 C  CA    . THR B 1 687 ? 118.851 123.891 156.051 1.00 45.25 ?  687 THR B CA    1 
ATOM   11095 C  C     . THR B 1 687 ? 119.883 123.033 156.769 1.00 45.70 ?  687 THR B C     1 
ATOM   11096 O  O     . THR B 1 687 ? 120.962 122.762 156.233 1.00 45.26 ?  687 THR B O     1 
ATOM   11097 C  CB    . THR B 1 687 ? 118.129 123.061 154.986 1.00 43.73 ?  687 THR B CB    1 
ATOM   11098 O  OG1   . THR B 1 687 ? 117.407 123.933 154.109 1.00 43.79 ?  687 THR B OG1   1 
ATOM   11099 C  CG2   . THR B 1 687 ? 117.154 122.098 155.641 1.00 42.22 ?  687 THR B CG2   1 
ATOM   11100 N  N     . LYS B 1 688 ? 119.546 122.614 157.983 1.00 40.87 ?  688 LYS B N     1 
ATOM   11101 C  CA    . LYS B 1 688 ? 120.458 121.823 158.800 1.00 43.33 ?  688 LYS B CA    1 
ATOM   11102 C  C     . LYS B 1 688 ? 120.581 120.400 158.265 1.00 48.17 ?  688 LYS B C     1 
ATOM   11103 O  O     . LYS B 1 688 ? 119.647 119.605 158.367 1.00 48.97 ?  688 LYS B O     1 
ATOM   11104 C  CB    . LYS B 1 688 ? 119.989 121.803 160.256 1.00 42.70 ?  688 LYS B CB    1 
ATOM   11105 C  CG    . LYS B 1 688 ? 120.924 121.070 161.200 1.00 41.41 ?  688 LYS B CG    1 
ATOM   11106 C  CD    . LYS B 1 688 ? 120.480 121.228 162.643 1.00 44.48 ?  688 LYS B CD    1 
ATOM   11107 C  CE    . LYS B 1 688 ? 121.511 120.656 163.602 1.00 46.73 ?  688 LYS B CE    1 
ATOM   11108 N  NZ    . LYS B 1 688 ? 121.105 120.838 165.022 1.00 44.27 ?  688 LYS B NZ    1 
ATOM   11109 N  N     . ASP C 2 37  ? 131.978 79.784  115.316 1.00 45.99 ?  16  ASP C N     1 
ATOM   11110 C  CA    . ASP C 2 37  ? 132.088 80.388  113.985 1.00 45.47 ?  16  ASP C CA    1 
ATOM   11111 C  C     . ASP C 2 37  ? 131.428 81.761  113.854 1.00 44.13 ?  16  ASP C C     1 
ATOM   11112 O  O     . ASP C 2 37  ? 131.542 82.404  112.808 1.00 44.46 ?  16  ASP C O     1 
ATOM   11113 C  CB    . ASP C 2 37  ? 131.493 79.443  112.938 1.00 45.90 ?  16  ASP C CB    1 
ATOM   11114 C  CG    . ASP C 2 37  ? 132.020 78.034  113.066 1.00 47.25 ?  16  ASP C CG    1 
ATOM   11115 O  OD1   . ASP C 2 37  ? 133.227 77.870  113.347 1.00 47.99 ?  16  ASP C OD1   1 
ATOM   11116 O  OD2   . ASP C 2 37  ? 131.222 77.091  112.890 1.00 49.50 -1 16  ASP C OD2   1 
ATOM   11117 N  N     . PHE C 2 38  ? 130.747 82.212  114.904 1.00 42.17 ?  17  PHE C N     1 
ATOM   11118 C  CA    . PHE C 2 38  ? 129.896 83.402  114.788 1.00 40.67 ?  17  PHE C CA    1 
ATOM   11119 C  C     . PHE C 2 38  ? 130.014 84.465  115.887 1.00 39.46 ?  17  PHE C C     1 
ATOM   11120 O  O     . PHE C 2 38  ? 129.689 85.630  115.647 1.00 39.17 ?  17  PHE C O     1 
ATOM   11121 C  CB    . PHE C 2 38  ? 128.424 82.985  114.613 1.00 40.24 ?  17  PHE C CB    1 
ATOM   11122 C  CG    . PHE C 2 38  ? 127.910 82.064  115.696 1.00 39.58 ?  17  PHE C CG    1 
ATOM   11123 C  CD1   . PHE C 2 38  ? 127.385 82.582  116.880 1.00 38.78 ?  17  PHE C CD1   1 
ATOM   11124 C  CD2   . PHE C 2 38  ? 127.937 80.680  115.525 1.00 39.43 ?  17  PHE C CD2   1 
ATOM   11125 C  CE1   . PHE C 2 38  ? 126.899 81.739  117.880 1.00 38.07 ?  17  PHE C CE1   1 
ATOM   11126 C  CE2   . PHE C 2 38  ? 127.454 79.825  116.521 1.00 39.10 ?  17  PHE C CE2   1 
ATOM   11127 C  CZ    . PHE C 2 38  ? 126.935 80.358  117.701 1.00 38.63 ?  17  PHE C CZ    1 
ATOM   11128 N  N     . THR C 2 39  ? 130.463 84.074  117.081 1.00 38.22 ?  18  THR C N     1 
ATOM   11129 C  CA    . THR C 2 39  ? 130.467 84.996  118.230 1.00 37.09 ?  18  THR C CA    1 
ATOM   11130 C  C     . THR C 2 39  ? 131.253 86.291  117.960 1.00 36.84 ?  18  THR C C     1 
ATOM   11131 O  O     . THR C 2 39  ? 130.763 87.391  118.264 1.00 36.13 ?  18  THR C O     1 
ATOM   11132 C  CB    . THR C 2 39  ? 130.897 84.307  119.559 1.00 36.59 ?  18  THR C CB    1 
ATOM   11133 O  OG1   . THR C 2 39  ? 129.827 83.476  120.019 1.00 36.50 ?  18  THR C OG1   1 
ATOM   11134 C  CG2   . THR C 2 39  ? 131.179 85.331  120.640 1.00 36.06 ?  18  THR C CG2   1 
ATOM   11135 N  N     . GLN C 2 40  ? 132.447 86.158  117.375 1.00 37.01 ?  19  GLN C N     1 
ATOM   11136 C  CA    . GLN C 2 40  ? 133.293 87.324  117.083 1.00 37.33 ?  19  GLN C CA    1 
ATOM   11137 C  C     . GLN C 2 40  ? 132.615 88.348  116.188 1.00 36.63 ?  19  GLN C C     1 
ATOM   11138 O  O     . GLN C 2 40  ? 132.703 89.549  116.441 1.00 36.10 ?  19  GLN C O     1 
ATOM   11139 C  CB    . GLN C 2 40  ? 134.642 86.921  116.488 1.00 38.24 ?  19  GLN C CB    1 
ATOM   11140 C  CG    . GLN C 2 40  ? 135.652 86.521  117.539 1.00 41.33 ?  19  GLN C CG    1 
ATOM   11141 C  CD    . GLN C 2 40  ? 137.070 86.933  117.193 1.00 45.15 ?  19  GLN C CD    1 
ATOM   11142 O  OE1   . GLN C 2 40  ? 137.463 86.948  116.021 1.00 47.33 ?  19  GLN C OE1   1 
ATOM   11143 N  NE2   . GLN C 2 40  ? 137.851 87.268  118.218 1.00 46.51 ?  19  GLN C NE2   1 
ATOM   11144 N  N     . MET C 2 41  ? 131.927 87.870  115.155 1.00 36.23 ?  20  MET C N     1 
ATOM   11145 C  CA    . MET C 2 41  ? 131.210 88.770  114.263 1.00 36.40 ?  20  MET C CA    1 
ATOM   11146 C  C     . MET C 2 41  ? 129.983 89.403  114.947 1.00 34.93 ?  20  MET C C     1 
ATOM   11147 O  O     . MET C 2 41  ? 129.668 90.562  114.691 1.00 34.20 ?  20  MET C O     1 
ATOM   11148 C  CB    . MET C 2 41  ? 130.908 88.114  112.898 1.00 37.35 ?  20  MET C CB    1 
ATOM   11149 C  CG    . MET C 2 41  ? 129.635 87.300  112.771 1.00 40.49 ?  20  MET C CG    1 
ATOM   11150 S  SD    . MET C 2 41  ? 129.359 86.808  111.040 1.00 48.68 ?  20  MET C SD    1 
ATOM   11151 C  CE    . MET C 2 41  ? 130.311 85.285  110.944 1.00 47.17 ?  20  MET C CE    1 
ATOM   11152 N  N     . PHE C 2 42  ? 129.331 88.663  115.848 1.00 33.75 ?  21  PHE C N     1 
ATOM   11153 C  CA    . PHE C 2 42  ? 128.258 89.247  116.666 1.00 32.62 ?  21  PHE C CA    1 
ATOM   11154 C  C     . PHE C 2 42  ? 128.789 90.255  117.678 1.00 32.59 ?  21  PHE C C     1 
ATOM   11155 O  O     . PHE C 2 42  ? 128.170 91.299  117.905 1.00 32.23 ?  21  PHE C O     1 
ATOM   11156 C  CB    . PHE C 2 42  ? 127.415 88.170  117.348 1.00 32.12 ?  21  PHE C CB    1 
ATOM   11157 C  CG    . PHE C 2 42  ? 126.363 87.579  116.456 1.00 31.04 ?  21  PHE C CG    1 
ATOM   11158 C  CD1   . PHE C 2 42  ? 125.064 88.085  116.459 1.00 30.75 ?  21  PHE C CD1   1 
ATOM   11159 C  CD2   . PHE C 2 42  ? 126.669 86.523  115.605 1.00 30.99 ?  21  PHE C CD2   1 
ATOM   11160 C  CE1   . PHE C 2 42  ? 124.081 87.541  115.625 1.00 30.30 ?  21  PHE C CE1   1 
ATOM   11161 C  CE2   . PHE C 2 42  ? 125.693 85.968  114.761 1.00 30.74 ?  21  PHE C CE2   1 
ATOM   11162 C  CZ    . PHE C 2 42  ? 124.398 86.479  114.773 1.00 30.48 ?  21  PHE C CZ    1 
ATOM   11163 N  N     . TYR C 2 43  ? 129.941 89.946  118.273 1.00 32.33 ?  22  TYR C N     1 
ATOM   11164 C  CA    . TYR C 2 43  ? 130.609 90.886  119.168 1.00 32.50 ?  22  TYR C CA    1 
ATOM   11165 C  C     . TYR C 2 43  ? 130.862 92.212  118.454 1.00 33.01 ?  22  TYR C C     1 
ATOM   11166 O  O     . TYR C 2 43  ? 130.501 93.276  118.965 1.00 32.50 ?  22  TYR C O     1 
ATOM   11167 C  CB    . TYR C 2 43  ? 131.920 90.310  119.737 1.00 32.53 ?  22  TYR C CB    1 
ATOM   11168 C  CG    . TYR C 2 43  ? 132.741 91.359  120.466 1.00 33.27 ?  22  TYR C CG    1 
ATOM   11169 C  CD1   . TYR C 2 43  ? 132.445 91.715  121.784 1.00 32.34 ?  22  TYR C CD1   1 
ATOM   11170 C  CD2   . TYR C 2 43  ? 133.786 92.023  119.820 1.00 33.71 ?  22  TYR C CD2   1 
ATOM   11171 C  CE1   . TYR C 2 43  ? 133.184 92.694  122.448 1.00 33.58 ?  22  TYR C CE1   1 
ATOM   11172 C  CE2   . TYR C 2 43  ? 134.530 93.010  120.470 1.00 35.12 ?  22  TYR C CE2   1 
ATOM   11173 C  CZ    . TYR C 2 43  ? 134.225 93.336  121.786 1.00 35.30 ?  22  TYR C CZ    1 
ATOM   11174 O  OH    . TYR C 2 43  ? 134.961 94.309  122.428 1.00 36.54 ?  22  TYR C OH    1 
ATOM   11175 N  N     . ASN C 2 44  ? 131.467 92.137  117.266 1.00 33.80 ?  23  ASN C N     1 
ATOM   11176 C  CA    . ASN C 2 44  ? 131.789 93.323  116.485 1.00 34.80 ?  23  ASN C CA    1 
ATOM   11177 C  C     . ASN C 2 44  ? 130.538 94.092  116.067 1.00 34.40 ?  23  ASN C C     1 
ATOM   11178 O  O     . ASN C 2 44  ? 130.509 95.316  116.146 1.00 33.99 ?  23  ASN C O     1 
ATOM   11179 C  CB    . ASN C 2 44  ? 132.646 92.964  115.260 1.00 35.46 ?  23  ASN C CB    1 
ATOM   11180 C  CG    . ASN C 2 44  ? 134.014 92.373  115.635 1.00 38.28 ?  23  ASN C CG    1 
ATOM   11181 O  OD1   . ASN C 2 44  ? 134.540 92.598  116.735 1.00 41.01 ?  23  ASN C OD1   1 
ATOM   11182 N  ND2   . ASN C 2 44  ? 134.597 91.618  114.706 1.00 39.13 ?  23  ASN C ND2   1 
ATOM   11183 N  N     . GLN C 2 45  ? 129.503 93.368  115.640 1.00 34.49 ?  24  GLN C N     1 
ATOM   11184 C  CA    . GLN C 2 45  ? 128.245 93.989  115.239 1.00 34.81 ?  24  GLN C CA    1 
ATOM   11185 C  C     . GLN C 2 45  ? 127.553 94.680  116.421 1.00 34.68 ?  24  GLN C C     1 
ATOM   11186 O  O     . GLN C 2 45  ? 127.088 95.815  116.294 1.00 34.59 ?  24  GLN C O     1 
ATOM   11187 C  CB    . GLN C 2 45  ? 127.320 92.966  114.573 1.00 34.83 ?  24  GLN C CB    1 
ATOM   11188 C  CG    . GLN C 2 45  ? 126.156 93.575  113.786 1.00 36.14 ?  24  GLN C CG    1 
ATOM   11189 C  CD    . GLN C 2 45  ? 126.604 94.466  112.623 1.00 38.04 ?  24  GLN C CD    1 
ATOM   11190 O  OE1   . GLN C 2 45  ? 127.671 94.268  112.036 1.00 38.57 ?  24  GLN C OE1   1 
ATOM   11191 N  NE2   . GLN C 2 45  ? 125.779 95.460  112.293 1.00 38.67 ?  24  GLN C NE2   1 
ATOM   11192 N  N     . ASN C 2 46  ? 127.502 94.009  117.568 1.00 34.71 ?  25  ASN C N     1 
ATOM   11193 C  CA    . ASN C 2 46  ? 126.877 94.595  118.753 1.00 34.99 ?  25  ASN C CA    1 
ATOM   11194 C  C     . ASN C 2 46  ? 127.568 95.878  119.214 1.00 35.69 ?  25  ASN C C     1 
ATOM   11195 O  O     . ASN C 2 46  ? 126.910 96.897  119.450 1.00 35.41 ?  25  ASN C O     1 
ATOM   11196 C  CB    . ASN C 2 46  ? 126.772 93.577  119.895 1.00 34.64 ?  25  ASN C CB    1 
ATOM   11197 C  CG    . ASN C 2 46  ? 125.577 92.661  119.743 1.00 34.71 ?  25  ASN C CG    1 
ATOM   11198 O  OD1   . ASN C 2 46  ? 124.508 92.942  120.276 1.00 35.68 ?  25  ASN C OD1   1 
ATOM   11199 N  ND2   . ASN C 2 46  ? 125.739 91.575  118.979 1.00 34.71 ?  25  ASN C ND2   1 
ATOM   11200 N  N     . VAL C 2 47  ? 128.894 95.842  119.316 1.00 36.69 ?  26  VAL C N     1 
ATOM   11201 C  CA    . VAL C 2 47  ? 129.626 97.018  119.790 1.00 38.00 ?  26  VAL C CA    1 
ATOM   11202 C  C     . VAL C 2 47  ? 129.611 98.177  118.784 1.00 38.90 ?  26  VAL C C     1 
ATOM   11203 O  O     . VAL C 2 47  ? 129.637 99.337  119.186 1.00 39.46 ?  26  VAL C O     1 
ATOM   11204 C  CB    . VAL C 2 47  ? 131.067 96.694  120.269 1.00 38.16 ?  26  VAL C CB    1 
ATOM   11205 C  CG1   . VAL C 2 47  ? 131.028 95.664  121.382 1.00 37.75 ?  26  VAL C CG1   1 
ATOM   11206 C  CG2   . VAL C 2 47  ? 131.952 96.228  119.114 1.00 38.81 ?  26  VAL C CG2   1 
ATOM   11207 N  N     . LYS C 2 48  ? 129.535 97.866  117.490 1.00 39.67 ?  27  LYS C N     1 
ATOM   11208 C  CA    . LYS C 2 48  ? 129.466 98.912  116.467 1.00 40.50 ?  27  LYS C CA    1 
ATOM   11209 C  C     . LYS C 2 48  ? 128.062 99.523  116.370 1.00 40.02 ?  27  LYS C C     1 
ATOM   11210 O  O     . LYS C 2 48  ? 127.875 100.586 115.774 1.00 40.55 ?  27  LYS C O     1 
ATOM   11211 C  CB    . LYS C 2 48  ? 129.944 98.393  115.097 1.00 41.23 ?  27  LYS C CB    1 
ATOM   11212 C  CG    . LYS C 2 48  ? 128.883 97.661  114.277 1.00 42.50 ?  27  LYS C CG    1 
ATOM   11213 C  CD    . LYS C 2 48  ? 129.399 97.227  112.897 1.00 44.92 ?  27  LYS C CD    1 
ATOM   11214 C  CE    . LYS C 2 48  ? 129.387 98.375  111.889 1.00 46.66 ?  27  LYS C CE    1 
ATOM   11215 N  NZ    . LYS C 2 48  ? 128.014 98.917  111.669 1.00 47.26 1  27  LYS C NZ    1 
ATOM   11216 N  N     . GLN C 2 49  ? 127.077 98.846  116.949 1.00 39.10 ?  28  GLN C N     1 
ATOM   11217 C  CA    . GLN C 2 49  ? 125.723 99.358  116.962 1.00 38.22 ?  28  GLN C CA    1 
ATOM   11218 C  C     . GLN C 2 49  ? 125.444 100.193 118.211 1.00 37.23 ?  28  GLN C C     1 
ATOM   11219 O  O     . GLN C 2 49  ? 124.339 100.711 118.356 1.00 37.40 ?  28  GLN C O     1 
ATOM   11220 C  CB    . GLN C 2 49  ? 124.697 98.222  116.812 1.00 38.69 ?  28  GLN C CB    1 
ATOM   11221 C  CG    . GLN C 2 49  ? 124.612 97.639  115.393 1.00 39.57 ?  28  GLN C CG    1 
ATOM   11222 C  CD    . GLN C 2 49  ? 123.465 96.651  115.198 1.00 41.20 ?  28  GLN C CD    1 
ATOM   11223 O  OE1   . GLN C 2 49  ? 123.333 96.054  114.129 1.00 42.94 ?  28  GLN C OE1   1 
ATOM   11224 N  NE2   . GLN C 2 49  ? 122.630 96.476  116.226 1.00 41.23 ?  28  GLN C NE2   1 
ATOM   11225 N  N     . PHE C 2 50  ? 126.440 100.343 119.090 1.00 35.83 ?  29  PHE C N     1 
ATOM   11226 C  CA    . PHE C 2 50  ? 126.237 101.060 120.357 1.00 34.51 ?  29  PHE C CA    1 
ATOM   11227 C  C     . PHE C 2 50  ? 125.674 102.472 120.168 1.00 33.81 ?  29  PHE C C     1 
ATOM   11228 O  O     . PHE C 2 50  ? 126.149 103.224 119.317 1.00 33.66 ?  29  PHE C O     1 
ATOM   11229 C  CB    . PHE C 2 50  ? 127.508 101.111 121.210 1.00 34.59 ?  29  PHE C CB    1 
ATOM   11230 C  CG    . PHE C 2 50  ? 127.317 101.816 122.541 1.00 34.59 ?  29  PHE C CG    1 
ATOM   11231 C  CD1   . PHE C 2 50  ? 126.590 101.213 123.574 1.00 34.34 ?  29  PHE C CD1   1 
ATOM   11232 C  CD2   . PHE C 2 50  ? 127.844 103.090 122.754 1.00 35.49 ?  29  PHE C CD2   1 
ATOM   11233 C  CE1   . PHE C 2 50  ? 126.403 101.863 124.803 1.00 33.88 ?  29  PHE C CE1   1 
ATOM   11234 C  CE2   . PHE C 2 50  ? 127.662 103.755 123.980 1.00 34.12 ?  29  PHE C CE2   1 
ATOM   11235 C  CZ    . PHE C 2 50  ? 126.942 103.141 125.004 1.00 33.87 ?  29  PHE C CZ    1 
ATOM   11236 N  N     . TRP C 2 51  ? 124.667 102.811 120.975 1.00 32.24 ?  30  TRP C N     1 
ATOM   11237 C  CA    . TRP C 2 51  ? 124.002 104.111 120.908 1.00 31.28 ?  30  TRP C CA    1 
ATOM   11238 C  C     . TRP C 2 51  ? 123.398 104.509 122.256 1.00 31.12 ?  30  TRP C C     1 
ATOM   11239 O  O     . TRP C 2 51  ? 123.254 103.666 123.149 1.00 30.71 ?  30  TRP C O     1 
ATOM   11240 C  CB    . TRP C 2 51  ? 122.925 104.109 119.813 1.00 30.85 ?  30  TRP C CB    1 
ATOM   11241 C  CG    . TRP C 2 51  ? 121.809 103.120 120.047 1.00 29.31 ?  30  TRP C CG    1 
ATOM   11242 C  CD1   . TRP C 2 51  ? 121.817 101.784 119.753 1.00 29.07 ?  30  TRP C CD1   1 
ATOM   11243 C  CD2   . TRP C 2 51  ? 120.537 103.390 120.642 1.00 28.33 ?  30  TRP C CD2   1 
ATOM   11244 N  NE1   . TRP C 2 51  ? 120.626 101.209 120.119 1.00 28.01 ?  30  TRP C NE1   1 
ATOM   11245 C  CE2   . TRP C 2 51  ? 119.819 102.172 120.667 1.00 27.67 ?  30  TRP C CE2   1 
ATOM   11246 C  CE3   . TRP C 2 51  ? 119.931 104.543 121.161 1.00 27.27 ?  30  TRP C CE3   1 
ATOM   11247 C  CZ2   . TRP C 2 51  ? 118.530 102.073 121.189 1.00 26.54 ?  30  TRP C CZ2   1 
ATOM   11248 C  CZ3   . TRP C 2 51  ? 118.644 104.447 121.672 1.00 27.07 ?  30  TRP C CZ3   1 
ATOM   11249 C  CH2   . TRP C 2 51  ? 117.959 103.217 121.688 1.00 26.52 ?  30  TRP C CH2   1 
ATOM   11250 N  N     . LEU C 2 52  ? 123.054 105.793 122.391 1.00 30.65 ?  31  LEU C N     1 
ATOM   11251 C  CA    . LEU C 2 52  ? 122.338 106.321 123.555 1.00 30.38 ?  31  LEU C CA    1 
ATOM   11252 C  C     . LEU C 2 52  ? 121.165 107.179 123.088 1.00 30.51 ?  31  LEU C C     1 
ATOM   11253 O  O     . LEU C 2 52  ? 121.298 107.900 122.097 1.00 30.77 ?  31  LEU C O     1 
ATOM   11254 C  CB    . LEU C 2 52  ? 123.275 107.159 124.440 1.00 30.45 ?  31  LEU C CB    1 
ATOM   11255 C  CG    . LEU C 2 52  ? 124.425 106.396 125.104 1.00 30.29 ?  31  LEU C CG    1 
ATOM   11256 C  CD1   . LEU C 2 52  ? 125.554 107.329 125.563 1.00 30.69 ?  31  LEU C CD1   1 
ATOM   11257 C  CD2   . LEU C 2 52  ? 123.913 105.518 126.257 1.00 29.91 ?  31  LEU C CD2   1 
ATOM   11258 N  N     . PRO C 2 53  ? 120.015 107.116 123.797 1.00 30.73 ?  32  PRO C N     1 
ATOM   11259 C  CA    . PRO C 2 53  ? 118.832 107.887 123.379 1.00 31.17 ?  32  PRO C CA    1 
ATOM   11260 C  C     . PRO C 2 53  ? 119.086 109.390 123.277 1.00 32.18 ?  32  PRO C C     1 
ATOM   11261 O  O     . PRO C 2 53  ? 118.465 110.061 122.436 1.00 32.66 ?  32  PRO C O     1 
ATOM   11262 C  CB    . PRO C 2 53  ? 117.805 107.598 124.480 1.00 30.99 ?  32  PRO C CB    1 
ATOM   11263 C  CG    . PRO C 2 53  ? 118.598 107.025 125.630 1.00 30.50 ?  32  PRO C CG    1 
ATOM   11264 C  CD    . PRO C 2 53  ? 119.735 106.300 124.995 1.00 30.46 ?  32  PRO C CD    1 
ATOM   11265 N  N     . GLU C 2 54  ? 119.998 109.902 124.107 1.00 32.62 ?  33  GLU C N     1 
ATOM   11266 C  CA    . GLU C 2 54  ? 120.352 111.331 124.110 1.00 33.44 ?  33  GLU C CA    1 
ATOM   11267 C  C     . GLU C 2 54  ? 120.954 111.819 122.787 1.00 33.59 ?  33  GLU C C     1 
ATOM   11268 O  O     . GLU C 2 54  ? 121.017 113.023 122.549 1.00 34.05 ?  33  GLU C O     1 
ATOM   11269 C  CB    . GLU C 2 54  ? 121.300 111.674 125.272 1.00 33.72 ?  33  GLU C CB    1 
ATOM   11270 C  CG    . GLU C 2 54  ? 120.650 111.661 126.670 1.00 34.53 ?  33  GLU C CG    1 
ATOM   11271 C  CD    . GLU C 2 54  ? 120.387 110.250 127.198 1.00 35.09 ?  33  GLU C CD    1 
ATOM   11272 O  OE1   . GLU C 2 54  ? 121.057 109.291 126.736 1.00 34.38 ?  33  GLU C OE1   1 
ATOM   11273 O  OE2   . GLU C 2 54  ? 119.506 110.103 128.076 1.00 35.53 -1 33  GLU C OE2   1 
ATOM   11274 N  N     . GLU C 2 55  ? 121.394 110.889 121.937 1.00 33.82 ?  34  GLU C N     1 
ATOM   11275 C  CA    . GLU C 2 55  ? 121.895 111.223 120.601 1.00 34.19 ?  34  GLU C CA    1 
ATOM   11276 C  C     . GLU C 2 55  ? 120.777 111.759 119.695 1.00 33.83 ?  34  GLU C C     1 
ATOM   11277 O  O     . GLU C 2 55  ? 121.047 112.436 118.704 1.00 33.93 ?  34  GLU C O     1 
ATOM   11278 C  CB    . GLU C 2 55  ? 122.548 110.004 119.925 1.00 34.52 ?  34  GLU C CB    1 
ATOM   11279 C  CG    . GLU C 2 55  ? 123.781 109.432 120.621 1.00 36.50 ?  34  GLU C CG    1 
ATOM   11280 C  CD    . GLU C 2 55  ? 124.519 108.418 119.752 1.00 40.03 ?  34  GLU C CD    1 
ATOM   11281 O  OE1   . GLU C 2 55  ? 125.352 108.830 118.914 1.00 42.43 ?  34  GLU C OE1   1 
ATOM   11282 O  OE2   . GLU C 2 55  ? 124.276 107.206 119.908 1.00 39.35 -1 34  GLU C OE2   1 
ATOM   11283 N  N     . ILE C 2 56  ? 119.533 111.419 120.034 1.00 33.31 ?  35  ILE C N     1 
ATOM   11284 C  CA    . ILE C 2 56  ? 118.345 111.792 119.264 1.00 33.14 ?  35  ILE C CA    1 
ATOM   11285 C  C     . ILE C 2 56  ? 117.567 112.865 120.033 1.00 32.58 ?  35  ILE C C     1 
ATOM   11286 O  O     . ILE C 2 56  ? 117.097 112.612 121.136 1.00 32.12 ?  35  ILE C O     1 
ATOM   11287 C  CB    . ILE C 2 56  ? 117.409 110.555 119.035 1.00 33.03 ?  35  ILE C CB    1 
ATOM   11288 C  CG1   . ILE C 2 56  ? 118.177 109.348 118.452 1.00 34.76 ?  35  ILE C CG1   1 
ATOM   11289 C  CG2   . ILE C 2 56  ? 116.187 110.920 118.183 1.00 33.61 ?  35  ILE C CG2   1 
ATOM   11290 C  CD1   . ILE C 2 56  ? 118.697 109.517 117.022 1.00 36.75 ?  35  ILE C CD1   1 
ATOM   11291 N  N     . ALA C 2 57  ? 117.444 114.060 119.458 1.00 32.36 ?  36  ALA C N     1 
ATOM   11292 C  CA    . ALA C 2 57  ? 116.642 115.123 120.071 1.00 32.17 ?  36  ALA C CA    1 
ATOM   11293 C  C     . ALA C 2 57  ? 115.153 114.864 119.820 1.00 31.76 ?  36  ALA C C     1 
ATOM   11294 O  O     . ALA C 2 57  ? 114.747 114.585 118.690 1.00 31.95 ?  36  ALA C O     1 
ATOM   11295 C  CB    . ALA C 2 57  ? 117.052 116.481 119.521 1.00 33.01 ?  36  ALA C CB    1 
ATOM   11296 N  N     . LEU C 2 58  ? 114.341 114.958 120.868 1.00 30.68 ?  37  LEU C N     1 
ATOM   11297 C  CA    . LEU C 2 58  ? 112.957 114.494 120.791 1.00 30.14 ?  37  LEU C CA    1 
ATOM   11298 C  C     . LEU C 2 58  ? 111.909 115.597 120.689 1.00 30.21 ?  37  LEU C C     1 
ATOM   11299 O  O     . LEU C 2 58  ? 110.739 115.318 120.395 1.00 29.91 ?  37  LEU C O     1 
ATOM   11300 C  CB    . LEU C 2 58  ? 112.642 113.562 121.967 1.00 29.46 ?  37  LEU C CB    1 
ATOM   11301 C  CG    . LEU C 2 58  ? 113.378 112.215 121.961 1.00 29.08 ?  37  LEU C CG    1 
ATOM   11302 C  CD1   . LEU C 2 58  ? 113.130 111.458 123.254 1.00 29.23 ?  37  LEU C CD1   1 
ATOM   11303 C  CD2   . LEU C 2 58  ? 112.975 111.362 120.760 1.00 28.84 ?  37  LEU C CD2   1 
ATOM   11304 N  N     . ASN C 2 59  ? 112.331 116.839 120.906 1.00 30.50 ?  38  ASN C N     1 
ATOM   11305 C  CA    . ASN C 2 59  ? 111.409 117.979 120.886 1.00 31.23 ?  38  ASN C CA    1 
ATOM   11306 C  C     . ASN C 2 59  ? 110.710 118.197 119.534 1.00 31.03 ?  38  ASN C C     1 
ATOM   11307 O  O     . ASN C 2 59  ? 109.660 118.830 119.474 1.00 30.82 ?  38  ASN C O     1 
ATOM   11308 C  CB    . ASN C 2 59  ? 112.093 119.262 121.397 1.00 31.98 ?  38  ASN C CB    1 
ATOM   11309 C  CG    . ASN C 2 59  ? 113.324 119.643 120.591 1.00 33.59 ?  38  ASN C CG    1 
ATOM   11310 O  OD1   . ASN C 2 59  ? 114.255 118.844 120.432 1.00 36.48 ?  38  ASN C OD1   1 
ATOM   11311 N  ND2   . ASN C 2 59  ? 113.343 120.875 120.089 1.00 34.77 ?  38  ASN C ND2   1 
ATOM   11312 N  N     . GLY C 2 60  ? 111.282 117.638 118.470 1.00 30.88 ?  39  GLY C N     1 
ATOM   11313 C  CA    . GLY C 2 60  ? 110.661 117.647 117.140 1.00 31.37 ?  39  GLY C CA    1 
ATOM   11314 C  C     . GLY C 2 60  ? 109.359 116.865 117.015 1.00 31.05 ?  39  GLY C C     1 
ATOM   11315 O  O     . GLY C 2 60  ? 108.539 117.187 116.166 1.00 31.21 ?  39  GLY C O     1 
ATOM   11316 N  N     . ASP C 2 61  ? 109.163 115.848 117.859 1.00 30.63 ?  40  ASP C N     1 
ATOM   11317 C  CA    . ASP C 2 61  ? 107.890 115.102 117.911 1.00 30.65 ?  40  ASP C CA    1 
ATOM   11318 C  C     . ASP C 2 61  ? 106.754 115.814 118.653 1.00 31.00 ?  40  ASP C C     1 
ATOM   11319 O  O     . ASP C 2 61  ? 105.618 115.339 118.621 1.00 30.91 ?  40  ASP C O     1 
ATOM   11320 C  CB    . ASP C 2 61  ? 108.081 113.730 118.568 1.00 30.00 ?  40  ASP C CB    1 
ATOM   11321 C  CG    . ASP C 2 61  ? 108.936 112.793 117.749 1.00 30.88 ?  40  ASP C CG    1 
ATOM   11322 O  OD1   . ASP C 2 61  ? 109.420 113.186 116.661 1.00 30.42 ?  40  ASP C OD1   1 
ATOM   11323 O  OD2   . ASP C 2 61  ? 109.128 111.648 118.212 1.00 31.17 -1 40  ASP C OD2   1 
ATOM   11324 N  N     . LEU C 2 62  ? 107.056 116.922 119.328 1.00 31.54 ?  41  LEU C N     1 
ATOM   11325 C  CA    . LEU C 2 62  ? 106.080 117.585 120.210 1.00 32.47 ?  41  LEU C CA    1 
ATOM   11326 C  C     . LEU C 2 62  ? 104.756 117.923 119.535 1.00 33.21 ?  41  LEU C C     1 
ATOM   11327 O  O     . LEU C 2 62  ? 103.687 117.734 120.126 1.00 32.84 ?  41  LEU C O     1 
ATOM   11328 C  CB    . LEU C 2 62  ? 106.671 118.844 120.849 1.00 33.14 ?  41  LEU C CB    1 
ATOM   11329 C  CG    . LEU C 2 62  ? 107.497 118.668 122.123 1.00 34.44 ?  41  LEU C CG    1 
ATOM   11330 C  CD1   . LEU C 2 62  ? 108.248 119.955 122.435 1.00 35.04 ?  41  LEU C CD1   1 
ATOM   11331 C  CD2   . LEU C 2 62  ? 106.603 118.253 123.298 1.00 35.52 ?  41  LEU C CD2   1 
ATOM   11332 N  N     . LEU C 2 63  ? 104.831 118.415 118.300 1.00 33.75 ?  42  LEU C N     1 
ATOM   11333 C  CA    . LEU C 2 63  ? 103.630 118.800 117.572 1.00 34.79 ?  42  LEU C CA    1 
ATOM   11334 C  C     . LEU C 2 63  ? 102.817 117.638 117.005 1.00 34.66 ?  42  LEU C C     1 
ATOM   11335 O  O     . LEU C 2 63  ? 101.598 117.627 117.166 1.00 34.67 ?  42  LEU C O     1 
ATOM   11336 C  CB    . LEU C 2 63  ? 103.934 119.844 116.495 1.00 35.27 ?  42  LEU C CB    1 
ATOM   11337 C  CG    . LEU C 2 63  ? 104.010 121.278 117.032 1.00 36.82 ?  42  LEU C CG    1 
ATOM   11338 C  CD1   . LEU C 2 63  ? 104.358 122.234 115.897 1.00 37.93 ?  42  LEU C CD1   1 
ATOM   11339 C  CD2   . LEU C 2 63  ? 102.706 121.711 117.701 1.00 37.85 ?  42  LEU C CD2   1 
ATOM   11340 N  N     . THR C 2 64  ? 103.463 116.669 116.349 1.00 34.70 ?  43  THR C N     1 
ATOM   11341 C  CA    . THR C 2 64  ? 102.716 115.502 115.851 1.00 35.10 ?  43  THR C CA    1 
ATOM   11342 C  C     . THR C 2 64  ? 102.090 114.690 116.996 1.00 34.78 ?  43  THR C C     1 
ATOM   11343 O  O     . THR C 2 64  ? 101.074 114.032 116.799 1.00 35.04 ?  43  THR C O     1 
ATOM   11344 C  CB    . THR C 2 64  ? 103.520 114.589 114.873 1.00 35.30 ?  43  THR C CB    1 
ATOM   11345 O  OG1   . THR C 2 64  ? 104.744 114.147 115.480 1.00 36.01 ?  43  THR C OG1   1 
ATOM   11346 C  CG2   . THR C 2 64  ? 103.823 115.320 113.565 1.00 35.96 ?  43  THR C CG2   1 
ATOM   11347 N  N     . TRP C 2 65  ? 102.678 114.768 118.192 1.00 34.63 ?  44  TRP C N     1 
ATOM   11348 C  CA    . TRP C 2 65  ? 102.112 114.124 119.385 1.00 34.37 ?  44  TRP C CA    1 
ATOM   11349 C  C     . TRP C 2 65  ? 100.865 114.859 119.872 1.00 35.13 ?  44  TRP C C     1 
ATOM   11350 O  O     . TRP C 2 65  ? 99.816  114.246 120.114 1.00 34.98 ?  44  TRP C O     1 
ATOM   11351 C  CB    . TRP C 2 65  ? 103.150 114.063 120.504 1.00 33.95 ?  44  TRP C CB    1 
ATOM   11352 C  CG    . TRP C 2 65  ? 102.598 113.617 121.821 1.00 33.26 ?  44  TRP C CG    1 
ATOM   11353 C  CD1   . TRP C 2 65  ? 102.308 114.404 122.901 1.00 32.51 ?  44  TRP C CD1   1 
ATOM   11354 C  CD2   . TRP C 2 65  ? 102.273 112.274 122.201 1.00 30.93 ?  44  TRP C CD2   1 
ATOM   11355 N  NE1   . TRP C 2 65  ? 101.826 113.631 123.935 1.00 31.66 ?  44  TRP C NE1   1 
ATOM   11356 C  CE2   . TRP C 2 65  ? 101.793 112.320 123.532 1.00 30.39 ?  44  TRP C CE2   1 
ATOM   11357 C  CE3   . TRP C 2 65  ? 102.345 111.035 121.550 1.00 30.36 ?  44  TRP C CE3   1 
ATOM   11358 C  CZ2   . TRP C 2 65  ? 101.378 111.178 124.219 1.00 29.16 ?  44  TRP C CZ2   1 
ATOM   11359 C  CZ3   . TRP C 2 65  ? 101.934 109.891 122.237 1.00 28.84 ?  44  TRP C CZ3   1 
ATOM   11360 C  CH2   . TRP C 2 65  ? 101.463 109.973 123.560 1.00 29.34 ?  44  TRP C CH2   1 
ATOM   11361 N  N     . LYS C 2 66  ? 101.001 116.174 120.029 1.00 35.69 ?  45  LYS C N     1 
ATOM   11362 C  CA    . LYS C 2 66  ? 99.900  117.048 120.406 1.00 36.38 ?  45  LYS C CA    1 
ATOM   11363 C  C     . LYS C 2 66  ? 98.660  116.828 119.532 1.00 36.24 ?  45  LYS C C     1 
ATOM   11364 O  O     . LYS C 2 66  ? 97.543  116.936 120.023 1.00 36.78 ?  45  LYS C O     1 
ATOM   11365 C  CB    . LYS C 2 66  ? 100.364 118.503 120.304 1.00 37.14 ?  45  LYS C CB    1 
ATOM   11366 C  CG    . LYS C 2 66  ? 99.339  119.547 120.713 1.00 38.91 ?  45  LYS C CG    1 
ATOM   11367 C  CD    . LYS C 2 66  ? 99.824  120.946 120.330 1.00 41.12 ?  45  LYS C CD    1 
ATOM   11368 C  CE    . LYS C 2 66  ? 99.003  122.021 121.023 1.00 43.00 ?  45  LYS C CE    1 
ATOM   11369 N  NZ    . LYS C 2 66  ? 98.883  121.757 122.490 1.00 44.38 1  45  LYS C NZ    1 
ATOM   11370 N  N     . TYR C 2 67  ? 98.881  116.483 118.260 1.00 36.03 ?  46  TYR C N     1 
ATOM   11371 C  CA    . TYR C 2 67  ? 97.829  116.367 117.237 1.00 36.03 ?  46  TYR C CA    1 
ATOM   11372 C  C     . TYR C 2 67  ? 97.089  115.023 117.206 1.00 35.25 ?  46  TYR C C     1 
ATOM   11373 O  O     . TYR C 2 67  ? 96.063  114.889 116.531 1.00 35.32 ?  46  TYR C O     1 
ATOM   11374 C  CB    . TYR C 2 67  ? 98.411  116.627 115.836 1.00 36.60 ?  46  TYR C CB    1 
ATOM   11375 C  CG    . TYR C 2 67  ? 98.995  118.017 115.612 1.00 37.85 ?  46  TYR C CG    1 
ATOM   11376 C  CD1   . TYR C 2 67  ? 98.730  119.062 116.496 1.00 38.97 ?  46  TYR C CD1   1 
ATOM   11377 C  CD2   . TYR C 2 67  ? 99.803  118.283 114.498 1.00 40.06 ?  46  TYR C CD2   1 
ATOM   11378 C  CE1   . TYR C 2 67  ? 99.267  120.333 116.300 1.00 40.36 ?  46  TYR C CE1   1 
ATOM   11379 C  CE2   . TYR C 2 67  ? 100.347 119.561 114.287 1.00 40.53 ?  46  TYR C CE2   1 
ATOM   11380 C  CZ    . TYR C 2 67  ? 100.068 120.580 115.197 1.00 41.43 ?  46  TYR C CZ    1 
ATOM   11381 O  OH    . TYR C 2 67  ? 100.578 121.853 115.015 1.00 41.48 ?  46  TYR C OH    1 
ATOM   11382 N  N     . LEU C 2 68  ? 97.619  114.027 117.909 1.00 33.80 ?  47  LEU C N     1 
ATOM   11383 C  CA    . LEU C 2 68  ? 96.979  112.718 117.967 1.00 32.77 ?  47  LEU C CA    1 
ATOM   11384 C  C     . LEU C 2 68  ? 95.753  112.769 118.868 1.00 31.84 ?  47  LEU C C     1 
ATOM   11385 O  O     . LEU C 2 68  ? 95.712  113.538 119.825 1.00 31.90 ?  47  LEU C O     1 
ATOM   11386 C  CB    . LEU C 2 68  ? 97.951  111.659 118.494 1.00 32.39 ?  47  LEU C CB    1 
ATOM   11387 C  CG    . LEU C 2 68  ? 99.215  111.280 117.719 1.00 32.68 ?  47  LEU C CG    1 
ATOM   11388 C  CD1   . LEU C 2 68  ? 99.982  110.216 118.498 1.00 33.03 ?  47  LEU C CD1   1 
ATOM   11389 C  CD2   . LEU C 2 68  ? 98.910  110.792 116.300 1.00 32.78 ?  47  LEU C CD2   1 
ATOM   11390 N  N     . GLY C 2 69  ? 94.763  111.935 118.570 1.00 30.99 ?  48  GLY C N     1 
ATOM   11391 C  CA    . GLY C 2 69  ? 93.603  111.786 119.447 1.00 30.58 ?  48  GLY C CA    1 
ATOM   11392 C  C     . GLY C 2 69  ? 93.970  111.200 120.804 1.00 29.87 ?  48  GLY C C     1 
ATOM   11393 O  O     . GLY C 2 69  ? 95.033  110.601 120.962 1.00 28.79 ?  48  GLY C O     1 
ATOM   11394 N  N     . LYS C 2 70  ? 93.096  111.384 121.788 1.00 29.89 ?  49  LYS C N     1 
ATOM   11395 C  CA    . LYS C 2 70  ? 93.331  110.844 123.126 1.00 29.49 ?  49  LYS C CA    1 
ATOM   11396 C  C     . LYS C 2 70  ? 93.493  109.312 123.113 1.00 28.74 ?  49  LYS C C     1 
ATOM   11397 O  O     . LYS C 2 70  ? 94.349  108.771 123.825 1.00 27.27 ?  49  LYS C O     1 
ATOM   11398 C  CB    . LYS C 2 70  ? 92.238  111.297 124.099 1.00 30.67 ?  49  LYS C CB    1 
ATOM   11399 C  CG    . LYS C 2 70  ? 92.444  112.746 124.606 1.00 33.73 ?  49  LYS C CG    1 
ATOM   11400 C  CD    . LYS C 2 70  ? 91.178  113.353 125.234 1.00 38.93 ?  49  LYS C CD    1 
ATOM   11401 C  CE    . LYS C 2 70  ? 90.917  112.869 126.666 1.00 41.04 ?  49  LYS C CE    1 
ATOM   11402 N  NZ    . LYS C 2 70  ? 91.866  113.438 127.669 1.00 42.21 1  49  LYS C NZ    1 
ATOM   11403 N  N     . ASN C 2 71  ? 92.683  108.637 122.291 1.00 27.54 ?  50  ASN C N     1 
ATOM   11404 C  CA    . ASN C 2 71  ? 92.788  107.188 122.098 1.00 27.00 ?  50  ASN C CA    1 
ATOM   11405 C  C     . ASN C 2 71  ? 94.159  106.763 121.572 1.00 26.19 ?  50  ASN C C     1 
ATOM   11406 O  O     . ASN C 2 71  ? 94.739  105.760 122.037 1.00 25.38 ?  50  ASN C O     1 
ATOM   11407 C  CB    . ASN C 2 71  ? 91.675  106.668 121.160 1.00 27.08 ?  50  ASN C CB    1 
ATOM   11408 C  CG    . ASN C 2 71  ? 91.710  107.302 119.749 1.00 28.69 ?  50  ASN C CG    1 
ATOM   11409 O  OD1   . ASN C 2 71  ? 91.887  108.524 119.582 1.00 30.45 ?  50  ASN C OD1   1 
ATOM   11410 N  ND2   . ASN C 2 71  ? 91.510  106.460 118.723 1.00 29.42 ?  50  ASN C ND2   1 
ATOM   11411 N  N     . GLU C 2 72  ? 94.668  107.528 120.607 1.00 24.91 ?  51  GLU C N     1 
ATOM   11412 C  CA    . GLU C 2 72  ? 95.952  107.232 119.984 1.00 24.97 ?  51  GLU C CA    1 
ATOM   11413 C  C     . GLU C 2 72  ? 97.109  107.415 120.972 1.00 24.45 ?  51  GLU C C     1 
ATOM   11414 O  O     . GLU C 2 72  ? 98.010  106.565 121.055 1.00 23.90 ?  51  GLU C O     1 
ATOM   11415 C  CB    . GLU C 2 72  ? 96.155  108.102 118.744 1.00 25.27 ?  51  GLU C CB    1 
ATOM   11416 C  CG    . GLU C 2 72  ? 95.177  107.806 117.609 1.00 26.16 ?  51  GLU C CG    1 
ATOM   11417 C  CD    . GLU C 2 72  ? 95.387  108.733 116.420 1.00 28.70 ?  51  GLU C CD    1 
ATOM   11418 O  OE1   . GLU C 2 72  ? 94.965  109.905 116.497 1.00 28.70 ?  51  GLU C OE1   1 
ATOM   11419 O  OE2   . GLU C 2 72  ? 95.974  108.291 115.407 1.00 28.92 -1 51  GLU C OE2   1 
ATOM   11420 N  N     . GLN C 2 73  ? 97.064  108.509 121.731 1.00 23.75 ?  52  GLN C N     1 
ATOM   11421 C  CA    . GLN C 2 73  ? 98.085  108.789 122.736 1.00 23.94 ?  52  GLN C CA    1 
ATOM   11422 C  C     . GLN C 2 73  ? 98.079  107.727 123.838 1.00 23.36 ?  52  GLN C C     1 
ATOM   11423 O  O     . GLN C 2 73  ? 99.134  107.323 124.312 1.00 22.95 ?  52  GLN C O     1 
ATOM   11424 C  CB    . GLN C 2 73  ? 97.879  110.177 123.362 1.00 24.28 ?  52  GLN C CB    1 
ATOM   11425 C  CG    . GLN C 2 73  ? 98.236  111.370 122.454 1.00 25.22 ?  52  GLN C CG    1 
ATOM   11426 C  CD    . GLN C 2 73  ? 98.103  112.724 123.160 1.00 29.02 ?  52  GLN C CD    1 
ATOM   11427 O  OE1   . GLN C 2 73  ? 97.732  112.794 124.330 1.00 32.08 ?  52  GLN C OE1   1 
ATOM   11428 N  NE2   . GLN C 2 73  ? 98.410  113.800 122.445 1.00 29.13 ?  52  GLN C NE2   1 
ATOM   11429 N  N     . ASP C 2 74  ? 96.882  107.310 124.253 1.00 23.02 ?  53  ASP C N     1 
ATOM   11430 C  CA    . ASP C 2 74  ? 96.724  106.294 125.286 1.00 23.44 ?  53  ASP C CA    1 
ATOM   11431 C  C     . ASP C 2 74  ? 97.358  104.970 124.843 1.00 23.00 ?  53  ASP C C     1 
ATOM   11432 O  O     . ASP C 2 74  ? 98.134  104.376 125.587 1.00 22.96 ?  53  ASP C O     1 
ATOM   11433 C  CB    . ASP C 2 74  ? 95.239  106.082 125.614 1.00 23.31 ?  53  ASP C CB    1 
ATOM   11434 C  CG    . ASP C 2 74  ? 95.029  105.163 126.801 1.00 25.80 ?  53  ASP C CG    1 
ATOM   11435 O  OD1   . ASP C 2 74  ? 95.499  105.495 127.920 1.00 27.95 ?  53  ASP C OD1   1 
ATOM   11436 O  OD2   . ASP C 2 74  ? 94.385  104.112 126.616 1.00 26.30 -1 53  ASP C OD2   1 
ATOM   11437 N  N     . THR C 2 75  ? 97.009  104.516 123.641 1.00 22.20 ?  54  THR C N     1 
ATOM   11438 C  CA    . THR C 2 75  ? 97.554  103.281 123.094 1.00 21.84 ?  54  THR C CA    1 
ATOM   11439 C  C     . THR C 2 75  ? 99.070  103.381 122.961 1.00 22.09 ?  54  THR C C     1 
ATOM   11440 O  O     . THR C 2 75  ? 99.786  102.460 123.337 1.00 21.88 ?  54  THR C O     1 
ATOM   11441 C  CB    . THR C 2 75  ? 96.894  102.904 121.738 1.00 21.74 ?  54  THR C CB    1 
ATOM   11442 O  OG1   . THR C 2 75  ? 95.516  102.604 121.968 1.00 22.09 ?  54  THR C OG1   1 
ATOM   11443 C  CG2   . THR C 2 75  ? 97.553  101.661 121.127 1.00 19.76 ?  54  THR C CG2   1 
ATOM   11444 N  N     . TYR C 2 76  ? 99.551  104.506 122.441 1.00 22.38 ?  55  TYR C N     1 
ATOM   11445 C  CA    . TYR C 2 76  ? 100.988 104.720 122.288 1.00 22.85 ?  55  TYR C CA    1 
ATOM   11446 C  C     . TYR C 2 76  ? 101.755 104.622 123.618 1.00 22.56 ?  55  TYR C C     1 
ATOM   11447 O  O     . TYR C 2 76  ? 102.774 103.940 123.683 1.00 21.97 ?  55  TYR C O     1 
ATOM   11448 C  CB    . TYR C 2 76  ? 101.254 106.062 121.618 1.00 23.57 ?  55  TYR C CB    1 
ATOM   11449 C  CG    . TYR C 2 76  ? 102.649 106.228 121.052 1.00 25.59 ?  55  TYR C CG    1 
ATOM   11450 C  CD1   . TYR C 2 76  ? 102.930 105.888 119.724 1.00 27.49 ?  55  TYR C CD1   1 
ATOM   11451 C  CD2   . TYR C 2 76  ? 103.677 106.758 121.830 1.00 27.70 ?  55  TYR C CD2   1 
ATOM   11452 C  CE1   . TYR C 2 76  ? 104.212 106.065 119.191 1.00 30.28 ?  55  TYR C CE1   1 
ATOM   11453 C  CE2   . TYR C 2 76  ? 104.967 106.934 121.309 1.00 30.38 ?  55  TYR C CE2   1 
ATOM   11454 C  CZ    . TYR C 2 76  ? 105.225 106.583 119.989 1.00 31.39 ?  55  TYR C CZ    1 
ATOM   11455 O  OH    . TYR C 2 76  ? 106.492 106.769 119.471 1.00 32.67 ?  55  TYR C OH    1 
ATOM   11456 N  N     . MET C 2 77  ? 101.270 105.303 124.659 1.00 23.14 ?  56  MET C N     1 
ATOM   11457 C  CA    . MET C 2 77  ? 101.911 105.275 125.987 1.00 23.90 ?  56  MET C CA    1 
ATOM   11458 C  C     . MET C 2 77  ? 101.965 103.855 126.533 1.00 23.24 ?  56  MET C C     1 
ATOM   11459 O  O     . MET C 2 77  ? 102.976 103.419 127.098 1.00 22.47 ?  56  MET C O     1 
ATOM   11460 C  CB    . MET C 2 77  ? 101.142 106.139 126.993 1.00 24.38 ?  56  MET C CB    1 
ATOM   11461 C  CG    . MET C 2 77  ? 101.114 107.634 126.712 1.00 28.52 ?  56  MET C CG    1 
ATOM   11462 S  SD    . MET C 2 77  ? 102.661 108.442 127.098 1.00 34.32 ?  56  MET C SD    1 
ATOM   11463 C  CE    . MET C 2 77  ? 102.740 108.251 128.882 1.00 33.84 ?  56  MET C CE    1 
ATOM   11464 N  N     . LYS C 2 78  ? 100.855 103.141 126.368 1.00 23.25 ?  57  LYS C N     1 
ATOM   11465 C  CA    . LYS C 2 78  ? 100.701 101.822 126.970 1.00 22.98 ?  57  LYS C CA    1 
ATOM   11466 C  C     . LYS C 2 78  ? 101.593 100.817 126.256 1.00 22.77 ?  57  LYS C C     1 
ATOM   11467 O  O     . LYS C 2 78  ? 102.256 100.007 126.897 1.00 22.56 ?  57  LYS C O     1 
ATOM   11468 C  CB    . LYS C 2 78  ? 99.225  101.406 126.976 1.00 22.99 ?  57  LYS C CB    1 
ATOM   11469 C  CG    . LYS C 2 78  ? 98.416  102.124 128.059 1.00 24.86 ?  57  LYS C CG    1 
ATOM   11470 C  CD    . LYS C 2 78  ? 96.915  101.859 127.943 1.00 27.37 ?  57  LYS C CD    1 
ATOM   11471 C  CE    . LYS C 2 78  ? 96.168  102.384 129.176 1.00 28.99 ?  57  LYS C CE    1 
ATOM   11472 N  NZ    . LYS C 2 78  ? 94.695  102.296 128.952 1.00 29.82 1  57  LYS C NZ    1 
ATOM   11473 N  N     . VAL C 2 79  ? 101.610 100.907 124.928 1.00 22.70 ?  58  VAL C N     1 
ATOM   11474 C  CA    . VAL C 2 79  ? 102.475 100.109 124.062 1.00 23.48 ?  58  VAL C CA    1 
ATOM   11475 C  C     . VAL C 2 79  ? 103.960 100.227 124.484 1.00 23.04 ?  58  VAL C C     1 
ATOM   11476 O  O     . VAL C 2 79  ? 104.642 99.205  124.704 1.00 22.83 ?  58  VAL C O     1 
ATOM   11477 C  CB    . VAL C 2 79  ? 102.202 100.517 122.580 1.00 24.24 ?  58  VAL C CB    1 
ATOM   11478 C  CG1   . VAL C 2 79  ? 103.449 100.505 121.715 1.00 25.71 ?  58  VAL C CG1   1 
ATOM   11479 C  CG2   . VAL C 2 79  ? 101.055 99.663  121.996 1.00 25.04 ?  58  VAL C CG2   1 
ATOM   11480 N  N     . LEU C 2 80  ? 104.439 101.457 124.646 1.00 22.84 ?  59  LEU C N     1 
ATOM   11481 C  CA    . LEU C 2 80  ? 105.830 101.683 125.045 1.00 23.35 ?  59  LEU C CA    1 
ATOM   11482 C  C     . LEU C 2 80  ? 106.088 101.219 126.483 1.00 22.75 ?  59  LEU C C     1 
ATOM   11483 O  O     . LEU C 2 80  ? 107.178 100.741 126.788 1.00 22.75 ?  59  LEU C O     1 
ATOM   11484 C  CB    . LEU C 2 80  ? 106.243 103.152 124.876 1.00 23.91 ?  59  LEU C CB    1 
ATOM   11485 C  CG    . LEU C 2 80  ? 106.362 103.827 123.495 1.00 26.63 ?  59  LEU C CG    1 
ATOM   11486 C  CD1   . LEU C 2 80  ? 107.196 105.094 123.605 1.00 26.99 ?  59  LEU C CD1   1 
ATOM   11487 C  CD2   . LEU C 2 80  ? 106.954 102.918 122.431 1.00 27.23 ?  59  LEU C CD2   1 
ATOM   11488 N  N     . ALA C 2 81  ? 105.078 101.338 127.349 1.00 22.28 ?  60  ALA C N     1 
ATOM   11489 C  CA    . ALA C 2 81  ? 105.181 100.863 128.732 1.00 22.21 ?  60  ALA C CA    1 
ATOM   11490 C  C     . ALA C 2 81  ? 105.332 99.339  128.791 1.00 22.07 ?  60  ALA C C     1 
ATOM   11491 O  O     . ALA C 2 81  ? 106.138 98.837  129.567 1.00 21.97 ?  60  ALA C O     1 
ATOM   11492 C  CB    . ALA C 2 81  ? 103.980 101.348 129.573 1.00 22.38 ?  60  ALA C CB    1 
ATOM   11493 N  N     . GLY C 2 82  ? 104.585 98.627  127.938 1.00 21.67 ?  61  GLY C N     1 
ATOM   11494 C  CA    . GLY C 2 82  ? 104.696 97.178  127.791 1.00 21.74 ?  61  GLY C CA    1 
ATOM   11495 C  C     . GLY C 2 82  ? 106.074 96.761  127.307 1.00 21.79 ?  61  GLY C C     1 
ATOM   11496 O  O     . GLY C 2 82  ? 106.636 95.755  127.766 1.00 21.93 ?  61  GLY C O     1 
ATOM   11497 N  N     . LEU C 2 83  ? 106.626 97.553  126.389 1.00 21.54 ?  62  LEU C N     1 
ATOM   11498 C  CA    . LEU C 2 83  ? 107.990 97.351  125.903 1.00 21.12 ?  62  LEU C CA    1 
ATOM   11499 C  C     . LEU C 2 83  ? 109.005 97.587  127.012 1.00 20.89 ?  62  LEU C C     1 
ATOM   11500 O  O     . LEU C 2 83  ? 109.957 96.815  127.147 1.00 20.84 ?  62  LEU C O     1 
ATOM   11501 C  CB    . LEU C 2 83  ? 108.304 98.269  124.715 1.00 21.23 ?  62  LEU C CB    1 
ATOM   11502 C  CG    . LEU C 2 83  ? 107.547 98.072  123.395 1.00 21.98 ?  62  LEU C CG    1 
ATOM   11503 C  CD1   . LEU C 2 83  ? 107.882 99.182  122.395 1.00 24.12 ?  62  LEU C CD1   1 
ATOM   11504 C  CD2   . LEU C 2 83  ? 107.826 96.717  122.775 1.00 22.03 ?  62  LEU C CD2   1 
ATOM   11505 N  N     . THR C 2 84  ? 108.800 98.651  127.791 1.00 19.93 ?  63  THR C N     1 
ATOM   11506 C  CA    . THR C 2 84  ? 109.693 98.982  128.899 1.00 19.71 ?  63  THR C CA    1 
ATOM   11507 C  C     . THR C 2 84  ? 109.776 97.831  129.888 1.00 19.63 ?  63  THR C C     1 
ATOM   11508 O  O     . THR C 2 84  ? 110.864 97.506  130.372 1.00 19.62 ?  63  THR C O     1 
ATOM   11509 C  CB    . THR C 2 84  ? 109.239 100.265 129.638 1.00 20.22 ?  63  THR C CB    1 
ATOM   11510 O  OG1   . THR C 2 84  ? 109.028 101.324 128.688 1.00 19.37 ?  63  THR C OG1   1 
ATOM   11511 C  CG2   . THR C 2 84  ? 110.268 100.680 130.661 1.00 19.45 ?  63  THR C CG2   1 
ATOM   11512 N  N     . LEU C 2 85  ? 108.631 97.225  130.191 1.00 19.66 ?  64  LEU C N     1 
ATOM   11513 C  CA    . LEU C 2 85  ? 108.576 96.104  131.125 1.00 20.51 ?  64  LEU C CA    1 
ATOM   11514 C  C     . LEU C 2 85  ? 109.399 94.919  130.610 1.00 20.84 ?  64  LEU C C     1 
ATOM   11515 O  O     . LEU C 2 85  ? 110.236 94.379  131.335 1.00 21.30 ?  64  LEU C O     1 
ATOM   11516 C  CB    . LEU C 2 85  ? 107.125 95.688  131.427 1.00 20.03 ?  64  LEU C CB    1 
ATOM   11517 C  CG    . LEU C 2 85  ? 107.000 94.481  132.385 1.00 21.43 ?  64  LEU C CG    1 
ATOM   11518 C  CD1   . LEU C 2 85  ? 107.517 94.806  133.806 1.00 21.61 ?  64  LEU C CD1   1 
ATOM   11519 C  CD2   . LEU C 2 85  ? 105.575 93.937  132.456 1.00 20.99 ?  64  LEU C CD2   1 
ATOM   11520 N  N     . LEU C 2 86  ? 109.166 94.540  129.359 1.00 21.37 ?  65  LEU C N     1 
ATOM   11521 C  CA    . LEU C 2 86  ? 109.917 93.460  128.714 1.00 21.92 ?  65  LEU C CA    1 
ATOM   11522 C  C     . LEU C 2 86  ? 111.438 93.685  128.753 1.00 21.76 ?  65  LEU C C     1 
ATOM   11523 O  O     . LEU C 2 86  ? 112.184 92.778  129.122 1.00 21.72 ?  65  LEU C O     1 
ATOM   11524 C  CB    . LEU C 2 86  ? 109.447 93.259  127.265 1.00 22.42 ?  65  LEU C CB    1 
ATOM   11525 C  CG    . LEU C 2 86  ? 108.043 92.700  126.956 1.00 24.26 ?  65  LEU C CG    1 
ATOM   11526 C  CD1   . LEU C 2 86  ? 107.795 92.735  125.448 1.00 24.67 ?  65  LEU C CD1   1 
ATOM   11527 C  CD2   . LEU C 2 86  ? 107.873 91.286  127.482 1.00 25.60 ?  65  LEU C CD2   1 
ATOM   11528 N  N     . ASP C 2 87  ? 111.889 94.881  128.371 1.00 21.75 ?  66  ASP C N     1 
ATOM   11529 C  CA    . ASP C 2 87  ? 113.323 95.227  128.418 1.00 21.99 ?  66  ASP C CA    1 
ATOM   11530 C  C     . ASP C 2 87  ? 113.904 95.289  129.835 1.00 21.76 ?  66  ASP C C     1 
ATOM   11531 O  O     . ASP C 2 87  ? 115.079 94.959  130.049 1.00 21.65 ?  66  ASP C O     1 
ATOM   11532 C  CB    . ASP C 2 87  ? 113.587 96.567  127.726 1.00 22.23 ?  66  ASP C CB    1 
ATOM   11533 C  CG    . ASP C 2 87  ? 113.979 96.407  126.283 1.00 24.59 ?  66  ASP C CG    1 
ATOM   11534 O  OD1   . ASP C 2 87  ? 114.788 95.503  125.971 1.00 27.46 ?  66  ASP C OD1   1 
ATOM   11535 O  OD2   . ASP C 2 87  ? 113.481 97.200  125.460 1.00 27.98 -1 66  ASP C OD2   1 
ATOM   11536 N  N     . THR C 2 88  ? 113.093 95.747  130.786 1.00 21.50 ?  67  THR C N     1 
ATOM   11537 C  CA    . THR C 2 88  ? 113.480 95.739  132.192 1.00 21.80 ?  67  THR C CA    1 
ATOM   11538 C  C     . THR C 2 88  ? 113.861 94.314  132.640 1.00 22.04 ?  67  THR C C     1 
ATOM   11539 O  O     . THR C 2 88  ? 114.922 94.107  133.246 1.00 22.21 ?  67  THR C O     1 
ATOM   11540 C  CB    . THR C 2 88  ? 112.366 96.324  133.077 1.00 22.15 ?  67  THR C CB    1 
ATOM   11541 O  OG1   . THR C 2 88  ? 112.111 97.672  132.674 1.00 22.23 ?  67  THR C OG1   1 
ATOM   11542 C  CG2   . THR C 2 88  ? 112.758 96.319  134.558 1.00 21.19 ?  67  THR C CG2   1 
ATOM   11543 N  N     . GLU C 2 89  ? 113.014 93.343  132.311 1.00 21.55 ?  68  GLU C N     1 
ATOM   11544 C  CA    . GLU C 2 89  ? 113.248 91.969  132.734 1.00 21.81 ?  68  GLU C CA    1 
ATOM   11545 C  C     . GLU C 2 89  ? 114.317 91.271  131.879 1.00 21.35 ?  68  GLU C C     1 
ATOM   11546 O  O     . GLU C 2 89  ? 115.094 90.465  132.389 1.00 21.34 ?  68  GLU C O     1 
ATOM   11547 C  CB    . GLU C 2 89  ? 111.931 91.187  132.798 1.00 22.25 ?  68  GLU C CB    1 
ATOM   11548 C  CG    . GLU C 2 89  ? 111.113 91.489  134.086 1.00 24.02 ?  68  GLU C CG    1 
ATOM   11549 C  CD    . GLU C 2 89  ? 111.934 91.306  135.365 1.00 25.78 ?  68  GLU C CD    1 
ATOM   11550 O  OE1   . GLU C 2 89  ? 112.644 90.286  135.492 1.00 26.69 ?  68  GLU C OE1   1 
ATOM   11551 O  OE2   . GLU C 2 89  ? 111.870 92.186  136.255 1.00 28.98 -1 68  GLU C OE2   1 
ATOM   11552 N  N     . GLN C 2 90  ? 114.389 91.622  130.597 1.00 20.82 ?  69  GLN C N     1 
ATOM   11553 C  CA    . GLN C 2 90  ? 115.425 91.088  129.719 1.00 21.28 ?  69  GLN C CA    1 
ATOM   11554 C  C     . GLN C 2 90  ? 116.814 91.556  130.165 1.00 21.24 ?  69  GLN C C     1 
ATOM   11555 O  O     . GLN C 2 90  ? 117.779 90.789  130.104 1.00 20.99 ?  69  GLN C O     1 
ATOM   11556 C  CB    . GLN C 2 90  ? 115.153 91.462  128.251 1.00 21.86 ?  69  GLN C CB    1 
ATOM   11557 C  CG    . GLN C 2 90  ? 115.988 90.653  127.232 1.00 24.29 ?  69  GLN C CG    1 
ATOM   11558 C  CD    . GLN C 2 90  ? 115.572 89.180  127.151 1.00 27.14 ?  69  GLN C CD    1 
ATOM   11559 O  OE1   . GLN C 2 90  ? 114.958 88.643  128.077 1.00 27.13 ?  69  GLN C OE1   1 
ATOM   11560 N  NE2   . GLN C 2 90  ? 115.923 88.521  126.043 1.00 27.69 ?  69  GLN C NE2   1 
ATOM   11561 N  N     . GLY C 2 91  ? 116.895 92.800  130.645 1.00 20.62 ?  70  GLY C N     1 
ATOM   11562 C  CA    . GLY C 2 91  ? 118.155 93.377  131.123 1.00 22.00 ?  70  GLY C CA    1 
ATOM   11563 C  C     . GLY C 2 91  ? 118.519 92.957  132.533 1.00 22.45 ?  70  GLY C C     1 
ATOM   11564 O  O     . GLY C 2 91  ? 119.673 92.623  132.788 1.00 23.53 ?  70  GLY C O     1 
ATOM   11565 N  N     . ASN C 2 92  ? 117.540 92.974  133.441 1.00 22.79 ?  71  ASN C N     1 
ATOM   11566 C  CA    . ASN C 2 92  ? 117.764 92.619  134.852 1.00 23.85 ?  71  ASN C CA    1 
ATOM   11567 C  C     . ASN C 2 92  ? 118.008 91.128  135.051 1.00 24.33 ?  71  ASN C C     1 
ATOM   11568 O  O     . ASN C 2 92  ? 118.790 90.734  135.924 1.00 24.17 ?  71  ASN C O     1 
ATOM   11569 C  CB    . ASN C 2 92  ? 116.558 93.003  135.719 1.00 23.74 ?  71  ASN C CB    1 
ATOM   11570 C  CG    . ASN C 2 92  ? 116.377 94.503  135.876 1.00 24.38 ?  71  ASN C CG    1 
ATOM   11571 O  OD1   . ASN C 2 92  ? 117.125 95.315  135.316 1.00 25.16 ?  71  ASN C OD1   1 
ATOM   11572 N  ND2   . ASN C 2 92  ? 115.364 94.878  136.640 1.00 24.07 ?  71  ASN C ND2   1 
ATOM   11573 N  N     . THR C 2 93  ? 117.340 90.306  134.240 1.00 23.97 ?  72  THR C N     1 
ATOM   11574 C  CA    . THR C 2 93  ? 117.205 88.875  134.552 1.00 24.97 ?  72  THR C CA    1 
ATOM   11575 C  C     . THR C 2 93  ? 117.625 87.979  133.396 1.00 24.52 ?  72  THR C C     1 
ATOM   11576 O  O     . THR C 2 93  ? 118.533 87.171  133.546 1.00 25.39 ?  72  THR C O     1 
ATOM   11577 C  CB    . THR C 2 93  ? 115.753 88.522  134.974 1.00 24.54 ?  72  THR C CB    1 
ATOM   11578 O  OG1   . THR C 2 93  ? 115.342 89.374  136.051 1.00 26.43 ?  72  THR C OG1   1 
ATOM   11579 C  CG2   . THR C 2 93  ? 115.650 87.074  135.427 1.00 26.83 ?  72  THR C CG2   1 
ATOM   11580 N  N     . GLY C 2 94  ? 116.964 88.138  132.259 1.00 24.37 ?  73  GLY C N     1 
ATOM   11581 C  CA    . GLY C 2 94  ? 117.102 87.223  131.115 1.00 24.24 ?  73  GLY C CA    1 
ATOM   11582 C  C     . GLY C 2 94  ? 118.507 87.120  130.561 1.00 24.94 ?  73  GLY C C     1 
ATOM   11583 O  O     . GLY C 2 94  ? 119.104 86.038  130.559 1.00 25.86 ?  73  GLY C O     1 
ATOM   11584 N  N     . MET C 2 95  ? 119.041 88.241  130.089 1.00 24.07 ?  74  MET C N     1 
ATOM   11585 C  CA    . MET C 2 95  ? 120.384 88.231  129.523 1.00 24.35 ?  74  MET C CA    1 
ATOM   11586 C  C     . MET C 2 95  ? 121.505 87.886  130.522 1.00 23.52 ?  74  MET C C     1 
ATOM   11587 O  O     . MET C 2 95  ? 122.367 87.087  130.170 1.00 23.40 ?  74  MET C O     1 
ATOM   11588 C  CB    . MET C 2 95  ? 120.674 89.516  128.747 1.00 24.38 ?  74  MET C CB    1 
ATOM   11589 C  CG    . MET C 2 95  ? 119.897 89.636  127.435 1.00 27.47 ?  74  MET C CG    1 
ATOM   11590 S  SD    . MET C 2 95  ? 120.348 88.304  126.290 1.00 32.54 ?  74  MET C SD    1 
ATOM   11591 C  CE    . MET C 2 95  ? 121.971 88.803  125.832 1.00 34.32 ?  74  MET C CE    1 
ATOM   11592 N  N     . PRO C 2 96  ? 121.498 88.470  131.754 1.00 23.36 ?  75  PRO C N     1 
ATOM   11593 C  CA    . PRO C 2 96  ? 122.512 88.086  132.759 1.00 23.27 ?  75  PRO C CA    1 
ATOM   11594 C  C     . PRO C 2 96  ? 122.489 86.610  133.143 1.00 23.77 ?  75  PRO C C     1 
ATOM   11595 O  O     . PRO C 2 96  ? 123.551 86.005  133.289 1.00 23.46 ?  75  PRO C O     1 
ATOM   11596 C  CB    . PRO C 2 96  ? 122.138 88.928  133.990 1.00 23.55 ?  75  PRO C CB    1 
ATOM   11597 C  CG    . PRO C 2 96  ? 121.442 90.121  133.432 1.00 23.85 ?  75  PRO C CG    1 
ATOM   11598 C  CD    . PRO C 2 96  ? 120.663 89.587  132.240 1.00 22.76 ?  75  PRO C CD    1 
ATOM   11599 N  N     . ILE C 2 97  ? 121.297 86.039  133.329 1.00 23.81 ?  76  ILE C N     1 
ATOM   11600 C  CA    . ILE C 2 97  ? 121.185 84.624  133.693 1.00 24.52 ?  76  ILE C CA    1 
ATOM   11601 C  C     . ILE C 2 97  ? 121.659 83.671  132.575 1.00 23.92 ?  76  ILE C C     1 
ATOM   11602 O  O     . ILE C 2 97  ? 122.365 82.687  132.840 1.00 23.99 ?  76  ILE C O     1 
ATOM   11603 C  CB    . ILE C 2 97  ? 119.766 84.265  134.219 1.00 24.49 ?  76  ILE C CB    1 
ATOM   11604 C  CG1   . ILE C 2 97  ? 119.818 83.012  135.090 1.00 27.08 ?  76  ILE C CG1   1 
ATOM   11605 C  CG2   . ILE C 2 97  ? 118.748 84.086  133.073 1.00 26.06 ?  76  ILE C CG2   1 
ATOM   11606 C  CD1   . ILE C 2 97  ? 118.674 82.940  136.090 1.00 31.37 ?  76  ILE C CD1   1 
ATOM   11607 N  N     . VAL C 2 98  ? 121.303 83.976  131.331 1.00 23.97 ?  77  VAL C N     1 
ATOM   11608 C  CA    . VAL C 2 98  ? 121.818 83.212  130.186 1.00 24.01 ?  77  VAL C CA    1 
ATOM   11609 C  C     . VAL C 2 98  ? 123.351 83.368  130.097 1.00 25.23 ?  77  VAL C C     1 
ATOM   11610 O  O     . VAL C 2 98  ? 124.070 82.382  129.905 1.00 25.77 ?  77  VAL C O     1 
ATOM   11611 C  CB    . VAL C 2 98  ? 121.113 83.615  128.865 1.00 23.98 ?  77  VAL C CB    1 
ATOM   11612 C  CG1   . VAL C 2 98  ? 121.834 83.031  127.653 1.00 23.17 ?  77  VAL C CG1   1 
ATOM   11613 C  CG2   . VAL C 2 98  ? 119.651 83.152  128.894 1.00 22.55 ?  77  VAL C CG2   1 
ATOM   11614 N  N     . ALA C 2 99  ? 123.849 84.590  130.294 1.00 25.42 ?  78  ALA C N     1 
ATOM   11615 C  CA    . ALA C 2 99  ? 125.303 84.824  130.314 1.00 26.72 ?  78  ALA C CA    1 
ATOM   11616 C  C     . ALA C 2 99  ? 125.998 83.935  131.350 1.00 27.46 ?  78  ALA C C     1 
ATOM   11617 O  O     . ALA C 2 99  ? 127.050 83.361  131.072 1.00 28.07 ?  78  ALA C O     1 
ATOM   11618 C  CB    . ALA C 2 99  ? 125.618 86.285  130.574 1.00 26.52 ?  78  ALA C CB    1 
ATOM   11619 N  N     . GLU C 2 100 ? 125.381 83.795  132.522 1.00 28.33 ?  79  GLU C N     1 
ATOM   11620 C  CA    . GLU C 2 100 ? 125.950 82.997  133.611 1.00 29.60 ?  79  GLU C CA    1 
ATOM   11621 C  C     . GLU C 2 100 ? 126.142 81.529  133.222 1.00 29.64 ?  79  GLU C C     1 
ATOM   11622 O  O     . GLU C 2 100 ? 127.131 80.896  133.609 1.00 29.72 ?  79  GLU C O     1 
ATOM   11623 C  CB    . GLU C 2 100 ? 125.087 83.111  134.868 1.00 29.70 ?  79  GLU C CB    1 
ATOM   11624 C  CG    . GLU C 2 100 ? 125.651 82.370  136.081 1.00 33.58 ?  79  GLU C CG    1 
ATOM   11625 C  CD    . GLU C 2 100 ? 124.729 82.381  137.284 1.00 37.83 ?  79  GLU C CD    1 
ATOM   11626 O  OE1   . GLU C 2 100 ? 123.697 83.096  137.275 1.00 40.64 ?  79  GLU C OE1   1 
ATOM   11627 O  OE2   . GLU C 2 100 ? 125.037 81.654  138.253 1.00 41.40 -1 79  GLU C OE2   1 
ATOM   11628 N  N     . HIS C 2 101 ? 125.207 80.995  132.439 1.00 29.43 ?  80  HIS C N     1 
ATOM   11629 C  CA    . HIS C 2 101 ? 125.191 79.568  132.148 1.00 29.74 ?  80  HIS C CA    1 
ATOM   11630 C  C     . HIS C 2 101 ? 125.871 79.166  130.838 1.00 30.18 ?  80  HIS C C     1 
ATOM   11631 O  O     . HIS C 2 101 ? 126.183 77.998  130.639 1.00 30.30 ?  80  HIS C O     1 
ATOM   11632 C  CB    . HIS C 2 101 ? 123.759 79.018  132.261 1.00 29.21 ?  80  HIS C CB    1 
ATOM   11633 C  CG    . HIS C 2 101 ? 123.252 78.989  133.670 1.00 29.60 ?  80  HIS C CG    1 
ATOM   11634 N  ND1   . HIS C 2 101 ? 122.554 80.036  134.235 1.00 30.06 ?  80  HIS C ND1   1 
ATOM   11635 C  CD2   . HIS C 2 101 ? 123.382 78.056  134.642 1.00 29.49 ?  80  HIS C CD2   1 
ATOM   11636 C  CE1   . HIS C 2 101 ? 122.263 79.744  135.491 1.00 29.56 ?  80  HIS C CE1   1 
ATOM   11637 N  NE2   . HIS C 2 101 ? 122.752 78.548  135.762 1.00 30.20 ?  80  HIS C NE2   1 
ATOM   11638 N  N     . VAL C 2 102 ? 126.112 80.135  129.960 1.00 30.70 ?  81  VAL C N     1 
ATOM   11639 C  CA    . VAL C 2 102 ? 126.782 79.888  128.686 1.00 31.47 ?  81  VAL C CA    1 
ATOM   11640 C  C     . VAL C 2 102 ? 128.295 79.934  128.888 1.00 32.45 ?  81  VAL C C     1 
ATOM   11641 O  O     . VAL C 2 102 ? 128.811 80.877  129.499 1.00 32.50 ?  81  VAL C O     1 
ATOM   11642 C  CB    . VAL C 2 102 ? 126.357 80.910  127.599 1.00 31.18 ?  81  VAL C CB    1 
ATOM   11643 C  CG1   . VAL C 2 102 ? 127.217 80.770  126.340 1.00 31.20 ?  81  VAL C CG1   1 
ATOM   11644 C  CG2   . VAL C 2 102 ? 124.890 80.723  127.241 1.00 31.28 ?  81  VAL C CG2   1 
ATOM   11645 N  N     . ASP C 2 103 ? 128.991 78.923  128.363 1.00 33.38 ?  82  ASP C N     1 
ATOM   11646 C  CA    . ASP C 2 103 ? 130.446 78.809  128.502 1.00 34.82 ?  82  ASP C CA    1 
ATOM   11647 C  C     . ASP C 2 103 ? 131.214 79.571  127.429 1.00 34.74 ?  82  ASP C C     1 
ATOM   11648 O  O     . ASP C 2 103 ? 130.812 79.595  126.259 1.00 35.00 ?  82  ASP C O     1 
ATOM   11649 C  CB    . ASP C 2 103 ? 130.879 77.335  128.498 1.00 35.82 ?  82  ASP C CB    1 
ATOM   11650 C  CG    . ASP C 2 103 ? 130.526 76.611  129.794 1.00 38.29 ?  82  ASP C CG    1 
ATOM   11651 O  OD1   . ASP C 2 103 ? 130.527 77.250  130.875 1.00 41.49 ?  82  ASP C OD1   1 
ATOM   11652 O  OD2   . ASP C 2 103 ? 130.249 75.398  129.735 1.00 41.10 -1 82  ASP C OD2   1 
ATOM   11653 N  N     . GLY C 2 104 ? 132.324 80.184  127.839 1.00 34.89 ?  83  GLY C N     1 
ATOM   11654 C  CA    . GLY C 2 104 ? 133.224 80.891  126.921 1.00 35.11 ?  83  GLY C CA    1 
ATOM   11655 C  C     . GLY C 2 104 ? 133.205 82.395  127.118 1.00 34.96 ?  83  GLY C C     1 
ATOM   11656 O  O     . GLY C 2 104 ? 132.147 83.021  127.020 1.00 34.57 ?  83  GLY C O     1 
ATOM   11657 N  N     . HIS C 2 105 ? 134.380 82.972  127.380 1.00 35.02 ?  84  HIS C N     1 
ATOM   11658 C  CA    . HIS C 2 105 ? 134.503 84.401  127.705 1.00 34.83 ?  84  HIS C CA    1 
ATOM   11659 C  C     . HIS C 2 105 ? 133.974 85.336  126.625 1.00 33.77 ?  84  HIS C C     1 
ATOM   11660 O  O     . HIS C 2 105 ? 133.408 86.386  126.937 1.00 33.25 ?  84  HIS C O     1 
ATOM   11661 C  CB    . HIS C 2 105 ? 135.944 84.771  128.074 1.00 36.09 ?  84  HIS C CB    1 
ATOM   11662 C  CG    . HIS C 2 105 ? 136.347 84.313  129.443 1.00 39.17 ?  84  HIS C CG    1 
ATOM   11663 N  ND1   . HIS C 2 105 ? 137.633 83.918  129.750 1.00 43.00 ?  84  HIS C ND1   1 
ATOM   11664 C  CD2   . HIS C 2 105 ? 135.627 84.167  130.583 1.00 41.84 ?  84  HIS C CD2   1 
ATOM   11665 C  CE1   . HIS C 2 105 ? 137.689 83.558  131.022 1.00 43.47 ?  84  HIS C CE1   1 
ATOM   11666 N  NE2   . HIS C 2 105 ? 136.485 83.700  131.550 1.00 43.10 ?  84  HIS C NE2   1 
ATOM   11667 N  N     . GLN C 2 106 ? 134.137 84.952  125.365 1.00 32.84 ?  85  GLN C N     1 
ATOM   11668 C  CA    . GLN C 2 106 ? 133.631 85.774  124.270 1.00 32.29 ?  85  GLN C CA    1 
ATOM   11669 C  C     . GLN C 2 106 ? 132.104 85.709  124.153 1.00 30.88 ?  85  GLN C C     1 
ATOM   11670 O  O     . GLN C 2 106 ? 131.455 86.734  123.914 1.00 30.44 ?  85  GLN C O     1 
ATOM   11671 C  CB    . GLN C 2 106 ? 134.288 85.393  122.952 1.00 32.85 ?  85  GLN C CB    1 
ATOM   11672 C  CG    . GLN C 2 106 ? 135.782 85.686  122.909 1.00 35.55 ?  85  GLN C CG    1 
ATOM   11673 C  CD    . GLN C 2 106 ? 136.419 85.198  121.635 1.00 38.12 ?  85  GLN C CD    1 
ATOM   11674 O  OE1   . GLN C 2 106 ? 135.821 85.277  120.562 1.00 39.96 ?  85  GLN C OE1   1 
ATOM   11675 N  NE2   . GLN C 2 106 ? 137.644 84.689  121.742 1.00 40.39 ?  85  GLN C NE2   1 
ATOM   11676 N  N     . ARG C 2 107 ? 131.539 84.514  124.315 1.00 29.75 ?  86  ARG C N     1 
ATOM   11677 C  CA    . ARG C 2 107 ? 130.079 84.358  124.325 1.00 28.87 ?  86  ARG C CA    1 
ATOM   11678 C  C     . ARG C 2 107 ? 129.490 85.153  125.482 1.00 28.16 ?  86  ARG C C     1 
ATOM   11679 O  O     . ARG C 2 107 ? 128.476 85.829  125.316 1.00 27.55 ?  86  ARG C O     1 
ATOM   11680 C  CB    . ARG C 2 107 ? 129.673 82.889  124.434 1.00 28.48 ?  86  ARG C CB    1 
ATOM   11681 C  CG    . ARG C 2 107 ? 129.931 82.098  123.164 1.00 29.86 ?  86  ARG C CG    1 
ATOM   11682 C  CD    . ARG C 2 107 ? 129.554 80.633  123.311 1.00 30.23 ?  86  ARG C CD    1 
ATOM   11683 N  NE    . ARG C 2 107 ? 129.389 80.052  121.985 1.00 33.04 ?  86  ARG C NE    1 
ATOM   11684 C  CZ    . ARG C 2 107 ? 128.733 78.934  121.723 1.00 31.54 ?  86  ARG C CZ    1 
ATOM   11685 N  NH1   . ARG C 2 107 ? 128.179 78.234  122.703 1.00 31.85 1  86  ARG C NH1   1 
ATOM   11686 N  NH2   . ARG C 2 107 ? 128.643 78.518  120.471 1.00 34.74 ?  86  ARG C NH2   1 
ATOM   11687 N  N     . LYS C 2 108 ? 130.138 85.081  126.643 1.00 27.65 ?  87  LYS C N     1 
ATOM   11688 C  CA    . LYS C 2 108 ? 129.698 85.851  127.811 1.00 27.96 ?  87  LYS C CA    1 
ATOM   11689 C  C     . LYS C 2 108 ? 129.792 87.354  127.597 1.00 27.75 ?  87  LYS C C     1 
ATOM   11690 O  O     . LYS C 2 108 ? 128.927 88.095  128.064 1.00 28.29 ?  87  LYS C O     1 
ATOM   11691 C  CB    . LYS C 2 108 ? 130.470 85.459  129.071 1.00 27.80 ?  87  LYS C CB    1 
ATOM   11692 C  CG    . LYS C 2 108 ? 130.150 84.067  129.575 1.00 29.04 ?  87  LYS C CG    1 
ATOM   11693 C  CD    . LYS C 2 108 ? 130.940 83.781  130.844 1.00 31.15 ?  87  LYS C CD    1 
ATOM   11694 C  CE    . LYS C 2 108 ? 130.814 82.326  131.259 1.00 32.05 ?  87  LYS C CE    1 
ATOM   11695 N  NZ    . LYS C 2 108 ? 129.506 82.073  131.912 1.00 30.88 1  87  LYS C NZ    1 
ATOM   11696 N  N     . ALA C 2 109 ? 130.832 87.804  126.895 1.00 27.69 ?  88  ALA C N     1 
ATOM   11697 C  CA    . ALA C 2 109 ? 130.991 89.233  126.591 1.00 27.46 ?  88  ALA C CA    1 
ATOM   11698 C  C     . ALA C 2 109 ? 129.871 89.775  125.699 1.00 26.87 ?  88  ALA C C     1 
ATOM   11699 O  O     . ALA C 2 109 ? 129.402 90.894  125.899 1.00 26.47 ?  88  ALA C O     1 
ATOM   11700 C  CB    . ALA C 2 109 ? 132.341 89.498  125.957 1.00 27.98 ?  88  ALA C CB    1 
ATOM   11701 N  N     . VAL C 2 110 ? 129.461 88.984  124.709 1.00 25.98 ?  89  VAL C N     1 
ATOM   11702 C  CA    . VAL C 2 110 ? 128.350 89.351  123.828 1.00 25.46 ?  89  VAL C CA    1 
ATOM   11703 C  C     . VAL C 2 110 ? 127.049 89.426  124.635 1.00 24.57 ?  89  VAL C C     1 
ATOM   11704 O  O     . VAL C 2 110 ? 126.326 90.425  124.572 1.00 23.62 ?  89  VAL C O     1 
ATOM   11705 C  CB    . VAL C 2 110 ? 128.209 88.360  122.646 1.00 25.80 ?  89  VAL C CB    1 
ATOM   11706 C  CG1   . VAL C 2 110 ? 126.909 88.596  121.866 1.00 25.44 ?  89  VAL C CG1   1 
ATOM   11707 C  CG2   . VAL C 2 110 ? 129.420 88.466  121.720 1.00 26.23 ?  89  VAL C CG2   1 
ATOM   11708 N  N     . LEU C 2 111 ? 126.779 88.385  125.420 1.00 24.33 ?  90  LEU C N     1 
ATOM   11709 C  CA    . LEU C 2 111 ? 125.559 88.346  126.226 1.00 23.93 ?  90  LEU C CA    1 
ATOM   11710 C  C     . LEU C 2 111 ? 125.504 89.451  127.282 1.00 23.77 ?  90  LEU C C     1 
ATOM   11711 O  O     . LEU C 2 111 ? 124.438 90.017  127.524 1.00 23.04 ?  90  LEU C O     1 
ATOM   11712 C  CB    . LEU C 2 111 ? 125.345 86.967  126.855 1.00 23.73 ?  90  LEU C CB    1 
ATOM   11713 C  CG    . LEU C 2 111 ? 125.124 85.832  125.850 1.00 24.50 ?  90  LEU C CG    1 
ATOM   11714 C  CD1   . LEU C 2 111 ? 125.391 84.479  126.490 1.00 24.02 ?  90  LEU C CD1   1 
ATOM   11715 C  CD2   . LEU C 2 111 ? 123.720 85.883  125.241 1.00 25.38 ?  90  LEU C CD2   1 
ATOM   11716 N  N     . ASN C 2 112 ? 126.646 89.745  127.914 1.00 24.24 ?  91  ASN C N     1 
ATOM   11717 C  CA    . ASN C 2 112 ? 126.743 90.883  128.842 1.00 24.95 ?  91  ASN C CA    1 
ATOM   11718 C  C     . ASN C 2 112 ? 126.476 92.229  128.174 1.00 24.25 ?  91  ASN C C     1 
ATOM   11719 O  O     . ASN C 2 112 ? 125.822 93.093  128.757 1.00 23.99 ?  91  ASN C O     1 
ATOM   11720 C  CB    . ASN C 2 112 ? 128.112 90.932  129.526 1.00 25.81 ?  91  ASN C CB    1 
ATOM   11721 C  CG    . ASN C 2 112 ? 128.169 90.073  130.759 1.00 29.96 ?  91  ASN C CG    1 
ATOM   11722 O  OD1   . ASN C 2 112 ? 127.890 90.546  131.863 1.00 35.44 ?  91  ASN C OD1   1 
ATOM   11723 N  ND2   . ASN C 2 112 ? 128.527 88.800  130.590 1.00 32.37 ?  91  ASN C ND2   1 
ATOM   11724 N  N     . PHE C 2 113 ? 127.017 92.414  126.970 1.00 23.60 ?  92  PHE C N     1 
ATOM   11725 C  CA    . PHE C 2 113 ? 126.767 93.629  126.202 1.00 23.32 ?  92  PHE C CA    1 
ATOM   11726 C  C     . PHE C 2 113 ? 125.277 93.776  125.860 1.00 22.63 ?  92  PHE C C     1 
ATOM   11727 O  O     . PHE C 2 113 ? 124.711 94.860  126.010 1.00 21.94 ?  92  PHE C O     1 
ATOM   11728 C  CB    . PHE C 2 113 ? 127.581 93.647  124.900 1.00 23.27 ?  92  PHE C CB    1 
ATOM   11729 C  CG    . PHE C 2 113 ? 127.552 94.977  124.198 1.00 24.66 ?  92  PHE C CG    1 
ATOM   11730 C  CD1   . PHE C 2 113 ? 128.504 95.960  124.501 1.00 25.72 ?  92  PHE C CD1   1 
ATOM   11731 C  CD2   . PHE C 2 113 ? 126.565 95.263  123.259 1.00 25.36 ?  92  PHE C CD2   1 
ATOM   11732 C  CE1   . PHE C 2 113 ? 128.472 97.203  123.867 1.00 25.92 ?  92  PHE C CE1   1 
ATOM   11733 C  CE2   . PHE C 2 113 ? 126.521 96.507  122.618 1.00 25.82 ?  92  PHE C CE2   1 
ATOM   11734 C  CZ    . PHE C 2 113 ? 127.474 97.480  122.927 1.00 25.80 ?  92  PHE C CZ    1 
ATOM   11735 N  N     . MET C 2 114 ? 124.668 92.688  125.381 1.00 22.03 ?  93  MET C N     1 
ATOM   11736 C  CA    . MET C 2 114 ? 123.229 92.669  125.084 1.00 22.14 ?  93  MET C CA    1 
ATOM   11737 C  C     . MET C 2 114 ? 122.377 93.001  126.322 1.00 21.64 ?  93  MET C C     1 
ATOM   11738 O  O     . MET C 2 114 ? 121.423 93.780  126.226 1.00 21.59 ?  93  MET C O     1 
ATOM   11739 C  CB    . MET C 2 114 ? 122.820 91.323  124.496 1.00 22.46 ?  93  MET C CB    1 
ATOM   11740 C  CG    . MET C 2 114 ? 123.381 91.066  123.107 1.00 23.80 ?  93  MET C CG    1 
ATOM   11741 S  SD    . MET C 2 114 ? 123.034 89.391  122.527 1.00 28.07 ?  93  MET C SD    1 
ATOM   11742 C  CE    . MET C 2 114 ? 123.510 89.572  120.789 1.00 26.42 ?  93  MET C CE    1 
ATOM   11743 N  N     . ALA C 2 115 ? 122.746 92.440  127.478 1.00 20.98 ?  94  ALA C N     1 
ATOM   11744 C  CA    . ALA C 2 115 ? 122.090 92.758  128.760 1.00 20.58 ?  94  ALA C CA    1 
ATOM   11745 C  C     . ALA C 2 115 ? 122.143 94.245  129.104 1.00 21.01 ?  94  ALA C C     1 
ATOM   11746 O  O     . ALA C 2 115 ? 121.147 94.835  129.562 1.00 21.06 ?  94  ALA C O     1 
ATOM   11747 C  CB    . ALA C 2 115 ? 122.713 91.921  129.903 1.00 20.83 ?  94  ALA C CB    1 
ATOM   11748 N  N     . MET C 2 116 ? 123.318 94.846  128.921 1.00 20.36 ?  95  MET C N     1 
ATOM   11749 C  CA    . MET C 2 116 ? 123.492 96.266  129.165 1.00 20.83 ?  95  MET C CA    1 
ATOM   11750 C  C     . MET C 2 116 ? 122.563 97.085  128.254 1.00 20.55 ?  95  MET C C     1 
ATOM   11751 O  O     . MET C 2 116 ? 121.893 98.010  128.711 1.00 20.70 ?  95  MET C O     1 
ATOM   11752 C  CB    . MET C 2 116 ? 124.964 96.653  128.969 1.00 20.64 ?  95  MET C CB    1 
ATOM   11753 C  CG    . MET C 2 116 ? 125.266 98.148  129.074 1.00 21.42 ?  95  MET C CG    1 
ATOM   11754 S  SD    . MET C 2 116 ? 124.867 99.036  127.556 1.00 22.51 ?  95  MET C SD    1 
ATOM   11755 C  CE    . MET C 2 116 ? 125.942 98.226  126.370 1.00 20.66 ?  95  MET C CE    1 
ATOM   11756 N  N     . MET C 2 117 ? 122.512 96.723  126.977 1.00 20.50 ?  96  MET C N     1 
ATOM   11757 C  CA    . MET C 2 117 ? 121.648 97.414  126.029 1.00 21.22 ?  96  MET C CA    1 
ATOM   11758 C  C     . MET C 2 117 ? 120.189 97.382  126.480 1.00 21.11 ?  96  MET C C     1 
ATOM   11759 O  O     . MET C 2 117 ? 119.506 98.408  126.424 1.00 20.71 ?  96  MET C O     1 
ATOM   11760 C  CB    . MET C 2 117 ? 121.803 96.841  124.613 1.00 21.35 ?  96  MET C CB    1 
ATOM   11761 C  CG    . MET C 2 117 ? 123.144 97.197  123.898 1.00 22.54 ?  96  MET C CG    1 
ATOM   11762 S  SD    . MET C 2 117 ? 123.541 98.957  123.793 1.00 24.89 ?  96  MET C SD    1 
ATOM   11763 C  CE    . MET C 2 117 ? 122.414 99.494  122.506 1.00 24.95 ?  96  MET C CE    1 
ATOM   11764 N  N     . GLU C 2 118 ? 119.732 96.219  126.944 1.00 21.18 ?  97  GLU C N     1 
ATOM   11765 C  CA    . GLU C 2 118 ? 118.347 96.043  127.396 1.00 21.99 ?  97  GLU C CA    1 
ATOM   11766 C  C     . GLU C 2 118 ? 117.938 97.062  128.461 1.00 22.10 ?  97  GLU C C     1 
ATOM   11767 O  O     . GLU C 2 118 ? 116.951 97.780  128.289 1.00 22.22 ?  97  GLU C O     1 
ATOM   11768 C  CB    . GLU C 2 118 ? 118.086 94.620  127.918 1.00 22.01 ?  97  GLU C CB    1 
ATOM   11769 C  CG    . GLU C 2 118 ? 118.453 93.454  126.992 1.00 24.38 ?  97  GLU C CG    1 
ATOM   11770 C  CD    . GLU C 2 118 ? 117.718 93.433  125.645 1.00 26.32 ?  97  GLU C CD    1 
ATOM   11771 O  OE1   . GLU C 2 118 ? 117.384 94.493  125.098 1.00 29.86 ?  97  GLU C OE1   1 
ATOM   11772 O  OE2   . GLU C 2 118 ? 117.519 92.335  125.100 1.00 29.19 -1 97  GLU C OE2   1 
ATOM   11773 N  N     . ASN C 2 119 ? 118.689 97.130  129.559 1.00 22.26 ?  98  ASN C N     1 
ATOM   11774 C  CA    . ASN C 2 119 ? 118.265 97.984  130.669 1.00 21.91 ?  98  ASN C CA    1 
ATOM   11775 C  C     . ASN C 2 119 ? 118.921 99.369  130.770 1.00 22.41 ?  98  ASN C C     1 
ATOM   11776 O  O     . ASN C 2 119 ? 118.306 100.305 131.276 1.00 23.07 ?  98  ASN C O     1 
ATOM   11777 C  CB    . ASN C 2 119 ? 118.210 97.226  132.014 1.00 21.93 ?  98  ASN C CB    1 
ATOM   11778 C  CG    . ASN C 2 119 ? 119.558 96.713  132.473 1.00 21.31 ?  98  ASN C CG    1 
ATOM   11779 O  OD1   . ASN C 2 119 ? 120.574 96.873  131.794 1.00 21.88 ?  98  ASN C OD1   1 
ATOM   11780 N  ND2   . ASN C 2 119 ? 119.574 96.097  133.654 1.00 21.73 ?  98  ASN C ND2   1 
ATOM   11781 N  N     . ALA C 2 120 ? 120.161 99.493  130.303 1.00 22.75 ?  99  ALA C N     1 
ATOM   11782 C  CA    . ALA C 2 120 ? 120.866 100.775 130.330 1.00 23.12 ?  99  ALA C CA    1 
ATOM   11783 C  C     . ALA C 2 120 ? 120.572 101.636 129.117 1.00 23.60 ?  99  ALA C C     1 
ATOM   11784 O  O     . ALA C 2 120 ? 120.713 102.860 129.192 1.00 24.14 ?  99  ALA C O     1 
ATOM   11785 C  CB    . ALA C 2 120 ? 122.386 100.580 130.502 1.00 23.28 ?  99  ALA C CB    1 
ATOM   11786 N  N     . VAL C 2 121 ? 120.160 101.014 128.007 1.00 23.23 ?  100 VAL C N     1 
ATOM   11787 C  CA    . VAL C 2 121 ? 119.861 101.784 126.785 1.00 23.74 ?  100 VAL C CA    1 
ATOM   11788 C  C     . VAL C 2 121 ? 118.391 101.730 126.367 1.00 23.62 ?  100 VAL C C     1 
ATOM   11789 O  O     . VAL C 2 121 ? 117.747 102.770 126.274 1.00 24.51 ?  100 VAL C O     1 
ATOM   11790 C  CB    . VAL C 2 121 ? 120.774 101.395 125.603 1.00 23.19 ?  100 VAL C CB    1 
ATOM   11791 C  CG1   . VAL C 2 121 ? 120.396 102.184 124.336 1.00 24.10 ?  100 VAL C CG1   1 
ATOM   11792 C  CG2   . VAL C 2 121 ? 122.247 101.637 125.968 1.00 23.48 ?  100 VAL C CG2   1 
ATOM   11793 N  N     . HIS C 2 122 ? 117.872 100.527 126.129 1.00 23.45 ?  101 HIS C N     1 
ATOM   11794 C  CA    . HIS C 2 122 ? 116.508 100.365 125.618 1.00 23.81 ?  101 HIS C CA    1 
ATOM   11795 C  C     . HIS C 2 122 ? 115.442 100.800 126.602 1.00 24.33 ?  101 HIS C C     1 
ATOM   11796 O  O     . HIS C 2 122 ? 114.619 101.659 126.271 1.00 24.80 ?  101 HIS C O     1 
ATOM   11797 C  CB    . HIS C 2 122 ? 116.227 98.927  125.192 1.00 23.30 ?  101 HIS C CB    1 
ATOM   11798 C  CG    . HIS C 2 122 ? 117.093 98.444  124.072 1.00 22.96 ?  101 HIS C CG    1 
ATOM   11799 N  ND1   . HIS C 2 122 ? 117.077 97.136  123.636 1.00 22.78 ?  101 HIS C ND1   1 
ATOM   11800 C  CD2   . HIS C 2 122 ? 118.023 99.083  123.325 1.00 23.25 ?  101 HIS C CD2   1 
ATOM   11801 C  CE1   . HIS C 2 122 ? 117.950 96.996  122.655 1.00 22.57 ?  101 HIS C CE1   1 
ATOM   11802 N  NE2   . HIS C 2 122 ? 118.536 98.161  122.447 1.00 21.75 ?  101 HIS C NE2   1 
ATOM   11803 N  N     . ALA C 2 123 ? 115.434 100.188 127.789 1.00 24.40 ?  102 ALA C N     1 
ATOM   11804 C  CA    . ALA C 2 123 ? 114.417 100.500 128.796 1.00 24.00 ?  102 ALA C CA    1 
ATOM   11805 C  C     . ALA C 2 123 ? 114.437 101.992 129.133 1.00 24.05 ?  102 ALA C C     1 
ATOM   11806 O  O     . ALA C 2 123 ? 113.383 102.605 129.287 1.00 23.89 ?  102 ALA C O     1 
ATOM   11807 C  CB    . ALA C 2 123 ? 114.605 99.647  130.050 1.00 23.73 ?  102 ALA C CB    1 
ATOM   11808 N  N     . LYS C 2 124 ? 115.633 102.571 129.225 1.00 24.36 ?  103 LYS C N     1 
ATOM   11809 C  CA    . LYS C 2 124 ? 115.787 103.996 129.539 1.00 24.31 ?  103 LYS C CA    1 
ATOM   11810 C  C     . LYS C 2 124 ? 115.279 104.940 128.443 1.00 23.84 ?  103 LYS C C     1 
ATOM   11811 O  O     . LYS C 2 124 ? 114.679 105.978 128.750 1.00 24.21 ?  103 LYS C O     1 
ATOM   11812 C  CB    . LYS C 2 124 ? 117.227 104.339 129.934 1.00 24.93 ?  103 LYS C CB    1 
ATOM   11813 C  CG    . LYS C 2 124 ? 117.376 105.765 130.483 1.00 26.37 ?  103 LYS C CG    1 
ATOM   11814 C  CD    . LYS C 2 124 ? 118.767 106.026 131.037 1.00 29.42 ?  103 LYS C CD    1 
ATOM   11815 C  CE    . LYS C 2 124 ? 118.933 107.501 131.414 1.00 31.51 ?  103 LYS C CE    1 
ATOM   11816 N  NZ    . LYS C 2 124 ? 118.862 108.402 130.225 1.00 32.37 1  103 LYS C NZ    1 
ATOM   11817 N  N     . SER C 2 125 ? 115.504 104.578 127.178 1.00 23.52 ?  104 SER C N     1 
ATOM   11818 C  CA    . SER C 2 125 ? 115.030 105.367 126.035 0.50 23.23 ?  104 SER C CA    1 
ATOM   11819 C  C     . SER C 2 125 ? 113.526 105.635 126.104 1.00 22.91 ?  104 SER C C     1 
ATOM   11820 O  O     . SER C 2 125 ? 113.059 106.695 125.708 1.00 22.33 ?  104 SER C O     1 
ATOM   11821 C  CB    . SER C 2 125 ? 115.356 104.663 124.713 0.50 23.25 ?  104 SER C CB    1 
ATOM   11822 O  OG    . SER C 2 125 ? 116.750 104.470 124.557 0.50 24.57 ?  104 SER C OG    1 
ATOM   11823 N  N     . TYR C 2 126 ? 112.762 104.661 126.593 1.00 22.72 ?  105 TYR C N     1 
ATOM   11824 C  CA    . TYR C 2 126 ? 111.314 104.849 126.690 1.00 23.34 ?  105 TYR C CA    1 
ATOM   11825 C  C     . TYR C 2 126 ? 110.962 105.957 127.655 1.00 23.32 ?  105 TYR C C     1 
ATOM   11826 O  O     . TYR C 2 126 ? 110.010 106.685 127.413 1.00 23.17 ?  105 TYR C O     1 
ATOM   11827 C  CB    . TYR C 2 126 ? 110.573 103.570 127.085 1.00 23.45 ?  105 TYR C CB    1 
ATOM   11828 C  CG    . TYR C 2 126 ? 110.822 102.401 126.161 1.00 25.16 ?  105 TYR C CG    1 
ATOM   11829 C  CD1   . TYR C 2 126 ? 110.466 102.456 124.816 1.00 26.75 ?  105 TYR C CD1   1 
ATOM   11830 C  CD2   . TYR C 2 126 ? 111.416 101.235 126.642 1.00 26.36 ?  105 TYR C CD2   1 
ATOM   11831 C  CE1   . TYR C 2 126 ? 110.714 101.373 123.964 1.00 28.22 ?  105 TYR C CE1   1 
ATOM   11832 C  CE2   . TYR C 2 126 ? 111.668 100.158 125.807 1.00 27.17 ?  105 TYR C CE2   1 
ATOM   11833 C  CZ    . TYR C 2 126 ? 111.302 100.226 124.475 1.00 29.26 ?  105 TYR C CZ    1 
ATOM   11834 O  OH    . TYR C 2 126 ? 111.540 99.146  123.649 1.00 30.76 ?  105 TYR C OH    1 
ATOM   11835 N  N     . SER C 2 127 ? 111.732 106.075 128.741 1.00 23.61 ?  106 SER C N     1 
ATOM   11836 C  CA    . SER C 2 127 ? 111.545 107.161 129.695 1.00 24.40 ?  106 SER C CA    1 
ATOM   11837 C  C     . SER C 2 127 ? 111.898 108.508 129.078 1.00 24.55 ?  106 SER C C     1 
ATOM   11838 O  O     . SER C 2 127 ? 111.282 109.506 129.416 1.00 24.74 ?  106 SER C O     1 
ATOM   11839 C  CB    . SER C 2 127 ? 112.341 106.938 130.980 1.00 24.54 ?  106 SER C CB    1 
ATOM   11840 O  OG    . SER C 2 127 ? 111.697 105.982 131.815 1.00 24.69 ?  106 SER C OG    1 
ATOM   11841 N  N     . ASN C 2 128 ? 112.891 108.533 128.189 1.00 25.28 ?  107 ASN C N     1 
ATOM   11842 C  CA    . ASN C 2 128 ? 113.228 109.760 127.460 1.00 25.88 ?  107 ASN C CA    1 
ATOM   11843 C  C     . ASN C 2 128 ? 112.044 110.193 126.606 1.00 25.48 ?  107 ASN C C     1 
ATOM   11844 O  O     . ASN C 2 128 ? 111.681 111.367 126.579 1.00 25.23 ?  107 ASN C O     1 
ATOM   11845 C  CB    . ASN C 2 128 ? 114.471 109.577 126.580 1.00 26.40 ?  107 ASN C CB    1 
ATOM   11846 C  CG    . ASN C 2 128 ? 115.773 109.600 127.372 1.00 27.90 ?  107 ASN C CG    1 
ATOM   11847 O  OD1   . ASN C 2 128 ? 115.823 109.193 128.534 1.00 30.62 ?  107 ASN C OD1   1 
ATOM   11848 N  ND2   . ASN C 2 128 ? 116.840 110.066 126.730 1.00 27.91 ?  107 ASN C ND2   1 
ATOM   11849 N  N     . ILE C 2 129 ? 111.438 109.230 125.918 1.00 25.44 ?  108 ILE C N     1 
ATOM   11850 C  CA    . ILE C 2 129 ? 110.242 109.511 125.125 1.00 25.48 ?  108 ILE C CA    1 
ATOM   11851 C  C     . ILE C 2 129 ? 109.097 109.999 126.028 1.00 25.93 ?  108 ILE C C     1 
ATOM   11852 O  O     . ILE C 2 129 ? 108.515 111.056 125.762 1.00 25.54 ?  108 ILE C O     1 
ATOM   11853 C  CB    . ILE C 2 129 ? 109.833 108.317 124.224 1.00 25.21 ?  108 ILE C CB    1 
ATOM   11854 C  CG1   . ILE C 2 129 ? 110.959 108.014 123.220 1.00 25.96 ?  108 ILE C CG1   1 
ATOM   11855 C  CG2   . ILE C 2 129 ? 108.503 108.612 123.497 1.00 24.43 ?  108 ILE C CG2   1 
ATOM   11856 C  CD1   . ILE C 2 129 ? 110.818 106.697 122.459 1.00 26.11 ?  108 ILE C CD1   1 
ATOM   11857 N  N     . PHE C 2 130 ? 108.793 109.251 127.094 1.00 26.04 ?  109 PHE C N     1 
ATOM   11858 C  CA    . PHE C 2 130 ? 107.728 109.640 128.037 1.00 26.66 ?  109 PHE C CA    1 
ATOM   11859 C  C     . PHE C 2 130 ? 107.935 111.046 128.608 1.00 27.38 ?  109 PHE C C     1 
ATOM   11860 O  O     . PHE C 2 130 ? 106.988 111.846 128.677 1.00 27.22 ?  109 PHE C O     1 
ATOM   11861 C  CB    . PHE C 2 130 ? 107.626 108.647 129.217 1.00 26.98 ?  109 PHE C CB    1 
ATOM   11862 C  CG    . PHE C 2 130 ? 107.069 107.292 128.856 1.00 27.46 ?  109 PHE C CG    1 
ATOM   11863 C  CD1   . PHE C 2 130 ? 106.171 107.134 127.806 1.00 28.57 ?  109 PHE C CD1   1 
ATOM   11864 C  CD2   . PHE C 2 130 ? 107.437 106.167 129.594 1.00 28.51 ?  109 PHE C CD2   1 
ATOM   11865 C  CE1   . PHE C 2 130 ? 105.663 105.876 127.485 1.00 29.17 ?  109 PHE C CE1   1 
ATOM   11866 C  CE2   . PHE C 2 130 ? 106.927 104.899 129.285 1.00 29.27 ?  109 PHE C CE2   1 
ATOM   11867 C  CZ    . PHE C 2 130 ? 106.036 104.751 128.233 1.00 28.83 ?  109 PHE C CZ    1 
ATOM   11868 N  N     . MET C 2 131 ? 109.167 111.350 129.016 1.00 27.52 ?  110 MET C N     1 
ATOM   11869 C  CA    . MET C 2 131 ? 109.460 112.628 129.674 1.00 29.07 ?  110 MET C CA    1 
ATOM   11870 C  C     . MET C 2 131 ? 109.327 113.824 128.746 1.00 29.58 ?  110 MET C C     1 
ATOM   11871 O  O     . MET C 2 131 ? 109.055 114.936 129.199 1.00 30.07 ?  110 MET C O     1 
ATOM   11872 C  CB    . MET C 2 131 ? 110.839 112.623 130.328 1.00 28.96 ?  110 MET C CB    1 
ATOM   11873 C  CG    . MET C 2 131 ? 110.858 111.917 131.667 1.00 31.09 ?  110 MET C CG    1 
ATOM   11874 S  SD    . MET C 2 131 ? 112.493 111.853 132.438 1.00 35.43 ?  110 MET C SD    1 
ATOM   11875 C  CE    . MET C 2 131 ? 113.402 110.797 131.313 1.00 33.13 ?  110 MET C CE    1 
ATOM   11876 N  N     . THR C 2 132 ? 109.513 113.582 127.454 1.00 30.25 ?  111 THR C N     1 
ATOM   11877 C  CA    . THR C 2 132 ? 109.329 114.605 126.428 1.00 30.97 ?  111 THR C CA    1 
ATOM   11878 C  C     . THR C 2 132 ? 107.845 114.863 126.146 1.00 31.36 ?  111 THR C C     1 
ATOM   11879 O  O     . THR C 2 132 ? 107.380 116.010 126.189 1.00 31.60 ?  111 THR C O     1 
ATOM   11880 C  CB    . THR C 2 132 ? 110.068 114.197 125.122 1.00 30.88 ?  111 THR C CB    1 
ATOM   11881 O  OG1   . THR C 2 132 ? 111.471 114.102 125.389 1.00 29.86 ?  111 THR C OG1   1 
ATOM   11882 C  CG2   . THR C 2 132 ? 109.843 115.217 123.995 1.00 31.44 ?  111 THR C CG2   1 
ATOM   11883 N  N     . LEU C 2 133 ? 107.108 113.791 125.872 1.00 31.34 ?  112 LEU C N     1 
ATOM   11884 C  CA    . LEU C 2 133 ? 105.734 113.900 125.377 1.00 31.68 ?  112 LEU C CA    1 
ATOM   11885 C  C     . LEU C 2 133 ? 104.642 114.060 126.439 1.00 31.96 ?  112 LEU C C     1 
ATOM   11886 O  O     . LEU C 2 133 ? 103.620 114.695 126.186 1.00 31.69 ?  112 LEU C O     1 
ATOM   11887 C  CB    . LEU C 2 133 ? 105.404 112.700 124.495 1.00 31.35 ?  112 LEU C CB    1 
ATOM   11888 C  CG    . LEU C 2 133 ? 106.363 112.388 123.341 1.00 32.14 ?  112 LEU C CG    1 
ATOM   11889 C  CD1   . LEU C 2 133 ? 105.903 111.132 122.639 1.00 32.15 ?  112 LEU C CD1   1 
ATOM   11890 C  CD2   . LEU C 2 133 ? 106.460 113.559 122.366 1.00 32.39 ?  112 LEU C CD2   1 
ATOM   11891 N  N     . ALA C 2 134 ? 104.857 113.484 127.617 1.00 32.12 ?  113 ALA C N     1 
ATOM   11892 C  CA    . ALA C 2 134 ? 103.786 113.352 128.595 1.00 32.53 ?  113 ALA C CA    1 
ATOM   11893 C  C     . ALA C 2 134 ? 104.070 114.060 129.914 1.00 33.15 ?  113 ALA C C     1 
ATOM   11894 O  O     . ALA C 2 134 ? 105.220 114.130 130.342 1.00 32.47 ?  113 ALA C O     1 
ATOM   11895 C  CB    . ALA C 2 134 ? 103.476 111.870 128.841 1.00 32.20 ?  113 ALA C CB    1 
ATOM   11896 N  N     . PRO C 2 135 ? 103.010 114.572 130.570 1.00 34.27 ?  114 PRO C N     1 
ATOM   11897 C  CA    . PRO C 2 135 ? 103.155 115.123 131.911 1.00 35.35 ?  114 PRO C CA    1 
ATOM   11898 C  C     . PRO C 2 135 ? 103.351 114.005 132.929 1.00 36.17 ?  114 PRO C C     1 
ATOM   11899 O  O     . PRO C 2 135 ? 102.945 112.866 132.684 1.00 35.92 ?  114 PRO C O     1 
ATOM   11900 C  CB    . PRO C 2 135 ? 101.831 115.862 132.143 1.00 35.48 ?  114 PRO C CB    1 
ATOM   11901 C  CG    . PRO C 2 135 ? 100.856 115.226 131.231 1.00 34.94 ?  114 PRO C CG    1 
ATOM   11902 C  CD    . PRO C 2 135 ? 101.620 114.645 130.078 1.00 34.50 ?  114 PRO C CD    1 
ATOM   11903 N  N     . THR C 2 136 ? 103.981 114.335 134.052 1.00 37.30 ?  115 THR C N     1 
ATOM   11904 C  CA    . THR C 2 136 ? 104.346 113.356 135.082 1.00 38.49 ?  115 THR C CA    1 
ATOM   11905 C  C     . THR C 2 136 ? 103.207 112.430 135.530 1.00 38.48 ?  115 THR C C     1 
ATOM   11906 O  O     . THR C 2 136 ? 103.441 111.239 135.769 1.00 38.74 ?  115 THR C O     1 
ATOM   11907 C  CB    . THR C 2 136 ? 104.953 114.061 136.313 1.00 38.95 ?  115 THR C CB    1 
ATOM   11908 O  OG1   . THR C 2 136 ? 106.010 114.922 135.879 1.00 40.08 ?  115 THR C OG1   1 
ATOM   11909 C  CG2   . THR C 2 136 ? 105.509 113.052 137.318 1.00 39.82 ?  115 THR C CG2   1 
ATOM   11910 N  N     . GLU C 2 137 ? 101.992 112.971 135.638 1.00 38.89 ?  116 GLU C N     1 
ATOM   11911 C  CA    . GLU C 2 137 ? 100.833 112.205 136.117 1.00 38.65 ?  116 GLU C CA    1 
ATOM   11912 C  C     . GLU C 2 137 ? 100.443 111.098 135.143 1.00 37.38 ?  116 GLU C C     1 
ATOM   11913 O  O     . GLU C 2 137 ? 100.069 110.003 135.559 1.00 37.22 ?  116 GLU C O     1 
ATOM   11914 C  CB    . GLU C 2 137 ? 99.623  113.109 136.438 1.00 39.52 ?  116 GLU C CB    1 
ATOM   11915 C  CG    . GLU C 2 137 ? 98.910  113.760 135.230 1.00 41.90 ?  116 GLU C CG    1 
ATOM   11916 C  CD    . GLU C 2 137 ? 98.909  115.298 135.257 1.00 46.43 ?  116 GLU C CD    1 
ATOM   11917 O  OE1   . GLU C 2 137 ? 99.642  115.905 136.074 1.00 47.84 ?  116 GLU C OE1   1 
ATOM   11918 O  OE2   . GLU C 2 137 ? 98.162  115.904 134.449 1.00 47.52 -1 116 GLU C OE2   1 
ATOM   11919 N  N     . THR C 2 138 ? 100.547 111.394 133.851 1.00 36.05 ?  117 THR C N     1 
ATOM   11920 C  CA    . THR C 2 138 ? 100.265 110.421 132.807 1.00 34.88 ?  117 THR C CA    1 
ATOM   11921 C  C     . THR C 2 138 ? 101.345 109.344 132.799 1.00 33.58 ?  117 THR C C     1 
ATOM   11922 O  O     . THR C 2 138 ? 101.045 108.165 132.589 1.00 33.61 ?  117 THR C O     1 
ATOM   11923 C  CB    . THR C 2 138 ? 100.164 111.093 131.431 1.00 34.85 ?  117 THR C CB    1 
ATOM   11924 O  OG1   . THR C 2 138 ? 99.243  112.186 131.513 1.00 35.98 ?  117 THR C OG1   1 
ATOM   11925 C  CG2   . THR C 2 138 ? 99.677  110.108 130.378 1.00 34.92 ?  117 THR C CG2   1 
ATOM   11926 N  N     . ILE C 2 139 ? 102.590 109.754 133.033 1.00 32.29 ?  118 ILE C N     1 
ATOM   11927 C  CA    . ILE C 2 139 ? 103.702 108.813 133.164 1.00 31.19 ?  118 ILE C CA    1 
ATOM   11928 C  C     . ILE C 2 139 ? 103.493 107.893 134.381 1.00 30.85 ?  118 ILE C C     1 
ATOM   11929 O  O     . ILE C 2 139 ? 103.597 106.673 134.256 1.00 29.77 ?  118 ILE C O     1 
ATOM   11930 C  CB    . ILE C 2 139 ? 105.088 109.522 133.221 1.00 31.25 ?  118 ILE C CB    1 
ATOM   11931 C  CG1   . ILE C 2 139 ? 105.327 110.379 131.965 1.00 30.12 ?  118 ILE C CG1   1 
ATOM   11932 C  CG2   . ILE C 2 139 ? 106.224 108.499 133.384 1.00 30.21 ?  118 ILE C CG2   1 
ATOM   11933 C  CD1   . ILE C 2 139 ? 106.612 111.225 132.022 1.00 29.41 ?  118 ILE C CD1   1 
ATOM   11934 N  N     . ASN C 2 140 ? 103.181 108.481 135.541 1.00 31.17 ?  119 ASN C N     1 
ATOM   11935 C  CA    . ASN C 2 140 ? 102.895 107.708 136.761 1.00 31.76 ?  119 ASN C CA    1 
ATOM   11936 C  C     . ASN C 2 140 ? 101.763 106.696 136.549 1.00 31.25 ?  119 ASN C C     1 
ATOM   11937 O  O     . ASN C 2 140 ? 101.883 105.535 136.943 1.00 31.47 ?  119 ASN C O     1 
ATOM   11938 C  CB    . ASN C 2 140 ? 102.537 108.621 137.943 1.00 32.65 ?  119 ASN C CB    1 
ATOM   11939 C  CG    . ASN C 2 140 ? 103.730 109.401 138.487 1.00 35.14 ?  119 ASN C CG    1 
ATOM   11940 O  OD1   . ASN C 2 140 ? 104.886 108.981 138.377 1.00 36.75 ?  119 ASN C OD1   1 
ATOM   11941 N  ND2   . ASN C 2 140 ? 103.438 110.547 139.110 1.00 38.05 ?  119 ASN C ND2   1 
ATOM   11942 N  N     . GLU C 2 141 ? 100.682 107.151 135.918 1.00 30.96 ?  120 GLU C N     1 
ATOM   11943 C  CA    . GLU C 2 141 ? 99.515  106.319 135.631 1.00 30.36 ?  120 GLU C CA    1 
ATOM   11944 C  C     . GLU C 2 141 ? 99.845  105.131 134.724 1.00 28.60 ?  120 GLU C C     1 
ATOM   11945 O  O     . GLU C 2 141 ? 99.376  104.022 134.969 1.00 27.94 ?  120 GLU C O     1 
ATOM   11946 C  CB    . GLU C 2 141 ? 98.395  107.153 135.001 1.00 30.86 ?  120 GLU C CB    1 
ATOM   11947 C  CG    . GLU C 2 141 ? 97.620  108.023 135.985 1.00 34.89 ?  120 GLU C CG    1 
ATOM   11948 C  CD    . GLU C 2 141 ? 96.658  108.977 135.290 1.00 39.82 ?  120 GLU C CD    1 
ATOM   11949 O  OE1   . GLU C 2 141 ? 96.382  108.790 134.079 1.00 41.95 ?  120 GLU C OE1   1 
ATOM   11950 O  OE2   . GLU C 2 141 ? 96.170  109.915 135.955 1.00 41.94 -1 120 GLU C OE2   1 
ATOM   11951 N  N     . VAL C 2 142 ? 100.643 105.352 133.682 1.00 27.29 ?  121 VAL C N     1 
ATOM   11952 C  CA    . VAL C 2 142 ? 100.966 104.236 132.767 1.00 25.89 ?  121 VAL C CA    1 
ATOM   11953 C  C     . VAL C 2 142 ? 101.851 103.171 133.427 1.00 25.11 ?  121 VAL C C     1 
ATOM   11954 O  O     . VAL C 2 142 ? 101.713 101.982 133.142 1.00 24.23 ?  121 VAL C O     1 
ATOM   11955 C  CB    . VAL C 2 142 ? 101.510 104.703 131.372 1.00 25.99 ?  121 VAL C CB    1 
ATOM   11956 C  CG1   . VAL C 2 142 ? 103.021 104.951 131.385 1.00 25.21 ?  121 VAL C CG1   1 
ATOM   11957 C  CG2   . VAL C 2 142 ? 101.169 103.676 130.304 1.00 25.78 ?  121 VAL C CG2   1 
ATOM   11958 N  N     . PHE C 2 143 ? 102.745 103.585 134.319 1.00 24.69 ?  122 PHE C N     1 
ATOM   11959 C  CA    . PHE C 2 143 ? 103.557 102.605 135.057 1.00 24.77 ?  122 PHE C CA    1 
ATOM   11960 C  C     . PHE C 2 143 ? 102.717 101.837 136.093 1.00 24.99 ?  122 PHE C C     1 
ATOM   11961 O  O     . PHE C 2 143 ? 102.947 100.652 136.338 1.00 24.73 ?  122 PHE C O     1 
ATOM   11962 C  CB    . PHE C 2 143 ? 104.811 103.247 135.662 1.00 24.83 ?  122 PHE C CB    1 
ATOM   11963 C  CG    . PHE C 2 143 ? 105.913 103.468 134.649 1.00 25.12 ?  122 PHE C CG    1 
ATOM   11964 C  CD1   . PHE C 2 143 ? 106.651 102.395 134.155 1.00 26.58 ?  122 PHE C CD1   1 
ATOM   11965 C  CD2   . PHE C 2 143 ? 106.197 104.740 134.176 1.00 24.49 ?  122 PHE C CD2   1 
ATOM   11966 C  CE1   . PHE C 2 143 ? 107.661 102.595 133.205 1.00 26.96 ?  122 PHE C CE1   1 
ATOM   11967 C  CE2   . PHE C 2 143 ? 107.197 104.951 133.237 1.00 25.79 ?  122 PHE C CE2   1 
ATOM   11968 C  CZ    . PHE C 2 143 ? 107.933 103.877 132.745 1.00 26.45 ?  122 PHE C CZ    1 
ATOM   11969 N  N     . GLU C 2 144 ? 101.729 102.510 136.678 1.00 25.22 ?  123 GLU C N     1 
ATOM   11970 C  CA    . GLU C 2 144 ? 100.747 101.824 137.524 1.00 25.72 ?  123 GLU C CA    1 
ATOM   11971 C  C     . GLU C 2 144 ? 99.923  100.835 136.701 1.00 25.08 ?  123 GLU C C     1 
ATOM   11972 O  O     . GLU C 2 144 ? 99.644  99.723  137.150 1.00 24.67 ?  123 GLU C O     1 
ATOM   11973 C  CB    . GLU C 2 144 ? 99.850  102.824 138.246 1.00 26.23 ?  123 GLU C CB    1 
ATOM   11974 C  CG    . GLU C 2 144 ? 100.578 103.571 139.352 1.00 29.96 ?  123 GLU C CG    1 
ATOM   11975 C  CD    . GLU C 2 144 ? 101.258 102.628 140.330 1.00 33.82 ?  123 GLU C CD    1 
ATOM   11976 O  OE1   . GLU C 2 144 ? 100.539 101.886 141.032 1.00 36.54 ?  123 GLU C OE1   1 
ATOM   11977 O  OE2   . GLU C 2 144 ? 102.507 102.613 140.385 1.00 35.84 -1 123 GLU C OE2   1 
ATOM   11978 N  N     . TRP C 2 145 ? 99.566  101.241 135.485 1.00 24.21 ?  124 TRP C N     1 
ATOM   11979 C  CA    . TRP C 2 145 ? 98.825  100.383 134.561 1.00 23.99 ?  124 TRP C CA    1 
ATOM   11980 C  C     . TRP C 2 145 ? 99.576  99.100  134.176 1.00 23.95 ?  124 TRP C C     1 
ATOM   11981 O  O     . TRP C 2 145 ? 98.949  98.031  134.056 1.00 23.31 ?  124 TRP C O     1 
ATOM   11982 C  CB    . TRP C 2 145 ? 98.407  101.166 133.307 1.00 24.13 ?  124 TRP C CB    1 
ATOM   11983 C  CG    . TRP C 2 145 ? 97.901  100.287 132.186 1.00 24.37 ?  124 TRP C CG    1 
ATOM   11984 C  CD1   . TRP C 2 145 ? 96.609  99.868  131.977 1.00 24.76 ?  124 TRP C CD1   1 
ATOM   11985 C  CD2   . TRP C 2 145 ? 98.684  99.727  131.124 1.00 23.31 ?  124 TRP C CD2   1 
ATOM   11986 N  NE1   . TRP C 2 145 ? 96.550  99.072  130.847 1.00 24.97 ?  124 TRP C NE1   1 
ATOM   11987 C  CE2   . TRP C 2 145 ? 97.805  98.973  130.306 1.00 24.20 ?  124 TRP C CE2   1 
ATOM   11988 C  CE3   . TRP C 2 145 ? 100.043 99.778  130.788 1.00 23.76 ?  124 TRP C CE3   1 
ATOM   11989 C  CZ2   . TRP C 2 145 ? 98.247  98.280  129.170 1.00 23.41 ?  124 TRP C CZ2   1 
ATOM   11990 C  CZ3   . TRP C 2 145 ? 100.484 99.086  129.661 1.00 23.29 ?  124 TRP C CZ3   1 
ATOM   11991 C  CH2   . TRP C 2 145 ? 99.582  98.353  128.862 1.00 22.93 ?  124 TRP C CH2   1 
ATOM   11992 N  N     . VAL C 2 146 ? 100.896 99.176  133.972 1.00 23.35 ?  125 VAL C N     1 
ATOM   11993 C  CA    . VAL C 2 146 ? 101.637 97.918  133.697 1.00 23.53 ?  125 VAL C CA    1 
ATOM   11994 C  C     . VAL C 2 146 ? 101.539 96.918  134.857 1.00 23.73 ?  125 VAL C C     1 
ATOM   11995 O  O     . VAL C 2 146 ? 101.353 95.734  134.619 1.00 23.03 ?  125 VAL C O     1 
ATOM   11996 C  CB    . VAL C 2 146 ? 103.111 98.071  133.092 1.00 23.63 ?  125 VAL C CB    1 
ATOM   11997 C  CG1   . VAL C 2 146 ? 103.498 99.490  132.776 1.00 24.40 ?  125 VAL C CG1   1 
ATOM   11998 C  CG2   . VAL C 2 146 ? 104.197 97.326  133.891 1.00 22.97 ?  125 VAL C CG2   1 
ATOM   11999 N  N     . LYS C 2 147 ? 101.605 97.413  136.096 1.00 24.06 ?  126 LYS C N     1 
ATOM   12000 C  CA    . LYS C 2 147 ? 101.551 96.541  137.282 1.00 25.41 ?  126 LYS C CA    1 
ATOM   12001 C  C     . LYS C 2 147 ? 100.246 95.749  137.399 1.00 25.82 ?  126 LYS C C     1 
ATOM   12002 O  O     . LYS C 2 147 ? 100.251 94.624  137.904 1.00 26.08 ?  126 LYS C O     1 
ATOM   12003 C  CB    . LYS C 2 147 ? 101.752 97.350  138.566 1.00 25.49 ?  126 LYS C CB    1 
ATOM   12004 C  CG    . LYS C 2 147 ? 103.138 97.934  138.751 1.00 27.52 ?  126 LYS C CG    1 
ATOM   12005 C  CD    . LYS C 2 147 ? 103.160 98.779  140.018 1.00 30.43 ?  126 LYS C CD    1 
ATOM   12006 C  CE    . LYS C 2 147 ? 104.389 99.662  140.082 1.00 33.10 ?  126 LYS C CE    1 
ATOM   12007 N  NZ    . LYS C 2 147 ? 104.315 100.558 141.269 1.00 34.86 1  126 LYS C NZ    1 
ATOM   12008 N  N     . GLN C 2 148 ? 99.143  96.337  136.938 1.00 26.45 ?  127 GLN C N     1 
ATOM   12009 C  CA    . GLN C 2 148 ? 97.815  95.739  137.108 1.00 26.85 ?  127 GLN C CA    1 
ATOM   12010 C  C     . GLN C 2 148 ? 97.239  95.099  135.844 1.00 26.01 ?  127 GLN C C     1 
ATOM   12011 O  O     . GLN C 2 148 ? 96.178  94.473  135.903 1.00 26.12 ?  127 GLN C O     1 
ATOM   12012 C  CB    . GLN C 2 148 ? 96.821  96.759  137.696 1.00 28.08 ?  127 GLN C CB    1 
ATOM   12013 C  CG    . GLN C 2 148 ? 96.549  97.988  136.825 1.00 30.69 ?  127 GLN C CG    1 
ATOM   12014 C  CD    . GLN C 2 148 ? 95.641  97.695  135.633 1.00 34.64 ?  127 GLN C CD    1 
ATOM   12015 O  OE1   . GLN C 2 148 ? 96.067  97.787  134.468 1.00 33.80 ?  127 GLN C OE1   1 
ATOM   12016 N  NE2   . GLN C 2 148 ? 94.384  97.328  135.916 1.00 36.24 ?  127 GLN C NE2   1 
ATOM   12017 N  N     . ASN C 2 149 ? 97.923  95.258  134.708 1.00 24.97 ?  128 ASN C N     1 
ATOM   12018 C  CA    . ASN C 2 149 ? 97.460  94.680  133.450 1.00 24.03 ?  128 ASN C CA    1 
ATOM   12019 C  C     . ASN C 2 149 ? 97.718  93.181  133.420 1.00 24.13 ?  128 ASN C C     1 
ATOM   12020 O  O     . ASN C 2 149 ? 98.875  92.761  133.507 1.00 22.93 ?  128 ASN C O     1 
ATOM   12021 C  CB    . ASN C 2 149 ? 98.174  95.325  132.272 1.00 23.97 ?  128 ASN C CB    1 
ATOM   12022 C  CG    . ASN C 2 149 ? 97.628  94.856  130.945 1.00 23.94 ?  128 ASN C CG    1 
ATOM   12023 O  OD1   . ASN C 2 149 ? 98.089  93.861  130.388 1.00 24.85 ?  128 ASN C OD1   1 
ATOM   12024 N  ND2   . ASN C 2 149 ? 96.604  95.541  130.453 1.00 24.76 ?  128 ASN C ND2   1 
ATOM   12025 N  N     . LYS C 2 150 ? 96.657  92.385  133.267 1.00 24.32 ?  129 LYS C N     1 
ATOM   12026 C  CA    . LYS C 2 150 ? 96.769  90.922  133.428 1.00 24.77 ?  129 LYS C CA    1 
ATOM   12027 C  C     . LYS C 2 150 ? 97.564  90.199  132.338 1.00 24.54 ?  129 LYS C C     1 
ATOM   12028 O  O     . LYS C 2 150 ? 98.215  89.192  132.615 1.00 24.17 ?  129 LYS C O     1 
ATOM   12029 C  CB    . LYS C 2 150 ? 95.399  90.267  133.644 1.00 25.27 ?  129 LYS C CB    1 
ATOM   12030 C  CG    . LYS C 2 150 ? 94.413  90.410  132.502 1.00 28.72 ?  129 LYS C CG    1 
ATOM   12031 C  CD    . LYS C 2 150 ? 93.250  89.436  132.699 1.00 33.40 ?  129 LYS C CD    1 
ATOM   12032 C  CE    . LYS C 2 150 ? 92.023  89.878  131.926 1.00 36.77 ?  129 LYS C CE    1 
ATOM   12033 N  NZ    . LYS C 2 150 ? 90.843  89.038  132.303 1.00 39.66 1  129 LYS C NZ    1 
ATOM   12034 N  N     . TYR C 2 151 ? 97.504  90.712  131.104 1.00 23.92 ?  130 TYR C N     1 
ATOM   12035 C  CA    . TYR C 2 151 ? 98.243  90.115  129.983 1.00 24.12 ?  130 TYR C CA    1 
ATOM   12036 C  C     . TYR C 2 151 ? 99.739  90.374  130.075 1.00 23.54 ?  130 TYR C C     1 
ATOM   12037 O  O     . TYR C 2 151 ? 100.557 89.494  129.770 1.00 23.32 ?  130 TYR C O     1 
ATOM   12038 C  CB    . TYR C 2 151 ? 97.676  90.611  128.640 1.00 24.53 ?  130 TYR C CB    1 
ATOM   12039 C  CG    . TYR C 2 151 ? 96.163  90.600  128.617 1.00 25.83 ?  130 TYR C CG    1 
ATOM   12040 C  CD1   . TYR C 2 151 ? 95.458  89.400  128.716 1.00 26.57 ?  130 TYR C CD1   1 
ATOM   12041 C  CD2   . TYR C 2 151 ? 95.436  91.794  128.544 1.00 27.87 ?  130 TYR C CD2   1 
ATOM   12042 C  CE1   . TYR C 2 151 ? 94.067  89.378  128.718 1.00 29.65 ?  130 TYR C CE1   1 
ATOM   12043 C  CE2   . TYR C 2 151 ? 94.036  91.783  128.549 1.00 29.91 ?  130 TYR C CE2   1 
ATOM   12044 C  CZ    . TYR C 2 151 ? 93.364  90.572  128.639 1.00 31.19 ?  130 TYR C CZ    1 
ATOM   12045 O  OH    . TYR C 2 151 ? 91.984  90.542  128.644 1.00 34.44 ?  130 TYR C OH    1 
ATOM   12046 N  N     . LEU C 2 152 ? 100.090 91.584  130.497 1.00 23.38 ?  131 LEU C N     1 
ATOM   12047 C  CA    . LEU C 2 152 ? 101.480 91.965  130.674 1.00 23.43 ?  131 LEU C CA    1 
ATOM   12048 C  C     . LEU C 2 152 ? 102.080 91.212  131.866 1.00 23.37 ?  131 LEU C C     1 
ATOM   12049 O  O     . LEU C 2 152 ? 103.211 90.723  131.786 1.00 23.05 ?  131 LEU C O     1 
ATOM   12050 C  CB    . LEU C 2 152 ? 101.562 93.478  130.871 1.00 23.73 ?  131 LEU C CB    1 
ATOM   12051 C  CG    . LEU C 2 152 ? 102.567 94.393  130.181 1.00 24.71 ?  131 LEU C CG    1 
ATOM   12052 C  CD1   . LEU C 2 152 ? 103.228 93.813  128.920 1.00 21.63 ?  131 LEU C CD1   1 
ATOM   12053 C  CD2   . LEU C 2 152 ? 101.886 95.705  129.868 1.00 26.87 ?  131 LEU C CD2   1 
ATOM   12054 N  N     . GLN C 2 153 ? 101.331 91.115  132.969 1.00 22.80 ?  132 GLN C N     1 
ATOM   12055 C  CA    . GLN C 2 153 ? 101.779 90.282  134.097 1.00 22.70 ?  132 GLN C CA    1 
ATOM   12056 C  C     . GLN C 2 153 ? 101.924 88.801  133.734 1.00 22.54 ?  132 GLN C C     1 
ATOM   12057 O  O     . GLN C 2 153 ? 102.923 88.168  134.108 1.00 21.73 ?  132 GLN C O     1 
ATOM   12058 C  CB    . GLN C 2 153 ? 100.905 90.474  135.339 1.00 23.07 ?  132 GLN C CB    1 
ATOM   12059 C  CG    . GLN C 2 153 ? 100.979 91.893  135.903 1.00 21.83 ?  132 GLN C CG    1 
ATOM   12060 C  CD    . GLN C 2 153 ? 102.398 92.324  136.282 1.00 22.34 ?  132 GLN C CD    1 
ATOM   12061 O  OE1   . GLN C 2 153 ? 103.128 91.592  136.955 1.00 24.07 ?  132 GLN C OE1   1 
ATOM   12062 N  NE2   . GLN C 2 153 ? 102.783 93.522  135.862 1.00 22.26 ?  132 GLN C NE2   1 
ATOM   12063 N  N     . LYS C 2 154 ? 100.948 88.254  133.004 1.00 22.53 ?  133 LYS C N     1 
ATOM   12064 C  CA    . LYS C 2 154 ? 101.045 86.861  132.567 1.00 22.84 ?  133 LYS C CA    1 
ATOM   12065 C  C     . LYS C 2 154 ? 102.287 86.611  131.709 1.00 22.42 ?  133 LYS C C     1 
ATOM   12066 O  O     . LYS C 2 154 ? 102.989 85.632  131.934 1.00 21.90 ?  133 LYS C O     1 
ATOM   12067 C  CB    . LYS C 2 154 ? 99.765  86.363  131.858 1.00 22.96 ?  133 LYS C CB    1 
ATOM   12068 C  CG    . LYS C 2 154 ? 99.817  84.868  131.418 1.00 23.45 ?  133 LYS C CG    1 
ATOM   12069 C  CD    . LYS C 2 154 ? 99.908  83.881  132.603 1.00 26.74 ?  133 LYS C CD    1 
ATOM   12070 C  CE    . LYS C 2 154 ? 99.913  82.423  132.124 1.00 27.93 ?  133 LYS C CE    1 
ATOM   12071 N  NZ    . LYS C 2 154 ? 100.204 81.445  133.206 1.00 27.86 1  133 LYS C NZ    1 
ATOM   12072 N  N     . LYS C 2 155 ? 102.576 87.493  130.747 1.00 22.77 ?  134 LYS C N     1 
ATOM   12073 C  CA    . LYS C 2 155 ? 103.707 87.237  129.850 1.00 22.87 ?  134 LYS C CA    1 
ATOM   12074 C  C     . LYS C 2 155 ? 105.042 87.346  130.579 1.00 22.30 ?  134 LYS C C     1 
ATOM   12075 O  O     . LYS C 2 155 ? 105.933 86.507  130.364 1.00 21.89 ?  134 LYS C O     1 
ATOM   12076 C  CB    . LYS C 2 155 ? 103.650 88.061  128.543 1.00 23.33 ?  134 LYS C CB    1 
ATOM   12077 C  CG    . LYS C 2 155 ? 104.026 89.519  128.626 1.00 24.25 ?  134 LYS C CG    1 
ATOM   12078 C  CD    . LYS C 2 155 ? 103.934 90.196  127.247 1.00 26.87 ?  134 LYS C CD    1 
ATOM   12079 C  CE    . LYS C 2 155 ? 102.514 90.668  126.954 1.00 28.26 ?  134 LYS C CE    1 
ATOM   12080 N  NZ    . LYS C 2 155 ? 102.505 91.590  125.778 1.00 28.97 1  134 LYS C NZ    1 
ATOM   12081 N  N     . ALA C 2 156 ? 105.156 88.336  131.465 1.00 21.96 ?  135 ALA C N     1 
ATOM   12082 C  CA    . ALA C 2 156 ? 106.313 88.445  132.374 1.00 22.43 ?  135 ALA C CA    1 
ATOM   12083 C  C     . ALA C 2 156 ? 106.464 87.229  133.290 1.00 22.02 ?  135 ALA C C     1 
ATOM   12084 O  O     . ALA C 2 156 ? 107.571 86.733  133.476 1.00 22.60 ?  135 ALA C O     1 
ATOM   12085 C  CB    . ALA C 2 156 ? 106.240 89.732  133.224 1.00 22.05 ?  135 ALA C CB    1 
ATOM   12086 N  N     . GLN C 2 157 ? 105.359 86.767  133.876 1.00 21.97 ?  136 GLN C N     1 
ATOM   12087 C  CA    . GLN C 2 157 ? 105.388 85.582  134.744 1.00 22.10 ?  136 GLN C CA    1 
ATOM   12088 C  C     . GLN C 2 157 ? 105.953 84.382  134.012 1.00 21.87 ?  136 GLN C C     1 
ATOM   12089 O  O     . GLN C 2 157 ? 106.774 83.650  134.562 1.00 21.75 ?  136 GLN C O     1 
ATOM   12090 C  CB    . GLN C 2 157 ? 103.989 85.210  135.236 1.00 22.50 ?  136 GLN C CB    1 
ATOM   12091 C  CG    . GLN C 2 157 ? 103.476 86.036  136.405 1.00 23.55 ?  136 GLN C CG    1 
ATOM   12092 C  CD    . GLN C 2 157 ? 101.968 85.913  136.531 1.00 26.93 ?  136 GLN C CD    1 
ATOM   12093 O  OE1   . GLN C 2 157 ? 101.384 84.932  136.074 1.00 26.36 ?  136 GLN C OE1   1 
ATOM   12094 N  NE2   . GLN C 2 157 ? 101.329 86.915  137.124 1.00 28.09 ?  136 GLN C NE2   1 
ATOM   12095 N  N     . MET C 2 158 ? 105.490 84.184  132.778 1.00 21.38 ?  137 MET C N     1 
ATOM   12096 C  CA    . MET C 2 158 ? 105.869 83.026  131.984 1.00 22.08 ?  137 MET C CA    1 
ATOM   12097 C  C     . MET C 2 158 ? 107.327 83.078  131.543 1.00 21.70 ?  137 MET C C     1 
ATOM   12098 O  O     . MET C 2 158 ? 108.044 82.076  131.598 1.00 21.83 ?  137 MET C O     1 
ATOM   12099 C  CB    . MET C 2 158 ? 104.986 82.922  130.744 1.00 22.05 ?  137 MET C CB    1 
ATOM   12100 C  CG    . MET C 2 158 ? 103.563 82.420  131.018 1.00 23.93 ?  137 MET C CG    1 
ATOM   12101 S  SD    . MET C 2 158 ? 102.563 82.556  129.522 1.00 27.75 ?  137 MET C SD    1 
ATOM   12102 C  CE    . MET C 2 158 ? 103.339 81.278  128.521 1.00 26.00 ?  137 MET C CE    1 
ATOM   12103 N  N     . ILE C 2 159 ? 107.750 84.240  131.068 1.00 20.90 ?  138 ILE C N     1 
ATOM   12104 C  CA    . ILE C 2 159 ? 109.098 84.375  130.540 1.00 20.60 ?  138 ILE C CA    1 
ATOM   12105 C  C     . ILE C 2 159 ? 110.121 84.326  131.679 1.00 20.36 ?  138 ILE C C     1 
ATOM   12106 O  O     . ILE C 2 159 ? 111.082 83.557  131.613 1.00 19.65 ?  138 ILE C O     1 
ATOM   12107 C  CB    . ILE C 2 159 ? 109.250 85.654  129.666 1.00 20.17 ?  138 ILE C CB    1 
ATOM   12108 C  CG1   . ILE C 2 159 ? 108.398 85.544  128.388 1.00 20.66 ?  138 ILE C CG1   1 
ATOM   12109 C  CG2   . ILE C 2 159 ? 110.731 85.965  129.392 1.00 20.62 ?  138 ILE C CG2   1 
ATOM   12110 C  CD1   . ILE C 2 159 ? 108.782 84.447  127.390 1.00 22.17 ?  138 ILE C CD1   1 
ATOM   12111 N  N     . VAL C 2 160 ? 109.896 85.123  132.724 1.00 19.58 ?  139 VAL C N     1 
ATOM   12112 C  CA    . VAL C 2 160 ? 110.822 85.201  133.858 1.00 19.88 ?  139 VAL C CA    1 
ATOM   12113 C  C     . VAL C 2 160 ? 110.847 83.876  134.627 1.00 19.44 ?  139 VAL C C     1 
ATOM   12114 O  O     . VAL C 2 160 ? 111.870 83.495  135.185 1.00 19.88 ?  139 VAL C O     1 
ATOM   12115 C  CB    . VAL C 2 160 ? 110.489 86.387  134.833 1.00 19.52 ?  139 VAL C CB    1 
ATOM   12116 C  CG1   . VAL C 2 160 ? 111.424 86.378  136.056 1.00 20.75 ?  139 VAL C CG1   1 
ATOM   12117 C  CG2   . VAL C 2 160 ? 110.619 87.727  134.118 1.00 20.03 ?  139 VAL C CG2   1 
ATOM   12118 N  N     . GLY C 2 161 ? 109.718 83.173  134.649 1.00 19.13 ?  140 GLY C N     1 
ATOM   12119 C  CA    . GLY C 2 161 ? 109.665 81.883  135.318 1.00 18.05 ?  140 GLY C CA    1 
ATOM   12120 C  C     . GLY C 2 161 ? 110.638 80.920  134.688 1.00 17.86 ?  140 GLY C C     1 
ATOM   12121 O  O     . GLY C 2 161 ? 111.372 80.209  135.382 1.00 17.47 ?  140 GLY C O     1 
ATOM   12122 N  N     . LEU C 2 162 ? 110.637 80.886  133.359 1.00 17.92 ?  141 LEU C N     1 
ATOM   12123 C  CA    . LEU C 2 162 ? 111.571 80.041  132.624 1.00 18.32 ?  141 LEU C CA    1 
ATOM   12124 C  C     . LEU C 2 162 ? 113.046 80.448  132.841 1.00 18.55 ?  141 LEU C C     1 
ATOM   12125 O  O     . LEU C 2 162 ? 113.902 79.582  133.016 1.00 18.49 ?  141 LEU C O     1 
ATOM   12126 C  CB    . LEU C 2 162 ? 111.206 80.030  131.134 1.00 18.50 ?  141 LEU C CB    1 
ATOM   12127 C  CG    . LEU C 2 162 ? 109.913 79.273  130.818 1.00 19.32 ?  141 LEU C CG    1 
ATOM   12128 C  CD1   . LEU C 2 162 ? 109.414 79.626  129.421 1.00 20.38 ?  141 LEU C CD1   1 
ATOM   12129 C  CD2   . LEU C 2 162 ? 110.106 77.762  130.973 1.00 19.94 ?  141 LEU C CD2   1 
ATOM   12130 N  N     . TYR C 2 163 ? 113.335 81.746  132.867 1.00 19.16 ?  142 TYR C N     1 
ATOM   12131 C  CA    . TYR C 2 163 ? 114.693 82.219  133.202 1.00 20.16 ?  142 TYR C CA    1 
ATOM   12132 C  C     . TYR C 2 163 ? 115.149 81.729  134.565 1.00 20.78 ?  142 TYR C C     1 
ATOM   12133 O  O     . TYR C 2 163 ? 116.293 81.300  134.739 1.00 20.36 ?  142 TYR C O     1 
ATOM   12134 C  CB    . TYR C 2 163 ? 114.783 83.755  133.194 1.00 20.34 ?  142 TYR C CB    1 
ATOM   12135 C  CG    . TYR C 2 163 ? 114.570 84.408  131.836 1.00 22.46 ?  142 TYR C CG    1 
ATOM   12136 C  CD1   . TYR C 2 163 ? 114.797 83.712  130.653 1.00 23.88 ?  142 TYR C CD1   1 
ATOM   12137 C  CD2   . TYR C 2 163 ? 114.150 85.730  131.744 1.00 22.41 ?  142 TYR C CD2   1 
ATOM   12138 C  CE1   . TYR C 2 163 ? 114.596 84.324  129.402 1.00 25.93 ?  142 TYR C CE1   1 
ATOM   12139 C  CE2   . TYR C 2 163 ? 113.953 86.344  130.510 1.00 22.07 ?  142 TYR C CE2   1 
ATOM   12140 C  CZ    . TYR C 2 163 ? 114.184 85.644  129.350 1.00 25.19 ?  142 TYR C CZ    1 
ATOM   12141 O  OH    . TYR C 2 163 ? 113.978 86.277  128.141 1.00 27.43 ?  142 TYR C OH    1 
ATOM   12142 N  N     . LYS C 2 164 ? 114.247 81.792  135.537 1.00 21.39 ?  143 LYS C N     1 
ATOM   12143 C  CA    . LYS C 2 164 ? 114.624 81.455  136.900 1.00 22.49 ?  143 LYS C CA    1 
ATOM   12144 C  C     . LYS C 2 164 ? 114.614 79.951  137.161 1.00 22.49 ?  143 LYS C C     1 
ATOM   12145 O  O     . LYS C 2 164 ? 115.126 79.499  138.180 1.00 22.45 ?  143 LYS C O     1 
ATOM   12146 C  CB    . LYS C 2 164 ? 113.797 82.247  137.910 1.00 23.16 ?  143 LYS C CB    1 
ATOM   12147 C  CG    . LYS C 2 164 ? 114.135 83.736  137.861 1.00 26.08 ?  143 LYS C CG    1 
ATOM   12148 C  CD    . LYS C 2 164 ? 113.777 84.446  139.133 1.00 30.38 ?  143 LYS C CD    1 
ATOM   12149 C  CE    . LYS C 2 164 ? 114.298 85.863  139.122 1.00 32.69 ?  143 LYS C CE    1 
ATOM   12150 N  NZ    . LYS C 2 164 ? 113.893 86.571  140.368 1.00 35.60 1  143 LYS C NZ    1 
ATOM   12151 N  N     . ALA C 2 165 ? 114.102 79.180  136.201 1.00 22.02 ?  144 ALA C N     1 
ATOM   12152 C  CA    . ALA C 2 165 ? 114.120 77.733  136.305 1.00 22.69 ?  144 ALA C CA    1 
ATOM   12153 C  C     . ALA C 2 165 ? 115.424 77.106  135.781 1.00 23.20 ?  144 ALA C C     1 
ATOM   12154 O  O     . ALA C 2 165 ? 115.635 75.910  135.938 1.00 23.80 ?  144 ALA C O     1 
ATOM   12155 C  CB    . ALA C 2 165 ? 112.885 77.121  135.601 1.00 21.79 ?  144 ALA C CB    1 
ATOM   12156 N  N     . ILE C 2 166 ? 116.300 77.901  135.162 1.00 23.97 ?  145 ILE C N     1 
ATOM   12157 C  CA    . ILE C 2 166 ? 117.571 77.366  134.661 1.00 24.29 ?  145 ILE C CA    1 
ATOM   12158 C  C     . ILE C 2 166 ? 118.370 76.731  135.802 1.00 25.49 ?  145 ILE C C     1 
ATOM   12159 O  O     . ILE C 2 166 ? 118.510 77.318  136.871 1.00 25.82 ?  145 ILE C O     1 
ATOM   12160 C  CB    . ILE C 2 166 ? 118.445 78.440  133.949 1.00 24.22 ?  145 ILE C CB    1 
ATOM   12161 C  CG1   . ILE C 2 166 ? 117.717 79.030  132.745 1.00 23.45 ?  145 ILE C CG1   1 
ATOM   12162 C  CG2   . ILE C 2 166 ? 119.777 77.837  133.500 1.00 23.42 ?  145 ILE C CG2   1 
ATOM   12163 C  CD1   . ILE C 2 166 ? 118.383 80.314  132.186 1.00 21.99 ?  145 ILE C CD1   1 
ATOM   12164 N  N     . GLN C 2 167 ? 118.839 75.511  135.579 1.00 26.83 ?  146 GLN C N     1 
ATOM   12165 C  CA    . GLN C 2 167 ? 119.653 74.810  136.562 1.00 28.85 ?  146 GLN C CA    1 
ATOM   12166 C  C     . GLN C 2 167 ? 121.067 74.717  136.022 1.00 29.77 ?  146 GLN C C     1 
ATOM   12167 O  O     . GLN C 2 167 ? 121.268 74.434  134.836 1.00 29.74 ?  146 GLN C O     1 
ATOM   12168 C  CB    . GLN C 2 167 ? 119.100 73.406  136.848 1.00 28.99 ?  146 GLN C CB    1 
ATOM   12169 C  CG    . GLN C 2 167 ? 117.800 73.382  137.653 1.00 30.30 ?  146 GLN C CG    1 
ATOM   12170 C  CD    . GLN C 2 167 ? 117.992 73.795  139.106 1.00 33.32 ?  146 GLN C CD    1 
ATOM   12171 O  OE1   . GLN C 2 167 ? 119.121 73.922  139.584 1.00 34.63 ?  146 GLN C OE1   1 
ATOM   12172 N  NE2   . GLN C 2 167 ? 116.886 73.984  139.822 1.00 32.32 ?  146 GLN C NE2   1 
ATOM   12173 N  N     . LYS C 2 168 ? 122.041 74.959  136.891 1.00 31.29 ?  147 LYS C N     1 
ATOM   12174 C  CA    . LYS C 2 168 ? 123.451 74.888  136.508 1.00 33.14 ?  147 LYS C CA    1 
ATOM   12175 C  C     . LYS C 2 168 ? 123.737 73.532  135.876 1.00 33.79 ?  147 LYS C C     1 
ATOM   12176 O  O     . LYS C 2 168 ? 123.201 72.507  136.310 1.00 34.06 ?  147 LYS C O     1 
ATOM   12177 C  CB    . LYS C 2 168 ? 124.346 75.130  137.721 1.00 33.44 ?  147 LYS C CB    1 
ATOM   12178 C  CG    . LYS C 2 168 ? 125.771 75.579  137.407 1.00 35.61 ?  147 LYS C CG    1 
ATOM   12179 C  CD    . LYS C 2 168 ? 126.530 75.827  138.706 1.00 38.40 ?  147 LYS C CD    1 
ATOM   12180 C  CE    . LYS C 2 168 ? 127.852 76.543  138.485 1.00 40.48 ?  147 LYS C CE    1 
ATOM   12181 N  NZ    . LYS C 2 168 ? 128.978 75.572  138.442 1.00 41.56 1  147 LYS C NZ    1 
ATOM   12182 N  N     . ASP C 2 169 ? 124.542 73.547  134.818 1.00 35.10 ?  148 ASP C N     1 
ATOM   12183 C  CA    . ASP C 2 169 ? 124.929 72.329  134.087 1.00 36.27 ?  148 ASP C CA    1 
ATOM   12184 C  C     . ASP C 2 169 ? 123.766 71.516  133.516 1.00 36.29 ?  148 ASP C C     1 
ATOM   12185 O  O     . ASP C 2 169 ? 123.937 70.352  133.149 1.00 36.95 ?  148 ASP C O     1 
ATOM   12186 C  CB    . ASP C 2 169 ? 125.801 71.429  134.969 1.00 37.15 ?  148 ASP C CB    1 
ATOM   12187 C  CG    . ASP C 2 169 ? 127.167 72.009  135.220 1.00 38.94 ?  148 ASP C CG    1 
ATOM   12188 O  OD1   . ASP C 2 169 ? 127.615 72.866  134.423 1.00 41.71 ?  148 ASP C OD1   1 
ATOM   12189 O  OD2   . ASP C 2 169 ? 127.794 71.605  136.220 1.00 41.64 -1 148 ASP C OD2   1 
ATOM   12190 N  N     . ASP C 2 170 ? 122.585 72.118  133.443 1.00 35.87 ?  149 ASP C N     1 
ATOM   12191 C  CA    . ASP C 2 170 ? 121.432 71.437  132.869 1.00 35.24 ?  149 ASP C CA    1 
ATOM   12192 C  C     . ASP C 2 170 ? 121.043 72.178  131.596 1.00 34.12 ?  149 ASP C C     1 
ATOM   12193 O  O     . ASP C 2 170 ? 120.402 73.247  131.635 1.00 33.52 ?  149 ASP C O     1 
ATOM   12194 C  CB    . ASP C 2 170 ? 120.285 71.350  133.882 1.00 36.09 ?  149 ASP C CB    1 
ATOM   12195 C  CG    . ASP C 2 170 ? 118.986 70.819  133.277 1.00 38.39 ?  149 ASP C CG    1 
ATOM   12196 O  OD1   . ASP C 2 170 ? 118.992 70.246  132.161 1.00 42.06 ?  149 ASP C OD1   1 
ATOM   12197 O  OD2   . ASP C 2 170 ? 117.940 70.968  133.938 1.00 42.21 -1 149 ASP C OD2   1 
ATOM   12198 N  N     . GLU C 2 171 ? 121.463 71.599  130.476 1.00 32.48 ?  150 GLU C N     1 
ATOM   12199 C  CA    . GLU C 2 171 ? 121.336 72.228  129.173 1.00 30.93 ?  150 GLU C CA    1 
ATOM   12200 C  C     . GLU C 2 171 ? 119.880 72.337  128.708 1.00 29.37 ?  150 GLU C C     1 
ATOM   12201 O  O     . GLU C 2 171 ? 119.542 73.244  127.948 1.00 28.99 ?  150 GLU C O     1 
ATOM   12202 C  CB    . GLU C 2 171 ? 122.217 71.513  128.131 1.00 31.30 ?  150 GLU C CB    1 
ATOM   12203 C  CG    . GLU C 2 171 ? 121.754 70.107  127.682 1.00 33.64 ?  150 GLU C CG    1 
ATOM   12204 C  CD    . GLU C 2 171 ? 122.820 69.320  126.882 1.00 36.40 ?  150 GLU C CD    1 
ATOM   12205 O  OE1   . GLU C 2 171 ? 123.920 69.855  126.625 1.00 38.62 ?  150 GLU C OE1   1 
ATOM   12206 O  OE2   . GLU C 2 171 ? 122.556 68.154  126.508 1.00 37.42 -1 150 GLU C OE2   1 
ATOM   12207 N  N     . ILE C 2 172 ? 119.029 71.416  129.160 1.00 27.68 ?  151 ILE C N     1 
ATOM   12208 C  CA    . ILE C 2 172 ? 117.617 71.433  128.768 1.00 26.26 ?  151 ILE C CA    1 
ATOM   12209 C  C     . ILE C 2 172 ? 116.886 72.631  129.381 1.00 24.85 ?  151 ILE C C     1 
ATOM   12210 O  O     . ILE C 2 172 ? 116.131 73.304  128.683 1.00 23.53 ?  151 ILE C O     1 
ATOM   12211 C  CB    . ILE C 2 172 ? 116.893 70.097  129.087 1.00 26.53 ?  151 ILE C CB    1 
ATOM   12212 C  CG1   . ILE C 2 172 ? 117.539 68.932  128.319 1.00 27.59 ?  151 ILE C CG1   1 
ATOM   12213 C  CG2   . ILE C 2 172 ? 115.380 70.194  128.812 1.00 26.51 ?  151 ILE C CG2   1 
ATOM   12214 C  CD1   . ILE C 2 172 ? 117.381 68.977  126.793 1.00 26.91 ?  151 ILE C CD1   1 
ATOM   12215 N  N     . SER C 2 173 ? 117.116 72.907  130.668 1.00 23.58 ?  152 SER C N     1 
ATOM   12216 C  CA    . SER C 2 173 ? 116.487 74.075  131.281 1.00 22.36 ?  152 SER C CA    1 
ATOM   12217 C  C     . SER C 2 173 ? 116.997 75.361  130.628 1.00 21.79 ?  152 SER C C     1 
ATOM   12218 O  O     . SER C 2 173 ? 116.248 76.336  130.488 1.00 20.91 ?  152 SER C O     1 
ATOM   12219 C  CB    . SER C 2 173 ? 116.670 74.099  132.804 1.00 22.43 ?  152 SER C CB    1 
ATOM   12220 O  OG    . SER C 2 173 ? 118.039 74.153  133.169 1.00 24.02 ?  152 SER C OG    1 
ATOM   12221 N  N     . LEU C 2 174 ? 118.270 75.353  130.231 1.00 21.65 ?  153 LEU C N     1 
ATOM   12222 C  CA    . LEU C 2 174 ? 118.873 76.494  129.545 1.00 21.86 ?  153 LEU C CA    1 
ATOM   12223 C  C     . LEU C 2 174 ? 118.234 76.708  128.171 1.00 21.98 ?  153 LEU C C     1 
ATOM   12224 O  O     . LEU C 2 174 ? 117.884 77.841  127.832 1.00 21.64 ?  153 LEU C O     1 
ATOM   12225 C  CB    . LEU C 2 174 ? 120.406 76.358  129.445 1.00 21.71 ?  153 LEU C CB    1 
ATOM   12226 C  CG    . LEU C 2 174 ? 121.204 77.471  128.737 1.00 22.04 ?  153 LEU C CG    1 
ATOM   12227 C  CD1   . LEU C 2 174 ? 120.887 78.863  129.281 1.00 21.99 ?  153 LEU C CD1   1 
ATOM   12228 C  CD2   . LEU C 2 174 ? 122.706 77.184  128.841 1.00 23.37 ?  153 LEU C CD2   1 
ATOM   12229 N  N     . PHE C 2 175 ? 118.079 75.627  127.399 1.00 22.17 ?  154 PHE C N     1 
ATOM   12230 C  CA    . PHE C 2 175 ? 117.389 75.676  126.090 1.00 22.02 ?  154 PHE C CA    1 
ATOM   12231 C  C     . PHE C 2 175 ? 116.000 76.293  126.200 1.00 21.86 ?  154 PHE C C     1 
ATOM   12232 O  O     . PHE C 2 175 ? 115.602 77.114  125.364 1.00 21.62 ?  154 PHE C O     1 
ATOM   12233 C  CB    . PHE C 2 175 ? 117.251 74.267  125.491 1.00 22.08 ?  154 PHE C CB    1 
ATOM   12234 C  CG    . PHE C 2 175 ? 116.407 74.215  124.232 1.00 21.99 ?  154 PHE C CG    1 
ATOM   12235 C  CD1   . PHE C 2 175 ? 116.963 74.522  122.987 1.00 20.87 ?  154 PHE C CD1   1 
ATOM   12236 C  CD2   . PHE C 2 175 ? 115.048 73.872  124.298 1.00 20.82 ?  154 PHE C CD2   1 
ATOM   12237 C  CE1   . PHE C 2 175 ? 116.186 74.504  121.828 1.00 20.27 ?  154 PHE C CE1   1 
ATOM   12238 C  CE2   . PHE C 2 175 ? 114.258 73.838  123.145 1.00 20.19 ?  154 PHE C CE2   1 
ATOM   12239 C  CZ    . PHE C 2 175 ? 114.830 74.150  121.899 1.00 20.93 ?  154 PHE C CZ    1 
ATOM   12240 N  N     . LYS C 2 176 ? 115.251 75.857  127.213 1.00 21.98 ?  155 LYS C N     1 
ATOM   12241 C  CA    . LYS C 2 176 ? 113.885 76.346  127.424 1.00 21.79 ?  155 LYS C CA    1 
ATOM   12242 C  C     . LYS C 2 176 ? 113.865 77.858  127.671 1.00 21.70 ?  155 LYS C C     1 
ATOM   12243 O  O     . LYS C 2 176 ? 113.025 78.576  127.110 1.00 21.10 ?  155 LYS C O     1 
ATOM   12244 C  CB    . LYS C 2 176 ? 113.209 75.577  128.566 1.00 22.00 ?  155 LYS C CB    1 
ATOM   12245 C  CG    . LYS C 2 176 ? 112.959 74.106  128.259 1.00 21.93 ?  155 LYS C CG    1 
ATOM   12246 C  CD    . LYS C 2 176 ? 112.352 73.378  129.445 1.00 23.06 ?  155 LYS C CD    1 
ATOM   12247 C  CE    . LYS C 2 176 ? 112.046 71.932  129.111 1.00 24.91 ?  155 LYS C CE    1 
ATOM   12248 N  NZ    . LYS C 2 176 ? 111.762 71.133  130.350 1.00 25.16 1  155 LYS C NZ    1 
ATOM   12249 N  N     . ALA C 2 177 ? 114.794 78.336  128.506 1.00 21.49 ?  156 ALA C N     1 
ATOM   12250 C  CA    . ALA C 2 177 ? 114.939 79.771  128.734 1.00 20.60 ?  156 ALA C CA    1 
ATOM   12251 C  C     . ALA C 2 177 ? 115.385 80.545  127.474 1.00 20.37 ?  156 ALA C C     1 
ATOM   12252 O  O     . ALA C 2 177 ? 114.938 81.663  127.252 1.00 19.61 ?  156 ALA C O     1 
ATOM   12253 C  CB    . ALA C 2 177 ? 115.885 80.049  129.899 1.00 20.88 ?  156 ALA C CB    1 
ATOM   12254 N  N     . MET C 2 178 ? 116.247 79.945  126.653 1.00 20.70 ?  157 MET C N     1 
ATOM   12255 C  CA    . MET C 2 178 ? 116.676 80.575  125.393 1.00 21.06 ?  157 MET C CA    1 
ATOM   12256 C  C     . MET C 2 178 ? 115.540 80.664  124.392 1.00 20.83 ?  157 MET C C     1 
ATOM   12257 O  O     . MET C 2 178 ? 115.487 81.610  123.599 1.00 21.28 ?  157 MET C O     1 
ATOM   12258 C  CB    . MET C 2 178 ? 117.853 79.821  124.746 1.00 20.68 ?  157 MET C CB    1 
ATOM   12259 C  CG    . MET C 2 178 ? 119.185 79.901  125.489 1.00 21.61 ?  157 MET C CG    1 
ATOM   12260 S  SD    . MET C 2 178 ? 120.392 78.774  124.753 1.00 24.32 ?  157 MET C SD    1 
ATOM   12261 C  CE    . MET C 2 178 ? 121.908 79.340  125.551 1.00 23.64 ?  157 MET C CE    1 
ATOM   12262 N  N     . VAL C 2 179 ? 114.653 79.670  124.392 1.00 20.76 ?  158 VAL C N     1 
ATOM   12263 C  CA    . VAL C 2 179 ? 113.457 79.720  123.542 1.00 20.14 ?  158 VAL C CA    1 
ATOM   12264 C  C     . VAL C 2 179 ? 112.575 80.887  124.000 1.00 20.35 ?  158 VAL C C     1 
ATOM   12265 O  O     . VAL C 2 179 ? 112.083 81.671  123.184 1.00 19.82 ?  158 VAL C O     1 
ATOM   12266 C  CB    . VAL C 2 179 ? 112.640 78.401  123.598 1.00 20.07 ?  158 VAL C CB    1 
ATOM   12267 C  CG1   . VAL C 2 179 ? 111.283 78.577  122.913 1.00 20.07 ?  158 VAL C CG1   1 
ATOM   12268 C  CG2   . VAL C 2 179 ? 113.417 77.262  122.946 1.00 20.57 ?  158 VAL C CG2   1 
ATOM   12269 N  N     . ALA C 2 180 ? 112.390 80.985  125.312 1.00 19.89 ?  159 ALA C N     1 
ATOM   12270 C  CA    . ALA C 2 180 ? 111.621 82.074  125.915 1.00 20.50 ?  159 ALA C CA    1 
ATOM   12271 C  C     . ALA C 2 180 ? 112.218 83.438  125.528 1.00 20.67 ?  159 ALA C C     1 
ATOM   12272 O  O     . ALA C 2 180 ? 111.486 84.350  125.140 1.00 21.27 ?  159 ALA C O     1 
ATOM   12273 C  CB    . ALA C 2 180 ? 111.602 81.916  127.420 1.00 20.03 ?  159 ALA C CB    1 
ATOM   12274 N  N     . SER C 2 181 ? 113.541 83.558  125.623 1.00 20.78 ?  160 SER C N     1 
ATOM   12275 C  CA    . SER C 2 181 ? 114.253 84.781  125.235 1.00 21.26 ?  160 SER C CA    1 
ATOM   12276 C  C     . SER C 2 181 ? 114.086 85.109  123.744 1.00 21.19 ?  160 SER C C     1 
ATOM   12277 O  O     . SER C 2 181 ? 113.801 86.249  123.394 1.00 20.89 ?  160 SER C O     1 
ATOM   12278 C  CB    . SER C 2 181 ? 115.740 84.693  125.612 1.00 21.42 ?  160 SER C CB    1 
ATOM   12279 O  OG    . SER C 2 181 ? 116.416 85.908  125.321 1.00 23.69 ?  160 SER C OG    1 
ATOM   12280 N  N     . VAL C 2 182 ? 114.263 84.118  122.864 1.00 20.99 ?  161 VAL C N     1 
ATOM   12281 C  CA    . VAL C 2 182 ? 113.989 84.358  121.442 1.00 21.18 ?  161 VAL C CA    1 
ATOM   12282 C  C     . VAL C 2 182 ? 112.538 84.825  121.231 1.00 21.15 ?  161 VAL C C     1 
ATOM   12283 O  O     . VAL C 2 182 ? 112.291 85.773  120.468 1.00 21.18 ?  161 VAL C O     1 
ATOM   12284 C  CB    . VAL C 2 182 ? 114.319 83.121  120.546 1.00 21.11 ?  161 VAL C CB    1 
ATOM   12285 C  CG1   . VAL C 2 182 ? 113.828 83.344  119.118 1.00 21.75 ?  161 VAL C CG1   1 
ATOM   12286 C  CG2   . VAL C 2 182 ? 115.821 82.844  120.553 1.00 20.98 ?  161 VAL C CG2   1 
ATOM   12287 N  N     . TYR C 2 183 ? 111.576 84.184  121.909 1.00 21.10 ?  162 TYR C N     1 
ATOM   12288 C  CA    . TYR C 2 183 ? 110.173 84.607  121.790 1.00 21.21 ?  162 TYR C CA    1 
ATOM   12289 C  C     . TYR C 2 183 ? 109.935 86.033  122.286 1.00 21.38 ?  162 TYR C C     1 
ATOM   12290 O  O     . TYR C 2 183 ? 109.096 86.744  121.745 1.00 20.97 ?  162 TYR C O     1 
ATOM   12291 C  CB    . TYR C 2 183 ? 109.197 83.639  122.491 1.00 21.50 ?  162 TYR C CB    1 
ATOM   12292 C  CG    . TYR C 2 183 ? 109.034 82.316  121.792 1.00 22.20 ?  162 TYR C CG    1 
ATOM   12293 C  CD1   . TYR C 2 183 ? 109.357 82.174  120.444 1.00 23.80 ?  162 TYR C CD1   1 
ATOM   12294 C  CD2   . TYR C 2 183 ? 108.535 81.202  122.475 1.00 23.71 ?  162 TYR C CD2   1 
ATOM   12295 C  CE1   . TYR C 2 183 ? 109.207 80.944  119.791 1.00 25.52 ?  162 TYR C CE1   1 
ATOM   12296 C  CE2   . TYR C 2 183 ? 108.378 79.981  121.838 1.00 24.01 ?  162 TYR C CE2   1 
ATOM   12297 C  CZ    . TYR C 2 183 ? 108.723 79.854  120.503 1.00 25.47 ?  162 TYR C CZ    1 
ATOM   12298 O  OH    . TYR C 2 183 ? 108.585 78.637  119.867 1.00 25.37 ?  162 TYR C OH    1 
ATOM   12299 N  N     . LEU C 2 184 ? 110.662 86.433  123.319 1.00 22.12 ?  163 LEU C N     1 
ATOM   12300 C  CA    . LEU C 2 184 ? 110.612 87.830  123.792 1.00 23.80 ?  163 LEU C CA    1 
ATOM   12301 C  C     . LEU C 2 184 ? 111.235 88.771  122.751 1.00 24.21 ?  163 LEU C C     1 
ATOM   12302 O  O     . LEU C 2 184 ? 110.644 89.779  122.423 1.00 24.72 ?  163 LEU C O     1 
ATOM   12303 C  CB    . LEU C 2 184 ? 111.310 87.977  125.148 1.00 23.52 ?  163 LEU C CB    1 
ATOM   12304 C  CG    . LEU C 2 184 ? 111.299 89.330  125.887 1.00 24.91 ?  163 LEU C CG    1 
ATOM   12305 C  CD1   . LEU C 2 184 ? 111.267 89.097  127.376 1.00 24.81 ?  163 LEU C CD1   1 
ATOM   12306 C  CD2   . LEU C 2 184 ? 112.482 90.235  125.516 1.00 26.39 ?  163 LEU C CD2   1 
ATOM   12307 N  N     . GLU C 2 185 ? 112.415 88.419  122.224 1.00 25.17 ?  164 GLU C N     1 
ATOM   12308 C  CA    . GLU C 2 185 ? 113.154 89.291  121.297 1.00 25.30 ?  164 GLU C CA    1 
ATOM   12309 C  C     . GLU C 2 185 ? 112.452 89.478  119.941 1.00 25.07 ?  164 GLU C C     1 
ATOM   12310 O  O     . GLU C 2 185 ? 112.387 90.594  119.398 1.00 24.49 ?  164 GLU C O     1 
ATOM   12311 C  CB    . GLU C 2 185 ? 114.574 88.739  121.032 1.00 26.17 ?  164 GLU C CB    1 
ATOM   12312 C  CG    . GLU C 2 185 ? 115.516 88.737  122.256 1.00 27.05 ?  164 GLU C CG    1 
ATOM   12313 C  CD    . GLU C 2 185 ? 116.093 90.121  122.579 1.00 29.23 ?  164 GLU C CD    1 
ATOM   12314 O  OE1   . GLU C 2 185 ? 115.772 91.121  121.875 1.00 28.79 ?  164 GLU C OE1   1 
ATOM   12315 O  OE2   . GLU C 2 185 ? 116.907 90.218  123.526 1.00 28.65 -1 164 GLU C OE2   1 
ATOM   12316 N  N     . SER C 2 186 ? 111.956 88.371  119.405 1.00 24.23 ?  165 SER C N     1 
ATOM   12317 C  CA    . SER C 2 186 ? 111.588 88.270  117.997 1.00 24.71 ?  165 SER C CA    1 
ATOM   12318 C  C     . SER C 2 186 ? 110.086 88.155  117.762 1.00 24.51 ?  165 SER C C     1 
ATOM   12319 O  O     . SER C 2 186 ? 109.639 88.219  116.619 1.00 24.87 ?  165 SER C O     1 
ATOM   12320 C  CB    . SER C 2 186 ? 112.290 87.060  117.367 1.00 25.06 ?  165 SER C CB    1 
ATOM   12321 O  OG    . SER C 2 186 ? 113.698 87.154  117.490 1.00 26.29 ?  165 SER C OG    1 
ATOM   12322 N  N     . PHE C 2 187 ? 109.321 87.972  118.835 1.00 24.71 ?  166 PHE C N     1 
ATOM   12323 C  CA    . PHE C 2 187 ? 107.867 87.842  118.749 1.00 25.69 ?  166 PHE C CA    1 
ATOM   12324 C  C     . PHE C 2 187 ? 107.135 88.845  119.655 1.00 25.87 ?  166 PHE C C     1 
ATOM   12325 O  O     . PHE C 2 187 ? 106.383 89.680  119.148 1.00 26.03 ?  166 PHE C O     1 
ATOM   12326 C  CB    . PHE C 2 187 ? 107.419 86.398  119.051 1.00 25.54 ?  166 PHE C CB    1 
ATOM   12327 C  CG    . PHE C 2 187 ? 105.925 86.239  119.246 1.00 26.64 ?  166 PHE C CG    1 
ATOM   12328 C  CD1   . PHE C 2 187 ? 105.028 86.544  118.214 1.00 25.90 ?  166 PHE C CD1   1 
ATOM   12329 C  CD2   . PHE C 2 187 ? 105.415 85.771  120.460 1.00 27.45 ?  166 PHE C CD2   1 
ATOM   12330 C  CE1   . PHE C 2 187 ? 103.639 86.400  118.394 1.00 25.64 ?  166 PHE C CE1   1 
ATOM   12331 C  CE2   . PHE C 2 187 ? 104.021 85.617  120.653 1.00 26.52 ?  166 PHE C CE2   1 
ATOM   12332 C  CZ    . PHE C 2 187 ? 103.139 85.932  119.617 1.00 27.18 ?  166 PHE C CZ    1 
ATOM   12333 N  N     . LEU C 2 188 ? 107.371 88.765  120.966 1.00 26.13 ?  167 LEU C N     1 
ATOM   12334 C  CA    . LEU C 2 188 ? 106.609 89.547  121.975 1.00 27.13 ?  167 LEU C CA    1 
ATOM   12335 C  C     . LEU C 2 188 ? 106.745 91.079  121.891 1.00 27.22 ?  167 LEU C C     1 
ATOM   12336 O  O     . LEU C 2 188 ? 105.808 91.807  122.245 1.00 28.03 ?  167 LEU C O     1 
ATOM   12337 C  CB    . LEU C 2 188 ? 106.967 89.105  123.403 1.00 26.89 ?  167 LEU C CB    1 
ATOM   12338 C  CG    . LEU C 2 188 ? 106.632 87.705  123.940 1.00 28.64 ?  167 LEU C CG    1 
ATOM   12339 C  CD1   . LEU C 2 188 ? 107.151 87.550  125.368 1.00 28.34 ?  167 LEU C CD1   1 
ATOM   12340 C  CD2   . LEU C 2 188 ? 105.144 87.404  123.891 1.00 27.90 ?  167 LEU C CD2   1 
ATOM   12341 N  N     . PHE C 2 189 ? 107.909 91.562  121.472 1.00 26.79 ?  168 PHE C N     1 
ATOM   12342 C  CA    . PHE C 2 189 ? 108.118 93.002  121.333 1.00 26.90 ?  168 PHE C CA    1 
ATOM   12343 C  C     . PHE C 2 189 ? 107.227 93.592  120.233 1.00 26.52 ?  168 PHE C C     1 
ATOM   12344 O  O     . PHE C 2 189 ? 106.968 94.803  120.215 1.00 26.02 ?  168 PHE C O     1 
ATOM   12345 C  CB    . PHE C 2 189 ? 109.586 93.326  120.990 1.00 27.03 ?  168 PHE C CB    1 
ATOM   12346 C  CG    . PHE C 2 189 ? 110.513 93.461  122.195 1.00 28.09 ?  168 PHE C CG    1 
ATOM   12347 C  CD1   . PHE C 2 189 ? 110.239 94.361  123.227 1.00 28.69 ?  168 PHE C CD1   1 
ATOM   12348 C  CD2   . PHE C 2 189 ? 111.699 92.739  122.253 1.00 29.15 ?  168 PHE C CD2   1 
ATOM   12349 C  CE1   . PHE C 2 189 ? 111.102 94.500  124.325 1.00 28.50 ?  168 PHE C CE1   1 
ATOM   12350 C  CE2   . PHE C 2 189 ? 112.577 92.867  123.345 1.00 30.19 ?  168 PHE C CE2   1 
ATOM   12351 C  CZ    . PHE C 2 189 ? 112.270 93.757  124.390 1.00 29.81 ?  168 PHE C CZ    1 
ATOM   12352 N  N     . TYR C 2 190 ? 106.776 92.747  119.306 1.00 26.18 ?  169 TYR C N     1 
ATOM   12353 C  CA    . TYR C 2 190 ? 106.236 93.272  118.056 1.00 26.24 ?  169 TYR C CA    1 
ATOM   12354 C  C     . TYR C 2 190 ? 104.809 93.839  118.110 1.00 25.94 ?  169 TYR C C     1 
ATOM   12355 O  O     . TYR C 2 190 ? 104.448 94.695  117.301 1.00 25.71 ?  169 TYR C O     1 
ATOM   12356 C  CB    . TYR C 2 190 ? 106.498 92.297  116.906 1.00 27.13 ?  169 TYR C CB    1 
ATOM   12357 C  CG    . TYR C 2 190 ? 107.951 92.389  116.489 1.00 28.07 ?  169 TYR C CG    1 
ATOM   12358 C  CD1   . TYR C 2 190 ? 108.940 91.661  117.160 1.00 29.54 ?  169 TYR C CD1   1 
ATOM   12359 C  CD2   . TYR C 2 190 ? 108.348 93.257  115.472 1.00 29.31 ?  169 TYR C CD2   1 
ATOM   12360 C  CE1   . TYR C 2 190 ? 110.286 91.769  116.798 1.00 30.44 ?  169 TYR C CE1   1 
ATOM   12361 C  CE2   . TYR C 2 190 ? 109.697 93.371  115.099 1.00 30.64 ?  169 TYR C CE2   1 
ATOM   12362 C  CZ    . TYR C 2 190 ? 110.658 92.627  115.772 1.00 30.40 ?  169 TYR C CZ    1 
ATOM   12363 O  OH    . TYR C 2 190 ? 111.983 92.742  115.417 1.00 28.85 ?  169 TYR C OH    1 
ATOM   12364 N  N     . SER C 2 191 ? 104.029 93.407  119.097 1.00 25.17 ?  170 SER C N     1 
ATOM   12365 C  CA    . SER C 2 191 ? 102.716 93.997  119.340 1.00 25.10 ?  170 SER C CA    1 
ATOM   12366 C  C     . SER C 2 191 ? 102.904 95.458  119.768 1.00 25.16 ?  170 SER C C     1 
ATOM   12367 O  O     . SER C 2 191 ? 102.043 96.304  119.504 1.00 25.30 ?  170 SER C O     1 
ATOM   12368 C  CB    . SER C 2 191 ? 101.946 93.205  120.397 1.00 24.56 ?  170 SER C CB    1 
ATOM   12369 O  OG    . SER C 2 191 ? 102.590 93.266  121.655 1.00 24.98 ?  170 SER C OG    1 
ATOM   12370 N  N     . GLY C 2 192 ? 104.044 95.723  120.416 1.00 24.32 ?  171 GLY C N     1 
ATOM   12371 C  CA    . GLY C 2 192 ? 104.464 97.059  120.818 1.00 23.97 ?  171 GLY C CA    1 
ATOM   12372 C  C     . GLY C 2 192 ? 105.103 97.861  119.696 1.00 23.85 ?  171 GLY C C     1 
ATOM   12373 O  O     . GLY C 2 192 ? 104.694 98.997  119.457 1.00 23.99 ?  171 GLY C O     1 
ATOM   12374 N  N     . PHE C 2 193 ? 106.079 97.273  119.002 1.00 23.28 ?  172 PHE C N     1 
ATOM   12375 C  CA    . PHE C 2 193 ? 106.777 97.947  117.892 1.00 23.85 ?  172 PHE C CA    1 
ATOM   12376 C  C     . PHE C 2 193 ? 105.856 98.421  116.766 1.00 23.72 ?  172 PHE C C     1 
ATOM   12377 O  O     . PHE C 2 193 ? 106.181 99.385  116.075 1.00 23.92 ?  172 PHE C O     1 
ATOM   12378 C  CB    . PHE C 2 193 ? 107.851 97.053  117.259 1.00 23.47 ?  172 PHE C CB    1 
ATOM   12379 C  CG    . PHE C 2 193 ? 109.095 96.877  118.101 1.00 24.32 ?  172 PHE C CG    1 
ATOM   12380 C  CD1   . PHE C 2 193 ? 109.458 97.821  119.063 1.00 22.28 ?  172 PHE C CD1   1 
ATOM   12381 C  CD2   . PHE C 2 193 ? 109.920 95.768  117.904 1.00 23.82 ?  172 PHE C CD2   1 
ATOM   12382 C  CE1   . PHE C 2 193 ? 110.612 97.657  119.841 1.00 23.41 ?  172 PHE C CE1   1 
ATOM   12383 C  CE2   . PHE C 2 193 ? 111.083 95.586  118.673 1.00 24.70 ?  172 PHE C CE2   1 
ATOM   12384 C  CZ    . PHE C 2 193 ? 111.432 96.538  119.643 1.00 24.87 ?  172 PHE C CZ    1 
ATOM   12385 N  N     . TYR C 2 194 ? 104.735 97.726  116.563 1.00 23.31 ?  173 TYR C N     1 
ATOM   12386 C  CA    . TYR C 2 194 ? 103.826 98.033  115.456 1.00 23.26 ?  173 TYR C CA    1 
ATOM   12387 C  C     . TYR C 2 194 ? 103.486 99.525  115.393 1.00 23.04 ?  173 TYR C C     1 
ATOM   12388 O  O     . TYR C 2 194 ? 103.540 100.139 114.324 1.00 23.47 ?  173 TYR C O     1 
ATOM   12389 C  CB    . TYR C 2 194 ? 102.524 97.217  115.541 1.00 23.13 ?  173 TYR C CB    1 
ATOM   12390 C  CG    . TYR C 2 194 ? 101.600 97.432  114.348 1.00 24.10 ?  173 TYR C CG    1 
ATOM   12391 C  CD1   . TYR C 2 194 ? 101.642 96.570  113.251 1.00 25.72 ?  173 TYR C CD1   1 
ATOM   12392 C  CD2   . TYR C 2 194 ? 100.709 98.505  114.307 1.00 27.04 ?  173 TYR C CD2   1 
ATOM   12393 C  CE1   . TYR C 2 194 ? 100.800 96.761  112.147 1.00 28.94 ?  173 TYR C CE1   1 
ATOM   12394 C  CE2   . TYR C 2 194 ? 99.868  98.713  113.198 1.00 27.84 ?  173 TYR C CE2   1 
ATOM   12395 C  CZ    . TYR C 2 194 ? 99.925  97.834  112.128 1.00 29.97 ?  173 TYR C CZ    1 
ATOM   12396 O  OH    . TYR C 2 194 ? 99.112  98.025  111.024 1.00 34.34 ?  173 TYR C OH    1 
ATOM   12397 N  N     . TYR C 2 195 ? 103.133 100.093 116.536 1.00 22.51 ?  174 TYR C N     1 
ATOM   12398 C  CA    . TYR C 2 195 ? 102.525 101.419 116.563 1.00 22.60 ?  174 TYR C CA    1 
ATOM   12399 C  C     . TYR C 2 195 ? 103.521 102.557 116.274 1.00 22.64 ?  174 TYR C C     1 
ATOM   12400 O  O     . TYR C 2 195 ? 103.217 103.419 115.442 1.00 22.39 ?  174 TYR C O     1 
ATOM   12401 C  CB    . TYR C 2 195 ? 101.746 101.623 117.862 1.00 22.32 ?  174 TYR C CB    1 
ATOM   12402 C  CG    . TYR C 2 195 ? 100.544 102.540 117.747 1.00 23.39 ?  174 TYR C CG    1 
ATOM   12403 C  CD1   . TYR C 2 195 ? 99.791  102.614 116.564 1.00 22.84 ?  174 TYR C CD1   1 
ATOM   12404 C  CD2   . TYR C 2 195 ? 100.137 103.304 118.838 1.00 22.23 ?  174 TYR C CD2   1 
ATOM   12405 C  CE1   . TYR C 2 195 ? 98.675  103.456 116.474 1.00 24.05 ?  174 TYR C CE1   1 
ATOM   12406 C  CE2   . TYR C 2 195 ? 99.018  104.136 118.763 1.00 24.11 ?  174 TYR C CE2   1 
ATOM   12407 C  CZ    . TYR C 2 195 ? 98.295  104.204 117.584 1.00 23.92 ?  174 TYR C CZ    1 
ATOM   12408 O  OH    . TYR C 2 195 ? 97.215  105.042 117.519 1.00 25.00 ?  174 TYR C OH    1 
ATOM   12409 N  N     . PRO C 2 196 ? 104.715 102.556 116.937 1.00 22.25 ?  175 PRO C N     1 
ATOM   12410 C  CA    . PRO C 2 196 ? 105.740 103.533 116.534 1.00 22.45 ?  175 PRO C CA    1 
ATOM   12411 C  C     . PRO C 2 196 ? 106.123 103.418 115.058 1.00 22.59 ?  175 PRO C C     1 
ATOM   12412 O  O     . PRO C 2 196 ? 106.345 104.447 114.408 1.00 22.19 ?  175 PRO C O     1 
ATOM   12413 C  CB    . PRO C 2 196 ? 106.947 103.195 117.421 1.00 22.25 ?  175 PRO C CB    1 
ATOM   12414 C  CG    . PRO C 2 196 ? 106.394 102.446 118.588 1.00 22.22 ?  175 PRO C CG    1 
ATOM   12415 C  CD    . PRO C 2 196 ? 105.155 101.742 118.094 1.00 22.32 ?  175 PRO C CD    1 
ATOM   12416 N  N     . LEU C 2 197 ? 106.190 102.189 114.535 1.00 21.92 ?  176 LEU C N     1 
ATOM   12417 C  CA    . LEU C 2 197 ? 106.505 101.975 113.121 1.00 22.35 ?  176 LEU C CA    1 
ATOM   12418 C  C     . LEU C 2 197 ? 105.381 102.490 112.215 1.00 22.60 ?  176 LEU C C     1 
ATOM   12419 O  O     . LEU C 2 197 ? 105.634 103.063 111.152 1.00 22.41 ?  176 LEU C O     1 
ATOM   12420 C  CB    . LEU C 2 197 ? 106.760 100.499 112.822 1.00 22.69 ?  176 LEU C CB    1 
ATOM   12421 C  CG    . LEU C 2 197 ? 107.956 99.774  113.453 1.00 23.68 ?  176 LEU C CG    1 
ATOM   12422 C  CD1   . LEU C 2 197 ? 107.955 98.302  113.010 1.00 23.70 ?  176 LEU C CD1   1 
ATOM   12423 C  CD2   . LEU C 2 197 ? 109.271 100.449 113.076 1.00 23.09 ?  176 LEU C CD2   1 
ATOM   12424 N  N     . TYR C 2 198 ? 104.141 102.278 112.652 1.00 22.64 ?  177 TYR C N     1 
ATOM   12425 C  CA    . TYR C 2 198 ? 102.960 102.705 111.916 1.00 22.92 ?  177 TYR C CA    1 
ATOM   12426 C  C     . TYR C 2 198 ? 102.965 104.238 111.771 1.00 23.68 ?  177 TYR C C     1 
ATOM   12427 O  O     . TYR C 2 198 ? 102.696 104.771 110.692 1.00 23.81 ?  177 TYR C O     1 
ATOM   12428 C  CB    . TYR C 2 198 ? 101.724 102.198 112.652 1.00 22.73 ?  177 TYR C CB    1 
ATOM   12429 C  CG    . TYR C 2 198 ? 100.382 102.570 112.082 1.00 22.91 ?  177 TYR C CG    1 
ATOM   12430 C  CD1   . TYR C 2 198 ? 99.893  101.942 110.936 1.00 23.49 ?  177 TYR C CD1   1 
ATOM   12431 C  CD2   . TYR C 2 198 ? 99.569  103.502 112.728 1.00 21.97 ?  177 TYR C CD2   1 
ATOM   12432 C  CE1   . TYR C 2 198 ? 98.636  102.259 110.420 1.00 23.57 ?  177 TYR C CE1   1 
ATOM   12433 C  CE2   . TYR C 2 198 ? 98.299  103.828 112.222 1.00 22.54 ?  177 TYR C CE2   1 
ATOM   12434 C  CZ    . TYR C 2 198 ? 97.847  103.204 111.068 1.00 22.88 ?  177 TYR C CZ    1 
ATOM   12435 O  OH    . TYR C 2 198 ? 96.597  103.501 110.557 1.00 23.17 ?  177 TYR C OH    1 
ATOM   12436 N  N     . PHE C 2 199 ? 103.317 104.940 112.842 1.00 23.50 ?  178 PHE C N     1 
ATOM   12437 C  CA    . PHE C 2 199 ? 103.446 106.396 112.774 1.00 24.60 ?  178 PHE C CA    1 
ATOM   12438 C  C     . PHE C 2 199 ? 104.652 106.886 111.961 1.00 24.72 ?  178 PHE C C     1 
ATOM   12439 O  O     . PHE C 2 199 ? 104.524 107.784 111.131 1.00 24.19 ?  178 PHE C O     1 
ATOM   12440 C  CB    . PHE C 2 199 ? 103.449 107.006 114.179 1.00 24.35 ?  178 PHE C CB    1 
ATOM   12441 C  CG    . PHE C 2 199 ? 102.092 107.046 114.814 1.00 26.36 ?  178 PHE C CG    1 
ATOM   12442 C  CD1   . PHE C 2 199 ? 100.981 107.485 114.093 1.00 28.53 ?  178 PHE C CD1   1 
ATOM   12443 C  CD2   . PHE C 2 199 ? 101.917 106.665 116.137 1.00 28.23 ?  178 PHE C CD2   1 
ATOM   12444 C  CE1   . PHE C 2 199 ? 99.712  107.520 114.681 1.00 29.37 ?  178 PHE C CE1   1 
ATOM   12445 C  CE2   . PHE C 2 199 ? 100.646 106.710 116.735 1.00 28.69 ?  178 PHE C CE2   1 
ATOM   12446 C  CZ    . PHE C 2 199 ? 99.553  107.133 116.009 1.00 28.43 ?  178 PHE C CZ    1 
ATOM   12447 N  N     . TYR C 2 200 ? 105.814 106.283 112.204 1.00 25.36 ?  179 TYR C N     1 
ATOM   12448 C  CA    . TYR C 2 200 ? 107.044 106.601 111.467 1.00 26.02 ?  179 TYR C CA    1 
ATOM   12449 C  C     . TYR C 2 200 ? 106.787 106.538 109.961 1.00 26.57 ?  179 TYR C C     1 
ATOM   12450 O  O     . TYR C 2 200 ? 107.189 107.432 109.208 1.00 26.30 ?  179 TYR C O     1 
ATOM   12451 C  CB    . TYR C 2 200 ? 108.154 105.610 111.844 1.00 26.19 ?  179 TYR C CB    1 
ATOM   12452 C  CG    . TYR C 2 200 ? 109.525 105.966 111.315 1.00 27.82 ?  179 TYR C CG    1 
ATOM   12453 C  CD1   . TYR C 2 200 ? 110.044 105.327 110.184 1.00 30.77 ?  179 TYR C CD1   1 
ATOM   12454 C  CD2   . TYR C 2 200 ? 110.311 106.932 111.947 1.00 29.20 ?  179 TYR C CD2   1 
ATOM   12455 C  CE1   . TYR C 2 200 ? 111.305 105.647 109.693 1.00 31.82 ?  179 TYR C CE1   1 
ATOM   12456 C  CE2   . TYR C 2 200 ? 111.571 107.262 111.468 1.00 30.44 ?  179 TYR C CE2   1 
ATOM   12457 C  CZ    . TYR C 2 200 ? 112.061 106.614 110.338 1.00 32.74 ?  179 TYR C CZ    1 
ATOM   12458 O  OH    . TYR C 2 200 ? 113.302 106.932 109.844 1.00 34.58 ?  179 TYR C OH    1 
ATOM   12459 N  N     . GLY C 2 201 ? 106.088 105.486 109.541 1.00 26.71 ?  180 GLY C N     1 
ATOM   12460 C  CA    . GLY C 2 201 ? 105.765 105.270 108.138 1.00 27.38 ?  180 GLY C CA    1 
ATOM   12461 C  C     . GLY C 2 201 ? 104.842 106.313 107.526 1.00 27.62 ?  180 GLY C C     1 
ATOM   12462 O  O     . GLY C 2 201 ? 104.777 106.422 106.314 1.00 28.25 ?  180 GLY C O     1 
ATOM   12463 N  N     . GLN C 2 202 ? 104.138 107.072 108.365 1.00 27.60 ?  181 GLN C N     1 
ATOM   12464 C  CA    . GLN C 2 202 ? 103.259 108.163 107.911 1.00 28.24 ?  181 GLN C CA    1 
ATOM   12465 C  C     . GLN C 2 202 ? 103.912 109.525 108.093 1.00 28.30 ?  181 GLN C C     1 
ATOM   12466 O  O     . GLN C 2 202 ? 103.262 110.551 107.883 1.00 27.98 ?  181 GLN C O     1 
ATOM   12467 C  CB    . GLN C 2 202 ? 101.956 108.193 108.715 1.00 27.90 ?  181 GLN C CB    1 
ATOM   12468 C  CG    . GLN C 2 202 ? 101.095 106.975 108.616 1.00 29.54 ?  181 GLN C CG    1 
ATOM   12469 C  CD    . GLN C 2 202 ? 99.904  107.061 109.544 1.00 31.54 ?  181 GLN C CD    1 
ATOM   12470 O  OE1   . GLN C 2 202 ? 98.987  107.859 109.327 1.00 32.11 ?  181 GLN C OE1   1 
ATOM   12471 N  NE2   . GLN C 2 202 ? 99.912  106.248 110.591 1.00 31.29 ?  181 GLN C NE2   1 
ATOM   12472 N  N     . GLY C 2 203 ? 105.172 109.527 108.529 1.00 28.14 ?  182 GLY C N     1 
ATOM   12473 C  CA    . GLY C 2 203 ? 105.906 110.755 108.792 1.00 28.38 ?  182 GLY C CA    1 
ATOM   12474 C  C     . GLY C 2 203 ? 105.502 111.421 110.090 1.00 28.71 ?  182 GLY C C     1 
ATOM   12475 O  O     . GLY C 2 203 ? 105.564 112.641 110.204 1.00 28.80 ?  182 GLY C O     1 
ATOM   12476 N  N     . LYS C 2 204 ? 105.073 110.617 111.062 1.00 28.24 ?  183 LYS C N     1 
ATOM   12477 C  CA    . LYS C 2 204 ? 104.638 111.125 112.353 1.00 28.48 ?  183 LYS C CA    1 
ATOM   12478 C  C     . LYS C 2 204 ? 105.479 110.518 113.472 1.00 27.82 ?  183 LYS C C     1 
ATOM   12479 O  O     . LYS C 2 204 ? 105.863 109.342 113.407 1.00 26.73 ?  183 LYS C O     1 
ATOM   12480 C  CB    . LYS C 2 204 ? 103.157 110.825 112.587 1.00 29.13 ?  183 LYS C CB    1 
ATOM   12481 C  CG    . LYS C 2 204 ? 102.213 111.547 111.625 1.00 30.41 ?  183 LYS C CG    1 
ATOM   12482 C  CD    . LYS C 2 204 ? 100.881 110.820 111.523 1.00 33.74 ?  183 LYS C CD    1 
ATOM   12483 C  CE    . LYS C 2 204 ? 99.901  111.586 110.619 1.00 36.26 ?  183 LYS C CE    1 
ATOM   12484 N  NZ    . LYS C 2 204 ? 98.589  110.880 110.553 1.00 39.17 1  183 LYS C NZ    1 
ATOM   12485 N  N     . LEU C 2 205 ? 105.755 111.329 114.491 1.00 27.77 ?  184 LEU C N     1 
ATOM   12486 C  CA    . LEU C 2 205 ? 106.575 110.919 115.639 1.00 27.79 ?  184 LEU C CA    1 
ATOM   12487 C  C     . LEU C 2 205 ? 107.895 110.288 115.187 1.00 27.85 ?  184 LEU C C     1 
ATOM   12488 O  O     . LEU C 2 205 ? 108.281 109.193 115.621 1.00 27.07 ?  184 LEU C O     1 
ATOM   12489 C  CB    . LEU C 2 205 ? 105.784 109.975 116.567 1.00 27.76 ?  184 LEU C CB    1 
ATOM   12490 C  CG    . LEU C 2 205 ? 104.452 110.522 117.096 1.00 28.62 ?  184 LEU C CG    1 
ATOM   12491 C  CD1   . LEU C 2 205 ? 103.705 109.466 117.886 1.00 29.18 ?  184 LEU C CD1   1 
ATOM   12492 C  CD2   . LEU C 2 205 ? 104.665 111.765 117.948 1.00 28.43 ?  184 LEU C CD2   1 
ATOM   12493 N  N     . MET C 2 206 ? 108.601 110.996 114.319 1.00 28.15 ?  185 MET C N     1 
ATOM   12494 C  CA    . MET C 2 206 ? 109.740 110.398 113.659 1.00 28.80 ?  185 MET C CA    1 
ATOM   12495 C  C     . MET C 2 206 ? 111.004 110.319 114.505 1.00 28.77 ?  185 MET C C     1 
ATOM   12496 O  O     . MET C 2 206 ? 111.851 109.465 114.252 1.00 28.79 ?  185 MET C O     1 
ATOM   12497 C  CB    . MET C 2 206 ? 109.977 111.074 112.322 1.00 29.96 ?  185 MET C CB    1 
ATOM   12498 C  CG    . MET C 2 206 ? 108.839 110.777 111.341 1.00 31.23 ?  185 MET C CG    1 
ATOM   12499 S  SD    . MET C 2 206 ? 109.354 111.111 109.678 1.00 40.10 ?  185 MET C SD    1 
ATOM   12500 C  CE    . MET C 2 206 ? 110.471 109.760 109.360 1.00 35.10 ?  185 MET C CE    1 
ATOM   12501 N  N     . GLN C 2 207 ? 111.121 111.174 115.516 1.00 28.62 ?  186 GLN C N     1 
ATOM   12502 C  CA    . GLN C 2 207 ? 112.280 111.124 116.414 1.00 29.10 ?  186 GLN C CA    1 
ATOM   12503 C  C     . GLN C 2 207 ? 112.167 109.942 117.379 1.00 28.52 ?  186 GLN C C     1 
ATOM   12504 O  O     . GLN C 2 207 ? 113.118 109.174 117.521 1.00 28.28 ?  186 GLN C O     1 
ATOM   12505 C  CB    . GLN C 2 207 ? 112.474 112.442 117.170 1.00 29.21 ?  186 GLN C CB    1 
ATOM   12506 C  CG    . GLN C 2 207 ? 112.786 113.639 116.269 1.00 31.41 ?  186 GLN C CG    1 
ATOM   12507 C  CD    . GLN C 2 207 ? 114.112 113.496 115.550 1.00 34.70 ?  186 GLN C CD    1 
ATOM   12508 O  OE1   . GLN C 2 207 ? 114.170 112.987 114.435 1.00 37.69 ?  186 GLN C OE1   1 
ATOM   12509 N  NE2   . GLN C 2 207 ? 115.191 113.917 116.200 1.00 34.75 ?  186 GLN C NE2   1 
ATOM   12510 N  N     . SER C 2 208 ? 111.003 109.805 118.026 1.00 28.38 ?  187 SER C N     1 
ATOM   12511 C  CA    . SER C 2 208 ? 110.666 108.617 118.822 1.00 28.25 ?  187 SER C CA    1 
ATOM   12512 C  C     . SER C 2 208 ? 110.811 107.366 117.964 1.00 28.00 ?  187 SER C C     1 
ATOM   12513 O  O     . SER C 2 208 ? 111.332 106.350 118.425 1.00 27.90 ?  187 SER C O     1 
ATOM   12514 C  CB    . SER C 2 208 ? 109.221 108.687 119.320 1.00 27.88 ?  187 SER C CB    1 
ATOM   12515 O  OG    . SER C 2 208 ? 109.012 109.798 120.167 1.00 30.27 ?  187 SER C OG    1 
ATOM   12516 N  N     . GLY C 2 209 ? 110.332 107.456 116.719 1.00 27.31 ?  188 GLY C N     1 
ATOM   12517 C  CA    . GLY C 2 209 ? 110.413 106.358 115.757 1.00 27.86 ?  188 GLY C CA    1 
ATOM   12518 C  C     . GLY C 2 209 ? 111.836 105.951 115.424 1.00 27.96 ?  188 GLY C C     1 
ATOM   12519 O  O     . GLY C 2 209 ? 112.115 104.764 115.215 1.00 27.84 ?  188 GLY C O     1 
ATOM   12520 N  N     . GLU C 2 210 ? 112.735 106.934 115.369 1.00 28.21 ?  189 GLU C N     1 
ATOM   12521 C  CA    . GLU C 2 210 ? 114.153 106.675 115.140 1.00 29.15 ?  189 GLU C CA    1 
ATOM   12522 C  C     . GLU C 2 210 ? 114.753 105.853 116.299 1.00 28.02 ?  189 GLU C C     1 
ATOM   12523 O  O     . GLU C 2 210 ? 115.512 104.906 116.081 1.00 27.15 ?  189 GLU C O     1 
ATOM   12524 C  CB    . GLU C 2 210 ? 114.906 107.995 114.960 1.00 30.17 ?  189 GLU C CB    1 
ATOM   12525 C  CG    . GLU C 2 210 ? 115.797 108.045 113.728 1.00 35.68 ?  189 GLU C CG    1 
ATOM   12526 C  CD    . GLU C 2 210 ? 115.015 108.301 112.436 1.00 40.25 ?  189 GLU C CD    1 
ATOM   12527 O  OE1   . GLU C 2 210 ? 114.377 109.371 112.295 1.00 42.98 ?  189 GLU C OE1   1 
ATOM   12528 O  OE2   . GLU C 2 210 ? 115.047 107.429 111.546 1.00 43.59 -1 189 GLU C OE2   1 
ATOM   12529 N  N     . ILE C 2 211 ? 114.404 106.222 117.529 1.00 27.57 ?  190 ILE C N     1 
ATOM   12530 C  CA    . ILE C 2 211 ? 114.807 105.452 118.711 1.00 27.47 ?  190 ILE C CA    1 
ATOM   12531 C  C     . ILE C 2 211 ? 114.317 104.002 118.625 1.00 26.69 ?  190 ILE C C     1 
ATOM   12532 O  O     . ILE C 2 211 ? 115.092 103.051 118.792 1.00 26.56 ?  190 ILE C O     1 
ATOM   12533 C  CB    . ILE C 2 211 ? 114.321 106.137 120.023 1.00 27.84 ?  190 ILE C CB    1 
ATOM   12534 C  CG1   . ILE C 2 211 ? 115.131 107.421 120.268 1.00 28.56 ?  190 ILE C CG1   1 
ATOM   12535 C  CG2   . ILE C 2 211 ? 114.413 105.160 121.218 1.00 27.27 ?  190 ILE C CG2   1 
ATOM   12536 C  CD1   . ILE C 2 211 ? 114.779 108.155 121.557 1.00 30.09 ?  190 ILE C CD1   1 
ATOM   12537 N  N     . ILE C 2 212 ? 113.034 103.843 118.322 1.00 26.33 ?  191 ILE C N     1 
ATOM   12538 C  CA    . ILE C 2 212 ? 112.414 102.526 118.215 1.00 25.96 ?  191 ILE C CA    1 
ATOM   12539 C  C     . ILE C 2 212 ? 113.080 101.655 117.141 1.00 25.46 ?  191 ILE C C     1 
ATOM   12540 O  O     . ILE C 2 212 ? 113.287 100.464 117.363 1.00 24.84 ?  191 ILE C O     1 
ATOM   12541 C  CB    . ILE C 2 212 ? 110.874 102.640 117.993 1.00 26.00 ?  191 ILE C CB    1 
ATOM   12542 C  CG1   . ILE C 2 212 ? 110.197 103.268 119.222 1.00 27.16 ?  191 ILE C CG1   1 
ATOM   12543 C  CG2   . ILE C 2 212 ? 110.245 101.292 117.669 1.00 26.87 ?  191 ILE C CG2   1 
ATOM   12544 C  CD1   . ILE C 2 212 ? 110.303 102.455 120.499 1.00 29.84 ?  191 ILE C CD1   1 
ATOM   12545 N  N     . ASN C 2 213 ? 113.416 102.247 115.992 1.00 25.35 ?  192 ASN C N     1 
ATOM   12546 C  CA    . ASN C 2 213 ? 114.124 101.524 114.930 1.00 25.60 ?  192 ASN C CA    1 
ATOM   12547 C  C     . ASN C 2 213 ? 115.503 101.041 115.366 1.00 25.14 ?  192 ASN C C     1 
ATOM   12548 O  O     . ASN C 2 213 ? 115.946 99.946  114.984 1.00 25.61 ?  192 ASN C O     1 
ATOM   12549 C  CB    . ASN C 2 213 ? 114.252 102.373 113.658 1.00 26.55 ?  192 ASN C CB    1 
ATOM   12550 C  CG    . ASN C 2 213 ? 113.048 102.244 112.751 1.00 28.10 ?  192 ASN C CG    1 
ATOM   12551 O  OD1   . ASN C 2 213 ? 112.747 101.161 112.238 1.00 31.67 ?  192 ASN C OD1   1 
ATOM   12552 N  ND2   . ASN C 2 213 ? 112.356 103.349 112.537 1.00 30.36 ?  192 ASN C ND2   1 
ATOM   12553 N  N     . LEU C 2 214 ? 116.182 101.852 116.168 1.00 24.54 ?  193 LEU C N     1 
ATOM   12554 C  CA    . LEU C 2 214 ? 117.473 101.445 116.729 1.00 24.40 ?  193 LEU C CA    1 
ATOM   12555 C  C     . LEU C 2 214 ? 117.306 100.280 117.705 1.00 23.55 ?  193 LEU C C     1 
ATOM   12556 O  O     . LEU C 2 214 ? 118.070 99.312  117.654 1.00 23.09 ?  193 LEU C O     1 
ATOM   12557 C  CB    . LEU C 2 214 ? 118.193 102.631 117.366 1.00 24.00 ?  193 LEU C CB    1 
ATOM   12558 C  CG    . LEU C 2 214 ? 118.760 103.675 116.379 1.00 25.69 ?  193 LEU C CG    1 
ATOM   12559 C  CD1   . LEU C 2 214 ? 119.196 104.952 117.098 1.00 26.28 ?  193 LEU C CD1   1 
ATOM   12560 C  CD2   . LEU C 2 214 ? 119.932 103.116 115.569 1.00 26.05 ?  193 LEU C CD2   1 
ATOM   12561 N  N     . ILE C 2 215 ? 116.300 100.370 118.580 1.00 23.19 ?  194 ILE C N     1 
ATOM   12562 C  CA    . ILE C 2 215 ? 115.948 99.269  119.484 1.00 22.88 ?  194 ILE C CA    1 
ATOM   12563 C  C     . ILE C 2 215 ? 115.635 98.007  118.665 1.00 23.81 ?  194 ILE C C     1 
ATOM   12564 O  O     . ILE C 2 215 ? 116.157 96.930  118.956 1.00 23.83 ?  194 ILE C O     1 
ATOM   12565 C  CB    . ILE C 2 215 ? 114.754 99.633  120.412 1.00 22.92 ?  194 ILE C CB    1 
ATOM   12566 C  CG1   . ILE C 2 215 ? 115.104 100.833 121.295 1.00 21.11 ?  194 ILE C CG1   1 
ATOM   12567 C  CG2   . ILE C 2 215 ? 114.318 98.436  121.271 1.00 21.89 ?  194 ILE C CG2   1 
ATOM   12568 C  CD1   . ILE C 2 215 ? 113.986 101.275 122.217 1.00 22.26 ?  194 ILE C CD1   1 
ATOM   12569 N  N     . LEU C 2 216 ? 114.823 98.146  117.617 1.00 24.23 ?  195 LEU C N     1 
ATOM   12570 C  CA    . LEU C 2 216 ? 114.421 96.993  116.803 1.00 25.41 ?  195 LEU C CA    1 
ATOM   12571 C  C     . LEU C 2 216 ? 115.615 96.351  116.093 1.00 25.63 ?  195 LEU C C     1 
ATOM   12572 O  O     . LEU C 2 216 ? 115.731 95.117  116.048 1.00 25.46 ?  195 LEU C O     1 
ATOM   12573 C  CB    . LEU C 2 216 ? 113.329 97.390  115.792 1.00 26.03 ?  195 LEU C CB    1 
ATOM   12574 C  CG    . LEU C 2 216 ? 112.707 96.340  114.860 1.00 28.00 ?  195 LEU C CG    1 
ATOM   12575 C  CD1   . LEU C 2 216 ? 111.356 96.846  114.381 1.00 31.45 ?  195 LEU C CD1   1 
ATOM   12576 C  CD2   . LEU C 2 216 ? 113.611 96.005  113.668 1.00 29.83 ?  195 LEU C CD2   1 
ATOM   12577 N  N     . ARG C 2 217 ? 116.496 97.187  115.552 1.00 25.98 ?  196 ARG C N     1 
ATOM   12578 C  CA    . ARG C 2 217 ? 117.733 96.725  114.932 1.00 26.73 ?  196 ARG C CA    1 
ATOM   12579 C  C     . ARG C 2 217 ? 118.559 95.865  115.921 1.00 25.95 ?  196 ARG C C     1 
ATOM   12580 O  O     . ARG C 2 217 ? 119.062 94.804  115.534 1.00 25.75 ?  196 ARG C O     1 
ATOM   12581 C  CB    . ARG C 2 217 ? 118.546 97.921  114.430 1.00 27.29 ?  196 ARG C CB    1 
ATOM   12582 C  CG    . ARG C 2 217 ? 119.732 97.581  113.518 1.00 30.12 ?  196 ARG C CG    1 
ATOM   12583 C  CD    . ARG C 2 217 ? 120.827 98.616  113.702 1.00 35.40 ?  196 ARG C CD    1 
ATOM   12584 N  NE    . ARG C 2 217 ? 121.001 98.859  115.134 1.00 39.87 ?  196 ARG C NE    1 
ATOM   12585 C  CZ    . ARG C 2 217 ? 121.696 99.850  115.679 1.00 40.55 ?  196 ARG C CZ    1 
ATOM   12586 N  NH1   . ARG C 2 217 ? 122.332 100.743 114.921 1.00 40.77 1  196 ARG C NH1   1 
ATOM   12587 N  NH2   . ARG C 2 217 ? 121.745 99.939  117.003 1.00 41.10 ?  196 ARG C NH2   1 
ATOM   12588 N  N     . ASP C 2 218 ? 118.676 96.317  117.175 1.00 24.70 ?  197 ASP C N     1 
ATOM   12589 C  CA    . ASP C 2 218 ? 119.337 95.540  118.242 1.00 24.55 ?  197 ASP C CA    1 
ATOM   12590 C  C     . ASP C 2 218 ? 118.616 94.205  118.516 1.00 24.23 ?  197 ASP C C     1 
ATOM   12591 O  O     . ASP C 2 218 ? 119.255 93.149  118.528 1.00 23.69 ?  197 ASP C O     1 
ATOM   12592 C  CB    . ASP C 2 218 ? 119.453 96.326  119.565 1.00 24.50 ?  197 ASP C CB    1 
ATOM   12593 C  CG    . ASP C 2 218 ? 120.394 97.541  119.485 1.00 25.84 ?  197 ASP C CG    1 
ATOM   12594 O  OD1   . ASP C 2 218 ? 121.310 97.586  118.634 1.00 26.91 ?  197 ASP C OD1   1 
ATOM   12595 O  OD2   . ASP C 2 218 ? 120.223 98.460  120.310 1.00 25.72 -1 197 ASP C OD2   1 
ATOM   12596 N  N     . GLU C 2 219 ? 117.293 94.244  118.708 1.00 23.92 ?  198 GLU C N     1 
ATOM   12597 C  CA    . GLU C 2 219 ? 116.571 93.016  119.082 1.00 24.20 ?  198 GLU C CA    1 
ATOM   12598 C  C     . GLU C 2 219 ? 116.663 91.959  117.997 1.00 24.02 ?  198 GLU C C     1 
ATOM   12599 O  O     . GLU C 2 219 ? 116.730 90.776  118.311 1.00 24.24 ?  198 GLU C O     1 
ATOM   12600 C  CB    . GLU C 2 219 ? 115.099 93.255  119.433 1.00 24.05 ?  198 GLU C CB    1 
ATOM   12601 C  CG    . GLU C 2 219 ? 114.775 94.507  120.227 1.00 25.03 ?  198 GLU C CG    1 
ATOM   12602 C  CD    . GLU C 2 219 ? 115.220 94.515  121.702 1.00 26.31 ?  198 GLU C CD    1 
ATOM   12603 O  OE1   . GLU C 2 219 ? 116.176 93.796  122.117 1.00 27.65 ?  198 GLU C OE1   1 
ATOM   12604 O  OE2   . GLU C 2 219 ? 114.593 95.307  122.459 1.00 26.87 -1 198 GLU C OE2   1 
ATOM   12605 N  N     . ALA C 2 220 ? 116.664 92.381  116.731 1.00 24.00 ?  199 ALA C N     1 
ATOM   12606 C  CA    . ALA C 2 220 ? 116.797 91.445  115.620 1.00 24.72 ?  199 ALA C CA    1 
ATOM   12607 C  C     . ALA C 2 220 ? 118.088 90.616  115.717 1.00 24.80 ?  199 ALA C C     1 
ATOM   12608 O  O     . ALA C 2 220 ? 118.054 89.394  115.543 1.00 25.04 ?  199 ALA C O     1 
ATOM   12609 C  CB    . ALA C 2 220 ? 116.705 92.173  114.255 1.00 24.66 ?  199 ALA C CB    1 
ATOM   12610 N  N     . ILE C 2 221 ? 119.211 91.272  116.001 1.00 24.85 ?  200 ILE C N     1 
ATOM   12611 C  CA    . ILE C 2 221 ? 120.488 90.554  116.164 1.00 25.07 ?  200 ILE C CA    1 
ATOM   12612 C  C     . ILE C 2 221 ? 120.554 89.768  117.482 1.00 23.86 ?  200 ILE C C     1 
ATOM   12613 O  O     . ILE C 2 221 ? 121.163 88.695  117.526 1.00 23.72 ?  200 ILE C O     1 
ATOM   12614 C  CB    . ILE C 2 221 ? 121.759 91.457  115.964 1.00 25.71 ?  200 ILE C CB    1 
ATOM   12615 C  CG1   . ILE C 2 221 ? 121.978 92.401  117.150 1.00 27.10 ?  200 ILE C CG1   1 
ATOM   12616 C  CG2   . ILE C 2 221 ? 121.695 92.201  114.616 1.00 27.18 ?  200 ILE C CG2   1 
ATOM   12617 C  CD1   . ILE C 2 221 ? 123.299 93.179  117.125 1.00 29.63 ?  200 ILE C CD1   1 
ATOM   12618 N  N     . HIS C 2 222 ? 119.919 90.286  118.534 1.00 22.79 ?  201 HIS C N     1 
ATOM   12619 C  CA    . HIS C 2 222 ? 119.818 89.552  119.816 1.00 22.48 ?  201 HIS C CA    1 
ATOM   12620 C  C     . HIS C 2 222 ? 119.053 88.241  119.647 1.00 22.04 ?  201 HIS C C     1 
ATOM   12621 O  O     . HIS C 2 222 ? 119.458 87.220  120.188 1.00 22.06 ?  201 HIS C O     1 
ATOM   12622 C  CB    . HIS C 2 222 ? 119.089 90.362  120.889 1.00 21.77 ?  201 HIS C CB    1 
ATOM   12623 C  CG    . HIS C 2 222 ? 119.803 91.596  121.331 1.00 21.76 ?  201 HIS C CG    1 
ATOM   12624 N  ND1   . HIS C 2 222 ? 119.337 92.382  122.361 1.00 20.70 ?  201 HIS C ND1   1 
ATOM   12625 C  CD2   . HIS C 2 222 ? 120.942 92.181  120.897 1.00 22.07 ?  201 HIS C CD2   1 
ATOM   12626 C  CE1   . HIS C 2 222 ? 120.153 93.404  122.537 1.00 22.26 ?  201 HIS C CE1   1 
ATOM   12627 N  NE2   . HIS C 2 222 ? 121.130 93.310  121.656 1.00 22.52 ?  201 HIS C NE2   1 
ATOM   12628 N  N     . GLY C 2 223 ? 117.929 88.292  118.930 1.00 22.35 ?  202 GLY C N     1 
ATOM   12629 C  CA    . GLY C 2 223 ? 117.111 87.101  118.644 1.00 22.01 ?  202 GLY C CA    1 
ATOM   12630 C  C     . GLY C 2 223 ? 117.836 86.056  117.801 1.00 22.73 ?  202 GLY C C     1 
ATOM   12631 O  O     . GLY C 2 223 ? 117.716 84.845  118.052 1.00 21.99 ?  202 GLY C O     1 
ATOM   12632 N  N     . VAL C 2 224 ? 118.598 86.513  116.804 1.00 22.45 ?  203 VAL C N     1 
ATOM   12633 C  CA    . VAL C 2 224 ? 119.399 85.599  115.987 1.00 22.54 ?  203 VAL C CA    1 
ATOM   12634 C  C     . VAL C 2 224 ? 120.475 84.918  116.835 1.00 22.28 ?  203 VAL C C     1 
ATOM   12635 O  O     . VAL C 2 224 ? 120.599 83.695  116.817 1.00 22.44 ?  203 VAL C O     1 
ATOM   12636 C  CB    . VAL C 2 224 ? 120.049 86.305  114.749 1.00 23.00 ?  203 VAL C CB    1 
ATOM   12637 C  CG1   . VAL C 2 224 ? 121.049 85.364  114.053 1.00 23.10 ?  203 VAL C CG1   1 
ATOM   12638 C  CG2   . VAL C 2 224 ? 118.966 86.769  113.739 1.00 23.14 ?  203 VAL C CG2   1 
ATOM   12639 N  N     . TYR C 2 225 ? 121.222 85.711  117.600 1.00 22.41 ?  204 TYR C N     1 
ATOM   12640 C  CA    . TYR C 2 225 ? 122.310 85.184  118.424 1.00 22.03 ?  204 TYR C CA    1 
ATOM   12641 C  C     . TYR C 2 225 ? 121.835 84.146  119.440 1.00 21.66 ?  204 TYR C C     1 
ATOM   12642 O  O     . TYR C 2 225 ? 122.364 83.027  119.482 1.00 21.72 ?  204 TYR C O     1 
ATOM   12643 C  CB    . TYR C 2 225 ? 123.085 86.310  119.126 1.00 22.22 ?  204 TYR C CB    1 
ATOM   12644 C  CG    . TYR C 2 225 ? 124.347 85.814  119.803 1.00 21.92 ?  204 TYR C CG    1 
ATOM   12645 C  CD1   . TYR C 2 225 ? 125.431 85.360  119.050 1.00 22.36 ?  204 TYR C CD1   1 
ATOM   12646 C  CD2   . TYR C 2 225 ? 124.451 85.791  121.195 1.00 21.43 ?  204 TYR C CD2   1 
ATOM   12647 C  CE1   . TYR C 2 225 ? 126.587 84.886  119.667 1.00 23.82 ?  204 TYR C CE1   1 
ATOM   12648 C  CE2   . TYR C 2 225 ? 125.608 85.327  121.829 1.00 21.49 ?  204 TYR C CE2   1 
ATOM   12649 C  CZ    . TYR C 2 225 ? 126.665 84.880  121.059 1.00 23.58 ?  204 TYR C CZ    1 
ATOM   12650 O  OH    . TYR C 2 225 ? 127.799 84.425  121.678 1.00 25.42 ?  204 TYR C OH    1 
ATOM   12651 N  N     . VAL C 2 226 ? 120.837 84.508  120.250 1.00 20.95 ?  205 VAL C N     1 
ATOM   12652 C  CA    . VAL C 2 226 ? 120.275 83.565  121.225 1.00 20.49 ?  205 VAL C CA    1 
ATOM   12653 C  C     . VAL C 2 226 ? 119.686 82.330  120.518 1.00 20.84 ?  205 VAL C C     1 
ATOM   12654 O  O     . VAL C 2 226 ? 119.855 81.195  120.985 1.00 21.10 ?  205 VAL C O     1 
ATOM   12655 C  CB    . VAL C 2 226 ? 119.263 84.241  122.191 1.00 20.57 ?  205 VAL C CB    1 
ATOM   12656 C  CG1   . VAL C 2 226 ? 118.672 83.214  123.157 1.00 20.35 ?  205 VAL C CG1   1 
ATOM   12657 C  CG2   . VAL C 2 226 ? 119.964 85.359  122.977 1.00 19.60 ?  205 VAL C CG2   1 
ATOM   12658 N  N     . GLY C 2 227 ? 119.047 82.547  119.373 1.00 21.08 ?  206 GLY C N     1 
ATOM   12659 C  CA    . GLY C 2 227 ? 118.578 81.434  118.533 1.00 21.43 ?  206 GLY C CA    1 
ATOM   12660 C  C     . GLY C 2 227 ? 119.670 80.441  118.157 1.00 21.95 ?  206 GLY C C     1 
ATOM   12661 O  O     . GLY C 2 227 ? 119.463 79.216  118.218 1.00 21.84 ?  206 GLY C O     1 
ATOM   12662 N  N     . LEU C 2 228 ? 120.838 80.955  117.773 1.00 22.09 ?  207 LEU C N     1 
ATOM   12663 C  CA    . LEU C 2 228 ? 121.967 80.084  117.430 1.00 22.96 ?  207 LEU C CA    1 
ATOM   12664 C  C     . LEU C 2 228 ? 122.466 79.275  118.636 1.00 22.60 ?  207 LEU C C     1 
ATOM   12665 O  O     . LEU C 2 228 ? 122.797 78.093  118.502 1.00 22.04 ?  207 LEU C O     1 
ATOM   12666 C  CB    . LEU C 2 228 ? 123.106 80.872  116.770 1.00 23.39 ?  207 LEU C CB    1 
ATOM   12667 C  CG    . LEU C 2 228 ? 122.838 81.489  115.385 1.00 24.35 ?  207 LEU C CG    1 
ATOM   12668 C  CD1   . LEU C 2 228 ? 123.886 82.568  115.080 1.00 25.01 ?  207 LEU C CD1   1 
ATOM   12669 C  CD2   . LEU C 2 228 ? 122.818 80.442  114.276 1.00 25.11 ?  207 LEU C CD2   1 
ATOM   12670 N  N     . LEU C 2 229 ? 122.492 79.895  119.814 1.00 22.37 ?  208 LEU C N     1 
ATOM   12671 C  CA    . LEU C 2 229 ? 122.861 79.173  121.046 1.00 22.62 ?  208 LEU C CA    1 
ATOM   12672 C  C     . LEU C 2 229 ? 121.856 78.073  121.404 1.00 22.77 ?  208 LEU C C     1 
ATOM   12673 O  O     . LEU C 2 229 ? 122.246 76.964  121.808 1.00 22.57 ?  208 LEU C O     1 
ATOM   12674 C  CB    . LEU C 2 229 ? 123.063 80.139  122.219 1.00 22.44 ?  208 LEU C CB    1 
ATOM   12675 C  CG    . LEU C 2 229 ? 124.114 81.239  122.010 1.00 23.54 ?  208 LEU C CG    1 
ATOM   12676 C  CD1   . LEU C 2 229 ? 124.143 82.187  123.207 1.00 23.37 ?  208 LEU C CD1   1 
ATOM   12677 C  CD2   . LEU C 2 229 ? 125.511 80.648  121.747 1.00 23.91 ?  208 LEU C CD2   1 
ATOM   12678 N  N     . ALA C 2 230 ? 120.568 78.377  121.243 1.00 22.42 ?  209 ALA C N     1 
ATOM   12679 C  CA    . ALA C 2 230 ? 119.509 77.394  121.462 1.00 22.02 ?  209 ALA C CA    1 
ATOM   12680 C  C     . ALA C 2 230 ? 119.652 76.198  120.514 1.00 22.58 ?  209 ALA C C     1 
ATOM   12681 O  O     . ALA C 2 230 ? 119.553 75.055  120.941 1.00 22.14 ?  209 ALA C O     1 
ATOM   12682 C  CB    . ALA C 2 230 ? 118.149 78.033  121.300 1.00 22.04 ?  209 ALA C CB    1 
ATOM   12683 N  N     . GLN C 2 231 ? 119.904 76.476  119.237 1.00 22.96 ?  210 GLN C N     1 
ATOM   12684 C  CA    . GLN C 2 231 ? 120.121 75.409  118.243 1.00 24.30 ?  210 GLN C CA    1 
ATOM   12685 C  C     . GLN C 2 231 ? 121.299 74.512  118.577 1.00 25.11 ?  210 GLN C C     1 
ATOM   12686 O  O     . GLN C 2 231 ? 121.255 73.306  118.312 1.00 24.97 ?  210 GLN C O     1 
ATOM   12687 C  CB    . GLN C 2 231 ? 120.298 75.996  116.847 1.00 24.38 ?  210 GLN C CB    1 
ATOM   12688 C  CG    . GLN C 2 231 ? 119.011 76.631  116.295 1.00 25.12 ?  210 GLN C CG    1 
ATOM   12689 C  CD    . GLN C 2 231 ? 119.202 77.208  114.909 1.00 28.08 ?  210 GLN C CD    1 
ATOM   12690 O  OE1   . GLN C 2 231 ? 119.637 76.508  113.993 1.00 27.83 ?  210 GLN C OE1   1 
ATOM   12691 N  NE2   . GLN C 2 231 ? 118.895 78.496  114.748 1.00 26.38 ?  210 GLN C NE2   1 
ATOM   12692 N  N     . GLU C 2 232 ? 122.353 75.095  119.153 1.00 25.80 ?  211 GLU C N     1 
ATOM   12693 C  CA    . GLU C 2 232 ? 123.503 74.308  119.609 1.00 27.16 ?  211 GLU C CA    1 
ATOM   12694 C  C     . GLU C 2 232 ? 123.073 73.224  120.593 1.00 26.47 ?  211 GLU C C     1 
ATOM   12695 O  O     . GLU C 2 232 ? 123.503 72.070  120.489 1.00 26.10 ?  211 GLU C O     1 
ATOM   12696 C  CB    . GLU C 2 232 ? 124.529 75.192  120.305 1.00 27.59 ?  211 GLU C CB    1 
ATOM   12697 C  CG    . GLU C 2 232 ? 125.584 75.762  119.405 1.00 32.55 ?  211 GLU C CG    1 
ATOM   12698 C  CD    . GLU C 2 232 ? 126.918 75.931  120.120 1.00 36.72 ?  211 GLU C CD    1 
ATOM   12699 O  OE1   . GLU C 2 232 ? 126.991 75.690  121.349 1.00 38.32 ?  211 GLU C OE1   1 
ATOM   12700 O  OE2   . GLU C 2 232 ? 127.898 76.301  119.443 1.00 40.62 -1 211 GLU C OE2   1 
ATOM   12701 N  N     . ILE C 2 233 ? 122.237 73.609  121.557 1.00 25.55 ?  212 ILE C N     1 
ATOM   12702 C  CA    . ILE C 2 233 ? 121.776 72.677  122.586 1.00 25.32 ?  212 ILE C CA    1 
ATOM   12703 C  C     . ILE C 2 233 ? 120.822 71.640  122.008 1.00 25.48 ?  212 ILE C C     1 
ATOM   12704 O  O     . ILE C 2 233 ? 120.983 70.440  122.244 1.00 25.82 ?  212 ILE C O     1 
ATOM   12705 C  CB    . ILE C 2 233 ? 121.129 73.409  123.782 1.00 25.39 ?  212 ILE C CB    1 
ATOM   12706 C  CG1   . ILE C 2 233 ? 122.194 74.221  124.524 1.00 24.37 ?  212 ILE C CG1   1 
ATOM   12707 C  CG2   . ILE C 2 233 ? 120.438 72.409  124.715 1.00 24.86 ?  212 ILE C CG2   1 
ATOM   12708 C  CD1   . ILE C 2 233 ? 121.619 75.285  125.446 1.00 25.10 ?  212 ILE C CD1   1 
ATOM   12709 N  N     . TYR C 2 234 ? 119.848 72.105  121.230 1.00 25.27 ?  213 TYR C N     1 
ATOM   12710 C  CA    . TYR C 2 234 ? 118.912 71.230  120.520 1.00 25.77 ?  213 TYR C CA    1 
ATOM   12711 C  C     . TYR C 2 234 ? 119.636 70.167  119.674 1.00 26.44 ?  213 TYR C C     1 
ATOM   12712 O  O     . TYR C 2 234 ? 119.243 68.998  119.659 1.00 26.29 ?  213 TYR C O     1 
ATOM   12713 C  CB    . TYR C 2 234 ? 117.991 72.088  119.638 1.00 25.67 ?  213 TYR C CB    1 
ATOM   12714 C  CG    . TYR C 2 234 ? 116.988 71.351  118.774 1.00 25.65 ?  213 TYR C CG    1 
ATOM   12715 C  CD1   . TYR C 2 234 ? 115.694 71.099  119.237 1.00 25.02 ?  213 TYR C CD1   1 
ATOM   12716 C  CD2   . TYR C 2 234 ? 117.316 70.956  117.467 1.00 26.59 ?  213 TYR C CD2   1 
ATOM   12717 C  CE1   . TYR C 2 234 ? 114.760 70.448  118.439 1.00 26.52 ?  213 TYR C CE1   1 
ATOM   12718 C  CE2   . TYR C 2 234 ? 116.389 70.296  116.659 1.00 27.00 ?  213 TYR C CE2   1 
ATOM   12719 C  CZ    . TYR C 2 234 ? 115.117 70.045  117.156 1.00 27.79 ?  213 TYR C CZ    1 
ATOM   12720 O  OH    . TYR C 2 234 ? 114.196 69.414  116.367 1.00 29.00 ?  213 TYR C OH    1 
ATOM   12721 N  N     . ASN C 2 235 ? 120.691 70.572  118.971 1.00 26.96 ?  214 ASN C N     1 
ATOM   12722 C  CA    . ASN C 2 235 ? 121.399 69.651  118.084 1.00 28.05 ?  214 ASN C CA    1 
ATOM   12723 C  C     . ASN C 2 235 ? 122.173 68.545  118.794 1.00 28.24 ?  214 ASN C C     1 
ATOM   12724 O  O     . ASN C 2 235 ? 122.558 67.566  118.163 1.00 28.63 ?  214 ASN C O     1 
ATOM   12725 C  CB    . ASN C 2 235 ? 122.287 70.407  117.083 1.00 28.38 ?  214 ASN C CB    1 
ATOM   12726 C  CG    . ASN C 2 235 ? 121.472 71.213  116.076 1.00 31.14 ?  214 ASN C CG    1 
ATOM   12727 O  OD1   . ASN C 2 235 ? 120.362 70.826  115.699 1.00 34.16 ?  214 ASN C OD1   1 
ATOM   12728 N  ND2   . ASN C 2 235 ? 122.021 72.341  115.642 1.00 32.42 ?  214 ASN C ND2   1 
ATOM   12729 N  N     . LYS C 2 236 ? 122.376 68.692  120.103 1.00 27.91 ?  215 LYS C N     1 
ATOM   12730 C  CA    . LYS C 2 236 ? 123.026 67.664  120.919 1.00 28.49 ?  215 LYS C CA    1 
ATOM   12731 C  C     . LYS C 2 236 ? 122.088 66.521  121.323 1.00 28.50 ?  215 LYS C C     1 
ATOM   12732 O  O     . LYS C 2 236 ? 122.541 65.477  121.799 1.00 28.98 ?  215 LYS C O     1 
ATOM   12733 C  CB    . LYS C 2 236 ? 123.637 68.282  122.181 1.00 28.10 ?  215 LYS C CB    1 
ATOM   12734 C  CG    . LYS C 2 236 ? 124.764 69.270  121.913 1.00 29.25 ?  215 LYS C CG    1 
ATOM   12735 C  CD    . LYS C 2 236 ? 125.336 69.826  123.207 1.00 30.19 ?  215 LYS C CD    1 
ATOM   12736 C  CE    . LYS C 2 236 ? 126.220 71.015  122.912 1.00 32.63 ?  215 LYS C CE    1 
ATOM   12737 N  NZ    . LYS C 2 236 ? 126.789 71.589  124.153 1.00 35.39 1  215 LYS C NZ    1 
ATOM   12738 N  N     . GLN C 2 237 ? 120.788 66.704  121.119 1.00 28.25 ?  216 GLN C N     1 
ATOM   12739 C  CA    . GLN C 2 237 ? 119.806 65.764  121.661 1.00 28.34 ?  216 GLN C CA    1 
ATOM   12740 C  C     . GLN C 2 237 ? 119.524 64.557  120.751 1.00 28.92 ?  216 GLN C C     1 
ATOM   12741 O  O     . GLN C 2 237 ? 119.789 64.599  119.549 1.00 28.53 ?  216 GLN C O     1 
ATOM   12742 C  CB    . GLN C 2 237 ? 118.510 66.510  122.014 1.00 27.68 ?  216 GLN C CB    1 
ATOM   12743 C  CG    . GLN C 2 237 ? 118.718 67.773  122.884 1.00 26.67 ?  216 GLN C CG    1 
ATOM   12744 C  CD    . GLN C 2 237 ? 119.566 67.532  124.128 1.00 25.32 ?  216 GLN C CD    1 
ATOM   12745 O  OE1   . GLN C 2 237 ? 119.388 66.541  124.840 1.00 25.49 ?  216 GLN C OE1   1 
ATOM   12746 N  NE2   . GLN C 2 237 ? 120.495 68.446  124.399 1.00 23.63 ?  216 GLN C NE2   1 
ATOM   12747 N  N     . THR C 2 238 ? 118.983 63.489  121.337 1.00 29.53 ?  217 THR C N     1 
ATOM   12748 C  CA    . THR C 2 238 ? 118.431 62.376  120.558 1.00 30.73 ?  217 THR C CA    1 
ATOM   12749 C  C     . THR C 2 238 ? 117.223 62.874  119.756 1.00 31.13 ?  217 THR C C     1 
ATOM   12750 O  O     . THR C 2 238 ? 116.666 63.948  120.052 1.00 30.17 ?  217 THR C O     1 
ATOM   12751 C  CB    . THR C 2 238 ? 117.938 61.228  121.456 1.00 30.79 ?  217 THR C CB    1 
ATOM   12752 O  OG1   . THR C 2 238 ? 116.786 61.665  122.191 1.00 31.16 ?  217 THR C OG1   1 
ATOM   12753 C  CG2   . THR C 2 238 ? 119.028 60.766  122.430 1.00 31.22 ?  217 THR C CG2   1 
ATOM   12754 N  N     . GLU C 2 239 ? 116.800 62.087  118.764 1.00 31.67 ?  218 GLU C N     1 
ATOM   12755 C  CA    . GLU C 2 239 ? 115.617 62.439  117.978 1.00 32.25 ?  218 GLU C CA    1 
ATOM   12756 C  C     . GLU C 2 239 ? 114.355 62.520  118.844 1.00 31.86 ?  218 GLU C C     1 
ATOM   12757 O  O     . GLU C 2 239 ? 113.516 63.404  118.653 1.00 31.09 ?  218 GLU C O     1 
ATOM   12758 C  CB    . GLU C 2 239 ? 115.434 61.476  116.792 1.00 33.29 ?  218 GLU C CB    1 
ATOM   12759 C  CG    . GLU C 2 239 ? 116.522 61.622  115.711 1.00 35.65 ?  218 GLU C CG    1 
ATOM   12760 C  CD    . GLU C 2 239 ? 116.589 63.034  115.116 1.00 39.17 ?  218 GLU C CD    1 
ATOM   12761 O  OE1   . GLU C 2 239 ? 115.519 63.600  114.775 1.00 41.08 ?  218 GLU C OE1   1 
ATOM   12762 O  OE2   . GLU C 2 239 ? 117.711 63.585  114.994 1.00 39.64 -1 218 GLU C OE2   1 
ATOM   12763 N  N     . GLU C 2 240 ? 114.254 61.615  119.819 1.00 31.72 ?  219 GLU C N     1 
ATOM   12764 C  CA    . GLU C 2 240 ? 113.139 61.587  120.756 1.00 31.76 ?  219 GLU C CA    1 
ATOM   12765 C  C     . GLU C 2 240 ? 113.093 62.864  121.608 1.00 30.21 ?  219 GLU C C     1 
ATOM   12766 O  O     . GLU C 2 240 ? 112.026 63.470  121.784 1.00 29.63 ?  219 GLU C O     1 
ATOM   12767 C  CB    . GLU C 2 240 ? 113.237 60.337  121.633 1.00 32.58 ?  219 GLU C CB    1 
ATOM   12768 C  CG    . GLU C 2 240 ? 112.015 60.062  122.494 1.00 36.93 ?  219 GLU C CG    1 
ATOM   12769 C  CD    . GLU C 2 240 ? 111.996 58.638  123.039 1.00 42.06 ?  219 GLU C CD    1 
ATOM   12770 O  OE1   . GLU C 2 240 ? 112.115 58.466  124.273 1.00 44.09 ?  219 GLU C OE1   1 
ATOM   12771 O  OE2   . GLU C 2 240 ? 111.870 57.688  122.232 1.00 44.45 -1 219 GLU C OE2   1 
ATOM   12772 N  N     . LYS C 2 241 ? 114.256 63.269  122.116 1.00 28.91 ?  220 LYS C N     1 
ATOM   12773 C  CA    . LYS C 2 241 ? 114.376 64.483  122.912 1.00 28.14 ?  220 LYS C CA    1 
ATOM   12774 C  C     . LYS C 2 241 ? 114.064 65.740  122.097 1.00 27.03 ?  220 LYS C C     1 
ATOM   12775 O  O     . LYS C 2 241 ? 113.385 66.647  122.589 1.00 26.72 ?  220 LYS C O     1 
ATOM   12776 C  CB    . LYS C 2 241 ? 115.766 64.591  123.548 1.00 27.83 ?  220 LYS C CB    1 
ATOM   12777 C  CG    . LYS C 2 241 ? 115.920 65.789  124.494 1.00 29.68 ?  220 LYS C CG    1 
ATOM   12778 C  CD    . LYS C 2 241 ? 115.732 65.400  125.954 1.00 33.58 ?  220 LYS C CD    1 
ATOM   12779 C  CE    . LYS C 2 241 ? 114.281 65.353  126.345 1.00 33.71 ?  220 LYS C CE    1 
ATOM   12780 N  NZ    . LYS C 2 241 ? 114.082 64.814  127.731 1.00 34.69 1  220 LYS C NZ    1 
ATOM   12781 N  N     . LYS C 2 242 ? 114.569 65.782  120.863 1.00 26.38 ?  221 LYS C N     1 
ATOM   12782 C  CA    . LYS C 2 242 ? 114.280 66.861  119.914 1.00 25.87 ?  221 LYS C CA    1 
ATOM   12783 C  C     . LYS C 2 242 ? 112.790 67.031  119.681 1.00 25.72 ?  221 LYS C C     1 
ATOM   12784 O  O     . LYS C 2 242 ? 112.285 68.162  119.671 1.00 24.52 ?  221 LYS C O     1 
ATOM   12785 C  CB    . LYS C 2 242 ? 114.970 66.621  118.570 1.00 25.83 ?  221 LYS C CB    1 
ATOM   12786 C  CG    . LYS C 2 242 ? 116.456 66.898  118.556 1.00 26.76 ?  221 LYS C CG    1 
ATOM   12787 C  CD    . LYS C 2 242 ? 116.996 66.753  117.138 1.00 28.40 ?  221 LYS C CD    1 
ATOM   12788 C  CE    . LYS C 2 242 ? 118.498 66.793  117.106 1.00 29.84 ?  221 LYS C CE    1 
ATOM   12789 N  NZ    . LYS C 2 242 ? 119.002 66.431  115.760 1.00 30.96 1  221 LYS C NZ    1 
ATOM   12790 N  N     . ALA C 2 243 ? 112.098 65.904  119.485 1.00 25.97 ?  222 ALA C N     1 
ATOM   12791 C  CA    . ALA C 2 243 ? 110.643 65.907  119.315 1.00 25.79 ?  222 ALA C CA    1 
ATOM   12792 C  C     . ALA C 2 243 ? 109.935 66.544  120.511 1.00 25.24 ?  222 ALA C C     1 
ATOM   12793 O  O     . ALA C 2 243 ? 108.985 67.321  120.332 1.00 25.37 ?  222 ALA C O     1 
ATOM   12794 C  CB    . ALA C 2 243 ? 110.124 64.492  119.052 1.00 26.17 ?  222 ALA C CB    1 
ATOM   12795 N  N     . GLU C 2 244 ? 110.406 66.250  121.721 1.00 25.02 ?  223 GLU C N     1 
ATOM   12796 C  CA    . GLU C 2 244 ? 109.858 66.880  122.933 1.00 25.08 ?  223 GLU C CA    1 
ATOM   12797 C  C     . GLU C 2 244 ? 110.161 68.387  123.002 1.00 24.70 ?  223 GLU C C     1 
ATOM   12798 O  O     . GLU C 2 244 ? 109.311 69.186  123.423 1.00 24.20 ?  223 GLU C O     1 
ATOM   12799 C  CB    . GLU C 2 244 ? 110.358 66.177  124.199 1.00 25.35 ?  223 GLU C CB    1 
ATOM   12800 C  CG    . GLU C 2 244 ? 109.765 66.763  125.492 1.00 26.67 ?  223 GLU C CG    1 
ATOM   12801 C  CD    . GLU C 2 244 ? 110.463 66.273  126.747 1.00 28.29 ?  223 GLU C CD    1 
ATOM   12802 O  OE1   . GLU C 2 244 ? 111.079 65.190  126.719 1.00 29.51 ?  223 GLU C OE1   1 
ATOM   12803 O  OE2   . GLU C 2 244 ? 110.396 66.979  127.769 1.00 29.09 -1 223 GLU C OE2   1 
ATOM   12804 N  N     . LEU C 2 245 ? 111.369 68.769  122.600 1.00 24.27 ?  224 LEU C N     1 
ATOM   12805 C  CA    . LEU C 2 245 ? 111.760 70.180  122.608 1.00 24.54 ?  224 LEU C CA    1 
ATOM   12806 C  C     . LEU C 2 245 ? 110.949 71.026  121.616 1.00 24.42 ?  224 LEU C C     1 
ATOM   12807 O  O     . LEU C 2 245 ? 110.596 72.169  121.917 1.00 24.10 ?  224 LEU C O     1 
ATOM   12808 C  CB    . LEU C 2 245 ? 113.277 70.334  122.392 1.00 23.86 ?  224 LEU C CB    1 
ATOM   12809 C  CG    . LEU C 2 245 ? 114.165 69.804  123.526 1.00 24.78 ?  224 LEU C CG    1 
ATOM   12810 C  CD1   . LEU C 2 245 ? 115.646 70.063  123.228 1.00 25.54 ?  224 LEU C CD1   1 
ATOM   12811 C  CD2   . LEU C 2 245 ? 113.786 70.397  124.890 1.00 25.29 ?  224 LEU C CD2   1 
ATOM   12812 N  N     . ARG C 2 246 ? 110.647 70.456  120.450 1.00 25.26 ?  225 ARG C N     1 
ATOM   12813 C  CA    . ARG C 2 246 ? 109.763 71.104  119.470 1.00 25.97 ?  225 ARG C CA    1 
ATOM   12814 C  C     . ARG C 2 246 ? 108.366 71.273  120.053 1.00 25.85 ?  225 ARG C C     1 
ATOM   12815 O  O     . ARG C 2 246 ? 107.751 72.328  119.890 1.00 25.01 ?  225 ARG C O     1 
ATOM   12816 C  CB    . ARG C 2 246 ? 109.705 70.321  118.141 1.00 26.65 ?  225 ARG C CB    1 
ATOM   12817 C  CG    . ARG C 2 246 ? 111.024 70.313  117.372 1.00 28.90 ?  225 ARG C CG    1 
ATOM   12818 C  CD    . ARG C 2 246 ? 110.871 69.880  115.893 1.00 31.26 ?  225 ARG C CD    1 
ATOM   12819 N  NE    . ARG C 2 246 ? 110.310 68.535  115.745 1.00 34.01 ?  225 ARG C NE    1 
ATOM   12820 C  CZ    . ARG C 2 246 ? 110.983 67.400  115.935 1.00 35.64 ?  225 ARG C CZ    1 
ATOM   12821 N  NH1   . ARG C 2 246 ? 112.262 67.420  116.290 1.00 36.11 1  225 ARG C NH1   1 
ATOM   12822 N  NH2   . ARG C 2 246 ? 110.369 66.234  115.769 1.00 37.05 ?  225 ARG C NH2   1 
ATOM   12823 N  N     . GLU C 2 247 ? 107.875 70.239  120.742 1.00 26.01 ?  226 GLU C N     1 
ATOM   12824 C  CA    . GLU C 2 247 ? 106.588 70.318  121.442 1.00 26.48 ?  226 GLU C CA    1 
ATOM   12825 C  C     . GLU C 2 247 ? 106.592 71.451  122.468 1.00 25.72 ?  226 GLU C C     1 
ATOM   12826 O  O     . GLU C 2 247 ? 105.649 72.254  122.519 1.00 25.16 ?  226 GLU C O     1 
ATOM   12827 C  CB    . GLU C 2 247 ? 106.242 69.002  122.145 1.00 27.18 ?  226 GLU C CB    1 
ATOM   12828 C  CG    . GLU C 2 247 ? 104.766 68.896  122.511 1.00 30.38 ?  226 GLU C CG    1 
ATOM   12829 C  CD    . GLU C 2 247 ? 104.499 68.194  123.830 1.00 35.77 ?  226 GLU C CD    1 
ATOM   12830 O  OE1   . GLU C 2 247 ? 105.289 67.321  124.246 1.00 38.02 ?  226 GLU C OE1   1 
ATOM   12831 O  OE2   . GLU C 2 247 ? 103.470 68.522  124.460 1.00 40.39 -1 226 GLU C OE2   1 
ATOM   12832 N  N     . PHE C 2 248 ? 107.653 71.513  123.275 1.00 24.71 ?  227 PHE C N     1 
ATOM   12833 C  CA    . PHE C 2 248 ? 107.800 72.589  124.254 1.00 23.71 ?  227 PHE C CA    1 
ATOM   12834 C  C     . PHE C 2 248 ? 107.732 73.953  123.562 1.00 23.14 ?  227 PHE C C     1 
ATOM   12835 O  O     . PHE C 2 248 ? 106.989 74.833  124.000 1.00 22.40 ?  227 PHE C O     1 
ATOM   12836 C  CB    . PHE C 2 248 ? 109.107 72.475  125.058 1.00 23.85 ?  227 PHE C CB    1 
ATOM   12837 C  CG    . PHE C 2 248 ? 109.450 73.734  125.813 1.00 23.64 ?  227 PHE C CG    1 
ATOM   12838 C  CD1   . PHE C 2 248 ? 108.863 73.994  127.054 1.00 23.07 ?  227 PHE C CD1   1 
ATOM   12839 C  CD2   . PHE C 2 248 ? 110.304 74.696  125.248 1.00 23.04 ?  227 PHE C CD2   1 
ATOM   12840 C  CE1   . PHE C 2 248 ? 109.151 75.168  127.750 1.00 22.73 ?  227 PHE C CE1   1 
ATOM   12841 C  CE2   . PHE C 2 248 ? 110.596 75.880  125.927 1.00 23.31 ?  227 PHE C CE2   1 
ATOM   12842 C  CZ    . PHE C 2 248 ? 110.021 76.119  127.186 1.00 21.51 ?  227 PHE C CZ    1 
ATOM   12843 N  N     . ALA C 2 249 ? 108.505 74.110  122.486 1.00 22.95 ?  228 ALA C N     1 
ATOM   12844 C  CA    . ALA C 2 249 ? 108.630 75.401  121.795 1.00 22.96 ?  228 ALA C CA    1 
ATOM   12845 C  C     . ALA C 2 249 ? 107.304 75.842  121.179 1.00 23.31 ?  228 ALA C C     1 
ATOM   12846 O  O     . ALA C 2 249 ? 106.920 77.009  121.279 1.00 22.63 ?  228 ALA C O     1 
ATOM   12847 C  CB    . ALA C 2 249 ? 109.720 75.337  120.728 1.00 22.40 ?  228 ALA C CB    1 
ATOM   12848 N  N     . ILE C 2 250 ? 106.615 74.898  120.547 1.00 23.66 ?  229 ILE C N     1 
ATOM   12849 C  CA    . ILE C 2 250 ? 105.332 75.174  119.901 1.00 25.00 ?  229 ILE C CA    1 
ATOM   12850 C  C     . ILE C 2 250 ? 104.211 75.409  120.923 1.00 24.64 ?  229 ILE C C     1 
ATOM   12851 O  O     . ILE C 2 250 ? 103.424 76.353  120.774 1.00 24.26 ?  229 ILE C O     1 
ATOM   12852 C  CB    . ILE C 2 250 ? 104.980 74.087  118.838 1.00 25.43 ?  229 ILE C CB    1 
ATOM   12853 C  CG1   . ILE C 2 250 ? 105.912 74.246  117.628 1.00 27.27 ?  229 ILE C CG1   1 
ATOM   12854 C  CG2   . ILE C 2 250 ? 103.512 74.240  118.352 1.00 27.62 ?  229 ILE C CG2   1 
ATOM   12855 C  CD1   . ILE C 2 250 ? 106.332 72.932  116.953 1.00 31.32 ?  229 ILE C CD1   1 
ATOM   12856 N  N     . ASP C 2 251 ? 104.156 74.587  121.971 1.00 24.78 ?  230 ASP C N     1 
ATOM   12857 C  CA    . ASP C 2 251 ? 103.198 74.817  123.068 1.00 25.20 ?  230 ASP C CA    1 
ATOM   12858 C  C     . ASP C 2 251 ? 103.399 76.181  123.728 1.00 24.08 ?  230 ASP C C     1 
ATOM   12859 O  O     . ASP C 2 251 ? 102.428 76.889  124.038 1.00 23.34 ?  230 ASP C O     1 
ATOM   12860 C  CB    . ASP C 2 251 ? 103.316 73.744  124.160 1.00 25.73 ?  230 ASP C CB    1 
ATOM   12861 C  CG    . ASP C 2 251 ? 102.701 72.423  123.761 1.00 28.78 ?  230 ASP C CG    1 
ATOM   12862 O  OD1   . ASP C 2 251 ? 102.077 72.333  122.678 1.00 29.99 ?  230 ASP C OD1   1 
ATOM   12863 O  OD2   . ASP C 2 251 ? 102.852 71.465  124.546 1.00 33.31 -1 230 ASP C OD2   1 
ATOM   12864 N  N     . LEU C 2 252 ? 104.660 76.541  123.956 1.00 22.98 ?  231 LEU C N     1 
ATOM   12865 C  CA    . LEU C 2 252 ? 104.968 77.829  124.579 1.00 21.63 ?  231 LEU C CA    1 
ATOM   12866 C  C     . LEU C 2 252 ? 104.571 78.974  123.653 1.00 21.66 ?  231 LEU C C     1 
ATOM   12867 O  O     . LEU C 2 252 ? 104.003 79.976  124.089 1.00 19.41 ?  231 LEU C O     1 
ATOM   12868 C  CB    . LEU C 2 252 ? 106.453 77.936  124.926 1.00 21.89 ?  231 LEU C CB    1 
ATOM   12869 C  CG    . LEU C 2 252 ? 106.946 79.274  125.508 1.00 21.33 ?  231 LEU C CG    1 
ATOM   12870 C  CD1   . LEU C 2 252 ? 106.196 79.649  126.803 1.00 20.89 ?  231 LEU C CD1   1 
ATOM   12871 C  CD2   . LEU C 2 252 ? 108.458 79.195  125.736 1.00 20.31 ?  231 LEU C CD2   1 
ATOM   12872 N  N     . LEU C 2 253 ? 104.885 78.820  122.370 1.00 22.28 ?  232 LEU C N     1 
ATOM   12873 C  CA    . LEU C 2 253 ? 104.552 79.858  121.400 1.00 23.05 ?  232 LEU C CA    1 
ATOM   12874 C  C     . LEU C 2 253 ? 103.045 80.088  121.350 1.00 23.36 ?  232 LEU C C     1 
ATOM   12875 O  O     . LEU C 2 253 ? 102.590 81.241  121.437 1.00 22.96 ?  232 LEU C O     1 
ATOM   12876 C  CB    . LEU C 2 253 ? 105.105 79.521  120.014 1.00 23.53 ?  232 LEU C CB    1 
ATOM   12877 C  CG    . LEU C 2 253 ? 104.797 80.580  118.948 1.00 25.63 ?  232 LEU C CG    1 
ATOM   12878 C  CD1   . LEU C 2 253 ? 105.474 81.914  119.263 1.00 25.88 ?  232 LEU C CD1   1 
ATOM   12879 C  CD2   . LEU C 2 253 ? 105.221 80.066  117.581 1.00 27.67 ?  232 LEU C CD2   1 
ATOM   12880 N  N     . ASN C 2 254 ? 102.280 78.999  121.228 1.00 23.55 ?  233 ASN C N     1 
ATOM   12881 C  CA    . ASN C 2 254 ? 100.808 79.082  121.229 1.00 24.61 ?  233 ASN C CA    1 
ATOM   12882 C  C     . ASN C 2 254 ? 100.230 79.722  122.494 1.00 23.57 ?  233 ASN C C     1 
ATOM   12883 O  O     . ASN C 2 254 ? 99.311  80.535  122.424 1.00 23.52 ?  233 ASN C O     1 
ATOM   12884 C  CB    . ASN C 2 254 ? 100.174 77.709  120.989 1.00 24.99 ?  233 ASN C CB    1 
ATOM   12885 C  CG    . ASN C 2 254 ? 100.067 77.365  119.509 1.00 28.92 ?  233 ASN C CG    1 
ATOM   12886 O  OD1   . ASN C 2 254 ? 99.455  78.094  118.725 1.00 33.75 ?  233 ASN C OD1   1 
ATOM   12887 N  ND2   . ASN C 2 254 ? 100.658 76.250  119.125 1.00 30.99 ?  233 ASN C ND2   1 
ATOM   12888 N  N     . GLN C 2 255 ? 100.775 79.358  123.651 1.00 23.22 ?  234 GLN C N     1 
ATOM   12889 C  CA    . GLN C 2 255 ? 100.323 79.945  124.905 1.00 22.54 ?  234 GLN C CA    1 
ATOM   12890 C  C     . GLN C 2 255 ? 100.603 81.461  124.957 1.00 22.00 ?  234 GLN C C     1 
ATOM   12891 O  O     . GLN C 2 255 ? 99.737  82.257  125.358 1.00 21.73 ?  234 GLN C O     1 
ATOM   12892 C  CB    . GLN C 2 255 ? 100.965 79.229  126.092 1.00 22.85 ?  234 GLN C CB    1 
ATOM   12893 C  CG    . GLN C 2 255 ? 100.321 79.571  127.419 1.00 23.87 ?  234 GLN C CG    1 
ATOM   12894 C  CD    . GLN C 2 255 ? 100.986 78.879  128.604 1.00 24.95 ?  234 GLN C CD    1 
ATOM   12895 O  OE1   . GLN C 2 255 ? 101.836 77.998  128.433 1.00 24.21 ?  234 GLN C OE1   1 
ATOM   12896 N  NE2   . GLN C 2 255 ? 100.616 79.299  129.815 1.00 25.97 ?  234 GLN C NE2   1 
ATOM   12897 N  N     . LEU C 2 256 ? 101.807 81.852  124.554 1.00 21.27 ?  235 LEU C N     1 
ATOM   12898 C  CA    . LEU C 2 256 ? 102.169 83.265  124.490 1.00 21.37 ?  235 LEU C CA    1 
ATOM   12899 C  C     . LEU C 2 256 ? 101.327 83.998  123.442 1.00 21.21 ?  235 LEU C C     1 
ATOM   12900 O  O     . LEU C 2 256 ? 100.895 85.130  123.657 1.00 20.75 ?  235 LEU C O     1 
ATOM   12901 C  CB    . LEU C 2 256 ? 103.660 83.411  124.159 1.00 20.93 ?  235 LEU C CB    1 
ATOM   12902 C  CG    . LEU C 2 256 ? 104.694 83.050  125.228 1.00 21.74 ?  235 LEU C CG    1 
ATOM   12903 C  CD1   . LEU C 2 256 ? 106.110 83.148  124.641 1.00 20.15 ?  235 LEU C CD1   1 
ATOM   12904 C  CD2   . LEU C 2 256 ? 104.566 83.927  126.473 1.00 20.90 ?  235 LEU C CD2   1 
ATOM   12905 N  N     . TYR C 2 257 ? 101.122 83.342  122.306 1.00 21.68 ?  236 TYR C N     1 
ATOM   12906 C  CA    . TYR C 2 257 ? 100.341 83.897  121.200 1.00 22.40 ?  236 TYR C CA    1 
ATOM   12907 C  C     . TYR C 2 257 ? 98.904  84.227  121.635 1.00 23.31 ?  236 TYR C C     1 
ATOM   12908 O  O     . TYR C 2 257 ? 98.428  85.359  121.419 1.00 22.99 ?  236 TYR C O     1 
ATOM   12909 C  CB    . TYR C 2 257 ? 100.360 82.937  120.007 1.00 22.81 ?  236 TYR C CB    1 
ATOM   12910 C  CG    . TYR C 2 257 ? 99.470  83.336  118.847 1.00 23.76 ?  236 TYR C CG    1 
ATOM   12911 C  CD1   . TYR C 2 257 ? 99.749  84.475  118.085 1.00 24.05 ?  236 TYR C CD1   1 
ATOM   12912 C  CD2   . TYR C 2 257 ? 98.343  82.584  118.522 1.00 24.04 ?  236 TYR C CD2   1 
ATOM   12913 C  CE1   . TYR C 2 257 ? 98.928  84.853  117.028 1.00 24.40 ?  236 TYR C CE1   1 
ATOM   12914 C  CE2   . TYR C 2 257 ? 97.517  82.954  117.462 1.00 26.30 ?  236 TYR C CE2   1 
ATOM   12915 C  CZ    . TYR C 2 257 ? 97.825  84.081  116.722 1.00 25.80 ?  236 TYR C CZ    1 
ATOM   12916 O  OH    . TYR C 2 257 ? 97.019  84.436  115.678 1.00 28.42 ?  236 TYR C OH    1 
ATOM   12917 N  N     . GLU C 2 258 ? 98.237  83.265  122.281 1.00 22.99 ?  237 GLU C N     1 
ATOM   12918 C  CA    . GLU C 2 258 ? 96.854  83.452  122.733 1.00 24.46 ?  237 GLU C CA    1 
ATOM   12919 C  C     . GLU C 2 258 ? 96.730  84.612  123.708 1.00 23.86 ?  237 GLU C C     1 
ATOM   12920 O  O     . GLU C 2 258 ? 95.790  85.401  123.622 1.00 24.01 ?  237 GLU C O     1 
ATOM   12921 C  CB    . GLU C 2 258 ? 96.269  82.159  123.328 1.00 25.21 ?  237 GLU C CB    1 
ATOM   12922 C  CG    . GLU C 2 258 ? 96.035  81.046  122.281 1.00 30.12 ?  237 GLU C CG    1 
ATOM   12923 C  CD    . GLU C 2 258 ? 94.955  81.403  121.256 1.00 35.29 ?  237 GLU C CD    1 
ATOM   12924 O  OE1   . GLU C 2 258 ? 94.023  82.172  121.589 1.00 37.71 ?  237 GLU C OE1   1 
ATOM   12925 O  OE2   . GLU C 2 258 ? 95.035  80.907  120.107 1.00 39.07 -1 237 GLU C OE2   1 
ATOM   12926 N  N     . ASN C 2 259 ? 97.697  84.731  124.616 1.00 23.25 ?  238 ASN C N     1 
ATOM   12927 C  CA    . ASN C 2 259 ? 97.751  85.869  125.531 1.00 23.10 ?  238 ASN C CA    1 
ATOM   12928 C  C     . ASN C 2 259 ? 98.005  87.190  124.781 1.00 22.68 ?  238 ASN C C     1 
ATOM   12929 O  O     . ASN C 2 259 ? 97.390  88.218  125.083 1.00 22.73 ?  238 ASN C O     1 
ATOM   12930 C  CB    . ASN C 2 259 ? 98.815  85.624  126.604 1.00 23.22 ?  238 ASN C CB    1 
ATOM   12931 C  CG    . ASN C 2 259 ? 98.897  86.752  127.611 1.00 24.46 ?  238 ASN C CG    1 
ATOM   12932 O  OD1   . ASN C 2 259 ? 97.992  86.942  128.430 1.00 26.28 ?  238 ASN C OD1   1 
ATOM   12933 N  ND2   . ASN C 2 259 ? 99.986  87.510  127.559 1.00 24.93 ?  238 ASN C ND2   1 
ATOM   12934 N  N     . GLU C 2 260 ? 98.889  87.155  123.787 1.00 22.64 ?  239 GLU C N     1 
ATOM   12935 C  CA    . GLU C 2 260 ? 99.227  88.358  123.024 1.00 23.18 ?  239 GLU C CA    1 
ATOM   12936 C  C     . GLU C 2 260 ? 98.031  88.874  122.205 1.00 23.40 ?  239 GLU C C     1 
ATOM   12937 O  O     . GLU C 2 260 ? 97.859  90.092  122.039 1.00 23.57 ?  239 GLU C O     1 
ATOM   12938 C  CB    . GLU C 2 260 ? 100.448 88.116  122.125 1.00 23.19 ?  239 GLU C CB    1 
ATOM   12939 C  CG    . GLU C 2 260 ? 101.269 89.392  121.819 1.00 24.33 ?  239 GLU C CG    1 
ATOM   12940 C  CD    . GLU C 2 260 ? 101.930 90.010  123.064 1.00 27.99 ?  239 GLU C CD    1 
ATOM   12941 O  OE1   . GLU C 2 260 ? 101.898 89.405  124.158 1.00 27.36 ?  239 GLU C OE1   1 
ATOM   12942 O  OE2   . GLU C 2 260 ? 102.483 91.126  122.950 1.00 28.98 -1 239 GLU C OE2   1 
ATOM   12943 N  N     . LEU C 2 261 ? 97.207  87.950  121.710 1.00 23.35 ?  240 LEU C N     1 
ATOM   12944 C  CA    . LEU C 2 261 ? 95.960  88.318  121.022 1.00 23.74 ?  240 LEU C CA    1 
ATOM   12945 C  C     . LEU C 2 261 ? 95.046  89.177  121.901 1.00 23.80 ?  240 LEU C C     1 
ATOM   12946 O  O     . LEU C 2 261 ? 94.545  90.226  121.465 1.00 23.33 ?  240 LEU C O     1 
ATOM   12947 C  CB    . LEU C 2 261 ? 95.202  87.075  120.549 1.00 24.09 ?  240 LEU C CB    1 
ATOM   12948 C  CG    . LEU C 2 261 ? 95.821  86.272  119.404 1.00 24.07 ?  240 LEU C CG    1 
ATOM   12949 C  CD1   . LEU C 2 261 ? 94.943  85.070  119.085 1.00 24.77 ?  240 LEU C CD1   1 
ATOM   12950 C  CD2   . LEU C 2 261 ? 96.027  87.154  118.155 1.00 24.38 ?  240 LEU C CD2   1 
ATOM   12951 N  N     . GLU C 2 262 ? 94.829  88.723  123.129 1.00 23.41 ?  241 GLU C N     1 
ATOM   12952 C  CA    . GLU C 2 262 ? 94.007  89.459  124.089 1.00 24.02 ?  241 GLU C CA    1 
ATOM   12953 C  C     . GLU C 2 262 ? 94.619  90.822  124.447 1.00 22.91 ?  241 GLU C C     1 
ATOM   12954 O  O     . GLU C 2 262 ? 93.906  91.813  124.539 1.00 22.94 ?  241 GLU C O     1 
ATOM   12955 C  CB    . GLU C 2 262 ? 93.800  88.617  125.349 1.00 24.92 ?  241 GLU C CB    1 
ATOM   12956 C  CG    . GLU C 2 262 ? 92.986  87.352  125.131 1.00 27.82 ?  241 GLU C CG    1 
ATOM   12957 C  CD    . GLU C 2 262 ? 92.782  86.569  126.415 1.00 33.08 ?  241 GLU C CD    1 
ATOM   12958 O  OE1   . GLU C 2 262 ? 93.695  85.814  126.823 1.00 36.94 ?  241 GLU C OE1   1 
ATOM   12959 O  OE2   . GLU C 2 262 ? 91.701  86.701  127.018 1.00 37.48 -1 241 GLU C OE2   1 
ATOM   12960 N  N     . TYR C 2 263 ? 95.937  90.851  124.657 1.00 21.84 ?  242 TYR C N     1 
ATOM   12961 C  CA    . TYR C 2 263 ? 96.688  92.083  124.894 1.00 21.66 ?  242 TYR C CA    1 
ATOM   12962 C  C     . TYR C 2 263 ? 96.538  93.046  123.722 1.00 21.28 ?  242 TYR C C     1 
ATOM   12963 O  O     . TYR C 2 263 ? 96.307  94.248  123.918 1.00 21.14 ?  242 TYR C O     1 
ATOM   12964 C  CB    . TYR C 2 263 ? 98.177  91.756  125.080 1.00 21.44 ?  242 TYR C CB    1 
ATOM   12965 C  CG    . TYR C 2 263 ? 99.095  92.938  125.361 1.00 21.89 ?  242 TYR C CG    1 
ATOM   12966 C  CD1   . TYR C 2 263 ? 99.044  93.614  126.581 1.00 22.52 ?  242 TYR C CD1   1 
ATOM   12967 C  CD2   . TYR C 2 263 ? 100.041 93.353  124.419 1.00 22.58 ?  242 TYR C CD2   1 
ATOM   12968 C  CE1   . TYR C 2 263 ? 99.900  94.682  126.850 1.00 22.67 ?  242 TYR C CE1   1 
ATOM   12969 C  CE2   . TYR C 2 263 ? 100.908 94.420  124.680 1.00 24.03 ?  242 TYR C CE2   1 
ATOM   12970 C  CZ    . TYR C 2 263 ? 100.833 95.071  125.906 1.00 23.75 ?  242 TYR C CZ    1 
ATOM   12971 O  OH    . TYR C 2 263 ? 101.675 96.130  126.183 1.00 26.82 ?  242 TYR C OH    1 
ATOM   12972 N  N     . THR C 2 264 ? 96.674  92.514  122.510 1.00 20.66 ?  243 THR C N     1 
ATOM   12973 C  CA    . THR C 2 264 ? 96.579  93.325  121.288 1.00 20.99 ?  243 THR C CA    1 
ATOM   12974 C  C     . THR C 2 264 ? 95.187  93.953  121.153 1.00 21.22 ?  243 THR C C     1 
ATOM   12975 O  O     . THR C 2 264 ? 95.066  95.158  120.887 1.00 20.95 ?  243 THR C O     1 
ATOM   12976 C  CB    . THR C 2 264 ? 96.934  92.489  120.028 1.00 20.58 ?  243 THR C CB    1 
ATOM   12977 O  OG1   . THR C 2 264 ? 98.310  92.105  120.095 1.00 20.84 ?  243 THR C OG1   1 
ATOM   12978 C  CG2   . THR C 2 264 ? 96.708  93.288  118.742 1.00 20.90 ?  243 THR C CG2   1 
ATOM   12979 N  N     . GLU C 2 265 ? 94.145  93.148  121.366 1.00 21.62 ?  244 GLU C N     1 
ATOM   12980 C  CA    . GLU C 2 265 ? 92.775  93.657  121.296 1.00 23.46 ?  244 GLU C CA    1 
ATOM   12981 C  C     . GLU C 2 265 ? 92.528  94.725  122.342 1.00 23.33 ?  244 GLU C C     1 
ATOM   12982 O  O     . GLU C 2 265 ? 91.924  95.762  122.064 1.00 22.86 ?  244 GLU C O     1 
ATOM   12983 C  CB    . GLU C 2 265 ? 91.747  92.534  121.442 1.00 24.31 ?  244 GLU C CB    1 
ATOM   12984 C  CG    . GLU C 2 265 ? 91.665  91.622  120.223 1.00 27.63 ?  244 GLU C CG    1 
ATOM   12985 C  CD    . GLU C 2 265 ? 90.627  90.516  120.387 1.00 33.27 ?  244 GLU C CD    1 
ATOM   12986 O  OE1   . GLU C 2 265 ? 89.621  90.732  121.102 1.00 35.56 ?  244 GLU C OE1   1 
ATOM   12987 O  OE2   . GLU C 2 265 ? 90.814  89.431  119.792 1.00 35.96 -1 244 GLU C OE2   1 
ATOM   12988 N  N     . ASP C 2 266 ? 93.010  94.468  123.549 1.00 23.36 ?  245 ASP C N     1 
ATOM   12989 C  CA    . ASP C 2 266 ? 92.865  95.412  124.645 1.00 24.18 ?  245 ASP C CA    1 
ATOM   12990 C  C     . ASP C 2 266 ? 93.476  96.788  124.317 1.00 23.96 ?  245 ASP C C     1 
ATOM   12991 O  O     . ASP C 2 266 ? 92.894  97.822  124.635 1.00 24.19 ?  245 ASP C O     1 
ATOM   12992 C  CB    . ASP C 2 266 ? 93.510  94.828  125.899 1.00 25.14 ?  245 ASP C CB    1 
ATOM   12993 C  CG    . ASP C 2 266 ? 93.191  95.622  127.129 1.00 27.35 ?  245 ASP C CG    1 
ATOM   12994 O  OD1   . ASP C 2 266 ? 91.991  95.812  127.417 1.00 28.45 ?  245 ASP C OD1   1 
ATOM   12995 O  OD2   . ASP C 2 266 ? 94.148  96.057  127.804 1.00 31.99 -1 245 ASP C OD2   1 
ATOM   12996 N  N     . LEU C 2 267 ? 94.633  96.794  123.666 1.00 23.34 ?  246 LEU C N     1 
ATOM   12997 C  CA    . LEU C 2 267 ? 95.315  98.049  123.334 1.00 23.53 ?  246 LEU C CA    1 
ATOM   12998 C  C     . LEU C 2 267 ? 94.835  98.714  122.053 1.00 22.94 ?  246 LEU C C     1 
ATOM   12999 O  O     . LEU C 2 267 ? 94.693  99.937  122.002 1.00 23.14 ?  246 LEU C O     1 
ATOM   13000 C  CB    . LEU C 2 267 ? 96.821  97.820  123.234 1.00 23.37 ?  246 LEU C CB    1 
ATOM   13001 C  CG    . LEU C 2 267 ? 97.581  97.567  124.537 1.00 26.17 ?  246 LEU C CG    1 
ATOM   13002 C  CD1   . LEU C 2 267 ? 99.047  97.391  124.209 1.00 27.31 ?  246 LEU C CD1   1 
ATOM   13003 C  CD2   . LEU C 2 267 ? 97.396  98.728  125.509 1.00 28.08 ?  246 LEU C CD2   1 
ATOM   13004 N  N     . TYR C 2 268 ? 94.611  97.910  121.017 1.00 22.46 ?  247 TYR C N     1 
ATOM   13005 C  CA    . TYR C 2 268 ? 94.385  98.449  119.679 1.00 22.00 ?  247 TYR C CA    1 
ATOM   13006 C  C     . TYR C 2 268 ? 92.948  98.628  119.220 1.00 22.26 ?  247 TYR C C     1 
ATOM   13007 O  O     . TYR C 2 268 ? 92.724  99.332  118.234 1.00 22.17 ?  247 TYR C O     1 
ATOM   13008 C  CB    . TYR C 2 268 ? 95.157  97.632  118.634 1.00 21.73 ?  247 TYR C CB    1 
ATOM   13009 C  CG    . TYR C 2 268 ? 96.651  97.838  118.694 1.00 21.49 ?  247 TYR C CG    1 
ATOM   13010 C  CD1   . TYR C 2 268 ? 97.478  96.903  119.325 1.00 19.45 ?  247 TYR C CD1   1 
ATOM   13011 C  CD2   . TYR C 2 268 ? 97.239  98.978  118.134 1.00 22.71 ?  247 TYR C CD2   1 
ATOM   13012 C  CE1   . TYR C 2 268 ? 98.861  97.097  119.391 1.00 20.30 ?  247 TYR C CE1   1 
ATOM   13013 C  CE2   . TYR C 2 268 ? 98.627  99.185  118.188 1.00 21.69 ?  247 TYR C CE2   1 
ATOM   13014 C  CZ    . TYR C 2 268 ? 99.425  98.233  118.804 1.00 21.40 ?  247 TYR C CZ    1 
ATOM   13015 O  OH    . TYR C 2 268 ? 100.781 98.429  118.851 1.00 22.11 ?  247 TYR C OH    1 
ATOM   13016 N  N     . ASP C 2 269 ? 91.978  97.991  119.885 1.00 22.40 ?  248 ASP C N     1 
ATOM   13017 C  CA    . ASP C 2 269 ? 90.570  98.169  119.487 1.00 22.75 ?  248 ASP C CA    1 
ATOM   13018 C  C     . ASP C 2 269 ? 90.161  99.643  119.476 1.00 22.55 ?  248 ASP C C     1 
ATOM   13019 O  O     . ASP C 2 269 ? 89.422  100.074 118.582 1.00 22.22 ?  248 ASP C O     1 
ATOM   13020 C  CB    . ASP C 2 269 ? 89.600  97.345  120.355 1.00 23.03 ?  248 ASP C CB    1 
ATOM   13021 C  CG    . ASP C 2 269 ? 89.517  95.888  119.930 1.00 25.02 ?  248 ASP C CG    1 
ATOM   13022 O  OD1   . ASP C 2 269 ? 90.036  95.524  118.854 1.00 26.85 ?  248 ASP C OD1   1 
ATOM   13023 O  OD2   . ASP C 2 269 ? 88.915  95.094  120.681 1.00 28.74 -1 248 ASP C OD2   1 
ATOM   13024 N  N     . GLN C 2 270 ? 90.649  100.412 120.453 1.00 22.21 ?  249 GLN C N     1 
ATOM   13025 C  CA    . GLN C 2 270 ? 90.296  101.848 120.539 1.00 22.39 ?  249 GLN C CA    1 
ATOM   13026 C  C     . GLN C 2 270 ? 90.893  102.718 119.425 1.00 21.65 ?  249 GLN C C     1 
ATOM   13027 O  O     . GLN C 2 270 ? 90.484  103.868 119.257 1.00 21.70 ?  249 GLN C O     1 
ATOM   13028 C  CB    . GLN C 2 270 ? 90.622  102.437 121.920 1.00 22.53 ?  249 GLN C CB    1 
ATOM   13029 C  CG    . GLN C 2 270 ? 92.117  102.413 122.331 1.00 22.73 ?  249 GLN C CG    1 
ATOM   13030 C  CD    . GLN C 2 270 ? 92.331  103.015 123.704 1.00 25.39 ?  249 GLN C CD    1 
ATOM   13031 O  OE1   . GLN C 2 270 ? 91.382  103.175 124.475 1.00 27.88 ?  249 GLN C OE1   1 
ATOM   13032 N  NE2   . GLN C 2 270 ? 93.575  103.365 124.020 1.00 24.88 ?  249 GLN C NE2   1 
ATOM   13033 N  N     . VAL C 2 271 ? 91.854  102.173 118.676 1.00 20.91 ?  250 VAL C N     1 
ATOM   13034 C  CA    . VAL C 2 271 ? 92.456  102.888 117.526 1.00 20.62 ?  250 VAL C CA    1 
ATOM   13035 C  C     . VAL C 2 271 ? 92.185  102.166 116.192 1.00 20.53 ?  250 VAL C C     1 
ATOM   13036 O  O     . VAL C 2 271 ? 92.638  102.607 115.124 1.00 20.05 ?  250 VAL C O     1 
ATOM   13037 C  CB    . VAL C 2 271 ? 93.987  103.199 117.724 1.00 20.32 ?  250 VAL C CB    1 
ATOM   13038 C  CG1   . VAL C 2 271 ? 94.200  104.160 118.889 1.00 20.35 ?  250 VAL C CG1   1 
ATOM   13039 C  CG2   . VAL C 2 271 ? 94.816  101.925 117.938 1.00 19.32 ?  250 VAL C CG2   1 
ATOM   13040 N  N     . GLY C 2 272 ? 91.433  101.066 116.270 1.00 20.29 ?  251 GLY C N     1 
ATOM   13041 C  CA    . GLY C 2 272 ? 90.927  100.368 115.085 1.00 20.51 ?  251 GLY C CA    1 
ATOM   13042 C  C     . GLY C 2 272 ? 91.919  99.477  114.355 1.00 20.99 ?  251 GLY C C     1 
ATOM   13043 O  O     . GLY C 2 272 ? 91.726  99.170  113.168 1.00 20.22 ?  251 GLY C O     1 
ATOM   13044 N  N     . LEU C 2 273 ? 92.980  99.057  115.050 1.00 20.76 ?  252 LEU C N     1 
ATOM   13045 C  CA    . LEU C 2 273 ? 94.102  98.400  114.372 1.00 21.38 ?  252 LEU C CA    1 
ATOM   13046 C  C     . LEU C 2 273 ? 94.382  96.955  114.776 1.00 21.86 ?  252 LEU C C     1 
ATOM   13047 O  O     . LEU C 2 273 ? 95.366  96.370  114.324 1.00 22.45 ?  252 LEU C O     1 
ATOM   13048 C  CB    . LEU C 2 273 ? 95.382  99.245  114.496 1.00 21.44 ?  252 LEU C CB    1 
ATOM   13049 C  CG    . LEU C 2 273 ? 95.372  100.679 113.962 1.00 22.02 ?  252 LEU C CG    1 
ATOM   13050 C  CD1   . LEU C 2 273 ? 96.711  101.343 114.261 1.00 22.86 ?  252 LEU C CD1   1 
ATOM   13051 C  CD2   . LEU C 2 273 ? 95.059  100.712 112.451 1.00 23.88 ?  252 LEU C CD2   1 
ATOM   13052 N  N     . SER C 2 274 ? 93.519  96.366  115.601 1.00 22.19 ?  253 SER C N     1 
ATOM   13053 C  CA    . SER C 2 274 ? 93.824  95.078  116.219 1.00 22.47 ?  253 SER C CA    1 
ATOM   13054 C  C     . SER C 2 274 ? 94.112  93.970  115.204 1.00 22.94 ?  253 SER C C     1 
ATOM   13055 O  O     . SER C 2 274 ? 95.076  93.227  115.354 1.00 22.07 ?  253 SER C O     1 
ATOM   13056 C  CB    . SER C 2 274 ? 92.696  94.655  117.164 1.00 22.91 ?  253 SER C CB    1 
ATOM   13057 O  OG    . SER C 2 274 ? 92.663  95.518  118.282 1.00 24.25 ?  253 SER C OG    1 
ATOM   13058 N  N     . HIS C 2 275 ? 93.294  93.892  114.157 1.00 24.59 ?  254 HIS C N     1 
ATOM   13059 C  CA    . HIS C 2 275 ? 93.454  92.857  113.130 1.00 25.66 ?  254 HIS C CA    1 
ATOM   13060 C  C     . HIS C 2 275 ? 94.791  92.990  112.381 1.00 26.01 ?  254 HIS C C     1 
ATOM   13061 O  O     . HIS C 2 275 ? 95.461  91.987  112.083 1.00 26.23 ?  254 HIS C O     1 
ATOM   13062 C  CB    . HIS C 2 275 ? 92.277  92.897  112.147 1.00 26.89 ?  254 HIS C CB    1 
ATOM   13063 C  CG    . HIS C 2 275 ? 92.308  91.807  111.122 1.00 29.10 ?  254 HIS C CG    1 
ATOM   13064 N  ND1   . HIS C 2 275 ? 92.401  90.471  111.457 1.00 32.70 ?  254 HIS C ND1   1 
ATOM   13065 C  CD2   . HIS C 2 275 ? 92.257  91.851  109.771 1.00 31.68 ?  254 HIS C CD2   1 
ATOM   13066 C  CE1   . HIS C 2 275 ? 92.409  89.743  110.355 1.00 33.55 ?  254 HIS C CE1   1 
ATOM   13067 N  NE2   . HIS C 2 275 ? 92.307  90.554  109.319 1.00 33.71 ?  254 HIS C NE2   1 
ATOM   13068 N  N     . ASP C 2 276 ? 95.164  94.229  112.084 1.00 25.93 ?  255 ASP C N     1 
ATOM   13069 C  CA    . ASP C 2 276 ? 96.431  94.530  111.423 1.00 26.65 ?  255 ASP C CA    1 
ATOM   13070 C  C     . ASP C 2 276 ? 97.637  94.125  112.273 1.00 25.61 ?  255 ASP C C     1 
ATOM   13071 O  O     . ASP C 2 276 ? 98.575  93.500  111.761 1.00 25.34 ?  255 ASP C O     1 
ATOM   13072 C  CB    . ASP C 2 276 ? 96.511  96.015  111.066 1.00 27.44 ?  255 ASP C CB    1 
ATOM   13073 C  CG    . ASP C 2 276 ? 96.493  96.252  109.572 1.00 32.09 ?  255 ASP C CG    1 
ATOM   13074 O  OD1   . ASP C 2 276 ? 97.211  95.522  108.847 1.00 36.67 ?  255 ASP C OD1   1 
ATOM   13075 O  OD2   . ASP C 2 276 ? 95.754  97.156  109.117 1.00 36.30 -1 255 ASP C OD2   1 
ATOM   13076 N  N     . VAL C 2 277 ? 97.600  94.484  113.560 1.00 24.17 ?  256 VAL C N     1 
ATOM   13077 C  CA    . VAL C 2 277 ? 98.668  94.125  114.503 1.00 23.71 ?  256 VAL C CA    1 
ATOM   13078 C  C     . VAL C 2 277 ? 98.791  92.605  114.635 1.00 23.48 ?  256 VAL C C     1 
ATOM   13079 O  O     . VAL C 2 277 ? 99.900  92.071  114.674 1.00 23.08 ?  256 VAL C O     1 
ATOM   13080 C  CB    . VAL C 2 277 ? 98.455  94.752  115.909 1.00 23.27 ?  256 VAL C CB    1 
ATOM   13081 C  CG1   . VAL C 2 277 ? 99.591  94.358  116.861 1.00 24.02 ?  256 VAL C CG1   1 
ATOM   13082 C  CG2   . VAL C 2 277 ? 98.348  96.268  115.822 1.00 23.35 ?  256 VAL C CG2   1 
ATOM   13083 N  N     . LYS C 2 278 ? 97.655  91.916  114.703 1.00 23.36 ?  257 LYS C N     1 
ATOM   13084 C  CA    . LYS C 2 278 ? 97.641  90.455  114.778 1.00 24.12 ?  257 LYS C CA    1 
ATOM   13085 C  C     . LYS C 2 278 ? 98.379  89.797  113.615 1.00 24.30 ?  257 LYS C C     1 
ATOM   13086 O  O     . LYS C 2 278 ? 99.119  88.821  113.809 1.00 24.37 ?  257 LYS C O     1 
ATOM   13087 C  CB    . LYS C 2 278 ? 96.212  89.921  114.867 1.00 24.22 ?  257 LYS C CB    1 
ATOM   13088 C  CG    . LYS C 2 278 ? 95.557  90.133  116.222 1.00 24.96 ?  257 LYS C CG    1 
ATOM   13089 C  CD    . LYS C 2 278 ? 94.098  89.702  116.154 1.00 26.34 ?  257 LYS C CD    1 
ATOM   13090 C  CE    . LYS C 2 278 ? 93.392  89.932  117.462 1.00 27.16 ?  257 LYS C CE    1 
ATOM   13091 N  NZ    . LYS C 2 278 ? 91.974  89.481  117.332 1.00 29.60 1  257 LYS C NZ    1 
ATOM   13092 N  N     . LYS C 2 279 ? 98.186  90.328  112.409 1.00 24.55 ?  258 LYS C N     1 
ATOM   13093 C  CA    . LYS C 2 279 ? 98.914  89.833  111.245 1.00 24.85 ?  258 LYS C CA    1 
ATOM   13094 C  C     . LYS C 2 279 ? 100.416 90.040  111.427 1.00 24.57 ?  258 LYS C C     1 
ATOM   13095 O  O     . LYS C 2 279 ? 101.209 89.163  111.087 1.00 24.07 ?  258 LYS C O     1 
ATOM   13096 C  CB    . LYS C 2 279 ? 98.439  90.533  109.971 1.00 25.30 ?  258 LYS C CB    1 
ATOM   13097 C  CG    . LYS C 2 279 ? 96.979  90.308  109.652 1.00 26.63 ?  258 LYS C CG    1 
ATOM   13098 C  CD    . LYS C 2 279 ? 96.617  91.052  108.373 1.00 29.30 ?  258 LYS C CD    1 
ATOM   13099 C  CE    . LYS C 2 279 ? 95.219  90.724  107.943 1.00 31.79 ?  258 LYS C CE    1 
ATOM   13100 N  NZ    . LYS C 2 279 ? 94.775  91.705  106.921 1.00 33.80 1  258 LYS C NZ    1 
ATOM   13101 N  N     . PHE C 2 280 ? 100.789 91.190  111.991 1.00 24.29 ?  259 PHE C N     1 
ATOM   13102 C  CA    . PHE C 2 280 ? 102.196 91.543  112.222 1.00 24.90 ?  259 PHE C CA    1 
ATOM   13103 C  C     . PHE C 2 280 ? 102.874 90.606  113.239 1.00 24.86 ?  259 PHE C C     1 
ATOM   13104 O  O     . PHE C 2 280 ? 104.009 90.166  113.029 1.00 24.68 ?  259 PHE C O     1 
ATOM   13105 C  CB    . PHE C 2 280 ? 102.287 93.013  112.656 1.00 24.70 ?  259 PHE C CB    1 
ATOM   13106 C  CG    . PHE C 2 280 ? 103.689 93.576  112.698 1.00 25.70 ?  259 PHE C CG    1 
ATOM   13107 C  CD1   . PHE C 2 280 ? 104.493 93.590  111.558 1.00 26.86 ?  259 PHE C CD1   1 
ATOM   13108 C  CD2   . PHE C 2 280 ? 104.188 94.140  113.879 1.00 26.19 ?  259 PHE C CD2   1 
ATOM   13109 C  CE1   . PHE C 2 280 ? 105.785 94.136  111.592 1.00 26.66 ?  259 PHE C CE1   1 
ATOM   13110 C  CE2   . PHE C 2 280 ? 105.471 94.693  113.922 1.00 26.52 ?  259 PHE C CE2   1 
ATOM   13111 C  CZ    . PHE C 2 280 ? 106.275 94.686  112.773 1.00 26.23 ?  259 PHE C CZ    1 
ATOM   13112 N  N     . ILE C 2 281 ? 102.174 90.297  114.332 1.00 25.53 ?  260 ILE C N     1 
ATOM   13113 C  CA    . ILE C 2 281 ? 102.742 89.416  115.356 1.00 26.21 ?  260 ILE C CA    1 
ATOM   13114 C  C     . ILE C 2 281 ? 102.892 87.972  114.856 1.00 26.47 ?  260 ILE C C     1 
ATOM   13115 O  O     . ILE C 2 281 ? 103.845 87.292  115.225 1.00 26.52 ?  260 ILE C O     1 
ATOM   13116 C  CB    . ILE C 2 281 ? 102.014 89.510  116.741 1.00 26.27 ?  260 ILE C CB    1 
ATOM   13117 C  CG1   . ILE C 2 281 ? 100.698 88.730  116.752 1.00 27.37 ?  260 ILE C CG1   1 
ATOM   13118 C  CG2   . ILE C 2 281 ? 101.831 90.987  117.158 1.00 26.92 ?  260 ILE C CG2   1 
ATOM   13119 C  CD1   . ILE C 2 281 ? 99.979  88.727  118.102 1.00 29.51 ?  260 ILE C CD1   1 
ATOM   13120 N  N     . ARG C 2 282 ? 101.980 87.529  113.989 1.00 26.57 ?  261 ARG C N     1 
ATOM   13121 C  CA    . ARG C 2 282 ? 102.095 86.203  113.374 1.00 26.84 ?  261 ARG C CA    1 
ATOM   13122 C  C     . ARG C 2 282 ? 103.311 86.134  112.450 1.00 27.34 ?  261 ARG C C     1 
ATOM   13123 O  O     . ARG C 2 282 ? 104.063 85.164  112.481 1.00 27.54 ?  261 ARG C O     1 
ATOM   13124 C  CB    . ARG C 2 282 ? 100.817 85.813  112.628 1.00 26.98 ?  261 ARG C CB    1 
ATOM   13125 C  CG    . ARG C 2 282 ? 99.696  85.319  113.522 1.00 26.53 ?  261 ARG C CG    1 
ATOM   13126 C  CD    . ARG C 2 282 ? 98.557  84.675  112.705 1.00 27.77 ?  261 ARG C CD    1 
ATOM   13127 N  NE    . ARG C 2 282 ? 97.799  85.649  111.925 1.00 28.67 ?  261 ARG C NE    1 
ATOM   13128 C  CZ    . ARG C 2 282 ? 96.773  86.363  112.393 1.00 29.68 ?  261 ARG C CZ    1 
ATOM   13129 N  NH1   . ARG C 2 282 ? 96.363  86.222  113.653 1.00 28.31 1  261 ARG C NH1   1 
ATOM   13130 N  NH2   . ARG C 2 282 ? 96.148  87.215  111.598 1.00 29.15 ?  261 ARG C NH2   1 
ATOM   13131 N  N     . TYR C 2 283 ? 103.493 87.180  111.646 1.00 27.78 ?  262 TYR C N     1 
ATOM   13132 C  CA    . TYR C 2 283 ? 104.675 87.346  110.802 1.00 28.18 ?  262 TYR C CA    1 
ATOM   13133 C  C     . TYR C 2 283 ? 105.970 87.204  111.622 1.00 27.08 ?  262 TYR C C     1 
ATOM   13134 O  O     . TYR C 2 283 ? 106.881 86.441  111.265 1.00 26.51 ?  262 TYR C O     1 
ATOM   13135 C  CB    . TYR C 2 283 ? 104.621 88.720  110.122 1.00 29.11 ?  262 TYR C CB    1 
ATOM   13136 C  CG    . TYR C 2 283 ? 105.778 89.018  109.200 1.00 32.56 ?  262 TYR C CG    1 
ATOM   13137 C  CD1   . TYR C 2 283 ? 105.854 88.430  107.936 1.00 36.59 ?  262 TYR C CD1   1 
ATOM   13138 C  CD2   . TYR C 2 283 ? 106.793 89.902  109.582 1.00 36.34 ?  262 TYR C CD2   1 
ATOM   13139 C  CE1   . TYR C 2 283 ? 106.918 88.704  107.072 1.00 39.47 ?  262 TYR C CE1   1 
ATOM   13140 C  CE2   . TYR C 2 283 ? 107.866 90.188  108.717 1.00 39.23 ?  262 TYR C CE2   1 
ATOM   13141 C  CZ    . TYR C 2 283 ? 107.917 89.581  107.467 1.00 40.48 ?  262 TYR C CZ    1 
ATOM   13142 O  OH    . TYR C 2 283 ? 108.960 89.843  106.608 1.00 44.00 ?  262 TYR C OH    1 
ATOM   13143 N  N     . ASN C 2 284 ? 106.031 87.921  112.736 1.00 26.08 ?  263 ASN C N     1 
ATOM   13144 C  CA    . ASN C 2 284 ? 107.206 87.878  113.592 1.00 25.73 ?  263 ASN C CA    1 
ATOM   13145 C  C     . ASN C 2 284 ? 107.367 86.589  114.401 1.00 25.24 ?  263 ASN C C     1 
ATOM   13146 O  O     . ASN C 2 284 ? 108.501 86.160  114.653 1.00 25.56 ?  263 ASN C O     1 
ATOM   13147 C  CB    . ASN C 2 284 ? 107.278 89.137  114.457 1.00 25.69 ?  263 ASN C CB    1 
ATOM   13148 C  CG    . ASN C 2 284 ? 107.711 90.346  113.659 1.00 26.39 ?  263 ASN C CG    1 
ATOM   13149 O  OD1   . ASN C 2 284 ? 108.890 90.496  113.329 1.00 26.91 ?  263 ASN C OD1   1 
ATOM   13150 N  ND2   . ASN C 2 284 ? 106.763 91.213  113.335 1.00 27.56 ?  263 ASN C ND2   1 
ATOM   13151 N  N     . ALA C 2 285 ? 106.254 85.955  114.780 1.00 24.51 ?  264 ALA C N     1 
ATOM   13152 C  CA    . ALA C 2 285 ? 106.311 84.598  115.356 1.00 24.19 ?  264 ALA C CA    1 
ATOM   13153 C  C     . ALA C 2 285 ? 107.064 83.611  114.441 1.00 24.63 ?  264 ALA C C     1 
ATOM   13154 O  O     . ALA C 2 285 ? 107.878 82.819  114.912 1.00 24.01 ?  264 ALA C O     1 
ATOM   13155 C  CB    . ALA C 2 285 ? 104.920 84.071  115.657 1.00 23.63 ?  264 ALA C CB    1 
ATOM   13156 N  N     . ASN C 2 286 ? 106.787 83.671  113.139 1.00 24.66 ?  265 ASN C N     1 
ATOM   13157 C  CA    . ASN C 2 286 ? 107.507 82.857  112.160 1.00 25.24 ?  265 ASN C CA    1 
ATOM   13158 C  C     . ASN C 2 286 ? 109.008 83.124  112.115 1.00 25.09 ?  265 ASN C C     1 
ATOM   13159 O  O     . ASN C 2 286 ? 109.797 82.185  111.918 1.00 24.14 ?  265 ASN C O     1 
ATOM   13160 C  CB    . ASN C 2 286 ? 106.906 83.013  110.751 1.00 25.62 ?  265 ASN C CB    1 
ATOM   13161 C  CG    . ASN C 2 286 ? 105.581 82.282  110.600 1.00 26.46 ?  265 ASN C CG    1 
ATOM   13162 O  OD1   . ASN C 2 286 ? 105.200 81.475  111.452 1.00 27.14 ?  265 ASN C OD1   1 
ATOM   13163 N  ND2   . ASN C 2 286 ? 104.861 82.577  109.516 1.00 27.89 ?  265 ASN C ND2   1 
ATOM   13164 N  N     . LYS C 2 287 ? 109.386 84.395  112.278 1.00 24.99 ?  266 LYS C N     1 
ATOM   13165 C  CA    . LYS C 2 287 ? 110.789 84.807  112.347 1.00 25.91 ?  266 LYS C CA    1 
ATOM   13166 C  C     . LYS C 2 287 ? 111.458 84.267  113.607 1.00 25.23 ?  266 LYS C C     1 
ATOM   13167 O  O     . LYS C 2 287 ? 112.616 83.845  113.564 1.00 25.34 ?  266 LYS C O     1 
ATOM   13168 C  CB    . LYS C 2 287 ? 110.929 86.329  112.335 1.00 25.96 ?  266 LYS C CB    1 
ATOM   13169 C  CG    . LYS C 2 287 ? 110.702 87.006  110.992 1.00 29.60 ?  266 LYS C CG    1 
ATOM   13170 C  CD    . LYS C 2 287 ? 111.138 88.473  111.100 1.00 34.20 ?  266 LYS C CD    1 
ATOM   13171 C  CE    . LYS C 2 287 ? 111.041 89.202  109.783 1.00 37.67 ?  266 LYS C CE    1 
ATOM   13172 N  NZ    . LYS C 2 287 ? 111.611 90.583  109.919 1.00 39.48 1  266 LYS C NZ    1 
ATOM   13173 N  N     . ALA C 2 288 ? 110.737 84.297  114.725 1.00 24.87 ?  267 ALA C N     1 
ATOM   13174 C  CA    . ALA C 2 288 ? 111.232 83.696  115.978 1.00 24.23 ?  267 ALA C CA    1 
ATOM   13175 C  C     . ALA C 2 288 ? 111.468 82.188  115.820 1.00 24.24 ?  267 ALA C C     1 
ATOM   13176 O  O     . ALA C 2 288 ? 112.517 81.674  116.214 1.00 23.96 ?  267 ALA C O     1 
ATOM   13177 C  CB    . ALA C 2 288 ? 110.271 83.968  117.120 1.00 24.23 ?  267 ALA C CB    1 
ATOM   13178 N  N     . LEU C 2 289 ? 110.498 81.482  115.240 1.00 24.63 ?  268 LEU C N     1 
ATOM   13179 C  CA    . LEU C 2 289 ? 110.662 80.052  114.969 1.00 25.14 ?  268 LEU C CA    1 
ATOM   13180 C  C     . LEU C 2 289 ? 111.875 79.810  114.084 1.00 25.58 ?  268 LEU C C     1 
ATOM   13181 O  O     . LEU C 2 289 ? 112.670 78.916  114.352 1.00 25.42 ?  268 LEU C O     1 
ATOM   13182 C  CB    . LEU C 2 289 ? 109.403 79.440  114.334 1.00 25.28 ?  268 LEU C CB    1 
ATOM   13183 C  CG    . LEU C 2 289 ? 108.220 79.243  115.286 1.00 25.93 ?  268 LEU C CG    1 
ATOM   13184 C  CD1   . LEU C 2 289 ? 106.927 79.075  114.514 1.00 26.50 ?  268 LEU C CD1   1 
ATOM   13185 C  CD2   . LEU C 2 289 ? 108.442 78.077  116.268 1.00 25.20 ?  268 LEU C CD2   1 
ATOM   13186 N  N     . MET C 2 290 ? 112.029 80.624  113.040 1.00 26.32 ?  269 MET C N     1 
ATOM   13187 C  CA    . MET C 2 290 ? 113.176 80.472  112.149 1.00 27.41 ?  269 MET C CA    1 
ATOM   13188 C  C     . MET C 2 290 ? 114.510 80.711  112.852 1.00 26.66 ?  269 MET C C     1 
ATOM   13189 O  O     . MET C 2 290 ? 115.481 79.997  112.589 1.00 26.69 ?  269 MET C O     1 
ATOM   13190 C  CB    . MET C 2 290 ? 113.024 81.330  110.898 1.00 28.28 ?  269 MET C CB    1 
ATOM   13191 C  CG    . MET C 2 290 ? 112.326 80.563  109.775 1.00 32.91 ?  269 MET C CG    1 
ATOM   13192 S  SD    . MET C 2 290 ? 111.819 81.616  108.412 1.00 42.49 ?  269 MET C SD    1 
ATOM   13193 C  CE    . MET C 2 290 ? 110.046 81.678  108.666 1.00 38.74 ?  269 MET C CE    1 
ATOM   13194 N  N     . ASN C 2 291 ? 114.544 81.683  113.766 1.00 25.48 ?  270 ASN C N     1 
ATOM   13195 C  CA    . ASN C 2 291 ? 115.733 81.943  114.593 1.00 25.39 ?  270 ASN C CA    1 
ATOM   13196 C  C     . ASN C 2 291 ? 116.123 80.725  115.447 1.00 25.18 ?  270 ASN C C     1 
ATOM   13197 O  O     . ASN C 2 291 ? 117.299 80.544  115.797 1.00 24.73 ?  270 ASN C O     1 
ATOM   13198 C  CB    . ASN C 2 291 ? 115.518 83.174  115.483 1.00 24.83 ?  270 ASN C CB    1 
ATOM   13199 C  CG    . ASN C 2 291 ? 115.605 84.492  114.705 1.00 25.58 ?  270 ASN C CG    1 
ATOM   13200 O  OD1   . ASN C 2 291 ? 116.057 84.529  113.564 1.00 25.58 ?  270 ASN C OD1   1 
ATOM   13201 N  ND2   . ASN C 2 291 ? 115.170 85.574  115.331 1.00 24.32 ?  270 ASN C ND2   1 
ATOM   13202 N  N     . LEU C 2 292 ? 115.123 79.892  115.745 1.00 25.09 ?  271 LEU C N     1 
ATOM   13203 C  CA    . LEU C 2 292 ? 115.293 78.635  116.488 1.00 25.46 ?  271 LEU C CA    1 
ATOM   13204 C  C     . LEU C 2 292 ? 115.528 77.402  115.600 1.00 26.18 ?  271 LEU C C     1 
ATOM   13205 O  O     . LEU C 2 292 ? 115.661 76.270  116.101 1.00 26.06 ?  271 LEU C O     1 
ATOM   13206 C  CB    . LEU C 2 292 ? 114.086 78.415  117.409 1.00 25.19 ?  271 LEU C CB    1 
ATOM   13207 C  CG    . LEU C 2 292 ? 113.927 79.437  118.547 1.00 25.03 ?  271 LEU C CG    1 
ATOM   13208 C  CD1   . LEU C 2 292 ? 112.565 79.306  119.192 1.00 24.50 ?  271 LEU C CD1   1 
ATOM   13209 C  CD2   . LEU C 2 292 ? 115.046 79.263  119.587 1.00 25.64 ?  271 LEU C CD2   1 
ATOM   13210 N  N     . GLY C 2 293 ? 115.585 77.618  114.287 1.00 26.71 ?  272 GLY C N     1 
ATOM   13211 C  CA    . GLY C 2 293 ? 115.788 76.529  113.323 1.00 28.06 ?  272 GLY C CA    1 
ATOM   13212 C  C     . GLY C 2 293 ? 114.551 75.696  113.025 1.00 29.34 ?  272 GLY C C     1 
ATOM   13213 O  O     . GLY C 2 293 ? 114.661 74.547  112.571 1.00 29.73 ?  272 GLY C O     1 
ATOM   13214 N  N     . PHE C 2 294 ? 113.375 76.268  113.276 1.00 29.88 ?  273 PHE C N     1 
ATOM   13215 C  CA    . PHE C 2 294 ? 112.105 75.584  113.044 1.00 31.24 ?  273 PHE C CA    1 
ATOM   13216 C  C     . PHE C 2 294 ? 111.364 76.182  111.840 1.00 32.42 ?  273 PHE C C     1 
ATOM   13217 O  O     . PHE C 2 294 ? 111.604 77.335  111.455 1.00 32.30 ?  273 PHE C O     1 
ATOM   13218 C  CB    . PHE C 2 294 ? 111.220 75.635  114.296 1.00 30.82 ?  273 PHE C CB    1 
ATOM   13219 C  CG    . PHE C 2 294 ? 111.828 74.970  115.513 1.00 30.93 ?  273 PHE C CG    1 
ATOM   13220 C  CD1   . PHE C 2 294 ? 112.384 73.694  115.435 1.00 30.85 ?  273 PHE C CD1   1 
ATOM   13221 C  CD2   . PHE C 2 294 ? 111.830 75.619  116.739 1.00 30.30 ?  273 PHE C CD2   1 
ATOM   13222 C  CE1   . PHE C 2 294 ? 112.947 73.089  116.557 1.00 30.75 ?  273 PHE C CE1   1 
ATOM   13223 C  CE2   . PHE C 2 294 ? 112.377 75.017  117.875 1.00 30.41 ?  273 PHE C CE2   1 
ATOM   13224 C  CZ    . PHE C 2 294 ? 112.933 73.747  117.785 1.00 30.88 ?  273 PHE C CZ    1 
ATOM   13225 N  N     . ASP C 2 295 ? 110.480 75.384  111.246 1.00 33.81 ?  274 ASP C N     1 
ATOM   13226 C  CA    . ASP C 2 295 ? 109.641 75.825  110.128 1.00 35.32 ?  274 ASP C CA    1 
ATOM   13227 C  C     . ASP C 2 295 ? 108.597 76.864  110.576 1.00 35.36 ?  274 ASP C C     1 
ATOM   13228 O  O     . ASP C 2 295 ? 108.131 76.813  111.711 1.00 34.78 ?  274 ASP C O     1 
ATOM   13229 C  CB    . ASP C 2 295 ? 108.913 74.624  109.508 1.00 35.95 ?  274 ASP C CB    1 
ATOM   13230 C  CG    . ASP C 2 295 ? 109.864 73.605  108.886 1.00 37.98 ?  274 ASP C CG    1 
ATOM   13231 O  OD1   . ASP C 2 295 ? 110.977 73.978  108.453 1.00 39.83 ?  274 ASP C OD1   1 
ATOM   13232 O  OD2   . ASP C 2 295 ? 109.485 72.415  108.828 1.00 40.03 -1 274 ASP C OD2   1 
ATOM   13233 N  N     . PRO C 2 296 ? 108.223 77.800  109.682 1.00 36.33 ?  275 PRO C N     1 
ATOM   13234 C  CA    . PRO C 2 296 ? 107.133 78.751  109.995 1.00 36.92 ?  275 PRO C CA    1 
ATOM   13235 C  C     . PRO C 2 296 ? 105.819 78.046  110.371 1.00 37.68 ?  275 PRO C C     1 
ATOM   13236 O  O     . PRO C 2 296 ? 105.504 76.990  109.815 1.00 38.07 ?  275 PRO C O     1 
ATOM   13237 C  CB    . PRO C 2 296 ? 106.965 79.546  108.690 1.00 36.82 ?  275 PRO C CB    1 
ATOM   13238 C  CG    . PRO C 2 296 ? 107.736 78.766  107.634 1.00 37.42 ?  275 PRO C CG    1 
ATOM   13239 C  CD    . PRO C 2 296 ? 108.837 78.080  108.372 1.00 36.41 ?  275 PRO C CD    1 
ATOM   13240 N  N     . TYR C 2 297 ? 105.070 78.630  111.306 1.00 38.10 ?  276 TYR C N     1 
ATOM   13241 C  CA    . TYR C 2 297 ? 103.859 78.008  111.861 1.00 38.96 ?  276 TYR C CA    1 
ATOM   13242 C  C     . TYR C 2 297 ? 102.568 78.675  111.369 1.00 39.71 ?  276 TYR C C     1 
ATOM   13243 O  O     . TYR C 2 297 ? 101.518 78.029  111.290 1.00 40.18 ?  276 TYR C O     1 
ATOM   13244 C  CB    . TYR C 2 297 ? 103.923 78.061  113.391 1.00 38.94 ?  276 TYR C CB    1 
ATOM   13245 C  CG    . TYR C 2 297 ? 102.813 77.374  114.159 1.00 39.64 ?  276 TYR C CG    1 
ATOM   13246 C  CD1   . TYR C 2 297 ? 102.841 75.997  114.393 1.00 40.43 ?  276 TYR C CD1   1 
ATOM   13247 C  CD2   . TYR C 2 297 ? 101.768 78.110  114.709 1.00 41.04 ?  276 TYR C CD2   1 
ATOM   13248 C  CE1   . TYR C 2 297 ? 101.828 75.368  115.119 1.00 41.69 ?  276 TYR C CE1   1 
ATOM   13249 C  CE2   . TYR C 2 297 ? 100.750 77.493  115.436 1.00 41.60 ?  276 TYR C CE2   1 
ATOM   13250 C  CZ    . TYR C 2 297 ? 100.788 76.125  115.641 1.00 41.92 ?  276 TYR C CZ    1 
ATOM   13251 O  OH    . TYR C 2 297 ? 99.784  75.521  116.368 1.00 42.52 ?  276 TYR C OH    1 
ATOM   13252 N  N     . PHE C 2 298 ? 102.642 79.963  111.054 1.00 39.85 ?  277 PHE C N     1 
ATOM   13253 C  CA    . PHE C 2 298 ? 101.471 80.699  110.591 1.00 40.77 ?  277 PHE C CA    1 
ATOM   13254 C  C     . PHE C 2 298 ? 101.557 80.955  109.095 1.00 41.95 ?  277 PHE C C     1 
ATOM   13255 O  O     . PHE C 2 298 ? 102.652 81.097  108.552 1.00 41.91 ?  277 PHE C O     1 
ATOM   13256 C  CB    . PHE C 2 298 ? 101.339 82.025  111.348 1.00 39.94 ?  277 PHE C CB    1 
ATOM   13257 C  CG    . PHE C 2 298 ? 101.109 81.866  112.826 1.00 39.09 ?  277 PHE C CG    1 
ATOM   13258 C  CD1   . PHE C 2 298 ? 102.125 82.142  113.733 1.00 37.84 ?  277 PHE C CD1   1 
ATOM   13259 C  CD2   . PHE C 2 298 ? 99.871  81.453  113.313 1.00 38.97 ?  277 PHE C CD2   1 
ATOM   13260 C  CE1   . PHE C 2 298 ? 101.920 82.004  115.104 1.00 37.46 ?  277 PHE C CE1   1 
ATOM   13261 C  CE2   . PHE C 2 298 ? 99.653  81.310  114.678 1.00 38.20 ?  277 PHE C CE2   1 
ATOM   13262 C  CZ    . PHE C 2 298 ? 100.681 81.587  115.578 1.00 37.91 ?  277 PHE C CZ    1 
ATOM   13263 N  N     . GLU C 2 299 ? 100.408 81.011  108.421 1.00 43.74 ?  278 GLU C N     1 
ATOM   13264 C  CA    . GLU C 2 299 ? 100.397 81.302  106.984 1.00 45.61 ?  278 GLU C CA    1 
ATOM   13265 C  C     . GLU C 2 299 ? 100.725 82.773  106.730 1.00 46.04 ?  278 GLU C C     1 
ATOM   13266 O  O     . GLU C 2 299 ? 100.425 83.637  107.554 1.00 45.88 ?  278 GLU C O     1 
ATOM   13267 C  CB    . GLU C 2 299 ? 99.057  80.934  106.337 1.00 46.43 ?  278 GLU C CB    1 
ATOM   13268 C  CG    . GLU C 2 299 ? 99.189  80.504  104.865 1.00 48.82 ?  278 GLU C CG    1 
ATOM   13269 C  CD    . GLU C 2 299 ? 97.891  80.618  104.080 1.00 51.86 ?  278 GLU C CD    1 
ATOM   13270 O  OE1   . GLU C 2 299 ? 97.907  80.305  102.868 1.00 53.35 ?  278 GLU C OE1   1 
ATOM   13271 O  OE2   . GLU C 2 299 ? 96.857  81.022  104.662 1.00 53.10 -1 278 GLU C OE2   1 
ATOM   13272 N  N     . GLU C 2 300 ? 101.356 83.044  105.588 1.00 47.16 ?  279 GLU C N     1 
ATOM   13273 C  CA    . GLU C 2 300 ? 101.723 84.406  105.187 1.00 47.75 ?  279 GLU C CA    1 
ATOM   13274 C  C     . GLU C 2 300 ? 100.498 85.295  104.924 1.00 47.71 ?  279 GLU C C     1 
ATOM   13275 O  O     . GLU C 2 300 ? 99.494  84.834  104.368 1.00 47.77 ?  279 GLU C O     1 
ATOM   13276 C  CB    . GLU C 2 300 ? 102.652 84.371  103.961 1.00 48.42 ?  279 GLU C CB    1 
ATOM   13277 C  CG    . GLU C 2 300 ? 102.145 83.516  102.794 1.00 50.63 ?  279 GLU C CG    1 
ATOM   13278 C  CD    . GLU C 2 300 ? 103.262 83.045  101.863 1.00 53.06 ?  279 GLU C CD    1 
ATOM   13279 O  OE1   . GLU C 2 300 ? 104.038 83.897  101.366 1.00 54.35 ?  279 GLU C OE1   1 
ATOM   13280 O  OE2   . GLU C 2 300 ? 103.355 81.820  101.619 1.00 53.32 -1 279 GLU C OE2   1 
ATOM   13281 N  N     . GLU C 2 301 ? 100.590 86.555  105.349 1.00 47.40 ?  280 GLU C N     1 
ATOM   13282 C  CA    . GLU C 2 301 ? 99.532  87.555  105.152 1.00 47.46 ?  280 GLU C CA    1 
ATOM   13283 C  C     . GLU C 2 301 ? 100.138 88.906  104.750 1.00 47.31 ?  280 GLU C C     1 
ATOM   13284 O  O     . GLU C 2 301 ? 101.306 89.175  105.040 1.00 47.21 ?  280 GLU C O     1 
ATOM   13285 C  CB    . GLU C 2 301 ? 98.706  87.735  106.433 1.00 47.19 ?  280 GLU C CB    1 
ATOM   13286 C  CG    . GLU C 2 301 ? 97.970  86.491  106.934 1.00 47.14 ?  280 GLU C CG    1 
ATOM   13287 C  CD    . GLU C 2 301 ? 97.613  86.583  108.415 1.00 47.21 ?  280 GLU C CD    1 
ATOM   13288 O  OE1   . GLU C 2 301 ? 96.421  86.778  108.727 1.00 46.97 ?  280 GLU C OE1   1 
ATOM   13289 O  OE2   . GLU C 2 301 ? 98.528  86.473  109.267 1.00 46.13 -1 280 GLU C OE2   1 
ATOM   13290 N  N     . ASP C 2 302 ? 99.343  89.749  104.091 1.00 47.15 ?  281 ASP C N     1 
ATOM   13291 C  CA    . ASP C 2 302 ? 99.792  91.093  103.712 1.00 47.04 ?  281 ASP C CA    1 
ATOM   13292 C  C     . ASP C 2 302 ? 99.821  92.020  104.931 1.00 46.05 ?  281 ASP C C     1 
ATOM   13293 O  O     . ASP C 2 302 ? 98.787  92.260  105.564 1.00 46.10 ?  281 ASP C O     1 
ATOM   13294 C  CB    . ASP C 2 302 ? 98.894  91.697  102.615 1.00 47.66 ?  281 ASP C CB    1 
ATOM   13295 C  CG    . ASP C 2 302 ? 99.112  91.059  101.240 1.00 49.53 ?  281 ASP C CG    1 
ATOM   13296 O  OD1   . ASP C 2 302 ? 100.258 90.676  100.915 1.00 50.58 ?  281 ASP C OD1   1 
ATOM   13297 O  OD2   . ASP C 2 302 ? 98.127  90.966  100.468 1.00 51.14 -1 281 ASP C OD2   1 
ATOM   13298 N  N     . ILE C 2 303 ? 101.010 92.521  105.259 1.00 44.96 ?  282 ILE C N     1 
ATOM   13299 C  CA    . ILE C 2 303 ? 101.195 93.480  106.354 1.00 43.99 ?  282 ILE C CA    1 
ATOM   13300 C  C     . ILE C 2 303 ? 100.933 94.901  105.845 1.00 43.53 ?  282 ILE C C     1 
ATOM   13301 O  O     . ILE C 2 303 ? 101.217 95.203  104.684 1.00 43.52 ?  282 ILE C O     1 
ATOM   13302 C  CB    . ILE C 2 303 ? 102.629 93.386  106.954 1.00 43.84 ?  282 ILE C CB    1 
ATOM   13303 C  CG1   . ILE C 2 303 ? 102.958 91.947  107.395 1.00 43.91 ?  282 ILE C CG1   1 
ATOM   13304 C  CG2   . ILE C 2 303 ? 102.833 94.397  108.096 1.00 43.55 ?  282 ILE C CG2   1 
ATOM   13305 C  CD1   . ILE C 2 303 ? 102.015 91.350  108.444 1.00 42.76 ?  282 ILE C CD1   1 
ATOM   13306 N  N     . ASN C 2 304 ? 100.384 95.759  106.705 1.00 42.51 ?  283 ASN C N     1 
ATOM   13307 C  CA    . ASN C 2 304 ? 100.139 97.159  106.357 1.00 41.93 ?  283 ASN C CA    1 
ATOM   13308 C  C     . ASN C 2 304 ? 101.402 97.790  105.750 1.00 41.78 ?  283 ASN C C     1 
ATOM   13309 O  O     . ASN C 2 304 ? 102.456 97.806  106.401 1.00 41.13 ?  283 ASN C O     1 
ATOM   13310 C  CB    . ASN C 2 304 ? 99.684  97.945  107.597 1.00 41.83 ?  283 ASN C CB    1 
ATOM   13311 C  CG    . ASN C 2 304 ? 98.951  99.241  107.250 1.00 41.27 ?  283 ASN C CG    1 
ATOM   13312 O  OD1   . ASN C 2 304 ? 99.377  100.007 106.388 1.00 41.28 ?  283 ASN C OD1   1 
ATOM   13313 N  ND2   . ASN C 2 304 ? 97.846  99.489  107.936 1.00 40.67 ?  283 ASN C ND2   1 
ATOM   13314 N  N     . PRO C 2 305 ? 101.308 98.293  104.495 1.00 41.74 ?  284 PRO C N     1 
ATOM   13315 C  CA    . PRO C 2 305 ? 102.495 98.843  103.821 1.00 41.82 ?  284 PRO C CA    1 
ATOM   13316 C  C     . PRO C 2 305 ? 103.079 100.067 104.534 1.00 41.56 ?  284 PRO C C     1 
ATOM   13317 O  O     . PRO C 2 305 ? 104.261 100.371 104.363 1.00 41.46 ?  284 PRO C O     1 
ATOM   13318 C  CB    . PRO C 2 305 ? 101.981 99.208  102.414 1.00 42.14 ?  284 PRO C CB    1 
ATOM   13319 C  CG    . PRO C 2 305 ? 100.508 99.321  102.549 1.00 42.59 ?  284 PRO C CG    1 
ATOM   13320 C  CD    . PRO C 2 305 ? 100.113 98.342  103.629 1.00 42.05 ?  284 PRO C CD    1 
ATOM   13321 N  N     . ILE C 2 306 ? 102.258 100.744 105.333 1.00 41.19 ?  285 ILE C N     1 
ATOM   13322 C  CA    . ILE C 2 306 ? 102.710 101.859 106.165 1.00 41.47 ?  285 ILE C CA    1 
ATOM   13323 C  C     . ILE C 2 306 ? 103.787 101.385 107.149 1.00 41.71 ?  285 ILE C C     1 
ATOM   13324 O  O     . ILE C 2 306 ? 104.828 102.023 107.296 1.00 41.38 ?  285 ILE C O     1 
ATOM   13325 C  CB    . ILE C 2 306 ? 101.533 102.497 106.949 1.00 41.22 ?  285 ILE C CB    1 
ATOM   13326 C  CG1   . ILE C 2 306 ? 100.491 103.082 105.986 1.00 41.27 ?  285 ILE C CG1   1 
ATOM   13327 C  CG2   . ILE C 2 306 ? 102.037 103.555 107.928 1.00 40.37 ?  285 ILE C CG2   1 
ATOM   13328 C  CD1   . ILE C 2 306 ? 99.151  103.384 106.641 1.00 41.85 ?  285 ILE C CD1   1 
ATOM   13329 N  N     . VAL C 2 307 ? 103.519 100.260 107.811 1.00 42.33 ?  286 VAL C N     1 
ATOM   13330 C  CA    . VAL C 2 307 ? 104.456 99.653  108.762 1.00 43.36 ?  286 VAL C CA    1 
ATOM   13331 C  C     . VAL C 2 307 ? 105.753 99.196  108.081 1.00 44.51 ?  286 VAL C C     1 
ATOM   13332 O  O     . VAL C 2 307 ? 106.827 99.289  108.671 1.00 44.57 ?  286 VAL C O     1 
ATOM   13333 C  CB    . VAL C 2 307 ? 103.782 98.506  109.553 1.00 42.97 ?  286 VAL C CB    1 
ATOM   13334 C  CG1   . VAL C 2 307 ? 104.816 97.634  110.284 1.00 42.86 ?  286 VAL C CG1   1 
ATOM   13335 C  CG2   . VAL C 2 307 ? 102.782 99.091  110.532 1.00 41.93 ?  286 VAL C CG2   1 
ATOM   13336 N  N     . LEU C 2 308 ? 105.636 98.731  106.837 1.00 46.21 ?  287 LEU C N     1 
ATOM   13337 C  CA    . LEU C 2 308 ? 106.788 98.331  106.015 1.00 47.66 ?  287 LEU C CA    1 
ATOM   13338 C  C     . LEU C 2 308 ? 107.653 99.524  105.610 1.00 48.82 ?  287 LEU C C     1 
ATOM   13339 O  O     . LEU C 2 308 ? 108.882 99.404  105.521 1.00 49.02 ?  287 LEU C O     1 
ATOM   13340 C  CB    . LEU C 2 308 ? 106.322 97.554  104.775 1.00 47.95 ?  287 LEU C CB    1 
ATOM   13341 C  CG    . LEU C 2 308 ? 106.203 96.023  104.869 1.00 48.23 ?  287 LEU C CG    1 
ATOM   13342 C  CD1   . LEU C 2 308 ? 105.951 95.504  106.292 1.00 48.10 ?  287 LEU C CD1   1 
ATOM   13343 C  CD2   . LEU C 2 308 ? 105.151 95.492  103.899 1.00 48.81 ?  287 LEU C CD2   1 
ATOM   13344 N  N     . ASN C 2 309 ? 107.007 100.665 105.365 1.00 49.80 ?  288 ASN C N     1 
ATOM   13345 C  CA    . ASN C 2 309 ? 107.708 101.934 105.194 1.00 51.09 ?  288 ASN C CA    1 
ATOM   13346 C  C     . ASN C 2 309 ? 108.310 102.455 106.503 1.00 51.08 ?  288 ASN C C     1 
ATOM   13347 O  O     . ASN C 2 309 ? 109.278 103.214 106.484 1.00 51.41 ?  288 ASN C O     1 
ATOM   13348 C  CB    . ASN C 2 309 ? 106.798 102.987 104.556 1.00 51.37 ?  288 ASN C CB    1 
ATOM   13349 C  CG    . ASN C 2 309 ? 106.703 102.837 103.051 1.00 53.22 ?  288 ASN C CG    1 
ATOM   13350 O  OD1   . ASN C 2 309 ? 106.513 101.732 102.530 1.00 54.39 ?  288 ASN C OD1   1 
ATOM   13351 N  ND2   . ASN C 2 309 ? 106.837 103.951 102.339 1.00 54.70 ?  288 ASN C ND2   1 
ATOM   13352 N  N     . GLY C 2 310 ? 107.731 102.042 107.631 1.00 51.25 ?  289 GLY C N     1 
ATOM   13353 C  CA    . GLY C 2 310 ? 108.280 102.339 108.955 1.00 51.35 ?  289 GLY C CA    1 
ATOM   13354 C  C     . GLY C 2 310 ? 109.623 101.669 109.216 1.00 51.86 ?  289 GLY C C     1 
ATOM   13355 O  O     . GLY C 2 310 ? 110.386 102.110 110.083 1.00 51.49 ?  289 GLY C O     1 
ATOM   13356 N  N     . LEU C 2 311 ? 109.911 100.603 108.468 1.00 52.45 ?  290 LEU C N     1 
ATOM   13357 C  CA    . LEU C 2 311 ? 111.190 99.895  108.564 1.00 52.99 ?  290 LEU C CA    1 
ATOM   13358 C  C     . LEU C 2 311 ? 112.245 100.519 107.648 1.00 53.65 ?  290 LEU C C     1 
ATOM   13359 O  O     . LEU C 2 311 ? 112.172 100.413 106.417 1.00 54.22 ?  290 LEU C O     1 
ATOM   13360 C  CB    . LEU C 2 311 ? 111.013 98.409  108.236 1.00 53.08 ?  290 LEU C CB    1 
ATOM   13361 C  CG    . LEU C 2 311 ? 110.303 97.500  109.243 1.00 53.33 ?  290 LEU C CG    1 
ATOM   13362 C  CD1   . LEU C 2 311 ? 109.901 96.190  108.581 1.00 53.79 ?  290 LEU C CD1   1 
ATOM   13363 C  CD2   . LEU C 2 311 ? 111.174 97.238  110.474 1.00 53.22 ?  290 LEU C CD2   1 
ATOM   13364 N  N     . LYS C 2 330 ? 138.282 110.925 115.648 1.00 58.93 ?  309 LYS C N     1 
ATOM   13365 C  CA    . LYS C 2 330 ? 139.735 110.803 115.631 1.00 61.98 ?  309 LYS C CA    1 
ATOM   13366 C  C     . LYS C 2 330 ? 140.231 110.265 114.293 1.00 61.97 ?  309 LYS C C     1 
ATOM   13367 O  O     . LYS C 2 330 ? 139.578 109.432 113.665 1.00 59.24 ?  309 LYS C O     1 
ATOM   13368 C  CB    . LYS C 2 330 ? 140.211 109.896 116.768 1.00 60.82 ?  309 LYS C CB    1 
ATOM   13369 C  CG    . LYS C 2 330 ? 139.882 110.413 118.158 1.00 60.80 ?  309 LYS C CG    1 
ATOM   13370 C  CD    . LYS C 2 330 ? 140.774 111.586 118.534 1.00 60.28 ?  309 LYS C CD    1 
ATOM   13371 C  CE    . LYS C 2 330 ? 141.613 111.275 119.763 1.00 62.15 ?  309 LYS C CE    1 
ATOM   13372 N  NZ    . LYS C 2 330 ? 140.900 110.379 120.714 1.00 62.59 1  309 LYS C NZ    1 
ATOM   13373 N  N     . ALA C 2 331 ? 141.391 110.751 113.863 1.00 55.97 ?  310 ALA C N     1 
ATOM   13374 C  CA    . ALA C 2 331 ? 142.020 110.322 112.626 1.00 53.20 ?  310 ALA C CA    1 
ATOM   13375 C  C     . ALA C 2 331 ? 143.374 109.693 112.923 1.00 52.13 ?  310 ALA C C     1 
ATOM   13376 O  O     . ALA C 2 331 ? 144.015 110.008 113.931 1.00 53.07 ?  310 ALA C O     1 
ATOM   13377 C  CB    . ALA C 2 331 ? 142.189 111.495 111.655 1.00 51.98 ?  310 ALA C CB    1 
ATOM   13378 N  N     . THR C 2 332 ? 143.799 108.793 112.038 1.00 45.82 ?  311 THR C N     1 
ATOM   13379 C  CA    . THR C 2 332 ? 145.089 108.136 112.191 1.00 46.85 ?  311 THR C CA    1 
ATOM   13380 C  C     . THR C 2 332 ? 146.216 109.161 112.194 1.00 43.12 ?  311 THR C C     1 
ATOM   13381 O  O     . THR C 2 332 ? 146.197 110.134 111.436 1.00 48.26 ?  311 THR C O     1 
ATOM   13382 C  CB    . THR C 2 332 ? 145.296 107.111 111.074 1.00 45.72 ?  311 THR C CB    1 
ATOM   13383 O  OG1   . THR C 2 332 ? 146.463 106.325 111.346 1.00 46.36 ?  311 THR C OG1   1 
ATOM   13384 C  CG2   . THR C 2 332 ? 145.430 107.801 109.728 1.00 44.89 ?  311 THR C CG2   1 
ATOM   13385 N  N     . VAL C 2 333 ? 147.197 108.940 113.065 1.00 42.01 ?  312 VAL C N     1 
ATOM   13386 C  CA    . VAL C 2 333 ? 148.246 109.912 113.350 1.00 38.55 ?  312 VAL C CA    1 
ATOM   13387 C  C     . VAL C 2 333 ? 149.586 109.297 112.970 1.00 41.18 ?  312 VAL C C     1 
ATOM   13388 O  O     . VAL C 2 333 ? 149.942 108.215 113.453 1.00 46.85 ?  312 VAL C O     1 
ATOM   13389 C  CB    . VAL C 2 333 ? 148.237 110.337 114.825 1.00 37.39 ?  312 VAL C CB    1 
ATOM   13390 C  CG1   . VAL C 2 333 ? 149.527 111.059 115.180 1.00 40.81 ?  312 VAL C CG1   1 
ATOM   13391 C  CG2   . VAL C 2 333 ? 147.026 111.202 115.127 1.00 39.47 ?  312 VAL C CG2   1 
ATOM   13392 N  N     . GLU C 2 334 ? 150.334 109.985 112.104 1.00 34.01 ?  313 GLU C N     1 
ATOM   13393 C  CA    . GLU C 2 334 ? 151.723 109.633 111.864 1.00 34.45 ?  313 GLU C CA    1 
ATOM   13394 C  C     . GLU C 2 334 ? 152.636 110.777 112.294 1.00 37.55 ?  313 GLU C C     1 
ATOM   13395 O  O     . GLU C 2 334 ? 152.274 111.950 112.158 1.00 40.51 ?  313 GLU C O     1 
ATOM   13396 C  CB    . GLU C 2 334 ? 152.002 109.316 110.390 1.00 34.27 ?  313 GLU C CB    1 
ATOM   13397 C  CG    . GLU C 2 334 ? 151.091 108.288 109.756 1.00 38.73 ?  313 GLU C CG    1 
ATOM   13398 C  CD    . GLU C 2 334 ? 151.503 107.969 108.331 1.00 42.14 ?  313 GLU C CD    1 
ATOM   13399 O  OE1   . GLU C 2 334 ? 152.554 107.320 108.147 1.00 40.76 ?  313 GLU C OE1   1 
ATOM   13400 O  OE2   . GLU C 2 334 ? 150.788 108.378 107.393 1.00 39.96 -1 313 GLU C OE2   1 
ATOM   13401 N  N     . PRO C 2 335 ? 153.820 110.473 112.817 1.00 33.56 ?  314 PRO C N     1 
ATOM   13402 C  CA    . PRO C 2 335 ? 154.779 111.534 113.136 1.00 34.05 ?  314 PRO C CA    1 
ATOM   13403 C  C     . PRO C 2 335 ? 155.336 112.164 111.868 1.00 35.93 ?  314 PRO C C     1 
ATOM   13404 O  O     . PRO C 2 335 ? 155.338 111.574 110.786 1.00 36.72 ?  314 PRO C O     1 
ATOM   13405 C  CB    . PRO C 2 335 ? 155.873 110.812 113.931 1.00 36.78 ?  314 PRO C CB    1 
ATOM   13406 C  CG    . PRO C 2 335 ? 155.288 109.472 114.293 1.00 33.20 ?  314 PRO C CG    1 
ATOM   13407 C  CD    . PRO C 2 335 ? 154.318 109.146 113.207 1.00 33.09 ?  314 PRO C CD    1 
ATOM   13408 N  N     . LEU C 2 336 ? 155.817 113.394 112.017 1.00 31.29 ?  315 LEU C N     1 
ATOM   13409 C  CA    . LEU C 2 336 ? 156.391 114.138 110.906 1.00 25.88 ?  315 LEU C CA    1 
ATOM   13410 C  C     . LEU C 2 336 ? 157.854 113.761 110.722 1.00 28.32 ?  315 LEU C C     1 
ATOM   13411 O  O     . LEU C 2 336 ? 158.651 113.857 111.661 1.00 26.34 ?  315 LEU C O     1 
ATOM   13412 C  CB    . LEU C 2 336 ? 156.262 115.644 111.137 1.00 25.22 ?  315 LEU C CB    1 
ATOM   13413 C  CG    . LEU C 2 336 ? 154.945 116.272 110.685 1.00 26.15 ?  315 LEU C CG    1 
ATOM   13414 C  CD1   . LEU C 2 336 ? 154.932 117.758 110.992 1.00 26.32 ?  315 LEU C CD1   1 
ATOM   13415 C  CD2   . LEU C 2 336 ? 154.745 116.028 109.200 1.00 21.64 ?  315 LEU C CD2   1 
ATOM   13416 N  N     . LYS C 2 337 ? 158.200 113.332 109.513 1.00 24.69 ?  316 LYS C N     1 
ATOM   13417 C  CA    . LYS C 2 337 ? 159.579 113.041 109.163 1.00 25.14 ?  316 LYS C CA    1 
ATOM   13418 C  C     . LYS C 2 337 ? 160.290 114.319 108.729 1.00 19.78 ?  316 LYS C C     1 
ATOM   13419 O  O     . LYS C 2 337 ? 159.664 115.309 108.349 1.00 30.21 ?  316 LYS C O     1 
ATOM   13420 C  CB    . LYS C 2 337 ? 159.647 111.999 108.046 1.00 29.25 ?  316 LYS C CB    1 
ATOM   13421 C  CG    . LYS C 2 337 ? 158.577 110.924 108.127 1.00 28.02 ?  316 LYS C CG    1 
ATOM   13422 C  CD    . LYS C 2 337 ? 159.151 109.603 108.609 1.00 27.52 ?  316 LYS C CD    1 
ATOM   13423 C  CE    . LYS C 2 337 ? 158.155 108.851 109.474 1.00 32.76 ?  316 LYS C CE    1 
ATOM   13424 N  NZ    . LYS C 2 337 ? 158.791 107.719 110.202 1.00 30.53 1  316 LYS C NZ    1 
ATOM   13425 N  N     . ASP C 2 338 ? 161.621 114.284 108.795 1.00 29.74 ?  317 ASP C N     1 
ATOM   13426 C  CA    . ASP C 2 338 ? 162.412 115.425 108.354 1.00 26.29 ?  317 ASP C CA    1 
ATOM   13427 C  C     . ASP C 2 338 ? 162.290 115.668 106.857 1.00 29.71 ?  317 ASP C C     1 
ATOM   13428 O  O     . ASP C 2 338 ? 162.589 116.775 106.395 1.00 21.95 ?  317 ASP C O     1 
ATOM   13429 C  CB    . ASP C 2 338 ? 163.880 115.227 108.734 1.00 25.78 ?  317 ASP C CB    1 
ATOM   13430 C  CG    . ASP C 2 338 ? 164.049 114.690 110.140 1.00 35.15 ?  317 ASP C CG    1 
ATOM   13431 O  OD1   . ASP C 2 338 ? 163.493 113.611 110.436 1.00 32.75 ?  317 ASP C OD1   1 
ATOM   13432 O  OD2   . ASP C 2 338 ? 164.737 115.347 110.950 1.00 36.30 -1 317 ASP C OD2   1 
ATOM   13433 N  N     . ASP C 2 339 ? 161.856 114.668 106.092 1.00 26.99 ?  318 ASP C N     1 
ATOM   13434 C  CA    . ASP C 2 339 ? 161.679 114.812 104.654 1.00 24.15 ?  318 ASP C CA    1 
ATOM   13435 C  C     . ASP C 2 339 ? 160.344 115.437 104.277 1.00 20.41 ?  318 ASP C C     1 
ATOM   13436 O  O     . ASP C 2 339 ? 160.161 115.814 103.114 1.00 28.59 ?  318 ASP C O     1 
ATOM   13437 C  CB    . ASP C 2 339 ? 161.816 113.449 103.966 1.00 23.02 ?  318 ASP C CB    1 
ATOM   13438 C  CG    . ASP C 2 339 ? 162.845 112.561 104.636 1.00 32.33 ?  318 ASP C CG    1 
ATOM   13439 O  OD1   . ASP C 2 339 ? 162.447 111.580 105.300 1.00 34.56 ?  318 ASP C OD1   1 
ATOM   13440 O  OD2   . ASP C 2 339 ? 164.054 112.844 104.499 1.00 32.78 -1 318 ASP C OD2   1 
ATOM   13441 N  N     . ASP C 2 340 ? 159.412 115.557 105.220 1.00 18.60 ?  319 ASP C N     1 
ATOM   13442 C  CA    . ASP C 2 340 ? 158.134 116.208 104.970 1.00 13.68 ?  319 ASP C CA    1 
ATOM   13443 C  C     . ASP C 2 340 ? 158.225 117.724 105.045 1.00 14.05 ?  319 ASP C C     1 
ATOM   13444 O  O     . ASP C 2 340 ? 157.244 118.407 104.734 1.00 30.27 ?  319 ASP C O     1 
ATOM   13445 C  CB    . ASP C 2 340 ? 157.080 115.707 105.962 1.00 12.38 ?  319 ASP C CB    1 
ATOM   13446 C  CG    . ASP C 2 340 ? 157.080 114.200 106.101 1.00 24.62 ?  319 ASP C CG    1 
ATOM   13447 O  OD1   . ASP C 2 340 ? 157.189 113.506 105.069 1.00 25.90 ?  319 ASP C OD1   1 
ATOM   13448 O  OD2   . ASP C 2 340 ? 156.965 113.708 107.242 1.00 30.97 -1 319 ASP C OD2   1 
ATOM   13449 N  N     . PHE C 2 341 ? 159.371 118.262 105.453 1.00 14.34 ?  320 PHE C N     1 
ATOM   13450 C  CA    . PHE C 2 341 ? 159.585 119.698 105.546 1.00 3.83  ?  320 PHE C CA    1 
ATOM   13451 C  C     . PHE C 2 341 ? 160.317 120.256 104.333 1.00 6.43  ?  320 PHE C C     1 
ATOM   13452 O  O     . PHE C 2 341 ? 160.642 121.447 104.313 1.00 11.38 ?  320 PHE C O     1 
ATOM   13453 C  CB    . PHE C 2 341 ? 160.362 120.028 106.820 1.00 8.01  ?  320 PHE C CB    1 
ATOM   13454 C  CG    . PHE C 2 341 ? 159.551 119.898 108.076 1.00 9.69  ?  320 PHE C CG    1 
ATOM   13455 C  CD1   . PHE C 2 341 ? 158.835 120.975 108.567 1.00 6.44  ?  320 PHE C CD1   1 
ATOM   13456 C  CD2   . PHE C 2 341 ? 159.506 118.699 108.766 1.00 7.94  ?  320 PHE C CD2   1 
ATOM   13457 C  CE1   . PHE C 2 341 ? 158.090 120.859 109.722 1.00 10.55 ?  320 PHE C CE1   1 
ATOM   13458 C  CE2   . PHE C 2 341 ? 158.760 118.578 109.921 1.00 8.92  ?  320 PHE C CE2   1 
ATOM   13459 C  CZ    . PHE C 2 341 ? 158.050 119.660 110.399 1.00 6.02  ?  320 PHE C CZ    1 
ATOM   13460 N  N     . TYR C 2 342 ? 160.583 119.427 103.328 1.00 6.07  ?  321 TYR C N     1 
ATOM   13461 C  CA    . TYR C 2 342 ? 161.317 119.838 102.142 1.00 12.59 ?  321 TYR C CA    1 
ATOM   13462 C  C     . TYR C 2 342 ? 160.569 119.380 100.901 1.00 16.10 ?  321 TYR C C     1 
ATOM   13463 O  O     . TYR C 2 342 ? 160.011 118.279 100.872 1.00 16.79 ?  321 TYR C O     1 
ATOM   13464 C  CB    . TYR C 2 342 ? 162.738 119.264 102.143 1.00 6.93  ?  321 TYR C CB    1 
ATOM   13465 C  CG    . TYR C 2 342 ? 163.580 119.741 103.302 1.00 3.43  ?  321 TYR C CG    1 
ATOM   13466 C  CD1   . TYR C 2 342 ? 163.579 119.059 104.511 1.00 8.24  ?  321 TYR C CD1   1 
ATOM   13467 C  CD2   . TYR C 2 342 ? 164.366 120.878 103.191 1.00 11.16 ?  321 TYR C CD2   1 
ATOM   13468 C  CE1   . TYR C 2 342 ? 164.344 119.492 105.575 1.00 12.34 ?  321 TYR C CE1   1 
ATOM   13469 C  CE2   . TYR C 2 342 ? 165.134 121.319 104.250 1.00 13.11 ?  321 TYR C CE2   1 
ATOM   13470 C  CZ    . TYR C 2 342 ? 165.120 120.623 105.439 1.00 17.37 ?  321 TYR C CZ    1 
ATOM   13471 O  OH    . TYR C 2 342 ? 165.884 121.062 106.495 1.00 21.45 ?  321 TYR C OH    1 
ATOM   13472 N  N     . PHE C 2 343 ? 160.557 120.231 99.880  1.00 12.77 ?  322 PHE C N     1 
ATOM   13473 C  CA    . PHE C 2 343 ? 159.828 119.941 98.652  1.00 15.81 ?  322 PHE C CA    1 
ATOM   13474 C  C     . PHE C 2 343 ? 160.648 120.346 97.432  1.00 24.63 ?  322 PHE C C     1 
ATOM   13475 O  O     . PHE C 2 343 ? 161.595 121.123 97.536  1.00 24.06 ?  322 PHE C O     1 
ATOM   13476 C  CB    . PHE C 2 343 ? 158.465 120.652 98.627  1.00 11.49 ?  322 PHE C CB    1 
ATOM   13477 C  CG    . PHE C 2 343 ? 157.780 120.726 99.968  1.00 8.46  ?  322 PHE C CG    1 
ATOM   13478 C  CD1   . PHE C 2 343 ? 158.159 121.664 100.918 1.00 8.80  ?  322 PHE C CD1   1 
ATOM   13479 C  CD2   . PHE C 2 343 ? 156.768 119.837 100.284 1.00 13.46 ?  322 PHE C CD2   1 
ATOM   13480 C  CE1   . PHE C 2 343 ? 157.533 121.716 102.145 1.00 5.58  ?  322 PHE C CE1   1 
ATOM   13481 C  CE2   . PHE C 2 343 ? 156.141 119.887 101.510 1.00 8.14  ?  322 PHE C CE2   1 
ATOM   13482 C  CZ    . PHE C 2 343 ? 156.523 120.825 102.441 1.00 2.41  ?  322 PHE C CZ    1 
ATOM   13483 N  N     . ASP D 2 37  ? 119.944 108.973 145.608 1.00 32.44 ?  16  ASP D N     1 
ATOM   13484 C  CA    . ASP D 2 37  ? 120.503 110.314 145.417 1.00 32.83 ?  16  ASP D CA    1 
ATOM   13485 C  C     . ASP D 2 37  ? 121.613 110.383 144.370 1.00 31.65 ?  16  ASP D C     1 
ATOM   13486 O  O     . ASP D 2 37  ? 122.080 111.478 144.045 1.00 32.65 ?  16  ASP D O     1 
ATOM   13487 C  CB    . ASP D 2 37  ? 121.077 110.856 146.735 1.00 33.73 ?  16  ASP D CB    1 
ATOM   13488 C  CG    . ASP D 2 37  ? 120.017 111.082 147.803 1.00 36.81 ?  16  ASP D CG    1 
ATOM   13489 O  OD1   . ASP D 2 37  ? 120.404 111.168 148.994 1.00 39.69 ?  16  ASP D OD1   1 
ATOM   13490 O  OD2   . ASP D 2 37  ? 118.813 111.168 147.470 1.00 39.67 -1 16  ASP D OD2   1 
ATOM   13491 N  N     . PHE D 2 38  ? 122.045 109.237 143.846 1.00 29.55 ?  17  PHE D N     1 
ATOM   13492 C  CA    . PHE D 2 38  ? 123.310 109.206 143.112 1.00 27.75 ?  17  PHE D CA    1 
ATOM   13493 C  C     . PHE D 2 38  ? 123.368 108.361 141.829 1.00 26.21 ?  17  PHE D C     1 
ATOM   13494 O  O     . PHE D 2 38  ? 124.253 108.565 141.006 1.00 25.93 ?  17  PHE D O     1 
ATOM   13495 C  CB    . PHE D 2 38  ? 124.450 108.799 144.074 1.00 27.37 ?  17  PHE D CB    1 
ATOM   13496 C  CG    . PHE D 2 38  ? 124.253 107.446 144.705 1.00 27.32 ?  17  PHE D CG    1 
ATOM   13497 C  CD1   . PHE D 2 38  ? 124.645 106.290 144.037 1.00 27.01 ?  17  PHE D CD1   1 
ATOM   13498 C  CD2   . PHE D 2 38  ? 123.676 107.324 145.963 1.00 28.02 ?  17  PHE D CD2   1 
ATOM   13499 C  CE1   . PHE D 2 38  ? 124.459 105.034 144.613 1.00 27.66 ?  17  PHE D CE1   1 
ATOM   13500 C  CE2   . PHE D 2 38  ? 123.483 106.075 146.540 1.00 27.68 ?  17  PHE D CE2   1 
ATOM   13501 C  CZ    . PHE D 2 38  ? 123.877 104.926 145.861 1.00 27.47 ?  17  PHE D CZ    1 
ATOM   13502 N  N     . THR D 2 39  ? 122.441 107.423 141.659 1.00 24.88 ?  18  THR D N     1 
ATOM   13503 C  CA    . THR D 2 39  ? 122.526 106.454 140.554 1.00 23.81 ?  18  THR D CA    1 
ATOM   13504 C  C     . THR D 2 39  ? 122.432 107.079 139.151 1.00 23.56 ?  18  THR D C     1 
ATOM   13505 O  O     . THR D 2 39  ? 123.180 106.709 138.245 1.00 23.02 ?  18  THR D O     1 
ATOM   13506 C  CB    . THR D 2 39  ? 121.539 105.276 140.748 1.00 23.40 ?  18  THR D CB    1 
ATOM   13507 O  OG1   . THR D 2 39  ? 122.083 104.367 141.713 1.00 23.77 ?  18  THR D OG1   1 
ATOM   13508 C  CG2   . THR D 2 39  ? 121.316 104.512 139.454 1.00 22.31 ?  18  THR D CG2   1 
ATOM   13509 N  N     . GLN D 2 40  ? 121.533 108.037 138.966 1.00 23.78 ?  19  GLN D N     1 
ATOM   13510 C  CA    . GLN D 2 40  ? 121.435 108.688 137.656 1.00 23.88 ?  19  GLN D CA    1 
ATOM   13511 C  C     . GLN D 2 40  ? 122.694 109.486 137.310 1.00 24.09 ?  19  GLN D C     1 
ATOM   13512 O  O     . GLN D 2 40  ? 123.170 109.439 136.184 1.00 23.15 ?  19  GLN D O     1 
ATOM   13513 C  CB    . GLN D 2 40  ? 120.170 109.542 137.548 1.00 24.53 ?  19  GLN D CB    1 
ATOM   13514 C  CG    . GLN D 2 40  ? 118.908 108.694 137.540 1.00 24.06 ?  19  GLN D CG    1 
ATOM   13515 C  CD    . GLN D 2 40  ? 117.701 109.420 136.993 1.00 25.83 ?  19  GLN D CD    1 
ATOM   13516 O  OE1   . GLN D 2 40  ? 117.825 110.486 136.395 1.00 25.90 ?  19  GLN D OE1   1 
ATOM   13517 N  NE2   . GLN D 2 40  ? 116.519 108.829 137.176 1.00 23.56 ?  19  GLN D NE2   1 
ATOM   13518 N  N     . MET D 2 41  ? 123.258 110.179 138.293 1.00 24.07 ?  20  MET D N     1 
ATOM   13519 C  CA    . MET D 2 41  ? 124.538 110.860 138.097 1.00 25.53 ?  20  MET D CA    1 
ATOM   13520 C  C     . MET D 2 41  ? 125.667 109.892 137.687 1.00 24.24 ?  20  MET D C     1 
ATOM   13521 O  O     . MET D 2 41  ? 126.445 110.190 136.776 1.00 23.16 ?  20  MET D O     1 
ATOM   13522 C  CB    . MET D 2 41  ? 124.915 111.639 139.361 1.00 26.79 ?  20  MET D CB    1 
ATOM   13523 C  CG    . MET D 2 41  ? 126.243 112.367 139.290 1.00 32.62 ?  20  MET D CG    1 
ATOM   13524 S  SD    . MET D 2 41  ? 126.717 112.953 140.934 1.00 44.01 ?  20  MET D SD    1 
ATOM   13525 C  CE    . MET D 2 41  ? 128.502 113.054 140.765 1.00 41.93 ?  20  MET D CE    1 
ATOM   13526 N  N     . PHE D 2 42  ? 125.746 108.733 138.344 1.00 23.31 ?  21  PHE D N     1 
ATOM   13527 C  CA    . PHE D 2 42  ? 126.771 107.749 137.992 1.00 23.44 ?  21  PHE D CA    1 
ATOM   13528 C  C     . PHE D 2 42  ? 126.499 107.097 136.652 1.00 23.55 ?  21  PHE D C     1 
ATOM   13529 O  O     . PHE D 2 42  ? 127.430 106.778 135.921 1.00 23.74 ?  21  PHE D O     1 
ATOM   13530 C  CB    . PHE D 2 42  ? 126.948 106.698 139.090 1.00 22.97 ?  21  PHE D CB    1 
ATOM   13531 C  CG    . PHE D 2 42  ? 127.897 107.127 140.153 1.00 23.86 ?  21  PHE D CG    1 
ATOM   13532 C  CD1   . PHE D 2 42  ? 129.237 106.752 140.099 1.00 24.55 ?  21  PHE D CD1   1 
ATOM   13533 C  CD2   . PHE D 2 42  ? 127.470 107.943 141.184 1.00 24.06 ?  21  PHE D CD2   1 
ATOM   13534 C  CE1   . PHE D 2 42  ? 130.133 107.172 141.085 1.00 25.78 ?  21  PHE D CE1   1 
ATOM   13535 C  CE2   . PHE D 2 42  ? 128.361 108.368 142.174 1.00 25.25 ?  21  PHE D CE2   1 
ATOM   13536 C  CZ    . PHE D 2 42  ? 129.686 107.988 142.122 1.00 25.79 ?  21  PHE D CZ    1 
ATOM   13537 N  N     . TYR D 2 43  ? 125.218 106.920 136.331 1.00 24.08 ?  22  TYR D N     1 
ATOM   13538 C  CA    . TYR D 2 43  ? 124.825 106.445 135.015 1.00 24.74 ?  22  TYR D CA    1 
ATOM   13539 C  C     . TYR D 2 43  ? 125.442 107.346 133.943 1.00 25.72 ?  22  TYR D C     1 
ATOM   13540 O  O     . TYR D 2 43  ? 126.082 106.863 133.004 1.00 25.56 ?  22  TYR D O     1 
ATOM   13541 C  CB    . TYR D 2 43  ? 123.297 106.394 134.855 1.00 24.90 ?  22  TYR D CB    1 
ATOM   13542 C  CG    . TYR D 2 43  ? 122.887 106.063 133.427 1.00 24.38 ?  22  TYR D CG    1 
ATOM   13543 C  CD1   . TYR D 2 43  ? 122.720 104.744 133.022 1.00 23.96 ?  22  TYR D CD1   1 
ATOM   13544 C  CD2   . TYR D 2 43  ? 122.727 107.072 132.474 1.00 24.73 ?  22  TYR D CD2   1 
ATOM   13545 C  CE1   . TYR D 2 43  ? 122.379 104.434 131.704 1.00 23.42 ?  22  TYR D CE1   1 
ATOM   13546 C  CE2   . TYR D 2 43  ? 122.374 106.777 131.155 1.00 26.65 ?  22  TYR D CE2   1 
ATOM   13547 C  CZ    . TYR D 2 43  ? 122.206 105.455 130.782 1.00 25.68 ?  22  TYR D CZ    1 
ATOM   13548 O  OH    . TYR D 2 43  ? 121.861 105.159 129.482 1.00 26.57 ?  22  TYR D OH    1 
ATOM   13549 N  N     . ASN D 2 44  ? 125.235 108.652 134.097 1.00 26.77 ?  23  ASN D N     1 
ATOM   13550 C  CA    . ASN D 2 44  ? 125.738 109.641 133.150 1.00 28.57 ?  23  ASN D CA    1 
ATOM   13551 C  C     . ASN D 2 44  ? 127.246 109.579 132.994 1.00 28.70 ?  23  ASN D C     1 
ATOM   13552 O  O     . ASN D 2 44  ? 127.749 109.474 131.873 1.00 28.99 ?  23  ASN D O     1 
ATOM   13553 C  CB    . ASN D 2 44  ? 125.271 111.045 133.543 1.00 29.62 ?  23  ASN D CB    1 
ATOM   13554 C  CG    . ASN D 2 44  ? 123.773 111.233 133.339 1.00 32.44 ?  23  ASN D CG    1 
ATOM   13555 O  OD1   . ASN D 2 44  ? 123.144 110.510 132.555 1.00 34.30 ?  23  ASN D OD1   1 
ATOM   13556 N  ND2   . ASN D 2 44  ? 123.192 112.201 134.043 1.00 35.17 ?  23  ASN D ND2   1 
ATOM   13557 N  N     . GLN D 2 45  ? 127.957 109.599 134.119 1.00 28.97 ?  24  GLN D N     1 
ATOM   13558 C  CA    . GLN D 2 45  ? 129.414 109.558 134.103 1.00 29.99 ?  24  GLN D CA    1 
ATOM   13559 C  C     . GLN D 2 45  ? 129.956 108.259 133.487 1.00 29.69 ?  24  GLN D C     1 
ATOM   13560 O  O     . GLN D 2 45  ? 130.931 108.288 132.737 1.00 30.01 ?  24  GLN D O     1 
ATOM   13561 C  CB    . GLN D 2 45  ? 129.987 109.785 135.507 1.00 30.27 ?  24  GLN D CB    1 
ATOM   13562 C  CG    . GLN D 2 45  ? 131.519 109.989 135.530 1.00 32.29 ?  24  GLN D CG    1 
ATOM   13563 C  CD    . GLN D 2 45  ? 131.973 111.230 134.772 1.00 35.95 ?  24  GLN D CD    1 
ATOM   13564 O  OE1   . GLN D 2 45  ? 131.233 112.211 134.655 1.00 36.72 ?  24  GLN D OE1   1 
ATOM   13565 N  NE2   . GLN D 2 45  ? 133.197 111.192 134.255 1.00 37.05 ?  24  GLN D NE2   1 
ATOM   13566 N  N     . ASN D 2 46  ? 129.308 107.134 133.783 1.00 28.93 ?  25  ASN D N     1 
ATOM   13567 C  CA    . ASN D 2 46  ? 129.700 105.857 133.211 1.00 28.70 ?  25  ASN D CA    1 
ATOM   13568 C  C     . ASN D 2 46  ? 129.560 105.796 131.696 1.00 29.05 ?  25  ASN D C     1 
ATOM   13569 O  O     . ASN D 2 46  ? 130.514 105.436 131.001 1.00 28.51 ?  25  ASN D O     1 
ATOM   13570 C  CB    . ASN D 2 46  ? 128.936 104.696 133.863 1.00 28.36 ?  25  ASN D CB    1 
ATOM   13571 C  CG    . ASN D 2 46  ? 129.625 104.179 135.107 1.00 28.45 ?  25  ASN D CG    1 
ATOM   13572 O  OD1   . ASN D 2 46  ? 130.362 103.197 135.043 1.00 28.03 ?  25  ASN D OD1   1 
ATOM   13573 N  ND2   . ASN D 2 46  ? 129.416 104.851 136.238 1.00 26.53 ?  25  ASN D ND2   1 
ATOM   13574 N  N     . VAL D 2 47  ? 128.387 106.170 131.185 1.00 29.66 ?  26  VAL D N     1 
ATOM   13575 C  CA    . VAL D 2 47  ? 128.120 106.038 129.752 1.00 31.15 ?  26  VAL D CA    1 
ATOM   13576 C  C     . VAL D 2 47  ? 128.914 107.052 128.934 1.00 32.39 ?  26  VAL D C     1 
ATOM   13577 O  O     . VAL D 2 47  ? 129.284 106.776 127.794 1.00 32.80 ?  26  VAL D O     1 
ATOM   13578 C  CB    . VAL D 2 47  ? 126.597 106.068 129.388 1.00 31.08 ?  26  VAL D CB    1 
ATOM   13579 C  CG1   . VAL D 2 47  ? 125.837 104.993 130.155 1.00 31.09 ?  26  VAL D CG1   1 
ATOM   13580 C  CG2   . VAL D 2 47  ? 125.979 107.455 129.612 1.00 30.81 ?  26  VAL D CG2   1 
ATOM   13581 N  N     . LYS D 2 48  ? 129.207 108.209 129.515 1.00 33.28 ?  27  LYS D N     1 
ATOM   13582 C  CA    . LYS D 2 48  ? 130.003 109.183 128.785 1.00 34.87 ?  27  LYS D CA    1 
ATOM   13583 C  C     . LYS D 2 48  ? 131.507 108.839 128.745 1.00 34.91 ?  27  LYS D C     1 
ATOM   13584 O  O     . LYS D 2 48  ? 132.257 109.430 127.973 1.00 34.92 ?  27  LYS D O     1 
ATOM   13585 C  CB    . LYS D 2 48  ? 129.722 110.614 129.265 1.00 35.45 ?  27  LYS D CB    1 
ATOM   13586 C  CG    . LYS D 2 48  ? 130.512 111.092 130.461 1.00 37.41 ?  27  LYS D CG    1 
ATOM   13587 C  CD    . LYS D 2 48  ? 130.416 112.622 130.569 1.00 40.91 ?  27  LYS D CD    1 
ATOM   13588 C  CE    . LYS D 2 48  ? 131.500 113.179 131.497 1.00 42.46 ?  27  LYS D CE    1 
ATOM   13589 N  NZ    . LYS D 2 48  ? 131.543 114.671 131.510 1.00 45.13 1  27  LYS D NZ    1 
ATOM   13590 N  N     . GLN D 2 49  ? 131.921 107.870 129.565 1.00 34.66 ?  28  GLN D N     1 
ATOM   13591 C  CA    . GLN D 2 49  ? 133.293 107.370 129.583 1.00 34.64 ?  28  GLN D CA    1 
ATOM   13592 C  C     . GLN D 2 49  ? 133.464 106.153 128.675 1.00 34.20 ?  28  GLN D C     1 
ATOM   13593 O  O     . GLN D 2 49  ? 134.519 105.518 128.694 1.00 34.53 ?  28  GLN D O     1 
ATOM   13594 C  CB    . GLN D 2 49  ? 133.720 106.993 131.016 1.00 34.89 ?  28  GLN D CB    1 
ATOM   13595 C  CG    . GLN D 2 49  ? 134.302 108.140 131.839 1.00 36.47 ?  28  GLN D CG    1 
ATOM   13596 C  CD    . GLN D 2 49  ? 134.532 107.781 133.309 1.00 38.37 ?  28  GLN D CD    1 
ATOM   13597 O  OE1   . GLN D 2 49  ? 134.430 108.643 134.183 1.00 40.68 ?  28  GLN D OE1   1 
ATOM   13598 N  NE2   . GLN D 2 49  ? 134.840 106.514 133.586 1.00 38.57 ?  28  GLN D NE2   1 
ATOM   13599 N  N     . PHE D 2 50  ? 132.439 105.818 127.891 1.00 33.42 ?  29  PHE D N     1 
ATOM   13600 C  CA    . PHE D 2 50  ? 132.492 104.618 127.056 1.00 32.57 ?  29  PHE D CA    1 
ATOM   13601 C  C     . PHE D 2 50  ? 133.627 104.729 126.037 1.00 32.60 ?  29  PHE D C     1 
ATOM   13602 O  O     . PHE D 2 50  ? 133.853 105.792 125.453 1.00 32.39 ?  29  PHE D O     1 
ATOM   13603 C  CB    . PHE D 2 50  ? 131.149 104.341 126.363 1.00 32.77 ?  29  PHE D CB    1 
ATOM   13604 C  CG    . PHE D 2 50  ? 131.145 103.086 125.512 1.00 32.24 ?  29  PHE D CG    1 
ATOM   13605 C  CD1   . PHE D 2 50  ? 131.085 101.826 126.100 1.00 31.50 ?  29  PHE D CD1   1 
ATOM   13606 C  CD2   . PHE D 2 50  ? 131.203 103.170 124.126 1.00 33.60 ?  29  PHE D CD2   1 
ATOM   13607 C  CE1   . PHE D 2 50  ? 131.085 100.675 125.327 1.00 33.02 ?  29  PHE D CE1   1 
ATOM   13608 C  CE2   . PHE D 2 50  ? 131.207 102.019 123.335 1.00 33.78 ?  29  PHE D CE2   1 
ATOM   13609 C  CZ    . PHE D 2 50  ? 131.140 100.771 123.935 1.00 33.13 ?  29  PHE D CZ    1 
ATOM   13610 N  N     . TRP D 2 51  ? 134.337 103.625 125.844 1.00 31.95 ?  30  TRP D N     1 
ATOM   13611 C  CA    . TRP D 2 51  ? 135.463 103.566 124.911 1.00 32.03 ?  30  TRP D CA    1 
ATOM   13612 C  C     . TRP D 2 51  ? 135.640 102.133 124.426 1.00 33.03 ?  30  TRP D C     1 
ATOM   13613 O  O     . TRP D 2 51  ? 135.046 101.203 124.977 1.00 32.54 ?  30  TRP D O     1 
ATOM   13614 C  CB    . TRP D 2 51  ? 136.752 104.096 125.557 1.00 31.19 ?  30  TRP D CB    1 
ATOM   13615 C  CG    . TRP D 2 51  ? 137.202 103.311 126.773 1.00 28.11 ?  30  TRP D CG    1 
ATOM   13616 C  CD1   . TRP D 2 51  ? 136.702 103.405 128.035 1.00 26.51 ?  30  TRP D CD1   1 
ATOM   13617 C  CD2   . TRP D 2 51  ? 138.234 102.313 126.824 1.00 25.93 ?  30  TRP D CD2   1 
ATOM   13618 N  NE1   . TRP D 2 51  ? 137.362 102.533 128.876 1.00 24.52 ?  30  TRP D NE1   1 
ATOM   13619 C  CE2   . TRP D 2 51  ? 138.303 101.850 128.159 1.00 24.42 ?  30  TRP D CE2   1 
ATOM   13620 C  CE3   . TRP D 2 51  ? 139.112 101.771 125.874 1.00 25.37 ?  30  TRP D CE3   1 
ATOM   13621 C  CZ2   . TRP D 2 51  ? 139.220 100.871 128.570 1.00 24.00 ?  30  TRP D CZ2   1 
ATOM   13622 C  CZ3   . TRP D 2 51  ? 140.018 100.791 126.282 1.00 24.99 ?  30  TRP D CZ3   1 
ATOM   13623 C  CH2   . TRP D 2 51  ? 140.062 100.352 127.618 1.00 23.72 ?  30  TRP D CH2   1 
ATOM   13624 N  N     . LEU D 2 52  ? 136.445 101.971 123.381 1.00 34.81 ?  31  LEU D N     1 
ATOM   13625 C  CA    . LEU D 2 52  ? 136.707 100.672 122.778 1.00 36.58 ?  31  LEU D CA    1 
ATOM   13626 C  C     . LEU D 2 52  ? 138.206 100.491 122.558 1.00 37.80 ?  31  LEU D C     1 
ATOM   13627 O  O     . LEU D 2 52  ? 138.907 101.462 122.288 1.00 37.92 ?  31  LEU D O     1 
ATOM   13628 C  CB    . LEU D 2 52  ? 135.943 100.531 121.452 1.00 36.95 ?  31  LEU D CB    1 
ATOM   13629 C  CG    . LEU D 2 52  ? 134.459 100.151 121.485 1.00 38.15 ?  31  LEU D CG    1 
ATOM   13630 C  CD1   . LEU D 2 52  ? 133.994 99.726  120.097 1.00 39.50 ?  31  LEU D CD1   1 
ATOM   13631 C  CD2   . LEU D 2 52  ? 134.177 99.032  122.482 1.00 37.94 ?  31  LEU D CD2   1 
ATOM   13632 N  N     . PRO D 2 53  ? 138.705 99.243  122.664 1.00 39.26 ?  32  PRO D N     1 
ATOM   13633 C  CA    . PRO D 2 53  ? 140.139 98.946  122.491 1.00 40.41 ?  32  PRO D CA    1 
ATOM   13634 C  C     . PRO D 2 53  ? 140.717 99.452  121.162 1.00 41.91 ?  32  PRO D C     1 
ATOM   13635 O  O     . PRO D 2 53  ? 141.803 100.043 121.143 1.00 42.52 ?  32  PRO D O     1 
ATOM   13636 C  CB    . PRO D 2 53  ? 140.185 97.414  122.522 1.00 40.42 ?  32  PRO D CB    1 
ATOM   13637 C  CG    . PRO D 2 53  ? 138.947 97.001  123.208 1.00 40.01 ?  32  PRO D CG    1 
ATOM   13638 C  CD    . PRO D 2 53  ? 137.912 98.021  122.885 1.00 39.30 ?  32  PRO D CD    1 
ATOM   13639 N  N     . GLU D 2 54  ? 139.982 99.237  120.075 1.00 43.27 ?  33  GLU D N     1 
ATOM   13640 C  CA    . GLU D 2 54  ? 140.399 99.616  118.715 1.00 45.17 ?  33  GLU D CA    1 
ATOM   13641 C  C     . GLU D 2 54  ? 140.811 101.086 118.539 1.00 45.57 ?  33  GLU D C     1 
ATOM   13642 O  O     . GLU D 2 54  ? 141.531 101.422 117.593 1.00 46.08 ?  33  GLU D O     1 
ATOM   13643 C  CB    . GLU D 2 54  ? 139.284 99.273  117.714 1.00 45.55 ?  33  GLU D CB    1 
ATOM   13644 C  CG    . GLU D 2 54  ? 139.245 97.809  117.269 1.00 48.19 ?  33  GLU D CG    1 
ATOM   13645 C  CD    . GLU D 2 54  ? 138.948 96.834  118.400 1.00 50.61 ?  33  GLU D CD    1 
ATOM   13646 O  OE1   . GLU D 2 54  ? 137.991 97.077  119.172 1.00 51.10 ?  33  GLU D OE1   1 
ATOM   13647 O  OE2   . GLU D 2 54  ? 139.681 95.822  118.514 1.00 52.64 -1 33  GLU D OE2   1 
ATOM   13648 N  N     . GLU D 2 55  ? 140.355 101.950 119.445 1.00 45.74 ?  34  GLU D N     1 
ATOM   13649 C  CA    . GLU D 2 55  ? 140.621 103.391 119.364 1.00 46.28 ?  34  GLU D CA    1 
ATOM   13650 C  C     . GLU D 2 55  ? 142.102 103.747 119.548 1.00 46.49 ?  34  GLU D C     1 
ATOM   13651 O  O     . GLU D 2 55  ? 142.581 104.741 118.994 1.00 46.73 ?  34  GLU D O     1 
ATOM   13652 C  CB    . GLU D 2 55  ? 139.765 104.162 120.374 1.00 46.17 ?  34  GLU D CB    1 
ATOM   13653 C  CG    . GLU D 2 55  ? 138.254 104.070 120.142 1.00 47.10 ?  34  GLU D CG    1 
ATOM   13654 C  CD    . GLU D 2 55  ? 137.460 104.905 121.144 1.00 48.43 ?  34  GLU D CD    1 
ATOM   13655 O  OE1   . GLU D 2 55  ? 137.613 106.147 121.146 1.00 49.62 ?  34  GLU D OE1   1 
ATOM   13656 O  OE2   . GLU D 2 55  ? 136.682 104.323 121.929 1.00 47.11 -1 34  GLU D OE2   1 
ATOM   13657 N  N     . ILE D 2 56  ? 142.816 102.938 120.330 1.00 46.23 ?  35  ILE D N     1 
ATOM   13658 C  CA    . ILE D 2 56  ? 144.244 103.144 120.560 1.00 46.25 ?  35  ILE D CA    1 
ATOM   13659 C  C     . ILE D 2 56  ? 145.044 102.150 119.720 1.00 46.30 ?  35  ILE D C     1 
ATOM   13660 O  O     . ILE D 2 56  ? 144.889 100.934 119.872 1.00 46.36 ?  35  ILE D O     1 
ATOM   13661 C  CB    . ILE D 2 56  ? 144.626 102.982 122.073 1.00 45.84 ?  35  ILE D CB    1 
ATOM   13662 C  CG1   . ILE D 2 56  ? 143.598 103.648 123.011 1.00 46.15 ?  35  ILE D CG1   1 
ATOM   13663 C  CG2   . ILE D 2 56  ? 146.068 103.462 122.340 1.00 45.72 ?  35  ILE D CG2   1 
ATOM   13664 C  CD1   . ILE D 2 56  ? 143.452 105.159 122.876 1.00 47.27 ?  35  ILE D CD1   1 
ATOM   13665 N  N     . ALA D 2 57  ? 145.887 102.664 118.829 1.00 46.51 ?  36  ALA D N     1 
ATOM   13666 C  CA    . ALA D 2 57  ? 146.801 101.820 118.056 1.00 46.56 ?  36  ALA D CA    1 
ATOM   13667 C  C     . ALA D 2 57  ? 147.971 101.396 118.948 1.00 46.08 ?  36  ALA D C     1 
ATOM   13668 O  O     . ALA D 2 57  ? 148.635 102.246 119.539 1.00 45.70 ?  36  ALA D O     1 
ATOM   13669 C  CB    . ALA D 2 57  ? 147.304 102.562 116.820 1.00 47.10 ?  36  ALA D CB    1 
ATOM   13670 N  N     . LEU D 2 58  ? 148.225 100.091 119.029 1.00 45.66 ?  37  LEU D N     1 
ATOM   13671 C  CA    . LEU D 2 58  ? 149.220 99.560  119.973 1.00 45.27 ?  37  LEU D CA    1 
ATOM   13672 C  C     . LEU D 2 58  ? 150.624 99.320  119.422 1.00 45.25 ?  37  LEU D C     1 
ATOM   13673 O  O     . LEU D 2 58  ? 151.590 99.259  120.190 1.00 44.82 ?  37  LEU D O     1 
ATOM   13674 C  CB    . LEU D 2 58  ? 148.704 98.278  120.626 1.00 45.05 ?  37  LEU D CB    1 
ATOM   13675 C  CG    . LEU D 2 58  ? 147.697 98.495  121.753 1.00 45.41 ?  37  LEU D CG    1 
ATOM   13676 C  CD1   . LEU D 2 58  ? 147.210 97.157  122.273 1.00 45.40 ?  37  LEU D CD1   1 
ATOM   13677 C  CD2   . LEU D 2 58  ? 148.310 99.326  122.879 1.00 44.70 ?  37  LEU D CD2   1 
ATOM   13678 N  N     . ASN D 2 59  ? 150.743 99.198  118.102 1.00 45.33 ?  38  ASN D N     1 
ATOM   13679 C  CA    . ASN D 2 59  ? 151.992 98.738  117.489 1.00 45.22 ?  38  ASN D CA    1 
ATOM   13680 C  C     . ASN D 2 59  ? 153.234 99.589  117.789 1.00 44.39 ?  38  ASN D C     1 
ATOM   13681 O  O     . ASN D 2 59  ? 154.344 99.053  117.887 1.00 44.33 ?  38  ASN D O     1 
ATOM   13682 C  CB    . ASN D 2 59  ? 151.811 98.553  115.985 1.00 46.22 ?  38  ASN D CB    1 
ATOM   13683 C  CG    . ASN D 2 59  ? 152.606 97.378  115.444 1.00 47.90 ?  38  ASN D CG    1 
ATOM   13684 O  OD1   . ASN D 2 59  ? 153.494 97.547  114.610 1.00 49.28 ?  38  ASN D OD1   1 
ATOM   13685 N  ND2   . ASN D 2 59  ? 152.287 96.173  115.919 1.00 49.18 ?  38  ASN D ND2   1 
ATOM   13686 N  N     . GLY D 2 60  ? 153.039 100.899 117.956 1.00 43.45 ?  39  GLY D N     1 
ATOM   13687 C  CA    . GLY D 2 60  ? 154.129 101.830 118.263 1.00 42.42 ?  39  GLY D CA    1 
ATOM   13688 C  C     . GLY D 2 60  ? 154.805 101.648 119.620 1.00 41.55 ?  39  GLY D C     1 
ATOM   13689 O  O     . GLY D 2 60  ? 155.820 102.290 119.907 1.00 41.29 ?  39  GLY D O     1 
ATOM   13690 N  N     . ASP D 2 61  ? 154.242 100.784 120.463 1.00 40.35 ?  40  ASP D N     1 
ATOM   13691 C  CA    . ASP D 2 61  ? 154.869 100.442 121.745 1.00 39.53 ?  40  ASP D CA    1 
ATOM   13692 C  C     . ASP D 2 61  ? 156.120 99.587  121.590 1.00 39.38 ?  40  ASP D C     1 
ATOM   13693 O  O     . ASP D 2 61  ? 156.982 99.575  122.466 1.00 38.90 ?  40  ASP D O     1 
ATOM   13694 C  CB    . ASP D 2 61  ? 153.880 99.719  122.646 1.00 38.93 ?  40  ASP D CB    1 
ATOM   13695 C  CG    . ASP D 2 61  ? 153.018 100.665 123.433 1.00 38.21 ?  40  ASP D CG    1 
ATOM   13696 O  OD1   . ASP D 2 61  ? 153.190 101.898 123.308 1.00 38.79 ?  40  ASP D OD1   1 
ATOM   13697 O  OD2   . ASP D 2 61  ? 152.169 100.169 124.191 1.00 38.02 -1 40  ASP D OD2   1 
ATOM   13698 N  N     . LEU D 2 62  ? 156.208 98.873  120.473 1.00 39.82 ?  41  LEU D N     1 
ATOM   13699 C  CA    . LEU D 2 62  ? 157.340 97.998  120.196 1.00 40.22 ?  41  LEU D CA    1 
ATOM   13700 C  C     . LEU D 2 62  ? 158.647 98.782  120.077 1.00 40.40 ?  41  LEU D C     1 
ATOM   13701 O  O     . LEU D 2 62  ? 159.729 98.216  120.237 1.00 40.91 ?  41  LEU D O     1 
ATOM   13702 C  CB    . LEU D 2 62  ? 157.072 97.171  118.936 1.00 40.52 ?  41  LEU D CB    1 
ATOM   13703 C  CG    . LEU D 2 62  ? 155.921 96.162  119.024 1.00 41.03 ?  41  LEU D CG    1 
ATOM   13704 C  CD1   . LEU D 2 62  ? 155.700 95.481  117.680 1.00 42.53 ?  41  LEU D CD1   1 
ATOM   13705 C  CD2   . LEU D 2 62  ? 156.162 95.127  120.131 1.00 41.89 ?  41  LEU D CD2   1 
ATOM   13706 N  N     . LEU D 2 63  ? 158.525 100.088 119.821 1.00 40.20 ?  42  LEU D N     1 
ATOM   13707 C  CA    . LEU D 2 63  ? 159.660 101.001 119.695 1.00 39.85 ?  42  LEU D CA    1 
ATOM   13708 C  C     . LEU D 2 63  ? 160.287 101.387 121.048 1.00 38.90 ?  42  LEU D C     1 
ATOM   13709 O  O     . LEU D 2 63  ? 161.407 101.912 121.096 1.00 39.48 ?  42  LEU D O     1 
ATOM   13710 C  CB    . LEU D 2 63  ? 159.224 102.254 118.919 1.00 40.50 ?  42  LEU D CB    1 
ATOM   13711 C  CG    . LEU D 2 63  ? 160.180 103.017 117.989 1.00 41.98 ?  42  LEU D CG    1 
ATOM   13712 C  CD1   . LEU D 2 63  ? 160.791 102.121 116.917 1.00 43.07 ?  42  LEU D CD1   1 
ATOM   13713 C  CD2   . LEU D 2 63  ? 159.434 104.160 117.323 1.00 43.17 ?  42  LEU D CD2   1 
ATOM   13714 N  N     . THR D 2 64  ? 159.575 101.147 122.146 1.00 37.28 ?  43  THR D N     1 
ATOM   13715 C  CA    . THR D 2 64  ? 160.169 101.334 123.479 1.00 35.53 ?  43  THR D CA    1 
ATOM   13716 C  C     . THR D 2 64  ? 160.320 100.016 124.229 1.00 34.57 ?  43  THR D C     1 
ATOM   13717 O  O     . THR D 2 64  ? 161.222 99.866  125.056 1.00 34.23 ?  43  THR D O     1 
ATOM   13718 C  CB    . THR D 2 64  ? 159.416 102.363 124.352 1.00 35.18 ?  43  THR D CB    1 
ATOM   13719 O  OG1   . THR D 2 64  ? 158.010 102.096 124.336 1.00 34.59 ?  43  THR D OG1   1 
ATOM   13720 C  CG2   . THR D 2 64  ? 159.664 103.758 123.851 1.00 35.48 ?  43  THR D CG2   1 
ATOM   13721 N  N     . TRP D 2 65  ? 159.436 99.066  123.921 1.00 33.62 ?  44  TRP D N     1 
ATOM   13722 C  CA    . TRP D 2 65  ? 159.458 97.724  124.524 1.00 32.87 ?  44  TRP D CA    1 
ATOM   13723 C  C     . TRP D 2 65  ? 160.800 97.015  124.294 1.00 33.46 ?  44  TRP D C     1 
ATOM   13724 O  O     . TRP D 2 65  ? 161.356 96.411  125.212 1.00 32.58 ?  44  TRP D O     1 
ATOM   13725 C  CB    . TRP D 2 65  ? 158.302 96.882  123.962 1.00 32.09 ?  44  TRP D CB    1 
ATOM   13726 C  CG    . TRP D 2 65  ? 158.255 95.461  124.454 1.00 30.42 ?  44  TRP D CG    1 
ATOM   13727 C  CD1   . TRP D 2 65  ? 158.589 94.341  123.745 1.00 29.35 ?  44  TRP D CD1   1 
ATOM   13728 C  CD2   . TRP D 2 65  ? 157.845 95.008  125.753 1.00 28.04 ?  44  TRP D CD2   1 
ATOM   13729 N  NE1   . TRP D 2 65  ? 158.412 93.219  124.520 1.00 28.44 ?  44  TRP D NE1   1 
ATOM   13730 C  CE2   . TRP D 2 65  ? 157.961 93.599  125.758 1.00 28.14 ?  44  TRP D CE2   1 
ATOM   13731 C  CE3   . TRP D 2 65  ? 157.400 95.653  126.915 1.00 27.11 ?  44  TRP D CE3   1 
ATOM   13732 C  CZ2   . TRP D 2 65  ? 157.639 92.820  126.877 1.00 27.21 ?  44  TRP D CZ2   1 
ATOM   13733 C  CZ3   . TRP D 2 65  ? 157.072 94.875  128.029 1.00 27.45 ?  44  TRP D CZ3   1 
ATOM   13734 C  CH2   . TRP D 2 65  ? 157.190 93.472  127.995 1.00 27.25 ?  44  TRP D CH2   1 
ATOM   13735 N  N     . LYS D 2 66  ? 161.302 97.109  123.064 1.00 34.52 ?  45  LYS D N     1 
ATOM   13736 C  CA    . LYS D 2 66  ? 162.578 96.513  122.676 1.00 36.41 ?  45  LYS D CA    1 
ATOM   13737 C  C     . LYS D 2 66  ? 163.775 97.043  123.463 1.00 36.26 ?  45  LYS D C     1 
ATOM   13738 O  O     . LYS D 2 66  ? 164.810 96.380  123.527 1.00 36.52 ?  45  LYS D O     1 
ATOM   13739 C  CB    . LYS D 2 66  ? 162.820 96.692  121.171 1.00 36.98 ?  45  LYS D CB    1 
ATOM   13740 C  CG    . LYS D 2 66  ? 162.541 95.439  120.345 1.00 40.03 ?  45  LYS D CG    1 
ATOM   13741 C  CD    . LYS D 2 66  ? 161.046 95.106  120.265 1.00 43.70 ?  45  LYS D CD    1 
ATOM   13742 C  CE    . LYS D 2 66  ? 160.793 93.879  119.383 1.00 45.57 ?  45  LYS D CE    1 
ATOM   13743 N  NZ    . LYS D 2 66  ? 161.227 94.082  117.969 1.00 46.59 1  45  LYS D NZ    1 
ATOM   13744 N  N     . TYR D 2 67  ? 163.626 98.219  124.067 1.00 36.26 ?  46  TYR D N     1 
ATOM   13745 C  CA    . TYR D 2 67  ? 164.724 98.825  124.826 1.00 36.90 ?  46  TYR D CA    1 
ATOM   13746 C  C     . TYR D 2 67  ? 164.697 98.554  126.333 1.00 36.28 ?  46  TYR D C     1 
ATOM   13747 O  O     . TYR D 2 67  ? 165.589 98.999  127.049 1.00 36.44 ?  46  TYR D O     1 
ATOM   13748 C  CB    . TYR D 2 67  ? 164.830 100.329 124.549 1.00 37.15 ?  46  TYR D CB    1 
ATOM   13749 C  CG    . TYR D 2 67  ? 165.014 100.663 123.088 1.00 39.40 ?  46  TYR D CG    1 
ATOM   13750 C  CD1   . TYR D 2 67  ? 165.899 99.933  122.290 1.00 41.26 ?  46  TYR D CD1   1 
ATOM   13751 C  CD2   . TYR D 2 67  ? 164.326 101.723 122.507 1.00 41.06 ?  46  TYR D CD2   1 
ATOM   13752 C  CE1   . TYR D 2 67  ? 166.072 100.235 120.940 1.00 43.03 ?  46  TYR D CE1   1 
ATOM   13753 C  CE2   . TYR D 2 67  ? 164.496 102.040 121.157 1.00 43.05 ?  46  TYR D CE2   1 
ATOM   13754 C  CZ    . TYR D 2 67  ? 165.369 101.295 120.380 1.00 43.80 ?  46  TYR D CZ    1 
ATOM   13755 O  OH    . TYR D 2 67  ? 165.533 101.608 119.043 1.00 45.18 ?  46  TYR D OH    1 
ATOM   13756 N  N     . LEU D 2 68  ? 163.681 97.841  126.814 1.00 35.71 ?  47  LEU D N     1 
ATOM   13757 C  CA    . LEU D 2 68  ? 163.627 97.476  128.231 1.00 34.92 ?  47  LEU D CA    1 
ATOM   13758 C  C     . LEU D 2 68  ? 164.483 96.236  128.506 1.00 34.32 ?  47  LEU D C     1 
ATOM   13759 O  O     . LEU D 2 68  ? 164.612 95.357  127.649 1.00 34.50 ?  47  LEU D O     1 
ATOM   13760 C  CB    . LEU D 2 68  ? 162.182 97.241  128.697 1.00 35.00 ?  47  LEU D CB    1 
ATOM   13761 C  CG    . LEU D 2 68  ? 161.113 98.314  128.427 1.00 35.82 ?  47  LEU D CG    1 
ATOM   13762 C  CD1   . LEU D 2 68  ? 159.770 97.862  128.979 1.00 35.95 ?  47  LEU D CD1   1 
ATOM   13763 C  CD2   . LEU D 2 68  ? 161.489 99.684  128.992 1.00 35.97 ?  47  LEU D CD2   1 
ATOM   13764 N  N     . GLY D 2 69  ? 165.063 96.175  129.703 1.00 33.50 ?  48  GLY D N     1 
ATOM   13765 C  CA    . GLY D 2 69  ? 165.769 94.985  130.172 1.00 32.41 ?  48  GLY D CA    1 
ATOM   13766 C  C     . GLY D 2 69  ? 164.837 93.803  130.400 1.00 32.15 ?  48  GLY D C     1 
ATOM   13767 O  O     . GLY D 2 69  ? 163.609 93.958  130.431 1.00 30.98 ?  48  GLY D O     1 
ATOM   13768 N  N     . LYS D 2 70  ? 165.426 92.622  130.570 1.00 32.14 ?  49  LYS D N     1 
ATOM   13769 C  CA    . LYS D 2 70  ? 164.664 91.401  130.809 1.00 32.25 ?  49  LYS D CA    1 
ATOM   13770 C  C     . LYS D 2 70  ? 163.811 91.480  132.074 1.00 31.24 ?  49  LYS D C     1 
ATOM   13771 O  O     . LYS D 2 70  ? 162.659 91.053  132.052 1.00 31.34 ?  49  LYS D O     1 
ATOM   13772 C  CB    . LYS D 2 70  ? 165.586 90.181  130.870 1.00 33.07 ?  49  LYS D CB    1 
ATOM   13773 C  CG    . LYS D 2 70  ? 166.342 89.914  129.577 1.00 35.74 ?  49  LYS D CG    1 
ATOM   13774 C  CD    . LYS D 2 70  ? 167.438 88.879  129.809 1.00 39.67 ?  49  LYS D CD    1 
ATOM   13775 C  CE    . LYS D 2 70  ? 168.410 88.829  128.640 1.00 40.96 ?  49  LYS D CE    1 
ATOM   13776 N  NZ    . LYS D 2 70  ? 169.615 88.048  129.014 1.00 42.55 1  49  LYS D NZ    1 
ATOM   13777 N  N     . ASN D 2 71  ? 164.368 92.031  133.158 1.00 29.92 ?  50  ASN D N     1 
ATOM   13778 C  CA    . ASN D 2 71  ? 163.627 92.173  134.417 1.00 29.37 ?  50  ASN D CA    1 
ATOM   13779 C  C     . ASN D 2 71  ? 162.430 93.107  134.270 1.00 28.35 ?  50  ASN D C     1 
ATOM   13780 O  O     . ASN D 2 71  ? 161.359 92.831  134.823 1.00 27.64 ?  50  ASN D O     1 
ATOM   13781 C  CB    . ASN D 2 71  ? 164.523 92.647  135.578 1.00 29.38 ?  50  ASN D CB    1 
ATOM   13782 C  CG    . ASN D 2 71  ? 165.423 91.542  136.127 1.00 31.22 ?  50  ASN D CG    1 
ATOM   13783 O  OD1   . ASN D 2 71  ? 165.076 90.359  136.107 1.00 33.03 ?  50  ASN D OD1   1 
ATOM   13784 N  ND2   . ASN D 2 71  ? 166.587 91.933  136.636 1.00 31.97 ?  50  ASN D ND2   1 
ATOM   13785 N  N     . GLU D 2 72  ? 162.614 94.196  133.519 1.00 27.72 ?  51  GLU D N     1 
ATOM   13786 C  CA    . GLU D 2 72  ? 161.521 95.144  133.256 1.00 27.70 ?  51  GLU D CA    1 
ATOM   13787 C  C     . GLU D 2 72  ? 160.401 94.498  132.437 1.00 27.62 ?  51  GLU D C     1 
ATOM   13788 O  O     . GLU D 2 72  ? 159.215 94.690  132.724 1.00 27.56 ?  51  GLU D O     1 
ATOM   13789 C  CB    . GLU D 2 72  ? 162.028 96.397  132.533 1.00 27.55 ?  51  GLU D CB    1 
ATOM   13790 C  CG    . GLU D 2 72  ? 163.099 97.193  133.287 1.00 28.77 ?  51  GLU D CG    1 
ATOM   13791 C  CD    . GLU D 2 72  ? 163.454 98.479  132.563 1.00 31.18 ?  51  GLU D CD    1 
ATOM   13792 O  OE1   . GLU D 2 72  ? 164.118 98.406  131.507 1.00 33.17 ?  51  GLU D OE1   1 
ATOM   13793 O  OE2   . GLU D 2 72  ? 163.061 99.560  133.045 1.00 31.66 -1 51  GLU D OE2   1 
ATOM   13794 N  N     . GLN D 2 73  ? 160.786 93.733  131.419 1.00 27.32 ?  52  GLN D N     1 
ATOM   13795 C  CA    . GLN D 2 73  ? 159.823 93.050  130.560 1.00 27.33 ?  52  GLN D CA    1 
ATOM   13796 C  C     . GLN D 2 73  ? 159.088 91.963  131.349 1.00 26.85 ?  52  GLN D C     1 
ATOM   13797 O  O     . GLN D 2 73  ? 157.869 91.812  131.222 1.00 26.24 ?  52  GLN D O     1 
ATOM   13798 C  CB    . GLN D 2 73  ? 160.512 92.465  129.334 1.00 27.65 ?  52  GLN D CB    1 
ATOM   13799 C  CG    . GLN D 2 73  ? 160.942 93.502  128.278 1.00 29.66 ?  52  GLN D CG    1 
ATOM   13800 C  CD    . GLN D 2 73  ? 161.450 92.865  126.985 1.00 32.60 ?  52  GLN D CD    1 
ATOM   13801 O  OE1   . GLN D 2 73  ? 161.844 91.702  126.965 1.00 34.76 ?  52  GLN D OE1   1 
ATOM   13802 N  NE2   . GLN D 2 73  ? 161.458 93.635  125.908 1.00 33.42 ?  52  GLN D NE2   1 
ATOM   13803 N  N     . ASP D 2 74  ? 159.836 91.244  132.184 1.00 26.26 ?  53  ASP D N     1 
ATOM   13804 C  CA    . ASP D 2 74  ? 159.295 90.192  133.052 1.00 26.50 ?  53  ASP D CA    1 
ATOM   13805 C  C     . ASP D 2 74  ? 158.296 90.757  134.052 1.00 25.81 ?  53  ASP D C     1 
ATOM   13806 O  O     . ASP D 2 74  ? 157.202 90.221  134.206 1.00 26.12 ?  53  ASP D O     1 
ATOM   13807 C  CB    . ASP D 2 74  ? 160.440 89.494  133.799 1.00 26.84 ?  53  ASP D CB    1 
ATOM   13808 C  CG    . ASP D 2 74  ? 159.983 88.284  134.613 1.00 29.50 ?  53  ASP D CG    1 
ATOM   13809 O  OD1   . ASP D 2 74  ? 159.500 87.293  134.025 1.00 32.08 ?  53  ASP D OD1   1 
ATOM   13810 O  OD2   . ASP D 2 74  ? 160.153 88.306  135.849 1.00 33.52 -1 53  ASP D OD2   1 
ATOM   13811 N  N     . THR D 2 75  ? 158.668 91.841  134.731 1.00 25.10 ?  54  THR D N     1 
ATOM   13812 C  CA    . THR D 2 75  ? 157.770 92.463  135.709 1.00 24.11 ?  54  THR D CA    1 
ATOM   13813 C  C     . THR D 2 75  ? 156.489 92.950  135.026 1.00 23.82 ?  54  THR D C     1 
ATOM   13814 O  O     . THR D 2 75  ? 155.386 92.679  135.502 1.00 23.81 ?  54  THR D O     1 
ATOM   13815 C  CB    . THR D 2 75  ? 158.463 93.604  136.479 1.00 23.80 ?  54  THR D CB    1 
ATOM   13816 O  OG1   . THR D 2 75  ? 159.557 93.063  137.231 1.00 24.62 ?  54  THR D OG1   1 
ATOM   13817 C  CG2   . THR D 2 75  ? 157.480 94.293  137.443 1.00 23.25 ?  54  THR D CG2   1 
ATOM   13818 N  N     . TYR D 2 76  ? 156.645 93.673  133.926 1.00 24.06 ?  55  TYR D N     1 
ATOM   13819 C  CA    . TYR D 2 76  ? 155.504 94.157  133.154 1.00 24.76 ?  55  TYR D CA    1 
ATOM   13820 C  C     . TYR D 2 76  ? 154.535 93.034  132.758 1.00 24.85 ?  55  TYR D C     1 
ATOM   13821 O  O     . TYR D 2 76  ? 153.324 93.158  132.966 1.00 24.83 ?  55  TYR D O     1 
ATOM   13822 C  CB    . TYR D 2 76  ? 155.967 94.911  131.908 1.00 24.78 ?  55  TYR D CB    1 
ATOM   13823 C  CG    . TYR D 2 76  ? 154.909 95.839  131.349 1.00 26.19 ?  55  TYR D CG    1 
ATOM   13824 C  CD1   . TYR D 2 76  ? 154.842 97.169  131.770 1.00 27.81 ?  55  TYR D CD1   1 
ATOM   13825 C  CD2   . TYR D 2 76  ? 153.968 95.394  130.415 1.00 28.03 ?  55  TYR D CD2   1 
ATOM   13826 C  CE1   . TYR D 2 76  ? 153.880 98.036  131.271 1.00 29.32 ?  55  TYR D CE1   1 
ATOM   13827 C  CE2   . TYR D 2 76  ? 152.989 96.260  129.907 1.00 29.01 ?  55  TYR D CE2   1 
ATOM   13828 C  CZ    . TYR D 2 76  ? 152.958 97.580  130.345 1.00 30.76 ?  55  TYR D CZ    1 
ATOM   13829 O  OH    . TYR D 2 76  ? 152.018 98.462  129.865 1.00 34.50 ?  55  TYR D OH    1 
ATOM   13830 N  N     . MET D 2 77  ? 155.069 91.954  132.190 1.00 25.76 ?  56  MET D N     1 
ATOM   13831 C  CA    . MET D 2 77  ? 154.255 90.795  131.809 1.00 26.81 ?  56  MET D CA    1 
ATOM   13832 C  C     . MET D 2 77  ? 153.482 90.225  133.002 1.00 26.23 ?  56  MET D C     1 
ATOM   13833 O  O     . MET D 2 77  ? 152.284 89.952  132.904 1.00 25.00 ?  56  MET D O     1 
ATOM   13834 C  CB    . MET D 2 77  ? 155.121 89.703  131.185 1.00 28.11 ?  56  MET D CB    1 
ATOM   13835 C  CG    . MET D 2 77  ? 155.697 90.037  129.804 1.00 32.52 ?  56  MET D CG    1 
ATOM   13836 S  SD    . MET D 2 77  ? 154.482 90.014  128.475 1.00 42.68 ?  56  MET D SD    1 
ATOM   13837 C  CE    . MET D 2 77  ? 153.806 91.673  128.536 1.00 38.97 ?  56  MET D CE    1 
ATOM   13838 N  N     . LYS D 2 78  ? 154.185 90.044  134.121 1.00 26.01 ?  57  LYS D N     1 
ATOM   13839 C  CA    . LYS D 2 78  ? 153.591 89.461  135.327 1.00 26.07 ?  57  LYS D CA    1 
ATOM   13840 C  C     . LYS D 2 78  ? 152.510 90.355  135.931 1.00 25.69 ?  57  LYS D C     1 
ATOM   13841 O  O     . LYS D 2 78  ? 151.468 89.866  136.385 1.00 25.58 ?  57  LYS D O     1 
ATOM   13842 C  CB    . LYS D 2 78  ? 154.668 89.139  136.372 1.00 26.08 ?  57  LYS D CB    1 
ATOM   13843 C  CG    . LYS D 2 78  ? 155.587 87.975  135.974 1.00 27.64 ?  57  LYS D CG    1 
ATOM   13844 C  CD    . LYS D 2 78  ? 156.739 87.811  136.958 1.00 29.47 ?  57  LYS D CD    1 
ATOM   13845 C  CE    . LYS D 2 78  ? 157.511 86.533  136.671 1.00 31.69 ?  57  LYS D CE    1 
ATOM   13846 N  NZ    . LYS D 2 78  ? 158.632 86.325  137.626 1.00 33.36 1  57  LYS D NZ    1 
ATOM   13847 N  N     . VAL D 2 79  ? 152.766 91.661  135.936 1.00 25.32 ?  58  VAL D N     1 
ATOM   13848 C  CA    . VAL D 2 79  ? 151.808 92.648  136.449 1.00 25.47 ?  58  VAL D CA    1 
ATOM   13849 C  C     . VAL D 2 79  ? 150.560 92.636  135.572 1.00 25.09 ?  58  VAL D C     1 
ATOM   13850 O  O     . VAL D 2 79  ? 149.432 92.581  136.068 1.00 24.46 ?  58  VAL D O     1 
ATOM   13851 C  CB    . VAL D 2 79  ? 152.453 94.062  136.478 1.00 25.83 ?  58  VAL D CB    1 
ATOM   13852 C  CG1   . VAL D 2 79  ? 151.413 95.152  136.354 1.00 27.35 ?  58  VAL D CG1   1 
ATOM   13853 C  CG2   . VAL D 2 79  ? 153.304 94.224  137.737 1.00 26.42 ?  58  VAL D CG2   1 
ATOM   13854 N  N     . LEU D 2 80  ? 150.786 92.638  134.260 1.00 25.27 ?  59  LEU D N     1 
ATOM   13855 C  CA    . LEU D 2 80  ? 149.709 92.670  133.296 1.00 25.55 ?  59  LEU D CA    1 
ATOM   13856 C  C     . LEU D 2 80  ? 148.811 91.445  133.459 1.00 24.94 ?  59  LEU D C     1 
ATOM   13857 O  O     . LEU D 2 80  ? 147.588 91.571  133.447 1.00 24.82 ?  59  LEU D O     1 
ATOM   13858 C  CB    . LEU D 2 80  ? 150.277 92.728  131.876 1.00 25.80 ?  59  LEU D CB    1 
ATOM   13859 C  CG    . LEU D 2 80  ? 149.920 93.857  130.904 1.00 28.76 ?  59  LEU D CG    1 
ATOM   13860 C  CD1   . LEU D 2 80  ? 149.948 93.292  129.483 1.00 30.25 ?  59  LEU D CD1   1 
ATOM   13861 C  CD2   . LEU D 2 80  ? 148.585 94.529  131.178 1.00 27.79 ?  59  LEU D CD2   1 
ATOM   13862 N  N     . ALA D 2 81  ? 149.425 90.272  133.618 1.00 24.86 ?  60  ALA D N     1 
ATOM   13863 C  CA    . ALA D 2 81  ? 148.680 89.017  133.795 1.00 24.60 ?  60  ALA D CA    1 
ATOM   13864 C  C     . ALA D 2 81  ? 147.897 89.036  135.104 1.00 23.80 ?  60  ALA D C     1 
ATOM   13865 O  O     . ALA D 2 81  ? 146.772 88.553  135.170 1.00 24.07 ?  60  ALA D O     1 
ATOM   13866 C  CB    . ALA D 2 81  ? 149.626 87.818  133.755 1.00 24.48 ?  60  ALA D CB    1 
ATOM   13867 N  N     . GLY D 2 82  ? 148.499 89.605  136.142 1.00 23.54 ?  61  GLY D N     1 
ATOM   13868 C  CA    . GLY D 2 82  ? 147.828 89.783  137.425 1.00 22.53 ?  61  GLY D CA    1 
ATOM   13869 C  C     . GLY D 2 82  ? 146.561 90.601  137.282 1.00 22.23 ?  61  GLY D C     1 
ATOM   13870 O  O     . GLY D 2 82  ? 145.499 90.201  137.758 1.00 21.27 ?  61  GLY D O     1 
ATOM   13871 N  N     . LEU D 2 83  ? 146.671 91.751  136.619 1.00 22.36 ?  62  LEU D N     1 
ATOM   13872 C  CA    . LEU D 2 83  ? 145.506 92.613  136.384 1.00 22.42 ?  62  LEU D CA    1 
ATOM   13873 C  C     . LEU D 2 83  ? 144.447 91.899  135.557 1.00 22.91 ?  62  LEU D C     1 
ATOM   13874 O  O     . LEU D 2 83  ? 143.251 91.973  135.869 1.00 22.99 ?  62  LEU D O     1 
ATOM   13875 C  CB    . LEU D 2 83  ? 145.912 93.917  135.686 1.00 22.19 ?  62  LEU D CB    1 
ATOM   13876 C  CG    . LEU D 2 83  ? 146.815 94.876  136.479 1.00 22.17 ?  62  LEU D CG    1 
ATOM   13877 C  CD1   . LEU D 2 83  ? 147.405 95.934  135.538 1.00 21.55 ?  62  LEU D CD1   1 
ATOM   13878 C  CD2   . LEU D 2 83  ? 146.019 95.524  137.598 1.00 22.42 ?  62  LEU D CD2   1 
ATOM   13879 N  N     . THR D 2 84  ? 144.890 91.191  134.523 1.00 23.39 ?  63  THR D N     1 
ATOM   13880 C  CA    . THR D 2 84  ? 143.975 90.486  133.628 1.00 24.42 ?  63  THR D CA    1 
ATOM   13881 C  C     . THR D 2 84  ? 143.154 89.445  134.393 1.00 24.55 ?  63  THR D C     1 
ATOM   13882 O  O     . THR D 2 84  ? 141.926 89.404  134.282 1.00 23.68 ?  63  THR D O     1 
ATOM   13883 C  CB    . THR D 2 84  ? 144.726 89.801  132.458 1.00 24.70 ?  63  THR D CB    1 
ATOM   13884 O  OG1   . THR D 2 84  ? 145.441 90.790  131.707 1.00 25.57 ?  63  THR D OG1   1 
ATOM   13885 C  CG2   . THR D 2 84  ? 143.741 89.110  131.530 1.00 25.36 ?  63  THR D CG2   1 
ATOM   13886 N  N     . LEU D 2 85  ? 143.854 88.620  135.165 1.00 25.38 ?  64  LEU D N     1 
ATOM   13887 C  CA    . LEU D 2 85  ? 143.223 87.559  135.939 1.00 26.44 ?  64  LEU D CA    1 
ATOM   13888 C  C     . LEU D 2 85  ? 142.227 88.104  136.966 1.00 25.96 ?  64  LEU D C     1 
ATOM   13889 O  O     . LEU D 2 85  ? 141.093 87.608  137.041 1.00 25.83 ?  64  LEU D O     1 
ATOM   13890 C  CB    . LEU D 2 85  ? 144.276 86.628  136.560 1.00 26.65 ?  64  LEU D CB    1 
ATOM   13891 C  CG    . LEU D 2 85  ? 144.891 85.661  135.529 1.00 29.62 ?  64  LEU D CG    1 
ATOM   13892 C  CD1   . LEU D 2 85  ? 146.258 85.162  135.958 1.00 31.57 ?  64  LEU D CD1   1 
ATOM   13893 C  CD2   . LEU D 2 85  ? 143.964 84.467  135.233 1.00 30.96 ?  64  LEU D CD2   1 
ATOM   13894 N  N     . LEU D 2 86  ? 142.613 89.141  137.712 1.00 25.63 ?  65  LEU D N     1 
ATOM   13895 C  CA    . LEU D 2 86  ? 141.686 89.752  138.668 1.00 25.59 ?  65  LEU D CA    1 
ATOM   13896 C  C     . LEU D 2 86  ? 140.470 90.397  138.006 1.00 25.60 ?  65  LEU D C     1 
ATOM   13897 O  O     . LEU D 2 86  ? 139.356 90.327  138.533 1.00 25.47 ?  65  LEU D O     1 
ATOM   13898 C  CB    . LEU D 2 86  ? 142.391 90.757  139.599 1.00 25.76 ?  65  LEU D CB    1 
ATOM   13899 C  CG    . LEU D 2 86  ? 143.372 90.163  140.619 1.00 26.71 ?  65  LEU D CG    1 
ATOM   13900 C  CD1   . LEU D 2 86  ? 144.243 91.242  141.255 1.00 28.01 ?  65  LEU D CD1   1 
ATOM   13901 C  CD2   . LEU D 2 86  ? 142.647 89.385  141.693 1.00 28.01 ?  65  LEU D CD2   1 
ATOM   13902 N  N     . ASP D 2 87  ? 140.678 91.035  136.860 1.00 25.49 ?  66  ASP D N     1 
ATOM   13903 C  CA    . ASP D 2 87  ? 139.592 91.733  136.193 1.00 25.83 ?  66  ASP D CA    1 
ATOM   13904 C  C     . ASP D 2 87  ? 138.559 90.765  135.598 1.00 26.20 ?  66  ASP D C     1 
ATOM   13905 O  O     . ASP D 2 87  ? 137.377 91.082  135.527 1.00 25.99 ?  66  ASP D O     1 
ATOM   13906 C  CB    . ASP D 2 87  ? 140.134 92.678  135.129 1.00 25.50 ?  66  ASP D CB    1 
ATOM   13907 C  CG    . ASP D 2 87  ? 139.272 93.897  134.963 1.00 25.76 ?  66  ASP D CG    1 
ATOM   13908 O  OD1   . ASP D 2 87  ? 138.606 94.290  135.951 1.00 26.91 ?  66  ASP D OD1   1 
ATOM   13909 O  OD2   . ASP D 2 87  ? 139.254 94.470  133.856 1.00 23.11 -1 66  ASP D OD2   1 
ATOM   13910 N  N     . THR D 2 88  ? 139.019 89.582  135.199 1.00 27.12 ?  67  THR D N     1 
ATOM   13911 C  CA    . THR D 2 88  ? 138.146 88.523  134.713 1.00 28.40 ?  67  THR D CA    1 
ATOM   13912 C  C     . THR D 2 88  ? 137.199 88.043  135.801 1.00 28.28 ?  67  THR D C     1 
ATOM   13913 O  O     . THR D 2 88  ? 136.018 87.822  135.541 1.00 28.10 ?  67  THR D O     1 
ATOM   13914 C  CB    . THR D 2 88  ? 138.954 87.334  134.158 1.00 29.04 ?  67  THR D CB    1 
ATOM   13915 O  OG1   . THR D 2 88  ? 139.780 87.796  133.087 1.00 31.00 ?  67  THR D OG1   1 
ATOM   13916 C  CG2   . THR D 2 88  ? 138.022 86.250  133.621 1.00 30.16 ?  67  THR D CG2   1 
ATOM   13917 N  N     . GLU D 2 89  ? 137.710 87.885  137.021 1.00 28.28 ?  68  GLU D N     1 
ATOM   13918 C  CA    . GLU D 2 89  ? 136.849 87.528  138.144 1.00 29.16 ?  68  GLU D CA    1 
ATOM   13919 C  C     . GLU D 2 89  ? 135.776 88.597  138.339 1.00 28.65 ?  68  GLU D C     1 
ATOM   13920 O  O     . GLU D 2 89  ? 134.621 88.277  138.579 1.00 28.44 ?  68  GLU D O     1 
ATOM   13921 C  CB    . GLU D 2 89  ? 137.651 87.344  139.441 1.00 29.32 ?  68  GLU D CB    1 
ATOM   13922 C  CG    . GLU D 2 89  ? 138.716 86.239  139.383 1.00 31.95 ?  68  GLU D CG    1 
ATOM   13923 C  CD    . GLU D 2 89  ? 138.145 84.838  139.189 1.00 35.19 ?  68  GLU D CD    1 
ATOM   13924 O  OE1   . GLU D 2 89  ? 136.929 84.622  139.395 1.00 35.47 ?  68  GLU D OE1   1 
ATOM   13925 O  OE2   . GLU D 2 89  ? 138.930 83.941  138.818 1.00 38.06 -1 68  GLU D OE2   1 
ATOM   13926 N  N     . GLN D 2 90  ? 136.162 89.864  138.215 1.00 28.45 ?  69  GLN D N     1 
ATOM   13927 C  CA    . GLN D 2 90  ? 135.216 90.964  138.405 1.00 28.47 ?  69  GLN D CA    1 
ATOM   13928 C  C     . GLN D 2 90  ? 134.128 90.979  137.322 1.00 28.97 ?  69  GLN D C     1 
ATOM   13929 O  O     . GLN D 2 90  ? 132.964 91.245  137.616 1.00 28.84 ?  69  GLN D O     1 
ATOM   13930 C  CB    . GLN D 2 90  ? 135.951 92.306  138.487 1.00 28.21 ?  69  GLN D CB    1 
ATOM   13931 C  CG    . GLN D 2 90  ? 135.130 93.444  139.093 1.00 27.75 ?  69  GLN D CG    1 
ATOM   13932 C  CD    . GLN D 2 90  ? 134.902 93.314  140.594 1.00 28.91 ?  69  GLN D CD    1 
ATOM   13933 O  OE1   . GLN D 2 90  ? 134.989 92.220  141.171 1.00 27.62 ?  69  GLN D OE1   1 
ATOM   13934 N  NE2   . GLN D 2 90  ? 134.584 94.440  141.235 1.00 28.23 ?  69  GLN D NE2   1 
ATOM   13935 N  N     . GLY D 2 91  ? 134.508 90.667  136.083 1.00 29.62 ?  70  GLY D N     1 
ATOM   13936 C  CA    . GLY D 2 91  ? 133.556 90.592  134.973 1.00 30.43 ?  70  GLY D CA    1 
ATOM   13937 C  C     . GLY D 2 91  ? 132.628 89.382  135.004 1.00 31.11 ?  70  GLY D C     1 
ATOM   13938 O  O     . GLY D 2 91  ? 131.436 89.488  134.700 1.00 30.77 ?  70  GLY D O     1 
ATOM   13939 N  N     . ASN D 2 92  ? 133.171 88.227  135.359 1.00 31.69 ?  71  ASN D N     1 
ATOM   13940 C  CA    . ASN D 2 92  ? 132.366 87.011  135.383 1.00 32.72 ?  71  ASN D CA    1 
ATOM   13941 C  C     . ASN D 2 92  ? 131.532 86.811  136.640 1.00 32.60 ?  71  ASN D C     1 
ATOM   13942 O  O     . ASN D 2 92  ? 130.467 86.192  136.575 1.00 33.12 ?  71  ASN D O     1 
ATOM   13943 C  CB    . ASN D 2 92  ? 133.236 85.788  135.124 1.00 33.68 ?  71  ASN D CB    1 
ATOM   13944 C  CG    . ASN D 2 92  ? 133.697 85.705  133.684 1.00 35.15 ?  71  ASN D CG    1 
ATOM   13945 O  OD1   . ASN D 2 92  ? 134.738 85.126  133.400 1.00 40.21 ?  71  ASN D OD1   1 
ATOM   13946 N  ND2   . ASN D 2 92  ? 132.927 86.296  132.767 1.00 36.91 ?  71  ASN D ND2   1 
ATOM   13947 N  N     . THR D 2 93  ? 132.004 87.350  137.765 1.00 31.76 ?  72  THR D N     1 
ATOM   13948 C  CA    . THR D 2 93  ? 131.362 87.115  139.054 1.00 31.47 ?  72  THR D CA    1 
ATOM   13949 C  C     . THR D 2 93  ? 131.047 88.391  139.830 1.00 30.62 ?  72  THR D C     1 
ATOM   13950 O  O     . THR D 2 93  ? 129.889 88.643  140.153 1.00 30.71 ?  72  THR D O     1 
ATOM   13951 C  CB    . THR D 2 93  ? 132.210 86.186  139.919 1.00 31.60 ?  72  THR D CB    1 
ATOM   13952 O  OG1   . THR D 2 93  ? 132.455 84.973  139.195 1.00 33.14 ?  72  THR D OG1   1 
ATOM   13953 C  CG2   . THR D 2 93  ? 131.496 85.864  141.222 1.00 31.89 ?  72  THR D CG2   1 
ATOM   13954 N  N     . GLY D 2 94  ? 132.074 89.187  140.119 1.00 29.61 ?  73  GLY D N     1 
ATOM   13955 C  CA    . GLY D 2 94  ? 131.940 90.358  140.987 1.00 28.47 ?  73  GLY D CA    1 
ATOM   13956 C  C     . GLY D 2 94  ? 130.827 91.323  140.631 1.00 27.90 ?  73  GLY D C     1 
ATOM   13957 O  O     . GLY D 2 94  ? 129.966 91.636  141.465 1.00 28.27 ?  73  GLY D O     1 
ATOM   13958 N  N     . MET D 2 95  ? 130.840 91.827  139.405 1.00 26.67 ?  74  MET D N     1 
ATOM   13959 C  CA    . MET D 2 95  ? 129.796 92.775  139.024 1.00 26.00 ?  74  MET D CA    1 
ATOM   13960 C  C     . MET D 2 95  ? 128.455 92.087  138.802 1.00 25.25 ?  74  MET D C     1 
ATOM   13961 O  O     . MET D 2 95  ? 127.440 92.602  139.252 1.00 24.97 ?  74  MET D O     1 
ATOM   13962 C  CB    . MET D 2 95  ? 130.186 93.632  137.813 1.00 26.00 ?  74  MET D CB    1 
ATOM   13963 C  CG    . MET D 2 95  ? 131.107 94.780  138.148 1.00 26.40 ?  74  MET D CG    1 
ATOM   13964 S  SD    . MET D 2 95  ? 130.403 95.977  139.310 1.00 28.10 ?  74  MET D SD    1 
ATOM   13965 C  CE    . MET D 2 95  ? 131.842 97.006  139.566 1.00 28.95 ?  74  MET D CE    1 
ATOM   13966 N  N     . PRO D 2 96  ? 128.440 90.934  138.106 1.00 24.98 ?  75  PRO D N     1 
ATOM   13967 C  CA    . PRO D 2 96  ? 127.110 90.330  137.904 1.00 24.59 ?  75  PRO D CA    1 
ATOM   13968 C  C     . PRO D 2 96  ? 126.436 89.853  139.188 1.00 23.90 ?  75  PRO D C     1 
ATOM   13969 O  O     . PRO D 2 96  ? 125.214 89.893  139.266 1.00 23.45 ?  75  PRO D O     1 
ATOM   13970 C  CB    . PRO D 2 96  ? 127.390 89.134  136.984 1.00 24.80 ?  75  PRO D CB    1 
ATOM   13971 C  CG    . PRO D 2 96  ? 128.663 89.507  136.258 1.00 25.75 ?  75  PRO D CG    1 
ATOM   13972 C  CD    . PRO D 2 96  ? 129.470 90.291  137.261 1.00 25.07 ?  75  PRO D CD    1 
ATOM   13973 N  N     . ILE D 2 97  ? 127.213 89.397  140.175 1.00 23.36 ?  76  ILE D N     1 
ATOM   13974 C  CA    . ILE D 2 97  ? 126.616 88.901  141.411 1.00 23.48 ?  76  ILE D CA    1 
ATOM   13975 C  C     . ILE D 2 97  ? 126.028 90.045  142.221 1.00 23.30 ?  76  ILE D C     1 
ATOM   13976 O  O     . ILE D 2 97  ? 124.973 89.890  142.832 1.00 23.45 ?  76  ILE D O     1 
ATOM   13977 C  CB    . ILE D 2 97  ? 127.598 88.041  142.256 1.00 23.96 ?  76  ILE D CB    1 
ATOM   13978 C  CG1   . ILE D 2 97  ? 126.832 87.063  143.141 1.00 24.71 ?  76  ILE D CG1   1 
ATOM   13979 C  CG2   . ILE D 2 97  ? 128.570 88.908  143.092 1.00 24.02 ?  76  ILE D CG2   1 
ATOM   13980 C  CD1   . ILE D 2 97  ? 127.590 85.728  143.342 1.00 29.17 ?  76  ILE D CD1   1 
ATOM   13981 N  N     . VAL D 2 98  ? 126.702 91.194  142.213 1.00 22.71 ?  77  VAL D N     1 
ATOM   13982 C  CA    . VAL D 2 98  ? 126.193 92.383  142.917 1.00 22.78 ?  77  VAL D CA    1 
ATOM   13983 C  C     . VAL D 2 98  ? 124.939 92.916  142.222 1.00 22.89 ?  77  VAL D C     1 
ATOM   13984 O  O     . VAL D 2 98  ? 123.954 93.258  142.877 1.00 23.72 ?  77  VAL D O     1 
ATOM   13985 C  CB    . VAL D 2 98  ? 127.292 93.470  143.077 1.00 22.49 ?  77  VAL D CB    1 
ATOM   13986 C  CG1   . VAL D 2 98  ? 126.710 94.795  143.601 1.00 21.91 ?  77  VAL D CG1   1 
ATOM   13987 C  CG2   . VAL D 2 98  ? 128.370 92.970  144.024 1.00 23.02 ?  77  VAL D CG2   1 
ATOM   13988 N  N     . ALA D 2 99  ? 124.960 92.952  140.890 1.00 23.19 ?  78  ALA D N     1 
ATOM   13989 C  CA    . ALA D 2 99  ? 123.782 93.372  140.117 1.00 23.05 ?  78  ALA D CA    1 
ATOM   13990 C  C     . ALA D 2 99  ? 122.577 92.479  140.425 1.00 23.52 ?  78  ALA D C     1 
ATOM   13991 O  O     . ALA D 2 99  ? 121.437 92.949  140.509 1.00 23.68 ?  78  ALA D O     1 
ATOM   13992 C  CB    . ALA D 2 99  ? 124.096 93.369  138.630 1.00 22.81 ?  78  ALA D CB    1 
ATOM   13993 N  N     . GLU D 2 100 ? 122.830 91.186  140.602 1.00 23.68 ?  79  GLU D N     1 
ATOM   13994 C  CA    . GLU D 2 100 ? 121.768 90.237  140.928 1.00 24.14 ?  79  GLU D CA    1 
ATOM   13995 C  C     . GLU D 2 100 ? 121.079 90.504  142.276 1.00 23.66 ?  79  GLU D C     1 
ATOM   13996 O  O     . GLU D 2 100 ? 119.852 90.416  142.382 1.00 22.94 ?  79  GLU D O     1 
ATOM   13997 C  CB    . GLU D 2 100 ? 122.324 88.814  140.891 1.00 24.47 ?  79  GLU D CB    1 
ATOM   13998 C  CG    . GLU D 2 100 ? 121.263 87.734  140.981 1.00 27.90 ?  79  GLU D CG    1 
ATOM   13999 C  CD    . GLU D 2 100 ? 121.856 86.343  141.122 1.00 32.30 ?  79  GLU D CD    1 
ATOM   14000 O  OE1   . GLU D 2 100 ? 123.003 86.125  140.672 1.00 32.88 ?  79  GLU D OE1   1 
ATOM   14001 O  OE2   . GLU D 2 100 ? 121.167 85.472  141.691 1.00 34.74 -1 79  GLU D OE2   1 
ATOM   14002 N  N     . HIS D 2 101 ? 121.864 90.820  143.304 1.00 23.62 ?  80  HIS D N     1 
ATOM   14003 C  CA    . HIS D 2 101 ? 121.318 90.990  144.664 1.00 23.99 ?  80  HIS D CA    1 
ATOM   14004 C  C     . HIS D 2 101 ? 120.869 92.407  145.045 1.00 24.35 ?  80  HIS D C     1 
ATOM   14005 O  O     . HIS D 2 101 ? 120.117 92.576  146.006 1.00 24.21 ?  80  HIS D O     1 
ATOM   14006 C  CB    . HIS D 2 101 ? 122.294 90.425  145.706 1.00 24.13 ?  80  HIS D CB    1 
ATOM   14007 C  CG    . HIS D 2 101 ? 122.474 88.939  145.607 1.00 24.76 ?  80  HIS D CG    1 
ATOM   14008 N  ND1   . HIS D 2 101 ? 121.732 88.048  146.354 1.00 25.68 ?  80  HIS D ND1   1 
ATOM   14009 C  CD2   . HIS D 2 101 ? 123.292 88.190  144.831 1.00 25.75 ?  80  HIS D CD2   1 
ATOM   14010 C  CE1   . HIS D 2 101 ? 122.091 86.813  146.045 1.00 26.21 ?  80  HIS D CE1   1 
ATOM   14011 N  NE2   . HIS D 2 101 ? 123.036 86.871  145.124 1.00 25.35 ?  80  HIS D NE2   1 
ATOM   14012 N  N     . VAL D 2 102 ? 121.332 93.420  144.314 1.00 24.50 ?  81  VAL D N     1 
ATOM   14013 C  CA    . VAL D 2 102 ? 120.917 94.800  144.565 1.00 25.50 ?  81  VAL D CA    1 
ATOM   14014 C  C     . VAL D 2 102 ? 119.497 95.033  144.023 1.00 26.14 ?  81  VAL D C     1 
ATOM   14015 O  O     . VAL D 2 102 ? 119.193 94.630  142.904 1.00 26.96 ?  81  VAL D O     1 
ATOM   14016 C  CB    . VAL D 2 102 ? 121.913 95.813  143.930 1.00 25.30 ?  81  VAL D CB    1 
ATOM   14017 C  CG1   . VAL D 2 102 ? 121.351 97.215  143.945 1.00 27.08 ?  81  VAL D CG1   1 
ATOM   14018 C  CG2   . VAL D 2 102 ? 123.236 95.790  144.678 1.00 25.41 ?  81  VAL D CG2   1 
ATOM   14019 N  N     . ASP D 2 103 ? 118.641 95.662  144.824 1.00 26.45 ?  82  ASP D N     1 
ATOM   14020 C  CA    . ASP D 2 103 ? 117.297 96.040  144.383 1.00 27.15 ?  82  ASP D CA    1 
ATOM   14021 C  C     . ASP D 2 103 ? 117.306 97.431  143.767 1.00 26.39 ?  82  ASP D C     1 
ATOM   14022 O  O     . ASP D 2 103 ? 118.001 98.335  144.249 1.00 26.40 ?  82  ASP D O     1 
ATOM   14023 C  CB    . ASP D 2 103 ? 116.299 96.006  145.545 1.00 27.72 ?  82  ASP D CB    1 
ATOM   14024 C  CG    . ASP D 2 103 ? 116.128 94.616  146.148 1.00 31.46 ?  82  ASP D CG    1 
ATOM   14025 O  OD1   . ASP D 2 103 ? 116.237 93.594  145.418 1.00 34.26 ?  82  ASP D OD1   1 
ATOM   14026 O  OD2   . ASP D 2 103 ? 115.870 94.544  147.372 1.00 35.52 -1 82  ASP D OD2   1 
ATOM   14027 N  N     . GLY D 2 104 ? 116.515 97.602  142.712 1.00 25.52 ?  83  GLY D N     1 
ATOM   14028 C  CA    . GLY D 2 104 ? 116.387 98.895  142.043 1.00 24.31 ?  83  GLY D CA    1 
ATOM   14029 C  C     . GLY D 2 104 ? 116.737 98.738  140.567 1.00 23.27 ?  83  GLY D C     1 
ATOM   14030 O  O     . GLY D 2 104 ? 117.821 98.268  140.225 1.00 22.38 ?  83  GLY D O     1 
ATOM   14031 N  N     . HIS D 2 105 ? 115.809 99.116  139.692 1.00 22.46 ?  84  HIS D N     1 
ATOM   14032 C  CA    . HIS D 2 105 ? 116.035 98.997  138.250 1.00 22.17 ?  84  HIS D CA    1 
ATOM   14033 C  C     . HIS D 2 105 ? 117.203 99.832  137.751 1.00 21.13 ?  84  HIS D C     1 
ATOM   14034 O  O     . HIS D 2 105 ? 117.961 99.383  136.894 1.00 20.91 ?  84  HIS D O     1 
ATOM   14035 C  CB    . HIS D 2 105 ? 114.761 99.350  137.471 1.00 22.07 ?  84  HIS D CB    1 
ATOM   14036 C  CG    . HIS D 2 105 ? 113.601 98.473  137.820 1.00 23.85 ?  84  HIS D CG    1 
ATOM   14037 N  ND1   . HIS D 2 105 ? 113.686 97.097  137.801 1.00 24.86 ?  84  HIS D ND1   1 
ATOM   14038 C  CD2   . HIS D 2 105 ? 112.346 98.769  138.231 1.00 25.19 ?  84  HIS D CD2   1 
ATOM   14039 C  CE1   . HIS D 2 105 ? 112.525 96.583  138.165 1.00 24.94 ?  84  HIS D CE1   1 
ATOM   14040 N  NE2   . HIS D 2 105 ? 111.698 97.577  138.437 1.00 26.41 ?  84  HIS D NE2   1 
ATOM   14041 N  N     . GLN D 2 106 ? 117.345 101.039 138.279 1.00 20.66 ?  85  GLN D N     1 
ATOM   14042 C  CA    . GLN D 2 106 ? 118.365 101.951 137.769 1.00 20.70 ?  85  GLN D CA    1 
ATOM   14043 C  C     . GLN D 2 106 ? 119.751 101.498 138.224 1.00 20.46 ?  85  GLN D C     1 
ATOM   14044 O  O     . GLN D 2 106 ? 120.709 101.566 137.453 1.00 20.72 ?  85  GLN D O     1 
ATOM   14045 C  CB    . GLN D 2 106 ? 118.043 103.411 138.129 1.00 20.60 ?  85  GLN D CB    1 
ATOM   14046 C  CG    . GLN D 2 106 ? 116.703 103.900 137.516 1.00 20.74 ?  85  GLN D CG    1 
ATOM   14047 C  CD    . GLN D 2 106 ? 116.246 105.278 138.010 1.00 22.11 ?  85  GLN D CD    1 
ATOM   14048 O  OE1   . GLN D 2 106 ? 117.058 106.124 138.370 1.00 22.88 ?  85  GLN D OE1   1 
ATOM   14049 N  NE2   . GLN D 2 106 ? 114.935 105.504 138.012 1.00 21.64 ?  85  GLN D NE2   1 
ATOM   14050 N  N     . ARG D 2 107 ? 119.839 100.987 139.454 1.00 20.17 ?  86  ARG D N     1 
ATOM   14051 C  CA    . ARG D 2 107 ? 121.094 100.440 139.975 1.00 20.29 ?  86  ARG D CA    1 
ATOM   14052 C  C     . ARG D 2 107 ? 121.512 99.209  139.188 1.00 20.07 ?  86  ARG D C     1 
ATOM   14053 O  O     . ARG D 2 107 ? 122.683 99.051  138.868 1.00 19.53 ?  86  ARG D O     1 
ATOM   14054 C  CB    . ARG D 2 107 ? 120.959 100.066 141.449 1.00 20.88 ?  86  ARG D CB    1 
ATOM   14055 C  CG    . ARG D 2 107 ? 120.572 101.222 142.311 1.00 22.56 ?  86  ARG D CG    1 
ATOM   14056 C  CD    . ARG D 2 107 ? 120.132 100.749 143.674 1.00 27.21 ?  86  ARG D CD    1 
ATOM   14057 N  NE    . ARG D 2 107 ? 120.276 101.878 144.573 1.00 31.70 ?  86  ARG D NE    1 
ATOM   14058 C  CZ    . ARG D 2 107 ? 120.373 101.799 145.884 1.00 32.23 ?  86  ARG D CZ    1 
ATOM   14059 N  NH1   . ARG D 2 107 ? 120.330 100.618 146.499 1.00 34.27 1  86  ARG D NH1   1 
ATOM   14060 N  NH2   . ARG D 2 107 ? 120.520 102.919 146.568 1.00 33.79 ?  86  ARG D NH2   1 
ATOM   14061 N  N     . LYS D 2 108 ? 120.553 98.330  138.894 1.00 19.61 ?  87  LYS D N     1 
ATOM   14062 C  CA    . LYS D 2 108 ? 120.851 97.146  138.089 1.00 19.92 ?  87  LYS D CA    1 
ATOM   14063 C  C     . LYS D 2 108 ? 121.382 97.524  136.702 1.00 20.08 ?  87  LYS D C     1 
ATOM   14064 O  O     . LYS D 2 108 ? 122.242 96.827  136.152 1.00 20.38 ?  87  LYS D O     1 
ATOM   14065 C  CB    . LYS D 2 108 ? 119.641 96.216  137.972 1.00 19.54 ?  87  LYS D CB    1 
ATOM   14066 C  CG    . LYS D 2 108 ? 119.229 95.562  139.277 1.00 20.55 ?  87  LYS D CG    1 
ATOM   14067 C  CD    . LYS D 2 108 ? 118.034 94.627  139.079 1.00 21.09 ?  87  LYS D CD    1 
ATOM   14068 C  CE    . LYS D 2 108 ? 117.632 93.927  140.373 1.00 22.98 ?  87  LYS D CE    1 
ATOM   14069 N  NZ    . LYS D 2 108 ? 118.647 92.874  140.759 1.00 22.30 1  87  LYS D NZ    1 
ATOM   14070 N  N     . ALA D 2 109 ? 120.867 98.615  136.138 1.00 19.72 ?  88  ALA D N     1 
ATOM   14071 C  CA    . ALA D 2 109 ? 121.308 99.063  134.822 1.00 19.83 ?  88  ALA D CA    1 
ATOM   14072 C  C     . ALA D 2 109 ? 122.748 99.576  134.862 1.00 19.84 ?  88  ALA D C     1 
ATOM   14073 O  O     . ALA D 2 109 ? 123.565 99.219  134.006 1.00 19.96 ?  88  ALA D O     1 
ATOM   14074 C  CB    . ALA D 2 109 ? 120.350 100.124 134.254 1.00 19.65 ?  88  ALA D CB    1 
ATOM   14075 N  N     . VAL D 2 110 ? 123.064 100.389 135.867 1.00 19.33 ?  89  VAL D N     1 
ATOM   14076 C  CA    . VAL D 2 110 ? 124.429 100.910 136.032 1.00 19.22 ?  89  VAL D CA    1 
ATOM   14077 C  C     . VAL D 2 110 ? 125.394 99.731  136.255 1.00 19.45 ?  89  VAL D C     1 
ATOM   14078 O  O     . VAL D 2 110 ? 126.402 99.592  135.549 1.00 18.97 ?  89  VAL D O     1 
ATOM   14079 C  CB    . VAL D 2 110 ? 124.490 101.982 137.158 1.00 19.01 ?  89  VAL D CB    1 
ATOM   14080 C  CG1   . VAL D 2 110 ? 125.953 102.404 137.481 1.00 19.90 ?  89  VAL D CG1   1 
ATOM   14081 C  CG2   . VAL D 2 110 ? 123.692 103.197 136.741 1.00 19.69 ?  89  VAL D CG2   1 
ATOM   14082 N  N     . LEU D 2 111 ? 125.038 98.844  137.186 1.00 19.27 ?  90  LEU D N     1 
ATOM   14083 C  CA    . LEU D 2 111 ? 125.851 97.652  137.435 1.00 19.96 ?  90  LEU D CA    1 
ATOM   14084 C  C     . LEU D 2 111 ? 126.051 96.777  136.191 1.00 20.30 ?  90  LEU D C     1 
ATOM   14085 O  O     . LEU D 2 111 ? 127.161 96.294  135.949 1.00 19.88 ?  90  LEU D O     1 
ATOM   14086 C  CB    . LEU D 2 111 ? 125.312 96.847  138.626 1.00 19.87 ?  90  LEU D CB    1 
ATOM   14087 C  CG    . LEU D 2 111 ? 125.450 97.582  139.961 1.00 20.24 ?  90  LEU D CG    1 
ATOM   14088 C  CD1   . LEU D 2 111 ? 124.610 96.949  141.082 1.00 21.85 ?  90  LEU D CD1   1 
ATOM   14089 C  CD2   . LEU D 2 111 ? 126.929 97.710  140.374 1.00 20.29 ?  90  LEU D CD2   1 
ATOM   14090 N  N     . ASN D 2 112 ? 124.994 96.597  135.395 1.00 20.92 ?  91  ASN D N     1 
ATOM   14091 C  CA    . ASN D 2 112 ? 125.115 95.907  134.089 1.00 20.70 ?  91  ASN D CA    1 
ATOM   14092 C  C     . ASN D 2 112 ? 126.095 96.583  133.147 1.00 20.57 ?  91  ASN D C     1 
ATOM   14093 O  O     . ASN D 2 112 ? 126.819 95.911  132.394 1.00 20.45 ?  91  ASN D O     1 
ATOM   14094 C  CB    . ASN D 2 112 ? 123.772 95.857  133.359 1.00 21.16 ?  91  ASN D CB    1 
ATOM   14095 C  CG    . ASN D 2 112 ? 123.020 94.561  133.583 1.00 21.98 ?  91  ASN D CG    1 
ATOM   14096 O  OD1   . ASN D 2 112 ? 123.434 93.699  134.364 1.00 25.37 ?  91  ASN D OD1   1 
ATOM   14097 N  ND2   . ASN D 2 112 ? 121.891 94.428  132.912 1.00 21.12 ?  91  ASN D ND2   1 
ATOM   14098 N  N     . PHE D 2 113 ? 126.053 97.913  133.124 1.00 19.70 ?  92  PHE D N     1 
ATOM   14099 C  CA    . PHE D 2 113 ? 126.968 98.668  132.297 1.00 20.02 ?  92  PHE D CA    1 
ATOM   14100 C  C     . PHE D 2 113 ? 128.422 98.436  132.738 1.00 19.97 ?  92  PHE D C     1 
ATOM   14101 O  O     . PHE D 2 113 ? 129.304 98.213  131.902 1.00 19.22 ?  92  PHE D O     1 
ATOM   14102 C  CB    . PHE D 2 113 ? 126.628 100.168 132.275 1.00 20.09 ?  92  PHE D CB    1 
ATOM   14103 C  CG    . PHE D 2 113 ? 127.448 100.932 131.295 1.00 20.54 ?  92  PHE D CG    1 
ATOM   14104 C  CD1   . PHE D 2 113 ? 127.019 101.079 129.975 1.00 20.14 ?  92  PHE D CD1   1 
ATOM   14105 C  CD2   . PHE D 2 113 ? 128.688 101.453 131.671 1.00 20.77 ?  92  PHE D CD2   1 
ATOM   14106 C  CE1   . PHE D 2 113 ? 127.803 101.761 129.049 1.00 20.54 ?  92  PHE D CE1   1 
ATOM   14107 C  CE2   . PHE D 2 113 ? 129.482 102.131 130.747 1.00 21.23 ?  92  PHE D CE2   1 
ATOM   14108 C  CZ    . PHE D 2 113 ? 129.032 102.280 129.429 1.00 20.92 ?  92  PHE D CZ    1 
ATOM   14109 N  N     . MET D 2 114 ? 128.655 98.478  134.046 1.00 19.67 ?  93  MET D N     1 
ATOM   14110 C  CA    . MET D 2 114 ? 129.981 98.206  134.586 1.00 20.55 ?  93  MET D CA    1 
ATOM   14111 C  C     . MET D 2 114 ? 130.458 96.788  134.265 1.00 20.82 ?  93  MET D C     1 
ATOM   14112 O  O     . MET D 2 114 ? 131.612 96.621  133.894 1.00 20.43 ?  93  MET D O     1 
ATOM   14113 C  CB    . MET D 2 114 ? 130.023 98.464  136.088 1.00 20.24 ?  93  MET D CB    1 
ATOM   14114 C  CG    . MET D 2 114 ? 129.623 99.888  136.414 1.00 22.05 ?  93  MET D CG    1 
ATOM   14115 S  SD    . MET D 2 114 ? 129.454 100.227 138.151 1.00 25.85 ?  93  MET D SD    1 
ATOM   14116 C  CE    . MET D 2 114 ? 129.704 102.009 138.130 1.00 27.57 ?  93  MET D CE    1 
ATOM   14117 N  N     . ALA D 2 115 ? 129.574 95.789  134.406 1.00 21.19 ?  94  ALA D N     1 
ATOM   14118 C  CA    . ALA D 2 115 ? 129.912 94.398  134.046 1.00 21.53 ?  94  ALA D CA    1 
ATOM   14119 C  C     . ALA D 2 115 ? 130.278 94.293  132.567 1.00 21.75 ?  94  ALA D C     1 
ATOM   14120 O  O     . ALA D 2 115 ? 131.256 93.633  132.217 1.00 22.18 ?  94  ALA D O     1 
ATOM   14121 C  CB    . ALA D 2 115 ? 128.771 93.436  134.395 1.00 21.32 ?  94  ALA D CB    1 
ATOM   14122 N  N     . MET D 2 116 ? 129.510 94.969  131.710 1.00 21.47 ?  95  MET D N     1 
ATOM   14123 C  CA    . MET D 2 116 ? 129.812 95.034  130.283 1.00 21.83 ?  95  MET D CA    1 
ATOM   14124 C  C     . MET D 2 116 ? 131.236 95.563  130.022 1.00 22.15 ?  95  MET D C     1 
ATOM   14125 O  O     . MET D 2 116 ? 131.977 94.983  129.232 1.00 22.09 ?  95  MET D O     1 
ATOM   14126 C  CB    . MET D 2 116 ? 128.766 95.887  129.546 1.00 21.72 ?  95  MET D CB    1 
ATOM   14127 C  CG    . MET D 2 116 ? 129.042 96.108  128.050 1.00 22.57 ?  95  MET D CG    1 
ATOM   14128 S  SD    . MET D 2 116 ? 130.280 97.382  127.692 1.00 22.75 ?  95  MET D SD    1 
ATOM   14129 C  CE    . MET D 2 116 ? 129.442 98.867  128.245 1.00 22.96 ?  95  MET D CE    1 
ATOM   14130 N  N     . MET D 2 117 ? 131.606 96.658  130.690 1.00 22.04 ?  96  MET D N     1 
ATOM   14131 C  CA    . MET D 2 117 ? 132.943 97.253  130.521 1.00 22.45 ?  96  MET D CA    1 
ATOM   14132 C  C     . MET D 2 117 ? 134.058 96.262  130.895 1.00 22.39 ?  96  MET D C     1 
ATOM   14133 O  O     . MET D 2 117 ? 135.081 96.184  130.212 1.00 21.88 ?  96  MET D O     1 
ATOM   14134 C  CB    . MET D 2 117 ? 133.077 98.564  131.322 1.00 22.00 ?  96  MET D CB    1 
ATOM   14135 C  CG    . MET D 2 117 ? 132.268 99.746  130.726 1.00 23.25 ?  96  MET D CG    1 
ATOM   14136 S  SD    . MET D 2 117 ? 132.719 100.154 129.023 1.00 24.28 ?  96  MET D SD    1 
ATOM   14137 C  CE    . MET D 2 117 ? 134.316 100.929 129.247 1.00 24.59 ?  96  MET D CE    1 
ATOM   14138 N  N     . GLU D 2 118 ? 133.846 95.493  131.963 1.00 22.66 ?  97  GLU D N     1 
ATOM   14139 C  CA    . GLU D 2 118 ? 134.818 94.472  132.373 1.00 23.52 ?  97  GLU D CA    1 
ATOM   14140 C  C     . GLU D 2 118 ? 135.024 93.429  131.288 1.00 24.25 ?  97  GLU D C     1 
ATOM   14141 O  O     . GLU D 2 118 ? 136.164 93.149  130.909 1.00 25.05 ?  97  GLU D O     1 
ATOM   14142 C  CB    . GLU D 2 118 ? 134.417 93.767  133.690 1.00 23.11 ?  97  GLU D CB    1 
ATOM   14143 C  CG    . GLU D 2 118 ? 133.914 94.672  134.822 1.00 23.08 ?  97  GLU D CG    1 
ATOM   14144 C  CD    . GLU D 2 118 ? 134.980 95.565  135.436 1.00 24.08 ?  97  GLU D CD    1 
ATOM   14145 O  OE1   . GLU D 2 118 ? 136.046 95.739  134.826 1.00 26.39 ?  97  GLU D OE1   1 
ATOM   14146 O  OE2   . GLU D 2 118 ? 134.739 96.121  136.527 1.00 27.52 -1 97  GLU D OE2   1 
ATOM   14147 N  N     . ASN D 2 119 ? 133.922 92.880  130.782 1.00 25.47 ?  98  ASN D N     1 
ATOM   14148 C  CA    . ASN D 2 119 ? 133.939 91.718  129.871 1.00 26.32 ?  98  ASN D CA    1 
ATOM   14149 C  C     . ASN D 2 119 ? 134.166 92.050  128.399 1.00 26.22 ?  98  ASN D C     1 
ATOM   14150 O  O     . ASN D 2 119 ? 134.851 91.299  127.675 1.00 26.54 ?  98  ASN D O     1 
ATOM   14151 C  CB    . ASN D 2 119 ? 132.636 90.910  130.010 1.00 26.72 ?  98  ASN D CB    1 
ATOM   14152 C  CG    . ASN D 2 119 ? 132.493 90.267  131.390 1.00 29.12 ?  98  ASN D CG    1 
ATOM   14153 O  OD1   . ASN D 2 119 ? 133.387 89.549  131.852 1.00 32.07 ?  98  ASN D OD1   1 
ATOM   14154 N  ND2   . ASN D 2 119 ? 131.383 90.550  132.062 1.00 29.12 ?  98  ASN D ND2   1 
ATOM   14155 N  N     . ALA D 2 120 ? 133.570 93.153  127.959 1.00 25.46 ?  99  ALA D N     1 
ATOM   14156 C  CA    . ALA D 2 120 ? 133.590 93.535  126.548 1.00 25.77 ?  99  ALA D CA    1 
ATOM   14157 C  C     . ALA D 2 120 ? 134.714 94.505  126.198 1.00 25.51 ?  99  ALA D C     1 
ATOM   14158 O  O     . ALA D 2 120 ? 135.173 94.530  125.053 1.00 26.64 ?  99  ALA D O     1 
ATOM   14159 C  CB    . ALA D 2 120 ? 132.233 94.122  126.127 1.00 25.75 ?  99  ALA D CB    1 
ATOM   14160 N  N     . VAL D 2 121 ? 135.150 95.305  127.165 1.00 24.40 ?  100 VAL D N     1 
ATOM   14161 C  CA    . VAL D 2 121 ? 136.111 96.363  126.873 1.00 24.15 ?  100 VAL D CA    1 
ATOM   14162 C  C     . VAL D 2 121 ? 137.465 96.100  127.537 1.00 23.94 ?  100 VAL D C     1 
ATOM   14163 O  O     . VAL D 2 121 ? 138.485 95.977  126.851 1.00 23.75 ?  100 VAL D O     1 
ATOM   14164 C  CB    . VAL D 2 121 ? 135.552 97.770  127.243 1.00 23.68 ?  100 VAL D CB    1 
ATOM   14165 C  CG1   . VAL D 2 121 ? 136.559 98.864  126.891 1.00 23.76 ?  100 VAL D CG1   1 
ATOM   14166 C  CG2   . VAL D 2 121 ? 134.231 98.020  126.509 1.00 23.99 ?  100 VAL D CG2   1 
ATOM   14167 N  N     . HIS D 2 122 ? 137.467 96.009  128.866 1.00 23.68 ?  101 HIS D N     1 
ATOM   14168 C  CA    . HIS D 2 122 ? 138.702 95.782  129.619 1.00 24.02 ?  101 HIS D CA    1 
ATOM   14169 C  C     . HIS D 2 122 ? 139.392 94.480  129.247 1.00 24.39 ?  101 HIS D C     1 
ATOM   14170 O  O     . HIS D 2 122 ? 140.599 94.475  129.015 1.00 24.71 ?  101 HIS D O     1 
ATOM   14171 C  CB    . HIS D 2 122 ? 138.470 95.844  131.134 1.00 23.20 ?  101 HIS D CB    1 
ATOM   14172 C  CG    . HIS D 2 122 ? 138.022 97.186  131.624 1.00 22.82 ?  101 HIS D CG    1 
ATOM   14173 N  ND1   . HIS D 2 122 ? 137.702 97.424  132.942 1.00 20.48 ?  101 HIS D ND1   1 
ATOM   14174 C  CD2   . HIS D 2 122 ? 137.815 98.355  130.968 1.00 21.03 ?  101 HIS D CD2   1 
ATOM   14175 C  CE1   . HIS D 2 122 ? 137.332 98.684  133.082 1.00 19.88 ?  101 HIS D CE1   1 
ATOM   14176 N  NE2   . HIS D 2 122 ? 137.394 99.272  131.899 1.00 21.62 ?  101 HIS D NE2   1 
ATOM   14177 N  N     . ALA D 2 123 ? 138.637 93.384  129.180 1.00 25.30 ?  102 ALA D N     1 
ATOM   14178 C  CA    . ALA D 2 123 ? 139.239 92.070  128.905 1.00 25.77 ?  102 ALA D CA    1 
ATOM   14179 C  C     . ALA D 2 123 ? 139.881 92.004  127.515 1.00 26.37 ?  102 ALA D C     1 
ATOM   14180 O  O     . ALA D 2 123 ? 140.959 91.422  127.344 1.00 25.87 ?  102 ALA D O     1 
ATOM   14181 C  CB    . ALA D 2 123 ? 138.210 90.946  129.085 1.00 26.43 ?  102 ALA D CB    1 
ATOM   14182 N  N     . LYS D 2 124 ? 139.212 92.606  126.531 1.00 26.51 ?  103 LYS D N     1 
ATOM   14183 C  CA    . LYS D 2 124 ? 139.733 92.669  125.173 1.00 27.22 ?  103 LYS D CA    1 
ATOM   14184 C  C     . LYS D 2 124 ? 140.980 93.565  125.114 1.00 26.63 ?  103 LYS D C     1 
ATOM   14185 O  O     . LYS D 2 124 ? 141.918 93.271  124.374 1.00 26.07 ?  103 LYS D O     1 
ATOM   14186 C  CB    . LYS D 2 124 ? 138.647 93.162  124.196 1.00 27.51 ?  103 LYS D CB    1 
ATOM   14187 C  CG    . LYS D 2 124 ? 139.105 93.357  122.734 1.00 30.58 ?  103 LYS D CG    1 
ATOM   14188 C  CD    . LYS D 2 124 ? 139.456 92.039  122.058 1.00 35.72 ?  103 LYS D CD    1 
ATOM   14189 C  CE    . LYS D 2 124 ? 139.940 92.236  120.619 1.00 37.33 ?  103 LYS D CE    1 
ATOM   14190 N  NZ    . LYS D 2 124 ? 138.843 92.760  119.764 1.00 40.73 1  103 LYS D NZ    1 
ATOM   14191 N  N     . SER D 2 125 ? 140.980 94.635  125.914 1.00 26.02 ?  104 SER D N     1 
ATOM   14192 C  CA    . SER D 2 125 ? 142.094 95.586  125.967 1.00 26.16 ?  104 SER D CA    1 
ATOM   14193 C  C     . SER D 2 125 ? 143.371 94.952  126.520 1.00 26.18 ?  104 SER D C     1 
ATOM   14194 O  O     . SER D 2 125 ? 144.460 95.171  125.976 1.00 26.06 ?  104 SER D O     1 
ATOM   14195 C  CB    . SER D 2 125 ? 141.726 96.821  126.792 1.00 26.10 ?  104 SER D CB    1 
ATOM   14196 O  OG    . SER D 2 125 ? 140.692 97.547  126.152 1.00 26.58 ?  104 SER D OG    1 
ATOM   14197 N  N     . TYR D 2 126 ? 143.229 94.175  127.591 1.00 25.68 ?  105 TYR D N     1 
ATOM   14198 C  CA    . TYR D 2 126 ? 144.362 93.455  128.185 1.00 26.12 ?  105 TYR D CA    1 
ATOM   14199 C  C     . TYR D 2 126 ? 144.920 92.420  127.203 1.00 26.38 ?  105 TYR D C     1 
ATOM   14200 O  O     . TYR D 2 126 ? 146.136 92.300  127.034 1.00 26.83 ?  105 TYR D O     1 
ATOM   14201 C  CB    . TYR D 2 126 ? 143.961 92.762  129.501 1.00 25.35 ?  105 TYR D CB    1 
ATOM   14202 C  CG    . TYR D 2 126 ? 143.877 93.673  130.711 1.00 25.46 ?  105 TYR D CG    1 
ATOM   14203 C  CD1   . TYR D 2 126 ? 144.968 94.456  131.092 1.00 25.41 ?  105 TYR D CD1   1 
ATOM   14204 C  CD2   . TYR D 2 126 ? 142.718 93.728  131.500 1.00 24.77 ?  105 TYR D CD2   1 
ATOM   14205 C  CE1   . TYR D 2 126 ? 144.905 95.294  132.203 1.00 25.89 ?  105 TYR D CE1   1 
ATOM   14206 C  CE2   . TYR D 2 126 ? 142.646 94.570  132.621 1.00 23.11 ?  105 TYR D CE2   1 
ATOM   14207 C  CZ    . TYR D 2 126 ? 143.749 95.336  132.972 1.00 25.38 ?  105 TYR D CZ    1 
ATOM   14208 O  OH    . TYR D 2 126 ? 143.714 96.171  134.068 1.00 23.31 ?  105 TYR D OH    1 
ATOM   14209 N  N     . SER D 2 127 ? 144.025 91.693  126.544 1.00 27.16 ?  106 SER D N     1 
ATOM   14210 C  CA    . SER D 2 127 ? 144.415 90.703  125.535 1.00 27.83 ?  106 SER D CA    1 
ATOM   14211 C  C     . SER D 2 127 ? 145.204 91.358  124.392 1.00 28.21 ?  106 SER D C     1 
ATOM   14212 O  O     . SER D 2 127 ? 146.268 90.858  124.004 1.00 28.30 ?  106 SER D O     1 
ATOM   14213 C  CB    . SER D 2 127 ? 143.179 89.957  125.005 1.00 28.37 ?  106 SER D CB    1 
ATOM   14214 O  OG    . SER D 2 127 ? 143.521 89.067  123.944 1.00 29.33 ?  106 SER D OG    1 
ATOM   14215 N  N     . ASN D 2 128 ? 144.681 92.474  123.873 1.00 28.27 ?  107 ASN D N     1 
ATOM   14216 C  CA    . ASN D 2 128 ? 145.348 93.278  122.837 1.00 28.79 ?  107 ASN D CA    1 
ATOM   14217 C  C     . ASN D 2 128 ? 146.758 93.725  123.214 1.00 28.53 ?  107 ASN D C     1 
ATOM   14218 O  O     . ASN D 2 128 ? 147.677 93.632  122.393 1.00 28.03 ?  107 ASN D O     1 
ATOM   14219 C  CB    . ASN D 2 128 ? 144.514 94.514  122.453 1.00 29.05 ?  107 ASN D CB    1 
ATOM   14220 C  CG    . ASN D 2 128 ? 143.241 94.156  121.680 1.00 30.48 ?  107 ASN D CG    1 
ATOM   14221 O  OD1   . ASN D 2 128 ? 143.057 93.020  121.251 1.00 32.19 ?  107 ASN D OD1   1 
ATOM   14222 N  ND2   . ASN D 2 128 ? 142.352 95.131  121.521 1.00 31.59 ?  107 ASN D ND2   1 
ATOM   14223 N  N     . ILE D 2 129 ? 146.923 94.234  124.437 1.00 28.21 ?  108 ILE D N     1 
ATOM   14224 C  CA    . ILE D 2 129 ? 148.255 94.619  124.921 1.00 28.76 ?  108 ILE D CA    1 
ATOM   14225 C  C     . ILE D 2 129 ? 149.213 93.416  124.905 1.00 29.83 ?  108 ILE D C     1 
ATOM   14226 O  O     . ILE D 2 129 ? 150.337 93.512  124.394 1.00 29.99 ?  108 ILE D O     1 
ATOM   14227 C  CB    . ILE D 2 129 ? 148.216 95.287  126.334 1.00 28.28 ?  108 ILE D CB    1 
ATOM   14228 C  CG1   . ILE D 2 129 ? 147.425 96.603  126.296 1.00 27.94 ?  108 ILE D CG1   1 
ATOM   14229 C  CG2   . ILE D 2 129 ? 149.639 95.552  126.845 1.00 27.52 ?  108 ILE D CG2   1 
ATOM   14230 C  CD1   . ILE D 2 129 ? 147.025 97.131  127.668 1.00 27.98 ?  108 ILE D CD1   1 
ATOM   14231 N  N     . PHE D 2 130 ? 148.769 92.291  125.458 1.00 30.86 ?  109 PHE D N     1 
ATOM   14232 C  CA    . PHE D 2 130 ? 149.573 91.072  125.471 1.00 32.76 ?  109 PHE D CA    1 
ATOM   14233 C  C     . PHE D 2 130 ? 150.003 90.615  124.074 1.00 34.37 ?  109 PHE D C     1 
ATOM   14234 O  O     . PHE D 2 130 ? 151.189 90.401  123.832 1.00 34.61 ?  109 PHE D O     1 
ATOM   14235 C  CB    . PHE D 2 130 ? 148.836 89.939  126.180 1.00 32.81 ?  109 PHE D CB    1 
ATOM   14236 C  CG    . PHE D 2 130 ? 149.204 89.785  127.628 1.00 33.84 ?  109 PHE D CG    1 
ATOM   14237 C  CD1   . PHE D 2 130 ? 150.475 89.350  127.993 1.00 34.61 ?  109 PHE D CD1   1 
ATOM   14238 C  CD2   . PHE D 2 130 ? 148.269 90.042  128.623 1.00 35.74 ?  109 PHE D CD2   1 
ATOM   14239 C  CE1   . PHE D 2 130 ? 150.821 89.193  129.335 1.00 36.99 ?  109 PHE D CE1   1 
ATOM   14240 C  CE2   . PHE D 2 130 ? 148.601 89.889  129.975 1.00 36.96 ?  109 PHE D CE2   1 
ATOM   14241 C  CZ    . PHE D 2 130 ? 149.880 89.464  130.333 1.00 36.91 ?  109 PHE D CZ    1 
ATOM   14242 N  N     . MET D 2 131 ? 149.034 90.485  123.168 1.00 35.90 ?  110 MET D N     1 
ATOM   14243 C  CA    . MET D 2 131 ? 149.279 90.017  121.802 1.00 37.94 ?  110 MET D CA    1 
ATOM   14244 C  C     . MET D 2 131 ? 150.240 90.921  121.042 1.00 38.05 ?  110 MET D C     1 
ATOM   14245 O  O     . MET D 2 131 ? 150.945 90.459  120.152 1.00 38.20 ?  110 MET D O     1 
ATOM   14246 C  CB    . MET D 2 131 ? 147.965 89.873  121.018 1.00 38.63 ?  110 MET D CB    1 
ATOM   14247 C  CG    . MET D 2 131 ? 147.043 88.745  121.510 1.00 42.34 ?  110 MET D CG    1 
ATOM   14248 S  SD    . MET D 2 131 ? 145.490 88.570  120.571 1.00 50.15 ?  110 MET D SD    1 
ATOM   14249 C  CE    . MET D 2 131 ? 144.576 90.048  121.029 1.00 48.14 ?  110 MET D CE    1 
ATOM   14250 N  N     . THR D 2 132 ? 150.262 92.205  121.398 1.00 38.12 ?  111 THR D N     1 
ATOM   14251 C  CA    . THR D 2 132 ? 151.174 93.161  120.769 1.00 38.79 ?  111 THR D CA    1 
ATOM   14252 C  C     . THR D 2 132 ? 152.628 92.976  121.240 1.00 38.81 ?  111 THR D C     1 
ATOM   14253 O  O     . THR D 2 132 ? 153.555 93.026  120.425 1.00 39.26 ?  111 THR D O     1 
ATOM   14254 C  CB    . THR D 2 132 ? 150.711 94.614  121.004 1.00 38.78 ?  111 THR D CB    1 
ATOM   14255 O  OG1   . THR D 2 132 ? 149.377 94.772  120.507 1.00 39.32 ?  111 THR D OG1   1 
ATOM   14256 C  CG2   . THR D 2 132 ? 151.616 95.603  120.276 1.00 39.75 ?  111 THR D CG2   1 
ATOM   14257 N  N     . LEU D 2 133 ? 152.811 92.749  122.542 1.00 38.34 ?  112 LEU D N     1 
ATOM   14258 C  CA    . LEU D 2 133 ? 154.136 92.735  123.169 1.00 38.36 ?  112 LEU D CA    1 
ATOM   14259 C  C     . LEU D 2 133 ? 154.820 91.367  123.220 1.00 38.94 ?  112 LEU D C     1 
ATOM   14260 O  O     . LEU D 2 133 ? 156.046 91.288  123.176 1.00 39.14 ?  112 LEU D O     1 
ATOM   14261 C  CB    . LEU D 2 133 ? 154.065 93.313  124.592 1.00 37.62 ?  112 LEU D CB    1 
ATOM   14262 C  CG    . LEU D 2 133 ? 153.471 94.711  124.784 1.00 36.50 ?  112 LEU D CG    1 
ATOM   14263 C  CD1   . LEU D 2 133 ? 153.260 95.001  126.274 1.00 35.80 ?  112 LEU D CD1   1 
ATOM   14264 C  CD2   . LEU D 2 133 ? 154.319 95.791  124.133 1.00 35.32 ?  112 LEU D CD2   1 
ATOM   14265 N  N     . ALA D 2 134 ? 154.046 90.295  123.327 1.00 39.41 ?  113 ALA D N     1 
ATOM   14266 C  CA    . ALA D 2 134 ? 154.650 88.963  123.449 1.00 40.33 ?  113 ALA D CA    1 
ATOM   14267 C  C     . ALA D 2 134 ? 154.136 87.985  122.398 1.00 41.05 ?  113 ALA D C     1 
ATOM   14268 O  O     . ALA D 2 134 ? 152.999 88.109  121.956 1.00 40.81 ?  113 ALA D O     1 
ATOM   14269 C  CB    . ALA D 2 134 ? 154.424 88.412  124.845 1.00 40.15 ?  113 ALA D CB    1 
ATOM   14270 N  N     . PRO D 2 135 ? 154.978 87.013  121.983 1.00 42.21 ?  114 PRO D N     1 
ATOM   14271 C  CA    . PRO D 2 135 ? 154.461 85.944  121.120 1.00 43.27 ?  114 PRO D CA    1 
ATOM   14272 C  C     . PRO D 2 135 ? 153.560 84.982  121.908 1.00 43.89 ?  114 PRO D C     1 
ATOM   14273 O  O     . PRO D 2 135 ? 153.643 84.928  123.138 1.00 43.31 ?  114 PRO D O     1 
ATOM   14274 C  CB    . PRO D 2 135 ? 155.727 85.229  120.642 1.00 43.69 ?  114 PRO D CB    1 
ATOM   14275 C  CG    . PRO D 2 135 ? 156.725 85.484  121.706 1.00 43.01 ?  114 PRO D CG    1 
ATOM   14276 C  CD    . PRO D 2 135 ? 156.418 86.849  122.260 1.00 42.16 ?  114 PRO D CD    1 
ATOM   14277 N  N     . THR D 2 136 ? 152.722 84.231  121.193 1.00 45.26 ?  115 THR D N     1 
ATOM   14278 C  CA    . THR D 2 136 ? 151.709 83.355  121.803 1.00 46.11 ?  115 THR D CA    1 
ATOM   14279 C  C     . THR D 2 136 ? 152.267 82.452  122.908 1.00 46.35 ?  115 THR D C     1 
ATOM   14280 O  O     . THR D 2 136 ? 151.674 82.355  123.987 1.00 46.25 ?  115 THR D O     1 
ATOM   14281 C  CB    . THR D 2 136 ? 150.955 82.513  120.737 1.00 46.59 ?  115 THR D CB    1 
ATOM   14282 O  OG1   . THR D 2 136 ? 150.427 83.385  119.732 1.00 47.80 ?  115 THR D OG1   1 
ATOM   14283 C  CG2   . THR D 2 136 ? 149.790 81.742  121.354 1.00 46.94 ?  115 THR D CG2   1 
ATOM   14284 N  N     . GLU D 2 137 ? 153.410 81.818  122.648 1.00 46.92 ?  116 GLU D N     1 
ATOM   14285 C  CA    . GLU D 2 137 ? 154.020 80.904  123.613 1.00 47.37 ?  116 GLU D CA    1 
ATOM   14286 C  C     . GLU D 2 137 ? 154.425 81.593  124.919 1.00 46.64 ?  116 GLU D C     1 
ATOM   14287 O  O     . GLU D 2 137 ? 154.267 81.012  125.994 1.00 46.89 ?  116 GLU D O     1 
ATOM   14288 C  CB    . GLU D 2 137 ? 155.212 80.155  122.997 1.00 48.04 ?  116 GLU D CB    1 
ATOM   14289 C  CG    . GLU D 2 137 ? 155.836 79.078  123.905 1.00 49.86 ?  116 GLU D CG    1 
ATOM   14290 C  CD    . GLU D 2 137 ? 154.955 77.834  124.100 1.00 52.40 ?  116 GLU D CD    1 
ATOM   14291 O  OE1   . GLU D 2 137 ? 153.776 77.969  124.497 1.00 52.97 ?  116 GLU D OE1   1 
ATOM   14292 O  OE2   . GLU D 2 137 ? 155.458 76.708  123.879 1.00 54.12 -1 116 GLU D OE2   1 
ATOM   14293 N  N     . THR D 2 138 ? 154.936 82.818  124.817 1.00 46.09 ?  117 THR D N     1 
ATOM   14294 C  CA    . THR D 2 138 ? 155.313 83.619  125.992 1.00 45.30 ?  117 THR D CA    1 
ATOM   14295 C  C     . THR D 2 138 ? 154.093 84.015  126.833 1.00 44.63 ?  117 THR D C     1 
ATOM   14296 O  O     . THR D 2 138 ? 154.148 83.988  128.066 1.00 44.51 ?  117 THR D O     1 
ATOM   14297 C  CB    . THR D 2 138 ? 156.108 84.883  125.584 1.00 45.20 ?  117 THR D CB    1 
ATOM   14298 O  OG1   . THR D 2 138 ? 157.261 84.498  124.828 1.00 45.69 ?  117 THR D OG1   1 
ATOM   14299 C  CG2   . THR D 2 138 ? 156.564 85.676  126.809 1.00 44.67 ?  117 THR D CG2   1 
ATOM   14300 N  N     . ILE D 2 139 ? 152.996 84.373  126.165 1.00 44.24 ?  118 ILE D N     1 
ATOM   14301 C  CA    . ILE D 2 139 ? 151.749 84.714  126.852 1.00 43.65 ?  118 ILE D CA    1 
ATOM   14302 C  C     . ILE D 2 139 ? 151.233 83.518  127.666 1.00 43.87 ?  118 ILE D C     1 
ATOM   14303 O  O     . ILE D 2 139 ? 150.922 83.655  128.853 1.00 43.36 ?  118 ILE D O     1 
ATOM   14304 C  CB    . ILE D 2 139 ? 150.679 85.245  125.863 1.00 43.68 ?  118 ILE D CB    1 
ATOM   14305 C  CG1   . ILE D 2 139 ? 151.119 86.599  125.287 1.00 43.30 ?  118 ILE D CG1   1 
ATOM   14306 C  CG2   . ILE D 2 139 ? 149.302 85.365  126.543 1.00 43.11 ?  118 ILE D CG2   1 
ATOM   14307 C  CD1   . ILE D 2 139 ? 150.377 87.038  124.031 1.00 43.41 ?  118 ILE D CD1   1 
ATOM   14308 N  N     . ASN D 2 140 ? 151.177 82.349  127.031 1.00 44.52 ?  119 ASN D N     1 
ATOM   14309 C  CA    . ASN D 2 140 ? 150.736 81.118  127.696 1.00 45.00 ?  119 ASN D CA    1 
ATOM   14310 C  C     . ASN D 2 140 ? 151.576 80.768  128.942 1.00 44.99 ?  119 ASN D C     1 
ATOM   14311 O  O     . ASN D 2 140 ? 151.026 80.351  129.970 1.00 44.61 ?  119 ASN D O     1 
ATOM   14312 C  CB    . ASN D 2 140 ? 150.699 79.943  126.703 1.00 45.74 ?  119 ASN D CB    1 
ATOM   14313 C  CG    . ASN D 2 140 ? 149.722 80.169  125.543 1.00 46.40 ?  119 ASN D CG    1 
ATOM   14314 O  OD1   . ASN D 2 140 ? 148.860 81.053  125.589 1.00 46.85 ?  119 ASN D OD1   1 
ATOM   14315 N  ND2   . ASN D 2 140 ? 149.854 79.355  124.498 1.00 48.16 ?  119 ASN D ND2   1 
ATOM   14316 N  N     . GLU D 2 141 ? 152.893 80.966  128.855 1.00 45.09 ?  120 GLU D N     1 
ATOM   14317 C  CA    . GLU D 2 141 ? 153.799 80.683  129.973 1.00 45.27 ?  120 GLU D CA    1 
ATOM   14318 C  C     . GLU D 2 141 ? 153.649 81.658  131.149 1.00 44.75 ?  120 GLU D C     1 
ATOM   14319 O  O     . GLU D 2 141 ? 153.660 81.242  132.312 1.00 44.37 ?  120 GLU D O     1 
ATOM   14320 C  CB    . GLU D 2 141 ? 155.254 80.644  129.501 1.00 45.75 ?  120 GLU D CB    1 
ATOM   14321 C  CG    . GLU D 2 141 ? 155.584 79.454  128.598 1.00 48.17 ?  120 GLU D CG    1 
ATOM   14322 C  CD    . GLU D 2 141 ? 157.043 79.401  128.192 1.00 50.15 ?  120 GLU D CD    1 
ATOM   14323 O  OE1   . GLU D 2 141 ? 157.921 79.498  129.076 1.00 50.90 ?  120 GLU D OE1   1 
ATOM   14324 O  OE2   . GLU D 2 141 ? 157.313 79.255  126.982 1.00 52.25 -1 120 GLU D OE2   1 
ATOM   14325 N  N     . VAL D 2 142 ? 153.528 82.949  130.839 1.00 44.31 ?  121 VAL D N     1 
ATOM   14326 C  CA    . VAL D 2 142 ? 153.311 83.978  131.858 1.00 43.91 ?  121 VAL D CA    1 
ATOM   14327 C  C     . VAL D 2 142 ? 152.010 83.713  132.623 1.00 43.71 ?  121 VAL D C     1 
ATOM   14328 O  O     . VAL D 2 142 ? 151.974 83.816  133.848 1.00 43.44 ?  121 VAL D O     1 
ATOM   14329 C  CB    . VAL D 2 142 ? 153.306 85.408  131.251 1.00 43.65 ?  121 VAL D CB    1 
ATOM   14330 C  CG1   . VAL D 2 142 ? 152.948 86.450  132.310 1.00 43.40 ?  121 VAL D CG1   1 
ATOM   14331 C  CG2   . VAL D 2 142 ? 154.667 85.734  130.645 1.00 43.96 ?  121 VAL D CG2   1 
ATOM   14332 N  N     . PHE D 2 143 ? 150.952 83.360  131.897 1.00 44.03 ?  122 PHE D N     1 
ATOM   14333 C  CA    . PHE D 2 143 ? 149.675 83.055  132.531 1.00 44.42 ?  122 PHE D CA    1 
ATOM   14334 C  C     . PHE D 2 143 ? 149.713 81.774  133.357 1.00 45.38 ?  122 PHE D C     1 
ATOM   14335 O  O     . PHE D 2 143 ? 149.084 81.705  134.409 1.00 45.50 ?  122 PHE D O     1 
ATOM   14336 C  CB    . PHE D 2 143 ? 148.526 83.054  131.521 1.00 44.27 ?  122 PHE D CB    1 
ATOM   14337 C  CG    . PHE D 2 143 ? 147.932 84.414  131.309 1.00 43.28 ?  122 PHE D CG    1 
ATOM   14338 C  CD1   . PHE D 2 143 ? 146.989 84.920  132.202 1.00 42.17 ?  122 PHE D CD1   1 
ATOM   14339 C  CD2   . PHE D 2 143 ? 148.339 85.207  130.244 1.00 42.76 ?  122 PHE D CD2   1 
ATOM   14340 C  CE1   . PHE D 2 143 ? 146.446 86.187  132.027 1.00 42.16 ?  122 PHE D CE1   1 
ATOM   14341 C  CE2   . PHE D 2 143 ? 147.803 86.476  130.059 1.00 42.77 ?  122 PHE D CE2   1 
ATOM   14342 C  CZ    . PHE D 2 143 ? 146.853 86.969  130.953 1.00 42.28 ?  122 PHE D CZ    1 
ATOM   14343 N  N     . GLU D 2 144 ? 150.467 80.781  132.892 1.00 46.18 ?  123 GLU D N     1 
ATOM   14344 C  CA    . GLU D 2 144 ? 150.728 79.578  133.682 1.00 47.19 ?  123 GLU D CA    1 
ATOM   14345 C  C     . GLU D 2 144 ? 151.430 79.922  135.005 1.00 46.99 ?  123 GLU D C     1 
ATOM   14346 O  O     . GLU D 2 144 ? 151.039 79.411  136.059 1.00 46.94 ?  123 GLU D O     1 
ATOM   14347 C  CB    . GLU D 2 144 ? 151.558 78.574  132.871 1.00 47.80 ?  123 GLU D CB    1 
ATOM   14348 C  CG    . GLU D 2 144 ? 151.776 77.210  133.535 1.00 49.54 ?  123 GLU D CG    1 
ATOM   14349 C  CD    . GLU D 2 144 ? 152.707 76.296  132.732 1.00 52.37 ?  123 GLU D CD    1 
ATOM   14350 O  OE1   . GLU D 2 144 ? 153.775 76.763  132.272 1.00 52.92 ?  123 GLU D OE1   1 
ATOM   14351 O  OE2   . GLU D 2 144 ? 152.373 75.104  132.565 1.00 53.55 -1 123 GLU D OE2   1 
ATOM   14352 N  N     . TRP D 2 145 ? 152.451 80.784  134.938 1.00 47.02 ?  124 TRP D N     1 
ATOM   14353 C  CA    . TRP D 2 145 ? 153.222 81.217  136.118 1.00 46.93 ?  124 TRP D CA    1 
ATOM   14354 C  C     . TRP D 2 145 ? 152.355 81.999  137.094 1.00 46.55 ?  124 TRP D C     1 
ATOM   14355 O  O     . TRP D 2 145 ? 152.312 81.684  138.280 1.00 46.42 ?  124 TRP D O     1 
ATOM   14356 C  CB    . TRP D 2 145 ? 154.428 82.077  135.709 1.00 47.07 ?  124 TRP D CB    1 
ATOM   14357 C  CG    . TRP D 2 145 ? 155.407 82.406  136.840 1.00 47.82 ?  124 TRP D CG    1 
ATOM   14358 C  CD1   . TRP D 2 145 ? 156.535 81.706  137.178 1.00 48.78 ?  124 TRP D CD1   1 
ATOM   14359 C  CD2   . TRP D 2 145 ? 155.347 83.524  137.751 1.00 47.80 ?  124 TRP D CD2   1 
ATOM   14360 N  NE1   . TRP D 2 145 ? 157.174 82.308  138.239 1.00 49.06 ?  124 TRP D NE1   1 
ATOM   14361 C  CE2   . TRP D 2 145 ? 156.467 83.422  138.613 1.00 48.24 ?  124 TRP D CE2   1 
ATOM   14362 C  CE3   . TRP D 2 145 ? 154.457 84.592  137.927 1.00 47.65 ?  124 TRP D CE3   1 
ATOM   14363 C  CZ2   . TRP D 2 145 ? 156.718 84.350  139.637 1.00 47.74 ?  124 TRP D CZ2   1 
ATOM   14364 C  CZ3   . TRP D 2 145 ? 154.706 85.516  138.945 1.00 46.92 ?  124 TRP D CZ3   1 
ATOM   14365 C  CH2   . TRP D 2 145 ? 155.831 85.385  139.786 1.00 47.88 ?  124 TRP D CH2   1 
ATOM   14366 N  N     . VAL D 2 146 ? 151.669 83.020  136.589 1.00 46.09 ?  125 VAL D N     1 
ATOM   14367 C  CA    . VAL D 2 146 ? 150.859 83.889  137.436 1.00 45.36 ?  125 VAL D CA    1 
ATOM   14368 C  C     . VAL D 2 146 ? 149.661 83.116  138.011 1.00 45.28 ?  125 VAL D C     1 
ATOM   14369 O  O     . VAL D 2 146 ? 149.241 83.367  139.146 1.00 45.29 ?  125 VAL D O     1 
ATOM   14370 C  CB    . VAL D 2 146 ? 150.491 85.215  136.695 1.00 45.33 ?  125 VAL D CB    1 
ATOM   14371 C  CG1   . VAL D 2 146 ? 149.532 86.056  137.497 1.00 44.97 ?  125 VAL D CG1   1 
ATOM   14372 C  CG2   . VAL D 2 146 ? 151.758 86.029  136.422 1.00 44.52 ?  125 VAL D CG2   1 
ATOM   14373 N  N     . LYS D 2 147 ? 149.154 82.146  137.250 1.00 44.98 ?  126 LYS D N     1 
ATOM   14374 C  CA    . LYS D 2 147 ? 148.077 81.265  137.724 1.00 44.65 ?  126 LYS D CA    1 
ATOM   14375 C  C     . LYS D 2 147 ? 148.498 80.395  138.919 1.00 44.06 ?  126 LYS D C     1 
ATOM   14376 O  O     . LYS D 2 147 ? 147.667 80.035  139.755 1.00 44.65 ?  126 LYS D O     1 
ATOM   14377 C  CB    . LYS D 2 147 ? 147.561 80.367  136.596 1.00 45.31 ?  126 LYS D CB    1 
ATOM   14378 C  CG    . LYS D 2 147 ? 146.043 80.290  136.526 1.00 46.54 ?  126 LYS D CG    1 
ATOM   14379 C  CD    . LYS D 2 147 ? 145.533 78.871  136.269 1.00 49.06 ?  126 LYS D CD    1 
ATOM   14380 C  CE    . LYS D 2 147 ? 145.351 78.098  137.583 1.00 50.46 ?  126 LYS D CE    1 
ATOM   14381 N  NZ    . LYS D 2 147 ? 144.323 77.019  137.482 1.00 51.33 1  126 LYS D NZ    1 
ATOM   14382 N  N     . GLN D 2 148 ? 149.784 80.062  138.994 1.00 42.58 ?  127 GLN D N     1 
ATOM   14383 C  CA    . GLN D 2 148 ? 150.321 79.253  140.088 1.00 41.39 ?  127 GLN D CA    1 
ATOM   14384 C  C     . GLN D 2 148 ? 150.886 80.106  141.231 1.00 39.56 ?  127 GLN D C     1 
ATOM   14385 O  O     . GLN D 2 148 ? 151.108 79.599  142.330 1.00 39.77 ?  127 GLN D O     1 
ATOM   14386 C  CB    . GLN D 2 148 ? 151.371 78.268  139.537 1.00 42.11 ?  127 GLN D CB    1 
ATOM   14387 C  CG    . GLN D 2 148 ? 152.554 77.957  140.450 1.00 44.08 ?  127 GLN D CG    1 
ATOM   14388 C  CD    . GLN D 2 148 ? 153.804 78.779  140.129 1.00 46.12 ?  127 GLN D CD    1 
ATOM   14389 O  OE1   . GLN D 2 148 ? 153.731 79.984  139.855 1.00 46.47 ?  127 GLN D OE1   1 
ATOM   14390 N  NE2   . GLN D 2 148 ? 154.965 78.125  140.179 1.00 45.69 ?  127 GLN D NE2   1 
ATOM   14391 N  N     . ASN D 2 149 ? 151.102 81.397  140.967 1.00 36.99 ?  128 ASN D N     1 
ATOM   14392 C  CA    . ASN D 2 149 ? 151.696 82.311  141.942 1.00 34.54 ?  128 ASN D CA    1 
ATOM   14393 C  C     . ASN D 2 149 ? 150.902 82.442  143.245 1.00 33.13 ?  128 ASN D C     1 
ATOM   14394 O  O     . ASN D 2 149 ? 149.715 82.758  143.232 1.00 32.62 ?  128 ASN D O     1 
ATOM   14395 C  CB    . ASN D 2 149 ? 151.913 83.695  141.326 1.00 34.24 ?  128 ASN D CB    1 
ATOM   14396 C  CG    . ASN D 2 149 ? 152.635 84.636  142.269 1.00 33.83 ?  128 ASN D CG    1 
ATOM   14397 O  OD1   . ASN D 2 149 ? 152.014 85.477  142.921 1.00 32.21 ?  128 ASN D OD1   1 
ATOM   14398 N  ND2   . ASN D 2 149 ? 153.952 84.476  142.369 1.00 33.26 ?  128 ASN D ND2   1 
ATOM   14399 N  N     . LYS D 2 150 ? 151.587 82.228  144.365 1.00 31.49 ?  129 LYS D N     1 
ATOM   14400 C  CA    . LYS D 2 150 ? 150.965 82.187  145.686 1.00 30.68 ?  129 LYS D CA    1 
ATOM   14401 C  C     . LYS D 2 150 ? 150.260 83.500  146.104 1.00 28.95 ?  129 LYS D C     1 
ATOM   14402 O  O     . LYS D 2 150 ? 149.164 83.467  146.676 1.00 27.90 ?  129 LYS D O     1 
ATOM   14403 C  CB    . LYS D 2 150 ? 152.026 81.757  146.710 1.00 31.17 ?  129 LYS D CB    1 
ATOM   14404 C  CG    . LYS D 2 150 ? 151.714 81.980  148.175 1.00 33.66 ?  129 LYS D CG    1 
ATOM   14405 C  CD    . LYS D 2 150 ? 152.906 81.515  149.026 1.00 38.08 ?  129 LYS D CD    1 
ATOM   14406 C  CE    . LYS D 2 150 ? 152.970 82.238  150.377 1.00 40.20 ?  129 LYS D CE    1 
ATOM   14407 N  NZ    . LYS D 2 150 ? 152.250 81.502  151.452 1.00 42.60 1  129 LYS D NZ    1 
ATOM   14408 N  N     . TYR D 2 151 ? 150.886 84.642  145.822 1.00 27.36 ?  130 TYR D N     1 
ATOM   14409 C  CA    . TYR D 2 151 ? 150.354 85.939  146.280 1.00 26.56 ?  130 TYR D CA    1 
ATOM   14410 C  C     . TYR D 2 151 ? 149.195 86.423  145.423 1.00 25.66 ?  130 TYR D C     1 
ATOM   14411 O  O     . TYR D 2 151 ? 148.239 86.994  145.955 1.00 25.61 ?  130 TYR D O     1 
ATOM   14412 C  CB    . TYR D 2 151 ? 151.467 87.000  146.393 1.00 26.32 ?  130 TYR D CB    1 
ATOM   14413 C  CG    . TYR D 2 151 ? 152.701 86.453  147.085 1.00 27.20 ?  130 TYR D CG    1 
ATOM   14414 C  CD1   . TYR D 2 151 ? 152.679 86.164  148.449 1.00 27.31 ?  130 TYR D CD1   1 
ATOM   14415 C  CD2   . TYR D 2 151 ? 153.864 86.172  146.369 1.00 27.22 ?  130 TYR D CD2   1 
ATOM   14416 C  CE1   . TYR D 2 151 ? 153.795 85.629  149.091 1.00 29.65 ?  130 TYR D CE1   1 
ATOM   14417 C  CE2   . TYR D 2 151 ? 154.993 85.634  147.005 1.00 28.75 ?  130 TYR D CE2   1 
ATOM   14418 C  CZ    . TYR D 2 151 ? 154.940 85.376  148.377 1.00 29.17 ?  130 TYR D CZ    1 
ATOM   14419 O  OH    . TYR D 2 151 ? 156.024 84.850  149.044 1.00 30.61 ?  130 TYR D OH    1 
ATOM   14420 N  N     . LEU D 2 152 ? 149.281 86.192  144.111 1.00 24.87 ?  131 LEU D N     1 
ATOM   14421 C  CA    . LEU D 2 152 ? 148.164 86.486  143.220 1.00 24.37 ?  131 LEU D CA    1 
ATOM   14422 C  C     . LEU D 2 152 ? 146.958 85.607  143.572 1.00 24.18 ?  131 LEU D C     1 
ATOM   14423 O  O     . LEU D 2 152 ? 145.856 86.120  143.762 1.00 23.16 ?  131 LEU D O     1 
ATOM   14424 C  CB    . LEU D 2 152 ? 148.527 86.331  141.739 1.00 24.45 ?  131 LEU D CB    1 
ATOM   14425 C  CG    . LEU D 2 152 ? 147.263 86.723  140.953 1.00 26.33 ?  131 LEU D CG    1 
ATOM   14426 C  CD1   . LEU D 2 152 ? 147.054 88.244  140.972 1.00 25.00 ?  131 LEU D CD1   1 
ATOM   14427 C  CD2   . LEU D 2 152 ? 147.209 86.169  139.559 1.00 29.15 ?  131 LEU D CD2   1 
ATOM   14428 N  N     . GLN D 2 153 ? 147.180 84.296  143.690 1.00 24.07 ?  132 GLN D N     1 
ATOM   14429 C  CA    . GLN D 2 153 ? 146.098 83.372  144.092 1.00 24.99 ?  132 GLN D CA    1 
ATOM   14430 C  C     . GLN D 2 153 ? 145.469 83.713  145.440 1.00 24.24 ?  132 GLN D C     1 
ATOM   14431 O  O     . GLN D 2 153 ? 144.233 83.702  145.582 1.00 23.75 ?  132 GLN D O     1 
ATOM   14432 C  CB    . GLN D 2 153 ? 146.558 81.904  144.054 1.00 25.84 ?  132 GLN D CB    1 
ATOM   14433 C  CG    . GLN D 2 153 ? 146.772 81.357  142.618 1.00 28.48 ?  132 GLN D CG    1 
ATOM   14434 C  CD    . GLN D 2 153 ? 145.503 81.382  141.751 1.00 30.95 ?  132 GLN D CD    1 
ATOM   14435 O  OE1   . GLN D 2 153 ? 144.402 81.156  142.240 1.00 31.78 ?  132 GLN D OE1   1 
ATOM   14436 N  NE2   . GLN D 2 153 ? 145.668 81.644  140.453 1.00 32.81 ?  132 GLN D NE2   1 
ATOM   14437 N  N     . LYS D 2 154 ? 146.296 84.028  146.434 1.00 24.00 ?  133 LYS D N     1 
ATOM   14438 C  CA    . LYS D 2 154 ? 145.737 84.343  147.748 1.00 24.43 ?  133 LYS D CA    1 
ATOM   14439 C  C     . LYS D 2 154 ? 144.684 85.456  147.654 1.00 23.40 ?  133 LYS D C     1 
ATOM   14440 O  O     . LYS D 2 154 ? 143.552 85.285  148.113 1.00 22.68 ?  133 LYS D O     1 
ATOM   14441 C  CB    . LYS D 2 154 ? 146.809 84.727  148.775 1.00 24.64 ?  133 LYS D CB    1 
ATOM   14442 C  CG    . LYS D 2 154 ? 146.179 85.013  150.149 1.00 28.01 ?  133 LYS D CG    1 
ATOM   14443 C  CD    . LYS D 2 154 ? 147.180 85.228  151.260 1.00 32.56 ?  133 LYS D CD    1 
ATOM   14444 C  CE    . LYS D 2 154 ? 147.893 83.946  151.615 1.00 34.45 ?  133 LYS D CE    1 
ATOM   14445 N  NZ    . LYS D 2 154 ? 148.887 84.184  152.709 1.00 36.11 1  133 LYS D NZ    1 
ATOM   14446 N  N     . LYS D 2 155 ? 145.053 86.589  147.058 1.00 23.07 ?  134 LYS D N     1 
ATOM   14447 C  CA    . LYS D 2 155 ? 144.101 87.690  146.934 1.00 22.70 ?  134 LYS D CA    1 
ATOM   14448 C  C     . LYS D 2 155 ? 142.938 87.358  146.000 1.00 21.96 ?  134 LYS D C     1 
ATOM   14449 O  O     . LYS D 2 155 ? 141.796 87.662  146.329 1.00 22.25 ?  134 LYS D O     1 
ATOM   14450 C  CB    . LYS D 2 155 ? 144.782 89.022  146.570 1.00 22.70 ?  134 LYS D CB    1 
ATOM   14451 C  CG    . LYS D 2 155 ? 145.449 89.096  145.211 1.00 23.62 ?  134 LYS D CG    1 
ATOM   14452 C  CD    . LYS D 2 155 ? 145.996 90.505  144.998 1.00 25.32 ?  134 LYS D CD    1 
ATOM   14453 C  CE    . LYS D 2 155 ? 147.290 90.461  144.189 1.00 27.09 ?  134 LYS D CE    1 
ATOM   14454 N  NZ    . LYS D 2 155 ? 147.785 91.842  143.918 1.00 26.65 1  134 LYS D NZ    1 
ATOM   14455 N  N     . ALA D 2 156 ? 143.201 86.714  144.862 1.00 21.76 ?  135 ALA D N     1 
ATOM   14456 C  CA    . ALA D 2 156 ? 142.104 86.382  143.935 1.00 21.83 ?  135 ALA D CA    1 
ATOM   14457 C  C     . ALA D 2 156 ? 141.043 85.507  144.624 1.00 22.30 ?  135 ALA D C     1 
ATOM   14458 O  O     . ALA D 2 156 ? 139.843 85.783  144.529 1.00 21.92 ?  135 ALA D O     1 
ATOM   14459 C  CB    . ALA D 2 156 ? 142.633 85.695  142.663 1.00 22.30 ?  135 ALA D CB    1 
ATOM   14460 N  N     . GLN D 2 157 ? 141.489 84.472  145.338 1.00 22.15 ?  136 GLN D N     1 
ATOM   14461 C  CA    . GLN D 2 157 ? 140.552 83.557  145.999 1.00 22.38 ?  136 GLN D CA    1 
ATOM   14462 C  C     . GLN D 2 157 ? 139.855 84.162  147.225 1.00 21.59 ?  136 GLN D C     1 
ATOM   14463 O  O     . GLN D 2 157 ? 138.712 83.814  147.519 1.00 21.44 ?  136 GLN D O     1 
ATOM   14464 C  CB    . GLN D 2 157 ? 141.220 82.216  146.354 1.00 22.94 ?  136 GLN D CB    1 
ATOM   14465 C  CG    . GLN D 2 157 ? 141.820 81.454  145.161 1.00 25.31 ?  136 GLN D CG    1 
ATOM   14466 C  CD    . GLN D 2 157 ? 140.898 81.389  143.940 1.00 28.02 ?  136 GLN D CD    1 
ATOM   14467 O  OE1   . GLN D 2 157 ? 139.680 81.222  144.058 1.00 27.14 ?  136 GLN D OE1   1 
ATOM   14468 N  NE2   . GLN D 2 157 ? 141.491 81.512  142.754 1.00 29.47 ?  136 GLN D NE2   1 
ATOM   14469 N  N     . MET D 2 158 ? 140.533 85.052  147.941 1.00 21.52 ?  137 MET D N     1 
ATOM   14470 C  CA    . MET D 2 158 ? 139.894 85.769  149.058 1.00 22.20 ?  137 MET D CA    1 
ATOM   14471 C  C     . MET D 2 158 ? 138.686 86.590  148.593 1.00 21.84 ?  137 MET D C     1 
ATOM   14472 O  O     . MET D 2 158 ? 137.628 86.567  149.226 1.00 21.91 ?  137 MET D O     1 
ATOM   14473 C  CB    . MET D 2 158 ? 140.889 86.679  149.779 1.00 22.52 ?  137 MET D CB    1 
ATOM   14474 C  CG    . MET D 2 158 ? 141.844 85.931  150.721 1.00 25.81 ?  137 MET D CG    1 
ATOM   14475 S  SD    . MET D 2 158 ? 143.026 87.019  151.564 1.00 31.19 ?  137 MET D SD    1 
ATOM   14476 C  CE    . MET D 2 158 ? 141.872 87.988  152.499 1.00 23.91 ?  137 MET D CE    1 
ATOM   14477 N  N     . ILE D 2 159 ? 138.860 87.306  147.484 1.00 21.41 ?  138 ILE D N     1 
ATOM   14478 C  CA    . ILE D 2 159 ? 137.807 88.146  146.920 1.00 21.51 ?  138 ILE D CA    1 
ATOM   14479 C  C     . ILE D 2 159 ? 136.645 87.278  146.409 1.00 21.77 ?  138 ILE D C     1 
ATOM   14480 O  O     . ILE D 2 159 ? 135.477 87.534  146.742 1.00 21.44 ?  138 ILE D O     1 
ATOM   14481 C  CB    . ILE D 2 159 ? 138.392 89.094  145.803 1.00 21.49 ?  138 ILE D CB    1 
ATOM   14482 C  CG1   . ILE D 2 159 ? 139.440 90.056  146.382 1.00 21.16 ?  138 ILE D CG1   1 
ATOM   14483 C  CG2   . ILE D 2 159 ? 137.290 89.866  145.067 1.00 22.34 ?  138 ILE D CG2   1 
ATOM   14484 C  CD1   . ILE D 2 159 ? 138.911 91.033  147.453 1.00 23.85 ?  138 ILE D CD1   1 
ATOM   14485 N  N     . VAL D 2 160 ? 136.982 86.253  145.618 1.00 21.96 ?  139 VAL D N     1 
ATOM   14486 C  CA    . VAL D 2 160 ? 136.007 85.329  145.021 1.00 22.59 ?  139 VAL D CA    1 
ATOM   14487 C  C     . VAL D 2 160 ? 135.217 84.590  146.111 1.00 22.36 ?  139 VAL D C     1 
ATOM   14488 O  O     . VAL D 2 160 ? 134.012 84.361  145.962 1.00 21.64 ?  139 VAL D O     1 
ATOM   14489 C  CB    . VAL D 2 160 ? 136.701 84.322  144.043 1.00 23.08 ?  139 VAL D CB    1 
ATOM   14490 C  CG1   . VAL D 2 160 ? 135.802 83.119  143.702 1.00 24.33 ?  139 VAL D CG1   1 
ATOM   14491 C  CG2   . VAL D 2 160 ? 137.140 85.036  142.754 1.00 22.87 ?  139 VAL D CG2   1 
ATOM   14492 N  N     . GLY D 2 161 ? 135.902 84.230  147.200 1.00 22.21 ?  140 GLY D N     1 
ATOM   14493 C  CA    . GLY D 2 161 ? 135.256 83.588  148.343 1.00 22.50 ?  140 GLY D CA    1 
ATOM   14494 C  C     . GLY D 2 161 ? 134.111 84.421  148.909 1.00 22.88 ?  140 GLY D C     1 
ATOM   14495 O  O     . GLY D 2 161 ? 133.034 83.888  149.210 1.00 23.54 ?  140 GLY D O     1 
ATOM   14496 N  N     . LEU D 2 162 ? 134.330 85.729  149.043 1.00 22.25 ?  141 LEU D N     1 
ATOM   14497 C  CA    . LEU D 2 162 ? 133.282 86.625  149.542 1.00 22.48 ?  141 LEU D CA    1 
ATOM   14498 C  C     . LEU D 2 162 ? 132.116 86.793  148.564 1.00 22.27 ?  141 LEU D C     1 
ATOM   14499 O  O     . LEU D 2 162 ? 130.969 86.909  148.997 1.00 22.31 ?  141 LEU D O     1 
ATOM   14500 C  CB    . LEU D 2 162 ? 133.855 87.982  149.998 1.00 22.07 ?  141 LEU D CB    1 
ATOM   14501 C  CG    . LEU D 2 162 ? 134.612 87.923  151.343 1.00 22.81 ?  141 LEU D CG    1 
ATOM   14502 C  CD1   . LEU D 2 162 ? 135.575 89.096  151.514 1.00 21.65 ?  141 LEU D CD1   1 
ATOM   14503 C  CD2   . LEU D 2 162 ? 133.676 87.779  152.548 1.00 23.35 ?  141 LEU D CD2   1 
ATOM   14504 N  N     . TYR D 2 163 ? 132.399 86.808  147.259 1.00 22.63 ?  142 TYR D N     1 
ATOM   14505 C  CA    . TYR D 2 163 ? 131.325 86.826  146.246 1.00 23.30 ?  142 TYR D CA    1 
ATOM   14506 C  C     . TYR D 2 163 ? 130.483 85.557  146.288 1.00 23.40 ?  142 TYR D C     1 
ATOM   14507 O  O     . TYR D 2 163 ? 129.271 85.615  146.144 1.00 23.75 ?  142 TYR D O     1 
ATOM   14508 C  CB    . TYR D 2 163 ? 131.875 86.950  144.832 1.00 23.22 ?  142 TYR D CB    1 
ATOM   14509 C  CG    . TYR D 2 163 ? 132.653 88.201  144.531 1.00 24.01 ?  142 TYR D CG    1 
ATOM   14510 C  CD1   . TYR D 2 163 ? 132.477 89.358  145.279 1.00 24.47 ?  142 TYR D CD1   1 
ATOM   14511 C  CD2   . TYR D 2 163 ? 133.565 88.223  143.480 1.00 24.62 ?  142 TYR D CD2   1 
ATOM   14512 C  CE1   . TYR D 2 163 ? 133.191 90.504  144.997 1.00 26.33 ?  142 TYR D CE1   1 
ATOM   14513 C  CE2   . TYR D 2 163 ? 134.279 89.371  143.178 1.00 26.07 ?  142 TYR D CE2   1 
ATOM   14514 C  CZ    . TYR D 2 163 ? 134.079 90.511  143.946 1.00 26.65 ?  142 TYR D CZ    1 
ATOM   14515 O  OH    . TYR D 2 163 ? 134.786 91.659  143.673 1.00 31.13 ?  142 TYR D OH    1 
ATOM   14516 N  N     . LYS D 2 164 ? 131.130 84.414  146.475 1.00 23.70 ?  143 LYS D N     1 
ATOM   14517 C  CA    . LYS D 2 164 ? 130.417 83.129  146.554 1.00 24.47 ?  143 LYS D CA    1 
ATOM   14518 C  C     . LYS D 2 164 ? 129.578 82.968  147.832 1.00 24.55 ?  143 LYS D C     1 
ATOM   14519 O  O     . LYS D 2 164 ? 128.689 82.116  147.893 1.00 24.49 ?  143 LYS D O     1 
ATOM   14520 C  CB    . LYS D 2 164 ? 131.412 81.973  146.431 1.00 24.98 ?  143 LYS D CB    1 
ATOM   14521 C  CG    . LYS D 2 164 ? 131.941 81.730  145.009 1.00 27.10 ?  143 LYS D CG    1 
ATOM   14522 C  CD    . LYS D 2 164 ? 132.820 80.488  144.992 1.00 30.75 ?  143 LYS D CD    1 
ATOM   14523 C  CE    . LYS D 2 164 ? 133.300 80.122  143.589 1.00 32.81 ?  143 LYS D CE    1 
ATOM   14524 N  NZ    . LYS D 2 164 ? 134.260 78.947  143.606 1.00 33.68 1  143 LYS D NZ    1 
ATOM   14525 N  N     . ALA D 2 165 ? 129.870 83.773  148.849 1.00 24.18 ?  144 ALA D N     1 
ATOM   14526 C  CA    . ALA D 2 165 ? 129.188 83.667  150.142 1.00 25.04 ?  144 ALA D CA    1 
ATOM   14527 C  C     . ALA D 2 165 ? 127.941 84.553  150.281 1.00 25.00 ?  144 ALA D C     1 
ATOM   14528 O  O     . ALA D 2 165 ? 127.270 84.515  151.323 1.00 25.50 ?  144 ALA D O     1 
ATOM   14529 C  CB    . ALA D 2 165 ? 130.170 83.941  151.294 1.00 25.02 ?  144 ALA D CB    1 
ATOM   14530 N  N     . ILE D 2 166 ? 127.630 85.347  149.254 1.00 24.60 ?  145 ILE D N     1 
ATOM   14531 C  CA    . ILE D 2 166 ? 126.417 86.166  149.273 1.00 24.40 ?  145 ILE D CA    1 
ATOM   14532 C  C     . ILE D 2 166 ? 125.188 85.247  149.319 1.00 25.75 ?  145 ILE D C     1 
ATOM   14533 O  O     . ILE D 2 166 ? 125.097 84.274  148.563 1.00 25.84 ?  145 ILE D O     1 
ATOM   14534 C  CB    . ILE D 2 166 ? 126.294 87.110  148.043 1.00 24.15 ?  145 ILE D CB    1 
ATOM   14535 C  CG1   . ILE D 2 166 ? 127.574 87.921  147.841 1.00 23.15 ?  145 ILE D CG1   1 
ATOM   14536 C  CG2   . ILE D 2 166 ? 125.095 88.043  148.206 1.00 22.72 ?  145 ILE D CG2   1 
ATOM   14537 C  CD1   . ILE D 2 166 ? 127.613 88.686  146.534 1.00 21.70 ?  145 ILE D CD1   1 
ATOM   14538 N  N     . GLN D 2 167 ? 124.270 85.545  150.230 1.00 26.52 ?  146 GLN D N     1 
ATOM   14539 C  CA    . GLN D 2 167 ? 123.029 84.791  150.339 1.00 28.77 ?  146 GLN D CA    1 
ATOM   14540 C  C     . GLN D 2 167 ? 121.840 85.656  149.944 1.00 29.20 ?  146 GLN D C     1 
ATOM   14541 O  O     . GLN D 2 167 ? 121.793 86.852  150.268 1.00 28.89 ?  146 GLN D O     1 
ATOM   14542 C  CB    . GLN D 2 167 ? 122.849 84.269  151.762 1.00 29.04 ?  146 GLN D CB    1 
ATOM   14543 C  CG    . GLN D 2 167 ? 123.901 83.254  152.166 1.00 31.87 ?  146 GLN D CG    1 
ATOM   14544 C  CD    . GLN D 2 167 ? 124.419 83.501  153.558 1.00 35.35 ?  146 GLN D CD    1 
ATOM   14545 O  OE1   . GLN D 2 167 ? 123.697 83.324  154.542 1.00 36.91 ?  146 GLN D OE1   1 
ATOM   14546 N  NE2   . GLN D 2 167 ? 125.682 83.913  153.653 1.00 36.19 ?  146 GLN D NE2   1 
ATOM   14547 N  N     . LYS D 2 168 ? 120.882 85.049  149.247 1.00 30.29 ?  147 LYS D N     1 
ATOM   14548 C  CA    . LYS D 2 168 ? 119.657 85.745  148.859 1.00 31.24 ?  147 LYS D CA    1 
ATOM   14549 C  C     . LYS D 2 168 ? 119.004 86.431  150.059 1.00 31.73 ?  147 LYS D C     1 
ATOM   14550 O  O     . LYS D 2 168 ? 118.919 85.843  151.137 1.00 31.46 ?  147 LYS D O     1 
ATOM   14551 C  CB    . LYS D 2 168 ? 118.679 84.781  148.194 1.00 31.92 ?  147 LYS D CB    1 
ATOM   14552 C  CG    . LYS D 2 168 ? 117.413 85.455  147.685 1.00 33.23 ?  147 LYS D CG    1 
ATOM   14553 C  CD    . LYS D 2 168 ? 116.583 84.516  146.825 1.00 36.06 ?  147 LYS D CD    1 
ATOM   14554 C  CE    . LYS D 2 168 ? 115.292 85.173  146.384 1.00 35.46 ?  147 LYS D CE    1 
ATOM   14555 N  NZ    . LYS D 2 168 ? 115.520 86.243  145.378 1.00 38.24 1  147 LYS D NZ    1 
ATOM   14556 N  N     . ASP D 2 169 ? 118.571 87.679  149.864 1.00 32.28 ?  148 ASP D N     1 
ATOM   14557 C  CA    . ASP D 2 169 ? 117.915 88.483  150.909 1.00 33.45 ?  148 ASP D CA    1 
ATOM   14558 C  C     . ASP D 2 169 ? 118.714 88.674  152.198 1.00 33.30 ?  148 ASP D C     1 
ATOM   14559 O  O     . ASP D 2 169 ? 118.136 88.913  153.260 1.00 34.32 ?  148 ASP D O     1 
ATOM   14560 C  CB    . ASP D 2 169 ? 116.539 87.898  151.272 1.00 34.63 ?  148 ASP D CB    1 
ATOM   14561 C  CG    . ASP D 2 169 ? 115.496 88.125  150.199 1.00 36.09 ?  148 ASP D CG    1 
ATOM   14562 O  OD1   . ASP D 2 169 ? 115.719 88.932  149.272 1.00 37.80 ?  148 ASP D OD1   1 
ATOM   14563 O  OD2   . ASP D 2 169 ? 114.431 87.482  150.301 1.00 40.47 -1 148 ASP D OD2   1 
ATOM   14564 N  N     . ASP D 2 170 ? 120.031 88.549  152.127 1.00 32.58 ?  149 ASP D N     1 
ATOM   14565 C  CA    . ASP D 2 170 ? 120.862 88.839  153.293 1.00 32.01 ?  149 ASP D CA    1 
ATOM   14566 C  C     . ASP D 2 170 ? 121.802 89.990  152.953 1.00 30.59 ?  149 ASP D C     1 
ATOM   14567 O  O     . ASP D 2 170 ? 122.795 89.811  152.247 1.00 29.11 ?  149 ASP D O     1 
ATOM   14568 C  CB    . ASP D 2 170 ? 121.624 87.595  153.757 1.00 32.93 ?  149 ASP D CB    1 
ATOM   14569 C  CG    . ASP D 2 170 ? 122.683 87.903  154.807 1.00 35.05 ?  149 ASP D CG    1 
ATOM   14570 O  OD1   . ASP D 2 170 ? 122.538 88.868  155.589 1.00 39.25 ?  149 ASP D OD1   1 
ATOM   14571 O  OD2   . ASP D 2 170 ? 123.670 87.158  154.864 1.00 39.22 -1 149 ASP D OD2   1 
ATOM   14572 N  N     . GLU D 2 171 ? 121.458 91.171  153.460 1.00 29.34 ?  150 GLU D N     1 
ATOM   14573 C  CA    . GLU D 2 171 ? 122.192 92.394  153.150 1.00 28.51 ?  150 GLU D CA    1 
ATOM   14574 C  C     . GLU D 2 171 ? 123.576 92.461  153.810 1.00 27.27 ?  150 GLU D C     1 
ATOM   14575 O  O     . GLU D 2 171 ? 124.445 93.174  153.334 1.00 26.62 ?  150 GLU D O     1 
ATOM   14576 C  CB    . GLU D 2 171 ? 121.349 93.631  153.492 1.00 29.09 ?  150 GLU D CB    1 
ATOM   14577 C  CG    . GLU D 2 171 ? 121.121 93.878  154.982 1.00 30.68 ?  150 GLU D CG    1 
ATOM   14578 C  CD    . GLU D 2 171 ? 120.134 95.006  155.239 1.00 33.92 ?  150 GLU D CD    1 
ATOM   14579 O  OE1   . GLU D 2 171 ? 119.661 95.625  154.255 1.00 36.31 ?  150 GLU D OE1   1 
ATOM   14580 O  OE2   . GLU D 2 171 ? 119.830 95.288  156.419 1.00 34.02 -1 150 GLU D OE2   1 
ATOM   14581 N  N     . ILE D 2 172 ? 123.782 91.701  154.885 1.00 26.19 ?  151 ILE D N     1 
ATOM   14582 C  CA    . ILE D 2 172 ? 125.089 91.648  155.541 1.00 25.49 ?  151 ILE D CA    1 
ATOM   14583 C  C     . ILE D 2 172 ? 126.120 90.970  154.633 1.00 24.61 ?  151 ILE D C     1 
ATOM   14584 O  O     . ILE D 2 172 ? 127.222 91.495  154.432 1.00 24.09 ?  151 ILE D O     1 
ATOM   14585 C  CB    . ILE D 2 172 ? 125.017 90.960  156.934 1.00 25.98 ?  151 ILE D CB    1 
ATOM   14586 C  CG1   . ILE D 2 172 ? 124.133 91.762  157.891 1.00 26.86 ?  151 ILE D CG1   1 
ATOM   14587 C  CG2   . ILE D 2 172 ? 126.423 90.733  157.552 1.00 26.50 ?  151 ILE D CG2   1 
ATOM   14588 C  CD1   . ILE D 2 172 ? 124.619 93.180  158.157 1.00 27.81 ?  151 ILE D CD1   1 
ATOM   14589 N  N     . SER D 2 173 ? 125.746 89.824  154.072 1.00 23.71 ?  152 SER D N     1 
ATOM   14590 C  CA    . SER D 2 173 ? 126.622 89.096  153.156 1.00 23.38 ?  152 SER D CA    1 
ATOM   14591 C  C     . SER D 2 173 ? 126.850 89.892  151.859 1.00 22.41 ?  152 SER D C     1 
ATOM   14592 O  O     . SER D 2 173 ? 127.934 89.848  151.270 1.00 21.43 ?  152 SER D O     1 
ATOM   14593 C  CB    . SER D 2 173 ? 126.075 87.692  152.868 1.00 23.90 ?  152 SER D CB    1 
ATOM   14594 O  OG    . SER D 2 173 ? 124.896 87.700  152.064 1.00 23.74 ?  152 SER D OG    1 
ATOM   14595 N  N     . LEU D 2 174 ? 125.833 90.633  151.431 1.00 21.63 ?  153 LEU D N     1 
ATOM   14596 C  CA    . LEU D 2 174 ? 125.979 91.498  150.258 1.00 20.75 ?  153 LEU D CA    1 
ATOM   14597 C  C     . LEU D 2 174 ? 126.986 92.608  150.552 1.00 20.96 ?  153 LEU D C     1 
ATOM   14598 O  O     . LEU D 2 174 ? 127.855 92.896  149.730 1.00 20.41 ?  153 LEU D O     1 
ATOM   14599 C  CB    . LEU D 2 174 ? 124.623 92.092  149.825 1.00 20.62 ?  153 LEU D CB    1 
ATOM   14600 C  CG    . LEU D 2 174 ? 124.644 93.056  148.620 1.00 19.55 ?  153 LEU D CG    1 
ATOM   14601 C  CD1   . LEU D 2 174 ? 125.335 92.411  147.413 1.00 20.44 ?  153 LEU D CD1   1 
ATOM   14602 C  CD2   . LEU D 2 174 ? 123.214 93.495  148.272 1.00 20.99 ?  153 LEU D CD2   1 
ATOM   14603 N  N     . PHE D 2 175 ? 126.870 93.224  151.728 1.00 21.07 ?  154 PHE D N     1 
ATOM   14604 C  CA    . PHE D 2 175 ? 127.788 94.288  152.129 1.00 21.32 ?  154 PHE D CA    1 
ATOM   14605 C  C     . PHE D 2 175 ? 129.242 93.802  152.135 1.00 21.08 ?  154 PHE D C     1 
ATOM   14606 O  O     . PHE D 2 175 ? 130.137 94.485  151.633 1.00 20.85 ?  154 PHE D O     1 
ATOM   14607 C  CB    . PHE D 2 175 ? 127.408 94.833  153.510 1.00 21.20 ?  154 PHE D CB    1 
ATOM   14608 C  CG    . PHE D 2 175 ? 128.447 95.732  154.114 1.00 22.46 ?  154 PHE D CG    1 
ATOM   14609 C  CD1   . PHE D 2 175 ? 128.403 97.108  153.894 1.00 21.21 ?  154 PHE D CD1   1 
ATOM   14610 C  CD2   . PHE D 2 175 ? 129.468 95.211  154.912 1.00 22.53 ?  154 PHE D CD2   1 
ATOM   14611 C  CE1   . PHE D 2 175 ? 129.347 97.945  154.453 1.00 22.11 ?  154 PHE D CE1   1 
ATOM   14612 C  CE2   . PHE D 2 175 ? 130.435 96.045  155.466 1.00 23.26 ?  154 PHE D CE2   1 
ATOM   14613 C  CZ    . PHE D 2 175 ? 130.373 97.417  155.243 1.00 22.08 ?  154 PHE D CZ    1 
ATOM   14614 N  N     . LYS D 2 176 ? 129.469 92.628  152.715 1.00 21.14 ?  155 LYS D N     1 
ATOM   14615 C  CA    . LYS D 2 176 ? 130.811 92.039  152.768 1.00 20.93 ?  155 LYS D CA    1 
ATOM   14616 C  C     . LYS D 2 176 ? 131.409 91.840  151.377 1.00 20.61 ?  155 LYS D C     1 
ATOM   14617 O  O     . LYS D 2 176 ? 132.590 92.126  151.149 1.00 20.62 ?  155 LYS D O     1 
ATOM   14618 C  CB    . LYS D 2 176 ? 130.768 90.724  153.529 1.00 21.27 ?  155 LYS D CB    1 
ATOM   14619 C  CG    . LYS D 2 176 ? 130.592 90.935  155.008 1.00 22.04 ?  155 LYS D CG    1 
ATOM   14620 C  CD    . LYS D 2 176 ? 130.443 89.631  155.774 1.00 25.24 ?  155 LYS D CD    1 
ATOM   14621 C  CE    . LYS D 2 176 ? 130.336 89.933  157.246 1.00 25.83 ?  155 LYS D CE    1 
ATOM   14622 N  NZ    . LYS D 2 176 ? 130.204 88.705  158.084 1.00 26.64 1  155 LYS D NZ    1 
ATOM   14623 N  N     . ALA D 2 177 ? 130.581 91.375  150.448 1.00 20.02 ?  156 ALA D N     1 
ATOM   14624 C  CA    . ALA D 2 177 ? 130.994 91.237  149.053 1.00 19.86 ?  156 ALA D CA    1 
ATOM   14625 C  C     . ALA D 2 177 ? 131.283 92.596  148.399 1.00 19.61 ?  156 ALA D C     1 
ATOM   14626 O  O     . ALA D 2 177 ? 132.181 92.717  147.563 1.00 19.69 ?  156 ALA D O     1 
ATOM   14627 C  CB    . ALA D 2 177 ? 129.936 90.507  148.293 1.00 19.99 ?  156 ALA D CB    1 
ATOM   14628 N  N     . MET D 2 178 ? 130.511 93.615  148.771 1.00 19.75 ?  157 MET D N     1 
ATOM   14629 C  CA    . MET D 2 178 ? 130.709 94.968  148.210 1.00 18.89 ?  157 MET D CA    1 
ATOM   14630 C  C     . MET D 2 178 ? 132.028 95.550  148.693 1.00 18.62 ?  157 MET D C     1 
ATOM   14631 O  O     . MET D 2 178 ? 132.746 96.201  147.925 1.00 18.10 ?  157 MET D O     1 
ATOM   14632 C  CB    . MET D 2 178 ? 129.553 95.890  148.589 1.00 18.82 ?  157 MET D CB    1 
ATOM   14633 C  CG    . MET D 2 178 ? 128.280 95.608  147.808 1.00 20.20 ?  157 MET D CG    1 
ATOM   14634 S  SD    . MET D 2 178 ? 126.936 96.633  148.423 1.00 23.78 ?  157 MET D SD    1 
ATOM   14635 C  CE    . MET D 2 178 ? 125.688 96.282  147.188 1.00 22.62 ?  157 MET D CE    1 
ATOM   14636 N  N     . VAL D 2 179 ? 132.348 95.286  149.961 1.00 18.34 ?  158 VAL D N     1 
ATOM   14637 C  CA    . VAL D 2 179 ? 133.629 95.674  150.532 1.00 18.75 ?  158 VAL D CA    1 
ATOM   14638 C  C     . VAL D 2 179 ? 134.771 95.024  149.759 1.00 18.86 ?  158 VAL D C     1 
ATOM   14639 O  O     . VAL D 2 179 ? 135.746 95.707  149.402 1.00 18.79 ?  158 VAL D O     1 
ATOM   14640 C  CB    . VAL D 2 179 ? 133.745 95.321  152.038 1.00 19.02 ?  158 VAL D CB    1 
ATOM   14641 C  CG1   . VAL D 2 179 ? 135.185 95.543  152.525 1.00 19.10 ?  158 VAL D CG1   1 
ATOM   14642 C  CG2   . VAL D 2 179 ? 132.751 96.146  152.869 1.00 18.94 ?  158 VAL D CG2   1 
ATOM   14643 N  N     . ALA D 2 180 ? 134.648 93.713  149.518 1.00 18.96 ?  159 ALA D N     1 
ATOM   14644 C  CA    . ALA D 2 180 ? 135.614 92.979  148.698 1.00 19.05 ?  159 ALA D CA    1 
ATOM   14645 C  C     . ALA D 2 180 ? 135.745 93.605  147.307 1.00 18.67 ?  159 ALA D C     1 
ATOM   14646 O  O     . ALA D 2 180 ? 136.862 93.812  146.816 1.00 17.72 ?  159 ALA D O     1 
ATOM   14647 C  CB    . ALA D 2 180 ? 135.226 91.493  148.591 1.00 19.43 ?  159 ALA D CB    1 
ATOM   14648 N  N     . SER D 2 181 ? 134.602 93.934  146.696 1.00 18.49 ?  160 SER D N     1 
ATOM   14649 C  CA    . SER D 2 181 ? 134.601 94.553  145.370 1.00 18.51 ?  160 SER D CA    1 
ATOM   14650 C  C     . SER D 2 181 ? 135.296 95.915  145.359 1.00 18.23 ?  160 SER D C     1 
ATOM   14651 O  O     . SER D 2 181 ? 136.116 96.187  144.492 1.00 18.18 ?  160 SER D O     1 
ATOM   14652 C  CB    . SER D 2 181 ? 133.177 94.696  144.825 1.00 18.51 ?  160 SER D CB    1 
ATOM   14653 O  OG    . SER D 2 181 ? 133.233 95.137  143.482 1.00 19.42 ?  160 SER D OG    1 
ATOM   14654 N  N     . VAL D 2 182 ? 134.970 96.763  146.332 1.00 18.43 ?  161 VAL D N     1 
ATOM   14655 C  CA    . VAL D 2 182 ? 135.640 98.062  146.456 1.00 18.09 ?  161 VAL D CA    1 
ATOM   14656 C  C     . VAL D 2 182 ? 137.147 97.890  146.670 1.00 18.41 ?  161 VAL D C     1 
ATOM   14657 O  O     . VAL D 2 182 ? 137.948 98.603  146.062 1.00 18.52 ?  161 VAL D O     1 
ATOM   14658 C  CB    . VAL D 2 182 ? 135.014 98.928  147.557 1.00 17.71 ?  161 VAL D CB    1 
ATOM   14659 C  CG1   . VAL D 2 182 ? 135.865 100.195 147.813 1.00 16.02 ?  161 VAL D CG1   1 
ATOM   14660 C  CG2   . VAL D 2 182 ? 133.586 99.317  147.150 1.00 17.78 ?  161 VAL D CG2   1 
ATOM   14661 N  N     . TYR D 2 183 ? 137.531 96.917  147.498 1.00 19.06 ?  162 TYR D N     1 
ATOM   14662 C  CA    . TYR D 2 183 ? 138.951 96.658  147.713 1.00 19.73 ?  162 TYR D CA    1 
ATOM   14663 C  C     . TYR D 2 183 ? 139.644 96.237  146.424 1.00 19.90 ?  162 TYR D C     1 
ATOM   14664 O  O     . TYR D 2 183 ? 140.785 96.608  146.202 1.00 20.73 ?  162 TYR D O     1 
ATOM   14665 C  CB    . TYR D 2 183 ? 139.209 95.638  148.837 1.00 19.84 ?  162 TYR D CB    1 
ATOM   14666 C  CG    . TYR D 2 183 ? 138.960 96.169  150.233 1.00 20.24 ?  162 TYR D CG    1 
ATOM   14667 C  CD1   . TYR D 2 183 ? 138.790 97.532  150.467 1.00 21.51 ?  162 TYR D CD1   1 
ATOM   14668 C  CD2   . TYR D 2 183 ? 138.915 95.304  151.334 1.00 20.45 ?  162 TYR D CD2   1 
ATOM   14669 C  CE1   . TYR D 2 183 ? 138.567 98.022  151.760 1.00 21.68 ?  162 TYR D CE1   1 
ATOM   14670 C  CE2   . TYR D 2 183 ? 138.714 95.787  152.633 1.00 19.97 ?  162 TYR D CE2   1 
ATOM   14671 C  CZ    . TYR D 2 183 ? 138.536 97.146  152.834 1.00 21.83 ?  162 TYR D CZ    1 
ATOM   14672 O  OH    . TYR D 2 183 ? 138.326 97.635  154.109 1.00 21.96 ?  162 TYR D OH    1 
ATOM   14673 N  N     . LEU D 2 184 ? 138.962 95.488  145.569 1.00 20.22 ?  163 LEU D N     1 
ATOM   14674 C  CA    . LEU D 2 184 ? 139.564 95.104  144.296 1.00 20.89 ?  163 LEU D CA    1 
ATOM   14675 C  C     . LEU D 2 184 ? 139.681 96.326  143.373 1.00 20.72 ?  163 LEU D C     1 
ATOM   14676 O  O     . LEU D 2 184 ? 140.770 96.644  142.904 1.00 21.07 ?  163 LEU D O     1 
ATOM   14677 C  CB    . LEU D 2 184 ? 138.807 93.931  143.641 1.00 21.16 ?  163 LEU D CB    1 
ATOM   14678 C  CG    . LEU D 2 184 ? 139.270 93.412  142.264 1.00 22.77 ?  163 LEU D CG    1 
ATOM   14679 C  CD1   . LEU D 2 184 ? 140.780 93.086  142.222 1.00 22.44 ?  163 LEU D CD1   1 
ATOM   14680 C  CD2   . LEU D 2 184 ? 138.461 92.199  141.830 1.00 24.75 ?  163 LEU D CD2   1 
ATOM   14681 N  N     . GLU D 2 185 ? 138.567 97.022  143.159 1.00 20.65 ?  164 GLU D N     1 
ATOM   14682 C  CA    . GLU D 2 185 ? 138.509 98.181  142.255 1.00 20.69 ?  164 GLU D CA    1 
ATOM   14683 C  C     . GLU D 2 185 ? 139.423 99.341  142.651 1.00 20.64 ?  164 GLU D C     1 
ATOM   14684 O  O     . GLU D 2 185 ? 140.034 99.986  141.787 1.00 20.25 ?  164 GLU D O     1 
ATOM   14685 C  CB    . GLU D 2 185 ? 137.072 98.715  142.164 1.00 21.03 ?  164 GLU D CB    1 
ATOM   14686 C  CG    . GLU D 2 185 ? 136.035 97.701  141.670 1.00 22.19 ?  164 GLU D CG    1 
ATOM   14687 C  CD    . GLU D 2 185 ? 135.965 97.578  140.150 1.00 24.19 ?  164 GLU D CD    1 
ATOM   14688 O  OE1   . GLU D 2 185 ? 136.770 98.192  139.428 1.00 27.97 ?  164 GLU D OE1   1 
ATOM   14689 O  OE2   . GLU D 2 185 ? 135.078 96.877  139.662 1.00 25.47 -1 164 GLU D OE2   1 
ATOM   14690 N  N     . SER D 2 186 ? 139.488 99.621  143.949 1.00 20.42 ?  165 SER D N     1 
ATOM   14691 C  CA    . SER D 2 186 ? 140.118 100.846 144.440 1.00 20.70 ?  165 SER D CA    1 
ATOM   14692 C  C     . SER D 2 186 ? 141.450 100.623 145.155 1.00 20.88 ?  165 SER D C     1 
ATOM   14693 O  O     . SER D 2 186 ? 142.070 101.580 145.617 1.00 21.21 ?  165 SER D O     1 
ATOM   14694 C  CB    . SER D 2 186 ? 139.159 101.610 145.372 1.00 21.25 ?  165 SER D CB    1 
ATOM   14695 O  OG    . SER D 2 186 ? 137.891 101.822 144.767 1.00 20.97 ?  165 SER D OG    1 
ATOM   14696 N  N     . PHE D 2 187 ? 141.904 99.372  145.246 1.00 20.94 ?  166 PHE D N     1 
ATOM   14697 C  CA    . PHE D 2 187 ? 143.071 99.083  146.067 1.00 21.19 ?  166 PHE D CA    1 
ATOM   14698 C  C     . PHE D 2 187 ? 143.953 97.990  145.463 1.00 21.22 ?  166 PHE D C     1 
ATOM   14699 O  O     . PHE D 2 187 ? 145.104 98.272  145.111 1.00 21.10 ?  166 PHE D O     1 
ATOM   14700 C  CB    . PHE D 2 187 ? 142.634 98.823  147.536 1.00 21.63 ?  166 PHE D CB    1 
ATOM   14701 C  CG    . PHE D 2 187 ? 143.627 98.062  148.375 1.00 24.05 ?  166 PHE D CG    1 
ATOM   14702 C  CD1   . PHE D 2 187 ? 144.920 98.544  148.582 1.00 25.52 ?  166 PHE D CD1   1 
ATOM   14703 C  CD2   . PHE D 2 187 ? 143.249 96.878  149.003 1.00 27.03 ?  166 PHE D CD2   1 
ATOM   14704 C  CE1   . PHE D 2 187 ? 145.818 97.845  149.378 1.00 26.73 ?  166 PHE D CE1   1 
ATOM   14705 C  CE2   . PHE D 2 187 ? 144.159 96.165  149.799 1.00 27.36 ?  166 PHE D CE2   1 
ATOM   14706 C  CZ    . PHE D 2 187 ? 145.438 96.652  149.979 1.00 27.87 ?  166 PHE D CZ    1 
ATOM   14707 N  N     . LEU D 2 188 ? 143.413 96.787  145.292 1.00 20.78 ?  167 LEU D N     1 
ATOM   14708 C  CA    . LEU D 2 188 ? 144.215 95.635  144.832 1.00 21.78 ?  167 LEU D CA    1 
ATOM   14709 C  C     . LEU D 2 188 ? 144.805 95.775  143.423 1.00 21.91 ?  167 LEU D C     1 
ATOM   14710 O  O     . LEU D 2 188 ? 145.888 95.253  143.158 1.00 22.87 ?  167 LEU D O     1 
ATOM   14711 C  CB    . LEU D 2 188 ? 143.413 94.337  144.922 1.00 22.32 ?  167 LEU D CB    1 
ATOM   14712 C  CG    . LEU D 2 188 ? 143.005 93.775  146.283 1.00 23.33 ?  167 LEU D CG    1 
ATOM   14713 C  CD1   . LEU D 2 188 ? 142.203 92.504  146.063 1.00 22.43 ?  167 LEU D CD1   1 
ATOM   14714 C  CD2   . LEU D 2 188 ? 144.206 93.506  147.199 1.00 25.71 ?  167 LEU D CD2   1 
ATOM   14715 N  N     . PHE D 2 189 ? 144.091 96.453  142.522 1.00 21.56 ?  168 PHE D N     1 
ATOM   14716 C  CA    . PHE D 2 189 ? 144.593 96.711  141.169 1.00 21.86 ?  168 PHE D CA    1 
ATOM   14717 C  C     . PHE D 2 189 ? 145.857 97.596  141.160 1.00 21.87 ?  168 PHE D C     1 
ATOM   14718 O  O     . PHE D 2 189 ? 146.639 97.565  140.206 1.00 21.79 ?  168 PHE D O     1 
ATOM   14719 C  CB    . PHE D 2 189 ? 143.526 97.411  140.307 1.00 21.79 ?  168 PHE D CB    1 
ATOM   14720 C  CG    . PHE D 2 189 ? 142.465 96.492  139.746 1.00 21.88 ?  168 PHE D CG    1 
ATOM   14721 C  CD1   . PHE D 2 189 ? 142.781 95.212  139.284 1.00 21.44 ?  168 PHE D CD1   1 
ATOM   14722 C  CD2   . PHE D 2 189 ? 141.145 96.933  139.651 1.00 22.82 ?  168 PHE D CD2   1 
ATOM   14723 C  CE1   . PHE D 2 189 ? 141.789 94.373  138.761 1.00 22.35 ?  168 PHE D CE1   1 
ATOM   14724 C  CE2   . PHE D 2 189 ? 140.145 96.111  139.129 1.00 22.08 ?  168 PHE D CE2   1 
ATOM   14725 C  CZ    . PHE D 2 189 ? 140.464 94.823  138.693 1.00 22.60 ?  168 PHE D CZ    1 
ATOM   14726 N  N     . TYR D 2 190 ? 146.044 98.399  142.203 1.00 21.91 ?  169 TYR D N     1 
ATOM   14727 C  CA    . TYR D 2 190 ? 147.037 99.481  142.130 1.00 22.52 ?  169 TYR D CA    1 
ATOM   14728 C  C     . TYR D 2 190 ? 148.500 99.062  142.283 1.00 22.75 ?  169 TYR D C     1 
ATOM   14729 O  O     . TYR D 2 190 ? 149.373 99.743  141.763 1.00 21.93 ?  169 TYR D O     1 
ATOM   14730 C  CB    . TYR D 2 190 ? 146.657 100.656 143.036 1.00 22.67 ?  169 TYR D CB    1 
ATOM   14731 C  CG    . TYR D 2 190 ? 145.536 101.466 142.418 1.00 24.77 ?  169 TYR D CG    1 
ATOM   14732 C  CD1   . TYR D 2 190 ? 144.218 100.998 142.431 1.00 25.65 ?  169 TYR D CD1   1 
ATOM   14733 C  CD2   . TYR D 2 190 ? 145.800 102.674 141.779 1.00 25.94 ?  169 TYR D CD2   1 
ATOM   14734 C  CE1   . TYR D 2 190 ? 143.188 101.731 141.831 1.00 26.62 ?  169 TYR D CE1   1 
ATOM   14735 C  CE2   . TYR D 2 190 ? 144.779 103.420 141.193 1.00 26.91 ?  169 TYR D CE2   1 
ATOM   14736 C  CZ    . TYR D 2 190 ? 143.482 102.944 141.219 1.00 27.39 ?  169 TYR D CZ    1 
ATOM   14737 O  OH    . TYR D 2 190 ? 142.485 103.696 140.625 1.00 27.50 ?  169 TYR D OH    1 
ATOM   14738 N  N     . SER D 2 191 ? 148.762 97.936  142.956 1.00 22.74 ?  170 SER D N     1 
ATOM   14739 C  CA    . SER D 2 191 ? 150.114 97.363  142.945 1.00 23.43 ?  170 SER D CA    1 
ATOM   14740 C  C     . SER D 2 191 ? 150.494 97.001  141.510 1.00 23.08 ?  170 SER D C     1 
ATOM   14741 O  O     . SER D 2 191 ? 151.656 97.031  141.144 1.00 23.67 ?  170 SER D O     1 
ATOM   14742 C  CB    . SER D 2 191 ? 150.227 96.133  143.860 1.00 23.39 ?  170 SER D CB    1 
ATOM   14743 O  OG    . SER D 2 191 ? 149.358 95.090  143.442 1.00 24.10 ?  170 SER D OG    1 
ATOM   14744 N  N     . GLY D 2 192 ? 149.491 96.699  140.696 1.00 22.82 ?  171 GLY D N     1 
ATOM   14745 C  CA    . GLY D 2 192 ? 149.683 96.393  139.284 1.00 22.08 ?  171 GLY D CA    1 
ATOM   14746 C  C     . GLY D 2 192 ? 149.737 97.625  138.396 1.00 22.12 ?  171 GLY D C     1 
ATOM   14747 O  O     . GLY D 2 192 ? 150.660 97.767  137.592 1.00 22.86 ?  171 GLY D O     1 
ATOM   14748 N  N     . PHE D 2 193 ? 148.759 98.518  138.540 1.00 21.48 ?  172 PHE D N     1 
ATOM   14749 C  CA    . PHE D 2 193 ? 148.707 99.763  137.751 1.00 21.06 ?  172 PHE D CA    1 
ATOM   14750 C  C     . PHE D 2 193 ? 149.990 100.585 137.871 1.00 21.13 ?  172 PHE D C     1 
ATOM   14751 O  O     . PHE D 2 193 ? 150.347 101.311 136.942 1.00 21.18 ?  172 PHE D O     1 
ATOM   14752 C  CB    . PHE D 2 193 ? 147.532 100.640 138.181 1.00 21.33 ?  172 PHE D CB    1 
ATOM   14753 C  CG    . PHE D 2 193 ? 146.174 100.122 137.770 1.00 20.93 ?  172 PHE D CG    1 
ATOM   14754 C  CD1   . PHE D 2 193 ? 146.003 99.361  136.614 1.00 20.88 ?  172 PHE D CD1   1 
ATOM   14755 C  CD2   . PHE D 2 193 ? 145.055 100.447 138.525 1.00 19.83 ?  172 PHE D CD2   1 
ATOM   14756 C  CE1   . PHE D 2 193 ? 144.731 98.908  136.243 1.00 22.31 ?  172 PHE D CE1   1 
ATOM   14757 C  CE2   . PHE D 2 193 ? 143.779 100.009 138.153 1.00 20.67 ?  172 PHE D CE2   1 
ATOM   14758 C  CZ    . PHE D 2 193 ? 143.619 99.239  137.011 1.00 21.00 ?  172 PHE D CZ    1 
ATOM   14759 N  N     . TYR D 2 194 ? 150.682 100.458 139.005 1.00 20.48 ?  173 TYR D N     1 
ATOM   14760 C  CA    . TYR D 2 194 ? 151.893 101.233 139.264 1.00 20.76 ?  173 TYR D CA    1 
ATOM   14761 C  C     . TYR D 2 194 ? 152.863 101.201 138.077 1.00 20.53 ?  173 TYR D C     1 
ATOM   14762 O  O     . TYR D 2 194 ? 153.336 102.239 137.605 1.00 19.89 ?  173 TYR D O     1 
ATOM   14763 C  CB    . TYR D 2 194 ? 152.606 100.748 140.551 1.00 20.94 ?  173 TYR D CB    1 
ATOM   14764 C  CG    . TYR D 2 194 ? 153.733 101.673 140.975 1.00 21.56 ?  173 TYR D CG    1 
ATOM   14765 C  CD1   . TYR D 2 194 ? 153.542 102.622 141.983 1.00 22.23 ?  173 TYR D CD1   1 
ATOM   14766 C  CD2   . TYR D 2 194 ? 154.986 101.616 140.352 1.00 22.00 ?  173 TYR D CD2   1 
ATOM   14767 C  CE1   . TYR D 2 194 ? 154.568 103.489 142.358 1.00 21.58 ?  173 TYR D CE1   1 
ATOM   14768 C  CE2   . TYR D 2 194 ? 156.010 102.467 140.724 1.00 20.52 ?  173 TYR D CE2   1 
ATOM   14769 C  CZ    . TYR D 2 194 ? 155.796 103.401 141.724 1.00 21.66 ?  173 TYR D CZ    1 
ATOM   14770 O  OH    . TYR D 2 194 ? 156.807 104.264 142.074 1.00 21.37 ?  173 TYR D OH    1 
ATOM   14771 N  N     . TYR D 2 195 ? 153.132 100.007 137.576 1.00 20.77 ?  174 TYR D N     1 
ATOM   14772 C  CA    . TYR D 2 195 ? 154.195 99.850  136.598 1.00 21.12 ?  174 TYR D CA    1 
ATOM   14773 C  C     . TYR D 2 195 ? 153.875 100.499 135.240 1.00 21.49 ?  174 TYR D C     1 
ATOM   14774 O  O     . TYR D 2 195 ? 154.689 101.285 134.746 1.00 21.60 ?  174 TYR D O     1 
ATOM   14775 C  CB    . TYR D 2 195 ? 154.610 98.380  136.495 1.00 21.23 ?  174 TYR D CB    1 
ATOM   14776 C  CG    . TYR D 2 195 ? 156.058 98.150  136.122 1.00 21.77 ?  174 TYR D CG    1 
ATOM   14777 C  CD1   . TYR D 2 195 ? 157.077 98.969  136.619 1.00 23.28 ?  174 TYR D CD1   1 
ATOM   14778 C  CD2   . TYR D 2 195 ? 156.412 97.093  135.286 1.00 22.87 ?  174 TYR D CD2   1 
ATOM   14779 C  CE1   . TYR D 2 195 ? 158.416 98.740  136.271 1.00 23.81 ?  174 TYR D CE1   1 
ATOM   14780 C  CE2   . TYR D 2 195 ? 157.741 96.856  134.944 1.00 24.09 ?  174 TYR D CE2   1 
ATOM   14781 C  CZ    . TYR D 2 195 ? 158.732 97.682  135.432 1.00 23.51 ?  174 TYR D CZ    1 
ATOM   14782 O  OH    . TYR D 2 195 ? 160.048 97.447  135.081 1.00 25.36 ?  174 TYR D OH    1 
ATOM   14783 N  N     . PRO D 2 196 ? 152.697 100.193 134.638 1.00 21.86 ?  175 PRO D N     1 
ATOM   14784 C  CA    . PRO D 2 196 ? 152.314 100.895 133.403 1.00 22.03 ?  175 PRO D CA    1 
ATOM   14785 C  C     . PRO D 2 196 ? 152.279 102.414 133.568 1.00 22.18 ?  175 PRO D C     1 
ATOM   14786 O  O     . PRO D 2 196 ? 152.684 103.128 132.647 1.00 23.00 ?  175 PRO D O     1 
ATOM   14787 C  CB    . PRO D 2 196 ? 150.901 100.376 133.108 1.00 21.50 ?  175 PRO D CB    1 
ATOM   14788 C  CG    . PRO D 2 196 ? 150.792 99.114  133.808 1.00 22.47 ?  175 PRO D CG    1 
ATOM   14789 C  CD    . PRO D 2 196 ? 151.794 99.063  134.923 1.00 20.91 ?  175 PRO D CD    1 
ATOM   14790 N  N     . LEU D 2 197 ? 151.814 102.901 134.720 1.00 21.70 ?  176 LEU D N     1 
ATOM   14791 C  CA    . LEU D 2 197 ? 151.818 104.344 135.000 1.00 22.40 ?  176 LEU D CA    1 
ATOM   14792 C  C     . LEU D 2 197 ? 153.234 104.915 135.116 1.00 22.58 ?  176 LEU D C     1 
ATOM   14793 O  O     . LEU D 2 197 ? 153.495 106.042 134.677 1.00 22.15 ?  176 LEU D O     1 
ATOM   14794 C  CB    . LEU D 2 197 ? 151.050 104.658 136.277 1.00 22.15 ?  176 LEU D CB    1 
ATOM   14795 C  CG    . LEU D 2 197 ? 149.522 104.520 136.289 1.00 23.08 ?  176 LEU D CG    1 
ATOM   14796 C  CD1   . LEU D 2 197 ? 149.053 104.531 137.734 1.00 21.62 ?  176 LEU D CD1   1 
ATOM   14797 C  CD2   . LEU D 2 197 ? 148.853 105.646 135.474 1.00 21.94 ?  176 LEU D CD2   1 
ATOM   14798 N  N     . TYR D 2 198 ? 154.127 104.125 135.718 1.00 22.76 ?  177 TYR D N     1 
ATOM   14799 C  CA    . TYR D 2 198 ? 155.547 104.460 135.838 1.00 23.23 ?  177 TYR D CA    1 
ATOM   14800 C  C     . TYR D 2 198 ? 156.196 104.614 134.462 1.00 23.91 ?  177 TYR D C     1 
ATOM   14801 O  O     . TYR D 2 198 ? 156.905 105.601 134.212 1.00 24.20 ?  177 TYR D O     1 
ATOM   14802 C  CB    . TYR D 2 198 ? 156.271 103.403 136.690 1.00 23.19 ?  177 TYR D CB    1 
ATOM   14803 C  CG    . TYR D 2 198 ? 157.747 103.647 136.933 1.00 23.52 ?  177 TYR D CG    1 
ATOM   14804 C  CD1   . TYR D 2 198 ? 158.178 104.716 137.705 1.00 24.85 ?  177 TYR D CD1   1 
ATOM   14805 C  CD2   . TYR D 2 198 ? 158.714 102.770 136.423 1.00 25.30 ?  177 TYR D CD2   1 
ATOM   14806 C  CE1   . TYR D 2 198 ? 159.537 104.934 137.949 1.00 26.05 ?  177 TYR D CE1   1 
ATOM   14807 C  CE2   . TYR D 2 198 ? 160.082 102.977 136.666 1.00 26.38 ?  177 TYR D CE2   1 
ATOM   14808 C  CZ    . TYR D 2 198 ? 160.476 104.059 137.429 1.00 26.68 ?  177 TYR D CZ    1 
ATOM   14809 O  OH    . TYR D 2 198 ? 161.811 104.283 137.685 1.00 30.01 ?  177 TYR D OH    1 
ATOM   14810 N  N     . PHE D 2 199 ? 155.954 103.660 133.562 1.00 24.84 ?  178 PHE D N     1 
ATOM   14811 C  CA    . PHE D 2 199 ? 156.434 103.806 132.184 1.00 25.81 ?  178 PHE D CA    1 
ATOM   14812 C  C     . PHE D 2 199 ? 155.785 104.969 131.445 1.00 26.23 ?  178 PHE D C     1 
ATOM   14813 O  O     . PHE D 2 199 ? 156.470 105.745 130.778 1.00 26.58 ?  178 PHE D O     1 
ATOM   14814 C  CB    . PHE D 2 199 ? 156.261 102.514 131.395 1.00 26.08 ?  178 PHE D CB    1 
ATOM   14815 C  CG    . PHE D 2 199 ? 157.269 101.461 131.743 1.00 28.71 ?  178 PHE D CG    1 
ATOM   14816 C  CD1   . PHE D 2 199 ? 158.618 101.779 131.850 1.00 32.03 ?  178 PHE D CD1   1 
ATOM   14817 C  CD2   . PHE D 2 199 ? 156.879 100.152 131.971 1.00 31.77 ?  178 PHE D CD2   1 
ATOM   14818 C  CE1   . PHE D 2 199 ? 159.569 100.804 132.188 1.00 32.29 ?  178 PHE D CE1   1 
ATOM   14819 C  CE2   . PHE D 2 199 ? 157.823 99.173  132.298 1.00 32.72 ?  178 PHE D CE2   1 
ATOM   14820 C  CZ    . PHE D 2 199 ? 159.168 99.507  132.405 1.00 31.91 ?  178 PHE D CZ    1 
ATOM   14821 N  N     . TYR D 2 200 ? 154.465 105.072 131.578 1.00 26.46 ?  179 TYR D N     1 
ATOM   14822 C  CA    . TYR D 2 200 ? 153.652 106.115 130.934 1.00 27.43 ?  179 TYR D CA    1 
ATOM   14823 C  C     . TYR D 2 200 ? 154.143 107.506 131.323 1.00 27.68 ?  179 TYR D C     1 
ATOM   14824 O  O     . TYR D 2 200 ? 154.200 108.405 130.485 1.00 28.71 ?  179 TYR D O     1 
ATOM   14825 C  CB    . TYR D 2 200 ? 152.204 105.932 131.375 1.00 27.27 ?  179 TYR D CB    1 
ATOM   14826 C  CG    . TYR D 2 200 ? 151.132 106.615 130.561 1.00 28.90 ?  179 TYR D CG    1 
ATOM   14827 C  CD1   . TYR D 2 200 ? 151.109 106.531 129.176 1.00 29.00 ?  179 TYR D CD1   1 
ATOM   14828 C  CD2   . TYR D 2 200 ? 150.091 107.294 131.202 1.00 30.14 ?  179 TYR D CD2   1 
ATOM   14829 C  CE1   . TYR D 2 200 ? 150.097 107.139 128.437 1.00 31.26 ?  179 TYR D CE1   1 
ATOM   14830 C  CE2   . TYR D 2 200 ? 149.073 107.894 130.480 1.00 31.86 ?  179 TYR D CE2   1 
ATOM   14831 C  CZ    . TYR D 2 200 ? 149.083 107.819 129.097 1.00 32.51 ?  179 TYR D CZ    1 
ATOM   14832 O  OH    . TYR D 2 200 ? 148.075 108.418 128.381 1.00 33.77 ?  179 TYR D OH    1 
ATOM   14833 N  N     . GLY D 2 201 ? 154.502 107.674 132.595 1.00 27.68 ?  180 GLY D N     1 
ATOM   14834 C  CA    . GLY D 2 201 ? 155.048 108.934 133.088 1.00 28.02 ?  180 GLY D CA    1 
ATOM   14835 C  C     . GLY D 2 201 ? 156.454 109.266 132.598 1.00 28.60 ?  180 GLY D C     1 
ATOM   14836 O  O     . GLY D 2 201 ? 156.896 110.398 132.740 1.00 28.44 ?  180 GLY D O     1 
ATOM   14837 N  N     . GLN D 2 202 ? 157.150 108.270 132.040 1.00 29.34 ?  181 GLN D N     1 
ATOM   14838 C  CA    . GLN D 2 202 ? 158.513 108.415 131.499 1.00 30.39 ?  181 GLN D CA    1 
ATOM   14839 C  C     . GLN D 2 202 ? 158.556 108.508 129.973 1.00 30.55 ?  181 GLN D C     1 
ATOM   14840 O  O     . GLN D 2 202 ? 159.638 108.646 129.394 1.00 31.23 ?  181 GLN D O     1 
ATOM   14841 C  CB    . GLN D 2 202 ? 159.354 107.182 131.835 1.00 30.31 ?  181 GLN D CB    1 
ATOM   14842 C  CG    . GLN D 2 202 ? 159.714 106.947 133.253 1.00 32.40 ?  181 GLN D CG    1 
ATOM   14843 C  CD    . GLN D 2 202 ? 160.534 105.681 133.383 1.00 33.85 ?  181 GLN D CD    1 
ATOM   14844 O  OE1   . GLN D 2 202 ? 160.045 104.650 133.837 1.00 33.94 ?  181 GLN D OE1   1 
ATOM   14845 N  NE2   . GLN D 2 202 ? 161.778 105.741 132.938 1.00 34.92 ?  181 GLN D NE2   1 
ATOM   14846 N  N     . GLY D 2 203 ? 157.410 108.359 129.318 1.00 30.57 ?  182 GLY D N     1 
ATOM   14847 C  CA    . GLY D 2 203 ? 157.364 108.363 127.854 1.00 30.83 ?  182 GLY D CA    1 
ATOM   14848 C  C     . GLY D 2 203 ? 157.557 106.993 127.220 1.00 30.80 ?  182 GLY D C     1 
ATOM   14849 O  O     . GLY D 2 203 ? 157.741 106.890 126.004 1.00 30.86 ?  182 GLY D O     1 
ATOM   14850 N  N     . LYS D 2 204 ? 157.510 105.943 128.040 1.00 30.14 ?  183 LYS D N     1 
ATOM   14851 C  CA    . LYS D 2 204 ? 157.645 104.567 127.551 1.00 30.35 ?  183 LYS D CA    1 
ATOM   14852 C  C     . LYS D 2 204 ? 156.301 103.844 127.510 1.00 29.52 ?  183 LYS D C     1 
ATOM   14853 O  O     . LYS D 2 204 ? 155.441 104.088 128.352 1.00 28.60 ?  183 LYS D O     1 
ATOM   14854 C  CB    . LYS D 2 204 ? 158.636 103.790 128.415 1.00 30.76 ?  183 LYS D CB    1 
ATOM   14855 C  CG    . LYS D 2 204 ? 160.073 104.315 128.323 1.00 32.95 ?  183 LYS D CG    1 
ATOM   14856 C  CD    . LYS D 2 204 ? 160.921 103.692 129.405 1.00 36.37 ?  183 LYS D CD    1 
ATOM   14857 C  CE    . LYS D 2 204 ? 162.358 104.178 129.358 1.00 38.47 ?  183 LYS D CE    1 
ATOM   14858 N  NZ    . LYS D 2 204 ? 163.050 103.715 130.598 1.00 40.21 1  183 LYS D NZ    1 
ATOM   14859 N  N     . LEU D 2 205 ? 156.138 102.949 126.532 1.00 29.47 ?  184 LEU D N     1 
ATOM   14860 C  CA    . LEU D 2 205 ? 154.900 102.176 126.348 1.00 29.06 ?  184 LEU D CA    1 
ATOM   14861 C  C     . LEU D 2 205 ? 153.644 103.057 126.520 1.00 28.96 ?  184 LEU D C     1 
ATOM   14862 O  O     . LEU D 2 205 ? 152.752 102.767 127.326 1.00 27.68 ?  184 LEU D O     1 
ATOM   14863 C  CB    . LEU D 2 205 ? 154.864 100.958 127.285 1.00 28.63 ?  184 LEU D CB    1 
ATOM   14864 C  CG    . LEU D 2 205 ? 156.027 99.956  127.208 1.00 29.00 ?  184 LEU D CG    1 
ATOM   14865 C  CD1   . LEU D 2 205 ? 155.856 98.862  128.265 1.00 28.90 ?  184 LEU D CD1   1 
ATOM   14866 C  CD2   . LEU D 2 205 ? 156.139 99.335  125.822 1.00 28.67 ?  184 LEU D CD2   1 
ATOM   14867 N  N     . MET D 2 206 ? 153.611 104.131 125.736 1.00 29.02 ?  185 MET D N     1 
ATOM   14868 C  CA    . MET D 2 206 ? 152.572 105.147 125.793 1.00 29.72 ?  185 MET D CA    1 
ATOM   14869 C  C     . MET D 2 206 ? 151.189 104.702 125.328 1.00 29.54 ?  185 MET D C     1 
ATOM   14870 O  O     . MET D 2 206 ? 150.187 105.189 125.846 1.00 29.47 ?  185 MET D O     1 
ATOM   14871 C  CB    . MET D 2 206 ? 153.012 106.381 124.996 1.00 30.69 ?  185 MET D CB    1 
ATOM   14872 C  CG    . MET D 2 206 ? 154.311 106.984 125.507 1.00 32.03 ?  185 MET D CG    1 
ATOM   14873 S  SD    . MET D 2 206 ? 154.177 107.465 127.238 1.00 36.63 ?  185 MET D SD    1 
ATOM   14874 C  CE    . MET D 2 206 ? 153.453 109.087 127.070 1.00 33.80 ?  185 MET D CE    1 
ATOM   14875 N  N     . GLN D 2 207 ? 151.135 103.807 124.342 1.00 29.56 ?  186 GLN D N     1 
ATOM   14876 C  CA    . GLN D 2 207 ? 149.858 103.331 123.801 1.00 29.17 ?  186 GLN D CA    1 
ATOM   14877 C  C     . GLN D 2 207 ? 149.163 102.408 124.796 1.00 28.26 ?  186 GLN D C     1 
ATOM   14878 O  O     . GLN D 2 207 ? 147.977 102.573 125.069 1.00 27.98 ?  186 GLN D O     1 
ATOM   14879 C  CB    . GLN D 2 207 ? 150.048 102.622 122.450 1.00 29.80 ?  186 GLN D CB    1 
ATOM   14880 C  CG    . GLN D 2 207 ? 150.790 103.445 121.397 1.00 31.75 ?  186 GLN D CG    1 
ATOM   14881 C  CD    . GLN D 2 207 ? 150.185 104.822 121.216 1.00 34.93 ?  186 GLN D CD    1 
ATOM   14882 O  OE1   . GLN D 2 207 ? 149.086 104.972 120.667 1.00 36.91 ?  186 GLN D OE1   1 
ATOM   14883 N  NE2   . GLN D 2 207 ? 150.896 105.840 121.690 1.00 36.09 ?  186 GLN D NE2   1 
ATOM   14884 N  N     . SER D 2 208 ? 149.900 101.441 125.338 0.50 27.75 ?  187 SER D N     1 
ATOM   14885 C  CA    . SER D 2 208 ? 149.342 100.541 126.341 0.50 27.12 ?  187 SER D CA    1 
ATOM   14886 C  C     . SER D 2 208 ? 149.091 101.281 127.651 0.50 26.72 ?  187 SER D C     1 
ATOM   14887 O  O     . SER D 2 208 ? 148.150 100.952 128.373 0.50 26.30 ?  187 SER D O     1 
ATOM   14888 C  CB    . SER D 2 208 ? 150.248 99.330  126.567 0.50 26.88 ?  187 SER D CB    1 
ATOM   14889 O  OG    . SER D 2 208 ? 151.571 99.740  126.834 0.50 26.59 ?  187 SER D OG    1 
ATOM   14890 N  N     . GLY D 2 209 ? 149.929 102.275 127.947 1.00 26.64 ?  188 GLY D N     1 
ATOM   14891 C  CA    . GLY D 2 209 ? 149.742 103.137 129.131 1.00 26.43 ?  188 GLY D CA    1 
ATOM   14892 C  C     . GLY D 2 209 ? 148.476 103.980 129.047 1.00 26.66 ?  188 GLY D C     1 
ATOM   14893 O  O     . GLY D 2 209 ? 147.806 104.218 130.052 1.00 26.57 ?  188 GLY D O     1 
ATOM   14894 N  N     . GLU D 2 210 ? 148.148 104.442 127.843 1.00 27.42 ?  189 GLU D N     1 
ATOM   14895 C  CA    . GLU D 2 210 ? 146.899 105.166 127.618 1.00 27.73 ?  189 GLU D CA    1 
ATOM   14896 C  C     . GLU D 2 210 ? 145.703 104.235 127.870 1.00 27.04 ?  189 GLU D C     1 
ATOM   14897 O  O     . GLU D 2 210 ? 144.752 104.606 128.558 1.00 26.57 ?  189 GLU D O     1 
ATOM   14898 C  CB    . GLU D 2 210 ? 146.852 105.770 126.203 1.00 28.28 ?  189 GLU D CB    1 
ATOM   14899 C  CG    . GLU D 2 210 ? 145.602 106.627 125.945 1.00 30.71 ?  189 GLU D CG    1 
ATOM   14900 C  CD    . GLU D 2 210 ? 145.656 107.445 124.656 1.00 35.43 ?  189 GLU D CD    1 
ATOM   14901 O  OE1   . GLU D 2 210 ? 146.590 107.261 123.836 1.00 36.89 ?  189 GLU D OE1   1 
ATOM   14902 O  OE2   . GLU D 2 210 ? 144.751 108.291 124.471 1.00 37.04 -1 189 GLU D OE2   1 
ATOM   14903 N  N     . ILE D 2 211 ? 145.769 103.026 127.321 1.00 26.80 ?  190 ILE D N     1 
ATOM   14904 C  CA    . ILE D 2 211 ? 144.747 102.015 127.577 1.00 26.92 ?  190 ILE D CA    1 
ATOM   14905 C  C     . ILE D 2 211 ? 144.595 101.752 129.069 1.00 26.45 ?  190 ILE D C     1 
ATOM   14906 O  O     . ILE D 2 211 ? 143.476 101.743 129.578 1.00 26.65 ?  190 ILE D O     1 
ATOM   14907 C  CB    . ILE D 2 211 ? 145.017 100.701 126.800 1.00 27.00 ?  190 ILE D CB    1 
ATOM   14908 C  CG1   . ILE D 2 211 ? 144.787 100.934 125.302 1.00 28.77 ?  190 ILE D CG1   1 
ATOM   14909 C  CG2   . ILE D 2 211 ? 144.108 99.569  127.308 1.00 26.82 ?  190 ILE D CG2   1 
ATOM   14910 C  CD1   . ILE D 2 211 ? 145.166 99.764  124.403 1.00 30.88 ?  190 ILE D CD1   1 
ATOM   14911 N  N     . ILE D 2 212 ? 145.713 101.568 129.777 1.00 26.49 ?  191 ILE D N     1 
ATOM   14912 C  CA    . ILE D 2 212 ? 145.658 101.263 131.208 1.00 25.73 ?  191 ILE D CA    1 
ATOM   14913 C  C     . ILE D 2 212 ? 145.025 102.418 131.986 1.00 25.48 ?  191 ILE D C     1 
ATOM   14914 O  O     . ILE D 2 212 ? 144.240 102.198 132.912 1.00 24.95 ?  191 ILE D O     1 
ATOM   14915 C  CB    . ILE D 2 212 ? 147.055 100.890 131.790 1.00 26.44 ?  191 ILE D CB    1 
ATOM   14916 C  CG1   . ILE D 2 212 ? 147.568 99.580  131.178 1.00 26.71 ?  191 ILE D CG1   1 
ATOM   14917 C  CG2   . ILE D 2 212 ? 147.011 100.799 133.331 1.00 26.01 ?  191 ILE D CG2   1 
ATOM   14918 C  CD1   . ILE D 2 212 ? 146.727 98.346  131.451 1.00 30.50 ?  191 ILE D CD1   1 
ATOM   14919 N  N     . ASN D 2 213 ? 145.350 103.644 131.586 1.00 24.79 ?  192 ASN D N     1 
ATOM   14920 C  CA    . ASN D 2 213 ? 144.783 104.825 132.220 1.00 24.80 ?  192 ASN D CA    1 
ATOM   14921 C  C     . ASN D 2 213 ? 143.251 104.907 132.056 1.00 24.44 ?  192 ASN D C     1 
ATOM   14922 O  O     . ASN D 2 213 ? 142.544 105.370 132.958 1.00 23.25 ?  192 ASN D O     1 
ATOM   14923 C  CB    . ASN D 2 213 ? 145.466 106.087 131.691 1.00 25.68 ?  192 ASN D CB    1 
ATOM   14924 C  CG    . ASN D 2 213 ? 145.664 107.140 132.766 1.00 27.89 ?  192 ASN D CG    1 
ATOM   14925 O  OD1   . ASN D 2 213 ? 145.831 106.827 133.942 1.00 31.05 ?  192 ASN D OD1   1 
ATOM   14926 N  ND2   . ASN D 2 213 ? 145.652 108.402 132.359 1.00 31.70 ?  192 ASN D ND2   1 
ATOM   14927 N  N     . LEU D 2 214 ? 142.746 104.443 130.912 1.00 23.60 ?  193 LEU D N     1 
ATOM   14928 C  CA    . LEU D 2 214 ? 141.303 104.432 130.667 1.00 23.84 ?  193 LEU D CA    1 
ATOM   14929 C  C     . LEU D 2 214 ? 140.636 103.365 131.516 1.00 23.48 ?  193 LEU D C     1 
ATOM   14930 O  O     . LEU D 2 214 ? 139.566 103.597 132.085 1.00 24.12 ?  193 LEU D O     1 
ATOM   14931 C  CB    . LEU D 2 214 ? 141.006 104.194 129.187 1.00 23.71 ?  193 LEU D CB    1 
ATOM   14932 C  CG    . LEU D 2 214 ? 141.291 105.381 128.257 1.00 25.29 ?  193 LEU D CG    1 
ATOM   14933 C  CD1   . LEU D 2 214 ? 141.098 104.974 126.795 1.00 25.41 ?  193 LEU D CD1   1 
ATOM   14934 C  CD2   . LEU D 2 214 ? 140.419 106.580 128.591 1.00 25.80 ?  193 LEU D CD2   1 
ATOM   14935 N  N     . ILE D 2 215 ? 141.282 102.202 131.603 1.00 22.89 ?  194 ILE D N     1 
ATOM   14936 C  CA    . ILE D 2 215 ? 140.805 101.108 132.437 1.00 22.25 ?  194 ILE D CA    1 
ATOM   14937 C  C     . ILE D 2 215 ? 140.755 101.573 133.888 1.00 22.55 ?  194 ILE D C     1 
ATOM   14938 O  O     . ILE D 2 215 ? 139.729 101.426 134.568 1.00 22.53 ?  194 ILE D O     1 
ATOM   14939 C  CB    . ILE D 2 215 ? 141.706 99.862  132.321 1.00 22.37 ?  194 ILE D CB    1 
ATOM   14940 C  CG1   . ILE D 2 215 ? 141.611 99.265  130.911 1.00 21.89 ?  194 ILE D CG1   1 
ATOM   14941 C  CG2   . ILE D 2 215 ? 141.344 98.829  133.407 1.00 20.25 ?  194 ILE D CG2   1 
ATOM   14942 C  CD1   . ILE D 2 215 ? 142.484 98.025  130.687 1.00 20.48 ?  194 ILE D CD1   1 
ATOM   14943 N  N     . LEU D 2 216 ? 141.860 102.149 134.353 1.00 22.35 ?  195 LEU D N     1 
ATOM   14944 C  CA    . LEU D 2 216 ? 141.971 102.596 135.739 1.00 22.51 ?  195 LEU D CA    1 
ATOM   14945 C  C     . LEU D 2 216 ? 140.877 103.618 136.061 1.00 22.30 ?  195 LEU D C     1 
ATOM   14946 O  O     . LEU D 2 216 ? 140.278 103.565 137.143 1.00 21.62 ?  195 LEU D O     1 
ATOM   14947 C  CB    . LEU D 2 216 ? 143.368 103.191 135.977 1.00 23.06 ?  195 LEU D CB    1 
ATOM   14948 C  CG    . LEU D 2 216 ? 143.793 103.869 137.289 1.00 23.98 ?  195 LEU D CG    1 
ATOM   14949 C  CD1   . LEU D 2 216 ? 145.296 103.967 137.300 1.00 24.44 ?  195 LEU D CD1   1 
ATOM   14950 C  CD2   . LEU D 2 216 ? 143.181 105.271 137.448 1.00 25.00 ?  195 LEU D CD2   1 
ATOM   14951 N  N     . ARG D 2 217 ? 140.630 104.542 135.126 1.00 21.64 ?  196 ARG D N     1 
ATOM   14952 C  CA    . ARG D 2 217 ? 139.575 105.549 135.289 1.00 22.49 ?  196 ARG D CA    1 
ATOM   14953 C  C     . ARG D 2 217 ? 138.180 104.895 135.448 1.00 21.56 ?  196 ARG D C     1 
ATOM   14954 O  O     . ARG D 2 217 ? 137.378 105.356 136.250 1.00 21.32 ?  196 ARG D O     1 
ATOM   14955 C  CB    . ARG D 2 217 ? 139.588 106.589 134.151 1.00 23.07 ?  196 ARG D CB    1 
ATOM   14956 C  CG    . ARG D 2 217 ? 138.616 107.769 134.365 1.00 25.64 ?  196 ARG D CG    1 
ATOM   14957 C  CD    . ARG D 2 217 ? 138.482 108.674 133.126 1.00 32.11 ?  196 ARG D CD    1 
ATOM   14958 N  NE    . ARG D 2 217 ? 138.009 107.939 131.945 1.00 35.06 ?  196 ARG D NE    1 
ATOM   14959 C  CZ    . ARG D 2 217 ? 137.603 108.503 130.812 1.00 37.65 ?  196 ARG D CZ    1 
ATOM   14960 N  NH1   . ARG D 2 217 ? 137.578 109.827 130.691 1.00 40.20 1  196 ARG D NH1   1 
ATOM   14961 N  NH2   . ARG D 2 217 ? 137.204 107.743 129.796 1.00 38.20 ?  196 ARG D NH2   1 
ATOM   14962 N  N     . ASP D 2 218 ? 137.903 103.830 134.694 1.00 21.34 ?  197 ASP D N     1 
ATOM   14963 C  CA    . ASP D 2 218 ? 136.682 103.036 134.900 1.00 21.09 ?  197 ASP D CA    1 
ATOM   14964 C  C     . ASP D 2 218 ? 136.659 102.365 136.289 1.00 20.65 ?  197 ASP D C     1 
ATOM   14965 O  O     . ASP D 2 218 ? 135.646 102.431 136.989 1.00 20.16 ?  197 ASP D O     1 
ATOM   14966 C  CB    . ASP D 2 218 ? 136.512 101.969 133.809 1.00 21.58 ?  197 ASP D CB    1 
ATOM   14967 C  CG    . ASP D 2 218 ? 136.247 102.560 132.425 1.00 22.60 ?  197 ASP D CG    1 
ATOM   14968 O  OD1   . ASP D 2 218 ? 135.760 103.710 132.322 1.00 24.72 ?  197 ASP D OD1   1 
ATOM   14969 O  OD2   . ASP D 2 218 ? 136.543 101.861 131.429 1.00 22.64 -1 197 ASP D OD2   1 
ATOM   14970 N  N     . GLU D 2 219 ? 137.756 101.721 136.692 1.00 20.59 ?  198 GLU D N     1 
ATOM   14971 C  CA    . GLU D 2 219 ? 137.770 101.025 137.998 1.00 20.66 ?  198 GLU D CA    1 
ATOM   14972 C  C     . GLU D 2 219 ? 137.563 101.998 139.162 1.00 20.45 ?  198 GLU D C     1 
ATOM   14973 O  O     . GLU D 2 219 ? 136.905 101.658 140.150 1.00 20.59 ?  198 GLU D O     1 
ATOM   14974 C  CB    . GLU D 2 219 ? 139.049 100.199 138.214 1.00 20.55 ?  198 GLU D CB    1 
ATOM   14975 C  CG    . GLU D 2 219 ? 139.558 99.382  136.986 1.00 21.99 ?  198 GLU D CG    1 
ATOM   14976 C  CD    . GLU D 2 219 ? 138.586 98.324  136.448 1.00 24.00 ?  198 GLU D CD    1 
ATOM   14977 O  OE1   . GLU D 2 219 ? 137.355 98.425  136.636 1.00 25.06 ?  198 GLU D OE1   1 
ATOM   14978 O  OE2   . GLU D 2 219 ? 139.060 97.382  135.792 1.00 24.49 -1 198 GLU D OE2   1 
ATOM   14979 N  N     . ALA D 2 220 ? 138.108 103.204 139.034 1.00 20.47 ?  199 ALA D N     1 
ATOM   14980 C  CA    . ALA D 2 220 ? 137.912 104.260 140.049 1.00 21.10 ?  199 ALA D CA    1 
ATOM   14981 C  C     . ALA D 2 220 ? 136.435 104.566 140.280 1.00 21.34 ?  199 ALA D C     1 
ATOM   14982 O  O     . ALA D 2 220 ? 135.964 104.500 141.414 1.00 21.19 ?  199 ALA D O     1 
ATOM   14983 C  CB    . ALA D 2 220 ? 138.686 105.531 139.690 1.00 21.09 ?  199 ALA D CB    1 
ATOM   14984 N  N     . ILE D 2 221 ? 135.702 104.869 139.206 1.00 21.31 ?  200 ILE D N     1 
ATOM   14985 C  CA    . ILE D 2 221 ? 134.263 105.092 139.324 1.00 21.80 ?  200 ILE D CA    1 
ATOM   14986 C  C     . ILE D 2 221 ? 133.479 103.838 139.768 1.00 20.90 ?  200 ILE D C     1 
ATOM   14987 O  O     . ILE D 2 221 ? 132.522 103.953 140.532 1.00 20.54 ?  200 ILE D O     1 
ATOM   14988 C  CB    . ILE D 2 221 ? 133.645 105.774 138.069 1.00 22.75 ?  200 ILE D CB    1 
ATOM   14989 C  CG1   . ILE D 2 221 ? 132.275 106.345 138.418 1.00 24.63 ?  200 ILE D CG1   1 
ATOM   14990 C  CG2   . ILE D 2 221 ? 133.512 104.799 136.902 1.00 23.38 ?  200 ILE D CG2   1 
ATOM   14991 C  CD1   . ILE D 2 221 ? 131.816 107.436 137.496 1.00 26.91 ?  200 ILE D CD1   1 
ATOM   14992 N  N     . HIS D 2 222 ? 133.903 102.646 139.330 1.00 20.31 ?  201 HIS D N     1 
ATOM   14993 C  CA    . HIS D 2 222 ? 133.275 101.411 139.808 1.00 20.25 ?  201 HIS D CA    1 
ATOM   14994 C  C     . HIS D 2 222 ? 133.395 101.310 141.327 1.00 20.51 ?  201 HIS D C     1 
ATOM   14995 O  O     . HIS D 2 222 ? 132.402 101.070 142.025 1.00 20.99 ?  201 HIS D O     1 
ATOM   14996 C  CB    . HIS D 2 222 ? 133.879 100.162 139.157 1.00 19.79 ?  201 HIS D CB    1 
ATOM   14997 C  CG    . HIS D 2 222 ? 133.714 100.091 137.670 1.00 19.25 ?  201 HIS D CG    1 
ATOM   14998 N  ND1   . HIS D 2 222 ? 134.331 99.120  136.910 1.00 18.35 ?  201 HIS D ND1   1 
ATOM   14999 C  CD2   . HIS D 2 222 ? 133.020 100.866 136.800 1.00 17.64 ?  201 HIS D CD2   1 
ATOM   15000 C  CE1   . HIS D 2 222 ? 134.016 99.288  135.638 1.00 18.28 ?  201 HIS D CE1   1 
ATOM   15001 N  NE2   . HIS D 2 222 ? 133.227 100.346 135.543 1.00 20.01 ?  201 HIS D NE2   1 
ATOM   15002 N  N     . GLY D 2 223 ? 134.611 101.516 141.836 1.00 20.33 ?  202 GLY D N     1 
ATOM   15003 C  CA    . GLY D 2 223 ? 134.874 101.497 143.281 1.00 19.94 ?  202 GLY D CA    1 
ATOM   15004 C  C     . GLY D 2 223 ? 134.051 102.512 144.066 1.00 19.80 ?  202 GLY D C     1 
ATOM   15005 O  O     . GLY D 2 223 ? 133.487 102.177 145.107 1.00 19.96 ?  202 GLY D O     1 
ATOM   15006 N  N     . VAL D 2 224 ? 133.952 103.742 143.559 1.00 19.49 ?  203 VAL D N     1 
ATOM   15007 C  CA    . VAL D 2 224 ? 133.148 104.783 144.221 1.00 18.88 ?  203 VAL D CA    1 
ATOM   15008 C  C     . VAL D 2 224 ? 131.660 104.410 144.270 1.00 18.55 ?  203 VAL D C     1 
ATOM   15009 O  O     . VAL D 2 224 ? 131.001 104.554 145.313 1.00 17.65 ?  203 VAL D O     1 
ATOM   15010 C  CB    . VAL D 2 224 ? 133.340 106.197 143.558 1.00 19.22 ?  203 VAL D CB    1 
ATOM   15011 C  CG1   . VAL D 2 224 ? 132.463 107.256 144.255 1.00 18.51 ?  203 VAL D CG1   1 
ATOM   15012 C  CG2   . VAL D 2 224 ? 134.822 106.625 143.602 1.00 19.69 ?  203 VAL D CG2   1 
ATOM   15013 N  N     . TYR D 2 225 ? 131.144 103.905 143.151 1.00 18.17 ?  204 TYR D N     1 
ATOM   15014 C  CA    . TYR D 2 225 ? 129.732 103.536 143.040 1.00 18.76 ?  204 TYR D CA    1 
ATOM   15015 C  C     . TYR D 2 225 ? 129.367 102.368 143.973 1.00 18.93 ?  204 TYR D C     1 
ATOM   15016 O  O     . TYR D 2 225 ? 128.421 102.461 144.768 1.00 18.77 ?  204 TYR D O     1 
ATOM   15017 C  CB    . TYR D 2 225 ? 129.355 103.203 141.583 1.00 18.96 ?  204 TYR D CB    1 
ATOM   15018 C  CG    . TYR D 2 225 ? 127.860 102.950 141.426 1.00 20.06 ?  204 TYR D CG    1 
ATOM   15019 C  CD1   . TYR D 2 225 ? 126.938 103.988 141.620 1.00 21.79 ?  204 TYR D CD1   1 
ATOM   15020 C  CD2   . TYR D 2 225 ? 127.368 101.677 141.121 1.00 19.51 ?  204 TYR D CD2   1 
ATOM   15021 C  CE1   . TYR D 2 225 ? 125.564 103.764 141.509 1.00 20.38 ?  204 TYR D CE1   1 
ATOM   15022 C  CE2   . TYR D 2 225 ? 125.980 101.444 141.001 1.00 19.38 ?  204 TYR D CE2   1 
ATOM   15023 C  CZ    . TYR D 2 225 ? 125.094 102.499 141.202 1.00 20.84 ?  204 TYR D CZ    1 
ATOM   15024 O  OH    . TYR D 2 225 ? 123.733 102.306 141.107 1.00 20.77 ?  204 TYR D OH    1 
ATOM   15025 N  N     . VAL D 2 226 ? 130.121 101.274 143.885 1.00 18.76 ?  205 VAL D N     1 
ATOM   15026 C  CA    . VAL D 2 226 ? 129.875 100.129 144.757 1.00 18.85 ?  205 VAL D CA    1 
ATOM   15027 C  C     . VAL D 2 226 ? 130.032 100.544 146.219 1.00 19.19 ?  205 VAL D C     1 
ATOM   15028 O  O     . VAL D 2 226 ? 129.281 100.077 147.077 1.00 19.87 ?  205 VAL D O     1 
ATOM   15029 C  CB    . VAL D 2 226 ? 130.771 98.935  144.405 1.00 19.28 ?  205 VAL D CB    1 
ATOM   15030 C  CG1   . VAL D 2 226 ? 130.536 97.756  145.387 1.00 18.22 ?  205 VAL D CG1   1 
ATOM   15031 C  CG2   . VAL D 2 226 ? 130.490 98.510  142.954 1.00 18.40 ?  205 VAL D CG2   1 
ATOM   15032 N  N     . GLY D 2 227 ? 130.986 101.440 146.486 1.00 18.53 ?  206 GLY D N     1 
ATOM   15033 C  CA    . GLY D 2 227 ? 131.163 102.019 147.831 1.00 18.74 ?  206 GLY D CA    1 
ATOM   15034 C  C     . GLY D 2 227 ? 129.923 102.702 148.382 1.00 19.17 ?  206 GLY D C     1 
ATOM   15035 O  O     . GLY D 2 227 ? 129.600 102.569 149.571 1.00 18.66 ?  206 GLY D O     1 
ATOM   15036 N  N     . LEU D 2 228 ? 129.234 103.454 147.526 1.00 19.00 ?  207 LEU D N     1 
ATOM   15037 C  CA    . LEU D 2 228 ? 127.999 104.127 147.937 1.00 19.73 ?  207 LEU D CA    1 
ATOM   15038 C  C     . LEU D 2 228 ? 126.888 103.110 148.231 1.00 19.76 ?  207 LEU D C     1 
ATOM   15039 O  O     . LEU D 2 228 ? 126.147 103.268 149.200 1.00 20.07 ?  207 LEU D O     1 
ATOM   15040 C  CB    . LEU D 2 228 ? 127.565 105.156 146.890 1.00 19.36 ?  207 LEU D CB    1 
ATOM   15041 C  CG    . LEU D 2 228 ? 128.467 106.395 146.771 1.00 20.50 ?  207 LEU D CG    1 
ATOM   15042 C  CD1   . LEU D 2 228 ? 128.103 107.204 145.539 1.00 19.87 ?  207 LEU D CD1   1 
ATOM   15043 C  CD2   . LEU D 2 228 ? 128.393 107.282 148.048 1.00 22.38 ?  207 LEU D CD2   1 
ATOM   15044 N  N     . LEU D 2 229 ? 126.805 102.052 147.425 1.00 19.27 ?  208 LEU D N     1 
ATOM   15045 C  CA    . LEU D 2 229 ? 125.849 100.959 147.689 1.00 19.47 ?  208 LEU D CA    1 
ATOM   15046 C  C     . LEU D 2 229 ? 126.130 100.230 149.009 1.00 19.67 ?  208 LEU D C     1 
ATOM   15047 O  O     . LEU D 2 229 ? 125.196 99.822  149.711 1.00 19.82 ?  208 LEU D O     1 
ATOM   15048 C  CB    . LEU D 2 229 ? 125.821 99.948  146.524 1.00 19.51 ?  208 LEU D CB    1 
ATOM   15049 C  CG    . LEU D 2 229 ? 125.408 100.421 145.120 1.00 19.48 ?  208 LEU D CG    1 
ATOM   15050 C  CD1   . LEU D 2 229 ? 125.606 99.287  144.097 1.00 20.14 ?  208 LEU D CD1   1 
ATOM   15051 C  CD2   . LEU D 2 229 ? 123.965 100.970 145.066 1.00 19.95 ?  208 LEU D CD2   1 
ATOM   15052 N  N     . ALA D 2 230 ? 127.409 100.056 149.343 1.00 19.43 ?  209 ALA D N     1 
ATOM   15053 C  CA    . ALA D 2 230 ? 127.802 99.462  150.628 1.00 20.29 ?  209 ALA D CA    1 
ATOM   15054 C  C     . ALA D 2 230 ? 127.447 100.363 151.813 1.00 21.17 ?  209 ALA D C     1 
ATOM   15055 O  O     . ALA D 2 230 ? 126.941 99.884  152.823 1.00 21.73 ?  209 ALA D O     1 
ATOM   15056 C  CB    . ALA D 2 230 ? 129.292 99.130  150.634 1.00 19.99 ?  209 ALA D CB    1 
ATOM   15057 N  N     . GLN D 2 231 ? 127.706 101.664 151.686 1.00 22.26 ?  210 GLN D N     1 
ATOM   15058 C  CA    . GLN D 2 231 ? 127.351 102.635 152.738 1.00 23.33 ?  210 GLN D CA    1 
ATOM   15059 C  C     . GLN D 2 231 ? 125.843 102.667 153.006 1.00 23.85 ?  210 GLN D C     1 
ATOM   15060 O  O     . GLN D 2 231 ? 125.418 102.814 154.148 1.00 24.91 ?  210 GLN D O     1 
ATOM   15061 C  CB    . GLN D 2 231 ? 127.832 104.044 152.379 1.00 23.49 ?  210 GLN D CB    1 
ATOM   15062 C  CG    . GLN D 2 231 ? 129.353 104.225 152.326 1.00 23.05 ?  210 GLN D CG    1 
ATOM   15063 C  CD    . GLN D 2 231 ? 129.743 105.650 151.936 1.00 24.65 ?  210 GLN D CD    1 
ATOM   15064 O  OE1   . GLN D 2 231 ? 129.262 106.612 152.534 1.00 25.85 ?  210 GLN D OE1   1 
ATOM   15065 N  NE2   . GLN D 2 231 ? 130.602 105.788 150.925 1.00 22.30 ?  210 GLN D NE2   1 
ATOM   15066 N  N     . GLU D 2 232 ? 125.042 102.550 151.950 1.00 24.36 ?  211 GLU D N     1 
ATOM   15067 C  CA    . GLU D 2 232 ? 123.592 102.439 152.091 1.00 24.83 ?  211 GLU D CA    1 
ATOM   15068 C  C     . GLU D 2 232 ? 123.192 101.275 153.004 1.00 24.34 ?  211 GLU D C     1 
ATOM   15069 O  O     . GLU D 2 232 ? 122.344 101.442 153.882 1.00 24.20 ?  211 GLU D O     1 
ATOM   15070 C  CB    . GLU D 2 232 ? 122.930 102.282 150.727 1.00 25.15 ?  211 GLU D CB    1 
ATOM   15071 C  CG    . GLU D 2 232 ? 121.430 102.423 150.754 1.00 28.55 ?  211 GLU D CG    1 
ATOM   15072 C  CD    . GLU D 2 232 ? 120.842 102.283 149.378 1.00 33.83 ?  211 GLU D CD    1 
ATOM   15073 O  OE1   . GLU D 2 232 ? 120.678 103.322 148.705 1.00 35.09 ?  211 GLU D OE1   1 
ATOM   15074 O  OE2   . GLU D 2 232 ? 120.585 101.135 148.952 1.00 35.51 -1 211 GLU D OE2   1 
ATOM   15075 N  N     . ILE D 2 233 ? 123.803 100.107 152.804 1.00 23.39 ?  212 ILE D N     1 
ATOM   15076 C  CA    . ILE D 2 233 ? 123.548 98.949  153.678 1.00 23.42 ?  212 ILE D CA    1 
ATOM   15077 C  C     . ILE D 2 233 ? 124.059 99.210  155.095 1.00 23.74 ?  212 ILE D C     1 
ATOM   15078 O  O     . ILE D 2 233 ? 123.339 99.006  156.071 1.00 24.61 ?  212 ILE D O     1 
ATOM   15079 C  CB    . ILE D 2 233 ? 124.142 97.633  153.106 1.00 22.81 ?  212 ILE D CB    1 
ATOM   15080 C  CG1   . ILE D 2 233 ? 123.427 97.243  151.805 1.00 22.94 ?  212 ILE D CG1   1 
ATOM   15081 C  CG2   . ILE D 2 233 ? 124.026 96.490  154.124 1.00 22.45 ?  212 ILE D CG2   1 
ATOM   15082 C  CD1   . ILE D 2 233 ? 124.163 96.163  150.981 1.00 22.21 ?  212 ILE D CD1   1 
ATOM   15083 N  N     . TYR D 2 234 ? 125.299 99.680  155.200 1.00 24.19 ?  213 TYR D N     1 
ATOM   15084 C  CA    . TYR D 2 234 ? 125.927 99.988  156.477 1.00 24.59 ?  213 TYR D CA    1 
ATOM   15085 C  C     . TYR D 2 234 ? 125.056 100.919 157.328 1.00 25.15 ?  213 TYR D C     1 
ATOM   15086 O  O     . TYR D 2 234 ? 124.911 100.701 158.533 1.00 24.94 ?  213 TYR D O     1 
ATOM   15087 C  CB    . TYR D 2 234 ? 127.298 100.626 156.237 1.00 24.41 ?  213 TYR D CB    1 
ATOM   15088 C  CG    . TYR D 2 234 ? 128.057 101.013 157.489 1.00 25.93 ?  213 TYR D CG    1 
ATOM   15089 C  CD1   . TYR D 2 234 ? 128.850 100.086 158.156 1.00 24.70 ?  213 TYR D CD1   1 
ATOM   15090 C  CD2   . TYR D 2 234 ? 127.987 102.317 157.999 1.00 26.11 ?  213 TYR D CD2   1 
ATOM   15091 C  CE1   . TYR D 2 234 ? 129.556 100.438 159.303 1.00 27.90 ?  213 TYR D CE1   1 
ATOM   15092 C  CE2   . TYR D 2 234 ? 128.693 102.676 159.140 1.00 27.70 ?  213 TYR D CE2   1 
ATOM   15093 C  CZ    . TYR D 2 234 ? 129.476 101.735 159.784 1.00 27.89 ?  213 TYR D CZ    1 
ATOM   15094 O  OH    . TYR D 2 234 ? 130.174 102.084 160.916 1.00 32.34 ?  213 TYR D OH    1 
ATOM   15095 N  N     . ASN D 2 235 ? 124.492 101.947 156.692 1.00 25.43 ?  214 ASN D N     1 
ATOM   15096 C  CA    . ASN D 2 235 ? 123.681 102.959 157.390 1.00 26.77 ?  214 ASN D CA    1 
ATOM   15097 C  C     . ASN D 2 235 ? 122.319 102.451 157.862 1.00 27.06 ?  214 ASN D C     1 
ATOM   15098 O  O     . ASN D 2 235 ? 121.644 103.113 158.645 1.00 27.42 ?  214 ASN D O     1 
ATOM   15099 C  CB    . ASN D 2 235 ? 123.471 104.199 156.518 1.00 26.80 ?  214 ASN D CB    1 
ATOM   15100 C  CG    . ASN D 2 235 ? 124.756 104.916 156.203 1.00 28.19 ?  214 ASN D CG    1 
ATOM   15101 O  OD1   . ASN D 2 235 ? 125.679 104.961 157.014 1.00 29.35 ?  214 ASN D OD1   1 
ATOM   15102 N  ND2   . ASN D 2 235 ? 124.821 105.495 155.015 1.00 30.84 ?  214 ASN D ND2   1 
ATOM   15103 N  N     . LYS D 2 236 ? 121.921 101.284 157.380 1.00 26.87 ?  215 LYS D N     1 
ATOM   15104 C  CA    . LYS D 2 236 ? 120.667 100.675 157.806 1.00 27.86 ?  215 LYS D CA    1 
ATOM   15105 C  C     . LYS D 2 236 ? 120.859 99.804  159.055 1.00 28.07 ?  215 LYS D C     1 
ATOM   15106 O  O     . LYS D 2 236 ? 119.896 99.251  159.584 1.00 28.22 ?  215 LYS D O     1 
ATOM   15107 C  CB    . LYS D 2 236 ? 120.057 99.855  156.668 1.00 27.52 ?  215 LYS D CB    1 
ATOM   15108 C  CG    . LYS D 2 236 ? 119.641 100.672 155.469 1.00 29.60 ?  215 LYS D CG    1 
ATOM   15109 C  CD    . LYS D 2 236 ? 118.535 99.992  154.679 1.00 34.24 ?  215 LYS D CD    1 
ATOM   15110 C  CE    . LYS D 2 236 ? 119.037 99.252  153.454 1.00 36.75 ?  215 LYS D CE    1 
ATOM   15111 N  NZ    . LYS D 2 236 ? 119.895 98.105  153.820 1.00 40.41 1  215 LYS D NZ    1 
ATOM   15112 N  N     . GLN D 2 237 ? 122.099 99.694  159.524 1.00 28.33 ?  216 GLN D N     1 
ATOM   15113 C  CA    . GLN D 2 237 ? 122.428 98.782  160.622 1.00 29.60 ?  216 GLN D CA    1 
ATOM   15114 C  C     . GLN D 2 237 ? 122.435 99.474  161.980 1.00 30.69 ?  216 GLN D C     1 
ATOM   15115 O  O     . GLN D 2 237 ? 122.578 100.698 162.063 1.00 30.85 ?  216 GLN D O     1 
ATOM   15116 C  CB    . GLN D 2 237 ? 123.794 98.102  160.387 1.00 29.08 ?  216 GLN D CB    1 
ATOM   15117 C  CG    . GLN D 2 237 ? 123.965 97.405  159.034 1.00 27.78 ?  216 GLN D CG    1 
ATOM   15118 C  CD    . GLN D 2 237 ? 122.817 96.471  158.686 1.00 28.38 ?  216 GLN D CD    1 
ATOM   15119 O  OE1   . GLN D 2 237 ? 122.433 95.616  159.483 1.00 29.30 ?  216 GLN D OE1   1 
ATOM   15120 N  NE2   . GLN D 2 237 ? 122.271 96.624  157.483 1.00 26.88 ?  216 GLN D NE2   1 
ATOM   15121 N  N     . THR D 2 238 ? 122.293 98.676  163.038 1.00 32.02 ?  217 THR D N     1 
ATOM   15122 C  CA    . THR D 2 238 ? 122.447 99.163  164.413 1.00 33.47 ?  217 THR D CA    1 
ATOM   15123 C  C     . THR D 2 238 ? 123.890 99.599  164.686 1.00 34.29 ?  217 THR D C     1 
ATOM   15124 O  O     . THR D 2 238 ? 124.800 99.339  163.881 1.00 33.78 ?  217 THR D O     1 
ATOM   15125 C  CB    . THR D 2 238 ? 122.044 98.075  165.448 1.00 34.00 ?  217 THR D CB    1 
ATOM   15126 O  OG1   . THR D 2 238 ? 122.960 96.971  165.372 1.00 34.33 ?  217 THR D OG1   1 
ATOM   15127 C  CG2   . THR D 2 238 ? 120.614 97.572  165.191 1.00 33.53 ?  217 THR D CG2   1 
ATOM   15128 N  N     . GLU D 2 239 ? 124.108 100.248 165.825 1.00 35.45 ?  218 GLU D N     1 
ATOM   15129 C  CA    . GLU D 2 239 ? 125.450 100.689 166.191 1.00 36.37 ?  218 GLU D CA    1 
ATOM   15130 C  C     . GLU D 2 239 ? 126.400 99.523  166.453 1.00 36.29 ?  218 GLU D C     1 
ATOM   15131 O  O     . GLU D 2 239 ? 127.568 99.574  166.054 1.00 36.18 ?  218 GLU D O     1 
ATOM   15132 C  CB    . GLU D 2 239 ? 125.414 101.660 167.375 1.00 37.27 ?  218 GLU D CB    1 
ATOM   15133 C  CG    . GLU D 2 239 ? 124.800 103.029 167.026 1.00 39.45 ?  218 GLU D CG    1 
ATOM   15134 C  CD    . GLU D 2 239 ? 125.499 103.726 165.861 1.00 41.22 ?  218 GLU D CD    1 
ATOM   15135 O  OE1   . GLU D 2 239 ? 126.749 103.776 165.842 1.00 42.62 ?  218 GLU D OE1   1 
ATOM   15136 O  OE2   . GLU D 2 239 ? 124.795 104.228 164.958 1.00 41.24 -1 218 GLU D OE2   1 
ATOM   15137 N  N     . GLU D 2 240 ? 125.899 98.473  167.100 1.00 36.66 ?  219 GLU D N     1 
ATOM   15138 C  CA    . GLU D 2 240 ? 126.710 97.282  167.363 1.00 37.01 ?  219 GLU D CA    1 
ATOM   15139 C  C     . GLU D 2 240 ? 127.062 96.561  166.061 1.00 35.85 ?  219 GLU D C     1 
ATOM   15140 O  O     . GLU D 2 240 ? 128.200 96.116  165.888 1.00 35.62 ?  219 GLU D O     1 
ATOM   15141 C  CB    . GLU D 2 240 ? 126.010 96.320  168.334 1.00 37.98 ?  219 GLU D CB    1 
ATOM   15142 C  CG    . GLU D 2 240 ? 126.877 95.109  168.714 1.00 40.87 ?  219 GLU D CG    1 
ATOM   15143 C  CD    . GLU D 2 240 ? 126.203 94.126  169.669 1.00 44.58 ?  219 GLU D CD    1 
ATOM   15144 O  OE1   . GLU D 2 240 ? 126.944 93.426  170.401 1.00 45.86 ?  219 GLU D OE1   1 
ATOM   15145 O  OE2   . GLU D 2 240 ? 124.950 94.045  169.689 1.00 45.75 -1 219 GLU D OE2   1 
ATOM   15146 N  N     . LYS D 2 241 ? 126.082 96.452  165.165 1.00 34.54 ?  220 LYS D N     1 
ATOM   15147 C  CA    . LYS D 2 241 ? 126.283 95.815  163.861 1.00 33.65 ?  220 LYS D CA    1 
ATOM   15148 C  C     . LYS D 2 241 ? 127.257 96.626  162.998 1.00 32.67 ?  220 LYS D C     1 
ATOM   15149 O  O     . LYS D 2 241 ? 128.079 96.045  162.294 1.00 32.05 ?  220 LYS D O     1 
ATOM   15150 C  CB    . LYS D 2 241 ? 124.948 95.603  163.140 1.00 33.30 ?  220 LYS D CB    1 
ATOM   15151 C  CG    . LYS D 2 241 ? 125.022 94.798  161.828 1.00 34.50 ?  220 LYS D CG    1 
ATOM   15152 C  CD    . LYS D 2 241 ? 125.562 93.376  162.026 1.00 36.30 ?  220 LYS D CD    1 
ATOM   15153 C  CE    . LYS D 2 241 ? 124.565 92.487  162.759 1.00 38.44 ?  220 LYS D CE    1 
ATOM   15154 N  NZ    . LYS D 2 241 ? 125.249 91.344  163.423 1.00 39.28 1  220 LYS D NZ    1 
ATOM   15155 N  N     . LYS D 2 242 ? 127.159 97.958  163.063 1.00 31.90 ?  221 LYS D N     1 
ATOM   15156 C  CA    . LYS D 2 242 ? 128.097 98.844  162.372 1.00 31.28 ?  221 LYS D CA    1 
ATOM   15157 C  C     . LYS D 2 242 ? 129.534 98.605  162.832 1.00 31.32 ?  221 LYS D C     1 
ATOM   15158 O  O     . LYS D 2 242 ? 130.420 98.431  162.004 1.00 30.72 ?  221 LYS D O     1 
ATOM   15159 C  CB    . LYS D 2 242 ? 127.727 100.321 162.571 1.00 31.38 ?  221 LYS D CB    1 
ATOM   15160 C  CG    . LYS D 2 242 ? 126.636 100.837 161.640 1.00 30.64 ?  221 LYS D CG    1 
ATOM   15161 C  CD    . LYS D 2 242 ? 126.356 102.313 161.917 1.00 32.51 ?  221 LYS D CD    1 
ATOM   15162 C  CE    . LYS D 2 242 ? 125.297 102.853 160.982 1.00 32.66 ?  221 LYS D CE    1 
ATOM   15163 N  NZ    . LYS D 2 242 ? 124.857 104.201 161.404 1.00 35.31 1  221 LYS D NZ    1 
ATOM   15164 N  N     . ALA D 2 243 ? 129.755 98.605  164.150 1.00 31.62 ?  222 ALA D N     1 
ATOM   15165 C  CA    . ALA D 2 243 ? 131.080 98.345  164.723 1.00 31.66 ?  222 ALA D CA    1 
ATOM   15166 C  C     . ALA D 2 243 ? 131.648 96.995  164.266 1.00 31.52 ?  222 ALA D C     1 
ATOM   15167 O  O     . ALA D 2 243 ? 132.853 96.859  164.037 1.00 31.41 ?  222 ALA D O     1 
ATOM   15168 C  CB    . ALA D 2 243 ? 131.027 98.425  166.253 1.00 31.89 ?  222 ALA D CB    1 
ATOM   15169 N  N     . GLU D 2 244 ? 130.758 96.018  164.116 1.00 31.35 ?  223 GLU D N     1 
ATOM   15170 C  CA    . GLU D 2 244 ? 131.096 94.677  163.671 1.00 31.54 ?  223 GLU D CA    1 
ATOM   15171 C  C     . GLU D 2 244 ? 131.481 94.651  162.174 1.00 30.63 ?  223 GLU D C     1 
ATOM   15172 O  O     . GLU D 2 244 ? 132.422 93.954  161.767 1.00 29.47 ?  223 GLU D O     1 
ATOM   15173 C  CB    . GLU D 2 244 ? 129.892 93.788  163.940 1.00 32.45 ?  223 GLU D CB    1 
ATOM   15174 C  CG    . GLU D 2 244 ? 130.107 92.309  163.847 1.00 35.31 ?  223 GLU D CG    1 
ATOM   15175 C  CD    . GLU D 2 244 ? 128.938 91.552  164.447 1.00 38.36 ?  223 GLU D CD    1 
ATOM   15176 O  OE1   . GLU D 2 244 ? 128.757 91.613  165.681 1.00 41.93 ?  223 GLU D OE1   1 
ATOM   15177 O  OE2   . GLU D 2 244 ? 128.190 90.904  163.688 1.00 39.37 -1 223 GLU D OE2   1 
ATOM   15178 N  N     . LEU D 2 245 ? 130.752 95.419  161.371 1.00 29.62 ?  224 LEU D N     1 
ATOM   15179 C  CA    . LEU D 2 245 ? 131.065 95.581  159.954 1.00 29.44 ?  224 LEU D CA    1 
ATOM   15180 C  C     . LEU D 2 245 ? 132.360 96.365  159.728 1.00 28.99 ?  224 LEU D C     1 
ATOM   15181 O  O     . LEU D 2 245 ? 133.096 96.070  158.791 1.00 28.63 ?  224 LEU D O     1 
ATOM   15182 C  CB    . LEU D 2 245 ? 129.895 96.238  159.213 1.00 29.06 ?  224 LEU D CB    1 
ATOM   15183 C  CG    . LEU D 2 245 ? 128.614 95.407  159.087 1.00 29.27 ?  224 LEU D CG    1 
ATOM   15184 C  CD1   . LEU D 2 245 ? 127.580 96.188  158.281 1.00 30.76 ?  224 LEU D CD1   1 
ATOM   15185 C  CD2   . LEU D 2 245 ? 128.872 94.052  158.435 1.00 28.11 ?  224 LEU D CD2   1 
ATOM   15186 N  N     . ARG D 2 246 ? 132.629 97.354  160.582 1.00 29.31 ?  225 ARG D N     1 
ATOM   15187 C  CA    . ARG D 2 246 ? 133.900 98.086  160.539 1.00 29.86 ?  225 ARG D CA    1 
ATOM   15188 C  C     . ARG D 2 246 ? 135.073 97.164  160.841 1.00 29.23 ?  225 ARG D C     1 
ATOM   15189 O  O     . ARG D 2 246 ? 136.090 97.214  160.164 1.00 28.95 ?  225 ARG D O     1 
ATOM   15190 C  CB    . ARG D 2 246 ? 133.928 99.253  161.533 1.00 30.56 ?  225 ARG D CB    1 
ATOM   15191 C  CG    . ARG D 2 246 ? 133.145 100.471 161.101 1.00 33.71 ?  225 ARG D CG    1 
ATOM   15192 C  CD    . ARG D 2 246 ? 133.622 101.754 161.808 1.00 37.42 ?  225 ARG D CD    1 
ATOM   15193 N  NE    . ARG D 2 246 ? 133.597 101.662 163.272 1.00 39.17 ?  225 ARG D NE    1 
ATOM   15194 C  CZ    . ARG D 2 246 ? 132.510 101.776 164.035 1.00 40.68 ?  225 ARG D CZ    1 
ATOM   15195 N  NH1   . ARG D 2 246 ? 131.311 101.979 163.495 1.00 40.28 1  225 ARG D NH1   1 
ATOM   15196 N  NH2   . ARG D 2 246 ? 132.622 101.675 165.356 1.00 41.65 ?  225 ARG D NH2   1 
ATOM   15197 N  N     . GLU D 2 247 ? 134.926 96.339  161.870 1.00 28.89 ?  226 GLU D N     1 
ATOM   15198 C  CA    . GLU D 2 247 ? 135.955 95.366  162.222 1.00 29.27 ?  226 GLU D CA    1 
ATOM   15199 C  C     . GLU D 2 247 ? 136.198 94.394  161.068 1.00 27.84 ?  226 GLU D C     1 
ATOM   15200 O  O     . GLU D 2 247 ? 137.354 94.094  160.757 1.00 27.37 ?  226 GLU D O     1 
ATOM   15201 C  CB    . GLU D 2 247 ? 135.598 94.615  163.517 1.00 30.21 ?  226 GLU D CB    1 
ATOM   15202 C  CG    . GLU D 2 247 ? 136.573 93.484  163.900 1.00 34.46 ?  226 GLU D CG    1 
ATOM   15203 C  CD    . GLU D 2 247 ? 138.006 93.970  164.101 1.00 40.77 ?  226 GLU D CD    1 
ATOM   15204 O  OE1   . GLU D 2 247 ? 138.233 94.787  165.025 1.00 44.03 ?  226 GLU D OE1   1 
ATOM   15205 O  OE2   . GLU D 2 247 ? 138.908 93.541  163.338 1.00 42.98 -1 226 GLU D OE2   1 
ATOM   15206 N  N     . PHE D 2 248 ? 135.121 93.923  160.435 1.00 26.73 ?  227 PHE D N     1 
ATOM   15207 C  CA    . PHE D 2 248 ? 135.231 93.074  159.241 1.00 26.15 ?  227 PHE D CA    1 
ATOM   15208 C  C     . PHE D 2 248 ? 136.066 93.744  158.148 1.00 25.33 ?  227 PHE D C     1 
ATOM   15209 O  O     . PHE D 2 248 ? 136.976 93.125  157.601 1.00 24.70 ?  227 PHE D O     1 
ATOM   15210 C  CB    . PHE D 2 248 ? 133.863 92.677  158.653 1.00 26.02 ?  227 PHE D CB    1 
ATOM   15211 C  CG    . PHE D 2 248 ? 133.953 92.130  157.228 1.00 25.61 ?  227 PHE D CG    1 
ATOM   15212 C  CD1   . PHE D 2 248 ? 134.216 90.783  156.999 1.00 26.51 ?  227 PHE D CD1   1 
ATOM   15213 C  CD2   . PHE D 2 248 ? 133.812 92.978  156.126 1.00 26.21 ?  227 PHE D CD2   1 
ATOM   15214 C  CE1   . PHE D 2 248 ? 134.325 90.278  155.703 1.00 26.16 ?  227 PHE D CE1   1 
ATOM   15215 C  CE2   . PHE D 2 248 ? 133.922 92.486  154.818 1.00 26.07 ?  227 PHE D CE2   1 
ATOM   15216 C  CZ    . PHE D 2 248 ? 134.183 91.128  154.611 1.00 25.82 ?  227 PHE D CZ    1 
ATOM   15217 N  N     . ALA D 2 249 ? 135.732 94.996  157.830 1.00 24.83 ?  228 ALA D N     1 
ATOM   15218 C  CA    . ALA D 2 249 ? 136.387 95.743  156.747 1.00 24.08 ?  228 ALA D CA    1 
ATOM   15219 C  C     . ALA D 2 249 ? 137.881 95.966  157.025 1.00 23.93 ?  228 ALA D C     1 
ATOM   15220 O  O     . ALA D 2 249 ? 138.716 95.800  156.133 1.00 22.51 ?  228 ALA D O     1 
ATOM   15221 C  CB    . ALA D 2 249 ? 135.682 97.088  156.538 1.00 24.18 ?  228 ALA D CB    1 
ATOM   15222 N  N     . ILE D 2 250 ? 138.205 96.346  158.261 1.00 24.20 ?  229 ILE D N     1 
ATOM   15223 C  CA    . ILE D 2 250 ? 139.594 96.594  158.652 1.00 24.86 ?  229 ILE D CA    1 
ATOM   15224 C  C     . ILE D 2 250 ? 140.396 95.288  158.678 1.00 24.68 ?  229 ILE D C     1 
ATOM   15225 O  O     . ILE D 2 250 ? 141.531 95.249  158.217 1.00 24.30 ?  229 ILE D O     1 
ATOM   15226 C  CB    . ILE D 2 250 ? 139.696 97.361  160.016 1.00 25.44 ?  229 ILE D CB    1 
ATOM   15227 C  CG1   . ILE D 2 250 ? 138.969 98.719  159.963 1.00 26.49 ?  229 ILE D CG1   1 
ATOM   15228 C  CG2   . ILE D 2 250 ? 141.156 97.547  160.453 1.00 27.13 ?  229 ILE D CG2   1 
ATOM   15229 C  CD1   . ILE D 2 250 ? 139.380 99.648  158.818 1.00 28.58 ?  229 ILE D CD1   1 
ATOM   15230 N  N     . ASP D 2 251 ? 139.798 94.223  159.213 1.00 24.90 ?  230 ASP D N     1 
ATOM   15231 C  CA    . ASP D 2 251 ? 140.432 92.909  159.248 1.00 25.04 ?  230 ASP D CA    1 
ATOM   15232 C  C     . ASP D 2 251 ? 140.730 92.406  157.823 1.00 24.25 ?  230 ASP D C     1 
ATOM   15233 O  O     . ASP D 2 251 ? 141.835 91.937  157.543 1.00 23.60 ?  230 ASP D O     1 
ATOM   15234 C  CB    . ASP D 2 251 ? 139.538 91.920  160.003 1.00 26.23 ?  230 ASP D CB    1 
ATOM   15235 C  CG    . ASP D 2 251 ? 140.065 90.502  159.970 1.00 28.91 ?  230 ASP D CG    1 
ATOM   15236 O  OD1   . ASP D 2 251 ? 141.117 90.226  160.584 1.00 32.03 ?  230 ASP D OD1   1 
ATOM   15237 O  OD2   . ASP D 2 251 ? 139.404 89.650  159.344 1.00 33.16 -1 230 ASP D OD2   1 
ATOM   15238 N  N     . LEU D 2 252 ? 139.739 92.501  156.941 1.00 23.43 ?  231 LEU D N     1 
ATOM   15239 C  CA    . LEU D 2 252 ? 139.925 92.137  155.539 1.00 22.79 ?  231 LEU D CA    1 
ATOM   15240 C  C     . LEU D 2 252 ? 141.029 92.978  154.891 1.00 22.71 ?  231 LEU D C     1 
ATOM   15241 O  O     . LEU D 2 252 ? 141.894 92.443  154.187 1.00 21.58 ?  231 LEU D O     1 
ATOM   15242 C  CB    . LEU D 2 252 ? 138.620 92.289  154.750 1.00 22.48 ?  231 LEU D CB    1 
ATOM   15243 C  CG    . LEU D 2 252 ? 138.699 91.926  153.255 1.00 21.05 ?  231 LEU D CG    1 
ATOM   15244 C  CD1   . LEU D 2 252 ? 139.175 90.473  153.039 1.00 22.94 ?  231 LEU D CD1   1 
ATOM   15245 C  CD2   . LEU D 2 252 ? 137.356 92.139  152.570 1.00 19.31 ?  231 LEU D CD2   1 
ATOM   15246 N  N     . LEU D 2 253 ? 140.990 94.290  155.126 1.00 22.90 ?  232 LEU D N     1 
ATOM   15247 C  CA    . LEU D 2 253 ? 142.013 95.186  154.567 1.00 23.78 ?  232 LEU D CA    1 
ATOM   15248 C  C     . LEU D 2 253 ? 143.418 94.761  155.011 1.00 23.75 ?  232 LEU D C     1 
ATOM   15249 O  O     . LEU D 2 253 ? 144.338 94.700  154.194 1.00 23.26 ?  232 LEU D O     1 
ATOM   15250 C  CB    . LEU D 2 253 ? 141.767 96.640  154.975 1.00 24.03 ?  232 LEU D CB    1 
ATOM   15251 C  CG    . LEU D 2 253 ? 142.915 97.605  154.630 1.00 26.46 ?  232 LEU D CG    1 
ATOM   15252 C  CD1   . LEU D 2 253 ? 142.963 97.844  153.139 1.00 26.52 ?  232 LEU D CD1   1 
ATOM   15253 C  CD2   . LEU D 2 253 ? 142.785 98.937  155.374 1.00 27.50 ?  232 LEU D CD2   1 
ATOM   15254 N  N     . ASN D 2 254 ? 143.569 94.497  156.310 1.00 24.63 ?  233 ASN D N     1 
ATOM   15255 C  CA    . ASN D 2 254 ? 144.836 94.017  156.868 1.00 25.49 ?  233 ASN D CA    1 
ATOM   15256 C  C     . ASN D 2 254 ? 145.361 92.737  156.201 1.00 24.94 ?  233 ASN D C     1 
ATOM   15257 O  O     . ASN D 2 254 ? 146.552 92.653  155.891 1.00 24.64 ?  233 ASN D O     1 
ATOM   15258 C  CB    . ASN D 2 254 ? 144.717 93.793  158.374 1.00 26.98 ?  233 ASN D CB    1 
ATOM   15259 C  CG    . ASN D 2 254 ? 144.972 95.053  159.170 1.00 29.94 ?  233 ASN D CG    1 
ATOM   15260 O  OD1   . ASN D 2 254 ? 145.871 95.842  158.850 1.00 34.55 ?  233 ASN D OD1   1 
ATOM   15261 N  ND2   . ASN D 2 254 ? 144.192 95.247  160.225 1.00 33.81 ?  233 ASN D ND2   1 
ATOM   15262 N  N     . GLN D 2 255 ? 144.482 91.755  155.997 1.00 24.08 ?  234 GLN D N     1 
ATOM   15263 C  CA    . GLN D 2 255 ? 144.883 90.498  155.359 1.00 24.35 ?  234 GLN D CA    1 
ATOM   15264 C  C     . GLN D 2 255 ? 145.369 90.762  153.946 1.00 23.26 ?  234 GLN D C     1 
ATOM   15265 O  O     . GLN D 2 255 ? 146.434 90.271  153.558 1.00 23.12 ?  234 GLN D O     1 
ATOM   15266 C  CB    . GLN D 2 255 ? 143.733 89.484  155.298 1.00 24.84 ?  234 GLN D CB    1 
ATOM   15267 C  CG    . GLN D 2 255 ? 143.343 88.846  156.612 1.00 27.45 ?  234 GLN D CG    1 
ATOM   15268 C  CD    . GLN D 2 255 ? 144.503 88.157  157.309 1.00 32.02 ?  234 GLN D CD    1 
ATOM   15269 O  OE1   . GLN D 2 255 ? 144.872 88.536  158.419 1.00 35.80 ?  234 GLN D OE1   1 
ATOM   15270 N  NE2   . GLN D 2 255 ? 145.082 87.141  156.666 1.00 32.12 ?  234 GLN D NE2   1 
ATOM   15271 N  N     . LEU D 2 256 ? 144.589 91.538  153.192 1.00 21.77 ?  235 LEU D N     1 
ATOM   15272 C  CA    . LEU D 2 256 ? 144.930 91.862  151.805 1.00 21.68 ?  235 LEU D CA    1 
ATOM   15273 C  C     . LEU D 2 256 ? 146.204 92.698  151.736 1.00 21.49 ?  235 LEU D C     1 
ATOM   15274 O  O     . LEU D 2 256 ? 147.048 92.471  150.876 1.00 20.89 ?  235 LEU D O     1 
ATOM   15275 C  CB    . LEU D 2 256 ? 143.781 92.600  151.092 1.00 20.49 ?  235 LEU D CB    1 
ATOM   15276 C  CG    . LEU D 2 256 ? 142.503 91.792  150.822 1.00 21.52 ?  235 LEU D CG    1 
ATOM   15277 C  CD1   . LEU D 2 256 ? 141.358 92.686  150.317 1.00 20.71 ?  235 LEU D CD1   1 
ATOM   15278 C  CD2   . LEU D 2 256 ? 142.751 90.659  149.836 1.00 20.74 ?  235 LEU D CD2   1 
ATOM   15279 N  N     . TYR D 2 257 ? 146.333 93.658  152.650 1.00 21.42 ?  236 TYR D N     1 
ATOM   15280 C  CA    . TYR D 2 257 ? 147.510 94.525  152.668 1.00 22.02 ?  236 TYR D CA    1 
ATOM   15281 C  C     . TYR D 2 257 ? 148.804 93.753  152.927 1.00 22.61 ?  236 TYR D C     1 
ATOM   15282 O  O     . TYR D 2 257 ? 149.814 93.987  152.262 1.00 22.19 ?  236 TYR D O     1 
ATOM   15283 C  CB    . TYR D 2 257 ? 147.343 95.659  153.676 1.00 22.06 ?  236 TYR D CB    1 
ATOM   15284 C  CG    . TYR D 2 257 ? 148.585 96.500  153.863 1.00 23.44 ?  236 TYR D CG    1 
ATOM   15285 C  CD1   . TYR D 2 257 ? 149.071 97.310  152.829 1.00 24.01 ?  236 TYR D CD1   1 
ATOM   15286 C  CD2   . TYR D 2 257 ? 149.268 96.495  155.077 1.00 25.22 ?  236 TYR D CD2   1 
ATOM   15287 C  CE1   . TYR D 2 257 ? 150.213 98.089  153.006 1.00 25.14 ?  236 TYR D CE1   1 
ATOM   15288 C  CE2   . TYR D 2 257 ? 150.416 97.261  155.261 1.00 26.71 ?  236 TYR D CE2   1 
ATOM   15289 C  CZ    . TYR D 2 257 ? 150.877 98.056  154.226 1.00 25.35 ?  236 TYR D CZ    1 
ATOM   15290 O  OH    . TYR D 2 257 ? 152.001 98.815  154.424 1.00 26.77 ?  236 TYR D OH    1 
ATOM   15291 N  N     . GLU D 2 258 ? 148.775 92.825  153.881 1.00 23.09 ?  237 GLU D N     1 
ATOM   15292 C  CA    . GLU D 2 258 ? 149.983 92.059  154.193 1.00 23.98 ?  237 GLU D CA    1 
ATOM   15293 C  C     . GLU D 2 258 ? 150.402 91.168  153.024 1.00 23.13 ?  237 GLU D C     1 
ATOM   15294 O  O     . GLU D 2 258 ? 151.589 91.038  152.739 1.00 23.02 ?  237 GLU D O     1 
ATOM   15295 C  CB    . GLU D 2 258 ? 149.826 91.264  155.498 1.00 25.20 ?  237 GLU D CB    1 
ATOM   15296 C  CG    . GLU D 2 258 ? 149.691 92.152  156.746 1.00 28.82 ?  237 GLU D CG    1 
ATOM   15297 C  CD    . GLU D 2 258 ? 150.979 92.889  157.139 1.00 34.48 ?  237 GLU D CD    1 
ATOM   15298 O  OE1   . GLU D 2 258 ? 152.098 92.384  156.863 1.00 37.75 ?  237 GLU D OE1   1 
ATOM   15299 O  OE2   . GLU D 2 258 ? 150.873 93.984  157.745 1.00 37.16 -1 237 GLU D OE2   1 
ATOM   15300 N  N     . ASN D 2 259 ? 149.427 90.591  152.334 1.00 22.12 ?  238 ASN D N     1 
ATOM   15301 C  CA    . ASN D 2 259 ? 149.691 89.849  151.101 1.00 22.35 ?  238 ASN D CA    1 
ATOM   15302 C  C     . ASN D 2 259 ? 150.184 90.747  149.934 1.00 22.11 ?  238 ASN D C     1 
ATOM   15303 O  O     . ASN D 2 259 ? 151.039 90.325  149.150 1.00 22.24 ?  238 ASN D O     1 
ATOM   15304 C  CB    . ASN D 2 259 ? 148.457 89.037  150.690 1.00 21.69 ?  238 ASN D CB    1 
ATOM   15305 C  CG    . ASN D 2 259 ? 148.694 88.208  149.440 1.00 23.38 ?  238 ASN D CG    1 
ATOM   15306 O  OD1   . ASN D 2 259 ? 149.410 87.196  149.470 1.00 23.95 ?  238 ASN D OD1   1 
ATOM   15307 N  ND2   . ASN D 2 259 ? 148.106 88.638  148.332 1.00 21.14 ?  238 ASN D ND2   1 
ATOM   15308 N  N     . GLU D 2 260 ? 149.650 91.969  149.830 1.00 21.95 ?  239 GLU D N     1 
ATOM   15309 C  CA    . GLU D 2 260 ? 150.116 92.952  148.830 1.00 22.50 ?  239 GLU D CA    1 
ATOM   15310 C  C     . GLU D 2 260 ? 151.592 93.306  149.009 1.00 22.03 ?  239 GLU D C     1 
ATOM   15311 O  O     . GLU D 2 260 ? 152.305 93.516  148.032 1.00 22.03 ?  239 GLU D O     1 
ATOM   15312 C  CB    . GLU D 2 260 ? 149.314 94.265  148.890 1.00 22.90 ?  239 GLU D CB    1 
ATOM   15313 C  CG    . GLU D 2 260 ? 147.981 94.283  148.123 1.00 25.84 ?  239 GLU D CG    1 
ATOM   15314 C  CD    . GLU D 2 260 ? 148.080 93.750  146.697 1.00 28.59 ?  239 GLU D CD    1 
ATOM   15315 O  OE1   . GLU D 2 260 ? 148.084 92.514  146.526 1.00 28.18 ?  239 GLU D OE1   1 
ATOM   15316 O  OE2   . GLU D 2 260 ? 148.111 94.566  145.746 1.00 30.32 -1 239 GLU D OE2   1 
ATOM   15317 N  N     . LEU D 2 261 ? 152.034 93.408  150.258 1.00 21.50 ?  240 LEU D N     1 
ATOM   15318 C  CA    . LEU D 2 261 ? 153.434 93.713  150.534 1.00 22.03 ?  240 LEU D CA    1 
ATOM   15319 C  C     . LEU D 2 261 ? 154.320 92.601  150.000 1.00 21.52 ?  240 LEU D C     1 
ATOM   15320 O  O     . LEU D 2 261 ? 155.342 92.875  149.370 1.00 21.44 ?  240 LEU D O     1 
ATOM   15321 C  CB    . LEU D 2 261 ? 153.686 93.924  152.024 1.00 21.57 ?  240 LEU D CB    1 
ATOM   15322 C  CG    . LEU D 2 261 ? 152.948 95.067  152.722 1.00 23.22 ?  240 LEU D CG    1 
ATOM   15323 C  CD1   . LEU D 2 261 ? 153.319 95.070  154.193 1.00 23.06 ?  240 LEU D CD1   1 
ATOM   15324 C  CD2   . LEU D 2 261 ? 153.274 96.414  152.077 1.00 23.52 ?  240 LEU D CD2   1 
ATOM   15325 N  N     . GLU D 2 262 ? 153.909 91.354  150.233 1.00 21.69 ?  241 GLU D N     1 
ATOM   15326 C  CA    . GLU D 2 262 ? 154.647 90.191  149.714 1.00 22.31 ?  241 GLU D CA    1 
ATOM   15327 C  C     . GLU D 2 262 ? 154.584 90.115  148.187 1.00 21.69 ?  241 GLU D C     1 
ATOM   15328 O  O     . GLU D 2 262 ? 155.591 89.845  147.527 1.00 21.75 ?  241 GLU D O     1 
ATOM   15329 C  CB    . GLU D 2 262 ? 154.114 88.886  150.314 1.00 22.46 ?  241 GLU D CB    1 
ATOM   15330 C  CG    . GLU D 2 262 ? 154.234 88.755  151.834 1.00 25.63 ?  241 GLU D CG    1 
ATOM   15331 C  CD    . GLU D 2 262 ? 153.767 87.385  152.307 1.00 29.83 ?  241 GLU D CD    1 
ATOM   15332 O  OE1   . GLU D 2 262 ? 152.541 87.170  152.412 1.00 33.22 ?  241 GLU D OE1   1 
ATOM   15333 O  OE2   . GLU D 2 262 ? 154.619 86.511  152.545 1.00 33.36 -1 241 GLU D OE2   1 
ATOM   15334 N  N     . TYR D 2 263 ? 153.393 90.332  147.632 1.00 21.42 ?  242 TYR D N     1 
ATOM   15335 C  CA    . TYR D 2 263 ? 153.189 90.379  146.179 1.00 21.04 ?  242 TYR D CA    1 
ATOM   15336 C  C     . TYR D 2 263 ? 154.119 91.425  145.550 1.00 21.15 ?  242 TYR D C     1 
ATOM   15337 O  O     . TYR D 2 263 ? 154.723 91.191  144.503 1.00 20.32 ?  242 TYR D O     1 
ATOM   15338 C  CB    . TYR D 2 263 ? 151.722 90.727  145.881 1.00 20.95 ?  242 TYR D CB    1 
ATOM   15339 C  CG    . TYR D 2 263 ? 151.373 90.912  144.415 1.00 21.86 ?  242 TYR D CG    1 
ATOM   15340 C  CD1   . TYR D 2 263 ? 151.142 89.810  143.591 1.00 23.53 ?  242 TYR D CD1   1 
ATOM   15341 C  CD2   . TYR D 2 263 ? 151.274 92.188  143.852 1.00 21.20 ?  242 TYR D CD2   1 
ATOM   15342 C  CE1   . TYR D 2 263 ? 150.820 89.972  142.252 1.00 23.34 ?  242 TYR D CE1   1 
ATOM   15343 C  CE2   . TYR D 2 263 ? 150.952 92.358  142.509 1.00 23.11 ?  242 TYR D CE2   1 
ATOM   15344 C  CZ    . TYR D 2 263 ? 150.733 91.244  141.716 1.00 23.27 ?  242 TYR D CZ    1 
ATOM   15345 O  OH    . TYR D 2 263 ? 150.413 91.408  140.385 1.00 27.07 ?  242 TYR D OH    1 
ATOM   15346 N  N     . THR D 2 264 ? 154.201 92.581  146.206 1.00 21.12 ?  243 THR D N     1 
ATOM   15347 C  CA    . THR D 2 264 ? 154.986 93.717  145.733 1.00 21.98 ?  243 THR D CA    1 
ATOM   15348 C  C     . THR D 2 264 ? 156.477 93.388  145.691 1.00 22.32 ?  243 THR D C     1 
ATOM   15349 O  O     . THR D 2 264 ? 157.120 93.582  144.661 1.00 21.78 ?  243 THR D O     1 
ATOM   15350 C  CB    . THR D 2 264 ? 154.707 94.974  146.587 1.00 21.68 ?  243 THR D CB    1 
ATOM   15351 O  OG1   . THR D 2 264 ? 153.349 95.376  146.389 1.00 23.29 ?  243 THR D OG1   1 
ATOM   15352 C  CG2   . THR D 2 264 ? 155.645 96.143  146.225 1.00 23.16 ?  243 THR D CG2   1 
ATOM   15353 N  N     . GLU D 2 265 ? 157.014 92.871  146.795 1.00 22.48 ?  244 GLU D N     1 
ATOM   15354 C  CA    . GLU D 2 265 ? 158.431 92.500  146.827 1.00 23.73 ?  244 GLU D CA    1 
ATOM   15355 C  C     . GLU D 2 265 ? 158.752 91.436  145.788 1.00 23.85 ?  244 GLU D C     1 
ATOM   15356 O  O     . GLU D 2 265 ? 159.780 91.517  145.127 1.00 24.40 ?  244 GLU D O     1 
ATOM   15357 C  CB    . GLU D 2 265 ? 158.845 92.029  148.213 1.00 23.19 ?  244 GLU D CB    1 
ATOM   15358 C  CG    . GLU D 2 265 ? 158.947 93.172  149.188 1.00 25.08 ?  244 GLU D CG    1 
ATOM   15359 C  CD    . GLU D 2 265 ? 159.186 92.717  150.612 1.00 27.30 ?  244 GLU D CD    1 
ATOM   15360 O  OE1   . GLU D 2 265 ? 159.479 91.526  150.831 1.00 27.77 ?  244 GLU D OE1   1 
ATOM   15361 O  OE2   . GLU D 2 265 ? 159.081 93.567  151.516 1.00 28.63 -1 244 GLU D OE2   1 
ATOM   15362 N  N     . ASP D 2 266 ? 157.847 90.470  145.632 1.00 24.13 ?  245 ASP D N     1 
ATOM   15363 C  CA    . ASP D 2 266 ? 158.007 89.369  144.677 1.00 25.22 ?  245 ASP D CA    1 
ATOM   15364 C  C     . ASP D 2 266 ? 158.177 89.862  143.223 1.00 24.84 ?  245 ASP D C     1 
ATOM   15365 O  O     . ASP D 2 266 ? 158.950 89.282  142.454 1.00 25.64 ?  245 ASP D O     1 
ATOM   15366 C  CB    . ASP D 2 266 ? 156.810 88.413  144.800 1.00 25.79 ?  245 ASP D CB    1 
ATOM   15367 C  CG    . ASP D 2 266 ? 156.952 87.162  143.944 1.00 27.71 ?  245 ASP D CG    1 
ATOM   15368 O  OD1   . ASP D 2 266 ? 157.957 86.450  144.094 1.00 31.57 ?  245 ASP D OD1   1 
ATOM   15369 O  OD2   . ASP D 2 266 ? 156.044 86.872  143.136 1.00 30.29 -1 245 ASP D OD2   1 
ATOM   15370 N  N     . LEU D 2 267 ? 157.476 90.933  142.863 1.00 24.07 ?  246 LEU D N     1 
ATOM   15371 C  CA    . LEU D 2 267 ? 157.495 91.460  141.496 1.00 23.98 ?  246 LEU D CA    1 
ATOM   15372 C  C     . LEU D 2 267 ? 158.471 92.615  141.270 1.00 22.83 ?  246 LEU D C     1 
ATOM   15373 O  O     . LEU D 2 267 ? 159.107 92.690  140.211 1.00 23.00 ?  246 LEU D O     1 
ATOM   15374 C  CB    . LEU D 2 267 ? 156.088 91.917  141.071 1.00 23.82 ?  246 LEU D CB    1 
ATOM   15375 C  CG    . LEU D 2 267 ? 155.042 90.815  140.858 1.00 26.05 ?  246 LEU D CG    1 
ATOM   15376 C  CD1   . LEU D 2 267 ? 153.811 91.373  140.198 1.00 26.74 ?  246 LEU D CD1   1 
ATOM   15377 C  CD2   . LEU D 2 267 ? 155.592 89.670  140.028 1.00 28.00 ?  246 LEU D CD2   1 
ATOM   15378 N  N     . TYR D 2 268 ? 158.579 93.504  142.258 1.00 21.68 ?  247 TYR D N     1 
ATOM   15379 C  CA    . TYR D 2 268 ? 159.268 94.785  142.074 1.00 20.95 ?  247 TYR D CA    1 
ATOM   15380 C  C     . TYR D 2 268 ? 160.691 94.899  142.637 1.00 21.43 ?  247 TYR D C     1 
ATOM   15381 O  O     . TYR D 2 268 ? 161.412 95.822  142.261 1.00 20.73 ?  247 TYR D O     1 
ATOM   15382 C  CB    . TYR D 2 268 ? 158.421 95.940  142.618 1.00 20.27 ?  247 TYR D CB    1 
ATOM   15383 C  CG    . TYR D 2 268 ? 157.182 96.256  141.800 1.00 19.54 ?  247 TYR D CG    1 
ATOM   15384 C  CD1   . TYR D 2 268 ? 155.926 95.824  142.210 1.00 18.52 ?  247 TYR D CD1   1 
ATOM   15385 C  CD2   . TYR D 2 268 ? 157.276 96.988  140.606 1.00 20.62 ?  247 TYR D CD2   1 
ATOM   15386 C  CE1   . TYR D 2 268 ? 154.761 96.127  141.457 1.00 18.33 ?  247 TYR D CE1   1 
ATOM   15387 C  CE2   . TYR D 2 268 ? 156.125 97.295  139.845 1.00 20.79 ?  247 TYR D CE2   1 
ATOM   15388 C  CZ    . TYR D 2 268 ? 154.880 96.867  140.285 1.00 20.23 ?  247 TYR D CZ    1 
ATOM   15389 O  OH    . TYR D 2 268 ? 153.763 97.172  139.532 1.00 20.50 ?  247 TYR D OH    1 
ATOM   15390 N  N     . ASP D 2 269 ? 161.096 93.997  143.539 1.00 21.65 ?  248 ASP D N     1 
ATOM   15391 C  CA    . ASP D 2 269 ? 162.490 94.016  143.997 1.00 22.30 ?  248 ASP D CA    1 
ATOM   15392 C  C     . ASP D 2 269 ? 163.502 93.914  142.831 1.00 22.54 ?  248 ASP D C     1 
ATOM   15393 O  O     . ASP D 2 269 ? 164.542 94.578  142.857 1.00 22.49 ?  248 ASP D O     1 
ATOM   15394 C  CB    . ASP D 2 269 ? 162.762 92.932  145.042 1.00 22.83 ?  248 ASP D CB    1 
ATOM   15395 C  CG    . ASP D 2 269 ? 162.317 93.339  146.443 1.00 23.55 ?  248 ASP D CG    1 
ATOM   15396 O  OD1   . ASP D 2 269 ? 161.939 94.511  146.643 1.00 24.95 ?  248 ASP D OD1   1 
ATOM   15397 O  OD2   . ASP D 2 269 ? 162.345 92.478  147.351 1.00 24.47 -1 248 ASP D OD2   1 
ATOM   15398 N  N     . GLN D 2 270 ? 163.194 93.099  141.820 1.00 22.79 ?  249 GLN D N     1 
ATOM   15399 C  CA    . GLN D 2 270 ? 164.104 92.901  140.685 1.00 23.41 ?  249 GLN D CA    1 
ATOM   15400 C  C     . GLN D 2 270 ? 164.286 94.149  139.816 1.00 22.83 ?  249 GLN D C     1 
ATOM   15401 O  O     . GLN D 2 270 ? 165.222 94.215  139.022 1.00 23.75 ?  249 GLN D O     1 
ATOM   15402 C  CB    . GLN D 2 270 ? 163.682 91.708  139.821 1.00 24.02 ?  249 GLN D CB    1 
ATOM   15403 C  CG    . GLN D 2 270 ? 162.387 91.916  139.015 1.00 25.40 ?  249 GLN D CG    1 
ATOM   15404 C  CD    . GLN D 2 270 ? 161.848 90.622  138.431 1.00 29.23 ?  249 GLN D CD    1 
ATOM   15405 O  OE1   . GLN D 2 270 ? 162.020 89.548  139.010 1.00 31.31 ?  249 GLN D OE1   1 
ATOM   15406 N  NE2   . GLN D 2 270 ? 161.180 90.718  137.283 1.00 30.04 ?  249 GLN D NE2   1 
ATOM   15407 N  N     . VAL D 2 271 ? 163.386 95.122  139.954 1.00 21.93 ?  250 VAL D N     1 
ATOM   15408 C  CA    . VAL D 2 271 ? 163.525 96.403  139.254 1.00 21.29 ?  250 VAL D CA    1 
ATOM   15409 C  C     . VAL D 2 271 ? 163.668 97.589  140.226 1.00 21.16 ?  250 VAL D C     1 
ATOM   15410 O  O     . VAL D 2 271 ? 163.578 98.750  139.818 1.00 21.54 ?  250 VAL D O     1 
ATOM   15411 C  CB    . VAL D 2 271 ? 162.362 96.626  138.233 1.00 21.62 ?  250 VAL D CB    1 
ATOM   15412 C  CG1   . VAL D 2 271 ? 162.419 95.578  137.123 1.00 21.36 ?  250 VAL D CG1   1 
ATOM   15413 C  CG2   . VAL D 2 271 ? 160.990 96.609  138.931 1.00 21.17 ?  250 VAL D CG2   1 
ATOM   15414 N  N     . GLY D 2 272 ? 163.868 97.284  141.514 1.00 20.92 ?  251 GLY D N     1 
ATOM   15415 C  CA    . GLY D 2 272 ? 164.208 98.286  142.544 1.00 20.61 ?  251 GLY D CA    1 
ATOM   15416 C  C     . GLY D 2 272 ? 163.138 99.299  142.945 1.00 20.77 ?  251 GLY D C     1 
ATOM   15417 O  O     . GLY D 2 272 ? 163.460 100.399 143.420 1.00 20.28 ?  251 GLY D O     1 
ATOM   15418 N  N     . LEU D 2 273 ? 161.869 98.932  142.784 1.00 19.85 ?  252 LEU D N     1 
ATOM   15419 C  CA    . LEU D 2 273 ? 160.789 99.904  142.959 1.00 20.09 ?  252 LEU D CA    1 
ATOM   15420 C  C     . LEU D 2 273 ? 159.880 99.698  144.174 1.00 19.88 ?  252 LEU D C     1 
ATOM   15421 O  O     . LEU D 2 273 ? 159.015 100.530 144.428 1.00 20.04 ?  252 LEU D O     1 
ATOM   15422 C  CB    . LEU D 2 273 ? 159.918 99.933  141.692 1.00 19.97 ?  252 LEU D CB    1 
ATOM   15423 C  CG    . LEU D 2 273 ? 160.612 100.292 140.386 1.00 20.26 ?  252 LEU D CG    1 
ATOM   15424 C  CD1   . LEU D 2 273 ? 159.559 100.367 139.303 1.00 18.98 ?  252 LEU D CD1   1 
ATOM   15425 C  CD2   . LEU D 2 273 ? 161.397 101.630 140.490 1.00 21.03 ?  252 LEU D CD2   1 
ATOM   15426 N  N     . SER D 2 274 ? 160.090 98.609  144.916 0.50 19.54 ?  253 SER D N     1 
ATOM   15427 C  CA    . SER D 2 274 ? 159.132 98.156  145.936 0.50 19.34 ?  253 SER D CA    1 
ATOM   15428 C  C     . SER D 2 274 ? 158.761 99.201  146.994 0.50 20.05 ?  253 SER D C     1 
ATOM   15429 O  O     . SER D 2 274 ? 157.592 99.315  147.362 0.50 20.31 ?  253 SER D O     1 
ATOM   15430 C  CB    . SER D 2 274 ? 159.609 96.859  146.604 0.50 18.97 ?  253 SER D CB    1 
ATOM   15431 O  OG    . SER D 2 274 ? 159.847 95.843  145.648 0.50 15.35 ?  253 SER D OG    1 
ATOM   15432 N  N     . HIS D 2 275 ? 159.749 99.947  147.485 1.00 20.77 ?  254 HIS D N     1 
ATOM   15433 C  CA    . HIS D 2 275 ? 159.502 101.020 148.470 1.00 21.18 ?  254 HIS D CA    1 
ATOM   15434 C  C     . HIS D 2 275 ? 158.420 102.006 147.996 1.00 21.50 ?  254 HIS D C     1 
ATOM   15435 O  O     . HIS D 2 275 ? 157.463 102.297 148.732 1.00 19.88 ?  254 HIS D O     1 
ATOM   15436 C  CB    . HIS D 2 275 ? 160.794 101.774 148.825 1.00 21.60 ?  254 HIS D CB    1 
ATOM   15437 C  CG    . HIS D 2 275 ? 160.570 102.953 149.723 1.00 22.43 ?  254 HIS D CG    1 
ATOM   15438 N  ND1   . HIS D 2 275 ? 160.571 102.856 151.100 1.00 22.77 ?  254 HIS D ND1   1 
ATOM   15439 C  CD2   . HIS D 2 275 ? 160.320 104.255 149.436 1.00 22.50 ?  254 HIS D CD2   1 
ATOM   15440 C  CE1   . HIS D 2 275 ? 160.337 104.050 151.620 1.00 24.05 ?  254 HIS D CE1   1 
ATOM   15441 N  NE2   . HIS D 2 275 ? 160.175 104.914 150.632 1.00 23.22 ?  254 HIS D NE2   1 
ATOM   15442 N  N     . ASP D 2 276 ? 158.572 102.496 146.765 1.00 22.34 ?  255 ASP D N     1 
ATOM   15443 C  CA    . ASP D 2 276 ? 157.622 103.452 146.201 1.00 23.19 ?  255 ASP D CA    1 
ATOM   15444 C  C     . ASP D 2 276 ? 156.274 102.819 145.886 1.00 22.17 ?  255 ASP D C     1 
ATOM   15445 O  O     . ASP D 2 276 ? 155.250 103.474 146.021 1.00 21.87 ?  255 ASP D O     1 
ATOM   15446 C  CB    . ASP D 2 276 ? 158.181 104.124 144.936 1.00 24.33 ?  255 ASP D CB    1 
ATOM   15447 C  CG    . ASP D 2 276 ? 159.011 105.374 145.238 1.00 27.58 ?  255 ASP D CG    1 
ATOM   15448 O  OD1   . ASP D 2 276 ? 158.818 106.007 146.300 1.00 31.10 ?  255 ASP D OD1   1 
ATOM   15449 O  OD2   . ASP D 2 276 ? 159.870 105.721 144.396 1.00 29.88 -1 255 ASP D OD2   1 
ATOM   15450 N  N     . VAL D 2 277 ? 156.277 101.565 145.434 1.00 21.21 ?  256 VAL D N     1 
ATOM   15451 C  CA    . VAL D 2 277 ? 155.021 100.852 145.180 1.00 20.51 ?  256 VAL D CA    1 
ATOM   15452 C  C     . VAL D 2 277 ? 154.205 100.692 146.468 1.00 20.32 ?  256 VAL D C     1 
ATOM   15453 O  O     . VAL D 2 277 ? 152.988 100.860 146.454 1.00 19.81 ?  256 VAL D O     1 
ATOM   15454 C  CB    . VAL D 2 277 ? 155.245 99.468  144.507 1.00 20.30 ?  256 VAL D CB    1 
ATOM   15455 C  CG1   . VAL D 2 277 ? 153.925 98.738  144.332 1.00 21.16 ?  256 VAL D CG1   1 
ATOM   15456 C  CG2   . VAL D 2 277 ? 155.923 99.639  143.158 1.00 19.06 ?  256 VAL D CG2   1 
ATOM   15457 N  N     . LYS D 2 278 ? 154.889 100.389 147.571 1.00 19.84 ?  257 LYS D N     1 
ATOM   15458 C  CA    . LYS D 2 278 ? 154.240 100.263 148.876 1.00 20.27 ?  257 LYS D CA    1 
ATOM   15459 C  C     . LYS D 2 278 ? 153.527 101.551 149.307 1.00 20.16 ?  257 LYS D C     1 
ATOM   15460 O  O     . LYS D 2 278 ? 152.413 101.485 149.821 1.00 19.88 ?  257 LYS D O     1 
ATOM   15461 C  CB    . LYS D 2 278 ? 155.226 99.785  149.946 1.00 20.20 ?  257 LYS D CB    1 
ATOM   15462 C  CG    . LYS D 2 278 ? 155.592 98.311  149.806 1.00 21.60 ?  257 LYS D CG    1 
ATOM   15463 C  CD    . LYS D 2 278 ? 156.769 97.932  150.698 1.00 21.53 ?  257 LYS D CD    1 
ATOM   15464 C  CE    . LYS D 2 278 ? 157.201 96.516  150.403 1.00 24.52 ?  257 LYS D CE    1 
ATOM   15465 N  NZ    . LYS D 2 278 ? 158.335 96.110  151.296 1.00 26.32 1  257 LYS D NZ    1 
ATOM   15466 N  N     . LYS D 2 279 ? 154.155 102.709 149.073 1.00 19.67 ?  258 LYS D N     1 
ATOM   15467 C  CA    . LYS D 2 279 ? 153.503 103.998 149.346 1.00 20.10 ?  258 LYS D CA    1 
ATOM   15468 C  C     . LYS D 2 279 ? 152.214 104.151 148.529 1.00 19.12 ?  258 LYS D C     1 
ATOM   15469 O  O     . LYS D 2 279 ? 151.206 104.637 149.047 1.00 18.59 ?  258 LYS D O     1 
ATOM   15470 C  CB    . LYS D 2 279 ? 154.444 105.189 149.078 1.00 20.54 ?  258 LYS D CB    1 
ATOM   15471 C  CG    . LYS D 2 279 ? 155.708 105.215 149.935 1.00 22.84 ?  258 LYS D CG    1 
ATOM   15472 C  CD    . LYS D 2 279 ? 156.304 106.637 150.063 1.00 24.16 ?  258 LYS D CD    1 
ATOM   15473 C  CE    . LYS D 2 279 ? 156.834 107.175 148.738 1.00 25.61 ?  258 LYS D CE    1 
ATOM   15474 N  NZ    . LYS D 2 279 ? 157.421 108.565 148.874 1.00 24.70 1  258 LYS D NZ    1 
ATOM   15475 N  N     . PHE D 2 280 ? 152.259 103.712 147.268 1.00 19.04 ?  259 PHE D N     1 
ATOM   15476 C  CA    . PHE D 2 280 ? 151.116 103.783 146.338 1.00 19.31 ?  259 PHE D CA    1 
ATOM   15477 C  C     . PHE D 2 280 ? 149.960 102.861 146.741 1.00 19.25 ?  259 PHE D C     1 
ATOM   15478 O  O     . PHE D 2 280 ? 148.784 103.225 146.614 1.00 19.71 ?  259 PHE D O     1 
ATOM   15479 C  CB    . PHE D 2 280 ? 151.579 103.441 144.922 1.00 19.04 ?  259 PHE D CB    1 
ATOM   15480 C  CG    . PHE D 2 280 ? 150.614 103.850 143.825 1.00 20.15 ?  259 PHE D CG    1 
ATOM   15481 C  CD1   . PHE D 2 280 ? 150.188 105.164 143.700 1.00 21.63 ?  259 PHE D CD1   1 
ATOM   15482 C  CD2   . PHE D 2 280 ? 150.181 102.911 142.887 1.00 19.95 ?  259 PHE D CD2   1 
ATOM   15483 C  CE1   . PHE D 2 280 ? 149.322 105.544 142.651 1.00 22.56 ?  259 PHE D CE1   1 
ATOM   15484 C  CE2   . PHE D 2 280 ? 149.326 103.269 141.846 1.00 20.29 ?  259 PHE D CE2   1 
ATOM   15485 C  CZ    . PHE D 2 280 ? 148.892 104.590 141.728 1.00 21.30 ?  259 PHE D CZ    1 
ATOM   15486 N  N     . ILE D 2 281 ? 150.290 101.661 147.210 1.00 19.36 ?  260 ILE D N     1 
ATOM   15487 C  CA    . ILE D 2 281 ? 149.294 100.750 147.781 1.00 19.45 ?  260 ILE D CA    1 
ATOM   15488 C  C     . ILE D 2 281 ? 148.542 101.375 148.976 1.00 19.61 ?  260 ILE D C     1 
ATOM   15489 O  O     . ILE D 2 281 ? 147.312 101.317 149.024 1.00 19.72 ?  260 ILE D O     1 
ATOM   15490 C  CB    . ILE D 2 281 ? 149.963 99.407  148.173 1.00 19.49 ?  260 ILE D CB    1 
ATOM   15491 C  CG1   . ILE D 2 281 ? 150.453 98.689  146.912 1.00 20.10 ?  260 ILE D CG1   1 
ATOM   15492 C  CG2   . ILE D 2 281 ? 149.038 98.514  149.030 1.00 20.53 ?  260 ILE D CG2   1 
ATOM   15493 C  CD1   . ILE D 2 281 ? 151.414 97.539  147.232 1.00 21.17 ?  260 ILE D CD1   1 
ATOM   15494 N  N     . ARG D 2 282 ? 149.274 101.973 149.918 1.00 19.75 ?  261 ARG D N     1 
ATOM   15495 C  CA    . ARG D 2 282 ? 148.659 102.554 151.128 1.00 20.34 ?  261 ARG D CA    1 
ATOM   15496 C  C     . ARG D 2 282 ? 147.769 103.746 150.796 1.00 21.18 ?  261 ARG D C     1 
ATOM   15497 O  O     . ARG D 2 282 ? 146.678 103.910 151.362 1.00 21.68 ?  261 ARG D O     1 
ATOM   15498 C  CB    . ARG D 2 282 ? 149.721 102.944 152.163 1.00 20.20 ?  261 ARG D CB    1 
ATOM   15499 C  CG    . ARG D 2 282 ? 150.392 101.759 152.833 1.00 20.57 ?  261 ARG D CG    1 
ATOM   15500 C  CD    . ARG D 2 282 ? 151.313 102.209 153.969 1.00 23.15 ?  261 ARG D CD    1 
ATOM   15501 N  NE    . ARG D 2 282 ? 152.559 102.824 153.505 1.00 23.46 ?  261 ARG D NE    1 
ATOM   15502 C  CZ    . ARG D 2 282 ? 153.679 102.155 153.235 1.00 22.84 ?  261 ARG D CZ    1 
ATOM   15503 N  NH1   . ARG D 2 282 ? 153.721 100.834 153.343 1.00 23.37 1  261 ARG D NH1   1 
ATOM   15504 N  NH2   . ARG D 2 282 ? 154.761 102.814 152.844 1.00 22.27 ?  261 ARG D NH2   1 
ATOM   15505 N  N     . TYR D 2 283 ? 148.255 104.584 149.888 1.00 21.46 ?  262 TYR D N     1 
ATOM   15506 C  CA    . TYR D 2 283 ? 147.502 105.737 149.397 1.00 22.97 ?  262 TYR D CA    1 
ATOM   15507 C  C     . TYR D 2 283 ? 146.170 105.279 148.763 1.00 22.12 ?  262 TYR D C     1 
ATOM   15508 O  O     . TYR D 2 283 ? 145.117 105.872 149.011 1.00 22.00 ?  262 TYR D O     1 
ATOM   15509 C  CB    . TYR D 2 283 ? 148.389 106.517 148.419 1.00 23.37 ?  262 TYR D CB    1 
ATOM   15510 C  CG    . TYR D 2 283 ? 147.700 107.536 147.543 1.00 27.31 ?  262 TYR D CG    1 
ATOM   15511 C  CD1   . TYR D 2 283 ? 147.501 108.844 147.985 1.00 30.79 ?  262 TYR D CD1   1 
ATOM   15512 C  CD2   . TYR D 2 283 ? 147.287 107.203 146.253 1.00 30.31 ?  262 TYR D CD2   1 
ATOM   15513 C  CE1   . TYR D 2 283 ? 146.868 109.796 147.168 1.00 33.18 ?  262 TYR D CE1   1 
ATOM   15514 C  CE2   . TYR D 2 283 ? 146.666 108.143 145.425 1.00 33.20 ?  262 TYR D CE2   1 
ATOM   15515 C  CZ    . TYR D 2 283 ? 146.467 109.438 145.890 1.00 34.74 ?  262 TYR D CZ    1 
ATOM   15516 O  OH    . TYR D 2 283 ? 145.859 110.367 145.067 1.00 37.63 ?  262 TYR D OH    1 
ATOM   15517 N  N     . ASN D 2 284 ? 146.209 104.197 147.991 1.00 21.63 ?  263 ASN D N     1 
ATOM   15518 C  CA    . ASN D 2 284 ? 144.994 103.683 147.363 1.00 21.41 ?  263 ASN D CA    1 
ATOM   15519 C  C     . ASN D 2 284 ? 144.090 102.903 148.323 1.00 20.86 ?  263 ASN D C     1 
ATOM   15520 O  O     . ASN D 2 284 ? 142.875 102.919 148.167 1.00 20.92 ?  263 ASN D O     1 
ATOM   15521 C  CB    . ASN D 2 284 ? 145.314 102.899 146.089 1.00 21.15 ?  263 ASN D CB    1 
ATOM   15522 C  CG    . ASN D 2 284 ? 145.693 103.816 144.934 1.00 22.59 ?  263 ASN D CG    1 
ATOM   15523 O  OD1   . ASN D 2 284 ? 144.841 104.511 144.375 1.00 22.35 ?  263 ASN D OD1   1 
ATOM   15524 N  ND2   . ASN D 2 284 ? 146.975 103.833 144.581 1.00 22.93 ?  263 ASN D ND2   1 
ATOM   15525 N  N     . ALA D 2 285 ? 144.684 102.236 149.312 1.00 20.92 ?  264 ALA D N     1 
ATOM   15526 C  CA    . ALA D 2 285 ? 143.916 101.643 150.421 1.00 20.77 ?  264 ALA D CA    1 
ATOM   15527 C  C     . ALA D 2 285 ? 143.063 102.691 151.143 1.00 21.13 ?  264 ALA D C     1 
ATOM   15528 O  O     . ALA D 2 285 ? 141.889 102.443 151.447 1.00 19.92 ?  264 ALA D O     1 
ATOM   15529 C  CB    . ALA D 2 285 ? 144.847 100.925 151.409 1.00 20.68 ?  264 ALA D CB    1 
ATOM   15530 N  N     . ASN D 2 286 ? 143.657 103.860 151.407 1.00 21.38 ?  265 ASN D N     1 
ATOM   15531 C  CA    . ASN D 2 286 ? 142.943 104.986 152.015 1.00 21.94 ?  265 ASN D CA    1 
ATOM   15532 C  C     . ASN D 2 286 ? 141.774 105.478 151.144 1.00 22.13 ?  265 ASN D C     1 
ATOM   15533 O  O     . ASN D 2 286 ? 140.715 105.812 151.662 1.00 21.95 ?  265 ASN D O     1 
ATOM   15534 C  CB    . ASN D 2 286 ? 143.896 106.148 152.301 1.00 22.22 ?  265 ASN D CB    1 
ATOM   15535 C  CG    . ASN D 2 286 ? 144.728 105.952 153.565 1.00 22.80 ?  265 ASN D CG    1 
ATOM   15536 O  OD1   . ASN D 2 286 ? 144.464 105.073 154.392 1.00 22.57 ?  265 ASN D OD1   1 
ATOM   15537 N  ND2   . ASN D 2 286 ? 145.753 106.785 153.710 1.00 23.91 ?  265 ASN D ND2   1 
ATOM   15538 N  N     . LYS D 2 287 ? 141.966 105.514 149.827 1.00 22.51 ?  266 LYS D N     1 
ATOM   15539 C  CA    . LYS D 2 287 ? 140.877 105.891 148.915 1.00 22.91 ?  266 LYS D CA    1 
ATOM   15540 C  C     . LYS D 2 287 ? 139.726 104.878 148.973 1.00 22.33 ?  266 LYS D C     1 
ATOM   15541 O  O     . LYS D 2 287 ? 138.565 105.267 148.997 1.00 22.24 ?  266 LYS D O     1 
ATOM   15542 C  CB    . LYS D 2 287 ? 141.382 106.051 147.474 1.00 23.65 ?  266 LYS D CB    1 
ATOM   15543 C  CG    . LYS D 2 287 ? 142.184 107.332 147.240 1.00 26.50 ?  266 LYS D CG    1 
ATOM   15544 C  CD    . LYS D 2 287 ? 142.642 107.427 145.773 1.00 31.30 ?  266 LYS D CD    1 
ATOM   15545 C  CE    . LYS D 2 287 ? 142.978 108.864 145.417 1.00 35.08 ?  266 LYS D CE    1 
ATOM   15546 N  NZ    . LYS D 2 287 ? 143.398 109.050 143.996 1.00 37.66 1  266 LYS D NZ    1 
ATOM   15547 N  N     . ALA D 2 288 ? 140.067 103.589 149.010 1.00 21.41 ?  267 ALA D N     1 
ATOM   15548 C  CA    . ALA D 2 288 ? 139.091 102.503 149.116 1.00 21.53 ?  267 ALA D CA    1 
ATOM   15549 C  C     . ALA D 2 288 ? 138.267 102.606 150.411 1.00 21.77 ?  267 ALA D C     1 
ATOM   15550 O  O     . ALA D 2 288 ? 137.032 102.462 150.401 1.00 21.59 ?  267 ALA D O     1 
ATOM   15551 C  CB    . ALA D 2 288 ? 139.795 101.142 149.021 1.00 21.33 ?  267 ALA D CB    1 
ATOM   15552 N  N     . LEU D 2 289 ? 138.946 102.880 151.516 1.00 21.71 ?  268 LEU D N     1 
ATOM   15553 C  CA    . LEU D 2 289 ? 138.261 103.109 152.783 1.00 22.36 ?  268 LEU D CA    1 
ATOM   15554 C  C     . LEU D 2 289 ? 137.336 104.315 152.696 1.00 23.01 ?  268 LEU D C     1 
ATOM   15555 O  O     . LEU D 2 289 ? 136.181 104.249 153.122 1.00 23.14 ?  268 LEU D O     1 
ATOM   15556 C  CB    . LEU D 2 289 ? 139.264 103.252 153.934 1.00 22.61 ?  268 LEU D CB    1 
ATOM   15557 C  CG    . LEU D 2 289 ? 140.004 101.958 154.334 1.00 21.22 ?  268 LEU D CG    1 
ATOM   15558 C  CD1   . LEU D 2 289 ? 141.180 102.265 155.248 1.00 20.77 ?  268 LEU D CD1   1 
ATOM   15559 C  CD2   . LEU D 2 289 ? 139.058 100.930 154.995 1.00 21.40 ?  268 LEU D CD2   1 
ATOM   15560 N  N     . MET D 2 290 ? 137.819 105.412 152.121 1.00 23.87 ?  269 MET D N     1 
ATOM   15561 C  CA    . MET D 2 290 ? 136.960 106.585 151.980 1.00 25.26 ?  269 MET D CA    1 
ATOM   15562 C  C     . MET D 2 290 ? 135.732 106.295 151.100 1.00 24.37 ?  269 MET D C     1 
ATOM   15563 O  O     . MET D 2 290 ? 134.641 106.758 151.417 1.00 23.97 ?  269 MET D O     1 
ATOM   15564 C  CB    . MET D 2 290 ? 137.757 107.812 151.551 1.00 25.94 ?  269 MET D CB    1 
ATOM   15565 C  CG    . MET D 2 290 ? 138.503 108.434 152.748 1.00 31.08 ?  269 MET D CG    1 
ATOM   15566 S  SD    . MET D 2 290 ? 139.505 109.881 152.338 1.00 41.28 ?  269 MET D SD    1 
ATOM   15567 C  CE    . MET D 2 290 ? 138.298 110.925 151.480 1.00 38.56 ?  269 MET D CE    1 
ATOM   15568 N  N     . ASN D 2 291 ? 135.899 105.492 150.045 1.00 23.66 ?  270 ASN D N     1 
ATOM   15569 C  CA    . ASN D 2 291 ? 134.748 105.016 149.241 1.00 23.17 ?  270 ASN D CA    1 
ATOM   15570 C  C     . ASN D 2 291 ? 133.676 104.280 150.050 1.00 23.22 ?  270 ASN D C     1 
ATOM   15571 O  O     . ASN D 2 291 ? 132.496 104.317 149.703 1.00 22.68 ?  270 ASN D O     1 
ATOM   15572 C  CB    . ASN D 2 291 ? 135.201 104.122 148.075 1.00 22.41 ?  270 ASN D CB    1 
ATOM   15573 C  CG    . ASN D 2 291 ? 135.940 104.891 147.004 1.00 21.93 ?  270 ASN D CG    1 
ATOM   15574 O  OD1   . ASN D 2 291 ? 135.919 106.126 146.980 1.00 20.94 ?  270 ASN D OD1   1 
ATOM   15575 N  ND2   . ASN D 2 291 ? 136.603 104.165 146.108 1.00 19.20 ?  270 ASN D ND2   1 
ATOM   15576 N  N     . LEU D 2 292 ? 134.107 103.613 151.120 1.00 23.53 ?  271 LEU D N     1 
ATOM   15577 C  CA    . LEU D 2 292 ? 133.210 102.877 152.013 1.00 24.21 ?  271 LEU D CA    1 
ATOM   15578 C  C     . LEU D 2 292 ? 132.760 103.726 153.206 1.00 25.14 ?  271 LEU D C     1 
ATOM   15579 O  O     . LEU D 2 292 ? 132.149 103.213 154.157 1.00 25.14 ?  271 LEU D O     1 
ATOM   15580 C  CB    . LEU D 2 292 ? 133.882 101.572 152.491 1.00 23.71 ?  271 LEU D CB    1 
ATOM   15581 C  CG    . LEU D 2 292 ? 134.209 100.511 151.430 1.00 23.37 ?  271 LEU D CG    1 
ATOM   15582 C  CD1   . LEU D 2 292 ? 135.210 99.486  151.971 1.00 23.28 ?  271 LEU D CD1   1 
ATOM   15583 C  CD2   . LEU D 2 292 ? 132.937 99.812  150.911 1.00 23.06 ?  271 LEU D CD2   1 
ATOM   15584 N  N     . GLY D 2 293 ? 133.055 105.026 153.144 1.00 25.82 ?  272 GLY D N     1 
ATOM   15585 C  CA    . GLY D 2 293 ? 132.683 105.963 154.197 1.00 27.13 ?  272 GLY D CA    1 
ATOM   15586 C  C     . GLY D 2 293 ? 133.470 105.811 155.482 1.00 27.99 ?  272 GLY D C     1 
ATOM   15587 O  O     . GLY D 2 293 ? 133.034 106.281 156.529 1.00 27.97 ?  272 GLY D O     1 
ATOM   15588 N  N     . PHE D 2 294 ? 134.631 105.153 155.405 1.00 28.02 ?  273 PHE D N     1 
ATOM   15589 C  CA    . PHE D 2 294 ? 135.498 104.945 156.572 1.00 28.75 ?  273 PHE D CA    1 
ATOM   15590 C  C     . PHE D 2 294 ? 136.692 105.907 156.592 1.00 29.00 ?  273 PHE D C     1 
ATOM   15591 O  O     . PHE D 2 294 ? 137.064 106.464 155.561 1.00 28.74 ?  273 PHE D O     1 
ATOM   15592 C  CB    . PHE D 2 294 ? 136.010 103.496 156.609 1.00 28.32 ?  273 PHE D CB    1 
ATOM   15593 C  CG    . PHE D 2 294 ? 134.929 102.469 156.806 1.00 28.66 ?  273 PHE D CG    1 
ATOM   15594 C  CD1   . PHE D 2 294 ? 133.897 102.685 157.719 1.00 30.23 ?  273 PHE D CD1   1 
ATOM   15595 C  CD2   . PHE D 2 294 ? 134.953 101.279 156.091 1.00 26.94 ?  273 PHE D CD2   1 
ATOM   15596 C  CE1   . PHE D 2 294 ? 132.892 101.729 157.903 1.00 31.04 ?  273 PHE D CE1   1 
ATOM   15597 C  CE2   . PHE D 2 294 ? 133.966 100.319 156.267 1.00 27.39 ?  273 PHE D CE2   1 
ATOM   15598 C  CZ    . PHE D 2 294 ? 132.934 100.535 157.172 1.00 29.80 ?  273 PHE D CZ    1 
ATOM   15599 N  N     . ASP D 2 295 ? 137.283 106.095 157.771 1.00 29.60 ?  274 ASP D N     1 
ATOM   15600 C  CA    . ASP D 2 295 ? 138.468 106.934 157.925 1.00 30.40 ?  274 ASP D CA    1 
ATOM   15601 C  C     . ASP D 2 295 ? 139.710 106.285 157.282 1.00 29.58 ?  274 ASP D C     1 
ATOM   15602 O  O     . ASP D 2 295 ? 139.796 105.060 157.198 1.00 28.68 ?  274 ASP D O     1 
ATOM   15603 C  CB    . ASP D 2 295 ? 138.746 107.217 159.407 1.00 31.44 ?  274 ASP D CB    1 
ATOM   15604 C  CG    . ASP D 2 295 ? 137.655 108.052 160.069 1.00 34.27 ?  274 ASP D CG    1 
ATOM   15605 O  OD1   . ASP D 2 295 ? 136.988 108.859 159.377 1.00 36.43 ?  274 ASP D OD1   1 
ATOM   15606 O  OD2   . ASP D 2 295 ? 137.474 107.897 161.296 1.00 38.03 -1 274 ASP D OD2   1 
ATOM   15607 N  N     . PRO D 2 296 ? 140.679 107.110 156.839 1.00 29.59 ?  275 PRO D N     1 
ATOM   15608 C  CA    . PRO D 2 296 ? 141.914 106.525 156.310 1.00 29.09 ?  275 PRO D CA    1 
ATOM   15609 C  C     . PRO D 2 296 ? 142.640 105.720 157.388 1.00 29.26 ?  275 PRO D C     1 
ATOM   15610 O  O     . PRO D 2 296 ? 142.601 106.077 158.565 1.00 29.36 ?  275 PRO D O     1 
ATOM   15611 C  CB    . PRO D 2 296 ? 142.748 107.747 155.901 1.00 29.49 ?  275 PRO D CB    1 
ATOM   15612 C  CG    . PRO D 2 296 ? 142.141 108.913 156.633 1.00 30.28 ?  275 PRO D CG    1 
ATOM   15613 C  CD    . PRO D 2 296 ? 140.690 108.585 156.792 1.00 29.63 ?  275 PRO D CD    1 
ATOM   15614 N  N     . TYR D 2 297 ? 143.276 104.631 156.985 1.00 28.97 ?  276 TYR D N     1 
ATOM   15615 C  CA    . TYR D 2 297 ? 143.967 103.751 157.920 1.00 29.63 ?  276 TYR D CA    1 
ATOM   15616 C  C     . TYR D 2 297 ? 145.453 104.124 158.048 1.00 29.55 ?  276 TYR D C     1 
ATOM   15617 O  O     . TYR D 2 297 ? 146.054 104.001 159.123 1.00 30.12 ?  276 TYR D O     1 
ATOM   15618 C  CB    . TYR D 2 297 ? 143.830 102.310 157.431 1.00 29.49 ?  276 TYR D CB    1 
ATOM   15619 C  CG    . TYR D 2 297 ? 144.207 101.250 158.431 1.00 31.19 ?  276 TYR D CG    1 
ATOM   15620 C  CD1   . TYR D 2 297 ? 143.500 101.114 159.630 1.00 31.93 ?  276 TYR D CD1   1 
ATOM   15621 C  CD2   . TYR D 2 297 ? 145.253 100.362 158.172 1.00 31.98 ?  276 TYR D CD2   1 
ATOM   15622 C  CE1   . TYR D 2 297 ? 143.835 100.133 160.554 1.00 33.86 ?  276 TYR D CE1   1 
ATOM   15623 C  CE2   . TYR D 2 297 ? 145.594 99.369  159.092 1.00 33.88 ?  276 TYR D CE2   1 
ATOM   15624 C  CZ    . TYR D 2 297 ? 144.873 99.264  160.276 1.00 34.42 ?  276 TYR D CZ    1 
ATOM   15625 O  OH    . TYR D 2 297 ? 145.197 98.300  161.197 1.00 37.63 ?  276 TYR D OH    1 
ATOM   15626 N  N     . PHE D 2 298 ? 146.025 104.574 156.937 1.00 29.10 ?  277 PHE D N     1 
ATOM   15627 C  CA    . PHE D 2 298 ? 147.455 104.844 156.822 1.00 28.97 ?  277 PHE D CA    1 
ATOM   15628 C  C     . PHE D 2 298 ? 147.728 106.352 156.827 1.00 29.77 ?  277 PHE D C     1 
ATOM   15629 O  O     . PHE D 2 298 ? 146.909 107.141 156.347 1.00 29.07 ?  277 PHE D O     1 
ATOM   15630 C  CB    . PHE D 2 298 ? 148.002 104.230 155.529 1.00 27.99 ?  277 PHE D CB    1 
ATOM   15631 C  CG    . PHE D 2 298 ? 147.853 102.729 155.448 1.00 27.61 ?  277 PHE D CG    1 
ATOM   15632 C  CD1   . PHE D 2 298 ? 146.924 102.153 154.591 1.00 25.91 ?  277 PHE D CD1   1 
ATOM   15633 C  CD2   . PHE D 2 298 ? 148.662 101.892 156.219 1.00 27.32 ?  277 PHE D CD2   1 
ATOM   15634 C  CE1   . PHE D 2 298 ? 146.795 100.777 154.510 1.00 26.65 ?  277 PHE D CE1   1 
ATOM   15635 C  CE2   . PHE D 2 298 ? 148.544 100.516 156.148 1.00 25.38 ?  277 PHE D CE2   1 
ATOM   15636 C  CZ    . PHE D 2 298 ? 147.608 99.951  155.302 1.00 26.20 ?  277 PHE D CZ    1 
ATOM   15637 N  N     . GLU D 2 299 ? 148.879 106.739 157.377 1.00 31.10 ?  278 GLU D N     1 
ATOM   15638 C  CA    . GLU D 2 299 ? 149.335 108.131 157.334 1.00 32.86 ?  278 GLU D CA    1 
ATOM   15639 C  C     . GLU D 2 299 ? 149.526 108.573 155.877 1.00 33.04 ?  278 GLU D C     1 
ATOM   15640 O  O     . GLU D 2 299 ? 149.834 107.754 155.006 1.00 32.23 ?  278 GLU D O     1 
ATOM   15641 C  CB    . GLU D 2 299 ? 150.641 108.302 158.130 1.00 33.45 ?  278 GLU D CB    1 
ATOM   15642 C  CG    . GLU D 2 299 ? 151.813 107.478 157.574 1.00 36.27 ?  278 GLU D CG    1 
ATOM   15643 C  CD    . GLU D 2 299 ? 153.148 107.734 158.259 1.00 40.47 ?  278 GLU D CD    1 
ATOM   15644 O  OE1   . GLU D 2 299 ? 153.189 107.873 159.503 1.00 41.72 ?  278 GLU D OE1   1 
ATOM   15645 O  OE2   . GLU D 2 299 ? 154.167 107.763 157.535 1.00 42.65 -1 278 GLU D OE2   1 
ATOM   15646 N  N     . GLU D 2 300 ? 149.331 109.866 155.630 1.00 34.09 ?  279 GLU D N     1 
ATOM   15647 C  CA    . GLU D 2 300 ? 149.497 110.451 154.306 1.00 35.06 ?  279 GLU D CA    1 
ATOM   15648 C  C     . GLU D 2 300 ? 150.966 110.399 153.884 1.00 34.97 ?  279 GLU D C     1 
ATOM   15649 O  O     . GLU D 2 300 ? 151.861 110.707 154.672 1.00 34.96 ?  279 GLU D O     1 
ATOM   15650 C  CB    . GLU D 2 300 ? 148.974 111.898 154.296 1.00 35.81 ?  279 GLU D CB    1 
ATOM   15651 C  CG    . GLU D 2 300 ? 148.926 112.542 152.909 1.00 38.58 ?  279 GLU D CG    1 
ATOM   15652 C  CD    . GLU D 2 300 ? 147.906 113.674 152.807 1.00 43.09 ?  279 GLU D CD    1 
ATOM   15653 O  OE1   . GLU D 2 300 ? 147.018 113.593 151.927 1.00 44.69 ?  279 GLU D OE1   1 
ATOM   15654 O  OE2   . GLU D 2 300 ? 147.983 114.635 153.607 1.00 44.94 -1 279 GLU D OE2   1 
ATOM   15655 N  N     . GLU D 2 301 ? 151.196 109.981 152.643 1.00 34.73 ?  280 GLU D N     1 
ATOM   15656 C  CA    . GLU D 2 301 ? 152.535 109.907 152.072 1.00 35.16 ?  280 GLU D CA    1 
ATOM   15657 C  C     . GLU D 2 301 ? 152.517 110.540 150.691 1.00 35.23 ?  280 GLU D C     1 
ATOM   15658 O  O     . GLU D 2 301 ? 151.482 110.550 150.017 1.00 34.92 ?  280 GLU D O     1 
ATOM   15659 C  CB    . GLU D 2 301 ? 152.991 108.446 151.956 1.00 35.10 ?  280 GLU D CB    1 
ATOM   15660 C  CG    . GLU D 2 301 ? 153.526 107.835 153.248 1.00 36.62 ?  280 GLU D CG    1 
ATOM   15661 C  CD    . GLU D 2 301 ? 153.710 106.320 153.157 1.00 37.59 ?  280 GLU D CD    1 
ATOM   15662 O  OE1   . GLU D 2 301 ? 152.729 105.607 152.858 1.00 38.10 ?  280 GLU D OE1   1 
ATOM   15663 O  OE2   . GLU D 2 301 ? 154.831 105.837 153.410 1.00 38.93 -1 280 GLU D OE2   1 
ATOM   15664 N  N     . ASP D 2 302 ? 153.658 111.069 150.266 1.00 35.60 ?  281 ASP D N     1 
ATOM   15665 C  CA    . ASP D 2 302 ? 153.775 111.591 148.909 1.00 35.96 ?  281 ASP D CA    1 
ATOM   15666 C  C     . ASP D 2 302 ? 153.994 110.421 147.958 1.00 35.01 ?  281 ASP D C     1 
ATOM   15667 O  O     . ASP D 2 302 ? 154.515 109.382 148.363 1.00 35.52 ?  281 ASP D O     1 
ATOM   15668 C  CB    . ASP D 2 302 ? 154.892 112.645 148.808 1.00 36.82 ?  281 ASP D CB    1 
ATOM   15669 C  CG    . ASP D 2 302 ? 156.295 112.081 149.101 1.00 39.01 ?  281 ASP D CG    1 
ATOM   15670 O  OD1   . ASP D 2 302 ? 156.433 111.019 149.759 1.00 40.83 ?  281 ASP D OD1   1 
ATOM   15671 O  OD2   . ASP D 2 302 ? 157.273 112.733 148.683 1.00 41.13 -1 281 ASP D OD2   1 
ATOM   15672 N  N     . ILE D 2 303 ? 153.563 110.566 146.713 1.00 33.94 ?  282 ILE D N     1 
ATOM   15673 C  CA    . ILE D 2 303 ? 153.714 109.493 145.732 1.00 33.00 ?  282 ILE D CA    1 
ATOM   15674 C  C     . ILE D 2 303 ? 154.818 109.795 144.710 1.00 31.59 ?  282 ILE D C     1 
ATOM   15675 O  O     . ILE D 2 303 ? 155.108 110.959 144.426 1.00 31.14 ?  282 ILE D O     1 
ATOM   15676 C  CB    . ILE D 2 303 ? 152.348 109.137 145.062 1.00 33.44 ?  282 ILE D CB    1 
ATOM   15677 C  CG1   . ILE D 2 303 ? 152.528 108.627 143.627 1.00 34.29 ?  282 ILE D CG1   1 
ATOM   15678 C  CG2   . ILE D 2 303 ? 151.398 110.323 145.114 1.00 35.47 ?  282 ILE D CG2   1 
ATOM   15679 C  CD1   . ILE D 2 303 ? 151.232 108.457 142.860 1.00 36.30 ?  282 ILE D CD1   1 
ATOM   15680 N  N     . ASN D 2 304 ? 155.444 108.741 144.188 1.00 29.53 ?  283 ASN D N     1 
ATOM   15681 C  CA    . ASN D 2 304 ? 156.452 108.875 143.139 1.00 28.49 ?  283 ASN D CA    1 
ATOM   15682 C  C     . ASN D 2 304 ? 155.987 109.839 142.027 1.00 27.87 ?  283 ASN D C     1 
ATOM   15683 O  O     . ASN D 2 304 ? 154.917 109.645 141.450 1.00 27.02 ?  283 ASN D O     1 
ATOM   15684 C  CB    . ASN D 2 304 ? 156.783 107.501 142.554 1.00 28.20 ?  283 ASN D CB    1 
ATOM   15685 C  CG    . ASN D 2 304 ? 157.885 107.563 141.530 1.00 28.17 ?  283 ASN D CG    1 
ATOM   15686 O  OD1   . ASN D 2 304 ? 157.636 107.827 140.358 1.00 29.01 ?  283 ASN D OD1   1 
ATOM   15687 N  ND2   . ASN D 2 304 ? 159.113 107.321 141.963 1.00 27.24 ?  283 ASN D ND2   1 
ATOM   15688 N  N     . PRO D 2 305 ? 156.783 110.889 141.737 1.00 28.00 ?  284 PRO D N     1 
ATOM   15689 C  CA    . PRO D 2 305 ? 156.355 111.917 140.774 1.00 27.58 ?  284 PRO D CA    1 
ATOM   15690 C  C     . PRO D 2 305 ? 156.218 111.424 139.332 1.00 27.01 ?  284 PRO D C     1 
ATOM   15691 O  O     . PRO D 2 305 ? 155.463 112.006 138.561 1.00 26.66 ?  284 PRO D O     1 
ATOM   15692 C  CB    . PRO D 2 305 ? 157.454 112.983 140.872 1.00 28.21 ?  284 PRO D CB    1 
ATOM   15693 C  CG    . PRO D 2 305 ? 158.613 112.307 141.461 1.00 28.80 ?  284 PRO D CG    1 
ATOM   15694 C  CD    . PRO D 2 305 ? 158.048 111.262 142.397 1.00 28.11 ?  284 PRO D CD    1 
ATOM   15695 N  N     . ILE D 2 306 ? 156.935 110.362 138.977 1.00 26.52 ?  285 ILE D N     1 
ATOM   15696 C  CA    . ILE D 2 306 ? 156.823 109.790 137.640 1.00 26.50 ?  285 ILE D CA    1 
ATOM   15697 C  C     . ILE D 2 306 ? 155.454 109.115 137.473 1.00 26.43 ?  285 ILE D C     1 
ATOM   15698 O  O     . ILE D 2 306 ? 154.742 109.346 136.485 1.00 26.00 ?  285 ILE D O     1 
ATOM   15699 C  CB    . ILE D 2 306 ? 157.995 108.828 137.323 1.00 26.88 ?  285 ILE D CB    1 
ATOM   15700 C  CG1   . ILE D 2 306 ? 159.329 109.592 137.396 1.00 26.98 ?  285 ILE D CG1   1 
ATOM   15701 C  CG2   . ILE D 2 306 ? 157.783 108.179 135.956 1.00 24.94 ?  285 ILE D CG2   1 
ATOM   15702 C  CD1   . ILE D 2 306 ? 160.562 108.736 137.294 1.00 26.65 ?  285 ILE D CD1   1 
ATOM   15703 N  N     . VAL D 2 307 ? 155.082 108.311 138.463 1.00 26.36 ?  286 VAL D N     1 
ATOM   15704 C  CA    . VAL D 2 307 ? 153.745 107.732 138.522 1.00 26.71 ?  286 VAL D CA    1 
ATOM   15705 C  C     . VAL D 2 307 ? 152.662 108.815 138.575 1.00 27.68 ?  286 VAL D C     1 
ATOM   15706 O  O     . VAL D 2 307 ? 151.652 108.696 137.881 1.00 27.92 ?  286 VAL D O     1 
ATOM   15707 C  CB    . VAL D 2 307 ? 153.616 106.705 139.679 1.00 26.37 ?  286 VAL D CB    1 
ATOM   15708 C  CG1   . VAL D 2 307 ? 152.154 106.285 139.901 1.00 25.48 ?  286 VAL D CG1   1 
ATOM   15709 C  CG2   . VAL D 2 307 ? 154.444 105.503 139.358 1.00 25.55 ?  286 VAL D CG2   1 
ATOM   15710 N  N     . LEU D 2 308 ? 152.879 109.880 139.353 1.00 28.80 ?  287 LEU D N     1 
ATOM   15711 C  CA    . LEU D 2 308 ? 151.939 111.012 139.351 1.00 30.07 ?  287 LEU D CA    1 
ATOM   15712 C  C     . LEU D 2 308 ? 151.769 111.634 137.961 1.00 30.38 ?  287 LEU D C     1 
ATOM   15713 O  O     . LEU D 2 308 ? 150.652 111.965 137.548 1.00 30.71 ?  287 LEU D O     1 
ATOM   15714 C  CB    . LEU D 2 308 ? 152.348 112.088 140.362 1.00 30.86 ?  287 LEU D CB    1 
ATOM   15715 C  CG    . LEU D 2 308 ? 151.887 111.857 141.805 1.00 32.62 ?  287 LEU D CG    1 
ATOM   15716 C  CD1   . LEU D 2 308 ? 152.520 112.866 142.737 1.00 33.97 ?  287 LEU D CD1   1 
ATOM   15717 C  CD2   . LEU D 2 308 ? 150.352 111.897 141.921 1.00 34.73 ?  287 LEU D CD2   1 
ATOM   15718 N  N     . ASN D 2 309 ? 152.872 111.781 137.236 1.00 30.81 ?  288 ASN D N     1 
ATOM   15719 C  CA    . ASN D 2 309 ? 152.814 112.317 135.880 1.00 31.25 ?  288 ASN D CA    1 
ATOM   15720 C  C     . ASN D 2 309 ? 152.035 111.394 134.941 1.00 31.83 ?  288 ASN D C     1 
ATOM   15721 O  O     . ASN D 2 309 ? 151.345 111.863 134.031 1.00 31.73 ?  288 ASN D O     1 
ATOM   15722 C  CB    . ASN D 2 309 ? 154.214 112.612 135.330 1.00 31.21 ?  288 ASN D CB    1 
ATOM   15723 C  CG    . ASN D 2 309 ? 154.168 113.354 134.004 1.00 31.41 ?  288 ASN D CG    1 
ATOM   15724 O  OD1   . ASN D 2 309 ? 153.393 114.303 133.838 1.00 31.88 ?  288 ASN D OD1   1 
ATOM   15725 N  ND2   . ASN D 2 309 ? 154.989 112.923 133.052 1.00 29.12 ?  288 ASN D ND2   1 
ATOM   15726 N  N     . GLY D 2 310 ? 152.146 110.086 135.175 1.00 32.04 ?  289 GLY D N     1 
ATOM   15727 C  CA    . GLY D 2 310 ? 151.344 109.098 134.464 1.00 33.04 ?  289 GLY D CA    1 
ATOM   15728 C  C     . GLY D 2 310 ? 149.864 109.236 134.797 1.00 33.85 ?  289 GLY D C     1 
ATOM   15729 O  O     . GLY D 2 310 ? 149.024 109.256 133.898 1.00 34.05 ?  289 GLY D O     1 
ATOM   15730 N  N     . LEU D 2 311 ? 149.552 109.336 136.089 1.00 34.33 ?  290 LEU D N     1 
ATOM   15731 C  CA    . LEU D 2 311 ? 148.172 109.453 136.568 1.00 35.77 ?  290 LEU D CA    1 
ATOM   15732 C  C     . LEU D 2 311 ? 147.462 110.705 136.063 1.00 37.01 ?  290 LEU D C     1 
ATOM   15733 O  O     . LEU D 2 311 ? 146.283 110.656 135.709 1.00 37.18 ?  290 LEU D O     1 
ATOM   15734 C  CB    . LEU D 2 311 ? 148.131 109.454 138.101 1.00 35.50 ?  290 LEU D CB    1 
ATOM   15735 C  CG    . LEU D 2 311 ? 147.991 108.161 138.899 1.00 35.45 ?  290 LEU D CG    1 
ATOM   15736 C  CD1   . LEU D 2 311 ? 148.173 108.469 140.394 1.00 35.28 ?  290 LEU D CD1   1 
ATOM   15737 C  CD2   . LEU D 2 311 ? 146.647 107.470 138.655 1.00 34.16 ?  290 LEU D CD2   1 
ATOM   15738 N  N     . LYS D 2 330 ? 116.122 118.376 148.470 1.00 42.55 ?  309 LYS D N     1 
ATOM   15739 C  CA    . LYS D 2 330 ? 114.717 118.320 148.083 1.00 44.90 ?  309 LYS D CA    1 
ATOM   15740 C  C     . LYS D 2 330 ? 113.801 118.186 149.293 1.00 43.76 ?  309 LYS D C     1 
ATOM   15741 O  O     . LYS D 2 330 ? 113.501 117.078 149.737 1.00 44.28 ?  309 LYS D O     1 
ATOM   15742 C  CB    . LYS D 2 330 ? 114.475 117.157 147.116 1.00 40.63 ?  309 LYS D CB    1 
ATOM   15743 C  CG    . LYS D 2 330 ? 113.134 117.216 146.399 1.00 43.98 ?  309 LYS D CG    1 
ATOM   15744 C  CD    . LYS D 2 330 ? 113.016 118.456 145.527 1.00 43.19 ?  309 LYS D CD    1 
ATOM   15745 C  CE    . LYS D 2 330 ? 113.045 118.096 144.051 1.00 45.38 ?  309 LYS D CE    1 
ATOM   15746 N  NZ    . LYS D 2 330 ? 113.231 119.295 143.189 1.00 43.90 1  309 LYS D NZ    1 
ATOM   15747 N  N     . ALA D 2 331 ? 113.362 119.322 149.827 1.00 41.98 ?  310 ALA D N     1 
ATOM   15748 C  CA    . ALA D 2 331 ? 112.395 119.317 150.911 1.00 42.36 ?  310 ALA D CA    1 
ATOM   15749 C  C     . ALA D 2 331 ? 111.019 118.916 150.388 1.00 42.70 ?  310 ALA D C     1 
ATOM   15750 O  O     . ALA D 2 331 ? 110.716 119.042 149.198 1.00 44.14 ?  310 ALA D O     1 
ATOM   15751 C  CB    . ALA D 2 331 ? 112.325 120.687 151.584 1.00 39.32 ?  310 ALA D CB    1 
ATOM   15752 N  N     . THR D 2 332 ? 110.184 118.423 151.297 1.00 33.29 ?  311 THR D N     1 
ATOM   15753 C  CA    . THR D 2 332 ? 108.856 117.932 150.937 1.00 32.46 ?  311 THR D CA    1 
ATOM   15754 C  C     . THR D 2 332 ? 108.011 119.104 150.457 1.00 32.78 ?  311 THR D C     1 
ATOM   15755 O  O     . THR D 2 332 ? 107.810 120.082 151.180 1.00 35.85 ?  311 THR D O     1 
ATOM   15756 C  CB    . THR D 2 332 ? 108.204 117.233 152.126 1.00 36.71 ?  311 THR D CB    1 
ATOM   15757 O  OG1   . THR D 2 332 ? 108.712 115.898 152.232 1.00 39.19 ?  311 THR D OG1   1 
ATOM   15758 C  CG2   . THR D 2 332 ? 106.693 117.170 151.944 1.00 34.82 ?  311 THR D CG2   1 
ATOM   15759 N  N     . VAL D 2 333 ? 107.524 119.018 149.221 1.00 30.31 ?  312 VAL D N     1 
ATOM   15760 C  CA    . VAL D 2 333 ? 106.676 120.061 148.657 1.00 24.24 ?  312 VAL D CA    1 
ATOM   15761 C  C     . VAL D 2 333 ? 105.270 119.912 149.219 1.00 30.13 ?  312 VAL D C     1 
ATOM   15762 O  O     . VAL D 2 333 ? 104.599 118.901 148.983 1.00 35.56 ?  312 VAL D O     1 
ATOM   15763 C  CB    . VAL D 2 333 ? 106.667 120.007 147.119 1.00 29.05 ?  312 VAL D CB    1 
ATOM   15764 C  CG1   . VAL D 2 333 ? 105.896 121.187 146.554 1.00 31.60 ?  312 VAL D CG1   1 
ATOM   15765 C  CG2   . VAL D 2 333 ? 108.089 119.982 146.583 1.00 29.59 ?  312 VAL D CG2   1 
ATOM   15766 N  N     . GLU D 2 334 ? 104.817 120.914 149.966 1.00 28.79 ?  313 GLU D N     1 
ATOM   15767 C  CA    . GLU D 2 334 ? 103.484 120.909 150.552 1.00 29.66 ?  313 GLU D CA    1 
ATOM   15768 C  C     . GLU D 2 334 ? 102.748 122.163 150.102 1.00 31.26 ?  313 GLU D C     1 
ATOM   15769 O  O     . GLU D 2 334 ? 103.242 123.280 150.332 1.00 34.83 ?  313 GLU D O     1 
ATOM   15770 C  CB    . GLU D 2 334 ? 103.558 120.841 152.079 1.00 29.26 ?  313 GLU D CB    1 
ATOM   15771 C  CG    . GLU D 2 334 ? 102.252 121.156 152.784 1.00 33.58 ?  313 GLU D CG    1 
ATOM   15772 C  CD    . GLU D 2 334 ? 102.326 120.904 154.278 1.00 35.28 ?  313 GLU D CD    1 
ATOM   15773 O  OE1   . GLU D 2 334 ? 103.418 121.073 154.857 1.00 33.47 ?  313 GLU D OE1   1 
ATOM   15774 O  OE2   . GLU D 2 334 ? 101.291 120.534 154.873 1.00 31.19 -1 313 GLU D OE2   1 
ATOM   15775 N  N     . PRO D 2 335 ? 101.590 122.039 149.455 1.00 31.21 ?  314 PRO D N     1 
ATOM   15776 C  CA    . PRO D 2 335 ? 100.913 123.222 148.913 1.00 33.35 ?  314 PRO D CA    1 
ATOM   15777 C  C     . PRO D 2 335 ? 100.462 124.173 150.013 1.00 33.18 ?  314 PRO D C     1 
ATOM   15778 O  O     . PRO D 2 335 ? 100.160 123.760 151.135 1.00 33.38 ?  314 PRO D O     1 
ATOM   15779 C  CB    . PRO D 2 335 ? 99.717  122.630 148.160 1.00 30.11 ?  314 PRO D CB    1 
ATOM   15780 C  CG    . PRO D 2 335 ? 99.515  121.279 148.772 1.00 31.03 ?  314 PRO D CG    1 
ATOM   15781 C  CD    . PRO D 2 335 ? 100.887 120.795 149.107 1.00 33.22 ?  314 PRO D CD    1 
ATOM   15782 N  N     . LEU D 2 336 ? 100.425 125.460 149.681 1.00 30.38 ?  315 LEU D N     1 
ATOM   15783 C  CA    . LEU D 2 336 ? 99.887  126.457 150.591 1.00 26.61 ?  315 LEU D CA    1 
ATOM   15784 C  C     . LEU D 2 336 ? 98.382  126.270 150.732 1.00 27.64 ?  315 LEU D C     1 
ATOM   15785 O  O     . LEU D 2 336 ? 97.646  126.204 149.745 1.00 34.77 ?  315 LEU D O     1 
ATOM   15786 C  CB    . LEU D 2 336 ? 100.204 127.866 150.090 1.00 22.39 ?  315 LEU D CB    1 
ATOM   15787 C  CG    . LEU D 2 336 ? 101.586 128.411 150.457 1.00 25.97 ?  315 LEU D CG    1 
ATOM   15788 C  CD1   . LEU D 2 336 ? 101.823 129.762 149.804 1.00 19.59 ?  315 LEU D CD1   1 
ATOM   15789 C  CD2   . LEU D 2 336 ? 101.752 128.505 151.967 1.00 27.01 ?  315 LEU D CD2   1 
ATOM   15790 N  N     . LYS D 2 337 ? 97.928  126.187 151.983 1.00 28.30 ?  316 LYS D N     1 
ATOM   15791 C  CA    . LYS D 2 337 ? 96.553  125.809 152.291 1.00 36.46 ?  316 LYS D CA    1 
ATOM   15792 C  C     . LYS D 2 337 ? 95.655  127.003 152.578 1.00 36.32 ?  316 LYS D C     1 
ATOM   15793 O  O     . LYS D 2 337 ? 94.539  126.811 153.075 1.00 40.02 ?  316 LYS D O     1 
ATOM   15794 C  CB    . LYS D 2 337 ? 96.522  124.852 153.485 1.00 33.57 ?  316 LYS D CB    1 
ATOM   15795 C  CG    . LYS D 2 337 ? 97.571  123.758 153.436 1.00 36.47 ?  316 LYS D CG    1 
ATOM   15796 C  CD    . LYS D 2 337 ? 96.969  122.410 153.789 1.00 38.79 ?  316 LYS D CD    1 
ATOM   15797 C  CE    . LYS D 2 337 ? 98.053  121.380 154.042 1.00 37.56 ?  316 LYS D CE    1 
ATOM   15798 N  NZ    . LYS D 2 337 ? 98.957  121.246 152.869 1.00 36.72 1  316 LYS D NZ    1 
ATOM   15799 N  N     . ASP D 2 338 ? 96.119  128.225 152.299 1.00 24.38 ?  317 ASP D N     1 
ATOM   15800 C  CA    . ASP D 2 338 ? 95.439  129.458 152.692 1.00 29.04 ?  317 ASP D CA    1 
ATOM   15801 C  C     . ASP D 2 338 ? 95.403  129.563 154.214 1.00 28.87 ?  317 ASP D C     1 
ATOM   15802 O  O     . ASP D 2 338 ? 95.683  128.584 154.915 1.00 33.66 ?  317 ASP D O     1 
ATOM   15803 C  CB    . ASP D 2 338 ? 94.030  129.538 152.094 1.00 31.69 ?  317 ASP D CB    1 
ATOM   15804 C  CG    . ASP D 2 338 ? 93.429  130.925 152.200 1.00 32.42 ?  317 ASP D CG    1 
ATOM   15805 O  OD1   . ASP D 2 338 ? 94.198  131.894 152.361 1.00 34.34 ?  317 ASP D OD1   1 
ATOM   15806 O  OD2   . ASP D 2 338 ? 92.189  131.045 152.121 1.00 28.35 -1 317 ASP D OD2   1 
ATOM   15807 N  N     . ASP D 2 339 ? 95.111  130.759 154.729 1.00 22.82 ?  318 ASP D N     1 
ATOM   15808 C  CA    . ASP D 2 339 ? 95.208  131.073 156.153 1.00 24.73 ?  318 ASP D CA    1 
ATOM   15809 C  C     . ASP D 2 339 ? 96.664  131.024 156.606 1.00 24.49 ?  318 ASP D C     1 
ATOM   15810 O  O     . ASP D 2 339 ? 96.970  131.280 157.774 1.00 31.22 ?  318 ASP D O     1 
ATOM   15811 C  CB    . ASP D 2 339 ? 94.338  130.135 156.998 1.00 23.30 ?  318 ASP D CB    1 
ATOM   15812 C  CG    . ASP D 2 339 ? 92.954  129.941 156.412 1.00 31.35 ?  318 ASP D CG    1 
ATOM   15813 O  OD1   . ASP D 2 339 ? 92.201  130.934 156.319 1.00 29.84 ?  318 ASP D OD1   1 
ATOM   15814 O  OD2   . ASP D 2 339 ? 92.618  128.797 156.039 1.00 30.37 -1 318 ASP D OD2   1 
ATOM   15815 N  N     . ASP D 2 340 ? 97.565  130.691 155.683 1.00 24.54 ?  319 ASP D N     1 
ATOM   15816 C  CA    . ASP D 2 340 ? 98.994  130.898 155.850 1.00 16.40 ?  319 ASP D CA    1 
ATOM   15817 C  C     . ASP D 2 340 ? 99.401  132.308 155.460 1.00 13.50 ?  319 ASP D C     1 
ATOM   15818 O  O     . ASP D 2 340 ? 100.551 132.700 155.679 1.00 33.12 ?  319 ASP D O     1 
ATOM   15819 C  CB    . ASP D 2 340 ? 99.776  129.881 155.016 1.00 15.31 ?  319 ASP D CB    1 
ATOM   15820 C  CG    . ASP D 2 340 ? 99.629  128.465 155.532 1.00 20.12 ?  319 ASP D CG    1 
ATOM   15821 O  OD1   . ASP D 2 340 ? 99.453  128.290 156.756 1.00 32.00 ?  319 ASP D OD1   1 
ATOM   15822 O  OD2   . ASP D 2 340 ? 99.688  127.526 154.712 1.00 22.25 -1 319 ASP D OD2   1 
ATOM   15823 N  N     . PHE D 2 341 ? 98.471  133.073 154.884 1.00 10.33 ?  320 PHE D N     1 
ATOM   15824 C  CA    . PHE D 2 341 ? 98.691  134.464 154.520 1.00 15.27 ?  320 PHE D CA    1 
ATOM   15825 C  C     . PHE D 2 341 ? 98.152  135.411 155.582 1.00 19.34 ?  320 PHE D C     1 
ATOM   15826 O  O     . PHE D 2 341 ? 98.247  136.632 155.415 1.00 16.81 ?  320 PHE D O     1 
ATOM   15827 C  CB    . PHE D 2 341 ? 98.026  134.771 153.174 1.00 19.36 ?  320 PHE D CB    1 
ATOM   15828 C  CG    . PHE D 2 341 ? 98.609  134.011 152.019 1.00 13.21 ?  320 PHE D CG    1 
ATOM   15829 C  CD1   . PHE D 2 341 ? 99.653  134.538 151.279 1.00 12.45 ?  320 PHE D CD1   1 
ATOM   15830 C  CD2   . PHE D 2 341 ? 98.113  132.766 151.675 1.00 11.41 ?  320 PHE D CD2   1 
ATOM   15831 C  CE1   . PHE D 2 341 ? 100.186 133.839 150.215 1.00 11.53 ?  320 PHE D CE1   1 
ATOM   15832 C  CE2   . PHE D 2 341 ? 98.645  132.063 150.614 1.00 15.13 ?  320 PHE D CE2   1 
ATOM   15833 C  CZ    . PHE D 2 341 ? 99.683  132.601 149.884 1.00 8.25  ?  320 PHE D CZ    1 
ATOM   15834 N  N     . TYR D 2 342 ? 97.588  134.880 156.664 1.00 12.30 ?  321 TYR D N     1 
ATOM   15835 C  CA    . TYR D 2 342 ? 96.963  135.677 157.706 1.00 16.33 ?  321 TYR D CA    1 
ATOM   15836 C  C     . TYR D 2 342 ? 97.586  135.317 159.044 1.00 22.82 ?  321 TYR D C     1 
ATOM   15837 O  O     . TYR D 2 342 ? 97.902  134.150 159.298 1.00 19.28 ?  321 TYR D O     1 
ATOM   15838 C  CB    . TYR D 2 342 ? 95.449  135.443 157.745 1.00 12.46 ?  321 TYR D CB    1 
ATOM   15839 C  CG    . TYR D 2 342 ? 94.754  135.790 156.449 1.00 15.87 ?  321 TYR D CG    1 
ATOM   15840 C  CD1   . TYR D 2 342 ? 94.371  137.094 156.169 1.00 18.56 ?  321 TYR D CD1   1 
ATOM   15841 C  CD2   . TYR D 2 342 ? 94.488  134.811 155.500 1.00 15.63 ?  321 TYR D CD2   1 
ATOM   15842 C  CE1   . TYR D 2 342 ? 93.739  137.414 154.984 1.00 14.14 ?  321 TYR D CE1   1 
ATOM   15843 C  CE2   . TYR D 2 342 ? 93.856  135.122 154.312 1.00 15.01 ?  321 TYR D CE2   1 
ATOM   15844 C  CZ    . TYR D 2 342 ? 93.484  136.424 154.059 1.00 17.53 ?  321 TYR D CZ    1 
ATOM   15845 O  OH    . TYR D 2 342 ? 92.853  136.738 152.877 1.00 21.36 ?  321 TYR D OH    1 
ATOM   15846 N  N     . PHE D 2 343 ? 97.767  136.323 159.893 1.00 12.45 ?  322 PHE D N     1 
ATOM   15847 C  CA    . PHE D 2 343 ? 98.459  136.132 161.160 1.00 16.01 ?  322 PHE D CA    1 
ATOM   15848 C  C     . PHE D 2 343 ? 97.770  136.899 162.283 1.00 27.60 ?  322 PHE D C     1 
ATOM   15849 O  O     . PHE D 2 343 ? 97.090  137.897 162.043 1.00 22.19 ?  322 PHE D O     1 
ATOM   15850 C  CB    . PHE D 2 343 ? 99.921  136.571 161.033 1.00 18.28 ?  322 PHE D CB    1 
ATOM   15851 C  CG    . PHE D 2 343 ? 100.611 136.027 159.814 1.00 19.26 ?  322 PHE D CG    1 
ATOM   15852 C  CD1   . PHE D 2 343 ? 101.213 134.781 159.838 1.00 20.02 ?  322 PHE D CD1   1 
ATOM   15853 C  CD2   . PHE D 2 343 ? 100.641 136.756 158.636 1.00 13.80 ?  322 PHE D CD2   1 
ATOM   15854 C  CE1   . PHE D 2 343 ? 101.839 134.278 158.716 1.00 12.20 ?  322 PHE D CE1   1 
ATOM   15855 C  CE2   . PHE D 2 343 ? 101.263 136.257 157.513 1.00 9.90  ?  322 PHE D CE2   1 
ATOM   15856 C  CZ    . PHE D 2 343 ? 101.863 135.016 157.552 1.00 11.36 ?  322 PHE D CZ    1 
HETATM 15857 P  PG    . ATP E 3 .   ? 106.649 136.923 79.855  1.00 68.91 ?  801 ATP A PG    1 
HETATM 15858 O  O1G   . ATP E 3 .   ? 105.494 137.401 79.041  1.00 61.99 ?  801 ATP A O1G   1 
HETATM 15859 O  O2G   . ATP E 3 .   ? 107.948 137.693 79.592  1.00 61.48 -1 801 ATP A O2G   1 
HETATM 15860 O  O3G   . ATP E 3 .   ? 106.374 136.906 81.362  1.00 57.91 ?  801 ATP A O3G   1 
HETATM 15861 P  PB    . ATP E 3 .   ? 108.089 134.567 78.689  1.00 68.42 ?  801 ATP A PB    1 
HETATM 15862 O  O1B   . ATP E 3 .   ? 108.003 134.804 77.234  1.00 59.48 -1 801 ATP A O1B   1 
HETATM 15863 O  O2B   . ATP E 3 .   ? 109.448 134.860 79.326  1.00 59.06 ?  801 ATP A O2B   1 
HETATM 15864 O  O3B   . ATP E 3 .   ? 107.002 135.405 79.494  1.00 62.04 ?  801 ATP A O3B   1 
HETATM 15865 P  PA    . ATP E 3 .   ? 107.716 132.168 80.382  1.00 63.87 ?  801 ATP A PA    1 
HETATM 15866 O  O1A   . ATP E 3 .   ? 108.771 131.136 80.313  1.00 60.02 -1 801 ATP A O1A   1 
HETATM 15867 O  O2A   . ATP E 3 .   ? 106.299 131.626 80.573  1.00 58.33 ?  801 ATP A O2A   1 
HETATM 15868 O  O3A   . ATP E 3 .   ? 107.699 133.072 79.072  1.00 62.45 ?  801 ATP A O3A   1 
HETATM 15869 O  "O5'" . ATP E 3 .   ? 108.007 133.209 81.531  1.00 59.78 ?  801 ATP A "O5'" 1 
HETATM 15870 C  "C5'" . ATP E 3 .   ? 106.963 133.654 82.422  1.00 58.13 ?  801 ATP A "C5'" 1 
HETATM 15871 C  "C4'" . ATP E 3 .   ? 107.569 134.544 83.477  1.00 59.51 ?  801 ATP A "C4'" 1 
HETATM 15872 O  "O4'" . ATP E 3 .   ? 107.957 133.744 84.617  1.00 62.13 ?  801 ATP A "O4'" 1 
HETATM 15873 C  "C3'" . ATP E 3 .   ? 108.832 135.288 83.053  1.00 57.82 ?  801 ATP A "C3'" 1 
HETATM 15874 O  "O3'" . ATP E 3 .   ? 108.514 136.545 82.468  1.00 58.51 ?  801 ATP A "O3'" 1 
HETATM 15875 C  "C2'" . ATP E 3 .   ? 109.572 135.458 84.380  1.00 58.31 ?  801 ATP A "C2'" 1 
HETATM 15876 O  "O2'" . ATP E 3 .   ? 109.076 136.564 85.123  1.00 58.66 ?  801 ATP A "O2'" 1 
HETATM 15877 C  "C1'" . ATP E 3 .   ? 109.235 134.140 85.082  1.00 58.50 ?  801 ATP A "C1'" 1 
HETATM 15878 N  N9    . ATP E 3 .   ? 110.179 133.062 84.808  1.00 58.48 ?  801 ATP A N9    1 
HETATM 15879 C  C8    . ATP E 3 .   ? 109.927 131.887 84.149  1.00 58.26 ?  801 ATP A C8    1 
HETATM 15880 N  N7    . ATP E 3 .   ? 110.968 131.097 84.047  1.00 56.05 ?  801 ATP A N7    1 
HETATM 15881 C  C5    . ATP E 3 .   ? 111.978 131.801 84.685  1.00 58.55 ?  801 ATP A C5    1 
HETATM 15882 C  C6    . ATP E 3 .   ? 113.335 131.510 84.923  1.00 56.46 ?  801 ATP A C6    1 
HETATM 15883 N  N6    . ATP E 3 .   ? 113.937 130.384 84.529  1.00 55.74 ?  801 ATP A N6    1 
HETATM 15884 N  N1    . ATP E 3 .   ? 114.066 132.429 85.592  1.00 57.23 ?  801 ATP A N1    1 
HETATM 15885 C  C2    . ATP E 3 .   ? 113.474 133.560 85.986  1.00 55.67 ?  801 ATP A C2    1 
HETATM 15886 N  N3    . ATP E 3 .   ? 112.206 133.941 85.820  1.00 57.17 ?  801 ATP A N3    1 
HETATM 15887 C  C4    . ATP E 3 .   ? 111.506 133.014 85.159  1.00 59.07 ?  801 ATP A C4    1 
HETATM 15888 P  PB    . GDP F 4 .   ? 105.489 150.805 81.636  1.00 70.96 ?  802 GDP A PB    1 
HETATM 15889 O  O1B   . GDP F 4 .   ? 106.591 149.930 81.091  1.00 59.03 ?  802 GDP A O1B   1 
HETATM 15890 O  O2B   . GDP F 4 .   ? 105.094 151.821 80.592  1.00 60.98 -1 802 GDP A O2B   1 
HETATM 15891 O  O3B   . GDP F 4 .   ? 104.293 149.953 81.990  1.00 60.51 ?  802 GDP A O3B   1 
HETATM 15892 O  O3A   . GDP F 4 .   ? 106.036 151.574 82.939  1.00 58.04 ?  802 GDP A O3A   1 
HETATM 15893 P  PA    . GDP F 4 .   ? 106.382 150.782 84.296  1.00 62.53 ?  802 GDP A PA    1 
HETATM 15894 O  O1A   . GDP F 4 .   ? 106.048 151.623 85.504  1.00 60.36 -1 802 GDP A O1A   1 
HETATM 15895 O  O2A   . GDP F 4 .   ? 105.659 149.459 84.363  1.00 57.51 ?  802 GDP A O2A   1 
HETATM 15896 O  "O5'" . GDP F 4 .   ? 107.973 150.560 84.190  1.00 58.41 ?  802 GDP A "O5'" 1 
HETATM 15897 C  "C5'" . GDP F 4 .   ? 108.745 150.415 85.375  1.00 58.74 ?  802 GDP A "C5'" 1 
HETATM 15898 C  "C4'" . GDP F 4 .   ? 109.721 149.258 85.238  1.00 56.36 ?  802 GDP A "C4'" 1 
HETATM 15899 O  "O4'" . GDP F 4 .   ? 109.929 148.701 86.538  1.00 56.52 ?  802 GDP A "O4'" 1 
HETATM 15900 C  "C3'" . GDP F 4 .   ? 109.158 148.168 84.344  1.00 58.64 ?  802 GDP A "C3'" 1 
HETATM 15901 O  "O3'" . GDP F 4 .   ? 110.042 147.935 83.244  1.00 59.90 ?  802 GDP A "O3'" 1 
HETATM 15902 C  "C2'" . GDP F 4 .   ? 109.063 146.921 85.199  1.00 57.17 ?  802 GDP A "C2'" 1 
HETATM 15903 O  "O2'" . GDP F 4 .   ? 109.777 145.847 84.583  1.00 58.14 ?  802 GDP A "O2'" 1 
HETATM 15904 C  "C1'" . GDP F 4 .   ? 109.710 147.288 86.525  1.00 54.02 ?  802 GDP A "C1'" 1 
HETATM 15905 N  N9    . GDP F 4 .   ? 108.891 146.876 87.696  1.00 54.87 ?  802 GDP A N9    1 
HETATM 15906 C  C8    . GDP F 4 .   ? 109.398 146.368 88.832  1.00 56.62 ?  802 GDP A C8    1 
HETATM 15907 N  N7    . GDP F 4 .   ? 108.425 146.087 89.732  1.00 56.41 ?  802 GDP A N7    1 
HETATM 15908 C  C5    . GDP F 4 .   ? 107.253 146.435 89.174  1.00 56.75 ?  802 GDP A C5    1 
HETATM 15909 C  C6    . GDP F 4 .   ? 105.831 146.404 89.589  1.00 57.45 ?  802 GDP A C6    1 
HETATM 15910 O  O6    . GDP F 4 .   ? 105.500 145.972 90.714  1.00 57.90 ?  802 GDP A O6    1 
HETATM 15911 N  N1    . GDP F 4 .   ? 104.914 146.851 88.725  1.00 57.76 ?  802 GDP A N1    1 
HETATM 15912 C  C2    . GDP F 4 .   ? 105.245 147.322 87.509  1.00 56.48 ?  802 GDP A C2    1 
HETATM 15913 N  N2    . GDP F 4 .   ? 104.258 147.756 86.692  1.00 57.02 ?  802 GDP A N2    1 
HETATM 15914 N  N3    . GDP F 4 .   ? 106.527 147.379 87.064  1.00 58.50 ?  802 GDP A N3    1 
HETATM 15915 C  C4    . GDP F 4 .   ? 107.561 146.958 87.835  1.00 57.68 ?  802 GDP A C4    1 
HETATM 15916 P  PA    . TTP G 5 .   ? 145.003 144.955 133.428 1.00 19.24 ?  803 TTP A PA    1 
HETATM 15917 O  O1A   . TTP G 5 .   ? 143.542 145.021 133.796 1.00 19.64 -1 803 TTP A O1A   1 
HETATM 15918 O  O2A   . TTP G 5 .   ? 145.413 146.147 132.602 1.00 31.54 ?  803 TTP A O2A   1 
HETATM 15919 O  O3A   . TTP G 5 .   ? 145.935 144.823 134.730 1.00 30.64 ?  803 TTP A O3A   1 
HETATM 15920 P  PB    . TTP G 5 .   ? 146.280 146.082 135.665 1.00 31.57 ?  803 TTP A PB    1 
HETATM 15921 O  O1B   . TTP G 5 .   ? 146.301 147.376 134.892 1.00 27.79 -1 803 TTP A O1B   1 
HETATM 15922 O  O2B   . TTP G 5 .   ? 145.303 146.166 136.810 1.00 31.36 ?  803 TTP A O2B   1 
HETATM 15923 O  O3B   . TTP G 5 .   ? 147.745 145.700 136.204 1.00 27.98 ?  803 TTP A O3B   1 
HETATM 15924 P  PG    . TTP G 5 .   ? 148.978 145.518 135.185 1.00 26.76 ?  803 TTP A PG    1 
HETATM 15925 O  O1G   . TTP G 5 .   ? 148.804 146.420 133.988 1.00 32.07 ?  803 TTP A O1G   1 
HETATM 15926 O  O2G   . TTP G 5 .   ? 150.271 145.847 135.885 1.00 34.92 -1 803 TTP A O2G   1 
HETATM 15927 O  O3G   . TTP G 5 .   ? 149.023 144.082 134.728 1.00 18.37 ?  803 TTP A O3G   1 
HETATM 15928 O  "O5'" . TTP G 5 .   ? 145.339 143.591 132.654 1.00 23.88 ?  803 TTP A "O5'" 1 
HETATM 15929 C  "C5'" . TTP G 5 .   ? 145.665 142.431 133.408 1.00 21.43 ?  803 TTP A "C5'" 1 
HETATM 15930 C  "C4'" . TTP G 5 .   ? 145.539 141.204 132.524 1.00 24.35 ?  803 TTP A "C4'" 1 
HETATM 15931 O  "O4'" . TTP G 5 .   ? 145.156 140.105 133.348 1.00 31.28 ?  803 TTP A "O4'" 1 
HETATM 15932 C  "C3'" . TTP G 5 .   ? 144.459 141.410 131.480 1.00 26.08 ?  803 TTP A "C3'" 1 
HETATM 15933 O  "O3'" . TTP G 5 .   ? 145.002 141.260 130.166 1.00 24.00 ?  803 TTP A "O3'" 1 
HETATM 15934 C  "C2'" . TTP G 5 .   ? 143.424 140.336 131.728 1.00 25.88 ?  803 TTP A "C2'" 1 
HETATM 15935 C  "C1'" . TTP G 5 .   ? 143.943 139.507 132.892 1.00 25.26 ?  803 TTP A "C1'" 1 
HETATM 15936 N  N1    . TTP G 5 .   ? 142.968 139.517 133.981 1.00 25.70 ?  803 TTP A N1    1 
HETATM 15937 C  C2    . TTP G 5 .   ? 142.426 138.301 134.451 1.00 25.54 ?  803 TTP A C2    1 
HETATM 15938 O  O2    . TTP G 5 .   ? 142.786 137.226 133.927 1.00 22.46 ?  803 TTP A O2    1 
HETATM 15939 N  N3    . TTP G 5 .   ? 141.533 138.278 135.448 1.00 24.38 ?  803 TTP A N3    1 
HETATM 15940 C  C4    . TTP G 5 .   ? 141.130 139.412 136.026 1.00 29.17 ?  803 TTP A C4    1 
HETATM 15941 O  O4    . TTP G 5 .   ? 140.298 139.389 136.957 1.00 37.02 ?  803 TTP A O4    1 
HETATM 15942 C  C5    . TTP G 5 .   ? 141.685 140.702 135.552 1.00 28.26 ?  803 TTP A C5    1 
HETATM 15943 C  C5M   . TTP G 5 .   ? 141.258 142.001 136.178 1.00 26.39 ?  803 TTP A C5M   1 
HETATM 15944 C  C6    . TTP G 5 .   ? 142.607 140.686 134.518 1.00 27.03 ?  803 TTP A C6    1 
HETATM 15945 MG MG    . MG  H 6 .   ? 147.283 146.969 132.249 1.00 18.30 ?  804 MG  A MG    1 
HETATM 15946 P  PA    . TTP I 5 .   ? 119.141 147.517 122.255 1.00 24.11 ?  801 TTP B PA    1 
HETATM 15947 O  O1A   . TTP I 5 .   ? 120.629 147.707 122.405 1.00 30.19 -1 801 TTP B O1A   1 
HETATM 15948 O  O2A   . TTP I 5 .   ? 118.384 148.638 122.922 1.00 22.18 ?  801 TTP B O2A   1 
HETATM 15949 O  O3A   . TTP I 5 .   ? 118.740 147.353 120.708 1.00 32.55 ?  801 TTP B O3A   1 
HETATM 15950 P  PB    . TTP I 5 .   ? 118.138 148.577 119.859 1.00 29.61 ?  801 TTP B PB    1 
HETATM 15951 O  O1B   . TTP I 5 .   ? 118.289 149.904 120.558 1.00 32.07 -1 801 TTP B O1B   1 
HETATM 15952 O  O2B   . TTP I 5 .   ? 118.795 148.625 118.502 1.00 29.33 ?  801 TTP B O2B   1 
HETATM 15953 O  O3B   . TTP I 5 .   ? 116.594 148.139 119.743 1.00 19.28 ?  801 TTP B O3B   1 
HETATM 15954 P  PG    . TTP I 5 .   ? 115.425 149.042 120.383 1.00 31.34 ?  801 TTP B PG    1 
HETATM 15955 O  O1G   . TTP I 5 .   ? 115.250 150.302 119.572 1.00 34.07 ?  801 TTP B O1G   1 
HETATM 15956 O  O2G   . TTP I 5 .   ? 114.135 148.261 120.382 1.00 23.32 -1 801 TTP B O2G   1 
HETATM 15957 O  O3G   . TTP I 5 .   ? 115.787 149.402 121.802 1.00 34.53 ?  801 TTP B O3G   1 
HETATM 15958 O  "O5'" . TTP I 5 .   ? 118.672 146.107 122.864 1.00 24.93 ?  801 TTP B "O5'" 1 
HETATM 15959 C  "C5'" . TTP I 5 .   ? 117.646 146.096 123.849 1.00 24.44 ?  801 TTP B "C5'" 1 
HETATM 15960 C  "C4'" . TTP I 5 .   ? 117.451 144.689 124.388 1.00 24.00 ?  801 TTP B "C4'" 1 
HETATM 15961 O  "O4'" . TTP I 5 .   ? 117.572 143.734 123.335 1.00 28.53 ?  801 TTP B "O4'" 1 
HETATM 15962 C  "C3'" . TTP I 5 .   ? 118.511 144.330 125.411 1.00 27.23 ?  801 TTP B "C3'" 1 
HETATM 15963 O  "O3'" . TTP I 5 .   ? 118.008 144.495 126.740 1.00 27.74 ?  801 TTP B "O3'" 1 
HETATM 15964 C  "C2'" . TTP I 5 .   ? 118.833 142.874 125.148 1.00 27.40 ?  801 TTP B "C2'" 1 
HETATM 15965 C  "C1'" . TTP I 5 .   ? 118.138 142.524 123.841 1.00 29.90 ?  801 TTP B "C1'" 1 
HETATM 15966 N  N1    . TTP I 5 .   ? 119.110 141.971 122.900 1.00 28.87 ?  801 TTP B N1    1 
HETATM 15967 C  C2    . TTP I 5 .   ? 119.319 140.576 122.868 1.00 27.67 ?  801 TTP B C2    1 
HETATM 15968 O  O2    . TTP I 5 .   ? 118.662 139.844 123.637 1.00 29.22 ?  801 TTP B O2    1 
HETATM 15969 N  N3    . TTP I 5 .   ? 120.199 140.018 122.026 1.00 25.56 ?  801 TTP B N3    1 
HETATM 15970 C  C4    . TTP I 5 .   ? 120.911 140.778 121.192 1.00 29.58 ?  801 TTP B C4    1 
HETATM 15971 O  O4    . TTP I 5 .   ? 121.732 140.257 120.410 1.00 38.14 ?  801 TTP B O4    1 
HETATM 15972 C  C5    . TTP I 5 .   ? 120.715 142.248 121.209 1.00 24.40 ?  801 TTP B C5    1 
HETATM 15973 C  C5M   . TTP I 5 .   ? 121.500 143.137 120.284 1.00 26.91 ?  801 TTP B C5M   1 
HETATM 15974 C  C6    . TTP I 5 .   ? 119.795 142.789 122.094 1.00 27.32 ?  801 TTP B C6    1 
HETATM 15975 MG MG    . MG  J 6 .   ? 117.408 150.423 122.841 1.00 37.62 ?  802 MG  B MG    1 
HETATM 15976 P  PG    . ATP K 3 .   ? 152.686 140.375 178.848 1.00 70.08 ?  803 ATP B PG    1 
HETATM 15977 O  O1G   . ATP K 3 .   ? 152.753 140.774 177.413 1.00 62.41 ?  803 ATP B O1G   1 
HETATM 15978 O  O2G   . ATP K 3 .   ? 152.762 141.560 179.817 1.00 61.28 -1 803 ATP B O2G   1 
HETATM 15979 O  O3G   . ATP K 3 .   ? 151.459 139.524 179.195 1.00 60.15 ?  803 ATP B O3G   1 
HETATM 15980 P  PB    . ATP K 3 .   ? 154.261 137.969 179.705 1.00 67.84 ?  803 ATP B PB    1 
HETATM 15981 O  O1B   . ATP K 3 .   ? 155.518 137.467 179.116 1.00 59.55 -1 803 ATP B O1B   1 
HETATM 15982 O  O2B   . ATP K 3 .   ? 154.186 137.949 181.232 1.00 61.48 ?  803 ATP B O2B   1 
HETATM 15983 O  O3B   . ATP K 3 .   ? 153.938 139.458 179.237 1.00 62.14 ?  803 ATP B O3B   1 
HETATM 15984 P  PA    . ATP K 3 .   ? 152.583 136.434 177.811 1.00 67.77 ?  803 ATP B PA    1 
HETATM 15985 O  O1A   . ATP K 3 .   ? 151.215 136.800 177.394 1.00 60.17 -1 803 ATP B O1A   1 
HETATM 15986 O  O2A   . ATP K 3 .   ? 152.820 134.939 178.022 1.00 60.55 ?  803 ATP B O2A   1 
HETATM 15987 O  O3A   . ATP K 3 .   ? 152.998 137.169 179.159 1.00 61.79 ?  803 ATP B O3A   1 
HETATM 15988 O  "O5'" . ATP K 3 .   ? 153.654 136.964 176.778 1.00 60.51 ?  803 ATP B "O5'" 1 
HETATM 15989 C  "C5'" . ATP K 3 .   ? 153.767 136.394 175.457 1.00 57.17 ?  803 ATP B "C5'" 1 
HETATM 15990 C  "C4'" . ATP K 3 .   ? 153.466 137.461 174.435 1.00 59.72 ?  803 ATP B "C4'" 1 
HETATM 15991 O  "O4'" . ATP K 3 .   ? 152.752 136.875 173.324 1.00 60.83 ?  803 ATP B "O4'" 1 
HETATM 15992 C  "C3'" . ATP K 3 .   ? 152.590 138.607 174.930 1.00 58.64 ?  803 ATP B "C3'" 1 
HETATM 15993 O  "O3'" . ATP K 3 .   ? 153.382 139.659 175.469 1.00 58.59 ?  803 ATP B "O3'" 1 
HETATM 15994 C  "C2'" . ATP K 3 .   ? 151.865 139.044 173.656 1.00 58.56 ?  803 ATP B "C2'" 1 
HETATM 15995 O  "O2'" . ATP K 3 .   ? 152.664 139.913 172.863 1.00 59.99 ?  803 ATP B "O2'" 1 
HETATM 15996 C  "C1'" . ATP K 3 .   ? 151.664 137.702 172.949 1.00 57.94 ?  803 ATP B "C1'" 1 
HETATM 15997 N  N9    . ATP K 3 .   ? 150.425 137.020 173.307 1.00 59.22 ?  803 ATP B N9    1 
HETATM 15998 C  C8    . ATP K 3 .   ? 150.284 135.919 174.110 1.00 57.41 ?  803 ATP B C8    1 
HETATM 15999 N  N7    . ATP K 3 .   ? 149.046 135.518 174.257 1.00 58.19 ?  803 ATP B N7    1 
HETATM 16000 C  C5    . ATP K 3 .   ? 148.317 136.419 173.496 1.00 58.18 ?  803 ATP B C5    1 
HETATM 16001 C  C6    . ATP K 3 .   ? 146.939 136.545 173.231 1.00 55.35 ?  803 ATP B C6    1 
HETATM 16002 N  N6    . ATP K 3 .   ? 146.008 135.726 173.728 1.00 55.86 ?  803 ATP B N6    1 
HETATM 16003 N  N1    . ATP K 3 .   ? 146.544 137.557 172.428 1.00 57.37 ?  803 ATP B N1    1 
HETATM 16004 C  C2    . ATP K 3 .   ? 147.468 138.382 171.930 1.00 55.85 ?  803 ATP B C2    1 
HETATM 16005 N  N3    . ATP K 3 .   ? 148.790 138.360 172.107 1.00 57.67 ?  803 ATP B N3    1 
HETATM 16006 C  C4    . ATP K 3 .   ? 149.154 137.351 172.904 1.00 59.74 ?  803 ATP B C4    1 
HETATM 16007 P  PB    . GDP L 4 .   ? 160.970 153.041 171.969 1.00 69.13 ?  804 GDP B PB    1 
HETATM 16008 O  O1B   . GDP L 4 .   ? 161.571 151.672 172.173 1.00 61.24 ?  804 GDP B O1B   1 
HETATM 16009 O  O2B   . GDP L 4 .   ? 161.053 153.822 173.258 1.00 59.98 -1 804 GDP B O2B   1 
HETATM 16010 O  O3B   . GDP L 4 .   ? 161.728 153.769 170.884 1.00 59.87 ?  804 GDP B O3B   1 
HETATM 16011 O  O3A   . GDP L 4 .   ? 159.425 152.894 171.549 1.00 58.19 ?  804 GDP B O3A   1 
HETATM 16012 P  PA    . GDP L 4 .   ? 158.980 152.278 170.130 1.00 64.69 ?  804 GDP B PA    1 
HETATM 16013 O  O1A   . GDP L 4 .   ? 159.293 153.216 168.990 1.00 59.39 -1 804 GDP B O1A   1 
HETATM 16014 O  O2A   . GDP L 4 .   ? 159.630 150.935 169.901 1.00 58.30 ?  804 GDP B O2A   1 
HETATM 16015 O  "O5'" . GDP L 4 .   ? 157.392 152.124 170.329 1.00 61.40 ?  804 GDP B "O5'" 1 
HETATM 16016 C  "C5'" . GDP L 4 .   ? 156.480 152.418 169.276 1.00 57.46 ?  804 GDP B "C5'" 1 
HETATM 16017 C  "C4'" . GDP L 4 .   ? 155.187 151.660 169.533 1.00 55.92 ?  804 GDP B "C4'" 1 
HETATM 16018 O  "O4'" . GDP L 4 .   ? 154.875 150.914 168.357 1.00 58.58 ?  804 GDP B "O4'" 1 
HETATM 16019 C  "C3'" . GDP L 4 .   ? 155.364 150.678 170.680 1.00 59.02 ?  804 GDP B "C3'" 1 
HETATM 16020 O  "O3'" . GDP L 4 .   ? 154.303 150.825 171.629 1.00 58.82 ?  804 GDP B "O3'" 1 
HETATM 16021 C  "C2'" . GDP L 4 .   ? 155.311 149.299 170.060 1.00 56.94 ?  804 GDP B "C2'" 1 
HETATM 16022 O  "O2'" . GDP L 4 .   ? 154.449 148.445 170.815 1.00 59.26 ?  804 GDP B "O2'" 1 
HETATM 16023 C  "C1'" . GDP L 4 .   ? 154.757 149.523 168.662 1.00 55.87 ?  804 GDP B "C1'" 1 
HETATM 16024 N  N9    . GDP L 4 .   ? 155.444 148.709 167.625 1.00 56.16 ?  804 GDP B N9    1 
HETATM 16025 C  C8    . GDP L 4 .   ? 154.826 148.156 166.566 1.00 57.86 ?  804 GDP B C8    1 
HETATM 16026 N  N7    . GDP L 4 .   ? 155.698 147.478 165.784 1.00 59.36 ?  804 GDP B N7    1 
HETATM 16027 C  C5    . GDP L 4 .   ? 156.917 147.604 166.336 1.00 59.05 ?  804 GDP B C5    1 
HETATM 16028 C  C6    . GDP L 4 .   ? 158.284 147.134 166.014 1.00 58.07 ?  804 GDP B C6    1 
HETATM 16029 O  O6    . GDP L 4 .   ? 158.498 146.437 164.999 1.00 59.08 ?  804 GDP B O6    1 
HETATM 16030 N  N1    . GDP L 4 .   ? 159.279 147.478 166.839 1.00 57.10 ?  804 GDP B N1    1 
HETATM 16031 C  C2    . GDP L 4 .   ? 159.073 148.227 167.936 1.00 57.92 ?  804 GDP B C2    1 
HETATM 16032 N  N2    . GDP L 4 .   ? 160.131 148.533 168.725 1.00 58.60 ?  804 GDP B N2    1 
HETATM 16033 N  N3    . GDP L 4 .   ? 157.849 148.691 168.291 1.00 60.62 ?  804 GDP B N3    1 
HETATM 16034 C  C4    . GDP L 4 .   ? 156.749 148.420 167.548 1.00 59.26 ?  804 GDP B C4    1 
HETATM 16035 MN MN    . MN  M 7 .   ? 117.090 92.147  123.196 0.85 25.05 ?  401 MN  C MN    1 
HETATM 16036 MN MN    . MN  N 7 .   ? 115.760 95.494  124.189 0.85 26.37 ?  402 MN  C MN    1 
HETATM 16037 MN MN    . MN  O 7 .   ? 135.774 97.391  137.512 1.00 22.51 ?  401 MN  D MN    1 
HETATM 16038 MN MN    . MN  P 7 .   ? 137.994 96.065  134.577 1.00 24.72 ?  402 MN  D MN    1 
# 
