data_9BZ2
# 
_entry.id   9BZ2 
# 
_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   9BZ2         pdb_00009bz2 10.2210/pdb9bz2/pdb 
WWPDB D_1000284420 ?            ?                   
EMDB  EMD-45051    ?            ?                   
# 
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                        9BZ2 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB .                                                                                             EMD-45037 'consensus EM volume' 
EMDB 'Class 14 model for turnover condition of Bacillus subtilis ribonucleotide reductase complex' EMD-45051 
'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                   9BZ2 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BZ2 
_struct.title                        'Class 14 model for turnover condition of Bacillus subtilis ribonucleotide reductase complex' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BZ2 
_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 9BZ2 A 1  ? 700 ? P50620 1 ? 700 ? 1 700 
2 1 9BZ2 B 1  ? 700 ? P50620 1 ? 700 ? 1 700 
3 2 9BZ2 C 22 ? 350 ? P50621 1 ? 329 ? 1 329 
4 2 9BZ2 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 9BZ2 MET C 1  ? UNP P50621 ? ? 'initiating methionine' -20 1  
3 9BZ2 GLY C 2  ? UNP P50621 ? ? 'expression tag'        -19 2  
3 9BZ2 SER C 3  ? UNP P50621 ? ? 'expression tag'        -18 3  
3 9BZ2 SER C 4  ? UNP P50621 ? ? 'expression tag'        -17 4  
3 9BZ2 HIS C 5  ? UNP P50621 ? ? 'expression tag'        -16 5  
3 9BZ2 HIS C 6  ? UNP P50621 ? ? 'expression tag'        -15 6  
3 9BZ2 HIS C 7  ? UNP P50621 ? ? 'expression tag'        -14 7  
3 9BZ2 HIS C 8  ? UNP P50621 ? ? 'expression tag'        -13 8  
3 9BZ2 HIS C 9  ? UNP P50621 ? ? 'expression tag'        -12 9  
3 9BZ2 HIS C 10 ? UNP P50621 ? ? 'expression tag'        -11 10 
3 9BZ2 SER C 11 ? UNP P50621 ? ? 'expression tag'        -10 11 
3 9BZ2 SER C 12 ? UNP P50621 ? ? 'expression tag'        -9  12 
3 9BZ2 GLY C 13 ? UNP P50621 ? ? 'expression tag'        -8  13 
3 9BZ2 LEU C 14 ? UNP P50621 ? ? 'expression tag'        -7  14 
3 9BZ2 VAL C 15 ? UNP P50621 ? ? 'expression tag'        -6  15 
3 9BZ2 PRO C 16 ? UNP P50621 ? ? 'expression tag'        -5  16 
3 9BZ2 ARG C 17 ? UNP P50621 ? ? 'expression tag'        -4  17 
3 9BZ2 GLY C 18 ? UNP P50621 ? ? 'expression tag'        -3  18 
3 9BZ2 SER C 19 ? UNP P50621 ? ? 'expression tag'        -2  19 
3 9BZ2 HIS C 20 ? UNP P50621 ? ? 'expression tag'        -1  20 
3 9BZ2 MET C 21 ? UNP P50621 ? ? 'expression tag'        0   21 
4 9BZ2 MET D 1  ? UNP P50621 ? ? 'initiating methionine' -20 22 
4 9BZ2 GLY D 2  ? UNP P50621 ? ? 'expression tag'        -19 23 
4 9BZ2 SER D 3  ? UNP P50621 ? ? 'expression tag'        -18 24 
4 9BZ2 SER D 4  ? UNP P50621 ? ? 'expression tag'        -17 25 
4 9BZ2 HIS D 5  ? UNP P50621 ? ? 'expression tag'        -16 26 
4 9BZ2 HIS D 6  ? UNP P50621 ? ? 'expression tag'        -15 27 
4 9BZ2 HIS D 7  ? UNP P50621 ? ? 'expression tag'        -14 28 
4 9BZ2 HIS D 8  ? UNP P50621 ? ? 'expression tag'        -13 29 
4 9BZ2 HIS D 9  ? UNP P50621 ? ? 'expression tag'        -12 30 
4 9BZ2 HIS D 10 ? UNP P50621 ? ? 'expression tag'        -11 31 
4 9BZ2 SER D 11 ? UNP P50621 ? ? 'expression tag'        -10 32 
4 9BZ2 SER D 12 ? UNP P50621 ? ? 'expression tag'        -9  33 
4 9BZ2 GLY D 13 ? UNP P50621 ? ? 'expression tag'        -8  34 
4 9BZ2 LEU D 14 ? UNP P50621 ? ? 'expression tag'        -7  35 
4 9BZ2 VAL D 15 ? UNP P50621 ? ? 'expression tag'        -6  36 
4 9BZ2 PRO D 16 ? UNP P50621 ? ? 'expression tag'        -5  37 
4 9BZ2 ARG D 17 ? UNP P50621 ? ? 'expression tag'        -4  38 
4 9BZ2 GLY D 18 ? UNP P50621 ? ? 'expression tag'        -3  39 
4 9BZ2 SER D 19 ? UNP P50621 ? ? 'expression tag'        -2  40 
4 9BZ2 HIS D 20 ? UNP P50621 ? ? 'expression tag'        -1  41 
4 9BZ2 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 ? ? ? ? ? ? ? 2.501 ? ? 
metalc6  metalc ? ? I TTP .   O3G ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.179 ? ? 
metalc7  metalc ? ? C ASP 87  OD1 ? ? ? 1_555 N MN . MN ? ? C ASP 66  C MN 402 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc8  metalc ? ? C GLU 118 OE2 ? ? ? 1_555 M MN . MN ? ? C GLU 97  C MN 401 1_555 ? ? ? ? ? ? ? 1.960 ? ? 
metalc9  metalc ? ? C GLU 118 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 97  C MN 402 1_555 ? ? ? ? ? ? ? 2.112 ? ? 
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 ? ? ? ? ? ? ? 2.129 ? ? 
metalc12 metalc ? ? C GLU 185 OE2 ? ? ? 1_555 M MN . MN ? ? C GLU 164 C MN 401 1_555 ? ? ? ? ? ? ? 1.965 ? ? 
metalc13 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 M MN . MN ? ? C GLU 198 C MN 401 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc14 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.711 ? ? 
metalc15 metalc ? ? C GLU 219 OE2 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc16 metalc ? ? C HIS 222 ND1 ? ? ? 1_555 M MN . MN ? ? C HIS 201 C MN 401 1_555 ? ? ? ? ? ? ? 2.409 ? ? 
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 ? ? ? ? ? ? ? 2.302 ? ? 
metalc23 metalc ? ? D GLU 185 OE2 ? ? ? 1_555 O MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc24 metalc ? ? D GLU 219 OE1 ? ? ? 1_555 O MN . MN ? ? D GLU 198 D MN 401 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc25 metalc ? ? D GLU 219 OE2 ? ? ? 1_555 P MN . MN ? ? D GLU 198 D MN 402 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc26 metalc ? ? D HIS 222 ND1 ? ? ? 1_555 O MN . MN ? ? D HIS 201 D MN 401 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O2A ? G TTP .   ? A TTP 803 ? 1_555 MG ? H MG . ? A MG 804 ? 1_555 O1B ? G TTP .   ? A TTP 803 ? 1_555 65.7  ? 
2  O2A ? G TTP .   ? A TTP 803 ? 1_555 MG ? H MG . ? A MG 804 ? 1_555 O1G ? G TTP .   ? A TTP 803 ? 1_555 111.2 ? 
3  O1B ? G TTP .   ? A TTP 803 ? 1_555 MG ? H MG . ? A MG 804 ? 1_555 O1G ? G TTP .   ? A TTP 803 ? 1_555 64.8  ? 
4  O2A ? I TTP .   ? B TTP 801 ? 1_555 MG ? J MG . ? B MG 802 ? 1_555 O1B ? I TTP .   ? B TTP 801 ? 1_555 71.7  ? 
5  O2A ? I TTP .   ? B TTP 801 ? 1_555 MG ? J MG . ? B MG 802 ? 1_555 O3G ? I TTP .   ? B TTP 801 ? 1_555 88.0  ? 
6  O1B ? I TTP .   ? B TTP 801 ? 1_555 MG ? J MG . ? B MG 802 ? 1_555 O3G ? I TTP .   ? B TTP 801 ? 1_555 74.3  ? 
7  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 118 ? C GLU 97  ? 1_555 89.6  ? 
8  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 120.6 ? 
9  OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 90.1  ? 
10 OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 138.4 ? 
11 OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 85.1  ? 
12 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 100.7 ? 
13 OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 117.3 ? 
14 OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 137.9 ? 
15 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 101.2 ? 
16 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 53.0  ? 
17 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 141.6 ? 
18 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 87.2  ? 
19 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 64.8  ? 
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 93.3  ? 
29 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 119.5 ? 
30 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 165.7 ? 
31 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 107.0 ? 
32 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 93.8  ? 
33 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 90.2  ? 
34 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 111.3 ? 
35 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 122.1 ? 
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 96.6  ? 
37 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 153.3 ? 
38 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 99.6  ? 
39 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 55.6  ? 
40 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 121.6 ? 
41 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 81.3  ? 
42 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 136.8 ? 
43 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 91.4  ? 
44 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 103.0 ? 
45 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 102.6 ? 
46 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 89.6  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 355 A . ? TYR 355 A PRO 356 A ? PRO 356 A 1 0.43 
2 TYR 355 B . ? TYR 355 B PRO 356 B ? PRO 356 B 1 0.74 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 6 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 3 ? 
AA8 ? 8 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA8 5 6 ? parallel      
AA8 6 7 ? parallel      
AA8 7 8 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLN A 19  ? LYS A 20  ? GLN A 19  LYS A 20  
AA1 2 LYS A 23  ? PHE A 24  ? LYS A 23  PHE A 24  
AA2 1 TYR A 149 ? PRO A 151 ? TYR A 149 PRO A 151 
AA2 2 LEU A 411 ? ASN A 415 ? LEU A 411 ASN A 415 
AA2 3 GLY A 462 ? MET A 466 ? GLY A 462 MET A 466 
AA3 1 CYS A 170 ? GLU A 174 ? CYS A 170 GLU A 174 
AA3 2 GLY A 198 ? ASN A 202 ? GLY A 198 ASN A 202 
AA3 3 GLY A 247 ? ASN A 252 ? GLY A 247 ASN A 252 
AA3 4 LEU A 278 ? ILE A 284 ? LEU A 278 ILE A 284 
AA3 5 TYR A 357 ? PHE A 360 ? TYR A 357 PHE A 360 
AA3 6 THR A 681 ? ILE A 682 ? THR A 681 ILE A 682 
AA4 1 ALA A 298 ? PHE A 301 ? ALA A 298 PHE A 301 
AA4 2 LYS A 334 ? ILE A 337 ? LYS A 334 ILE A 337 
AA5 1 ILE A 601 ? TYR A 606 ? ILE A 601 TYR A 606 
AA5 2 SER A 609 ? PRO A 614 ? SER A 609 PRO A 614 
AA6 1 LEU A 656 ? LEU A 658 ? LEU A 656 LEU A 658 
AA6 2 ALA A 685 ? THR A 687 ? ALA A 685 THR A 687 
AA7 1 TYR B 149 ? PRO B 151 ? TYR B 149 PRO B 151 
AA7 2 SER B 408 ? ASN B 415 ? SER B 408 ASN B 415 
AA7 3 ILE B 461 ? MET B 466 ? ILE B 461 MET B 466 
AA8 1 TYR B 149 ? PRO B 151 ? TYR B 149 PRO B 151 
AA8 2 SER B 408 ? ASN B 415 ? SER B 408 ASN B 415 
AA8 3 CYS B 170 ? GLU B 174 ? CYS B 170 GLU B 174 
AA8 4 GLY B 198 ? ASN B 202 ? GLY B 198 ASN B 202 
AA8 5 GLY B 247 ? ASN B 252 ? GLY B 247 ASN B 252 
AA8 6 LEU B 278 ? ILE B 284 ? LEU B 278 ILE B 284 
AA8 7 TYR B 357 ? PHE B 360 ? TYR B 357 PHE B 360 
AA8 8 THR B 681 ? ILE B 682 ? THR B 681 ILE B 682 
AA9 1 ALA B 298 ? PHE B 301 ? ALA B 298 PHE B 301 
AA9 2 LYS B 334 ? ILE B 337 ? LYS B 334 ILE B 337 
AB1 1 ILE B 601 ? TYR B 606 ? ILE B 601 TYR B 606 
AB1 2 SER B 609 ? PRO B 614 ? SER B 609 PRO B 614 
AB2 1 LEU B 656 ? LYS B 659 ? LEU B 656 LYS B 659 
AB2 2 ALA B 685 ? LYS B 688 ? ALA B 685 LYS B 688 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 20  ? N LYS A 20  O LYS A 23  ? O LYS A 23  
AA2 1 2 N GLN A 150 ? N GLN A 150 O SER A 413 ? O SER A 413 
AA2 2 3 N GLY A 412 ? N GLY A 412 O GLY A 464 ? O GLY A 464 
AA3 1 2 N LEU A 173 ? N LEU A 173 O SER A 200 ? O SER A 200 
AA3 2 3 N LEU A 201 ? N LEU A 201 O TYR A 250 ? O TYR A 250 
AA3 3 4 N GLY A 247 ? N GLY A 247 O SER A 279 ? O SER A 279 
AA3 4 5 N VAL A 282 ? N VAL A 282 O TYR A 357 ? O TYR A 357 
AA3 5 6 N ILE A 358 ? N ILE A 358 O ILE A 682 ? O ILE A 682 
AA4 1 2 N ALA A 298 ? N ALA A 298 O ILE A 337 ? O ILE A 337 
AA5 1 2 N GLU A 602 ? N GLU A 602 O TYR A 613 ? O TYR A 613 
AA6 1 2 N LEU A 656 ? N LEU A 656 O ARG A 686 ? O ARG A 686 
AA7 1 2 N GLN B 150 ? N GLN B 150 O SER B 413 ? O SER B 413 
AA7 2 3 N GLY B 412 ? N GLY B 412 O GLY B 464 ? O GLY B 464 
AA8 1 2 N GLN B 150 ? N GLN B 150 O SER B 413 ? O SER B 413 
AA8 2 3 O CYS B 409 ? O CYS B 409 N CYS B 170 ? N CYS B 170 
AA8 3 4 N LEU B 173 ? N LEU B 173 O SER B 200 ? O SER B 200 
AA8 4 5 N LEU B 201 ? N LEU B 201 O TYR B 250 ? O TYR B 250 
AA8 5 6 N GLY B 247 ? N GLY B 247 O SER B 279 ? O SER B 279 
AA8 6 7 N VAL B 282 ? N VAL B 282 O TYR B 357 ? O TYR B 357 
AA8 7 8 N ILE B 358 ? N ILE B 358 O ILE B 682 ? O ILE B 682 
AA9 1 2 N ALA B 298 ? N ALA B 298 O ILE B 337 ? O ILE B 337 
AB1 1 2 N ARG B 604 ? N ARG B 604 O THR B 611 ? O THR B 611 
AB2 1 2 N LEU B 658 ? N LEU B 658 O ARG B 686 ? O ARG B 686 
# 
_pdbx_entry_details.entry_id                   9BZ2 
_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 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             N 
_pdbx_validate_rmsd_angle.auth_asym_id_1             D 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_1              42 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             D 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_2              42 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_3             D 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              42 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                97.79 
_pdbx_validate_rmsd_angle.angle_target_value         110.40 
_pdbx_validate_rmsd_angle.angle_deviation            -12.61 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.00 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
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 ? ? -69.54  2.76    
2  1 ASP A 398 ? ? 39.48   35.65   
3  1 SER A 593 ? ? 56.70   -153.87 
4  1 ASP B 215 ? ? 74.87   -2.83   
5  1 SER B 593 ? ? 60.62   -154.16 
6  1 THR C 72  ? ? -128.08 -59.01  
7  1 ASP C 148 ? ? 58.08   15.65   
8  1 PHE C 166 ? ? -125.63 -60.86  
9  1 THR D 72  ? ? -128.19 -58.51  
10 1 PHE D 166 ? ? -144.16 -61.14  
11 1 ASP D 317 ? ? 64.25   164.42  
12 1 ASP D 318 ? ? 66.34   -1.38   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BZ2 
_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                    9BZ2 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.83 
_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               31000 
_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                        9BZ2 
_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              9BZ2 
_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                9BZ2 
_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              9BZ2 
_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           9BZ2 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'Class 14 model for turnover condition of Bacillus subtilis ribonucleotide reductase complex' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          1423 
_em_entity_assembly_naturalsource.organism             'Bacillus subtilis' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       COUNTING 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    20 
_em_imaging_optics.energyfilter_name          ? 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ?               ? 
'IMAGE ACQUISITION'        ? 2  ? ? ? ?               ? 
MASKING                    ? 3  ? ? ? ?               ? 
'CTF CORRECTION'           ? 4  1 ? ? ?               ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ?               ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?               ? 
'MODEL FITTING'            ? 7  ? 1 ? 'UCSF ChimeraX' ? 
OTHER                      ? 8  ? ? ? ?               ? 
'INITIAL EULER ASSIGNMENT' ? 9  1 ? ? RELION          ? 
'FINAL EULER ASSIGNMENT'   ? 10 1 ? ? RELION          ? 
CLASSIFICATION             ? 11 1 ? ? ?               ? 
RECONSTRUCTION             ? 12 1 ? ? RELION          ? 
'MODEL REFINEMENT'         ? 13 ? 1 ? ?               ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)' 'United States' MCB-1942668 1 
'National Science Foundation (NSF, United States)' 'United States' DMR-1719875 2 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
1 'experimental model' PDB 9BYH 
2 'experimental model' PDB 4DR0 
# 
_atom_sites.entry_id                    9BZ2 
_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   ? 105.486 119.415 98.224  1.00 61.20 ?  6   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 6   ? 106.565 120.139 97.566  1.00 61.32 ?  6   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 6   ? 106.000 121.127 96.545  1.00 62.07 ?  6   VAL A C     1 
ATOM   4     O  O     . VAL A 1 6   ? 105.188 120.760 95.696  1.00 60.69 ?  6   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 6   ? 107.572 119.160 96.915  1.00 61.34 ?  6   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 6   ? 106.866 118.195 95.970  1.00 61.29 ?  6   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 6   ? 108.668 119.922 96.189  1.00 59.53 ?  6   VAL A CG2   1 
ATOM   8     N  N     . PRO A 1 7   ? 106.412 122.388 96.644  1.00 58.51 ?  7   PRO A N     1 
ATOM   9     C  CA    . PRO A 1 7   ? 105.914 123.403 95.708  1.00 54.85 ?  7   PRO A CA    1 
ATOM   10    C  C     . PRO A 1 7   ? 106.480 123.204 94.311  1.00 54.57 ?  7   PRO A C     1 
ATOM   11    O  O     . PRO A 1 7   ? 107.531 122.595 94.112  1.00 55.81 ?  7   PRO A O     1 
ATOM   12    C  CB    . PRO A 1 7   ? 106.382 124.732 96.311  1.00 53.42 ?  7   PRO A CB    1 
ATOM   13    C  CG    . PRO A 1 7   ? 107.157 124.409 97.534  1.00 53.02 ?  7   PRO A CG    1 
ATOM   14    C  CD    . PRO A 1 7   ? 107.320 122.937 97.664  1.00 55.87 ?  7   PRO A CD    1 
ATOM   15    N  N     . LYS A 1 8   ? 105.753 123.750 93.331  1.00 54.03 ?  8   LYS A N     1 
ATOM   16    C  CA    . LYS A 1 8   ? 106.102 123.534 91.929  1.00 53.45 ?  8   LYS A CA    1 
ATOM   17    C  C     . LYS A 1 8   ? 107.474 124.106 91.594  1.00 55.16 ?  8   LYS A C     1 
ATOM   18    O  O     . LYS A 1 8   ? 108.257 123.477 90.870  1.00 57.31 ?  8   LYS A O     1 
ATOM   19    C  CB    . LYS A 1 8   ? 105.031 124.146 91.026  1.00 55.50 ?  8   LYS A CB    1 
ATOM   20    C  CG    . LYS A 1 8   ? 105.370 124.112 89.545  1.00 55.15 ?  8   LYS A CG    1 
ATOM   21    C  CD    . LYS A 1 8   ? 104.434 125.004 88.746  1.00 55.42 ?  8   LYS A CD    1 
ATOM   22    C  CE    . LYS A 1 8   ? 104.858 125.085 87.289  1.00 55.63 ?  8   LYS A CE    1 
ATOM   23    N  NZ    . LYS A 1 8   ? 104.144 126.170 86.561  1.00 56.86 1  8   LYS A NZ    1 
ATOM   24    N  N     . TRP A 1 9   ? 107.783 125.302 92.103  1.00 54.44 ?  9   TRP A N     1 
ATOM   25    C  CA    . TRP A 1 9   ? 109.080 125.901 91.811  1.00 52.69 ?  9   TRP A CA    1 
ATOM   26    C  C     . TRP A 1 9   ? 110.216 125.077 92.399  1.00 51.63 ?  9   TRP A C     1 
ATOM   27    O  O     . TRP A 1 9   ? 111.295 124.993 91.803  1.00 53.76 ?  9   TRP A O     1 
ATOM   28    C  CB    . TRP A 1 9   ? 109.137 127.339 92.329  1.00 52.54 ?  9   TRP A CB    1 
ATOM   29    C  CG    . TRP A 1 9   ? 108.920 127.483 93.804  1.00 49.94 ?  9   TRP A CG    1 
ATOM   30    C  CD1   . TRP A 1 9   ? 109.866 127.397 94.781  1.00 49.74 ?  9   TRP A CD1   1 
ATOM   31    C  CD2   . TRP A 1 9   ? 107.682 127.761 94.470  1.00 51.38 ?  9   TRP A CD2   1 
ATOM   32    N  NE1   . TRP A 1 9   ? 109.297 127.593 96.015  1.00 49.45 ?  9   TRP A NE1   1 
ATOM   33    C  CE2   . TRP A 1 9   ? 107.957 127.821 95.851  1.00 51.17 ?  9   TRP A CE2   1 
ATOM   34    C  CE3   . TRP A 1 9   ? 106.371 127.961 94.034  1.00 49.58 ?  9   TRP A CE3   1 
ATOM   35    C  CZ2   . TRP A 1 9   ? 106.967 128.072 96.798  1.00 49.84 ?  9   TRP A CZ2   1 
ATOM   36    C  CZ3   . TRP A 1 9   ? 105.390 128.208 94.975  1.00 51.27 ?  9   TRP A CZ3   1 
ATOM   37    C  CH2   . TRP A 1 9   ? 105.693 128.259 96.341  1.00 51.47 ?  9   TRP A CH2   1 
ATOM   38    N  N     . ILE A 1 10  ? 109.990 124.445 93.551  1.00 54.01 ?  10  ILE A N     1 
ATOM   39    C  CA    . ILE A 1 10  ? 111.026 123.610 94.146  1.00 53.77 ?  10  ILE A CA    1 
ATOM   40    C  C     . ILE A 1 10  ? 111.250 122.355 93.309  1.00 53.66 ?  10  ILE A C     1 
ATOM   41    O  O     . ILE A 1 10  ? 112.389 121.905 93.142  1.00 56.41 ?  10  ILE A O     1 
ATOM   42    C  CB    . ILE A 1 10  ? 110.669 123.278 95.606  1.00 54.66 ?  10  ILE A CB    1 
ATOM   43    C  CG1   . ILE A 1 10  ? 110.797 124.536 96.467  1.00 54.34 ?  10  ILE A CG1   1 
ATOM   44    C  CG2   . ILE A 1 10  ? 111.571 122.179 96.144  1.00 54.60 ?  10  ILE A CG2   1 
ATOM   45    C  CD1   . ILE A 1 10  ? 110.770 124.276 97.952  1.00 55.93 ?  10  ILE A CD1   1 
ATOM   46    N  N     . GLN A 1 11  ? 110.179 121.773 92.764  1.00 57.00 ?  11  GLN A N     1 
ATOM   47    C  CA    . GLN A 1 11  ? 110.355 120.647 91.849  1.00 57.95 ?  11  GLN A CA    1 
ATOM   48    C  C     . GLN A 1 11  ? 111.115 121.069 90.598  1.00 57.73 ?  11  GLN A C     1 
ATOM   49    O  O     . GLN A 1 11  ? 112.013 120.354 90.136  1.00 59.00 ?  11  GLN A O     1 
ATOM   50    C  CB    . GLN A 1 11  ? 109.003 120.042 91.470  1.00 57.52 ?  11  GLN A CB    1 
ATOM   51    C  CG    . GLN A 1 11  ? 108.023 119.902 92.618  1.00 58.92 ?  11  GLN A CG    1 
ATOM   52    C  CD    . GLN A 1 11  ? 106.579 119.969 92.161  1.00 60.78 ?  11  GLN A CD    1 
ATOM   53    O  OE1   . GLN A 1 11  ? 106.296 120.017 90.965  1.00 58.86 ?  11  GLN A OE1   1 
ATOM   54    N  NE2   . GLN A 1 11  ? 105.657 119.973 93.117  1.00 58.93 ?  11  GLN A NE2   1 
ATOM   55    N  N     . LEU A 1 12  ? 110.773 122.232 90.038  1.00 53.91 ?  12  LEU A N     1 
ATOM   56    C  CA    . LEU A 1 12  ? 111.477 122.712 88.853  1.00 52.66 ?  12  LEU A CA    1 
ATOM   57    C  C     . LEU A 1 12  ? 112.943 123.000 89.150  1.00 54.69 ?  12  LEU A C     1 
ATOM   58    O  O     . LEU A 1 12  ? 113.796 122.850 88.269  1.00 56.24 ?  12  LEU A O     1 
ATOM   59    C  CB    . LEU A 1 12  ? 110.788 123.960 88.301  1.00 52.80 ?  12  LEU A CB    1 
ATOM   60    C  CG    . LEU A 1 12  ? 109.618 123.717 87.347  1.00 53.51 ?  12  LEU A CG    1 
ATOM   61    C  CD1   . LEU A 1 12  ? 108.844 125.003 87.104  1.00 55.35 ?  12  LEU A CD1   1 
ATOM   62    C  CD2   . LEU A 1 12  ? 110.112 123.131 86.034  1.00 52.97 ?  12  LEU A CD2   1 
ATOM   63    N  N     . ASN A 1 13  ? 113.254 123.417 90.378  1.00 53.32 ?  13  ASN A N     1 
ATOM   64    C  CA    . ASN A 1 13  ? 114.641 123.653 90.760  1.00 51.61 ?  13  ASN A CA    1 
ATOM   65    C  C     . ASN A 1 13  ? 115.398 122.345 90.964  1.00 53.33 ?  13  ASN A C     1 
ATOM   66    O  O     . ASN A 1 13  ? 116.550 122.219 90.536  1.00 57.21 ?  13  ASN A O     1 
ATOM   67    C  CB    . ASN A 1 13  ? 114.696 124.507 92.027  1.00 52.13 ?  13  ASN A CB    1 
ATOM   68    C  CG    . ASN A 1 13  ? 116.113 124.812 92.463  1.00 51.95 ?  13  ASN A CG    1 
ATOM   69    O  OD1   . ASN A 1 13  ? 116.662 124.146 93.339  1.00 52.22 ?  13  ASN A OD1   1 
ATOM   70    N  ND2   . ASN A 1 13  ? 116.713 125.826 91.851  1.00 53.37 ?  13  ASN A ND2   1 
ATOM   71    N  N     . ASN A 1 14  ? 114.772 121.364 91.618  1.00 56.37 ?  14  ASN A N     1 
ATOM   72    C  CA    . ASN A 1 14  ? 115.405 120.062 91.801  1.00 55.27 ?  14  ASN A CA    1 
ATOM   73    C  C     . ASN A 1 14  ? 115.524 119.287 90.498  1.00 55.96 ?  14  ASN A C     1 
ATOM   74    O  O     . ASN A 1 14  ? 116.305 118.332 90.429  1.00 59.84 ?  14  ASN A O     1 
ATOM   75    C  CB    . ASN A 1 14  ? 114.637 119.239 92.836  1.00 55.43 ?  14  ASN A CB    1 
ATOM   76    C  CG    . ASN A 1 14  ? 114.654 119.874 94.213  1.00 58.93 ?  14  ASN A CG    1 
ATOM   77    O  OD1   . ASN A 1 14  ? 114.675 121.095 94.347  1.00 59.21 ?  14  ASN A OD1   1 
ATOM   78    N  ND2   . ASN A 1 14  ? 114.642 119.040 95.246  1.00 59.70 ?  14  ASN A ND2   1 
ATOM   79    N  N     . GLU A 1 15  ? 114.773 119.672 89.466  1.00 57.11 ?  15  GLU A N     1 
ATOM   80    C  CA    . GLU A 1 15  ? 114.929 119.040 88.162  1.00 58.53 ?  15  GLU A CA    1 
ATOM   81    C  C     . GLU A 1 15  ? 116.250 119.390 87.490  1.00 58.60 ?  15  GLU A C     1 
ATOM   82    O  O     . GLU A 1 15  ? 116.566 118.803 86.449  1.00 61.66 ?  15  GLU A O     1 
ATOM   83    C  CB    . GLU A 1 15  ? 113.760 119.420 87.249  1.00 58.15 ?  15  GLU A CB    1 
ATOM   84    C  CG    . GLU A 1 15  ? 112.493 118.620 87.509  1.00 58.81 ?  15  GLU A CG    1 
ATOM   85    C  CD    . GLU A 1 15  ? 111.301 119.130 86.723  1.00 61.24 ?  15  GLU A CD    1 
ATOM   86    O  OE1   . GLU A 1 15  ? 111.507 119.691 85.627  1.00 60.87 ?  15  GLU A OE1   1 
ATOM   87    O  OE2   . GLU A 1 15  ? 110.159 118.969 87.200  1.00 59.03 -1 15  GLU A OE2   1 
ATOM   88    N  N     . ILE A 1 16  ? 117.017 120.333 88.043  1.00 58.15 ?  16  ILE A N     1 
ATOM   89    C  CA    . ILE A 1 16  ? 118.325 120.667 87.479  1.00 58.69 ?  16  ILE A CA    1 
ATOM   90    C  C     . ILE A 1 16  ? 119.253 119.461 87.541  1.00 57.58 ?  16  ILE A C     1 
ATOM   91    O  O     . ILE A 1 16  ? 119.928 119.121 86.561  1.00 58.61 ?  16  ILE A O     1 
ATOM   92    C  CB    . ILE A 1 16  ? 118.935 121.874 88.213  1.00 57.30 ?  16  ILE A CB    1 
ATOM   93    C  CG1   . ILE A 1 16  ? 118.207 123.164 87.841  1.00 56.73 ?  16  ILE A CG1   1 
ATOM   94    C  CG2   . ILE A 1 16  ? 120.421 121.996 87.906  1.00 57.89 ?  16  ILE A CG2   1 
ATOM   95    C  CD1   . ILE A 1 16  ? 118.343 124.237 88.887  1.00 56.64 ?  16  ILE A CD1   1 
ATOM   96    N  N     . MET A 1 17  ? 119.300 118.796 88.698  1.00 57.91 ?  17  MET A N     1 
ATOM   97    C  CA    . MET A 1 17  ? 120.215 117.672 88.871  1.00 60.77 ?  17  MET A CA    1 
ATOM   98    C  C     . MET A 1 17  ? 119.845 116.497 87.980  1.00 60.83 ?  17  MET A C     1 
ATOM   99    O  O     . MET A 1 17  ? 120.717 115.698 87.620  1.00 61.69 ?  17  MET A O     1 
ATOM   100   C  CB    . MET A 1 17  ? 120.239 117.236 90.336  1.00 60.42 ?  17  MET A CB    1 
ATOM   101   C  CG    . MET A 1 17  ? 120.635 118.333 91.307  1.00 59.88 ?  17  MET A CG    1 
ATOM   102   S  SD    . MET A 1 17  ? 121.688 119.618 90.609  1.00 62.45 ?  17  MET A SD    1 
ATOM   103   C  CE    . MET A 1 17  ? 123.257 118.759 90.536  1.00 58.33 ?  17  MET A CE    1 
ATOM   104   N  N     . ILE A 1 18  ? 118.570 116.368 87.621  1.00 63.10 ?  18  ILE A N     1 
ATOM   105   C  CA    . ILE A 1 18  ? 118.138 115.305 86.718  1.00 63.93 ?  18  ILE A CA    1 
ATOM   106   C  C     . ILE A 1 18  ? 118.783 115.569 85.361  1.00 64.49 ?  18  ILE A C     1 
ATOM   107   O  O     . ILE A 1 18  ? 118.527 116.598 84.729  1.00 66.32 ?  18  ILE A O     1 
ATOM   108   C  CB    . ILE A 1 18  ? 116.608 115.227 86.610  1.00 63.43 ?  18  ILE A CB    1 
ATOM   109   C  CG1   . ILE A 1 18  ? 115.979 114.456 87.784  1.00 64.00 ?  18  ILE A CG1   1 
ATOM   110   C  CG2   . ILE A 1 18  ? 116.195 114.565 85.302  1.00 63.67 ?  18  ILE A CG2   1 
ATOM   111   C  CD1   . ILE A 1 18  ? 116.521 114.759 89.168  1.00 63.77 ?  18  ILE A CD1   1 
ATOM   112   N  N     . GLN A 1 19  ? 119.635 114.649 84.918  1.00 67.59 ?  19  GLN A N     1 
ATOM   113   C  CA    . GLN A 1 19  ? 120.441 114.875 83.729  1.00 69.12 ?  19  GLN A CA    1 
ATOM   114   C  C     . GLN A 1 19  ? 119.707 114.397 82.482  1.00 70.12 ?  19  GLN A C     1 
ATOM   115   O  O     . GLN A 1 19  ? 119.237 113.257 82.424  1.00 70.79 ?  19  GLN A O     1 
ATOM   116   C  CB    . GLN A 1 19  ? 121.787 114.160 83.859  1.00 70.18 ?  19  GLN A CB    1 
ATOM   117   C  CG    . GLN A 1 19  ? 122.759 114.850 84.802  1.00 68.31 ?  19  GLN A CG    1 
ATOM   118   C  CD    . GLN A 1 19  ? 124.200 114.453 84.551  1.00 70.65 ?  19  GLN A CD    1 
ATOM   119   O  OE1   . GLN A 1 19  ? 124.514 113.828 83.538  1.00 71.53 ?  19  GLN A OE1   1 
ATOM   120   N  NE2   . GLN A 1 19  ? 125.083 114.815 85.472  1.00 69.08 ?  19  GLN A NE2   1 
ATOM   121   N  N     . LYS A 1 20  ? 119.610 115.276 81.490  1.00 72.27 ?  20  LYS A N     1 
ATOM   122   C  CA    . LYS A 1 20  ? 119.042 114.948 80.191  1.00 73.91 ?  20  LYS A CA    1 
ATOM   123   C  C     . LYS A 1 20  ? 120.148 115.009 79.148  1.00 76.01 ?  20  LYS A C     1 
ATOM   124   O  O     . LYS A 1 20  ? 120.834 116.030 79.027  1.00 75.81 ?  20  LYS A O     1 
ATOM   125   C  CB    . LYS A 1 20  ? 117.904 115.907 79.832  1.00 71.70 ?  20  LYS A CB    1 
ATOM   126   C  CG    . LYS A 1 20  ? 117.608 116.009 78.344  1.00 73.05 ?  20  LYS A CG    1 
ATOM   127   C  CD    . LYS A 1 20  ? 118.074 117.340 77.773  1.00 74.70 ?  20  LYS A CD    1 
ATOM   128   C  CE    . LYS A 1 20  ? 118.335 117.240 76.279  1.00 74.77 ?  20  LYS A CE    1 
ATOM   129   N  NZ    . LYS A 1 20  ? 118.287 118.573 75.616  1.00 74.65 1  20  LYS A NZ    1 
ATOM   130   N  N     . ASP A 1 21  ? 120.320 113.914 78.407  1.00 77.71 ?  21  ASP A N     1 
ATOM   131   C  CA    . ASP A 1 21  ? 121.399 113.781 77.427  1.00 78.08 ?  21  ASP A CA    1 
ATOM   132   C  C     . ASP A 1 21  ? 122.764 113.993 78.080  1.00 78.21 ?  21  ASP A C     1 
ATOM   133   O  O     . ASP A 1 21  ? 123.678 114.571 77.486  1.00 77.84 ?  21  ASP A O     1 
ATOM   134   C  CB    . ASP A 1 21  ? 121.202 114.738 76.248  1.00 78.03 ?  21  ASP A CB    1 
ATOM   135   C  CG    . ASP A 1 21  ? 121.971 114.310 75.014  1.00 79.20 ?  21  ASP A CG    1 
ATOM   136   O  OD1   . ASP A 1 21  ? 121.976 113.100 74.706  1.00 77.85 ?  21  ASP A OD1   1 
ATOM   137   O  OD2   . ASP A 1 21  ? 122.573 115.183 74.353  1.00 77.64 -1 21  ASP A OD2   1 
ATOM   138   N  N     . GLY A 1 22  ? 122.903 113.524 79.318  1.00 74.06 ?  22  GLY A N     1 
ATOM   139   C  CA    . GLY A 1 22  ? 124.155 113.663 80.033  1.00 72.25 ?  22  GLY A CA    1 
ATOM   140   C  C     . GLY A 1 22  ? 124.513 115.077 80.425  1.00 73.50 ?  22  GLY A C     1 
ATOM   141   O  O     . GLY A 1 22  ? 125.686 115.359 80.681  1.00 74.68 ?  22  GLY A O     1 
ATOM   142   N  N     . LYS A 1 23  ? 123.536 115.979 80.481  1.00 69.34 ?  23  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 23  ? 123.778 117.370 80.827  1.00 67.22 ?  23  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 23  ? 122.767 117.830 81.867  1.00 68.95 ?  23  LYS A C     1 
ATOM   145   O  O     . LYS A 1 23  ? 121.611 117.397 81.870  1.00 70.38 ?  23  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 23  ? 123.700 118.282 79.595  1.00 68.25 ?  23  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 23  ? 124.780 118.025 78.560  1.00 68.58 ?  23  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 23  ? 124.519 118.816 77.289  1.00 68.77 ?  23  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 23  ? 125.464 118.398 76.177  1.00 71.00 ?  23  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 23  ? 125.091 119.009 74.872  1.00 69.00 1  23  LYS A NZ    1 
ATOM   151   N  N     . PHE A 1 24  ? 123.217 118.715 82.752  1.00 62.03 ?  24  PHE A N     1 
ATOM   152   C  CA    . PHE A 1 24  ? 122.329 119.289 83.751  1.00 59.31 ?  24  PHE A CA    1 
ATOM   153   C  C     . PHE A 1 24  ? 121.333 120.234 83.091  1.00 59.62 ?  24  PHE A C     1 
ATOM   154   O  O     . PHE A 1 24  ? 121.679 120.988 82.179  1.00 59.64 ?  24  PHE A O     1 
ATOM   155   C  CB    . PHE A 1 24  ? 123.136 120.036 84.812  1.00 57.58 ?  24  PHE A CB    1 
ATOM   156   C  CG    . PHE A 1 24  ? 124.006 119.145 85.650  1.00 59.16 ?  24  PHE A CG    1 
ATOM   157   C  CD1   . PHE A 1 24  ? 123.469 118.405 86.686  1.00 60.30 ?  24  PHE A CD1   1 
ATOM   158   C  CD2   . PHE A 1 24  ? 125.365 119.052 85.401  1.00 60.20 ?  24  PHE A CD2   1 
ATOM   159   C  CE1   . PHE A 1 24  ? 124.269 117.585 87.455  1.00 61.28 ?  24  PHE A CE1   1 
ATOM   160   C  CE2   . PHE A 1 24  ? 126.170 118.235 86.169  1.00 58.77 ?  24  PHE A CE2   1 
ATOM   161   C  CZ    . PHE A 1 24  ? 125.621 117.502 87.198  1.00 59.24 ?  24  PHE A CZ    1 
ATOM   162   N  N     . GLN A 1 25  ? 120.085 120.186 83.557  1.00 59.49 ?  25  GLN A N     1 
ATOM   163   C  CA    . GLN A 1 25  ? 119.030 121.049 83.028  1.00 61.28 ?  25  GLN A CA    1 
ATOM   164   C  C     . GLN A 1 25  ? 119.095 122.392 83.749  1.00 60.68 ?  25  GLN A C     1 
ATOM   165   O  O     . GLN A 1 25  ? 118.284 122.716 84.621  1.00 62.38 ?  25  GLN A O     1 
ATOM   166   C  CB    . GLN A 1 25  ? 117.665 120.389 83.183  1.00 61.69 ?  25  GLN A CB    1 
ATOM   167   C  CG    . GLN A 1 25  ? 117.479 119.146 82.331  1.00 60.60 ?  25  GLN A CG    1 
ATOM   168   C  CD    . GLN A 1 25  ? 116.214 118.390 82.677  1.00 61.28 ?  25  GLN A CD    1 
ATOM   169   O  OE1   . GLN A 1 25  ? 115.141 118.678 82.150  1.00 60.75 ?  25  GLN A OE1   1 
ATOM   170   N  NE2   . GLN A 1 25  ? 116.335 117.414 83.569  1.00 60.63 ?  25  GLN A NE2   1 
ATOM   171   N  N     . PHE A 1 26  ? 120.101 123.186 83.375  1.00 56.32 ?  26  PHE A N     1 
ATOM   172   C  CA    . PHE A 1 26  ? 120.275 124.503 83.979  1.00 54.81 ?  26  PHE A CA    1 
ATOM   173   C  C     . PHE A 1 26  ? 119.117 125.430 83.631  1.00 56.40 ?  26  PHE A C     1 
ATOM   174   O  O     . PHE A 1 26  ? 118.637 126.181 84.490  1.00 56.54 ?  26  PHE A O     1 
ATOM   175   C  CB    . PHE A 1 26  ? 121.602 125.112 83.529  1.00 51.71 ?  26  PHE A CB    1 
ATOM   176   C  CG    . PHE A 1 26  ? 122.809 124.372 84.028  1.00 54.69 ?  26  PHE A CG    1 
ATOM   177   C  CD1   . PHE A 1 26  ? 122.959 124.095 85.375  1.00 52.92 ?  26  PHE A CD1   1 
ATOM   178   C  CD2   . PHE A 1 26  ? 123.792 123.951 83.148  1.00 52.64 ?  26  PHE A CD2   1 
ATOM   179   C  CE1   . PHE A 1 26  ? 124.069 123.415 85.837  1.00 52.85 ?  26  PHE A CE1   1 
ATOM   180   C  CE2   . PHE A 1 26  ? 124.902 123.269 83.604  1.00 50.88 ?  26  PHE A CE2   1 
ATOM   181   C  CZ    . PHE A 1 26  ? 125.042 123.002 84.950  1.00 52.70 ?  26  PHE A CZ    1 
ATOM   182   N  N     . ASP A 1 27  ? 118.652 125.385 82.378  1.00 58.64 ?  27  ASP A N     1 
ATOM   183   C  CA    . ASP A 1 27  ? 117.576 126.271 81.947  1.00 58.79 ?  27  ASP A CA    1 
ATOM   184   C  C     . ASP A 1 27  ? 116.309 126.068 82.767  1.00 59.03 ?  27  ASP A C     1 
ATOM   185   O  O     . ASP A 1 27  ? 115.524 127.009 82.939  1.00 59.44 ?  27  ASP A O     1 
ATOM   186   C  CB    . ASP A 1 27  ? 117.291 126.059 80.458  1.00 59.79 ?  27  ASP A CB    1 
ATOM   187   C  CG    . ASP A 1 27  ? 116.928 124.621 80.127  1.00 62.16 ?  27  ASP A CG    1 
ATOM   188   O  OD1   . ASP A 1 27  ? 115.855 124.153 80.560  1.00 62.25 ?  27  ASP A OD1   1 
ATOM   189   O  OD2   . ASP A 1 27  ? 117.723 123.955 79.431  1.00 62.20 -1 27  ASP A OD2   1 
ATOM   190   N  N     . LYS A 1 28  ? 116.101 124.855 83.290  1.00 56.53 ?  28  LYS A N     1 
ATOM   191   C  CA    . LYS A 1 28  ? 114.936 124.601 84.131  1.00 58.97 ?  28  LYS A CA    1 
ATOM   192   C  C     . LYS A 1 28  ? 114.889 125.549 85.318  1.00 59.60 ?  28  LYS A C     1 
ATOM   193   O  O     . LYS A 1 28  ? 113.800 125.947 85.750  1.00 59.48 ?  28  LYS A O     1 
ATOM   194   C  CB    . LYS A 1 28  ? 114.941 123.150 84.610  1.00 58.52 ?  28  LYS A CB    1 
ATOM   195   C  CG    . LYS A 1 28  ? 114.419 122.158 83.586  1.00 60.37 ?  28  LYS A CG    1 
ATOM   196   C  CD    . LYS A 1 28  ? 112.952 121.849 83.817  1.00 59.68 ?  28  LYS A CD    1 
ATOM   197   C  CE    . LYS A 1 28  ? 112.269 121.425 82.530  1.00 58.32 ?  28  LYS A CE    1 
ATOM   198   N  NZ    . LYS A 1 28  ? 112.367 122.475 81.479  1.00 59.76 1  28  LYS A NZ    1 
ATOM   199   N  N     . ASP A 1 29  ? 116.057 125.940 85.839  1.00 57.46 ?  29  ASP A N     1 
ATOM   200   C  CA    . ASP A 1 29  ? 116.097 126.906 86.934  1.00 54.95 ?  29  ASP A CA    1 
ATOM   201   C  C     . ASP A 1 29  ? 115.319 128.162 86.579  1.00 53.98 ?  29  ASP A C     1 
ATOM   202   O  O     . ASP A 1 29  ? 114.528 128.658 87.390  1.00 56.72 ?  29  ASP A O     1 
ATOM   203   C  CB    . ASP A 1 29  ? 117.543 127.257 87.278  1.00 55.38 ?  29  ASP A CB    1 
ATOM   204   C  CG    . ASP A 1 29  ? 117.716 127.647 88.732  1.00 56.18 ?  29  ASP A CG    1 
ATOM   205   O  OD1   . ASP A 1 29  ? 116.911 127.194 89.572  1.00 55.71 ?  29  ASP A OD1   1 
ATOM   206   O  OD2   . ASP A 1 29  ? 118.661 128.405 89.036  1.00 55.40 -1 29  ASP A OD2   1 
ATOM   207   N  N     . LYS A 1 30  ? 115.504 128.670 85.357  1.00 54.92 ?  30  LYS A N     1 
ATOM   208   C  CA    . LYS A 1 30  ? 114.755 129.843 84.919  1.00 56.30 ?  30  LYS A CA    1 
ATOM   209   C  C     . LYS A 1 30  ? 113.258 129.610 85.064  1.00 55.88 ?  30  LYS A C     1 
ATOM   210   O  O     . LYS A 1 30  ? 112.540 130.440 85.635  1.00 58.29 ?  30  LYS A O     1 
ATOM   211   C  CB    . LYS A 1 30  ? 115.112 130.183 83.472  1.00 57.24 ?  30  LYS A CB    1 
ATOM   212   C  CG    . LYS A 1 30  ? 116.573 130.542 83.260  1.00 59.30 ?  30  LYS A CG    1 
ATOM   213   C  CD    . LYS A 1 30  ? 116.862 130.846 81.798  1.00 59.58 ?  30  LYS A CD    1 
ATOM   214   C  CE    . LYS A 1 30  ? 118.357 130.925 81.536  1.00 58.77 ?  30  LYS A CE    1 
ATOM   215   N  NZ    . LYS A 1 30  ? 118.700 130.594 80.125  1.00 58.18 1  30  LYS A NZ    1 
ATOM   216   N  N     . GLU A 1 31  ? 112.780 128.453 84.595  1.00 57.35 ?  31  GLU A N     1 
ATOM   217   C  CA    . GLU A 1 31  ? 111.366 128.131 84.741  1.00 56.70 ?  31  GLU A CA    1 
ATOM   218   C  C     . GLU A 1 31  ? 110.950 128.178 86.203  1.00 56.29 ?  31  GLU A C     1 
ATOM   219   O  O     . GLU A 1 31  ? 109.898 128.738 86.539  1.00 58.26 ?  31  GLU A O     1 
ATOM   220   C  CB    . GLU A 1 31  ? 111.073 126.753 84.140  1.00 56.01 ?  31  GLU A CB    1 
ATOM   221   C  CG    . GLU A 1 31  ? 111.799 126.426 82.828  1.00 58.50 ?  31  GLU A CG    1 
ATOM   222   C  CD    . GLU A 1 31  ? 111.407 127.317 81.651  1.00 61.13 ?  31  GLU A CD    1 
ATOM   223   O  OE1   . GLU A 1 31  ? 111.441 128.560 81.770  1.00 60.18 ?  31  GLU A OE1   1 
ATOM   224   O  OE2   . GLU A 1 31  ? 111.058 126.758 80.590  1.00 59.93 -1 31  GLU A OE2   1 
ATOM   225   N  N     . ALA A 1 32  ? 111.791 127.636 87.089  1.00 50.08 ?  32  ALA A N     1 
ATOM   226   C  CA    . ALA A 1 32  ? 111.499 127.677 88.516  1.00 48.71 ?  32  ALA A CA    1 
ATOM   227   C  C     . ALA A 1 32  ? 111.222 129.103 88.969  1.00 52.68 ?  32  ALA A C     1 
ATOM   228   O  O     . ALA A 1 32  ? 110.230 129.364 89.661  1.00 55.36 ?  32  ALA A O     1 
ATOM   229   C  CB    . ALA A 1 32  ? 112.658 127.070 89.308  1.00 47.76 ?  32  ALA A CB    1 
ATOM   230   N  N     . VAL A 1 33  ? 112.062 130.050 88.535  1.00 50.76 ?  33  VAL A N     1 
ATOM   231   C  CA    . VAL A 1 33  ? 111.861 131.445 88.918  1.00 49.52 ?  33  VAL A CA    1 
ATOM   232   C  C     . VAL A 1 33  ? 110.461 131.887 88.530  1.00 50.65 ?  33  VAL A C     1 
ATOM   233   O  O     . VAL A 1 33  ? 109.714 132.437 89.349  1.00 52.98 ?  33  VAL A O     1 
ATOM   234   C  CB    . VAL A 1 33  ? 112.925 132.349 88.272  1.00 50.41 ?  33  VAL A CB    1 
ATOM   235   C  CG1   . VAL A 1 33  ? 113.058 133.651 89.052  1.00 48.62 ?  33  VAL A CG1   1 
ATOM   236   C  CG2   . VAL A 1 33  ? 114.249 131.637 88.179  1.00 50.88 ?  33  VAL A CG2   1 
ATOM   237   N  N     . HIS A 1 34  ? 110.068 131.598 87.287  1.00 47.66 ?  34  HIS A N     1 
ATOM   238   C  CA    . HIS A 1 34  ? 108.729 131.949 86.834  1.00 47.52 ?  34  HIS A CA    1 
ATOM   239   C  C     . HIS A 1 34  ? 107.684 131.367 87.772  1.00 50.23 ?  34  HIS A C     1 
ATOM   240   O  O     . HIS A 1 34  ? 106.804 132.084 88.264  1.00 54.05 ?  34  HIS A O     1 
ATOM   241   C  CB    . HIS A 1 34  ? 108.520 131.456 85.404  1.00 50.92 ?  34  HIS A CB    1 
ATOM   242   C  CG    . HIS A 1 34  ? 107.603 132.318 84.594  1.00 50.54 ?  34  HIS A CG    1 
ATOM   243   N  ND1   . HIS A 1 34  ? 106.309 132.594 84.978  1.00 53.04 ?  34  HIS A ND1   1 
ATOM   244   C  CD2   . HIS A 1 34  ? 107.797 132.970 83.424  1.00 51.78 ?  34  HIS A CD2   1 
ATOM   245   C  CE1   . HIS A 1 34  ? 105.744 133.376 84.076  1.00 54.94 ?  34  HIS A CE1   1 
ATOM   246   N  NE2   . HIS A 1 34  ? 106.624 133.620 83.124  1.00 54.28 ?  34  HIS A NE2   1 
ATOM   247   N  N     . SER A 1 35  ? 107.812 130.075 88.088  1.00 48.83 ?  35  SER A N     1 
ATOM   248   C  CA    . SER A 1 35  ? 106.883 129.456 89.024  1.00 49.75 ?  35  SER A CA    1 
ATOM   249   C  C     . SER A 1 35  ? 106.929 130.168 90.366  1.00 50.04 ?  35  SER A C     1 
ATOM   250   O  O     . SER A 1 35  ? 105.887 130.527 90.928  1.00 52.60 ?  35  SER A O     1 
ATOM   251   C  CB    . SER A 1 35  ? 107.211 127.971 89.182  1.00 50.64 ?  35  SER A CB    1 
ATOM   252   O  OG    . SER A 1 35  ? 106.436 127.384 90.213  1.00 52.65 ?  35  SER A OG    1 
ATOM   253   N  N     . TYR A 1 36  ? 108.140 130.443 90.861  1.00 47.40 ?  36  TYR A N     1 
ATOM   254   C  CA    . TYR A 1 36  ? 108.277 131.098 92.157  1.00 48.30 ?  36  TYR A CA    1 
ATOM   255   C  C     . TYR A 1 36  ? 107.598 132.457 92.161  1.00 46.43 ?  36  TYR A C     1 
ATOM   256   O  O     . TYR A 1 36  ? 107.203 132.951 93.221  1.00 46.71 ?  36  TYR A O     1 
ATOM   257   C  CB    . TYR A 1 36  ? 109.753 131.236 92.525  1.00 46.66 ?  36  TYR A CB    1 
ATOM   258   C  CG    . TYR A 1 36  ? 109.992 131.779 93.915  1.00 45.89 ?  36  TYR A CG    1 
ATOM   259   C  CD1   . TYR A 1 36  ? 109.502 131.118 95.034  1.00 46.40 ?  36  TYR A CD1   1 
ATOM   260   C  CD2   . TYR A 1 36  ? 110.712 132.949 94.110  1.00 45.04 ?  36  TYR A CD2   1 
ATOM   261   C  CE1   . TYR A 1 36  ? 109.721 131.609 96.306  1.00 44.74 ?  36  TYR A CE1   1 
ATOM   262   C  CE2   . TYR A 1 36  ? 110.935 133.447 95.378  1.00 44.92 ?  36  TYR A CE2   1 
ATOM   263   C  CZ    . TYR A 1 36  ? 110.438 132.773 96.471  1.00 45.50 ?  36  TYR A CZ    1 
ATOM   264   O  OH    . TYR A 1 36  ? 110.660 133.269 97.736  1.00 47.43 ?  36  TYR A OH    1 
ATOM   265   N  N     . PHE A 1 37  ? 107.435 133.067 90.988  1.00 48.48 ?  37  PHE A N     1 
ATOM   266   C  CA    . PHE A 1 37  ? 106.711 134.323 90.889  1.00 49.98 ?  37  PHE A CA    1 
ATOM   267   C  C     . PHE A 1 37  ? 105.256 134.137 90.491  1.00 52.80 ?  37  PHE A C     1 
ATOM   268   O  O     . PHE A 1 37  ? 104.416 134.959 90.866  1.00 56.29 ?  37  PHE A O     1 
ATOM   269   C  CB    . PHE A 1 37  ? 107.401 135.257 89.889  1.00 51.07 ?  37  PHE A CB    1 
ATOM   270   C  CG    . PHE A 1 37  ? 108.588 135.972 90.462  1.00 51.02 ?  37  PHE A CG    1 
ATOM   271   C  CD1   . PHE A 1 37  ? 108.434 137.177 91.124  1.00 50.72 ?  37  PHE A CD1   1 
ATOM   272   C  CD2   . PHE A 1 37  ? 109.856 135.430 90.356  1.00 50.97 ?  37  PHE A CD2   1 
ATOM   273   C  CE1   . PHE A 1 37  ? 109.524 137.833 91.659  1.00 50.45 ?  37  PHE A CE1   1 
ATOM   274   C  CE2   . PHE A 1 37  ? 110.948 136.081 90.887  1.00 50.90 ?  37  PHE A CE2   1 
ATOM   275   C  CZ    . PHE A 1 37  ? 110.782 137.283 91.542  1.00 49.87 ?  37  PHE A CZ    1 
ATOM   276   N  N     . VAL A 1 38  ? 104.934 133.071 89.757  1.00 54.56 ?  38  VAL A N     1 
ATOM   277   C  CA    . VAL A 1 38  ? 103.550 132.874 89.340  1.00 53.41 ?  38  VAL A CA    1 
ATOM   278   C  C     . VAL A 1 38  ? 102.730 132.268 90.471  1.00 53.94 ?  38  VAL A C     1 
ATOM   279   O  O     . VAL A 1 38  ? 101.546 132.587 90.632  1.00 55.77 ?  38  VAL A O     1 
ATOM   280   C  CB    . VAL A 1 38  ? 103.500 132.016 88.061  1.00 53.67 ?  38  VAL A CB    1 
ATOM   281   C  CG1   . VAL A 1 38  ? 102.205 131.222 87.978  1.00 56.03 ?  38  VAL A CG1   1 
ATOM   282   C  CG2   . VAL A 1 38  ? 103.649 132.901 86.839  1.00 52.77 ?  38  VAL A CG2   1 
ATOM   283   N  N     . ASP A 1 39  ? 103.342 131.415 91.288  1.00 52.80 ?  39  ASP A N     1 
ATOM   284   C  CA    . ASP A 1 39  ? 102.630 130.694 92.334  1.00 53.63 ?  39  ASP A CA    1 
ATOM   285   C  C     . ASP A 1 39  ? 102.729 131.354 93.703  1.00 57.33 ?  39  ASP A C     1 
ATOM   286   O  O     . ASP A 1 39  ? 101.751 131.342 94.456  1.00 58.77 ?  39  ASP A O     1 
ATOM   287   C  CB    . ASP A 1 39  ? 103.153 129.258 92.428  1.00 55.81 ?  39  ASP A CB    1 
ATOM   288   C  CG    . ASP A 1 39  ? 103.241 128.580 91.076  1.00 57.71 ?  39  ASP A CG    1 
ATOM   289   O  OD1   . ASP A 1 39  ? 102.369 128.840 90.222  1.00 56.94 ?  39  ASP A OD1   1 
ATOM   290   O  OD2   . ASP A 1 39  ? 104.185 127.790 90.867  1.00 58.02 -1 39  ASP A OD2   1 
ATOM   291   N  N     . TYR A 1 40  ? 103.880 131.929 94.054  1.00 55.98 ?  40  TYR A N     1 
ATOM   292   C  CA    . TYR A 1 40  ? 104.113 132.400 95.413  1.00 53.64 ?  40  TYR A CA    1 
ATOM   293   C  C     . TYR A 1 40  ? 104.266 133.912 95.512  1.00 58.23 ?  40  TYR A C     1 
ATOM   294   O  O     . TYR A 1 40  ? 103.525 134.555 96.260  1.00 60.63 ?  40  TYR A O     1 
ATOM   295   C  CB    . TYR A 1 40  ? 105.351 131.707 95.997  1.00 53.89 ?  40  TYR A CB    1 
ATOM   296   C  CG    . TYR A 1 40  ? 105.501 131.889 97.490  1.00 54.81 ?  40  TYR A CG    1 
ATOM   297   C  CD1   . TYR A 1 40  ? 106.193 132.973 98.012  1.00 53.49 ?  40  TYR A CD1   1 
ATOM   298   C  CD2   . TYR A 1 40  ? 104.944 130.978 98.378  1.00 55.81 ?  40  TYR A CD2   1 
ATOM   299   C  CE1   . TYR A 1 40  ? 106.330 133.144 99.375  1.00 55.23 ?  40  TYR A CE1   1 
ATOM   300   C  CE2   . TYR A 1 40  ? 105.077 131.141 99.743  1.00 57.31 ?  40  TYR A CE2   1 
ATOM   301   C  CZ    . TYR A 1 40  ? 105.769 132.225 100.235 1.00 58.22 ?  40  TYR A CZ    1 
ATOM   302   O  OH    . TYR A 1 40  ? 105.903 132.389 101.594 1.00 57.01 ?  40  TYR A OH    1 
ATOM   303   N  N     . ILE A 1 41  ? 105.214 134.503 94.781  1.00 55.03 ?  41  ILE A N     1 
ATOM   304   C  CA    . ILE A 1 41  ? 105.589 135.891 95.044  1.00 51.74 ?  41  ILE A CA    1 
ATOM   305   C  C     . ILE A 1 41  ? 104.434 136.833 94.726  1.00 50.75 ?  41  ILE A C     1 
ATOM   306   O  O     . ILE A 1 41  ? 104.079 137.698 95.537  1.00 53.01 ?  41  ILE A O     1 
ATOM   307   C  CB    . ILE A 1 41  ? 106.858 136.268 94.260  1.00 49.42 ?  41  ILE A CB    1 
ATOM   308   C  CG1   . ILE A 1 41  ? 108.071 135.527 94.824  1.00 48.58 ?  41  ILE A CG1   1 
ATOM   309   C  CG2   . ILE A 1 41  ? 107.094 137.765 94.329  1.00 48.07 ?  41  ILE A CG2   1 
ATOM   310   C  CD1   . ILE A 1 41  ? 108.249 135.694 96.315  1.00 46.20 ?  41  ILE A CD1   1 
ATOM   311   N  N     . ASN A 1 42  ? 103.819 136.677 93.552  1.00 51.13 ?  42  ASN A N     1 
ATOM   312   C  CA    . ASN A 1 42  ? 102.722 137.564 93.180  1.00 51.45 ?  42  ASN A CA    1 
ATOM   313   C  C     . ASN A 1 42  ? 101.500 137.357 94.066  1.00 55.41 ?  42  ASN A C     1 
ATOM   314   O  O     . ASN A 1 42  ? 100.780 138.317 94.360  1.00 56.50 ?  42  ASN A O     1 
ATOM   315   C  CB    . ASN A 1 42  ? 102.358 137.365 91.709  1.00 52.87 ?  42  ASN A CB    1 
ATOM   316   C  CG    . ASN A 1 42  ? 103.478 137.770 90.773  1.00 53.98 ?  42  ASN A CG    1 
ATOM   317   O  OD1   . ASN A 1 42  ? 104.436 138.426 91.180  1.00 57.56 ?  42  ASN A OD1   1 
ATOM   318   N  ND2   . ASN A 1 42  ? 103.364 137.379 89.509  1.00 54.07 ?  42  ASN A ND2   1 
ATOM   319   N  N     . GLN A 1 43  ? 101.248 136.118 94.496  1.00 57.91 ?  43  GLN A N     1 
ATOM   320   C  CA    . GLN A 1 43  ? 100.101 135.851 95.358  1.00 55.47 ?  43  GLN A CA    1 
ATOM   321   C  C     . GLN A 1 43  ? 100.261 136.511 96.723  1.00 55.81 ?  43  GLN A C     1 
ATOM   322   O  O     . GLN A 1 43  ? 99.290  137.032 97.283  1.00 56.47 ?  43  GLN A O     1 
ATOM   323   C  CB    . GLN A 1 43  ? 99.903  134.344 95.510  1.00 55.39 ?  43  GLN A CB    1 
ATOM   324   C  CG    . GLN A 1 43  ? 98.967  133.729 94.482  1.00 57.56 ?  43  GLN A CG    1 
ATOM   325   C  CD    . GLN A 1 43  ? 99.511  133.809 93.068  1.00 58.38 ?  43  GLN A CD    1 
ATOM   326   O  OE1   . GLN A 1 43  ? 100.711 133.992 92.862  1.00 57.94 ?  43  GLN A OE1   1 
ATOM   327   N  NE2   . GLN A 1 43  ? 98.628  133.673 92.086  1.00 56.72 ?  43  GLN A NE2   1 
ATOM   328   N  N     . ASN A 1 44  ? 101.474 136.497 97.274  1.00 54.90 ?  44  ASN A N     1 
ATOM   329   C  CA    . ASN A 1 44  ? 101.734 137.021 98.608  1.00 55.01 ?  44  ASN A CA    1 
ATOM   330   C  C     . ASN A 1 44  ? 102.323 138.427 98.596  1.00 54.27 ?  44  ASN A C     1 
ATOM   331   O  O     . ASN A 1 44  ? 102.824 138.883 99.627  1.00 54.47 ?  44  ASN A O     1 
ATOM   332   C  CB    . ASN A 1 44  ? 102.657 136.071 99.375  1.00 53.41 ?  44  ASN A CB    1 
ATOM   333   C  CG    . ASN A 1 44  ? 102.091 134.667 99.481  1.00 55.83 ?  44  ASN A CG    1 
ATOM   334   O  OD1   . ASN A 1 44  ? 101.666 134.234 100.550 1.00 56.75 ?  44  ASN A OD1   1 
ATOM   335   N  ND2   . ASN A 1 44  ? 102.086 133.948 98.364  1.00 56.44 ?  44  ASN A ND2   1 
ATOM   336   N  N     . THR A 1 45  ? 102.275 139.121 97.463  1.00 54.15 ?  45  THR A N     1 
ATOM   337   C  CA    . THR A 1 45  ? 102.757 140.493 97.367  1.00 55.09 ?  45  THR A CA    1 
ATOM   338   C  C     . THR A 1 45  ? 101.586 141.452 97.524  1.00 55.66 ?  45  THR A C     1 
ATOM   339   O  O     . THR A 1 45  ? 100.595 141.356 96.791  1.00 56.05 ?  45  THR A O     1 
ATOM   340   C  CB    . THR A 1 45  ? 103.464 140.738 96.032  1.00 55.01 ?  45  THR A CB    1 
ATOM   341   O  OG1   . THR A 1 45  ? 104.795 140.208 96.091  1.00 57.88 ?  45  THR A OG1   1 
ATOM   342   C  CG2   . THR A 1 45  ? 103.536 142.228 95.725  1.00 53.39 ?  45  THR A CG2   1 
ATOM   343   N  N     . VAL A 1 46  ? 101.699 142.370 98.482  1.00 55.46 ?  46  VAL A N     1 
ATOM   344   C  CA    . VAL A 1 46  ? 100.644 143.349 98.715  1.00 55.19 ?  46  VAL A CA    1 
ATOM   345   C  C     . VAL A 1 46  ? 100.678 144.383 97.598  1.00 55.73 ?  46  VAL A C     1 
ATOM   346   O  O     . VAL A 1 46  ? 101.718 144.993 97.328  1.00 58.54 ?  46  VAL A O     1 
ATOM   347   C  CB    . VAL A 1 46  ? 100.803 144.012 100.089 1.00 55.20 ?  46  VAL A CB    1 
ATOM   348   C  CG1   . VAL A 1 46  ? 99.791  145.132 100.257 1.00 54.96 ?  46  VAL A CG1   1 
ATOM   349   C  CG2   . VAL A 1 46  ? 100.647 142.987 101.192 1.00 54.62 ?  46  VAL A CG2   1 
ATOM   350   N  N     . PHE A 1 47  ? 99.539  144.585 96.945  1.00 59.11 ?  47  PHE A N     1 
ATOM   351   C  CA    . PHE A 1 47  ? 99.421  145.544 95.860  1.00 59.69 ?  47  PHE A CA    1 
ATOM   352   C  C     . PHE A 1 47  ? 98.515  146.696 96.273  1.00 61.94 ?  47  PHE A C     1 
ATOM   353   O  O     . PHE A 1 47  ? 97.555  146.517 97.027  1.00 63.68 ?  47  PHE A O     1 
ATOM   354   C  CB    . PHE A 1 47  ? 98.877  144.885 94.590  1.00 60.14 ?  47  PHE A CB    1 
ATOM   355   C  CG    . PHE A 1 47  ? 99.238  145.616 93.329  1.00 62.75 ?  47  PHE A CG    1 
ATOM   356   C  CD1   . PHE A 1 47  ? 100.504 145.495 92.781  1.00 61.43 ?  47  PHE A CD1   1 
ATOM   357   C  CD2   . PHE A 1 47  ? 98.314  146.430 92.695  1.00 62.25 ?  47  PHE A CD2   1 
ATOM   358   C  CE1   . PHE A 1 47  ? 100.842 146.169 91.623  1.00 61.54 ?  47  PHE A CE1   1 
ATOM   359   C  CE2   . PHE A 1 47  ? 98.646  147.107 91.535  1.00 61.58 ?  47  PHE A CE2   1 
ATOM   360   C  CZ    . PHE A 1 47  ? 99.910  146.975 91.000  1.00 61.77 ?  47  PHE A CZ    1 
ATOM   361   N  N     . PHE A 1 48  ? 98.835  147.881 95.767  1.00 57.51 ?  48  PHE A N     1 
ATOM   362   C  CA    . PHE A 1 48  ? 98.102  149.098 96.068  1.00 57.86 ?  48  PHE A CA    1 
ATOM   363   C  C     . PHE A 1 48  ? 97.598  149.724 94.774  1.00 58.93 ?  48  PHE A C     1 
ATOM   364   O  O     . PHE A 1 48  ? 98.129  149.471 93.689  1.00 61.11 ?  48  PHE A O     1 
ATOM   365   C  CB    . PHE A 1 48  ? 98.975  150.100 96.834  1.00 57.18 ?  48  PHE A CB    1 
ATOM   366   C  CG    . PHE A 1 48  ? 99.464  149.592 98.162  1.00 56.27 ?  48  PHE A CG    1 
ATOM   367   C  CD1   . PHE A 1 48  ? 100.601 148.805 98.245  1.00 56.87 ?  48  PHE A CD1   1 
ATOM   368   C  CD2   . PHE A 1 48  ? 98.794  149.913 99.330  1.00 58.06 ?  48  PHE A CD2   1 
ATOM   369   C  CE1   . PHE A 1 48  ? 101.055 148.344 99.465  1.00 57.84 ?  48  PHE A CE1   1 
ATOM   370   C  CE2   . PHE A 1 48  ? 99.243  149.452 100.554 1.00 58.40 ?  48  PHE A CE2   1 
ATOM   371   C  CZ    . PHE A 1 48  ? 100.375 148.667 100.620 1.00 57.22 ?  48  PHE A CZ    1 
ATOM   372   N  N     . HIS A 1 49  ? 96.552  150.544 94.903  1.00 63.64 ?  49  HIS A N     1 
ATOM   373   C  CA    . HIS A 1 49  ? 95.972  151.188 93.729  1.00 66.40 ?  49  HIS A CA    1 
ATOM   374   C  C     . HIS A 1 49  ? 96.967  152.119 93.050  1.00 67.18 ?  49  HIS A C     1 
ATOM   375   O  O     . HIS A 1 49  ? 96.951  152.257 91.822  1.00 67.16 ?  49  HIS A O     1 
ATOM   376   C  CB    . HIS A 1 49  ? 94.707  151.951 94.121  1.00 67.54 ?  49  HIS A CB    1 
ATOM   377   C  CG    . HIS A 1 49  ? 93.978  152.550 92.958  1.00 69.46 ?  49  HIS A CG    1 
ATOM   378   N  ND1   . HIS A 1 49  ? 93.582  151.808 91.867  1.00 68.49 ?  49  HIS A ND1   1 
ATOM   379   C  CD2   . HIS A 1 49  ? 93.571  153.819 92.719  1.00 67.80 ?  49  HIS A CD2   1 
ATOM   380   C  CE1   . HIS A 1 49  ? 92.964  152.594 91.003  1.00 68.74 ?  49  HIS A CE1   1 
ATOM   381   N  NE2   . HIS A 1 49  ? 92.944  153.820 91.496  1.00 69.21 ?  49  HIS A NE2   1 
ATOM   382   N  N     . ASN A 1 50  ? 97.836  152.761 93.826  1.00 64.74 ?  50  ASN A N     1 
ATOM   383   C  CA    . ASN A 1 50  ? 98.872  153.625 93.280  1.00 63.49 ?  50  ASN A CA    1 
ATOM   384   C  C     . ASN A 1 50  ? 100.028 153.686 94.267  1.00 62.85 ?  50  ASN A C     1 
ATOM   385   O  O     . ASN A 1 50  ? 99.910  153.263 95.420  1.00 61.77 ?  50  ASN A O     1 
ATOM   386   C  CB    . ASN A 1 50  ? 98.325  155.023 92.954  1.00 62.57 ?  50  ASN A CB    1 
ATOM   387   C  CG    . ASN A 1 50  ? 97.955  155.818 94.195  1.00 64.44 ?  50  ASN A CG    1 
ATOM   388   O  OD1   . ASN A 1 50  ? 97.810  155.266 95.285  1.00 64.51 ?  50  ASN A OD1   1 
ATOM   389   N  ND2   . ASN A 1 50  ? 97.800  157.125 94.030  1.00 63.77 ?  50  ASN A ND2   1 
ATOM   390   N  N     . LEU A 1 51  ? 101.160 154.213 93.796  1.00 57.68 ?  51  LEU A N     1 
ATOM   391   C  CA    . LEU A 1 51  ? 102.348 154.284 94.639  1.00 56.20 ?  51  LEU A CA    1 
ATOM   392   C  C     . LEU A 1 51  ? 102.147 155.219 95.823  1.00 57.94 ?  51  LEU A C     1 
ATOM   393   O  O     . LEU A 1 51  ? 102.779 155.034 96.869  1.00 59.15 ?  51  LEU A O     1 
ATOM   394   C  CB    . LEU A 1 51  ? 103.552 154.729 93.812  1.00 55.60 ?  51  LEU A CB    1 
ATOM   395   C  CG    . LEU A 1 51  ? 104.909 154.789 94.514  1.00 55.06 ?  51  LEU A CG    1 
ATOM   396   C  CD1   . LEU A 1 51  ? 105.354 153.402 94.949  1.00 54.14 ?  51  LEU A CD1   1 
ATOM   397   C  CD2   . LEU A 1 51  ? 105.941 155.430 93.607  1.00 54.35 ?  51  LEU A CD2   1 
ATOM   398   N  N     . LYS A 1 52  ? 101.287 156.230 95.679  1.00 57.99 ?  52  LYS A N     1 
ATOM   399   C  CA    . LYS A 1 52  ? 101.016 157.134 96.792  1.00 57.65 ?  52  LYS A CA    1 
ATOM   400   C  C     . LYS A 1 52  ? 100.408 156.377 97.967  1.00 58.88 ?  52  LYS A C     1 
ATOM   401   O  O     . LYS A 1 52  ? 100.811 156.568 99.121  1.00 59.30 ?  52  LYS A O     1 
ATOM   402   C  CB    . LYS A 1 52  ? 100.090 158.261 96.333  1.00 57.85 ?  52  LYS A CB    1 
ATOM   403   C  CG    . LYS A 1 52  ? 100.428 159.628 96.910  1.00 58.85 ?  52  LYS A CG    1 
ATOM   404   C  CD    . LYS A 1 52  ? 100.048 159.733 98.374  1.00 59.24 ?  52  LYS A CD    1 
ATOM   405   C  CE    . LYS A 1 52  ? 100.254 161.144 98.896  1.00 59.48 ?  52  LYS A CE    1 
ATOM   406   N  NZ    . LYS A 1 52  ? 100.446 161.164 100.372 1.00 59.50 1  52  LYS A NZ    1 
ATOM   407   N  N     . GLU A 1 53  ? 99.442  155.499 97.686  1.00 60.58 ?  53  GLU A N     1 
ATOM   408   C  CA    . GLU A 1 53  ? 98.834  154.697 98.742  1.00 60.45 ?  53  GLU A CA    1 
ATOM   409   C  C     . GLU A 1 53  ? 99.851  153.757 99.375  1.00 60.19 ?  53  GLU A C     1 
ATOM   410   O  O     . GLU A 1 53  ? 99.858  153.572 100.597 1.00 60.00 ?  53  GLU A O     1 
ATOM   411   C  CB    . GLU A 1 53  ? 97.651  153.907 98.184  1.00 61.07 ?  53  GLU A CB    1 
ATOM   412   C  CG    . GLU A 1 53  ? 96.836  153.174 99.237  1.00 62.36 ?  53  GLU A CG    1 
ATOM   413   C  CD    . GLU A 1 53  ? 95.840  152.207 98.630  1.00 63.76 ?  53  GLU A CD    1 
ATOM   414   O  OE1   . GLU A 1 53  ? 95.799  151.038 99.069  1.00 62.97 ?  53  GLU A OE1   1 
ATOM   415   O  OE2   . GLU A 1 53  ? 95.098  152.612 97.710  1.00 62.77 -1 53  GLU A OE2   1 
ATOM   416   N  N     . LYS A 1 54  ? 100.716 153.152 98.558  1.00 58.66 ?  54  LYS A N     1 
ATOM   417   C  CA    . LYS A 1 54  ? 101.737 152.252 99.088  1.00 54.61 ?  54  LYS A CA    1 
ATOM   418   C  C     . LYS A 1 54  ? 102.686 152.990 100.023 1.00 52.64 ?  54  LYS A C     1 
ATOM   419   O  O     . LYS A 1 54  ? 102.994 152.511 101.122 1.00 55.36 ?  54  LYS A O     1 
ATOM   420   C  CB    . LYS A 1 54  ? 102.512 151.610 97.938  1.00 54.10 ?  54  LYS A CB    1 
ATOM   421   C  CG    . LYS A 1 54  ? 103.758 150.865 98.377  1.00 57.14 ?  54  LYS A CG    1 
ATOM   422   C  CD    . LYS A 1 54  ? 104.221 149.892 97.311  1.00 55.57 ?  54  LYS A CD    1 
ATOM   423   C  CE    . LYS A 1 54  ? 105.433 149.107 97.769  1.00 55.37 ?  54  LYS A CE    1 
ATOM   424   N  NZ    . LYS A 1 54  ? 105.614 147.860 96.978  1.00 55.79 1  54  LYS A NZ    1 
ATOM   425   N  N     . LEU A 1 55  ? 103.158 154.163 99.600  1.00 53.92 ?  55  LEU A N     1 
ATOM   426   C  CA    . LEU A 1 55  ? 104.077 154.935 100.429 1.00 55.07 ?  55  LEU A CA    1 
ATOM   427   C  C     . LEU A 1 55  ? 103.398 155.413 101.705 1.00 57.40 ?  55  LEU A C     1 
ATOM   428   O  O     . LEU A 1 55  ? 104.007 155.392 102.780 1.00 58.63 ?  55  LEU A O     1 
ATOM   429   C  CB    . LEU A 1 55  ? 104.632 156.116 99.637  1.00 55.64 ?  55  LEU A CB    1 
ATOM   430   C  CG    . LEU A 1 55  ? 105.537 155.762 98.455  1.00 56.12 ?  55  LEU A CG    1 
ATOM   431   C  CD1   . LEU A 1 55  ? 105.858 157.004 97.643  1.00 56.83 ?  55  LEU A CD1   1 
ATOM   432   C  CD2   . LEU A 1 55  ? 106.811 155.079 98.926  1.00 53.50 ?  55  LEU A CD2   1 
ATOM   433   N  N     . ASP A 1 56  ? 102.135 155.840 101.609 1.00 60.10 ?  56  ASP A N     1 
ATOM   434   C  CA    . ASP A 1 56  ? 101.410 156.260 102.803 1.00 59.38 ?  56  ASP A CA    1 
ATOM   435   C  C     . ASP A 1 56  ? 101.236 155.103 103.778 1.00 57.92 ?  56  ASP A C     1 
ATOM   436   O  O     . ASP A 1 56  ? 101.419 155.271 104.988 1.00 57.64 ?  56  ASP A O     1 
ATOM   437   C  CB    . ASP A 1 56  ? 100.050 156.841 102.415 1.00 60.22 ?  56  ASP A CB    1 
ATOM   438   C  CG    . ASP A 1 56  ? 100.159 158.233 101.831 1.00 62.26 ?  56  ASP A CG    1 
ATOM   439   O  OD1   . ASP A 1 56  ? 99.149  158.730 101.288 1.00 62.19 ?  56  ASP A OD1   1 
ATOM   440   O  OD2   . ASP A 1 56  ? 101.253 158.830 101.914 1.00 61.30 -1 56  ASP A OD2   1 
ATOM   441   N  N     . TYR A 1 57  ? 100.888 153.919 103.270 1.00 52.63 ?  57  TYR A N     1 
ATOM   442   C  CA    . TYR A 1 57  ? 100.719 152.762 104.141 1.00 54.65 ?  57  TYR A CA    1 
ATOM   443   C  C     . TYR A 1 57  ? 102.034 152.364 104.795 1.00 56.13 ?  57  TYR A C     1 
ATOM   444   O  O     . TYR A 1 57  ? 102.063 152.018 105.982 1.00 57.38 ?  57  TYR A O     1 
ATOM   445   C  CB    . TYR A 1 57  ? 100.137 151.590 103.351 1.00 53.46 ?  57  TYR A CB    1 
ATOM   446   C  CG    . TYR A 1 57  ? 100.047 150.306 104.143 1.00 55.24 ?  57  TYR A CG    1 
ATOM   447   C  CD1   . TYR A 1 57  ? 98.982  150.072 105.003 1.00 54.93 ?  57  TYR A CD1   1 
ATOM   448   C  CD2   . TYR A 1 57  ? 101.027 149.327 104.030 1.00 55.44 ?  57  TYR A CD2   1 
ATOM   449   C  CE1   . TYR A 1 57  ? 98.898  148.900 105.730 1.00 55.25 ?  57  TYR A CE1   1 
ATOM   450   C  CE2   . TYR A 1 57  ? 100.950 148.155 104.753 1.00 55.86 ?  57  TYR A CE2   1 
ATOM   451   C  CZ    . TYR A 1 57  ? 99.884  147.945 105.601 1.00 55.58 ?  57  TYR A CZ    1 
ATOM   452   O  OH    . TYR A 1 57  ? 99.804  146.776 106.320 1.00 56.63 ?  57  TYR A OH    1 
ATOM   453   N  N     . LEU A 1 58  ? 103.133 152.398 104.038 1.00 51.42 ?  58  LEU A N     1 
ATOM   454   C  CA    . LEU A 1 58  ? 104.418 151.990 104.596 1.00 50.27 ?  58  LEU A CA    1 
ATOM   455   C  C     . LEU A 1 58  ? 104.929 153.001 105.616 1.00 51.95 ?  58  LEU A C     1 
ATOM   456   O  O     . LEU A 1 58  ? 105.512 152.618 106.636 1.00 52.72 ?  58  LEU A O     1 
ATOM   457   C  CB    . LEU A 1 58  ? 105.431 151.781 103.473 1.00 49.61 ?  58  LEU A CB    1 
ATOM   458   C  CG    . LEU A 1 58  ? 105.146 150.569 102.580 1.00 50.58 ?  58  LEU A CG    1 
ATOM   459   C  CD1   . LEU A 1 58  ? 105.964 150.621 101.302 1.00 51.28 ?  58  LEU A CD1   1 
ATOM   460   C  CD2   . LEU A 1 58  ? 105.404 149.274 103.330 1.00 51.20 ?  58  LEU A CD2   1 
ATOM   461   N  N     . VAL A 1 59  ? 104.719 154.294 105.364 1.00 53.73 ?  59  VAL A N     1 
ATOM   462   C  CA    . VAL A 1 59  ? 105.166 155.314 106.308 1.00 54.61 ?  59  VAL A CA    1 
ATOM   463   C  C     . VAL A 1 59  ? 104.313 155.288 107.572 1.00 57.60 ?  59  VAL A C     1 
ATOM   464   O  O     . VAL A 1 59  ? 104.833 155.338 108.692 1.00 56.54 ?  59  VAL A O     1 
ATOM   465   C  CB    . VAL A 1 59  ? 105.145 156.699 105.640 1.00 54.59 ?  59  VAL A CB    1 
ATOM   466   C  CG1   . VAL A 1 59  ? 105.148 157.794 106.689 1.00 53.14 ?  59  VAL A CG1   1 
ATOM   467   C  CG2   . VAL A 1 59  ? 106.333 156.851 104.705 1.00 54.08 ?  59  VAL A CG2   1 
ATOM   468   N  N     . GLU A 1 60  ? 102.990 155.202 107.409 1.00 60.48 ?  60  GLU A N     1 
ATOM   469   C  CA    . GLU A 1 60  ? 102.091 155.262 108.556 1.00 58.01 ?  60  GLU A CA    1 
ATOM   470   C  C     . GLU A 1 60  ? 102.255 154.048 109.461 1.00 57.85 ?  60  GLU A C     1 
ATOM   471   O  O     . GLU A 1 60  ? 102.198 154.172 110.690 1.00 58.08 ?  60  GLU A O     1 
ATOM   472   C  CB    . GLU A 1 60  ? 100.644 155.389 108.078 1.00 58.23 ?  60  GLU A CB    1 
ATOM   473   C  CG    . GLU A 1 60  ? 100.282 156.776 107.570 1.00 59.63 ?  60  GLU A CG    1 
ATOM   474   C  CD    . GLU A 1 60  ? 99.080  156.765 106.645 1.00 61.74 ?  60  GLU A CD    1 
ATOM   475   O  OE1   . GLU A 1 60  ? 98.422  155.708 106.534 1.00 59.38 ?  60  GLU A OE1   1 
ATOM   476   O  OE2   . GLU A 1 60  ? 98.794  157.811 106.026 1.00 61.31 -1 60  GLU A OE2   1 
ATOM   477   N  N     . ASN A 1 61  ? 102.460 152.868 108.878 1.00 53.71 ?  61  ASN A N     1 
ATOM   478   C  CA    . ASN A 1 61  ? 102.619 151.639 109.646 1.00 52.50 ?  61  ASN A CA    1 
ATOM   479   C  C     . ASN A 1 61  ? 104.044 151.433 110.147 1.00 54.36 ?  61  ASN A C     1 
ATOM   480   O  O     . ASN A 1 61  ? 104.404 150.303 110.500 1.00 54.46 ?  61  ASN A O     1 
ATOM   481   C  CB    . ASN A 1 61  ? 102.175 150.437 108.812 1.00 53.45 ?  61  ASN A CB    1 
ATOM   482   C  CG    . ASN A 1 61  ? 100.668 150.318 108.719 1.00 56.30 ?  61  ASN A CG    1 
ATOM   483   O  OD1   . ASN A 1 61  ? 99.966  151.313 108.547 1.00 54.48 ?  61  ASN A OD1   1 
ATOM   484   N  ND2   . ASN A 1 61  ? 100.162 149.095 108.833 1.00 55.68 ?  61  ASN A ND2   1 
ATOM   485   N  N     . GLN A 1 62  ? 104.850 152.496 110.177 1.00 53.25 ?  62  GLN A N     1 
ATOM   486   C  CA    . GLN A 1 62  ? 106.210 152.467 110.720 1.00 52.66 ?  62  GLN A CA    1 
ATOM   487   C  C     . GLN A 1 62  ? 107.107 151.478 109.981 1.00 52.40 ?  62  GLN A C     1 
ATOM   488   O  O     . GLN A 1 62  ? 108.002 150.872 110.576 1.00 53.31 ?  62  GLN A O     1 
ATOM   489   C  CB    . GLN A 1 62  ? 106.205 152.164 112.222 1.00 51.98 ?  62  GLN A CB    1 
ATOM   490   C  CG    . GLN A 1 62  ? 105.135 152.911 113.006 1.00 51.77 ?  62  GLN A CG    1 
ATOM   491   C  CD    . GLN A 1 62  ? 105.269 154.416 112.893 1.00 54.59 ?  62  GLN A CD    1 
ATOM   492   O  OE1   . GLN A 1 62  ? 106.197 155.011 113.438 1.00 54.15 ?  62  GLN A OE1   1 
ATOM   493   N  NE2   . GLN A 1 62  ? 104.339 155.040 112.180 1.00 54.94 ?  62  GLN A NE2   1 
ATOM   494   N  N     . TYR A 1 63  ? 106.877 151.300 108.681 1.00 50.12 ?  63  TYR A N     1 
ATOM   495   C  CA    . TYR A 1 63  ? 107.783 150.510 107.855 1.00 46.66 ?  63  TYR A CA    1 
ATOM   496   C  C     . TYR A 1 63  ? 108.939 151.354 107.332 1.00 48.34 ?  63  TYR A C     1 
ATOM   497   O  O     . TYR A 1 63  ? 110.096 150.927 107.380 1.00 49.61 ?  63  TYR A O     1 
ATOM   498   C  CB    . TYR A 1 63  ? 107.028 149.876 106.682 1.00 47.01 ?  63  TYR A CB    1 
ATOM   499   C  CG    . TYR A 1 63  ? 106.072 148.776 107.076 1.00 49.24 ?  63  TYR A CG    1 
ATOM   500   C  CD1   . TYR A 1 63  ? 106.529 147.624 107.699 1.00 48.39 ?  63  TYR A CD1   1 
ATOM   501   C  CD2   . TYR A 1 63  ? 104.714 148.887 106.816 1.00 50.04 ?  63  TYR A CD2   1 
ATOM   502   C  CE1   . TYR A 1 63  ? 105.659 146.616 108.056 1.00 48.45 ?  63  TYR A CE1   1 
ATOM   503   C  CE2   . TYR A 1 63  ? 103.837 147.883 107.168 1.00 50.57 ?  63  TYR A CE2   1 
ATOM   504   C  CZ    . TYR A 1 63  ? 104.313 146.752 107.790 1.00 50.75 ?  63  TYR A CZ    1 
ATOM   505   O  OH    . TYR A 1 63  ? 103.437 145.752 108.142 1.00 53.58 ?  63  TYR A OH    1 
ATOM   506   N  N     . TYR A 1 64  ? 108.639 152.549 106.834 1.00 47.25 ?  64  TYR A N     1 
ATOM   507   C  CA    . TYR A 1 64  ? 109.629 153.455 106.273 1.00 43.93 ?  64  TYR A CA    1 
ATOM   508   C  C     . TYR A 1 64  ? 109.882 154.623 107.217 1.00 46.86 ?  64  TYR A C     1 
ATOM   509   O  O     . TYR A 1 64  ? 109.201 154.802 108.228 1.00 49.91 ?  64  TYR A O     1 
ATOM   510   C  CB    . TYR A 1 64  ? 109.175 153.984 104.909 1.00 45.49 ?  64  TYR A CB    1 
ATOM   511   C  CG    . TYR A 1 64  ? 109.303 152.991 103.783 1.00 45.64 ?  64  TYR A CG    1 
ATOM   512   C  CD1   . TYR A 1 64  ? 109.922 151.762 103.978 1.00 42.74 ?  64  TYR A CD1   1 
ATOM   513   C  CD2   . TYR A 1 64  ? 108.809 153.283 102.522 1.00 47.43 ?  64  TYR A CD2   1 
ATOM   514   C  CE1   . TYR A 1 64  ? 110.039 150.854 102.949 1.00 40.32 ?  64  TYR A CE1   1 
ATOM   515   C  CE2   . TYR A 1 64  ? 108.923 152.384 101.488 1.00 46.63 ?  64  TYR A CE2   1 
ATOM   516   C  CZ    . TYR A 1 64  ? 109.536 151.171 101.706 1.00 44.90 ?  64  TYR A CZ    1 
ATOM   517   O  OH    . TYR A 1 64  ? 109.647 150.275 100.670 1.00 44.35 ?  64  TYR A OH    1 
ATOM   518   N  N     . GLU A 1 65  ? 110.883 155.422 106.862 1.00 52.27 ?  65  GLU A N     1 
ATOM   519   C  CA    . GLU A 1 65  ? 111.158 156.673 107.550 1.00 50.80 ?  65  GLU A CA    1 
ATOM   520   C  C     . GLU A 1 65  ? 110.562 157.836 106.767 1.00 53.51 ?  65  GLU A C     1 
ATOM   521   O  O     . GLU A 1 65  ? 110.589 157.848 105.533 1.00 54.80 ?  65  GLU A O     1 
ATOM   522   C  CB    . GLU A 1 65  ? 112.663 156.880 107.729 1.00 50.17 ?  65  GLU A CB    1 
ATOM   523   C  CG    . GLU A 1 65  ? 113.271 156.106 108.886 1.00 51.49 ?  65  GLU A CG    1 
ATOM   524   C  CD    . GLU A 1 65  ? 114.744 155.815 108.682 1.00 52.41 ?  65  GLU A CD    1 
ATOM   525   O  OE1   . GLU A 1 65  ? 115.387 156.527 107.882 1.00 53.30 ?  65  GLU A OE1   1 
ATOM   526   O  OE2   . GLU A 1 65  ? 115.264 154.882 109.328 1.00 52.68 -1 65  GLU A OE2   1 
ATOM   527   N  N     . GLU A 1 66  ? 110.014 158.809 107.495 1.00 54.86 ?  66  GLU A N     1 
ATOM   528   C  CA    . GLU A 1 66  ? 109.432 159.983 106.855 1.00 54.45 ?  66  GLU A CA    1 
ATOM   529   C  C     . GLU A 1 66  ? 110.495 160.945 106.343 1.00 56.09 ?  66  GLU A C     1 
ATOM   530   O  O     . GLU A 1 66  ? 110.262 161.646 105.351 1.00 56.40 ?  66  GLU A O     1 
ATOM   531   C  CB    . GLU A 1 66  ? 108.509 160.713 107.835 1.00 55.78 ?  66  GLU A CB    1 
ATOM   532   C  CG    . GLU A 1 66  ? 107.003 160.705 107.512 1.00 57.32 ?  66  GLU A CG    1 
ATOM   533   C  CD    . GLU A 1 66  ? 106.615 161.312 106.161 1.00 58.41 ?  66  GLU A CD    1 
ATOM   534   O  OE1   . GLU A 1 66  ? 107.479 161.543 105.291 1.00 58.37 ?  66  GLU A OE1   1 
ATOM   535   O  OE2   . GLU A 1 66  ? 105.405 161.565 105.971 1.00 55.35 -1 66  GLU A OE2   1 
ATOM   536   N  N     . GLU A 1 67  ? 111.655 160.995 107.000 1.00 54.76 ?  67  GLU A N     1 
ATOM   537   C  CA    . GLU A 1 67  ? 112.636 162.037 106.708 1.00 55.13 ?  67  GLU A CA    1 
ATOM   538   C  C     . GLU A 1 67  ? 113.185 161.913 105.291 1.00 55.53 ?  67  GLU A C     1 
ATOM   539   O  O     . GLU A 1 67  ? 113.248 162.902 104.552 1.00 55.42 ?  67  GLU A O     1 
ATOM   540   C  CB    . GLU A 1 67  ? 113.771 161.983 107.731 1.00 56.55 ?  67  GLU A CB    1 
ATOM   541   C  CG    . GLU A 1 67  ? 113.301 161.951 109.176 1.00 57.39 ?  67  GLU A CG    1 
ATOM   542   C  CD    . GLU A 1 67  ? 113.282 160.550 109.752 1.00 60.75 ?  67  GLU A CD    1 
ATOM   543   O  OE1   . GLU A 1 67  ? 114.363 160.037 110.110 1.00 59.46 ?  67  GLU A OE1   1 
ATOM   544   O  OE2   . GLU A 1 67  ? 112.184 159.961 109.849 1.00 57.42 -1 67  GLU A OE2   1 
ATOM   545   N  N     . PHE A 1 68  ? 113.584 160.703 104.890 1.00 48.39 ?  68  PHE A N     1 
ATOM   546   C  CA    . PHE A 1 68  ? 114.223 160.551 103.587 1.00 44.87 ?  68  PHE A CA    1 
ATOM   547   C  C     . PHE A 1 68  ? 113.216 160.660 102.448 1.00 44.22 ?  68  PHE A C     1 
ATOM   548   O  O     . PHE A 1 68  ? 113.574 161.104 101.351 1.00 47.66 ?  68  PHE A O     1 
ATOM   549   C  CB    . PHE A 1 68  ? 114.986 159.225 103.523 1.00 46.19 ?  68  PHE A CB    1 
ATOM   550   C  CG    . PHE A 1 68  ? 114.164 158.061 103.049 1.00 44.21 ?  68  PHE A CG    1 
ATOM   551   C  CD1   . PHE A 1 68  ? 113.315 157.395 103.917 1.00 44.39 ?  68  PHE A CD1   1 
ATOM   552   C  CD2   . PHE A 1 68  ? 114.264 157.611 101.743 1.00 39.83 ?  68  PHE A CD2   1 
ATOM   553   C  CE1   . PHE A 1 68  ? 112.566 156.319 103.484 1.00 42.62 ?  68  PHE A CE1   1 
ATOM   554   C  CE2   . PHE A 1 68  ? 113.519 156.536 101.305 1.00 43.07 ?  68  PHE A CE2   1 
ATOM   555   C  CZ    . PHE A 1 68  ? 112.670 155.887 102.178 1.00 45.52 ?  68  PHE A CZ    1 
ATOM   556   N  N     . LEU A 1 69  ? 111.962 160.269 102.682 1.00 46.25 ?  69  LEU A N     1 
ATOM   557   C  CA    . LEU A 1 69  ? 110.942 160.429 101.652 1.00 46.48 ?  69  LEU A CA    1 
ATOM   558   C  C     . LEU A 1 69  ? 110.459 161.869 101.544 1.00 48.21 ?  69  LEU A C     1 
ATOM   559   O  O     . LEU A 1 69  ? 110.024 162.291 100.467 1.00 45.42 ?  69  LEU A O     1 
ATOM   560   C  CB    . LEU A 1 69  ? 109.760 159.499 101.929 1.00 45.84 ?  69  LEU A CB    1 
ATOM   561   C  CG    . LEU A 1 69  ? 109.972 158.030 101.555 1.00 43.33 ?  69  LEU A CG    1 
ATOM   562   C  CD1   . LEU A 1 69  ? 108.770 157.189 101.949 1.00 43.30 ?  69  LEU A CD1   1 
ATOM   563   C  CD2   . LEU A 1 69  ? 110.270 157.886 100.071 1.00 42.58 ?  69  LEU A CD2   1 
ATOM   564   N  N     . SER A 1 70  ? 110.529 162.633 102.636 1.00 50.75 ?  70  SER A N     1 
ATOM   565   C  CA    . SER A 1 70  ? 110.068 164.016 102.614 1.00 49.04 ?  70  SER A CA    1 
ATOM   566   C  C     . SER A 1 70  ? 110.986 164.927 101.811 1.00 49.55 ?  70  SER A C     1 
ATOM   567   O  O     . SER A 1 70  ? 110.573 166.032 101.445 1.00 51.31 ?  70  SER A O     1 
ATOM   568   C  CB    . SER A 1 70  ? 109.932 164.545 104.043 1.00 50.83 ?  70  SER A CB    1 
ATOM   569   O  OG    . SER A 1 70  ? 111.203 164.798 104.615 1.00 52.71 ?  70  SER A OG    1 
ATOM   570   N  N     . LEU A 1 71  ? 112.217 164.495 101.530 1.00 44.06 ?  71  LEU A N     1 
ATOM   571   C  CA    . LEU A 1 71  ? 113.140 165.311 100.752 1.00 43.61 ?  71  LEU A CA    1 
ATOM   572   C  C     . LEU A 1 71  ? 112.761 165.392 99.280  1.00 44.26 ?  71  LEU A C     1 
ATOM   573   O  O     . LEU A 1 71  ? 113.299 166.246 98.568  1.00 44.16 ?  71  LEU A O     1 
ATOM   574   C  CB    . LEU A 1 71  ? 114.563 164.766 100.884 1.00 45.70 ?  71  LEU A CB    1 
ATOM   575   C  CG    . LEU A 1 71  ? 115.073 164.535 102.305 1.00 47.64 ?  71  LEU A CG    1 
ATOM   576   C  CD1   . LEU A 1 71  ? 116.168 163.482 102.314 1.00 47.24 ?  71  LEU A CD1   1 
ATOM   577   C  CD2   . LEU A 1 71  ? 115.571 165.837 102.908 1.00 45.83 ?  71  LEU A CD2   1 
ATOM   578   N  N     . TYR A 1 72  ? 111.861 164.535 98.812  1.00 44.00 ?  72  TYR A N     1 
ATOM   579   C  CA    . TYR A 1 72  ? 111.424 164.529 97.425  1.00 44.48 ?  72  TYR A CA    1 
ATOM   580   C  C     . TYR A 1 72  ? 109.937 164.835 97.350  1.00 46.44 ?  72  TYR A C     1 
ATOM   581   O  O     . TYR A 1 72  ? 109.169 164.500 98.256  1.00 47.83 ?  72  TYR A O     1 
ATOM   582   C  CB    . TYR A 1 72  ? 111.681 163.174 96.748  1.00 43.94 ?  72  TYR A CB    1 
ATOM   583   C  CG    . TYR A 1 72  ? 113.056 162.589 96.967  1.00 41.73 ?  72  TYR A CG    1 
ATOM   584   C  CD1   . TYR A 1 72  ? 113.359 161.896 98.131  1.00 42.19 ?  72  TYR A CD1   1 
ATOM   585   C  CD2   . TYR A 1 72  ? 114.043 162.708 96.000  1.00 40.29 ?  72  TYR A CD2   1 
ATOM   586   C  CE1   . TYR A 1 72  ? 114.610 161.355 98.333  1.00 41.19 ?  72  TYR A CE1   1 
ATOM   587   C  CE2   . TYR A 1 72  ? 115.297 162.166 96.191  1.00 40.28 ?  72  TYR A CE2   1 
ATOM   588   C  CZ    . TYR A 1 72  ? 115.574 161.492 97.360  1.00 40.85 ?  72  TYR A CZ    1 
ATOM   589   O  OH    . TYR A 1 72  ? 116.821 160.952 97.560  1.00 43.51 ?  72  TYR A OH    1 
ATOM   590   N  N     . SER A 1 73  ? 109.537 165.480 96.259  1.00 51.19 ?  73  SER A N     1 
ATOM   591   C  CA    . SER A 1 73  ? 108.126 165.528 95.923  1.00 50.58 ?  73  SER A CA    1 
ATOM   592   C  C     . SER A 1 73  ? 107.665 164.143 95.481  1.00 52.96 ?  73  SER A C     1 
ATOM   593   O  O     . SER A 1 73  ? 108.465 163.299 95.067  1.00 52.97 ?  73  SER A O     1 
ATOM   594   C  CB    . SER A 1 73  ? 107.867 166.557 94.823  1.00 50.80 ?  73  SER A CB    1 
ATOM   595   O  OG    . SER A 1 73  ? 108.238 166.050 93.553  1.00 50.85 ?  73  SER A OG    1 
ATOM   596   N  N     . PHE A 1 74  ? 106.357 163.902 95.586  1.00 55.14 ?  74  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 74  ? 105.837 162.594 95.208  1.00 53.82 ?  74  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 74  ? 106.069 162.301 93.732  1.00 55.08 ?  74  PHE A C     1 
ATOM   599   O  O     . PHE A 1 74  ? 106.227 161.138 93.349  1.00 56.91 ?  74  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 74  ? 104.349 162.486 95.538  1.00 54.87 ?  74  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 74  ? 103.687 161.282 94.932  1.00 56.02 ?  74  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 74  ? 103.964 160.015 95.416  1.00 54.35 ?  74  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 74  ? 102.803 161.412 93.874  1.00 56.03 ?  74  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 74  ? 103.370 158.901 94.860  1.00 56.64 ?  74  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 74  ? 102.203 160.300 93.315  1.00 56.94 ?  74  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 74  ? 102.488 159.043 93.810  1.00 57.05 ?  74  PHE A CZ    1 
ATOM   607   N  N     . GLU A 1 75  ? 106.093 163.338 92.889  1.00 54.57 ?  75  GLU A N     1 
ATOM   608   C  CA    . GLU A 1 75  ? 106.369 163.128 91.472  1.00 55.54 ?  75  GLU A CA    1 
ATOM   609   C  C     . GLU A 1 75  ? 107.774 162.575 91.262  1.00 57.99 ?  75  GLU A C     1 
ATOM   610   O  O     . GLU A 1 75  ? 107.979 161.674 90.443  1.00 58.35 ?  75  GLU A O     1 
ATOM   611   C  CB    . GLU A 1 75  ? 106.180 164.437 90.695  1.00 54.90 ?  75  GLU A CB    1 
ATOM   612   C  CG    . GLU A 1 75  ? 104.805 165.161 90.809  1.00 55.52 ?  75  GLU A CG    1 
ATOM   613   C  CD    . GLU A 1 75  ? 103.550 164.274 90.716  1.00 58.83 ?  75  GLU A CD    1 
ATOM   614   O  OE1   . GLU A 1 75  ? 103.630 163.032 90.695  1.00 59.31 ?  75  GLU A OE1   1 
ATOM   615   O  OE2   . GLU A 1 75  ? 102.440 164.851 90.670  1.00 57.49 -1 75  GLU A OE2   1 
ATOM   616   N  N     . ASP A 1 76  ? 108.752 163.093 92.007  1.00 52.85 ?  76  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 76  ? 110.120 162.597 91.888  1.00 49.88 ?  76  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 76  ? 110.238 161.154 92.368  1.00 49.23 ?  76  ASP A C     1 
ATOM   619   O  O     . ASP A 1 76  ? 110.930 160.342 91.744  1.00 53.95 ?  76  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 76  ? 111.070 163.506 92.664  1.00 52.85 ?  76  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 76  ? 111.218 164.872 92.022  1.00 55.11 ?  76  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 76  ? 110.515 165.142 91.026  1.00 54.60 ?  76  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 76  ? 112.044 165.672 92.508  1.00 53.49 -1 76  ASP A OD2   1 
ATOM   624   N  N     . ILE A 1 77  ? 109.569 160.815 93.474  1.00 44.02 ?  77  ILE A N     1 
ATOM   625   C  CA    . ILE A 1 77  ? 109.595 159.438 93.967  1.00 45.79 ?  77  ILE A CA    1 
ATOM   626   C  C     . ILE A 1 77  ? 108.942 158.500 92.961  1.00 44.53 ?  77  ILE A C     1 
ATOM   627   O  O     . ILE A 1 77  ? 109.436 157.394 92.704  1.00 47.23 ?  77  ILE A O     1 
ATOM   628   C  CB    . ILE A 1 77  ? 108.913 159.353 95.346  1.00 46.81 ?  77  ILE A CB    1 
ATOM   629   C  CG1   . ILE A 1 77  ? 109.658 160.222 96.358  1.00 46.87 ?  77  ILE A CG1   1 
ATOM   630   C  CG2   . ILE A 1 77  ? 108.858 157.913 95.827  1.00 44.75 ?  77  ILE A CG2   1 
ATOM   631   C  CD1   . ILE A 1 77  ? 108.940 160.376 97.676  1.00 45.19 ?  77  ILE A CD1   1 
ATOM   632   N  N     . LYS A 1 78  ? 107.816 158.922 92.382  1.00 48.26 ?  78  LYS A N     1 
ATOM   633   C  CA    . LYS A 1 78  ? 107.153 158.112 91.367  1.00 49.51 ?  78  LYS A CA    1 
ATOM   634   C  C     . LYS A 1 78  ? 108.037 157.938 90.140  1.00 49.50 ?  78  LYS A C     1 
ATOM   635   O  O     . LYS A 1 78  ? 108.073 156.856 89.544  1.00 51.38 ?  78  LYS A O     1 
ATOM   636   C  CB    . LYS A 1 78  ? 105.814 158.745 90.985  1.00 51.36 ?  78  LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 78  ? 104.975 157.915 90.032  1.00 50.07 ?  78  LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 78  ? 103.618 158.556 89.803  1.00 51.85 ?  78  LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 78  ? 102.918 157.945 88.605  1.00 53.23 ?  78  LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 78  ? 101.828 158.827 88.109  1.00 50.53 1  78  LYS A NZ    1 
ATOM   641   N  N     . GLU A 1 79  ? 108.757 158.990 89.745  1.00 50.11 ?  79  GLU A N     1 
ATOM   642   C  CA    . GLU A 1 79  ? 109.673 158.878 88.615  1.00 50.50 ?  79  GLU A CA    1 
ATOM   643   C  C     . GLU A 1 79  ? 110.812 157.913 88.916  1.00 48.79 ?  79  GLU A C     1 
ATOM   644   O  O     . GLU A 1 79  ? 111.229 157.145 88.043  1.00 48.81 ?  79  GLU A O     1 
ATOM   645   C  CB    . GLU A 1 79  ? 110.221 160.257 88.238  1.00 50.57 ?  79  GLU A CB    1 
ATOM   646   C  CG    . GLU A 1 79  ? 109.668 160.886 86.941  1.00 51.59 ?  79  GLU A CG    1 
ATOM   647   C  CD    . GLU A 1 79  ? 109.891 160.063 85.663  1.00 55.08 ?  79  GLU A CD    1 
ATOM   648   O  OE1   . GLU A 1 79  ? 109.872 160.678 84.575  1.00 55.04 ?  79  GLU A OE1   1 
ATOM   649   O  OE2   . GLU A 1 79  ? 110.089 158.833 85.715  1.00 54.19 -1 79  GLU A OE2   1 
ATOM   650   N  N     . VAL A 1 80  ? 111.331 157.939 90.144  1.00 44.57 ?  80  VAL A N     1 
ATOM   651   C  CA    . VAL A 1 80  ? 112.387 157.002 90.521  1.00 41.51 ?  80  VAL A CA    1 
ATOM   652   C  C     . VAL A 1 80  ? 111.870 155.566 90.487  1.00 45.35 ?  80  VAL A C     1 
ATOM   653   O  O     . VAL A 1 80  ? 112.543 154.658 89.979  1.00 46.84 ?  80  VAL A O     1 
ATOM   654   C  CB    . VAL A 1 80  ? 112.952 157.376 91.902  1.00 40.87 ?  80  VAL A CB    1 
ATOM   655   C  CG1   . VAL A 1 80  ? 113.871 156.286 92.416  1.00 41.66 ?  80  VAL A CG1   1 
ATOM   656   C  CG2   . VAL A 1 80  ? 113.692 158.698 91.822  1.00 40.91 ?  80  VAL A CG2   1 
ATOM   657   N  N     . PHE A 1 81  ? 110.667 155.338 91.020  1.00 41.17 ?  81  PHE A N     1 
ATOM   658   C  CA    . PHE A 1 81  ? 110.083 153.999 90.981  1.00 39.00 ?  81  PHE A CA    1 
ATOM   659   C  C     . PHE A 1 81  ? 109.831 153.546 89.547  1.00 43.72 ?  81  PHE A C     1 
ATOM   660   O  O     . PHE A 1 81  ? 110.036 152.374 89.210  1.00 47.44 ?  81  PHE A O     1 
ATOM   661   C  CB    . PHE A 1 81  ? 108.785 153.969 91.788  1.00 40.74 ?  81  PHE A CB    1 
ATOM   662   C  CG    . PHE A 1 81  ? 108.977 153.627 93.239  1.00 39.06 ?  81  PHE A CG    1 
ATOM   663   C  CD1   . PHE A 1 81  ? 109.349 154.601 94.151  1.00 40.39 ?  81  PHE A CD1   1 
ATOM   664   C  CD2   . PHE A 1 81  ? 108.785 152.334 93.691  1.00 38.70 ?  81  PHE A CD2   1 
ATOM   665   C  CE1   . PHE A 1 81  ? 109.524 154.292 95.486  1.00 41.25 ?  81  PHE A CE1   1 
ATOM   666   C  CE2   . PHE A 1 81  ? 108.959 152.019 95.026  1.00 39.22 ?  81  PHE A CE2   1 
ATOM   667   C  CZ    . PHE A 1 81  ? 109.329 153.000 95.923  1.00 39.43 ?  81  PHE A CZ    1 
ATOM   668   N  N     . LYS A 1 82  ? 109.376 154.461 88.689  1.00 45.50 ?  82  LYS A N     1 
ATOM   669   C  CA    . LYS A 1 82  ? 109.154 154.129 87.287  1.00 44.86 ?  82  LYS A CA    1 
ATOM   670   C  C     . LYS A 1 82  ? 110.464 153.791 86.589  1.00 44.10 ?  82  LYS A C     1 
ATOM   671   O  O     . LYS A 1 82  ? 110.509 152.886 85.751  1.00 46.58 ?  82  LYS A O     1 
ATOM   672   C  CB    . LYS A 1 82  ? 108.449 155.286 86.581  1.00 46.41 ?  82  LYS A CB    1 
ATOM   673   C  CG    . LYS A 1 82  ? 106.950 155.328 86.808  1.00 47.69 ?  82  LYS A CG    1 
ATOM   674   C  CD    . LYS A 1 82  ? 106.278 156.314 85.868  1.00 49.23 ?  82  LYS A CD    1 
ATOM   675   C  CE    . LYS A 1 82  ? 104.889 155.841 85.479  1.00 48.47 ?  82  LYS A CE    1 
ATOM   676   N  NZ    . LYS A 1 82  ? 104.806 154.354 85.440  1.00 48.61 1  82  LYS A NZ    1 
ATOM   677   N  N     . THR A 1 83  ? 111.536 154.516 86.911  1.00 41.81 ?  83  THR A N     1 
ATOM   678   C  CA    . THR A 1 83  ? 112.845 154.185 86.358  1.00 42.61 ?  83  THR A CA    1 
ATOM   679   C  C     . THR A 1 83  ? 113.295 152.803 86.814  1.00 44.80 ?  83  THR A C     1 
ATOM   680   O  O     . THR A 1 83  ? 113.882 152.043 86.035  1.00 47.02 ?  83  THR A O     1 
ATOM   681   C  CB    . THR A 1 83  ? 113.872 155.244 86.764  1.00 42.16 ?  83  THR A CB    1 
ATOM   682   O  OG1   . THR A 1 83  ? 113.400 156.541 86.376  1.00 47.88 ?  83  THR A OG1   1 
ATOM   683   C  CG2   . THR A 1 83  ? 115.207 154.981 86.089  1.00 43.17 ?  83  THR A CG2   1 
ATOM   684   N  N     . ALA A 1 84  ? 113.030 152.464 88.077  1.00 38.43 ?  84  ALA A N     1 
ATOM   685   C  CA    . ALA A 1 84  ? 113.372 151.130 88.567  1.00 35.86 ?  84  ALA A CA    1 
ATOM   686   C  C     . ALA A 1 84  ? 112.585 150.049 87.839  1.00 39.07 ?  84  ALA A C     1 
ATOM   687   O  O     . ALA A 1 84  ? 113.140 149.008 87.469  1.00 42.31 ?  84  ALA A O     1 
ATOM   688   C  CB    . ALA A 1 84  ? 113.131 151.045 90.071  1.00 36.56 ?  84  ALA A CB    1 
ATOM   689   N  N     . TYR A 1 85  ? 111.290 150.274 87.623  1.00 44.03 ?  85  TYR A N     1 
ATOM   690   C  CA    . TYR A 1 85  ? 110.443 149.270 86.991  1.00 39.83 ?  85  TYR A CA    1 
ATOM   691   C  C     . TYR A 1 85  ? 110.579 149.226 85.474  1.00 40.48 ?  85  TYR A C     1 
ATOM   692   O  O     . TYR A 1 85  ? 110.151 148.242 84.862  1.00 41.84 ?  85  TYR A O     1 
ATOM   693   C  CB    . TYR A 1 85  ? 108.978 149.510 87.363  1.00 41.64 ?  85  TYR A CB    1 
ATOM   694   C  CG    . TYR A 1 85  ? 108.581 148.932 88.702  1.00 41.09 ?  85  TYR A CG    1 
ATOM   695   C  CD1   . TYR A 1 85  ? 108.110 147.631 88.803  1.00 39.31 ?  85  TYR A CD1   1 
ATOM   696   C  CD2   . TYR A 1 85  ? 108.677 149.685 89.864  1.00 42.16 ?  85  TYR A CD2   1 
ATOM   697   C  CE1   . TYR A 1 85  ? 107.745 147.095 90.021  1.00 41.12 ?  85  TYR A CE1   1 
ATOM   698   C  CE2   . TYR A 1 85  ? 108.314 149.158 91.088  1.00 42.11 ?  85  TYR A CE2   1 
ATOM   699   C  CZ    . TYR A 1 85  ? 107.848 147.864 91.160  1.00 43.05 ?  85  TYR A CZ    1 
ATOM   700   O  OH    . TYR A 1 85  ? 107.485 147.333 92.375  1.00 43.05 ?  85  TYR A OH    1 
ATOM   701   N  N     . ALA A 1 86  ? 111.161 150.256 84.854  1.00 40.35 ?  86  ALA A N     1 
ATOM   702   C  CA    . ALA A 1 86  ? 111.318 150.261 83.406  1.00 40.94 ?  86  ALA A CA    1 
ATOM   703   C  C     . ALA A 1 86  ? 112.344 149.246 82.928  1.00 45.40 ?  86  ALA A C     1 
ATOM   704   O  O     . ALA A 1 86  ? 112.292 148.831 81.766  1.00 45.64 ?  86  ALA A O     1 
ATOM   705   C  CB    . ALA A 1 86  ? 111.708 151.658 82.925  1.00 39.65 ?  86  ALA A CB    1 
ATOM   706   N  N     . LYS A 1 87  ? 113.275 148.842 83.794  1.00 43.91 ?  87  LYS A N     1 
ATOM   707   C  CA    . LYS A 1 87  ? 114.251 147.829 83.411  1.00 41.44 ?  87  LYS A CA    1 
ATOM   708   C  C     . LYS A 1 87  ? 113.588 146.480 83.162  1.00 42.51 ?  87  LYS A C     1 
ATOM   709   O  O     . LYS A 1 87  ? 114.093 145.682 82.364  1.00 44.65 ?  87  LYS A O     1 
ATOM   710   C  CB    . LYS A 1 87  ? 115.329 147.714 84.492  1.00 41.57 ?  87  LYS A CB    1 
ATOM   711   C  CG    . LYS A 1 87  ? 116.268 146.528 84.332  1.00 43.60 ?  87  LYS A CG    1 
ATOM   712   C  CD    . LYS A 1 87  ? 117.683 146.976 84.026  1.00 40.15 ?  87  LYS A CD    1 
ATOM   713   C  CE    . LYS A 1 87  ? 118.611 145.787 83.851  1.00 40.86 ?  87  LYS A CE    1 
ATOM   714   N  NZ    . LYS A 1 87  ? 119.488 145.941 82.658  1.00 42.63 1  87  LYS A NZ    1 
ATOM   715   N  N     . LYS A 1 88  ? 112.446 146.228 83.805  1.00 43.17 ?  88  LYS A N     1 
ATOM   716   C  CA    . LYS A 1 88  ? 111.783 144.924 83.763  1.00 41.87 ?  88  LYS A CA    1 
ATOM   717   C  C     . LYS A 1 88  ? 112.741 143.828 84.220  1.00 40.24 ?  88  LYS A C     1 
ATOM   718   O  O     . LYS A 1 88  ? 112.878 142.779 83.585  1.00 43.96 ?  88  LYS A O     1 
ATOM   719   C  CB    . LYS A 1 88  ? 111.223 144.628 82.369  1.00 43.41 ?  88  LYS A CB    1 
ATOM   720   C  CG    . LYS A 1 88  ? 109.797 145.110 82.152  1.00 44.06 ?  88  LYS A CG    1 
ATOM   721   C  CD    . LYS A 1 88  ? 109.768 146.419 81.378  1.00 44.79 ?  88  LYS A CD    1 
ATOM   722   C  CE    . LYS A 1 88  ? 108.652 147.328 81.868  1.00 45.47 ?  88  LYS A CE    1 
ATOM   723   N  NZ    . LYS A 1 88  ? 108.713 148.676 81.235  1.00 43.81 1  88  LYS A NZ    1 
ATOM   724   N  N     . PHE A 1 89  ? 113.420 144.090 85.335  1.00 39.10 ?  89  PHE A N     1 
ATOM   725   C  CA    . PHE A 1 89  ? 114.418 143.163 85.847  1.00 33.63 ?  89  PHE A CA    1 
ATOM   726   C  C     . PHE A 1 89  ? 113.784 141.824 86.192  1.00 40.27 ?  89  PHE A C     1 
ATOM   727   O  O     . PHE A 1 89  ? 112.715 141.760 86.807  1.00 42.10 ?  89  PHE A O     1 
ATOM   728   C  CB    . PHE A 1 89  ? 115.106 143.750 87.081  1.00 34.46 ?  89  PHE A CB    1 
ATOM   729   C  CG    . PHE A 1 89  ? 116.053 142.799 87.754  1.00 34.23 ?  89  PHE A CG    1 
ATOM   730   C  CD1   . PHE A 1 89  ? 117.346 142.647 87.288  1.00 34.64 ?  89  PHE A CD1   1 
ATOM   731   C  CD2   . PHE A 1 89  ? 115.649 142.053 88.848  1.00 35.69 ?  89  PHE A CD2   1 
ATOM   732   C  CE1   . PHE A 1 89  ? 118.218 141.771 87.901  1.00 37.08 ?  89  PHE A CE1   1 
ATOM   733   C  CE2   . PHE A 1 89  ? 116.517 141.174 89.462  1.00 32.64 ?  89  PHE A CE2   1 
ATOM   734   C  CZ    . PHE A 1 89  ? 117.803 141.034 88.990  1.00 35.02 ?  89  PHE A CZ    1 
ATOM   735   N  N     . ARG A 1 90  ? 114.454 140.748 85.790  1.00 41.70 ?  90  ARG A N     1 
ATOM   736   C  CA    . ARG A 1 90  ? 114.023 139.392 86.095  1.00 40.07 ?  90  ARG A CA    1 
ATOM   737   C  C     . ARG A 1 90  ? 115.173 138.650 86.752  1.00 39.11 ?  90  ARG A C     1 
ATOM   738   O  O     . ARG A 1 90  ? 116.302 138.682 86.252  1.00 40.65 ?  90  ARG A O     1 
ATOM   739   C  CB    . ARG A 1 90  ? 113.567 138.655 84.830  1.00 39.99 ?  90  ARG A CB    1 
ATOM   740   C  CG    . ARG A 1 90  ? 112.486 139.372 84.043  1.00 41.43 ?  90  ARG A CG    1 
ATOM   741   C  CD    . ARG A 1 90  ? 111.157 139.349 84.777  1.00 42.63 ?  90  ARG A CD    1 
ATOM   742   N  NE    . ARG A 1 90  ? 110.194 140.270 84.186  1.00 44.13 ?  90  ARG A NE    1 
ATOM   743   C  CZ    . ARG A 1 90  ? 109.641 141.290 84.828  1.00 45.93 ?  90  ARG A CZ    1 
ATOM   744   N  NH1   . ARG A 1 90  ? 109.925 141.544 86.095  1.00 45.56 1  90  ARG A NH1   1 
ATOM   745   N  NH2   . ARG A 1 90  ? 108.781 142.072 84.184  1.00 43.70 ?  90  ARG A NH2   1 
ATOM   746   N  N     . PHE A 1 91  ? 114.891 137.997 87.870  1.00 36.18 ?  91  PHE A N     1 
ATOM   747   C  CA    . PHE A 1 91  ? 115.897 137.169 88.515  1.00 37.86 ?  91  PHE A CA    1 
ATOM   748   C  C     . PHE A 1 91  ? 116.225 135.982 87.617  1.00 43.33 ?  91  PHE A C     1 
ATOM   749   O  O     . PHE A 1 91  ? 115.316 135.250 87.211  1.00 44.55 ?  91  PHE A O     1 
ATOM   750   C  CB    . PHE A 1 91  ? 115.404 136.688 89.877  1.00 35.06 ?  91  PHE A CB    1 
ATOM   751   C  CG    . PHE A 1 91  ? 115.319 137.775 90.910  1.00 39.65 ?  91  PHE A CG    1 
ATOM   752   C  CD1   . PHE A 1 91  ? 116.441 138.157 91.627  1.00 41.67 ?  91  PHE A CD1   1 
ATOM   753   C  CD2   . PHE A 1 91  ? 114.120 138.418 91.162  1.00 38.52 ?  91  PHE A CD2   1 
ATOM   754   C  CE1   . PHE A 1 91  ? 116.367 139.156 92.578  1.00 39.51 ?  91  PHE A CE1   1 
ATOM   755   C  CE2   . PHE A 1 91  ? 114.040 139.418 92.112  1.00 38.91 ?  91  PHE A CE2   1 
ATOM   756   C  CZ    . PHE A 1 91  ? 115.165 139.787 92.820  1.00 38.48 ?  91  PHE A CZ    1 
ATOM   757   N  N     . PRO A 1 92  ? 117.499 135.758 87.282  1.00 43.39 ?  92  PRO A N     1 
ATOM   758   C  CA    . PRO A 1 92  ? 117.829 134.664 86.359  1.00 42.30 ?  92  PRO A CA    1 
ATOM   759   C  C     . PRO A 1 92  ? 117.788 133.288 86.995  1.00 43.13 ?  92  PRO A C     1 
ATOM   760   O  O     . PRO A 1 92  ? 117.675 132.293 86.266  1.00 44.76 ?  92  PRO A O     1 
ATOM   761   C  CB    . PRO A 1 92  ? 119.246 135.018 85.899  1.00 42.75 ?  92  PRO A CB    1 
ATOM   762   C  CG    . PRO A 1 92  ? 119.835 135.712 87.082  1.00 43.24 ?  92  PRO A CG    1 
ATOM   763   C  CD    . PRO A 1 92  ? 118.705 136.457 87.761  1.00 40.50 ?  92  PRO A CD    1 
ATOM   764   N  N     . SER A 1 93  ? 117.875 133.198 88.319  1.00 42.55 ?  93  SER A N     1 
ATOM   765   C  CA    . SER A 1 93  ? 117.882 131.927 89.022  1.00 41.96 ?  93  SER A CA    1 
ATOM   766   C  C     . SER A 1 93  ? 116.887 131.985 90.172  1.00 44.09 ?  93  SER A C     1 
ATOM   767   O  O     . SER A 1 93  ? 116.572 133.057 90.694  1.00 47.27 ?  93  SER A O     1 
ATOM   768   C  CB    . SER A 1 93  ? 119.281 131.582 89.547  1.00 43.27 ?  93  SER A CB    1 
ATOM   769   O  OG    . SER A 1 93  ? 119.505 132.163 90.819  1.00 45.05 ?  93  SER A OG    1 
ATOM   770   N  N     . PHE A 1 94  ? 116.383 130.809 90.551  1.00 43.75 ?  94  PHE A N     1 
ATOM   771   C  CA    . PHE A 1 94  ? 115.398 130.741 91.625  1.00 40.05 ?  94  PHE A CA    1 
ATOM   772   C  C     . PHE A 1 94  ? 115.988 131.213 92.947  1.00 42.38 ?  94  PHE A C     1 
ATOM   773   O  O     . PHE A 1 94  ? 115.311 131.894 93.727  1.00 44.10 ?  94  PHE A O     1 
ATOM   774   C  CB    . PHE A 1 94  ? 114.859 129.317 91.760  1.00 40.38 ?  94  PHE A CB    1 
ATOM   775   C  CG    . PHE A 1 94  ? 114.304 129.010 93.122  1.00 41.40 ?  94  PHE A CG    1 
ATOM   776   C  CD1   . PHE A 1 94  ? 113.099 129.555 93.531  1.00 41.31 ?  94  PHE A CD1   1 
ATOM   777   C  CD2   . PHE A 1 94  ? 114.989 128.181 93.993  1.00 44.07 ?  94  PHE A CD2   1 
ATOM   778   C  CE1   . PHE A 1 94  ? 112.591 129.281 94.784  1.00 41.35 ?  94  PHE A CE1   1 
ATOM   779   C  CE2   . PHE A 1 94  ? 114.482 127.902 95.247  1.00 45.35 ?  94  PHE A CE2   1 
ATOM   780   C  CZ    . PHE A 1 94  ? 113.281 128.452 95.642  1.00 41.55 ?  94  PHE A CZ    1 
ATOM   781   N  N     . MET A 1 95  ? 117.245 130.857 93.220  1.00 41.51 ?  95  MET A N     1 
ATOM   782   C  CA    . MET A 1 95  ? 117.843 131.198 94.504  1.00 39.30 ?  95  MET A CA    1 
ATOM   783   C  C     . MET A 1 95  ? 118.007 132.701 94.678  1.00 41.31 ?  95  MET A C     1 
ATOM   784   O  O     . MET A 1 95  ? 117.915 133.197 95.804  1.00 42.06 ?  95  MET A O     1 
ATOM   785   C  CB    . MET A 1 95  ? 119.189 130.491 94.666  1.00 40.51 ?  95  MET A CB    1 
ATOM   786   C  CG    . MET A 1 95  ? 119.822 130.614 96.053  1.00 43.89 ?  95  MET A CG    1 
ATOM   787   S  SD    . MET A 1 95  ? 118.951 129.884 97.464  1.00 54.57 ?  95  MET A SD    1 
ATOM   788   C  CE    . MET A 1 95  ? 117.937 128.616 96.704  1.00 45.92 ?  95  MET A CE    1 
ATOM   789   N  N     . SER A 1 96  ? 118.235 133.442 93.593  1.00 38.56 ?  96  SER A N     1 
ATOM   790   C  CA    . SER A 1 96  ? 118.339 134.895 93.704  1.00 34.14 ?  96  SER A CA    1 
ATOM   791   C  C     . SER A 1 96  ? 117.050 135.496 94.252  1.00 38.41 ?  96  SER A C     1 
ATOM   792   O  O     . SER A 1 96  ? 117.059 136.227 95.253  1.00 40.40 ?  96  SER A O     1 
ATOM   793   C  CB    . SER A 1 96  ? 118.671 135.494 92.338  1.00 32.01 ?  96  SER A CB    1 
ATOM   794   O  OG    . SER A 1 96  ? 119.664 134.734 91.676  1.00 36.90 ?  96  SER A OG    1 
ATOM   795   N  N     . ALA A 1 97  ? 115.923 135.173 93.615  1.00 38.59 ?  97  ALA A N     1 
ATOM   796   C  CA    . ALA A 1 97  ? 114.637 135.693 94.061  1.00 34.80 ?  97  ALA A CA    1 
ATOM   797   C  C     . ALA A 1 97  ? 114.275 135.162 95.438  1.00 35.83 ?  97  ALA A C     1 
ATOM   798   O  O     . ALA A 1 97  ? 113.726 135.896 96.267  1.00 41.87 ?  97  ALA A O     1 
ATOM   799   C  CB    . ALA A 1 97  ? 113.551 135.339 93.047  1.00 36.02 ?  97  ALA A CB    1 
ATOM   800   N  N     . PHE A 1 98  ? 114.564 133.885 95.699  1.00 37.46 ?  98  PHE A N     1 
ATOM   801   C  CA    . PHE A 1 98  ? 114.253 133.315 97.004  1.00 37.31 ?  98  PHE A CA    1 
ATOM   802   C  C     . PHE A 1 98  ? 115.022 134.024 98.110  1.00 37.48 ?  98  PHE A C     1 
ATOM   803   O  O     . PHE A 1 98  ? 114.447 134.382 99.142  1.00 46.19 ?  98  PHE A O     1 
ATOM   804   C  CB    . PHE A 1 98  ? 114.563 131.818 97.012  1.00 41.86 ?  98  PHE A CB    1 
ATOM   805   C  CG    . PHE A 1 98  ? 114.316 131.159 98.337  1.00 42.40 ?  98  PHE A CG    1 
ATOM   806   C  CD1   . PHE A 1 98  ? 113.033 130.809 98.720  1.00 42.56 ?  98  PHE A CD1   1 
ATOM   807   C  CD2   . PHE A 1 98  ? 115.364 130.897 99.203  1.00 41.56 ?  98  PHE A CD2   1 
ATOM   808   C  CE1   . PHE A 1 98  ? 112.801 130.205 99.939  1.00 43.31 ?  98  PHE A CE1   1 
ATOM   809   C  CE2   . PHE A 1 98  ? 115.137 130.294 100.424 1.00 42.84 ?  98  PHE A CE2   1 
ATOM   810   C  CZ    . PHE A 1 98  ? 113.854 129.948 100.793 1.00 44.36 ?  98  PHE A CZ    1 
ATOM   811   N  N     . LYS A 1 99  ? 116.320 134.254 97.902  1.00 38.45 ?  99  LYS A N     1 
ATOM   812   C  CA    . LYS A 1 99  ? 117.129 134.931 98.906  1.00 36.82 ?  99  LYS A CA    1 
ATOM   813   C  C     . LYS A 1 99  ? 116.673 136.367 99.103  1.00 38.12 ?  99  LYS A C     1 
ATOM   814   O  O     . LYS A 1 99  ? 116.622 136.852 100.241 1.00 43.28 ?  99  LYS A O     1 
ATOM   815   C  CB    . LYS A 1 99  ? 118.604 134.882 98.509  1.00 37.70 ?  99  LYS A CB    1 
ATOM   816   C  CG    . LYS A 1 99  ? 119.271 133.544 98.776  1.00 39.76 ?  99  LYS A CG    1 
ATOM   817   C  CD    . LYS A 1 99  ? 118.979 133.043 100.178 1.00 41.23 ?  99  LYS A CD    1 
ATOM   818   C  CE    . LYS A 1 99  ? 120.238 132.528 100.853 1.00 39.84 ?  99  LYS A CE    1 
ATOM   819   N  NZ    . LYS A 1 99  ? 120.058 132.401 102.324 1.00 43.67 1  99  LYS A NZ    1 
ATOM   820   N  N     . PHE A 1 100 ? 116.329 137.068 98.019  1.00 33.98 ?  100 PHE A N     1 
ATOM   821   C  CA    . PHE A 1 100 ? 115.861 138.440 98.190  1.00 32.03 ?  100 PHE A CA    1 
ATOM   822   C  C     . PHE A 1 100 ? 114.547 138.487 98.959  1.00 35.49 ?  100 PHE A C     1 
ATOM   823   O  O     . PHE A 1 100 ? 114.406 139.253 99.920  1.00 40.64 ?  100 PHE A O     1 
ATOM   824   C  CB    . PHE A 1 100 ? 115.698 139.145 96.847  1.00 29.77 ?  100 PHE A CB    1 
ATOM   825   C  CG    . PHE A 1 100 ? 115.053 140.492 96.975  1.00 36.38 ?  100 PHE A CG    1 
ATOM   826   C  CD1   . PHE A 1 100 ? 115.760 141.561 97.500  1.00 36.19 ?  100 PHE A CD1   1 
ATOM   827   C  CD2   . PHE A 1 100 ? 113.729 140.680 96.624  1.00 35.11 ?  100 PHE A CD2   1 
ATOM   828   C  CE1   . PHE A 1 100 ? 115.168 142.797 97.645  1.00 35.16 ?  100 PHE A CE1   1 
ATOM   829   C  CE2   . PHE A 1 100 ? 113.130 141.914 96.770  1.00 35.41 ?  100 PHE A CE2   1 
ATOM   830   C  CZ    . PHE A 1 100 ? 113.852 142.974 97.281  1.00 35.14 ?  100 PHE A CZ    1 
ATOM   831   N  N     . TYR A 1 101 ? 113.569 137.676 98.554  1.00 38.04 ?  101 TYR A N     1 
ATOM   832   C  CA    . TYR A 1 101 ? 112.246 137.745 99.157  1.00 37.60 ?  101 TYR A CA    1 
ATOM   833   C  C     . TYR A 1 101 ? 112.163 137.030 100.498 1.00 38.38 ?  101 TYR A C     1 
ATOM   834   O  O     . TYR A 1 101 ? 111.136 137.139 101.175 1.00 44.60 ?  101 TYR A O     1 
ATOM   835   C  CB    . TYR A 1 101 ? 111.203 137.180 98.190  1.00 36.13 ?  101 TYR A CB    1 
ATOM   836   C  CG    . TYR A 1 101 ? 110.887 138.123 97.051  1.00 32.59 ?  101 TYR A CG    1 
ATOM   837   C  CD1   . TYR A 1 101 ? 110.100 139.248 97.255  1.00 36.94 ?  101 TYR A CD1   1 
ATOM   838   C  CD2   . TYR A 1 101 ? 111.389 137.898 95.777  1.00 34.18 ?  101 TYR A CD2   1 
ATOM   839   C  CE1   . TYR A 1 101 ? 109.818 140.116 96.221  1.00 38.04 ?  101 TYR A CE1   1 
ATOM   840   C  CE2   . TYR A 1 101 ? 111.111 138.760 94.738  1.00 36.49 ?  101 TYR A CE2   1 
ATOM   841   C  CZ    . TYR A 1 101 ? 110.324 139.868 94.965  1.00 38.47 ?  101 TYR A CZ    1 
ATOM   842   O  OH    . TYR A 1 101 ? 110.044 140.730 93.930  1.00 41.93 ?  101 TYR A OH    1 
ATOM   843   N  N     . ASN A 1 102 ? 113.209 136.307 100.898 1.00 41.74 ?  102 ASN A N     1 
ATOM   844   C  CA    . ASN A 1 102 ? 113.267 135.715 102.225 1.00 45.03 ?  102 ASN A CA    1 
ATOM   845   C  C     . ASN A 1 102 ? 114.156 136.488 103.187 1.00 45.97 ?  102 ASN A C     1 
ATOM   846   O  O     . ASN A 1 102 ? 113.980 136.358 104.404 1.00 48.30 ?  102 ASN A O     1 
ATOM   847   C  CB    . ASN A 1 102 ? 113.768 134.268 102.136 1.00 42.99 ?  102 ASN A CB    1 
ATOM   848   C  CG    . ASN A 1 102 ? 112.641 133.256 102.174 1.00 46.78 ?  102 ASN A CG    1 
ATOM   849   O  OD1   . ASN A 1 102 ? 111.816 133.192 101.263 1.00 48.92 ?  102 ASN A OD1   1 
ATOM   850   N  ND2   . ASN A 1 102 ? 112.604 132.453 103.230 1.00 44.50 ?  102 ASN A ND2   1 
ATOM   851   N  N     . ASP A 1 103 ? 115.099 137.282 102.680 1.00 41.29 ?  103 ASP A N     1 
ATOM   852   C  CA    . ASP A 1 103 ? 116.046 137.990 103.528 1.00 41.46 ?  103 ASP A CA    1 
ATOM   853   C  C     . ASP A 1 103 ? 115.934 139.504 103.457 1.00 40.82 ?  103 ASP A C     1 
ATOM   854   O  O     . ASP A 1 103 ? 116.121 140.166 104.479 1.00 45.01 ?  103 ASP A O     1 
ATOM   855   C  CB    . ASP A 1 103 ? 117.483 137.593 103.167 1.00 44.47 ?  103 ASP A CB    1 
ATOM   856   C  CG    . ASP A 1 103 ? 117.799 136.157 103.528 1.00 48.51 ?  103 ASP A CG    1 
ATOM   857   O  OD1   . ASP A 1 103 ? 116.949 135.502 104.165 1.00 47.69 ?  103 ASP A OD1   1 
ATOM   858   O  OD2   . ASP A 1 103 ? 118.897 135.683 103.172 1.00 50.67 -1 103 ASP A OD2   1 
ATOM   859   N  N     . TYR A 1 104 ? 115.633 140.070 102.291 1.00 34.75 ?  104 TYR A N     1 
ATOM   860   C  CA    . TYR A 1 104 ? 115.716 141.511 102.099 1.00 38.48 ?  104 TYR A CA    1 
ATOM   861   C  C     . TYR A 1 104 ? 114.388 142.184 101.792 1.00 39.62 ?  104 TYR A C     1 
ATOM   862   O  O     . TYR A 1 104 ? 114.226 143.359 102.125 1.00 43.43 ?  104 TYR A O     1 
ATOM   863   C  CB    . TYR A 1 104 ? 116.710 141.839 100.974 1.00 38.18 ?  104 TYR A CB    1 
ATOM   864   C  CG    . TYR A 1 104 ? 118.101 141.314 101.239 1.00 40.21 ?  104 TYR A CG    1 
ATOM   865   C  CD1   . TYR A 1 104 ? 119.003 142.038 102.008 1.00 37.87 ?  104 TYR A CD1   1 
ATOM   866   C  CD2   . TYR A 1 104 ? 118.510 140.089 100.731 1.00 35.30 ?  104 TYR A CD2   1 
ATOM   867   C  CE1   . TYR A 1 104 ? 120.272 141.559 102.257 1.00 36.61 ?  104 TYR A CE1   1 
ATOM   868   C  CE2   . TYR A 1 104 ? 119.775 139.601 100.977 1.00 35.79 ?  104 TYR A CE2   1 
ATOM   869   C  CZ    . TYR A 1 104 ? 120.653 140.340 101.740 1.00 39.06 ?  104 TYR A CZ    1 
ATOM   870   O  OH    . TYR A 1 104 ? 121.917 139.858 101.985 1.00 40.64 ?  104 TYR A OH    1 
ATOM   871   N  N     . ALA A 1 105 ? 113.443 141.489 101.165 1.00 40.76 ?  105 ALA A N     1 
ATOM   872   C  CA    . ALA A 1 105 ? 112.161 142.104 100.853 1.00 38.14 ?  105 ALA A CA    1 
ATOM   873   C  C     . ALA A 1 105 ? 111.403 142.435 102.133 1.00 42.98 ?  105 ALA A C     1 
ATOM   874   O  O     . ALA A 1 105 ? 111.343 141.629 103.065 1.00 44.65 ?  105 ALA A O     1 
ATOM   875   C  CB    . ALA A 1 105 ? 111.325 141.180 99.969  1.00 37.75 ?  105 ALA A CB    1 
ATOM   876   N  N     . LEU A 1 106 ? 110.828 143.633 102.174 1.00 44.74 ?  106 LEU A N     1 
ATOM   877   C  CA    . LEU A 1 106 ? 110.080 144.061 103.347 1.00 40.94 ?  106 LEU A CA    1 
ATOM   878   C  C     . LEU A 1 106 ? 108.783 143.273 103.462 1.00 45.24 ?  106 LEU A C     1 
ATOM   879   O  O     . LEU A 1 106 ? 108.018 143.166 102.499 1.00 46.46 ?  106 LEU A O     1 
ATOM   880   C  CB    . LEU A 1 106 ? 109.786 145.557 103.274 1.00 44.43 ?  106 LEU A CB    1 
ATOM   881   C  CG    . LEU A 1 106 ? 109.038 146.162 104.464 1.00 43.46 ?  106 LEU A CG    1 
ATOM   882   C  CD1   . LEU A 1 106 ? 109.889 146.100 105.722 1.00 42.46 ?  106 LEU A CD1   1 
ATOM   883   C  CD2   . LEU A 1 106 ? 108.624 147.591 104.163 1.00 43.80 ?  106 LEU A CD2   1 
ATOM   884   N  N     . LYS A 1 107 ? 108.536 142.724 104.646 1.00 50.99 ?  107 LYS A N     1 
ATOM   885   C  CA    . LYS A 1 107 ? 107.340 141.948 104.925 1.00 50.88 ?  107 LYS A CA    1 
ATOM   886   C  C     . LYS A 1 107 ? 106.529 142.627 106.020 1.00 54.09 ?  107 LYS A C     1 
ATOM   887   O  O     . LYS A 1 107 ? 107.040 143.454 106.780 1.00 54.52 ?  107 LYS A O     1 
ATOM   888   C  CB    . LYS A 1 107 ? 107.689 140.514 105.343 1.00 51.63 ?  107 LYS A CB    1 
ATOM   889   C  CG    . LYS A 1 107 ? 108.838 139.899 104.561 1.00 50.31 ?  107 LYS A CG    1 
ATOM   890   C  CD    . LYS A 1 107 ? 108.333 138.915 103.520 1.00 50.99 ?  107 LYS A CD    1 
ATOM   891   C  CE    . LYS A 1 107 ? 109.060 137.584 103.622 1.00 54.46 ?  107 LYS A CE    1 
ATOM   892   N  NZ    . LYS A 1 107 ? 108.798 136.714 102.442 1.00 51.38 1  107 LYS A NZ    1 
ATOM   893   N  N     . THR A 1 108 ? 105.250 142.269 106.087 1.00 58.40 ?  108 THR A N     1 
ATOM   894   C  CA    . THR A 1 108 ? 104.374 142.800 107.118 1.00 57.21 ?  108 THR A CA    1 
ATOM   895   C  C     . THR A 1 108 ? 104.834 142.333 108.500 1.00 59.00 ?  108 THR A C     1 
ATOM   896   O  O     . THR A 1 108 ? 105.703 141.470 108.640 1.00 59.19 ?  108 THR A O     1 
ATOM   897   C  CB    . THR A 1 108 ? 102.930 142.370 106.865 1.00 57.88 ?  108 THR A CB    1 
ATOM   898   O  OG1   . THR A 1 108 ? 102.863 140.940 106.796 1.00 63.02 ?  108 THR A OG1   1 
ATOM   899   C  CG2   . THR A 1 108 ? 102.424 142.956 105.557 1.00 57.15 ?  108 THR A CG2   1 
ATOM   900   N  N     . ASN A 1 109 ? 104.234 142.926 109.536 1.00 60.83 ?  109 ASN A N     1 
ATOM   901   C  CA    . ASN A 1 109 ? 104.587 142.554 110.903 1.00 62.67 ?  109 ASN A CA    1 
ATOM   902   C  C     . ASN A 1 109 ? 104.285 141.088 111.183 1.00 64.04 ?  109 ASN A C     1 
ATOM   903   O  O     . ASN A 1 109 ? 104.955 140.463 112.012 1.00 64.25 ?  109 ASN A O     1 
ATOM   904   C  CB    . ASN A 1 109 ? 103.847 143.445 111.901 1.00 62.17 ?  109 ASN A CB    1 
ATOM   905   C  CG    . ASN A 1 109 ? 104.166 144.914 111.717 1.00 61.16 ?  109 ASN A CG    1 
ATOM   906   O  OD1   . ASN A 1 109 ? 104.347 145.386 110.595 1.00 60.42 ?  109 ASN A OD1   1 
ATOM   907   N  ND2   . ASN A 1 109 ? 104.237 145.648 112.821 1.00 61.63 ?  109 ASN A ND2   1 
ATOM   908   N  N     . ASP A 1 110 ? 103.288 140.526 110.506 1.00 65.81 ?  110 ASP A N     1 
ATOM   909   C  CA    . ASP A 1 110 ? 102.934 139.121 110.641 1.00 64.93 ?  110 ASP A CA    1 
ATOM   910   C  C     . ASP A 1 110 ? 103.759 138.208 109.742 1.00 67.09 ?  110 ASP A C     1 
ATOM   911   O  O     . ASP A 1 110 ? 103.596 136.985 109.812 1.00 67.07 ?  110 ASP A O     1 
ATOM   912   C  CB    . ASP A 1 110 ? 101.441 138.936 110.359 1.00 67.12 ?  110 ASP A CB    1 
ATOM   913   C  CG    . ASP A 1 110 ? 101.060 139.358 108.952 1.00 68.83 ?  110 ASP A CG    1 
ATOM   914   O  OD1   . ASP A 1 110 ? 101.942 139.863 108.226 1.00 68.34 ?  110 ASP A OD1   1 
ATOM   915   O  OD2   . ASP A 1 110 ? 99.883  139.195 108.574 1.00 66.30 -1 110 ASP A OD2   1 
ATOM   916   N  N     . LYS A 1 111 ? 104.635 138.773 108.906 1.00 66.76 ?  111 LYS A N     1 
ATOM   917   C  CA    . LYS A 1 111 ? 105.585 138.010 108.093 1.00 65.22 ?  111 LYS A CA    1 
ATOM   918   C  C     . LYS A 1 111 ? 104.894 137.008 107.169 1.00 67.30 ?  111 LYS A C     1 
ATOM   919   O  O     . LYS A 1 111 ? 105.416 135.920 106.920 1.00 68.62 ?  111 LYS A O     1 
ATOM   920   C  CB    . LYS A 1 111 ? 106.616 137.289 108.968 1.00 66.02 ?  111 LYS A CB    1 
ATOM   921   C  CG    . LYS A 1 111 ? 107.214 138.143 110.075 1.00 66.12 ?  111 LYS A CG    1 
ATOM   922   C  CD    . LYS A 1 111 ? 107.930 139.359 109.510 1.00 67.95 ?  111 LYS A CD    1 
ATOM   923   C  CE    . LYS A 1 111 ? 109.147 138.957 108.693 1.00 68.19 ?  111 LYS A CE    1 
ATOM   924   N  NZ    . LYS A 1 111 ? 109.892 140.145 108.186 1.00 65.71 1  111 LYS A NZ    1 
ATOM   925   N  N     . LYS A 1 112 ? 103.719 137.359 106.647 1.00 65.38 ?  112 LYS A N     1 
ATOM   926   C  CA    . LYS A 1 112 ? 103.017 136.502 105.704 1.00 66.35 ?  112 LYS A CA    1 
ATOM   927   C  C     . LYS A 1 112 ? 102.792 137.155 104.349 1.00 66.89 ?  112 LYS A C     1 
ATOM   928   O  O     . LYS A 1 112 ? 102.411 136.461 103.401 1.00 68.20 ?  112 LYS A O     1 
ATOM   929   C  CB    . LYS A 1 112 ? 101.662 136.062 106.276 1.00 67.22 ?  112 LYS A CB    1 
ATOM   930   C  CG    . LYS A 1 112 ? 100.568 137.106 106.143 1.00 67.45 ?  112 LYS A CG    1 
ATOM   931   C  CD    . LYS A 1 112 ? 99.192  136.503 106.371 1.00 67.24 ?  112 LYS A CD    1 
ATOM   932   C  CE    . LYS A 1 112 ? 99.143  135.716 107.671 1.00 69.30 ?  112 LYS A CE    1 
ATOM   933   N  NZ    . LYS A 1 112 ? 99.590  136.534 108.833 1.00 66.57 1  112 LYS A NZ    1 
ATOM   934   N  N     . LYS A 1 113 ? 103.012 138.462 104.233 1.00 59.81 ?  113 LYS A N     1 
ATOM   935   C  CA    . LYS A 1 113 ? 102.804 139.183 102.989 1.00 58.38 ?  113 LYS A CA    1 
ATOM   936   C  C     . LYS A 1 113 ? 104.068 139.946 102.628 1.00 59.83 ?  113 LYS A C     1 
ATOM   937   O  O     . LYS A 1 113 ? 104.875 140.290 103.496 1.00 60.10 ?  113 LYS A O     1 
ATOM   938   C  CB    . LYS A 1 113 ? 101.620 140.150 103.094 1.00 58.07 ?  113 LYS A CB    1 
ATOM   939   C  CG    . LYS A 1 113 ? 100.265 139.504 102.857 1.00 58.53 ?  113 LYS A CG    1 
ATOM   940   C  CD    . LYS A 1 113 ? 100.057 139.177 101.388 1.00 59.74 ?  113 LYS A CD    1 
ATOM   941   C  CE    . LYS A 1 113 ? 98.658  138.642 101.136 1.00 58.90 ?  113 LYS A CE    1 
ATOM   942   N  NZ    . LYS A 1 113 ? 98.454  138.267 99.709  1.00 60.00 1  113 LYS A NZ    1 
ATOM   943   N  N     . ILE A 1 114 ? 104.235 140.204 101.334 1.00 53.46 ?  114 ILE A N     1 
ATOM   944   C  CA    . ILE A 1 114 ? 105.412 140.879 100.803 1.00 51.44 ?  114 ILE A CA    1 
ATOM   945   C  C     . ILE A 1 114 ? 105.017 142.304 100.446 1.00 49.75 ?  114 ILE A C     1 
ATOM   946   O  O     . ILE A 1 114 ? 104.151 142.521 99.590  1.00 52.17 ?  114 ILE A O     1 
ATOM   947   C  CB    . ILE A 1 114 ? 105.987 140.140 99.587  1.00 51.20 ?  114 ILE A CB    1 
ATOM   948   C  CG1   . ILE A 1 114 ? 106.721 138.876 100.034 1.00 50.03 ?  114 ILE A CG1   1 
ATOM   949   C  CG2   . ILE A 1 114 ? 106.919 141.045 98.800  1.00 48.71 ?  114 ILE A CG2   1 
ATOM   950   C  CD1   . ILE A 1 114 ? 106.844 137.832 98.953  1.00 50.18 ?  114 ILE A CD1   1 
ATOM   951   N  N     . LEU A 1 115 ? 105.648 143.274 101.105 1.00 46.17 ?  115 LEU A N     1 
ATOM   952   C  CA    . LEU A 1 115 ? 105.376 144.679 100.838 1.00 46.36 ?  115 LEU A CA    1 
ATOM   953   C  C     . LEU A 1 115 ? 106.311 145.274 99.796  1.00 47.43 ?  115 LEU A C     1 
ATOM   954   O  O     . LEU A 1 115 ? 105.921 146.212 99.091  1.00 49.19 ?  115 LEU A O     1 
ATOM   955   C  CB    . LEU A 1 115 ? 105.480 145.492 102.130 1.00 47.39 ?  115 LEU A CB    1 
ATOM   956   C  CG    . LEU A 1 115 ? 104.431 145.194 103.201 1.00 48.80 ?  115 LEU A CG    1 
ATOM   957   C  CD1   . LEU A 1 115 ? 104.941 145.609 104.568 1.00 46.26 ?  115 LEU A CD1   1 
ATOM   958   C  CD2   . LEU A 1 115 ? 103.123 145.896 102.876 1.00 45.93 ?  115 LEU A CD2   1 
ATOM   959   N  N     . GLU A 1 116 ? 107.528 144.751 99.677  1.00 45.75 ?  116 GLU A N     1 
ATOM   960   C  CA    . GLU A 1 116 ? 108.543 145.311 98.796  1.00 42.66 ?  116 GLU A CA    1 
ATOM   961   C  C     . GLU A 1 116 ? 108.936 144.296 97.735  1.00 42.32 ?  116 GLU A C     1 
ATOM   962   O  O     . GLU A 1 116 ? 109.266 143.150 98.057  1.00 46.46 ?  116 GLU A O     1 
ATOM   963   C  CB    . GLU A 1 116 ? 109.784 145.732 99.586  1.00 43.84 ?  116 GLU A CB    1 
ATOM   964   C  CG    . GLU A 1 116 ? 109.909 147.226 99.799  1.00 44.60 ?  116 GLU A CG    1 
ATOM   965   C  CD    . GLU A 1 116 ? 111.149 147.596 100.584 1.00 43.95 ?  116 GLU A CD    1 
ATOM   966   O  OE1   . GLU A 1 116 ? 111.852 146.678 101.056 1.00 42.41 ?  116 GLU A OE1   1 
ATOM   967   O  OE2   . GLU A 1 116 ? 111.422 148.806 100.730 1.00 46.49 -1 116 GLU A OE2   1 
ATOM   968   N  N     . ARG A 1 117 ? 108.902 144.721 96.476  1.00 41.40 ?  117 ARG A N     1 
ATOM   969   C  CA    . ARG A 1 117 ? 109.525 143.969 95.401  1.00 42.35 ?  117 ARG A CA    1 
ATOM   970   C  C     . ARG A 1 117 ? 111.000 144.353 95.312  1.00 42.07 ?  117 ARG A C     1 
ATOM   971   O  O     . ARG A 1 117 ? 111.505 145.166 96.090  1.00 45.43 ?  117 ARG A O     1 
ATOM   972   C  CB    . ARG A 1 117 ? 108.801 144.226 94.082  1.00 42.96 ?  117 ARG A CB    1 
ATOM   973   C  CG    . ARG A 1 117 ? 107.330 143.842 94.091  1.00 43.74 ?  117 ARG A CG    1 
ATOM   974   C  CD    . ARG A 1 117 ? 106.837 143.515 92.693  1.00 46.22 ?  117 ARG A CD    1 
ATOM   975   N  NE    . ARG A 1 117 ? 106.939 142.093 92.393  1.00 47.84 ?  117 ARG A NE    1 
ATOM   976   C  CZ    . ARG A 1 117 ? 105.906 141.263 92.331  1.00 44.68 ?  117 ARG A CZ    1 
ATOM   977   N  NH1   . ARG A 1 117 ? 104.670 141.681 92.548  1.00 45.48 1  117 ARG A NH1   1 
ATOM   978   N  NH2   . ARG A 1 117 ? 106.119 139.983 92.042  1.00 45.28 ?  117 ARG A NH2   1 
ATOM   979   N  N     . TYR A 1 118 ? 111.710 143.756 94.353  1.00 35.82 ?  118 TYR A N     1 
ATOM   980   C  CA    . TYR A 1 118 ? 113.098 144.147 94.132  1.00 33.09 ?  118 TYR A CA    1 
ATOM   981   C  C     . TYR A 1 118 ? 113.191 145.597 93.678  1.00 35.83 ?  118 TYR A C     1 
ATOM   982   O  O     . TYR A 1 118 ? 114.041 146.357 94.159  1.00 36.46 ?  118 TYR A O     1 
ATOM   983   C  CB    . TYR A 1 118 ? 113.752 143.219 93.112  1.00 33.04 ?  118 TYR A CB    1 
ATOM   984   C  CG    . TYR A 1 118 ? 115.261 143.271 93.125  1.00 34.61 ?  118 TYR A CG    1 
ATOM   985   C  CD1   . TYR A 1 118 ? 115.965 143.205 94.318  1.00 34.13 ?  118 TYR A CD1   1 
ATOM   986   C  CD2   . TYR A 1 118 ? 115.980 143.392 91.947  1.00 32.57 ?  118 TYR A CD2   1 
ATOM   987   C  CE1   . TYR A 1 118 ? 117.342 143.252 94.336  1.00 32.21 ?  118 TYR A CE1   1 
ATOM   988   C  CE2   . TYR A 1 118 ? 117.358 143.438 91.953  1.00 28.54 ?  118 TYR A CE2   1 
ATOM   989   C  CZ    . TYR A 1 118 ? 118.034 143.368 93.151  1.00 33.42 ?  118 TYR A CZ    1 
ATOM   990   O  OH    . TYR A 1 118 ? 119.408 143.417 93.161  1.00 41.14 ?  118 TYR A OH    1 
ATOM   991   N  N     . GLU A 1 119 ? 112.309 146.002 92.762  1.00 38.05 ?  119 GLU A N     1 
ATOM   992   C  CA    . GLU A 1 119 ? 112.318 147.379 92.284  1.00 33.51 ?  119 GLU A CA    1 
ATOM   993   C  C     . GLU A 1 119 ? 111.950 148.354 93.395  1.00 34.98 ?  119 GLU A C     1 
ATOM   994   O  O     . GLU A 1 119 ? 112.518 149.446 93.476  1.00 41.26 ?  119 GLU A O     1 
ATOM   995   C  CB    . GLU A 1 119 ? 111.371 147.525 91.095  1.00 34.53 ?  119 GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 119 ? 111.830 146.798 89.841  1.00 33.42 ?  119 GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 119 ? 111.290 145.384 89.754  1.00 38.33 ?  119 GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 119 ? 111.044 144.769 90.813  1.00 40.04 ?  119 GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 119 ? 111.113 144.886 88.623  1.00 39.80 -1 119 GLU A OE2   1 
ATOM   1000  N  N     . ASP A 1 120 ? 111.009 147.977 94.264  1.00 38.34 ?  120 ASP A N     1 
ATOM   1001  C  CA    . ASP A 1 120 ? 110.631 148.853 95.370  1.00 35.32 ?  120 ASP A CA    1 
ATOM   1002  C  C     . ASP A 1 120 ? 111.793 149.057 96.334  1.00 36.45 ?  120 ASP A C     1 
ATOM   1003  O  O     . ASP A 1 120 ? 112.085 150.189 96.741  1.00 37.89 ?  120 ASP A O     1 
ATOM   1004  C  CB    . ASP A 1 120 ? 109.424 148.279 96.111  1.00 39.27 ?  120 ASP A CB    1 
ATOM   1005  C  CG    . ASP A 1 120 ? 108.251 148.021 95.196  1.00 44.42 ?  120 ASP A CG    1 
ATOM   1006  O  OD1   . ASP A 1 120 ? 107.973 148.878 94.333  1.00 42.64 ?  120 ASP A OD1   1 
ATOM   1007  O  OD2   . ASP A 1 120 ? 107.604 146.963 95.340  1.00 48.92 -1 120 ASP A OD2   1 
ATOM   1008  N  N     . ARG A 1 121 ? 112.464 147.968 96.716  1.00 35.02 ?  121 ARG A N     1 
ATOM   1009  C  CA    . ARG A 1 121 ? 113.601 148.081 97.622  1.00 32.20 ?  121 ARG A CA    1 
ATOM   1010  C  C     . ARG A 1 121 ? 114.722 148.892 96.990  1.00 33.06 ?  121 ARG A C     1 
ATOM   1011  O  O     . ARG A 1 121 ? 115.338 149.736 97.651  1.00 38.75 ?  121 ARG A O     1 
ATOM   1012  C  CB    . ARG A 1 121 ? 114.097 146.690 98.017  1.00 30.88 ?  121 ARG A CB    1 
ATOM   1013  C  CG    . ARG A 1 121 ? 115.381 146.692 98.832  1.00 30.04 ?  121 ARG A CG    1 
ATOM   1014  C  CD    . ARG A 1 121 ? 115.094 146.443 100.303 1.00 29.75 ?  121 ARG A CD    1 
ATOM   1015  N  NE    . ARG A 1 121 ? 114.364 147.546 100.916 1.00 37.01 ?  121 ARG A NE    1 
ATOM   1016  C  CZ    . ARG A 1 121 ? 114.924 148.519 101.621 1.00 36.31 ?  121 ARG A CZ    1 
ATOM   1017  N  NH1   . ARG A 1 121 ? 116.228 148.552 101.842 1.00 34.61 1  121 ARG A NH1   1 
ATOM   1018  N  NH2   . ARG A 1 121 ? 114.156 149.483 102.122 1.00 33.20 ?  121 ARG A NH2   1 
ATOM   1019  N  N     . ILE A 1 122 ? 114.995 148.656 95.705  1.00 30.77 ?  122 ILE A N     1 
ATOM   1020  C  CA    . ILE A 1 122 ? 116.050 149.397 95.023  1.00 28.80 ?  122 ILE A CA    1 
ATOM   1021  C  C     . ILE A 1 122 ? 115.706 150.880 94.951  1.00 30.77 ?  122 ILE A C     1 
ATOM   1022  O  O     . ILE A 1 122 ? 116.565 151.738 95.177  1.00 34.25 ?  122 ILE A O     1 
ATOM   1023  C  CB    . ILE A 1 122 ? 116.304 148.794 93.629  1.00 30.30 ?  122 ILE A CB    1 
ATOM   1024  C  CG1   . ILE A 1 122 ? 117.159 147.533 93.756  1.00 26.40 ?  122 ILE A CG1   1 
ATOM   1025  C  CG2   . ILE A 1 122 ? 116.970 149.808 92.708  1.00 28.94 ?  122 ILE A CG2   1 
ATOM   1026  C  CD1   . ILE A 1 122 ? 117.574 146.942 92.440  1.00 28.85 ?  122 ILE A CD1   1 
ATOM   1027  N  N     . SER A 1 123 ? 114.447 151.207 94.649  1.00 31.33 ?  123 SER A N     1 
ATOM   1028  C  CA    . SER A 1 123 ? 114.030 152.604 94.596  1.00 32.29 ?  123 SER A CA    1 
ATOM   1029  C  C     . SER A 1 123 ? 114.157 153.270 95.958  1.00 30.43 ?  123 SER A C     1 
ATOM   1030  O  O     . SER A 1 123 ? 114.597 154.420 96.056  1.00 32.18 ?  123 SER A O     1 
ATOM   1031  C  CB    . SER A 1 123 ? 112.591 152.706 94.094  1.00 28.37 ?  123 SER A CB    1 
ATOM   1032  O  OG    . SER A 1 123 ? 112.368 151.839 93.001  1.00 32.84 ?  123 SER A OG    1 
ATOM   1033  N  N     . ILE A 1 124 ? 113.768 152.566 97.022  1.00 30.02 ?  124 ILE A N     1 
ATOM   1034  C  CA    . ILE A 1 124 ? 113.866 153.140 98.360  1.00 32.25 ?  124 ILE A CA    1 
ATOM   1035  C  C     . ILE A 1 124 ? 115.322 153.380 98.735  1.00 32.94 ?  124 ILE A C     1 
ATOM   1036  O  O     . ILE A 1 124 ? 115.671 154.435 99.281  1.00 38.22 ?  124 ILE A O     1 
ATOM   1037  C  CB    . ILE A 1 124 ? 113.149 152.235 99.378  1.00 36.78 ?  124 ILE A CB    1 
ATOM   1038  C  CG1   . ILE A 1 124 ? 111.635 152.365 99.214  1.00 37.74 ?  124 ILE A CG1   1 
ATOM   1039  C  CG2   . ILE A 1 124 ? 113.567 152.579 100.798 1.00 29.38 ?  124 ILE A CG2   1 
ATOM   1040  C  CD1   . ILE A 1 124 ? 111.147 153.798 99.158  1.00 32.41 ?  124 ILE A CD1   1 
ATOM   1041  N  N     . VAL A 1 125 ? 116.198 152.416 98.438  1.00 30.55 ?  125 VAL A N     1 
ATOM   1042  C  CA    . VAL A 1 125 ? 117.614 152.582 98.754  1.00 29.88 ?  125 VAL A CA    1 
ATOM   1043  C  C     . VAL A 1 125 ? 118.211 153.726 97.941  1.00 24.99 ?  125 VAL A C     1 
ATOM   1044  O  O     . VAL A 1 125 ? 119.036 154.496 98.443  1.00 32.24 ?  125 VAL A O     1 
ATOM   1045  C  CB    . VAL A 1 125 ? 118.373 151.260 98.530  1.00 30.99 ?  125 VAL A CB    1 
ATOM   1046  C  CG1   . VAL A 1 125 ? 119.855 151.450 98.772  1.00 30.65 ?  125 VAL A CG1   1 
ATOM   1047  C  CG2   . VAL A 1 125 ? 117.839 150.186 99.455  1.00 25.85 ?  125 VAL A CG2   1 
ATOM   1048  N  N     . ALA A 1 126 ? 117.800 153.859 96.678  1.00 23.57 ?  126 ALA A N     1 
ATOM   1049  C  CA    . ALA A 1 126 ? 118.289 154.955 95.845  1.00 22.17 ?  126 ALA A CA    1 
ATOM   1050  C  C     . ALA A 1 126 ? 117.830 156.308 96.374  1.00 29.36 ?  126 ALA A C     1 
ATOM   1051  O  O     . ALA A 1 126 ? 118.611 157.267 96.406  1.00 33.76 ?  126 ALA A O     1 
ATOM   1052  C  CB    . ALA A 1 126 ? 117.821 154.762 94.405  1.00 29.36 ?  126 ALA A CB    1 
ATOM   1053  N  N     . LEU A 1 127 ? 116.563 156.407 96.782  1.00 31.34 ?  127 LEU A N     1 
ATOM   1054  C  CA    . LEU A 1 127 ? 116.057 157.658 97.337  1.00 27.26 ?  127 LEU A CA    1 
ATOM   1055  C  C     . LEU A 1 127 ? 116.768 158.006 98.636  1.00 30.16 ?  127 LEU A C     1 
ATOM   1056  O  O     . LEU A 1 127 ? 117.043 159.181 98.908  1.00 36.11 ?  127 LEU A O     1 
ATOM   1057  C  CB    . LEU A 1 127 ? 114.548 157.563 97.554  1.00 32.59 ?  127 LEU A CB    1 
ATOM   1058  C  CG    . LEU A 1 127 ? 113.686 157.506 96.293  1.00 30.20 ?  127 LEU A CG    1 
ATOM   1059  C  CD1   . LEU A 1 127 ? 112.322 156.914 96.604  1.00 35.03 ?  127 LEU A CD1   1 
ATOM   1060  C  CD2   . LEU A 1 127 ? 113.543 158.885 95.671  1.00 31.61 ?  127 LEU A CD2   1 
ATOM   1061  N  N     . PHE A 1 128 ? 117.067 156.998 99.456  1.00 29.65 ?  128 PHE A N     1 
ATOM   1062  C  CA    . PHE A 1 128 ? 117.849 157.241 100.662 1.00 27.44 ?  128 PHE A CA    1 
ATOM   1063  C  C     . PHE A 1 128 ? 119.258 157.712 100.321 1.00 27.67 ?  128 PHE A C     1 
ATOM   1064  O  O     . PHE A 1 128 ? 119.789 158.621 100.970 1.00 39.06 ?  128 PHE A O     1 
ATOM   1065  C  CB    . PHE A 1 128 ? 117.897 155.974 101.516 1.00 27.29 ?  128 PHE A CB    1 
ATOM   1066  C  CG    . PHE A 1 128 ? 118.846 156.062 102.672 1.00 32.64 ?  128 PHE A CG    1 
ATOM   1067  C  CD1   . PHE A 1 128 ? 120.086 155.451 102.615 1.00 28.84 ?  128 PHE A CD1   1 
ATOM   1068  C  CD2   . PHE A 1 128 ? 118.494 156.749 103.821 1.00 32.00 ?  128 PHE A CD2   1 
ATOM   1069  C  CE1   . PHE A 1 128 ? 120.960 155.533 103.675 1.00 31.85 ?  128 PHE A CE1   1 
ATOM   1070  C  CE2   . PHE A 1 128 ? 119.365 156.831 104.887 1.00 35.22 ?  128 PHE A CE2   1 
ATOM   1071  C  CZ    . PHE A 1 128 ? 120.599 156.222 104.815 1.00 33.47 ?  128 PHE A CZ    1 
ATOM   1072  N  N     . PHE A 1 129 ? 119.878 157.101 99.309  1.00 24.44 ?  129 PHE A N     1 
ATOM   1073  C  CA    . PHE A 1 129 ? 121.232 157.475 98.916  1.00 22.14 ?  129 PHE A CA    1 
ATOM   1074  C  C     . PHE A 1 129 ? 121.294 158.912 98.416  1.00 28.86 ?  129 PHE A C     1 
ATOM   1075  O  O     . PHE A 1 129 ? 122.203 159.666 98.780  1.00 28.00 ?  129 PHE A O     1 
ATOM   1076  C  CB    . PHE A 1 129 ? 121.741 156.530 97.828  1.00 22.02 ?  129 PHE A CB    1 
ATOM   1077  C  CG    . PHE A 1 129 ? 122.228 155.209 98.338  1.00 23.96 ?  129 PHE A CG    1 
ATOM   1078  C  CD1   . PHE A 1 129 ? 122.475 155.013 99.683  1.00 24.20 ?  129 PHE A CD1   1 
ATOM   1079  C  CD2   . PHE A 1 129 ? 122.451 154.163 97.459  1.00 22.46 ?  129 PHE A CD2   1 
ATOM   1080  C  CE1   . PHE A 1 129 ? 122.927 153.793 100.141 1.00 24.48 ?  129 PHE A CE1   1 
ATOM   1081  C  CE2   . PHE A 1 129 ? 122.906 152.945 97.914  1.00 24.48 ?  129 PHE A CE2   1 
ATOM   1082  C  CZ    . PHE A 1 129 ? 123.145 152.759 99.256  1.00 26.83 ?  129 PHE A CZ    1 
ATOM   1083  N  N     . ALA A 1 130 ? 120.336 159.307 97.574  1.00 30.83 ?  130 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 130 ? 120.432 160.595 96.896  1.00 31.96 ?  130 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 130 ? 120.225 161.765 97.848  1.00 40.33 ?  130 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 130 ? 120.732 162.863 97.590  1.00 42.45 ?  130 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 130 ? 119.423 160.657 95.754  1.00 32.00 ?  130 ALA A CB    1 
ATOM   1088  N  N     . ASN A 1 131 ? 119.483 161.555 98.937  1.00 40.41 ?  131 ASN A N     1 
ATOM   1089  C  CA    . ASN A 1 131 ? 119.274 162.577 99.965  1.00 38.34 ?  131 ASN A CA    1 
ATOM   1090  C  C     . ASN A 1 131 ? 118.627 163.837 99.389  1.00 41.21 ?  131 ASN A C     1 
ATOM   1091  O  O     . ASN A 1 131 ? 118.978 164.960 99.757  1.00 46.33 ?  131 ASN A O     1 
ATOM   1092  C  CB    . ASN A 1 131 ? 120.586 162.918 100.677 1.00 34.85 ?  131 ASN A CB    1 
ATOM   1093  C  CG    . ASN A 1 131 ? 120.374 163.369 102.107 1.00 43.68 ?  131 ASN A CG    1 
ATOM   1094  O  OD1   . ASN A 1 131 ? 119.401 162.983 102.754 1.00 43.08 ?  131 ASN A OD1   1 
ATOM   1095  N  ND2   . ASN A 1 131 ? 121.288 164.192 102.609 1.00 44.19 ?  131 ASN A ND2   1 
ATOM   1096  N  N     . GLY A 1 132 ? 117.675 163.653 98.477  1.00 39.55 ?  132 GLY A N     1 
ATOM   1097  C  CA    . GLY A 1 132 ? 116.889 164.749 97.945  1.00 39.30 ?  132 GLY A CA    1 
ATOM   1098  C  C     . GLY A 1 132 ? 117.101 165.053 96.478  1.00 43.26 ?  132 GLY A C     1 
ATOM   1099  O  O     . GLY A 1 132 ? 116.375 165.894 95.931  1.00 45.37 ?  132 GLY A O     1 
ATOM   1100  N  N     . ASP A 1 133 ? 118.061 164.408 95.819  1.00 43.29 ?  133 ASP A N     1 
ATOM   1101  C  CA    . ASP A 1 133 ? 118.350 164.656 94.409  1.00 41.14 ?  133 ASP A CA    1 
ATOM   1102  C  C     . ASP A 1 133 ? 117.655 163.591 93.569  1.00 42.99 ?  133 ASP A C     1 
ATOM   1103  O  O     . ASP A 1 133 ? 118.039 162.418 93.599  1.00 47.06 ?  133 ASP A O     1 
ATOM   1104  C  CB    . ASP A 1 133 ? 119.857 164.657 94.161  1.00 43.53 ?  133 ASP A CB    1 
ATOM   1105  C  CG    . ASP A 1 133 ? 120.237 165.360 92.873  1.00 46.21 ?  133 ASP A CG    1 
ATOM   1106  O  OD1   . ASP A 1 133 ? 119.331 165.668 92.070  1.00 48.02 ?  133 ASP A OD1   1 
ATOM   1107  O  OD2   . ASP A 1 133 ? 121.444 165.601 92.662  1.00 46.08 -1 133 ASP A OD2   1 
ATOM   1108  N  N     . THR A 1 134 ? 116.632 164.001 92.814  1.00 45.97 ?  134 THR A N     1 
ATOM   1109  C  CA    . THR A 1 134 ? 115.877 163.041 92.014  1.00 41.92 ?  134 THR A CA    1 
ATOM   1110  C  C     . THR A 1 134 ? 116.734 162.436 90.904  1.00 43.76 ?  134 THR A C     1 
ATOM   1111  O  O     . THR A 1 134 ? 116.635 161.236 90.626  1.00 44.74 ?  134 THR A O     1 
ATOM   1112  C  CB    . THR A 1 134 ? 114.625 163.704 91.435  1.00 45.87 ?  134 THR A CB    1 
ATOM   1113  O  OG1   . THR A 1 134 ? 114.004 162.821 90.492  1.00 48.16 ?  134 THR A OG1   1 
ATOM   1114  C  CG2   . THR A 1 134 ? 114.965 165.025 90.754  1.00 46.73 ?  134 THR A CG2   1 
ATOM   1115  N  N     . GLU A 1 135 ? 117.575 163.247 90.258  1.00 42.46 ?  135 GLU A N     1 
ATOM   1116  C  CA    . GLU A 1 135 ? 118.449 162.716 89.215  1.00 43.05 ?  135 GLU A CA    1 
ATOM   1117  C  C     . GLU A 1 135 ? 119.481 161.757 89.793  1.00 43.92 ?  135 GLU A C     1 
ATOM   1118  O  O     . GLU A 1 135 ? 119.761 160.707 89.204  1.00 43.52 ?  135 GLU A O     1 
ATOM   1119  C  CB    . GLU A 1 135 ? 119.134 163.862 88.470  1.00 43.57 ?  135 GLU A CB    1 
ATOM   1120  C  CG    . GLU A 1 135 ? 118.238 164.574 87.470  1.00 44.06 ?  135 GLU A CG    1 
ATOM   1121  C  CD    . GLU A 1 135 ? 117.139 163.680 86.928  1.00 47.86 ?  135 GLU A CD    1 
ATOM   1122  O  OE1   . GLU A 1 135 ? 117.417 162.891 86.001  1.00 47.89 ?  135 GLU A OE1   1 
ATOM   1123  O  OE2   . GLU A 1 135 ? 115.996 163.771 87.423  1.00 48.27 -1 135 GLU A OE2   1 
ATOM   1124  N  N     . LYS A 1 136 ? 120.053 162.098 90.949  1.00 35.81 ?  136 LYS A N     1 
ATOM   1125  C  CA    . LYS A 1 136 ? 120.977 161.186 91.614  1.00 32.22 ?  136 LYS A CA    1 
ATOM   1126  C  C     . LYS A 1 136 ? 120.269 159.905 92.036  1.00 33.99 ?  136 LYS A C     1 
ATOM   1127  O  O     . LYS A 1 136 ? 120.843 158.812 91.957  1.00 39.30 ?  136 LYS A O     1 
ATOM   1128  C  CB    . LYS A 1 136 ? 121.612 161.879 92.819  1.00 38.68 ?  136 LYS A CB    1 
ATOM   1129  C  CG    . LYS A 1 136 ? 122.761 161.119 93.451  1.00 37.05 ?  136 LYS A CG    1 
ATOM   1130  C  CD    . LYS A 1 136 ? 124.076 161.422 92.758  1.00 36.18 ?  136 LYS A CD    1 
ATOM   1131  C  CE    . LYS A 1 136 ? 125.254 160.969 93.603  1.00 38.80 ?  136 LYS A CE    1 
ATOM   1132  N  NZ    . LYS A 1 136 ? 126.551 161.443 93.049  1.00 39.04 1  136 LYS A NZ    1 
ATOM   1133  N  N     . ALA A 1 137 ? 119.019 160.020 92.490  1.00 33.83 ?  137 ALA A N     1 
ATOM   1134  C  CA    . ALA A 1 137 ? 118.247 158.833 92.846  1.00 30.50 ?  137 ALA A CA    1 
ATOM   1135  C  C     . ALA A 1 137 ? 118.011 157.945 91.632  1.00 31.42 ?  137 ALA A C     1 
ATOM   1136  O  O     . ALA A 1 137 ? 118.095 156.717 91.728  1.00 33.06 ?  137 ALA A O     1 
ATOM   1137  C  CB    . ALA A 1 137 ? 116.917 159.240 93.480  1.00 29.01 ?  137 ALA A CB    1 
ATOM   1138  N  N     . LYS A 1 138 ? 117.711 158.548 90.479  1.00 35.80 ?  138 LYS A N     1 
ATOM   1139  C  CA    . LYS A 1 138 ? 117.533 157.761 89.264  1.00 34.99 ?  138 LYS A CA    1 
ATOM   1140  C  C     . LYS A 1 138 ? 118.841 157.113 88.828  1.00 31.55 ?  138 LYS A C     1 
ATOM   1141  O  O     . LYS A 1 138 ? 118.844 155.984 88.324  1.00 33.93 ?  138 LYS A O     1 
ATOM   1142  C  CB    . LYS A 1 138 ? 116.964 158.636 88.147  1.00 39.13 ?  138 LYS A CB    1 
ATOM   1143  C  CG    . LYS A 1 138 ? 115.502 159.001 88.335  1.00 39.27 ?  138 LYS A CG    1 
ATOM   1144  C  CD    . LYS A 1 138 ? 115.177 160.332 87.682  1.00 37.78 ?  138 LYS A CD    1 
ATOM   1145  C  CE    . LYS A 1 138 ? 114.804 160.151 86.221  1.00 37.18 ?  138 LYS A CE    1 
ATOM   1146  N  NZ    . LYS A 1 138 ? 114.781 161.448 85.491  1.00 39.98 1  138 LYS A NZ    1 
ATOM   1147  N  N     . GLU A 1 139 ? 119.964 157.813 89.011  1.00 36.22 ?  139 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 139 ? 121.262 157.210 88.718  1.00 32.63 ?  139 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 139 ? 121.524 156.007 89.614  1.00 32.19 ?  139 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 139 ? 122.006 154.969 89.148  1.00 40.53 ?  139 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 139 ? 122.375 158.245 88.878  1.00 33.71 ?  139 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 139 ? 122.332 159.373 87.866  1.00 36.98 ?  139 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 139 ? 123.458 160.368 88.061  1.00 45.18 ?  139 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 139 ? 124.595 159.932 88.336  1.00 43.35 ?  139 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 139 ? 123.206 161.585 87.938  1.00 41.43 -1 139 GLU A OE2   1 
ATOM   1156  N  N     . TYR A 1 140 ? 121.209 156.126 90.906  1.00 23.52 ?  140 TYR A N     1 
ATOM   1157  C  CA    . TYR A 1 140 ? 121.368 154.996 91.816  1.00 27.69 ?  140 TYR A CA    1 
ATOM   1158  C  C     . TYR A 1 140 ? 120.446 153.845 91.435  1.00 28.10 ?  140 TYR A C     1 
ATOM   1159  O  O     . TYR A 1 140 ? 120.829 152.672 91.530  1.00 33.30 ?  140 TYR A O     1 
ATOM   1160  C  CB    . TYR A 1 140 ? 121.099 155.433 93.254  1.00 28.73 ?  140 TYR A CB    1 
ATOM   1161  C  CG    . TYR A 1 140 ? 122.237 156.175 93.908  1.00 30.16 ?  140 TYR A CG    1 
ATOM   1162  C  CD1   . TYR A 1 140 ? 123.499 155.608 94.002  1.00 28.80 ?  140 TYR A CD1   1 
ATOM   1163  C  CD2   . TYR A 1 140 ? 122.045 157.438 94.445  1.00 30.41 ?  140 TYR A CD2   1 
ATOM   1164  C  CE1   . TYR A 1 140 ? 124.538 156.282 94.603  1.00 29.52 ?  140 TYR A CE1   1 
ATOM   1165  C  CE2   . TYR A 1 140 ? 123.077 158.119 95.049  1.00 30.02 ?  140 TYR A CE2   1 
ATOM   1166  C  CZ    . TYR A 1 140 ? 124.320 157.539 95.126  1.00 25.73 ?  140 TYR A CZ    1 
ATOM   1167  O  OH    . TYR A 1 140 ? 125.346 158.222 95.730  1.00 31.30 ?  140 TYR A OH    1 
ATOM   1168  N  N     . VAL A 1 141 ? 119.217 154.162 91.024  1.00 32.97 ?  141 VAL A N     1 
ATOM   1169  C  CA    . VAL A 1 141 ? 118.275 153.128 90.607  1.00 30.44 ?  141 VAL A CA    1 
ATOM   1170  C  C     . VAL A 1 141 ? 118.797 152.397 89.378  1.00 29.32 ?  141 VAL A C     1 
ATOM   1171  O  O     . VAL A 1 141 ? 118.711 151.168 89.290  1.00 34.54 ?  141 VAL A O     1 
ATOM   1172  C  CB    . VAL A 1 141 ? 116.882 153.740 90.368  1.00 32.31 ?  141 VAL A CB    1 
ATOM   1173  C  CG1   . VAL A 1 141 ? 116.241 153.168 89.118  1.00 28.92 ?  141 VAL A CG1   1 
ATOM   1174  C  CG2   . VAL A 1 141 ? 115.991 153.487 91.565  1.00 32.26 ?  141 VAL A CG2   1 
ATOM   1175  N  N     . ASN A 1 142 ? 119.345 153.137 88.412  1.00 27.50 ?  142 ASN A N     1 
ATOM   1176  C  CA    . ASN A 1 142 ? 119.919 152.493 87.236  1.00 29.40 ?  142 ASN A CA    1 
ATOM   1177  C  C     . ASN A 1 142 ? 121.156 151.681 87.595  1.00 29.06 ?  142 ASN A C     1 
ATOM   1178  O  O     . ASN A 1 142 ? 121.425 150.652 86.966  1.00 36.97 ?  142 ASN A O     1 
ATOM   1179  C  CB    . ASN A 1 142 ? 120.257 153.538 86.176  1.00 29.77 ?  142 ASN A CB    1 
ATOM   1180  C  CG    . ASN A 1 142 ? 119.031 154.050 85.454  1.00 32.97 ?  142 ASN A CG    1 
ATOM   1181  O  OD1   . ASN A 1 142 ? 118.113 153.288 85.149  1.00 32.44 ?  142 ASN A OD1   1 
ATOM   1182  N  ND2   . ASN A 1 142 ? 119.006 155.348 85.176  1.00 33.88 ?  142 ASN A ND2   1 
ATOM   1183  N  N     . LEU A 1 143 ? 121.917 152.129 88.594  1.00 28.20 ?  143 LEU A N     1 
ATOM   1184  C  CA    . LEU A 1 143 ? 123.089 151.382 89.034  1.00 25.80 ?  143 LEU A CA    1 
ATOM   1185  C  C     . LEU A 1 143 ? 122.699 150.054 89.670  1.00 25.05 ?  143 LEU A C     1 
ATOM   1186  O  O     . LEU A 1 143 ? 123.317 149.020 89.392  1.00 28.27 ?  143 LEU A O     1 
ATOM   1187  C  CB    . LEU A 1 143 ? 123.896 152.227 90.016  1.00 23.48 ?  143 LEU A CB    1 
ATOM   1188  C  CG    . LEU A 1 143 ? 125.363 151.856 90.214  1.00 28.00 ?  143 LEU A CG    1 
ATOM   1189  C  CD1   . LEU A 1 143 ? 126.155 152.199 88.971  1.00 28.70 ?  143 LEU A CD1   1 
ATOM   1190  C  CD2   . LEU A 1 143 ? 125.920 152.576 91.426  1.00 29.39 ?  143 LEU A CD2   1 
ATOM   1191  N  N     . MET A 1 144 ? 121.682 150.064 90.530  1.00 28.78 ?  144 MET A N     1 
ATOM   1192  C  CA    . MET A 1 144 ? 121.295 148.864 91.265  1.00 23.13 ?  144 MET A CA    1 
ATOM   1193  C  C     . MET A 1 144 ? 120.383 147.935 90.477  1.00 25.40 ?  144 MET A C     1 
ATOM   1194  O  O     . MET A 1 144 ? 120.394 146.723 90.722  1.00 29.77 ?  144 MET A O     1 
ATOM   1195  C  CB    . MET A 1 144 ? 120.616 149.251 92.579  1.00 23.68 ?  144 MET A CB    1 
ATOM   1196  C  CG    . MET A 1 144 ? 121.420 150.222 93.418  1.00 26.24 ?  144 MET A CG    1 
ATOM   1197  S  SD    . MET A 1 144 ? 120.923 150.219 95.145  1.00 33.43 ?  144 MET A SD    1 
ATOM   1198  C  CE    . MET A 1 144 ? 120.169 151.837 95.247  1.00 28.66 ?  144 MET A CE    1 
ATOM   1199  N  N     . ILE A 1 145 ? 119.591 148.460 89.545  1.00 29.37 ?  145 ILE A N     1 
ATOM   1200  C  CA    . ILE A 1 145 ? 118.737 147.609 88.728  1.00 28.87 ?  145 ILE A CA    1 
ATOM   1201  C  C     . ILE A 1 145 ? 119.519 146.981 87.577  1.00 31.49 ?  145 ILE A C     1 
ATOM   1202  O  O     . ILE A 1 145 ? 119.158 145.900 87.103  1.00 35.53 ?  145 ILE A O     1 
ATOM   1203  C  CB    . ILE A 1 145 ? 117.511 148.392 88.221  1.00 27.96 ?  145 ILE A CB    1 
ATOM   1204  C  CG1   . ILE A 1 145 ? 116.327 147.449 88.002  1.00 30.70 ?  145 ILE A CG1   1 
ATOM   1205  C  CG2   . ILE A 1 145 ? 117.830 149.160 86.945  1.00 32.52 ?  145 ILE A CG2   1 
ATOM   1206  C  CD1   . ILE A 1 145 ? 115.845 146.764 89.258  1.00 28.51 ?  145 ILE A CD1   1 
ATOM   1207  N  N     . ASN A 1 146 ? 120.588 147.636 87.119  1.00 23.60 ?  146 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 146 ? 121.572 146.967 86.280  1.00 26.02 ?  146 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 146 ? 122.441 146.016 87.085  1.00 25.75 ?  146 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 146 ? 123.220 145.261 86.493  1.00 30.46 ?  146 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 146 ? 122.453 147.993 85.567  1.00 25.53 ?  146 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 146 ? 121.697 148.786 84.522  1.00 30.32 ?  146 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 146 ? 120.612 148.397 84.097  1.00 35.31 ?  146 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 146 ? 122.271 149.907 84.102  1.00 30.38 ?  146 ASN A ND2   1 
ATOM   1215  N  N     . GLN A 1 147 ? 122.325 146.050 88.413  1.00 23.38 ?  147 GLN A N     1 
ATOM   1216  C  CA    . GLN A 1 147 ? 123.078 145.181 89.315  1.00 20.38 ?  147 GLN A CA    1 
ATOM   1217  C  C     . GLN A 1 147 ? 124.580 145.372 89.140  1.00 26.35 ?  147 GLN A C     1 
ATOM   1218  O  O     . GLN A 1 147 ? 125.365 144.435 89.286  1.00 35.68 ?  147 GLN A O     1 
ATOM   1219  C  CB    . GLN A 1 147 ? 122.681 143.715 89.132  1.00 24.70 ?  147 GLN A CB    1 
ATOM   1220  C  CG    . GLN A 1 147 ? 121.300 143.388 89.673  1.00 23.57 ?  147 GLN A CG    1 
ATOM   1221  C  CD    . GLN A 1 147 ? 121.139 141.923 90.012  1.00 26.46 ?  147 GLN A CD    1 
ATOM   1222  O  OE1   . GLN A 1 147 ? 120.508 141.570 91.008  1.00 28.11 ?  147 GLN A OE1   1 
ATOM   1223  N  NE2   . GLN A 1 147 ? 121.712 141.058 89.185  1.00 35.92 ?  147 GLN A NE2   1 
ATOM   1224  N  N     . GLU A 1 148 ? 124.984 146.602 88.819  1.00 25.21 ?  148 GLU A N     1 
ATOM   1225  C  CA    . GLU A 1 148 ? 126.403 146.929 88.758  1.00 22.94 ?  148 GLU A CA    1 
ATOM   1226  C  C     . GLU A 1 148 ? 126.987 147.114 90.151  1.00 24.69 ?  148 GLU A C     1 
ATOM   1227  O  O     . GLU A 1 148 ? 128.122 146.704 90.413  1.00 29.83 ?  148 GLU A O     1 
ATOM   1228  C  CB    . GLU A 1 148 ? 126.615 148.189 87.919  1.00 20.80 ?  148 GLU A CB    1 
ATOM   1229  C  CG    . GLU A 1 148 ? 126.127 148.071 86.488  1.00 24.20 ?  148 GLU A CG    1 
ATOM   1230  C  CD    . GLU A 1 148 ? 126.007 149.416 85.802  1.00 33.09 ?  148 GLU A CD    1 
ATOM   1231  O  OE1   . GLU A 1 148 ? 124.998 150.114 86.033  1.00 36.31 ?  148 GLU A OE1   1 
ATOM   1232  O  OE2   . GLU A 1 148 ? 126.922 149.777 85.033  1.00 36.13 -1 148 GLU A OE2   1 
ATOM   1233  N  N     . TYR A 1 149 ? 126.226 147.721 91.054  1.00 18.43 ?  149 TYR A N     1 
ATOM   1234  C  CA    . TYR A 1 149 ? 126.655 147.940 92.426  1.00 20.58 ?  149 TYR A CA    1 
ATOM   1235  C  C     . TYR A 1 149 ? 125.599 147.398 93.373  1.00 22.59 ?  149 TYR A C     1 
ATOM   1236  O  O     . TYR A 1 149 ? 124.398 147.504 93.107  1.00 30.54 ?  149 TYR A O     1 
ATOM   1237  C  CB    . TYR A 1 149 ? 126.898 149.425 92.702  1.00 22.04 ?  149 TYR A CB    1 
ATOM   1238  C  CG    . TYR A 1 149 ? 127.069 149.756 94.165  1.00 21.96 ?  149 TYR A CG    1 
ATOM   1239  C  CD1   . TYR A 1 149 ? 128.159 149.284 94.883  1.00 17.07 ?  149 TYR A CD1   1 
ATOM   1240  C  CD2   . TYR A 1 149 ? 126.137 150.542 94.831  1.00 19.77 ?  149 TYR A CD2   1 
ATOM   1241  C  CE1   . TYR A 1 149 ? 128.317 149.586 96.221  1.00 22.13 ?  149 TYR A CE1   1 
ATOM   1242  C  CE2   . TYR A 1 149 ? 126.287 150.849 96.167  1.00 17.50 ?  149 TYR A CE2   1 
ATOM   1243  C  CZ    . TYR A 1 149 ? 127.378 150.368 96.857  1.00 19.19 ?  149 TYR A CZ    1 
ATOM   1244  O  OH    . TYR A 1 149 ? 127.531 150.671 98.189  1.00 20.73 ?  149 TYR A OH    1 
ATOM   1245  N  N     . GLN A 1 150 ? 126.053 146.816 94.475  1.00 19.43 ?  150 GLN A N     1 
ATOM   1246  C  CA    . GLN A 1 150 ? 125.171 146.237 95.483  1.00 14.05 ?  150 GLN A CA    1 
ATOM   1247  C  C     . GLN A 1 150 ? 125.576 146.787 96.841  1.00 17.22 ?  150 GLN A C     1 
ATOM   1248  O  O     . GLN A 1 150 ? 126.705 146.519 97.301  1.00 18.47 ?  150 GLN A O     1 
ATOM   1249  C  CB    . GLN A 1 150 ? 125.249 144.713 95.457  1.00 19.49 ?  150 GLN A CB    1 
ATOM   1250  C  CG    . GLN A 1 150 ? 124.541 144.013 96.601  1.00 20.50 ?  150 GLN A CG    1 
ATOM   1251  C  CD    . GLN A 1 150 ? 123.083 144.403 96.712  1.00 17.04 ?  150 GLN A CD    1 
ATOM   1252  O  OE1   . GLN A 1 150 ? 122.278 144.100 95.831  1.00 22.92 ?  150 GLN A OE1   1 
ATOM   1253  N  NE2   . GLN A 1 150 ? 122.733 145.074 97.800  1.00 19.47 ?  150 GLN A NE2   1 
ATOM   1254  N  N     . PRO A 1 151 ? 124.726 147.576 97.494  1.00 24.37 ?  151 PRO A N     1 
ATOM   1255  C  CA    . PRO A 1 151 ? 124.994 147.938 98.887  1.00 10.14 ?  151 PRO A CA    1 
ATOM   1256  C  C     . PRO A 1 151 ? 125.009 146.693 99.757  1.00 13.12 ?  151 PRO A C     1 
ATOM   1257  O  O     . PRO A 1 151 ? 124.353 145.694 99.460  1.00 25.36 ?  151 PRO A O     1 
ATOM   1258  C  CB    . PRO A 1 151 ? 123.828 148.866 99.249  1.00 19.55 ?  151 PRO A CB    1 
ATOM   1259  C  CG    . PRO A 1 151 ? 123.300 149.352 97.940  1.00 19.21 ?  151 PRO A CG    1 
ATOM   1260  C  CD    . PRO A 1 151 ? 123.521 148.235 96.969  1.00 19.61 ?  151 PRO A CD    1 
ATOM   1261  N  N     . SER A 1 152 ? 125.786 146.756 100.835 1.00 23.35 ?  152 SER A N     1 
ATOM   1262  C  CA    . SER A 1 152 ? 125.927 145.614 101.721 1.00 19.59 ?  152 SER A CA    1 
ATOM   1263  C  C     . SER A 1 152 ? 124.573 145.214 102.306 1.00 22.03 ?  152 SER A C     1 
ATOM   1264  O  O     . SER A 1 152 ? 123.583 145.943 102.218 1.00 27.11 ?  152 SER A O     1 
ATOM   1265  C  CB    . SER A 1 152 ? 126.911 145.930 102.843 1.00 19.84 ?  152 SER A CB    1 
ATOM   1266  O  OG    . SER A 1 152 ? 126.418 146.968 103.669 1.00 23.90 ?  152 SER A OG    1 
ATOM   1267  N  N     . THR A 1 153 ? 124.545 144.028 102.909 1.00 26.99 ?  153 THR A N     1 
ATOM   1268  C  CA    . THR A 1 153 ? 123.325 143.546 103.548 1.00 21.18 ?  153 THR A CA    1 
ATOM   1269  C  C     . THR A 1 153 ? 122.735 144.538 104.546 1.00 30.64 ?  153 THR A C     1 
ATOM   1270  O  O     . THR A 1 153 ? 121.514 144.763 104.491 1.00 32.29 ?  153 THR A O     1 
ATOM   1271  C  CB    . THR A 1 153 ? 123.593 142.188 104.218 1.00 26.27 ?  153 THR A CB    1 
ATOM   1272  O  OG1   . THR A 1 153 ? 123.766 141.182 103.212 1.00 31.38 ?  153 THR A OG1   1 
ATOM   1273  C  CG2   . THR A 1 153 ? 122.440 141.795 105.129 1.00 25.56 ?  153 THR A CG2   1 
ATOM   1274  N  N     . PRO A 1 154 ? 123.504 145.169 105.444 1.00 28.10 ?  154 PRO A N     1 
ATOM   1275  C  CA    . PRO A 1 154 ? 122.891 146.198 106.305 1.00 20.25 ?  154 PRO A CA    1 
ATOM   1276  C  C     . PRO A 1 154 ? 122.290 147.350 105.520 1.00 20.45 ?  154 PRO A C     1 
ATOM   1277  O  O     . PRO A 1 154 ? 121.128 147.713 105.746 1.00 28.25 ?  154 PRO A O     1 
ATOM   1278  C  CB    . PRO A 1 154 ? 124.062 146.657 107.184 1.00 22.33 ?  154 PRO A CB    1 
ATOM   1279  C  CG    . PRO A 1 154 ? 125.026 145.551 107.146 1.00 18.21 ?  154 PRO A CG    1 
ATOM   1280  C  CD    . PRO A 1 154 ? 124.915 144.939 105.800 1.00 19.76 ?  154 PRO A CD    1 
ATOM   1281  N  N     . THR A 1 155 ? 123.053 147.934 104.596 1.00 21.90 ?  155 THR A N     1 
ATOM   1282  C  CA    . THR A 1 155 ? 122.550 149.066 103.825 1.00 22.24 ?  155 THR A CA    1 
ATOM   1283  C  C     . THR A 1 155 ? 121.369 148.656 102.953 1.00 24.01 ?  155 THR A C     1 
ATOM   1284  O  O     . THR A 1 155 ? 120.329 149.322 102.947 1.00 25.79 ?  155 THR A O     1 
ATOM   1285  C  CB    . THR A 1 155 ? 123.669 149.656 102.967 1.00 20.44 ?  155 THR A CB    1 
ATOM   1286  O  OG1   . THR A 1 155 ? 124.826 149.886 103.780 1.00 26.23 ?  155 THR A OG1   1 
ATOM   1287  C  CG2   . THR A 1 155 ? 123.223 150.970 102.351 1.00 15.83 ?  155 THR A CG2   1 
ATOM   1288  N  N     . PHE A 1 156 ? 121.508 147.553 102.218 1.00 26.18 ?  156 PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 156 ? 120.444 147.136 101.309 1.00 22.55 ?  156 PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 156 ? 119.170 146.787 102.067 1.00 29.74 ?  156 PHE A C     1 
ATOM   1291  O  O     . PHE A 1 156 ? 118.064 147.120 101.624 1.00 25.60 ?  156 PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 156 ? 120.907 145.950 100.466 1.00 21.93 ?  156 PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 156 ? 120.053 145.696 99.260  1.00 27.63 ?  156 PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 156 ? 119.840 146.694 98.326  1.00 24.70 ?  156 PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 156 ? 119.461 144.460 99.061  1.00 23.84 ?  156 PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 156 ? 119.054 146.466 97.215  1.00 24.94 ?  156 PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 156 ? 118.676 144.226 97.952  1.00 25.17 ?  156 PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 156 ? 118.471 145.230 97.029  1.00 29.02 ?  156 PHE A CZ    1 
ATOM   1299  N  N     . LEU A 1 157 ? 119.302 146.111 103.207 1.00 29.89 ?  157 LEU A N     1 
ATOM   1300  C  CA    . LEU A 1 157 ? 118.133 145.668 103.957 1.00 24.18 ?  157 LEU A CA    1 
ATOM   1301  C  C     . LEU A 1 157 ? 117.470 146.810 104.721 1.00 27.71 ?  157 LEU A C     1 
ATOM   1302  O  O     . LEU A 1 157 ? 116.238 146.877 104.786 1.00 38.07 ?  157 LEU A O     1 
ATOM   1303  C  CB    . LEU A 1 157 ? 118.534 144.547 104.917 1.00 29.60 ?  157 LEU A CB    1 
ATOM   1304  C  CG    . LEU A 1 157 ? 117.530 144.154 106.000 1.00 30.16 ?  157 LEU A CG    1 
ATOM   1305  C  CD1   . LEU A 1 157 ? 116.510 143.177 105.451 1.00 31.34 ?  157 LEU A CD1   1 
ATOM   1306  C  CD2   . LEU A 1 157 ? 118.248 143.561 107.201 1.00 25.42 ?  157 LEU A CD2   1 
ATOM   1307  N  N     . ASN A 1 158 ? 118.259 147.720 105.292 1.00 29.43 ?  158 ASN A N     1 
ATOM   1308  C  CA    . ASN A 1 158 ? 117.741 148.661 106.274 1.00 28.29 ?  158 ASN A CA    1 
ATOM   1309  C  C     . ASN A 1 158 ? 117.565 150.080 105.750 1.00 29.21 ?  158 ASN A C     1 
ATOM   1310  O  O     . ASN A 1 158 ? 116.950 150.896 106.441 1.00 35.75 ?  158 ASN A O     1 
ATOM   1311  C  CB    . ASN A 1 158 ? 118.660 148.691 107.500 1.00 28.05 ?  158 ASN A CB    1 
ATOM   1312  C  CG    . ASN A 1 158 ? 118.682 147.373 108.242 1.00 33.65 ?  158 ASN A CG    1 
ATOM   1313  O  OD1   . ASN A 1 158 ? 117.640 146.766 108.484 1.00 37.04 ?  158 ASN A OD1   1 
ATOM   1314  N  ND2   . ASN A 1 158 ? 119.876 146.919 108.603 1.00 34.74 ?  158 ASN A ND2   1 
ATOM   1315  N  N     . ALA A 1 159 ? 118.082 150.402 104.566 1.00 27.74 ?  159 ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 159 ? 117.984 151.771 104.072 1.00 27.63 ?  159 ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 159 ? 116.527 152.161 103.872 1.00 33.43 ?  159 ALA A C     1 
ATOM   1318  O  O     . ALA A 1 159 ? 115.783 151.482 103.159 1.00 39.61 ?  159 ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 159 ? 118.757 151.927 102.764 1.00 29.21 ?  159 ALA A CB    1 
ATOM   1320  N  N     . GLY A 1 160 ? 116.123 153.258 104.508 1.00 36.32 ?  160 GLY A N     1 
ATOM   1321  C  CA    . GLY A 1 160 ? 114.773 153.756 104.388 1.00 36.92 ?  160 GLY A CA    1 
ATOM   1322  C  C     . GLY A 1 160 ? 113.749 153.091 105.280 1.00 39.04 ?  160 GLY A C     1 
ATOM   1323  O  O     . GLY A 1 160 ? 112.558 153.396 105.153 1.00 44.26 ?  160 GLY A O     1 
ATOM   1324  N  N     . ARG A 1 161 ? 114.163 152.197 106.173 1.00 41.42 ?  161 ARG A N     1 
ATOM   1325  C  CA    . ARG A 1 161 ? 113.245 151.475 107.046 1.00 41.58 ?  161 ARG A CA    1 
ATOM   1326  C  C     . ARG A 1 161 ? 113.335 152.025 108.462 1.00 43.09 ?  161 ARG A C     1 
ATOM   1327  O  O     . ARG A 1 161 ? 114.436 152.226 108.984 1.00 45.61 ?  161 ARG A O     1 
ATOM   1328  C  CB    . ARG A 1 161 ? 113.556 149.978 107.042 1.00 37.99 ?  161 ARG A CB    1 
ATOM   1329  C  CG    . ARG A 1 161 ? 113.264 149.286 105.724 1.00 40.07 ?  161 ARG A CG    1 
ATOM   1330  C  CD    . ARG A 1 161 ? 113.186 147.781 105.903 1.00 39.67 ?  161 ARG A CD    1 
ATOM   1331  N  NE    . ARG A 1 161 ? 113.196 147.079 104.626 1.00 42.62 ?  161 ARG A NE    1 
ATOM   1332  C  CZ    . ARG A 1 161 ? 113.363 145.771 104.492 1.00 43.82 ?  161 ARG A CZ    1 
ATOM   1333  N  NH1   . ARG A 1 161 ? 113.526 144.983 105.543 1.00 39.86 1  161 ARG A NH1   1 
ATOM   1334  N  NH2   . ARG A 1 161 ? 113.369 145.239 103.274 1.00 43.40 ?  161 ARG A NH2   1 
ATOM   1335  N  N     . LYS A 1 162 ? 112.176 152.269 109.080 1.00 48.38 ?  162 LYS A N     1 
ATOM   1336  C  CA    . LYS A 1 162 ? 112.162 152.780 110.447 1.00 50.04 ?  162 LYS A CA    1 
ATOM   1337  C  C     . LYS A 1 162 ? 112.576 151.703 111.444 1.00 49.96 ?  162 LYS A C     1 
ATOM   1338  O  O     . LYS A 1 162 ? 113.381 151.955 112.347 1.00 51.28 ?  162 LYS A O     1 
ATOM   1339  C  CB    . LYS A 1 162 ? 110.777 153.330 110.790 1.00 49.53 ?  162 LYS A CB    1 
ATOM   1340  C  CG    . LYS A 1 162 ? 110.734 154.124 112.086 1.00 48.91 ?  162 LYS A CG    1 
ATOM   1341  C  CD    . LYS A 1 162 ? 110.039 155.464 111.903 1.00 49.75 ?  162 LYS A CD    1 
ATOM   1342  C  CE    . LYS A 1 162 ? 108.639 155.291 111.341 1.00 52.02 ?  162 LYS A CE    1 
ATOM   1343  N  NZ    . LYS A 1 162 ? 108.248 156.427 110.461 1.00 52.03 1  162 LYS A NZ    1 
ATOM   1344  N  N     . ARG A 1 163 ? 112.034 150.497 111.295 1.00 49.65 ?  163 ARG A N     1 
ATOM   1345  C  CA    . ARG A 1 163 ? 112.402 149.366 112.147 1.00 51.16 ?  163 ARG A CA    1 
ATOM   1346  C  C     . ARG A 1 163 ? 113.638 148.722 111.536 1.00 52.31 ?  163 ARG A C     1 
ATOM   1347  O  O     . ARG A 1 163 ? 113.551 147.828 110.693 1.00 53.52 ?  163 ARG A O     1 
ATOM   1348  C  CB    . ARG A 1 163 ? 111.245 148.380 112.266 1.00 53.63 ?  163 ARG A CB    1 
ATOM   1349  C  CG    . ARG A 1 163 ? 111.114 147.715 113.631 1.00 52.96 ?  163 ARG A CG    1 
ATOM   1350  C  CD    . ARG A 1 163 ? 112.251 146.745 113.911 1.00 52.96 ?  163 ARG A CD    1 
ATOM   1351  N  NE    . ARG A 1 163 ? 112.524 145.871 112.776 1.00 53.32 ?  163 ARG A NE    1 
ATOM   1352  C  CZ    . ARG A 1 163 ? 113.715 145.357 112.497 1.00 53.85 ?  163 ARG A CZ    1 
ATOM   1353  N  NH1   . ARG A 1 163 ? 114.771 145.614 113.250 1.00 53.22 1  163 ARG A NH1   1 
ATOM   1354  N  NH2   . ARG A 1 163 ? 113.847 144.569 111.434 1.00 52.27 ?  163 ARG A NH2   1 
ATOM   1355  N  N     . ARG A 1 164 ? 114.810 149.184 111.965 1.00 50.24 ?  164 ARG A N     1 
ATOM   1356  C  CA    . ARG A 1 164 ? 116.054 148.792 111.325 1.00 50.56 ?  164 ARG A CA    1 
ATOM   1357  C  C     . ARG A 1 164 ? 117.197 148.861 112.324 1.00 49.30 ?  164 ARG A C     1 
ATOM   1358  O  O     . ARG A 1 164 ? 117.115 149.534 113.354 1.00 50.46 ?  164 ARG A O     1 
ATOM   1359  C  CB    . ARG A 1 164 ? 116.367 149.689 110.124 1.00 46.90 ?  164 ARG A CB    1 
ATOM   1360  C  CG    . ARG A 1 164 ? 116.930 151.048 110.519 1.00 43.57 ?  164 ARG A CG    1 
ATOM   1361  C  CD    . ARG A 1 164 ? 117.634 151.721 109.355 1.00 46.79 ?  164 ARG A CD    1 
ATOM   1362  N  NE    . ARG A 1 164 ? 118.074 153.074 109.675 1.00 46.54 ?  164 ARG A NE    1 
ATOM   1363  C  CZ    . ARG A 1 164 ? 119.137 153.364 110.412 1.00 49.60 ?  164 ARG A CZ    1 
ATOM   1364  N  NH1   . ARG A 1 164 ? 119.896 152.416 110.935 1.00 48.82 1  164 ARG A NH1   1 
ATOM   1365  N  NH2   . ARG A 1 164 ? 119.447 154.639 110.630 1.00 47.91 ?  164 ARG A NH2   1 
ATOM   1366  N  N     . GLY A 1 165 ? 118.271 148.142 112.001 1.00 43.35 ?  165 GLY A N     1 
ATOM   1367  C  CA    . GLY A 1 165 ? 119.542 148.313 112.667 1.00 42.46 ?  165 GLY A CA    1 
ATOM   1368  C  C     . GLY A 1 165 ? 120.388 149.357 111.965 1.00 45.44 ?  165 GLY A C     1 
ATOM   1369  O  O     . GLY A 1 165 ? 119.944 150.054 111.051 1.00 46.28 ?  165 GLY A O     1 
ATOM   1370  N  N     . GLU A 1 166 ? 121.638 149.461 112.403 1.00 39.87 ?  166 GLU A N     1 
ATOM   1371  C  CA    . GLU A 1 166 ? 122.547 150.397 111.765 1.00 37.89 ?  166 GLU A CA    1 
ATOM   1372  C  C     . GLU A 1 166 ? 122.960 149.886 110.386 1.00 38.58 ?  166 GLU A C     1 
ATOM   1373  O  O     . GLU A 1 166 ? 122.962 148.683 110.111 1.00 36.64 ?  166 GLU A O     1 
ATOM   1374  C  CB    . GLU A 1 166 ? 123.782 150.631 112.635 1.00 35.65 ?  166 GLU A CB    1 
ATOM   1375  C  CG    . GLU A 1 166 ? 123.763 151.945 113.408 1.00 38.87 ?  166 GLU A CG    1 
ATOM   1376  C  CD    . GLU A 1 166 ? 123.671 153.171 112.510 1.00 45.97 ?  166 GLU A CD    1 
ATOM   1377  O  OE1   . GLU A 1 166 ? 124.021 153.076 111.314 1.00 48.15 ?  166 GLU A OE1   1 
ATOM   1378  O  OE2   . GLU A 1 166 ? 123.246 154.236 113.005 1.00 43.24 -1 166 GLU A OE2   1 
ATOM   1379  N  N     . LEU A 1 167 ? 123.313 150.828 109.512 1.00 30.76 ?  167 LEU A N     1 
ATOM   1380  C  CA    . LEU A 1 167 ? 123.751 150.489 108.166 1.00 25.60 ?  167 LEU A CA    1 
ATOM   1381  C  C     . LEU A 1 167 ? 125.187 149.991 108.121 1.00 28.67 ?  167 LEU A C     1 
ATOM   1382  O  O     . LEU A 1 167 ? 125.625 149.503 107.074 1.00 30.69 ?  167 LEU A O     1 
ATOM   1383  C  CB    . LEU A 1 167 ? 123.599 151.699 107.244 1.00 26.21 ?  167 LEU A CB    1 
ATOM   1384  C  CG    . LEU A 1 167 ? 122.176 152.202 107.014 1.00 25.34 ?  167 LEU A CG    1 
ATOM   1385  C  CD1   . LEU A 1 167 ? 122.148 153.163 105.851 1.00 27.51 ?  167 LEU A CD1   1 
ATOM   1386  C  CD2   . LEU A 1 167 ? 121.234 151.044 106.766 1.00 27.01 ?  167 LEU A CD2   1 
ATOM   1387  N  N     . VAL A 1 168 ? 125.923 150.107 109.220 1.00 29.92 ?  168 VAL A N     1 
ATOM   1388  C  CA    . VAL A 1 168 ? 127.278 149.582 109.335 1.00 20.10 ?  168 VAL A CA    1 
ATOM   1389  C  C     . VAL A 1 168 ? 127.228 148.349 110.220 1.00 25.75 ?  168 VAL A C     1 
ATOM   1390  O  O     . VAL A 1 168 ? 126.582 148.361 111.276 1.00 33.49 ?  168 VAL A O     1 
ATOM   1391  C  CB    . VAL A 1 168 ? 128.237 150.638 109.912 1.00 24.69 ?  168 VAL A CB    1 
ATOM   1392  C  CG1   . VAL A 1 168 ? 129.654 150.093 109.970 1.00 29.31 ?  168 VAL A CG1   1 
ATOM   1393  C  CG2   . VAL A 1 168 ? 128.184 151.913 109.087 1.00 27.55 ?  168 VAL A CG2   1 
ATOM   1394  N  N     . SER A 1 169 ? 127.890 147.276 109.789 1.00 26.07 ?  169 SER A N     1 
ATOM   1395  C  CA    . SER A 1 169 ? 127.944 146.053 110.574 1.00 29.38 ?  169 SER A CA    1 
ATOM   1396  C  C     . SER A 1 169 ? 129.354 145.555 110.841 1.00 32.50 ?  169 SER A C     1 
ATOM   1397  O  O     . SER A 1 169 ? 129.509 144.494 111.456 1.00 38.92 ?  169 SER A O     1 
ATOM   1398  C  CB    . SER A 1 169 ? 127.131 144.940 109.900 1.00 30.68 ?  169 SER A CB    1 
ATOM   1399  O  OG    . SER A 1 169 ? 125.746 145.121 110.135 1.00 38.06 ?  169 SER A OG    1 
ATOM   1400  N  N     . CYS A 1 170 ? 130.381 146.270 110.400 1.00 26.32 ?  170 CYS A N     1 
ATOM   1401  C  CA    . CYS A 1 170 ? 131.757 145.946 110.750 1.00 24.16 ?  170 CYS A CA    1 
ATOM   1402  C  C     . CYS A 1 170 ? 132.280 147.033 111.680 1.00 23.58 ?  170 CYS A C     1 
ATOM   1403  O  O     . CYS A 1 170 ? 132.337 148.209 111.304 1.00 26.85 ?  170 CYS A O     1 
ATOM   1404  C  CB    . CYS A 1 170 ? 132.630 145.788 109.501 1.00 30.30 ?  170 CYS A CB    1 
ATOM   1405  S  SG    . CYS A 1 170 ? 133.030 147.286 108.574 1.00 48.74 ?  170 CYS A SG    1 
ATOM   1406  N  N     . PHE A 1 171 ? 132.622 146.641 112.903 1.00 23.10 ?  171 PHE A N     1 
ATOM   1407  C  CA    . PHE A 1 171 ? 133.117 147.559 113.918 1.00 10.69 ?  171 PHE A CA    1 
ATOM   1408  C  C     . PHE A 1 171 ? 134.390 146.991 114.515 1.00 15.01 ?  171 PHE A C     1 
ATOM   1409  O  O     . PHE A 1 171 ? 134.444 145.808 114.864 1.00 22.56 ?  171 PHE A O     1 
ATOM   1410  C  CB    . PHE A 1 171 ? 132.076 147.792 115.016 1.00 15.76 ?  171 PHE A CB    1 
ATOM   1411  C  CG    . PHE A 1 171 ? 130.787 148.365 114.513 1.00 17.29 ?  171 PHE A CG    1 
ATOM   1412  C  CD1   . PHE A 1 171 ? 130.708 149.693 114.141 1.00 19.36 ?  171 PHE A CD1   1 
ATOM   1413  C  CD2   . PHE A 1 171 ? 129.654 147.576 114.414 1.00 15.63 ?  171 PHE A CD2   1 
ATOM   1414  C  CE1   . PHE A 1 171 ? 129.528 150.224 113.673 1.00 14.98 ?  171 PHE A CE1   1 
ATOM   1415  C  CE2   . PHE A 1 171 ? 128.468 148.105 113.951 1.00 16.79 ?  171 PHE A CE2   1 
ATOM   1416  C  CZ    . PHE A 1 171 ? 128.406 149.430 113.580 1.00 16.17 ?  171 PHE A CZ    1 
ATOM   1417  N  N     . LEU A 1 172 ? 135.412 147.832 114.626 1.00 14.71 ?  172 LEU A N     1 
ATOM   1418  C  CA    . LEU A 1 172 ? 136.680 147.454 115.228 1.00 9.06  ?  172 LEU A CA    1 
ATOM   1419  C  C     . LEU A 1 172 ? 136.896 148.306 116.466 1.00 13.65 ?  172 LEU A C     1 
ATOM   1420  O  O     . LEU A 1 172 ? 136.876 149.539 116.384 1.00 16.89 ?  172 LEU A O     1 
ATOM   1421  C  CB    . LEU A 1 172 ? 137.838 147.633 114.246 1.00 14.71 ?  172 LEU A CB    1 
ATOM   1422  C  CG    . LEU A 1 172 ? 137.957 146.634 113.095 1.00 6.10  ?  172 LEU A CG    1 
ATOM   1423  C  CD1   . LEU A 1 172 ? 136.984 146.976 111.980 1.00 8.62  ?  172 LEU A CD1   1 
ATOM   1424  C  CD2   . LEU A 1 172 ? 139.378 146.612 112.575 1.00 13.30 ?  172 LEU A CD2   1 
ATOM   1425  N  N     . LEU A 1 173 ? 137.101 147.656 117.605 1.00 16.08 ?  173 LEU A N     1 
ATOM   1426  C  CA    . LEU A 1 173 ? 137.276 148.341 118.875 1.00 12.47 ?  173 LEU A CA    1 
ATOM   1427  C  C     . LEU A 1 173 ? 138.681 148.115 119.407 1.00 11.97 ?  173 LEU A C     1 
ATOM   1428  O  O     . LEU A 1 173 ? 139.211 147.002 119.344 1.00 16.59 ?  173 LEU A O     1 
ATOM   1429  C  CB    . LEU A 1 173 ? 136.257 147.863 119.910 1.00 16.96 ?  173 LEU A CB    1 
ATOM   1430  C  CG    . LEU A 1 173 ? 134.779 147.875 119.527 1.00 20.16 ?  173 LEU A CG    1 
ATOM   1431  C  CD1   . LEU A 1 173 ? 133.937 147.490 120.730 1.00 19.08 ?  173 LEU A CD1   1 
ATOM   1432  C  CD2   . LEU A 1 173 ? 134.364 149.232 118.985 1.00 16.49 ?  173 LEU A CD2   1 
ATOM   1433  N  N     . GLU A 1 174 ? 139.282 149.180 119.922 1.00 25.98 ?  174 GLU A N     1 
ATOM   1434  C  CA    . GLU A 1 174 ? 140.525 149.083 120.669 1.00 23.68 ?  174 GLU A CA    1 
ATOM   1435  C  C     . GLU A 1 174 ? 140.214 149.034 122.157 1.00 20.40 ?  174 GLU A C     1 
ATOM   1436  O  O     . GLU A 1 174 ? 139.455 149.861 122.670 1.00 29.43 ?  174 GLU A O     1 
ATOM   1437  C  CB    . GLU A 1 174 ? 141.436 150.272 120.361 1.00 26.29 ?  174 GLU A CB    1 
ATOM   1438  C  CG    . GLU A 1 174 ? 141.916 150.336 118.924 1.00 22.14 ?  174 GLU A CG    1 
ATOM   1439  C  CD    . GLU A 1 174 ? 143.322 149.803 118.759 1.00 25.00 ?  174 GLU A CD    1 
ATOM   1440  O  OE1   . GLU A 1 174 ? 143.967 149.496 119.783 1.00 28.05 ?  174 GLU A OE1   1 
ATOM   1441  O  OE2   . GLU A 1 174 ? 143.786 149.691 117.606 1.00 28.48 -1 174 GLU A OE2   1 
ATOM   1442  N  N     . VAL A 1 175 ? 140.798 148.061 122.846 1.00 19.84 ?  175 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 175 ? 140.585 147.870 124.276 1.00 20.81 ?  175 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 175 ? 141.876 148.225 124.997 1.00 18.94 ?  175 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 175 ? 142.921 147.607 124.757 1.00 26.83 ?  175 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 175 ? 140.147 146.434 124.600 1.00 22.21 ?  175 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 175 ? 139.633 146.345 126.027 1.00 14.41 ?  175 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 175 ? 139.089 145.967 123.613 1.00 19.87 ?  175 VAL A CG2   1 
ATOM   1449  N  N     . ASN A 1 176 ? 141.806 149.218 125.878 1.00 18.41 ?  176 ASN A N     1 
ATOM   1450  C  CA    . ASN A 1 176 ? 142.960 149.604 126.668 1.00 20.00 ?  176 ASN A CA    1 
ATOM   1451  C  C     . ASN A 1 176 ? 143.086 148.708 127.896 1.00 23.60 ?  176 ASN A C     1 
ATOM   1452  O  O     . ASN A 1 176 ? 142.130 148.060 128.329 1.00 24.22 ?  176 ASN A O     1 
ATOM   1453  C  CB    . ASN A 1 176 ? 142.859 151.071 127.084 1.00 18.83 ?  176 ASN A CB    1 
ATOM   1454  C  CG    . ASN A 1 176 ? 144.203 151.764 127.102 1.00 21.31 ?  176 ASN A CG    1 
ATOM   1455  O  OD1   . ASN A 1 176 ? 145.241 151.127 127.279 1.00 27.96 ?  176 ASN A OD1   1 
ATOM   1456  N  ND2   . ASN A 1 176 ? 144.192 153.078 126.915 1.00 20.44 ?  176 ASN A ND2   1 
ATOM   1457  N  N     . ASP A 1 177 ? 144.292 148.684 128.465 1.00 23.65 ?  177 ASP A N     1 
ATOM   1458  C  CA    . ASP A 1 177 ? 144.625 147.765 129.553 1.00 20.06 ?  177 ASP A CA    1 
ATOM   1459  C  C     . ASP A 1 177 ? 144.138 148.345 130.879 1.00 24.85 ?  177 ASP A C     1 
ATOM   1460  O  O     . ASP A 1 177 ? 144.905 148.860 131.696 1.00 35.39 ?  177 ASP A O     1 
ATOM   1461  C  CB    . ASP A 1 177 ? 146.123 147.494 129.576 1.00 19.80 ?  177 ASP A CB    1 
ATOM   1462  C  CG    . ASP A 1 177 ? 146.496 146.381 130.527 1.00 25.30 ?  177 ASP A CG    1 
ATOM   1463  O  OD1   . ASP A 1 177 ? 145.767 145.369 130.578 1.00 28.44 ?  177 ASP A OD1   1 
ATOM   1464  O  OD2   . ASP A 1 177 ? 147.523 146.518 131.223 1.00 31.09 -1 177 ASP A OD2   1 
ATOM   1465  N  N     . SER A 1 178 ? 142.828 148.251 131.092 1.00 20.57 ?  178 SER A N     1 
ATOM   1466  C  CA    . SER A 1 178 ? 142.227 148.678 132.347 1.00 17.37 ?  178 SER A CA    1 
ATOM   1467  C  C     . SER A 1 178 ? 140.874 148.002 132.494 1.00 17.74 ?  178 SER A C     1 
ATOM   1468  O  O     . SER A 1 178 ? 140.266 147.568 131.513 1.00 27.43 ?  178 SER A O     1 
ATOM   1469  C  CB    . SER A 1 178 ? 142.082 150.202 132.416 1.00 16.60 ?  178 SER A CB    1 
ATOM   1470  O  OG    . SER A 1 178 ? 140.820 150.618 131.932 1.00 20.62 ?  178 SER A OG    1 
ATOM   1471  N  N     . LEU A 1 179 ? 140.410 147.914 133.743 1.00 22.74 ?  179 LEU A N     1 
ATOM   1472  C  CA    . LEU A 1 179 ? 139.090 147.346 133.998 1.00 19.48 ?  179 LEU A CA    1 
ATOM   1473  C  C     . LEU A 1 179 ? 137.989 148.253 133.467 1.00 18.74 ?  179 LEU A C     1 
ATOM   1474  O  O     . LEU A 1 179 ? 136.980 147.772 132.942 1.00 22.22 ?  179 LEU A O     1 
ATOM   1475  C  CB    . LEU A 1 179 ? 138.900 147.095 135.492 1.00 26.25 ?  179 LEU A CB    1 
ATOM   1476  C  CG    . LEU A 1 179 ? 137.665 146.267 135.854 1.00 18.81 ?  179 LEU A CG    1 
ATOM   1477  C  CD1   . LEU A 1 179 ? 137.885 144.804 135.511 1.00 21.68 ?  179 LEU A CD1   1 
ATOM   1478  C  CD2   . LEU A 1 179 ? 137.311 146.433 137.322 1.00 18.45 ?  179 LEU A CD2   1 
ATOM   1479  N  N     . ASN A 1 180 ? 138.163 149.571 133.602 1.00 21.73 ?  180 ASN A N     1 
ATOM   1480  C  CA    . ASN A 1 180 ? 137.200 150.508 133.035 1.00 19.79 ?  180 ASN A CA    1 
ATOM   1481  C  C     . ASN A 1 180 ? 137.114 150.352 131.523 1.00 20.72 ?  180 ASN A C     1 
ATOM   1482  O  O     . ASN A 1 180 ? 136.017 150.326 130.953 1.00 24.18 ?  180 ASN A O     1 
ATOM   1483  C  CB    . ASN A 1 180 ? 137.585 151.941 133.400 1.00 21.19 ?  180 ASN A CB    1 
ATOM   1484  C  CG    . ASN A 1 180 ? 137.169 152.318 134.804 1.00 26.79 ?  180 ASN A CG    1 
ATOM   1485  O  OD1   . ASN A 1 180 ? 136.185 151.802 135.334 1.00 33.12 ?  180 ASN A OD1   1 
ATOM   1486  N  ND2   . ASN A 1 180 ? 137.921 153.223 135.418 1.00 26.38 ?  180 ASN A ND2   1 
ATOM   1487  N  N     . ASP A 1 181 ? 138.265 150.231 130.861 1.00 21.75 ?  181 ASP A N     1 
ATOM   1488  C  CA    . ASP A 1 181 ? 138.275 150.075 129.412 1.00 12.47 ?  181 ASP A CA    1 
ATOM   1489  C  C     . ASP A 1 181 ? 137.700 148.729 128.993 1.00 18.69 ?  181 ASP A C     1 
ATOM   1490  O  O     . ASP A 1 181 ? 137.016 148.636 127.972 1.00 26.03 ?  181 ASP A O     1 
ATOM   1491  C  CB    . ASP A 1 181 ? 139.695 150.249 128.878 1.00 20.67 ?  181 ASP A CB    1 
ATOM   1492  C  CG    . ASP A 1 181 ? 140.202 151.667 129.034 1.00 28.75 ?  181 ASP A CG    1 
ATOM   1493  O  OD1   . ASP A 1 181 ? 139.635 152.573 128.393 1.00 31.69 ?  181 ASP A OD1   1 
ATOM   1494  O  OD2   . ASP A 1 181 ? 141.169 151.876 129.796 1.00 29.88 -1 181 ASP A OD2   1 
ATOM   1495  N  N     . ILE A 1 182 ? 137.956 147.676 129.769 1.00 20.59 ?  182 ILE A N     1 
ATOM   1496  C  CA    . ILE A 1 182 ? 137.396 146.367 129.448 1.00 17.82 ?  182 ILE A CA    1 
ATOM   1497  C  C     . ILE A 1 182 ? 135.877 146.382 129.586 1.00 19.62 ?  182 ILE A C     1 
ATOM   1498  O  O     . ILE A 1 182 ? 135.154 145.859 128.727 1.00 25.76 ?  182 ILE A O     1 
ATOM   1499  C  CB    . ILE A 1 182 ? 138.042 145.284 130.331 1.00 18.58 ?  182 ILE A CB    1 
ATOM   1500  C  CG1   . ILE A 1 182 ? 139.426 144.930 129.790 1.00 20.04 ?  182 ILE A CG1   1 
ATOM   1501  C  CG2   . ILE A 1 182 ? 137.162 144.044 130.407 1.00 21.02 ?  182 ILE A CG2   1 
ATOM   1502  C  CD1   . ILE A 1 182 ? 140.276 144.167 130.760 1.00 21.69 ?  182 ILE A CD1   1 
ATOM   1503  N  N     . SER A 1 183 ? 135.367 146.983 130.663 1.00 20.91 ?  183 SER A N     1 
ATOM   1504  C  CA    . SER A 1 183 ? 133.923 147.079 130.841 1.00 19.31 ?  183 SER A CA    1 
ATOM   1505  C  C     . SER A 1 183 ? 133.288 147.935 129.752 1.00 23.27 ?  183 SER A C     1 
ATOM   1506  O  O     . SER A 1 183 ? 132.212 147.603 129.241 1.00 25.87 ?  183 SER A O     1 
ATOM   1507  C  CB    . SER A 1 183 ? 133.603 147.643 132.224 1.00 19.40 ?  183 SER A CB    1 
ATOM   1508  O  OG    . SER A 1 183 ? 134.072 148.972 132.355 1.00 29.39 ?  183 SER A OG    1 
ATOM   1509  N  N     . ARG A 1 184 ? 133.943 149.038 129.380 1.00 25.20 ?  184 ARG A N     1 
ATOM   1510  C  CA    . ARG A 1 184 ? 133.428 149.868 128.298 1.00 19.46 ?  184 ARG A CA    1 
ATOM   1511  C  C     . ARG A 1 184 ? 133.444 149.119 126.972 1.00 23.51 ?  184 ARG A C     1 
ATOM   1512  O  O     . ARG A 1 184 ? 132.530 149.276 126.159 1.00 28.66 ?  184 ARG A O     1 
ATOM   1513  C  CB    . ARG A 1 184 ? 134.235 151.161 128.197 1.00 15.25 ?  184 ARG A CB    1 
ATOM   1514  C  CG    . ARG A 1 184 ? 133.735 152.113 127.127 1.00 24.35 ?  184 ARG A CG    1 
ATOM   1515  C  CD    . ARG A 1 184 ? 132.261 152.420 127.302 1.00 24.56 ?  184 ARG A CD    1 
ATOM   1516  N  NE    . ARG A 1 184 ? 132.040 153.493 128.262 1.00 32.26 ?  184 ARG A NE    1 
ATOM   1517  C  CZ    . ARG A 1 184 ? 130.948 153.620 129.003 1.00 29.75 ?  184 ARG A CZ    1 
ATOM   1518  N  NH1   . ARG A 1 184 ? 129.954 152.751 128.922 1.00 25.23 1  184 ARG A NH1   1 
ATOM   1519  N  NH2   . ARG A 1 184 ? 130.851 154.644 129.845 1.00 26.89 ?  184 ARG A NH2   1 
ATOM   1520  N  N     . ALA A 1 185 ? 134.475 148.306 126.733 1.00 24.15 ?  185 ALA A N     1 
ATOM   1521  C  CA    . ALA A 1 185 ? 134.523 147.503 125.517 1.00 16.96 ?  185 ALA A CA    1 
ATOM   1522  C  C     . ALA A 1 185 ? 133.392 146.487 125.486 1.00 20.26 ?  185 ALA A C     1 
ATOM   1523  O  O     . ALA A 1 185 ? 132.770 146.274 124.441 1.00 23.61 ?  185 ALA A O     1 
ATOM   1524  C  CB    . ALA A 1 185 ? 135.875 146.804 125.402 1.00 16.52 ?  185 ALA A CB    1 
ATOM   1525  N  N     . ILE A 1 186 ? 133.109 145.851 126.625 1.00 23.68 ?  186 ILE A N     1 
ATOM   1526  C  CA    . ILE A 1 186 ? 131.986 144.917 126.701 1.00 20.75 ?  186 ILE A CA    1 
ATOM   1527  C  C     . ILE A 1 186 ? 130.677 145.640 126.408 1.00 20.06 ?  186 ILE A C     1 
ATOM   1528  O  O     . ILE A 1 186 ? 129.830 145.155 125.644 1.00 27.89 ?  186 ILE A O     1 
ATOM   1529  C  CB    . ILE A 1 186 ? 131.953 144.228 128.078 1.00 26.09 ?  186 ILE A CB    1 
ATOM   1530  C  CG1   . ILE A 1 186 ? 133.156 143.299 128.246 1.00 24.61 ?  186 ILE A CG1   1 
ATOM   1531  C  CG2   . ILE A 1 186 ? 130.654 143.459 128.267 1.00 24.04 ?  186 ILE A CG2   1 
ATOM   1532  C  CD1   . ILE A 1 186 ? 133.518 143.036 129.689 1.00 23.67 ?  186 ILE A CD1   1 
ATOM   1533  N  N     . ASP A 1 187 ? 130.497 146.819 127.007 1.00 21.52 ?  187 ASP A N     1 
ATOM   1534  C  CA    . ASP A 1 187 ? 129.278 147.592 126.789 1.00 19.03 ?  187 ASP A CA    1 
ATOM   1535  C  C     . ASP A 1 187 ? 129.125 147.985 125.323 1.00 23.82 ?  187 ASP A C     1 
ATOM   1536  O  O     . ASP A 1 187 ? 128.043 147.850 124.743 1.00 28.16 ?  187 ASP A O     1 
ATOM   1537  C  CB    . ASP A 1 187 ? 129.283 148.834 127.679 1.00 17.96 ?  187 ASP A CB    1 
ATOM   1538  C  CG    . ASP A 1 187 ? 128.357 149.920 127.170 1.00 28.50 ?  187 ASP A CG    1 
ATOM   1539  O  OD1   . ASP A 1 187 ? 127.153 149.642 126.988 1.00 30.94 ?  187 ASP A OD1   1 
ATOM   1540  O  OD2   . ASP A 1 187 ? 128.834 151.052 126.948 1.00 34.22 -1 187 ASP A OD2   1 
ATOM   1541  N  N     . ILE A 1 188 ? 130.205 148.473 124.710 1.00 22.45 ?  188 ILE A N     1 
ATOM   1542  C  CA    . ILE A 1 188 ? 130.144 148.909 123.318 1.00 21.59 ?  188 ILE A CA    1 
ATOM   1543  C  C     . ILE A 1 188 ? 129.902 147.723 122.396 1.00 23.18 ?  188 ILE A C     1 
ATOM   1544  O  O     . ILE A 1 188 ? 129.167 147.830 121.410 1.00 27.73 ?  188 ILE A O     1 
ATOM   1545  C  CB    . ILE A 1 188 ? 131.427 149.675 122.941 1.00 22.36 ?  188 ILE A CB    1 
ATOM   1546  C  CG1   . ILE A 1 188 ? 131.541 150.966 123.750 1.00 22.66 ?  188 ILE A CG1   1 
ATOM   1547  C  CG2   . ILE A 1 188 ? 131.436 150.014 121.466 1.00 21.91 ?  188 ILE A CG2   1 
ATOM   1548  C  CD1   . ILE A 1 188 ? 132.852 151.688 123.555 1.00 22.60 ?  188 ILE A CD1   1 
ATOM   1549  N  N     . SER A 1 189 ? 130.514 146.575 122.697 1.00 18.21 ?  189 SER A N     1 
ATOM   1550  C  CA    . SER A 1 189 ? 130.258 145.374 121.913 1.00 12.23 ?  189 SER A CA    1 
ATOM   1551  C  C     . SER A 1 189 ? 128.793 144.975 121.991 1.00 19.79 ?  189 SER A C     1 
ATOM   1552  O  O     . SER A 1 189 ? 128.185 144.615 120.977 1.00 28.18 ?  189 SER A O     1 
ATOM   1553  C  CB    . SER A 1 189 ? 131.151 144.233 122.399 1.00 20.99 ?  189 SER A CB    1 
ATOM   1554  O  OG    . SER A 1 189 ? 132.513 144.615 122.403 1.00 27.35 ?  189 SER A OG    1 
ATOM   1555  N  N     . MET A 1 190 ? 128.208 145.044 123.188 1.00 25.42 ?  190 MET A N     1 
ATOM   1556  C  CA    . MET A 1 190 ? 126.790 144.734 123.337 1.00 22.32 ?  190 MET A CA    1 
ATOM   1557  C  C     . MET A 1 190 ? 125.924 145.716 122.557 1.00 18.68 ?  190 MET A C     1 
ATOM   1558  O  O     . MET A 1 190 ? 124.959 145.316 121.897 1.00 22.42 ?  190 MET A O     1 
ATOM   1559  C  CB    . MET A 1 190 ? 126.407 144.750 124.813 1.00 25.23 ?  190 MET A CB    1 
ATOM   1560  C  CG    . MET A 1 190 ? 126.735 143.474 125.552 1.00 18.79 ?  190 MET A CG    1 
ATOM   1561  S  SD    . MET A 1 190 ? 126.792 143.752 127.327 1.00 37.97 ?  190 MET A SD    1 
ATOM   1562  C  CE    . MET A 1 190 ? 125.564 142.576 127.867 1.00 27.75 ?  190 MET A CE    1 
ATOM   1563  N  N     . GLN A 1 191 ? 126.255 147.007 122.622 1.00 21.05 ?  191 GLN A N     1 
ATOM   1564  C  CA    . GLN A 1 191 ? 125.456 148.014 121.930 1.00 22.57 ?  191 GLN A CA    1 
ATOM   1565  C  C     . GLN A 1 191 ? 125.547 147.855 120.417 1.00 24.99 ?  191 GLN A C     1 
ATOM   1566  O  O     . GLN A 1 191 ? 124.555 148.051 119.706 1.00 30.62 ?  191 GLN A O     1 
ATOM   1567  C  CB    . GLN A 1 191 ? 125.894 149.419 122.344 1.00 22.31 ?  191 GLN A CB    1 
ATOM   1568  C  CG    . GLN A 1 191 ? 125.764 149.707 123.828 1.00 21.20 ?  191 GLN A CG    1 
ATOM   1569  C  CD    . GLN A 1 191 ? 124.325 149.795 124.289 1.00 27.26 ?  191 GLN A CD    1 
ATOM   1570  O  OE1   . GLN A 1 191 ? 123.416 150.021 123.491 1.00 28.28 ?  191 GLN A OE1   1 
ATOM   1571  N  NE2   . GLN A 1 191 ? 124.110 149.621 125.587 1.00 25.51 ?  191 GLN A NE2   1 
ATOM   1572  N  N     . LEU A 1 192 ? 126.730 147.512 119.905 1.00 24.46 ?  192 LEU A N     1 
ATOM   1573  C  CA    . LEU A 1 192 ? 126.895 147.359 118.465 1.00 19.42 ?  192 LEU A CA    1 
ATOM   1574  C  C     . LEU A 1 192 ? 126.306 146.051 117.957 1.00 23.47 ?  192 LEU A C     1 
ATOM   1575  O  O     . LEU A 1 192 ? 125.809 146.004 116.826 1.00 33.19 ?  192 LEU A O     1 
ATOM   1576  C  CB    . LEU A 1 192 ? 128.373 147.459 118.091 1.00 20.09 ?  192 LEU A CB    1 
ATOM   1577  C  CG    . LEU A 1 192 ? 129.051 148.800 118.377 1.00 18.88 ?  192 LEU A CG    1 
ATOM   1578  C  CD1   . LEU A 1 192 ? 130.558 148.666 118.253 1.00 18.46 ?  192 LEU A CD1   1 
ATOM   1579  C  CD2   . LEU A 1 192 ? 128.524 149.892 117.465 1.00 16.55 ?  192 LEU A CD2   1 
ATOM   1580  N  N     . SER A 1 193 ? 126.352 144.984 118.758 1.00 19.30 ?  193 SER A N     1 
ATOM   1581  C  CA    . SER A 1 193 ? 125.646 143.762 118.393 1.00 21.10 ?  193 SER A CA    1 
ATOM   1582  C  C     . SER A 1 193 ? 124.140 143.974 118.432 1.00 30.66 ?  193 SER A C     1 
ATOM   1583  O  O     . SER A 1 193 ? 123.400 143.374 117.645 1.00 35.65 ?  193 SER A O     1 
ATOM   1584  C  CB    . SER A 1 193 ? 126.057 142.620 119.320 1.00 23.76 ?  193 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 193 ? 127.461 142.599 119.501 1.00 29.24 ?  193 SER A OG    1 
ATOM   1586  N  N     . LYS A 1 194 ? 123.670 144.820 119.351 1.00 28.35 ?  194 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 194 ? 122.262 145.200 119.371 1.00 26.81 ?  194 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 194 ? 121.870 145.902 118.077 1.00 33.98 ?  194 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 194 ? 120.775 145.680 117.548 1.00 37.52 ?  194 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 194 ? 121.988 146.092 120.581 1.00 25.61 ?  194 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 194 ? 120.642 146.785 120.566 1.00 31.84 ?  194 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 194 ? 120.527 147.787 121.702 1.00 34.30 ?  194 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 194 ? 119.102 148.290 121.851 1.00 30.41 ?  194 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 194 ? 118.985 149.314 122.924 1.00 33.10 1  194 LYS A NZ    1 
ATOM   1595  N  N     . LEU A 1 195 ? 122.754 146.751 117.553 1.00 34.63 ?  195 LEU A N     1 
ATOM   1596  C  CA    . LEU A 1 195 ? 122.524 147.409 116.274 1.00 32.10 ?  195 LEU A CA    1 
ATOM   1597  C  C     . LEU A 1 195 ? 122.633 146.453 115.093 1.00 34.27 ?  195 LEU A C     1 
ATOM   1598  O  O     . LEU A 1 195 ? 122.306 146.847 113.969 1.00 37.81 ?  195 LEU A O     1 
ATOM   1599  C  CB    . LEU A 1 195 ? 123.511 148.562 116.092 1.00 32.31 ?  195 LEU A CB    1 
ATOM   1600  C  CG    . LEU A 1 195 ? 123.349 149.746 117.046 1.00 35.80 ?  195 LEU A CG    1 
ATOM   1601  C  CD1   . LEU A 1 195 ? 124.467 150.754 116.839 1.00 35.62 ?  195 LEU A CD1   1 
ATOM   1602  C  CD2   . LEU A 1 195 ? 121.991 150.399 116.859 1.00 33.64 ?  195 LEU A CD2   1 
ATOM   1603  N  N     . GLY A 1 196 ? 123.087 145.224 115.316 1.00 34.97 ?  196 GLY A N     1 
ATOM   1604  C  CA    . GLY A 1 196 ? 123.223 144.256 114.251 1.00 33.07 ?  196 GLY A CA    1 
ATOM   1605  C  C     . GLY A 1 196 ? 124.595 144.168 113.629 1.00 37.29 ?  196 GLY A C     1 
ATOM   1606  O  O     . GLY A 1 196 ? 124.739 143.533 112.578 1.00 40.02 ?  196 GLY A O     1 
ATOM   1607  N  N     . GLY A 1 197 ? 125.607 144.775 114.239 1.00 34.21 ?  197 GLY A N     1 
ATOM   1608  C  CA    . GLY A 1 197 ? 126.933 144.792 113.663 1.00 24.52 ?  197 GLY A CA    1 
ATOM   1609  C  C     . GLY A 1 197 ? 127.863 143.743 114.241 1.00 23.86 ?  197 GLY A C     1 
ATOM   1610  O  O     . GLY A 1 197 ? 127.749 143.348 115.398 1.00 33.65 ?  197 GLY A O     1 
ATOM   1611  N  N     . GLY A 1 198 ? 128.796 143.291 113.404 1.00 17.12 ?  198 GLY A N     1 
ATOM   1612  C  CA    . GLY A 1 198 ? 129.858 142.414 113.867 1.00 16.73 ?  198 GLY A CA    1 
ATOM   1613  C  C     . GLY A 1 198 ? 130.981 143.238 114.464 1.00 17.59 ?  198 GLY A C     1 
ATOM   1614  O  O     . GLY A 1 198 ? 131.456 144.200 113.851 1.00 18.46 ?  198 GLY A O     1 
ATOM   1615  N  N     . VAL A 1 199 ? 131.411 142.862 115.663 1.00 21.76 ?  199 VAL A N     1 
ATOM   1616  C  CA    . VAL A 1 199 ? 132.342 143.656 116.454 1.00 13.39 ?  199 VAL A CA    1 
ATOM   1617  C  C     . VAL A 1 199 ? 133.657 142.906 116.570 1.00 11.65 ?  199 VAL A C     1 
ATOM   1618  O  O     . VAL A 1 199 ? 133.681 141.737 116.971 1.00 16.01 ?  199 VAL A O     1 
ATOM   1619  C  CB    . VAL A 1 199 ? 131.768 143.966 117.846 1.00 13.59 ?  199 VAL A CB    1 
ATOM   1620  C  CG1   . VAL A 1 199 ? 132.713 144.865 118.617 1.00 15.15 ?  199 VAL A CG1   1 
ATOM   1621  C  CG2   . VAL A 1 199 ? 130.400 144.598 117.719 1.00 18.65 ?  199 VAL A CG2   1 
ATOM   1622  N  N     . SER A 1 200 ? 134.749 143.580 116.228 1.00 15.20 ?  200 SER A N     1 
ATOM   1623  C  CA    . SER A 1 200 ? 136.095 143.056 116.400 1.00 3.66  ?  200 SER A CA    1 
ATOM   1624  C  C     . SER A 1 200 ? 136.809 143.886 117.455 1.00 11.73 ?  200 SER A C     1 
ATOM   1625  O  O     . SER A 1 200 ? 136.758 145.120 117.419 1.00 21.37 ?  200 SER A O     1 
ATOM   1626  C  CB    . SER A 1 200 ? 136.869 143.083 115.084 1.00 9.17  ?  200 SER A CB    1 
ATOM   1627  O  OG    . SER A 1 200 ? 138.063 142.329 115.177 1.00 16.25 ?  200 SER A OG    1 
ATOM   1628  N  N     . LEU A 1 201 ? 137.464 143.212 118.394 1.00 16.66 ?  201 LEU A N     1 
ATOM   1629  C  CA    . LEU A 1 201 ? 138.151 143.866 119.496 1.00 9.22  ?  201 LEU A CA    1 
ATOM   1630  C  C     . LEU A 1 201 ? 139.624 143.487 119.475 1.00 7.69  ?  201 LEU A C     1 
ATOM   1631  O  O     . LEU A 1 201 ? 139.963 142.308 119.333 1.00 9.39  ?  201 LEU A O     1 
ATOM   1632  C  CB    . LEU A 1 201 ? 137.527 143.482 120.840 1.00 16.07 ?  201 LEU A CB    1 
ATOM   1633  C  CG    . LEU A 1 201 ? 136.059 143.865 121.027 1.00 14.03 ?  201 LEU A CG    1 
ATOM   1634  C  CD1   . LEU A 1 201 ? 135.161 142.656 120.827 1.00 14.27 ?  201 LEU A CD1   1 
ATOM   1635  C  CD2   . LEU A 1 201 ? 135.835 144.486 122.393 1.00 15.95 ?  201 LEU A CD2   1 
ATOM   1636  N  N     . ASN A 1 202 ? 140.488 144.486 119.623 1.00 13.18 ?  202 ASN A N     1 
ATOM   1637  C  CA    . ASN A 1 202 ? 141.922 144.266 119.741 1.00 7.05  ?  202 ASN A CA    1 
ATOM   1638  C  C     . ASN A 1 202 ? 142.264 144.053 121.209 1.00 13.85 ?  202 ASN A C     1 
ATOM   1639  O  O     . ASN A 1 202 ? 142.013 144.928 122.044 1.00 25.93 ?  202 ASN A O     1 
ATOM   1640  C  CB    . ASN A 1 202 ? 142.697 145.453 119.171 1.00 8.39  ?  202 ASN A CB    1 
ATOM   1641  C  CG    . ASN A 1 202 ? 144.176 145.170 119.028 1.00 11.78 ?  202 ASN A CG    1 
ATOM   1642  O  OD1   . ASN A 1 202 ? 144.590 144.020 118.888 1.00 17.73 ?  202 ASN A OD1   1 
ATOM   1643  N  ND2   . ASN A 1 202 ? 144.984 146.222 119.061 1.00 14.87 ?  202 ASN A ND2   1 
ATOM   1644  N  N     . LEU A 1 203 ? 142.832 142.890 121.524 1.00 8.33  ?  203 LEU A N     1 
ATOM   1645  C  CA    . LEU A 1 203 ? 143.171 142.538 122.897 1.00 9.55  ?  203 LEU A CA    1 
ATOM   1646  C  C     . LEU A 1 203 ? 144.671 142.545 123.150 1.00 12.58 ?  203 LEU A C     1 
ATOM   1647  O  O     . LEU A 1 203 ? 145.114 142.079 124.205 1.00 14.59 ?  203 LEU A O     1 
ATOM   1648  C  CB    . LEU A 1 203 ? 142.584 141.171 123.250 1.00 15.42 ?  203 LEU A CB    1 
ATOM   1649  C  CG    . LEU A 1 203 ? 141.065 141.025 123.139 1.00 15.72 ?  203 LEU A CG    1 
ATOM   1650  C  CD1   . LEU A 1 203 ? 140.603 139.798 123.896 1.00 14.37 ?  203 LEU A CD1   1 
ATOM   1651  C  CD2   . LEU A 1 203 ? 140.349 142.269 123.645 1.00 12.05 ?  203 LEU A CD2   1 
ATOM   1652  N  N     . SER A 1 204 ? 145.464 143.070 122.213 1.00 17.27 ?  204 SER A N     1 
ATOM   1653  C  CA    . SER A 1 204 ? 146.914 143.050 122.365 1.00 15.28 ?  204 SER A CA    1 
ATOM   1654  C  C     . SER A 1 204 ? 147.396 144.011 123.443 1.00 17.32 ?  204 SER A C     1 
ATOM   1655  O  O     . SER A 1 204 ? 148.409 143.740 124.097 1.00 27.44 ?  204 SER A O     1 
ATOM   1656  C  CB    . SER A 1 204 ? 147.583 143.380 121.032 1.00 12.39 ?  204 SER A CB    1 
ATOM   1657  O  OG    . SER A 1 204 ? 147.110 142.531 120.003 1.00 20.84 ?  204 SER A OG    1 
ATOM   1658  N  N     . LYS A 1 205 ? 146.698 145.131 123.641 1.00 18.64 ?  205 LYS A N     1 
ATOM   1659  C  CA    . LYS A 1 205 ? 147.087 146.067 124.687 1.00 21.79 ?  205 LYS A CA    1 
ATOM   1660  C  C     . LYS A 1 205 ? 146.812 145.523 126.080 1.00 22.02 ?  205 LYS A C     1 
ATOM   1661  O  O     . LYS A 1 205 ? 147.423 145.990 127.046 1.00 28.08 ?  205 LYS A O     1 
ATOM   1662  C  CB    . LYS A 1 205 ? 146.364 147.399 124.497 1.00 22.28 ?  205 LYS A CB    1 
ATOM   1663  C  CG    . LYS A 1 205 ? 146.819 148.164 123.276 1.00 21.54 ?  205 LYS A CG    1 
ATOM   1664  C  CD    . LYS A 1 205 ? 146.105 149.491 123.158 1.00 25.34 ?  205 LYS A CD    1 
ATOM   1665  C  CE    . LYS A 1 205 ? 146.713 150.329 122.050 1.00 28.62 ?  205 LYS A CE    1 
ATOM   1666  N  NZ    . LYS A 1 205 ? 146.604 149.665 120.724 1.00 24.12 1  205 LYS A NZ    1 
ATOM   1667  N  N     . LEU A 1 206 ? 145.911 144.554 126.203 1.00 18.83 ?  206 LEU A N     1 
ATOM   1668  C  CA    . LEU A 1 206 ? 145.614 143.961 127.497 1.00 12.03 ?  206 LEU A CA    1 
ATOM   1669  C  C     . LEU A 1 206 ? 146.803 143.150 127.996 1.00 18.40 ?  206 LEU A C     1 
ATOM   1670  O  O     . LEU A 1 206 ? 147.415 142.389 127.242 1.00 24.65 ?  206 LEU A O     1 
ATOM   1671  C  CB    . LEU A 1 206 ? 144.378 143.073 127.397 1.00 16.39 ?  206 LEU A CB    1 
ATOM   1672  C  CG    . LEU A 1 206 ? 143.073 143.801 127.075 1.00 21.56 ?  206 LEU A CG    1 
ATOM   1673  C  CD1   . LEU A 1 206 ? 141.928 142.814 127.000 1.00 19.17 ?  206 LEU A CD1   1 
ATOM   1674  C  CD2   . LEU A 1 206 ? 142.793 144.876 128.108 1.00 21.52 ?  206 LEU A CD2   1 
ATOM   1675  N  N     . ARG A 1 207 ? 147.128 143.317 129.273 1.00 25.76 ?  207 ARG A N     1 
ATOM   1676  C  CA    . ARG A 1 207 ? 148.268 142.618 129.842 1.00 22.21 ?  207 ARG A CA    1 
ATOM   1677  C  C     . ARG A 1 207 ? 147.963 141.132 130.003 1.00 27.34 ?  207 ARG A C     1 
ATOM   1678  O  O     . ARG A 1 207 ? 146.814 140.724 130.188 1.00 33.02 ?  207 ARG A O     1 
ATOM   1679  C  CB    . ARG A 1 207 ? 148.664 143.241 131.180 1.00 25.46 ?  207 ARG A CB    1 
ATOM   1680  C  CG    . ARG A 1 207 ? 147.621 143.156 132.272 1.00 20.93 ?  207 ARG A CG    1 
ATOM   1681  C  CD    . ARG A 1 207 ? 148.044 143.980 133.475 1.00 21.04 ?  207 ARG A CD    1 
ATOM   1682  N  NE    . ARG A 1 207 ? 147.687 145.385 133.321 1.00 29.59 ?  207 ARG A NE    1 
ATOM   1683  C  CZ    . ARG A 1 207 ? 147.746 146.285 134.293 1.00 23.85 ?  207 ARG A CZ    1 
ATOM   1684  N  NH1   . ARG A 1 207 ? 148.163 145.965 135.506 1.00 28.40 1  207 ARG A NH1   1 
ATOM   1685  N  NH2   . ARG A 1 207 ? 147.374 147.536 134.041 1.00 19.28 ?  207 ARG A NH2   1 
ATOM   1686  N  N     . ALA A 1 208 ? 149.015 140.320 129.925 1.00 28.20 ?  208 ALA A N     1 
ATOM   1687  C  CA    . ALA A 1 208 ? 148.872 138.875 129.857 1.00 25.93 ?  208 ALA A CA    1 
ATOM   1688  C  C     . ALA A 1 208 ? 148.513 138.300 131.225 1.00 31.00 ?  208 ALA A C     1 
ATOM   1689  O  O     . ALA A 1 208 ? 148.399 139.013 132.224 1.00 33.88 ?  208 ALA A O     1 
ATOM   1690  C  CB    . ALA A 1 208 ? 150.152 138.243 129.314 1.00 27.47 ?  208 ALA A CB    1 
ATOM   1691  N  N     . LYS A 1 209 ? 148.318 136.986 131.264 1.00 30.80 ?  209 LYS A N     1 
ATOM   1692  C  CA    . LYS A 1 209 ? 147.987 136.315 132.514 1.00 25.81 ?  209 LYS A CA    1 
ATOM   1693  C  C     . LYS A 1 209 ? 149.216 136.243 133.411 1.00 33.73 ?  209 LYS A C     1 
ATOM   1694  O  O     . LYS A 1 209 ? 150.318 135.928 132.949 1.00 34.47 ?  209 LYS A O     1 
ATOM   1695  C  CB    . LYS A 1 209 ? 147.445 134.915 132.240 1.00 28.85 ?  209 LYS A CB    1 
ATOM   1696  C  CG    . LYS A 1 209 ? 146.984 134.178 133.484 1.00 32.40 ?  209 LYS A CG    1 
ATOM   1697  C  CD    . LYS A 1 209 ? 146.889 132.679 133.255 1.00 32.56 ?  209 LYS A CD    1 
ATOM   1698  C  CE    . LYS A 1 209 ? 148.017 132.168 132.373 1.00 35.58 ?  209 LYS A CE    1 
ATOM   1699  N  NZ    . LYS A 1 209 ? 147.875 130.715 132.084 1.00 35.06 1  209 LYS A NZ    1 
ATOM   1700  N  N     . GLY A 1 210 ? 149.024 136.524 134.696 1.00 37.65 ?  210 GLY A N     1 
ATOM   1701  C  CA    . GLY A 1 210 ? 150.125 136.548 135.633 1.00 32.83 ?  210 GLY A CA    1 
ATOM   1702  C  C     . GLY A 1 210 ? 150.823 137.880 135.768 1.00 35.30 ?  210 GLY A C     1 
ATOM   1703  O  O     . GLY A 1 210 ? 151.956 137.920 136.261 1.00 40.60 ?  210 GLY A O     1 
ATOM   1704  N  N     . GLU A 1 211 ? 150.191 138.968 135.344 1.00 33.92 ?  211 GLU A N     1 
ATOM   1705  C  CA    . GLU A 1 211 ? 150.756 140.302 135.468 1.00 31.71 ?  211 GLU A CA    1 
ATOM   1706  C  C     . GLU A 1 211 ? 150.223 140.987 136.722 1.00 34.75 ?  211 GLU A C     1 
ATOM   1707  O  O     . GLU A 1 211 ? 149.326 140.489 137.405 1.00 36.62 ?  211 GLU A O     1 
ATOM   1708  C  CB    . GLU A 1 211 ? 150.448 141.136 134.223 1.00 30.32 ?  211 GLU A CB    1 
ATOM   1709  C  CG    . GLU A 1 211 ? 151.111 140.607 132.968 1.00 33.60 ?  211 GLU A CG    1 
ATOM   1710  C  CD    . GLU A 1 211 ? 151.891 141.670 132.227 1.00 36.43 ?  211 GLU A CD    1 
ATOM   1711  O  OE1   . GLU A 1 211 ? 152.893 142.167 132.782 1.00 39.07 ?  211 GLU A OE1   1 
ATOM   1712  O  OE2   . GLU A 1 211 ? 151.516 141.999 131.083 1.00 30.88 -1 211 GLU A OE2   1 
ATOM   1713  N  N     . ALA A 1 212 ? 150.792 142.151 137.019 1.00 33.78 ?  212 ALA A N     1 
ATOM   1714  C  CA    . ALA A 1 212 ? 150.504 142.854 138.260 1.00 33.97 ?  212 ALA A CA    1 
ATOM   1715  C  C     . ALA A 1 212 ? 149.384 143.868 138.078 1.00 39.38 ?  212 ALA A C     1 
ATOM   1716  O  O     . ALA A 1 212 ? 149.335 144.590 137.077 1.00 41.12 ?  212 ALA A O     1 
ATOM   1717  C  CB    . ALA A 1 212 ? 151.758 143.555 138.782 1.00 35.82 ?  212 ALA A CB    1 
ATOM   1718  N  N     . ILE A 1 213 ? 148.481 143.912 139.055 1.00 32.09 ?  213 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 147.441 144.932 139.142 1.00 34.78 ?  213 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 147.696 145.718 140.419 1.00 36.14 ?  213 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 147.566 145.175 141.524 1.00 40.58 ?  213 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 146.031 144.327 139.139 1.00 34.49 ?  213 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 145.879 143.317 138.000 1.00 34.39 ?  213 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 144.983 145.422 139.027 1.00 29.79 ?  213 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 144.646 142.451 138.120 1.00 30.50 ?  213 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 148.047 146.997 140.271 1.00 41.13 ?  214 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 148.399 147.858 141.403 1.00 40.28 ?  214 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 149.514 147.238 142.242 1.00 46.68 ?  214 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 149.464 147.229 143.474 1.00 49.91 ?  214 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 147.174 148.176 142.262 1.00 40.44 ?  214 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 146.331 149.321 141.730 1.00 40.01 ?  214 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 145.133 149.597 142.622 1.00 42.30 ?  214 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 144.449 150.897 142.232 1.00 44.11 ?  214 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 143.256 151.176 143.077 1.00 42.67 1  214 LYS A NZ    1 
ATOM   1735  N  N     . ASP A 1 215 ? 150.525 146.702 141.556 1.00 47.70 ?  215 ASP A N     1 
ATOM   1736  C  CA    . ASP A 1 215 ? 151.743 146.188 142.188 1.00 49.79 ?  215 ASP A CA    1 
ATOM   1737  C  C     . ASP A 1 215 ? 151.458 145.014 143.124 1.00 48.44 ?  215 ASP A C     1 
ATOM   1738  O  O     . ASP A 1 215 ? 152.101 144.858 144.164 1.00 48.37 ?  215 ASP A O     1 
ATOM   1739  C  CB    . ASP A 1 215 ? 152.496 147.299 142.922 1.00 48.76 ?  215 ASP A CB    1 
ATOM   1740  C  CG    . ASP A 1 215 ? 152.837 148.468 142.017 1.00 52.47 ?  215 ASP A CG    1 
ATOM   1741  O  OD1   . ASP A 1 215 ? 153.220 148.227 140.854 1.00 51.00 ?  215 ASP A OD1   1 
ATOM   1742  O  OD2   . ASP A 1 215 ? 152.726 149.627 142.470 1.00 51.63 -1 215 ASP A OD2   1 
ATOM   1743  N  N     . VAL A 1 216 ? 150.490 144.178 142.757 1.00 43.69 ?  216 VAL A N     1 
ATOM   1744  C  CA    . VAL A 1 216 ? 150.301 142.870 143.375 1.00 45.86 ?  216 VAL A CA    1 
ATOM   1745  C  C     . VAL A 1 216 ? 150.494 141.823 142.284 1.00 46.94 ?  216 VAL A C     1 
ATOM   1746  O  O     . VAL A 1 216 ? 149.961 141.962 141.177 1.00 49.98 ?  216 VAL A O     1 
ATOM   1747  C  CB    . VAL A 1 216 ? 148.933 142.747 144.085 1.00 44.85 ?  216 VAL A CB    1 
ATOM   1748  C  CG1   . VAL A 1 216 ? 148.394 144.124 144.455 1.00 43.90 ?  216 VAL A CG1   1 
ATOM   1749  C  CG2   . VAL A 1 216 ? 147.912 141.961 143.270 1.00 43.37 ?  216 VAL A CG2   1 
ATOM   1750  N  N     . GLU A 1 217 ? 151.312 140.816 142.573 1.00 48.48 ?  217 GLU A N     1 
ATOM   1751  C  CA    . GLU A 1 217 ? 151.822 139.937 141.531 1.00 48.13 ?  217 GLU A CA    1 
ATOM   1752  C  C     . GLU A 1 217 ? 150.843 138.810 141.216 1.00 49.28 ?  217 GLU A C     1 
ATOM   1753  O  O     . GLU A 1 217 ? 150.014 138.417 142.041 1.00 51.39 ?  217 GLU A O     1 
ATOM   1754  C  CB    . GLU A 1 217 ? 153.176 139.354 141.938 1.00 50.28 ?  217 GLU A CB    1 
ATOM   1755  C  CG    . GLU A 1 217 ? 154.195 140.376 142.430 1.00 50.51 ?  217 GLU A CG    1 
ATOM   1756  C  CD    . GLU A 1 217 ? 154.093 141.711 141.715 1.00 52.26 ?  217 GLU A CD    1 
ATOM   1757  O  OE1   . GLU A 1 217 ? 154.650 141.835 140.605 1.00 53.56 ?  217 GLU A OE1   1 
ATOM   1758  O  OE2   . GLU A 1 217 ? 153.466 142.639 142.268 1.00 49.24 -1 217 GLU A OE2   1 
ATOM   1759  N  N     . ASN A 1 218 ? 150.963 138.285 139.991 1.00 44.02 ?  218 ASN A N     1 
ATOM   1760  C  CA    . ASN A 1 218 ? 150.185 137.134 139.525 1.00 44.04 ?  218 ASN A CA    1 
ATOM   1761  C  C     . ASN A 1 218 ? 148.685 137.368 139.687 1.00 47.82 ?  218 ASN A C     1 
ATOM   1762  O  O     . ASN A 1 218 ? 147.944 136.487 140.126 1.00 46.76 ?  218 ASN A O     1 
ATOM   1763  C  CB    . ASN A 1 218 ? 150.617 135.854 140.241 1.00 43.02 ?  218 ASN A CB    1 
ATOM   1764  C  CG    . ASN A 1 218 ? 150.644 134.651 139.318 1.00 48.15 ?  218 ASN A CG    1 
ATOM   1765  O  OD1   . ASN A 1 218 ? 151.175 134.717 138.209 1.00 50.06 ?  218 ASN A OD1   1 
ATOM   1766  N  ND2   . ASN A 1 218 ? 150.070 133.544 139.773 1.00 47.54 ?  218 ASN A ND2   1 
ATOM   1767  N  N     . ALA A 1 219 ? 148.233 138.567 139.325 1.00 38.03 ?  219 ALA A N     1 
ATOM   1768  C  CA    . ALA A 1 219 ? 146.852 138.969 139.551 1.00 33.65 ?  219 ALA A CA    1 
ATOM   1769  C  C     . ALA A 1 219 ? 146.002 138.979 138.290 1.00 35.31 ?  219 ALA A C     1 
ATOM   1770  O  O     . ALA A 1 219 ? 144.800 138.709 138.368 1.00 36.61 ?  219 ALA A O     1 
ATOM   1771  C  CB    . ALA A 1 219 ? 146.810 140.360 140.188 1.00 35.87 ?  219 ALA A CB    1 
ATOM   1772  N  N     . THR A 1 220 ? 146.589 139.283 137.138 1.00 36.45 ?  220 THR A N     1 
ATOM   1773  C  CA    . THR A 1 220 ? 145.809 139.414 135.916 1.00 30.45 ?  220 THR A CA    1 
ATOM   1774  C  C     . THR A 1 220 ? 145.345 138.051 135.419 1.00 34.14 ?  220 THR A C     1 
ATOM   1775  O  O     . THR A 1 220 ? 146.085 137.064 135.473 1.00 35.22 ?  220 THR A O     1 
ATOM   1776  C  CB    . THR A 1 220 ? 146.633 140.113 134.835 1.00 27.27 ?  220 THR A CB    1 
ATOM   1777  O  OG1   . THR A 1 220 ? 147.184 141.326 135.363 1.00 35.48 ?  220 THR A OG1   1 
ATOM   1778  C  CG2   . THR A 1 220 ? 145.763 140.447 133.636 1.00 29.46 ?  220 THR A CG2   1 
ATOM   1779  N  N     . LYS A 1 221 ? 144.105 138.001 134.932 1.00 35.92 ?  221 LYS A N     1 
ATOM   1780  C  CA    . LYS A 1 221 ? 143.569 136.794 134.320 1.00 30.05 ?  221 LYS A CA    1 
ATOM   1781  C  C     . LYS A 1 221 ? 143.983 136.639 132.864 1.00 33.95 ?  221 LYS A C     1 
ATOM   1782  O  O     . LYS A 1 221 ? 143.720 135.587 132.271 1.00 40.03 ?  221 LYS A O     1 
ATOM   1783  C  CB    . LYS A 1 221 ? 142.042 136.785 134.418 1.00 29.97 ?  221 LYS A CB    1 
ATOM   1784  C  CG    . LYS A 1 221 ? 141.516 136.571 135.821 1.00 32.25 ?  221 LYS A CG    1 
ATOM   1785  C  CD    . LYS A 1 221 ? 140.203 135.812 135.803 1.00 33.02 ?  221 LYS A CD    1 
ATOM   1786  C  CE    . LYS A 1 221 ? 139.875 135.254 137.175 1.00 33.42 ?  221 LYS A CE    1 
ATOM   1787  N  NZ    . LYS A 1 221 ? 138.735 134.299 137.127 1.00 36.29 1  221 LYS A NZ    1 
ATOM   1788  N  N     . GLY A 1 222 ? 144.617 137.648 132.281 1.00 31.76 ?  222 GLY A N     1 
ATOM   1789  C  CA    . GLY A 1 222 ? 145.014 137.588 130.895 1.00 26.99 ?  222 GLY A CA    1 
ATOM   1790  C  C     . GLY A 1 222 ? 143.891 137.989 129.959 1.00 27.61 ?  222 GLY A C     1 
ATOM   1791  O  O     . GLY A 1 222 ? 142.830 138.473 130.364 1.00 33.53 ?  222 GLY A O     1 
ATOM   1792  N  N     . VAL A 1 223 ? 144.145 137.780 128.667 1.00 25.41 ?  223 VAL A N     1 
ATOM   1793  C  CA    . VAL A 1 223 ? 143.137 138.100 127.665 1.00 24.51 ?  223 VAL A CA    1 
ATOM   1794  C  C     . VAL A 1 223 ? 142.062 137.028 127.568 1.00 18.93 ?  223 VAL A C     1 
ATOM   1795  O  O     . VAL A 1 223 ? 141.009 137.281 126.977 1.00 22.69 ?  223 VAL A O     1 
ATOM   1796  C  CB    . VAL A 1 223 ? 143.779 138.325 126.284 1.00 22.73 ?  223 VAL A CB    1 
ATOM   1797  C  CG1   . VAL A 1 223 ? 144.996 139.219 126.407 1.00 20.06 ?  223 VAL A CG1   1 
ATOM   1798  C  CG2   . VAL A 1 223 ? 144.146 136.997 125.641 1.00 20.14 ?  223 VAL A CG2   1 
ATOM   1799  N  N     . VAL A 1 224 ? 142.286 135.843 128.138 1.00 27.29 ?  224 VAL A N     1 
ATOM   1800  C  CA    . VAL A 1 224 ? 141.289 134.781 128.040 1.00 23.25 ?  224 VAL A CA    1 
ATOM   1801  C  C     . VAL A 1 224 ? 140.055 135.096 128.884 1.00 27.16 ?  224 VAL A C     1 
ATOM   1802  O  O     . VAL A 1 224 ? 138.927 134.808 128.467 1.00 29.49 ?  224 VAL A O     1 
ATOM   1803  C  CB    . VAL A 1 224 ? 141.914 133.430 128.426 1.00 30.45 ?  224 VAL A CB    1 
ATOM   1804  C  CG1   . VAL A 1 224 ? 140.873 132.325 128.384 1.00 28.30 ?  224 VAL A CG1   1 
ATOM   1805  C  CG2   . VAL A 1 224 ? 143.066 133.106 127.494 1.00 28.17 ?  224 VAL A CG2   1 
ATOM   1806  N  N     . GLY A 1 225 ? 140.233 135.686 130.066 1.00 26.05 ?  225 GLY A N     1 
ATOM   1807  C  CA    . GLY A 1 225 ? 139.078 136.114 130.842 1.00 23.64 ?  225 GLY A CA    1 
ATOM   1808  C  C     . GLY A 1 225 ? 138.289 137.204 130.144 1.00 21.95 ?  225 GLY A C     1 
ATOM   1809  O  O     . GLY A 1 225 ? 137.053 137.215 130.176 1.00 29.10 ?  225 GLY A O     1 
ATOM   1810  N  N     . VAL A 1 226 ? 138.993 138.134 129.497 1.00 22.04 ?  226 VAL A N     1 
ATOM   1811  C  CA    . VAL A 1 226 ? 138.324 139.166 128.713 1.00 21.14 ?  226 VAL A CA    1 
ATOM   1812  C  C     . VAL A 1 226 ? 137.579 138.541 127.542 1.00 19.41 ?  226 VAL A C     1 
ATOM   1813  O  O     . VAL A 1 226 ? 136.488 138.987 127.173 1.00 22.12 ?  226 VAL A O     1 
ATOM   1814  C  CB    . VAL A 1 226 ? 139.338 140.222 128.242 1.00 19.03 ?  226 VAL A CB    1 
ATOM   1815  C  CG1   . VAL A 1 226 ? 138.622 141.386 127.576 1.00 26.23 ?  226 VAL A CG1   1 
ATOM   1816  C  CG2   . VAL A 1 226 ? 140.176 140.702 129.409 1.00 16.46 ?  226 VAL A CG2   1 
ATOM   1817  N  N     . MET A 1 227 ? 138.157 137.501 126.938 1.00 21.13 ?  227 MET A N     1 
ATOM   1818  C  CA    . MET A 1 227 ? 137.472 136.801 125.856 1.00 23.66 ?  227 MET A CA    1 
ATOM   1819  C  C     . MET A 1 227 ? 136.220 136.102 126.359 1.00 23.17 ?  227 MET A C     1 
ATOM   1820  O  O     . MET A 1 227 ? 135.207 136.064 125.659 1.00 28.48 ?  227 MET A O     1 
ATOM   1821  C  CB    . MET A 1 227 ? 138.404 135.794 125.187 1.00 20.13 ?  227 MET A CB    1 
ATOM   1822  C  CG    . MET A 1 227 ? 139.560 136.411 124.438 1.00 17.73 ?  227 MET A CG    1 
ATOM   1823  S  SD    . MET A 1 227 ? 140.818 135.190 124.049 1.00 36.51 ?  227 MET A SD    1 
ATOM   1824  C  CE    . MET A 1 227 ? 139.938 134.207 122.844 1.00 24.79 ?  227 MET A CE    1 
ATOM   1825  N  N     . LYS A 1 228 ? 136.276 135.521 127.558 1.00 21.26 ?  228 LYS A N     1 
ATOM   1826  C  CA    . LYS A 1 228 ? 135.081 134.915 128.138 1.00 22.96 ?  228 LYS A CA    1 
ATOM   1827  C  C     . LYS A 1 228 ? 133.999 135.960 128.374 1.00 21.81 ?  228 LYS A C     1 
ATOM   1828  O  O     . LYS A 1 228 ? 132.818 135.729 128.074 1.00 24.62 ?  228 LYS A O     1 
ATOM   1829  C  CB    . LYS A 1 228 ? 135.430 134.208 129.447 1.00 24.81 ?  228 LYS A CB    1 
ATOM   1830  C  CG    . LYS A 1 228 ? 136.050 132.835 129.277 1.00 27.57 ?  228 LYS A CG    1 
ATOM   1831  C  CD    . LYS A 1 228 ? 136.609 132.331 130.599 1.00 30.30 ?  228 LYS A CD    1 
ATOM   1832  C  CE    . LYS A 1 228 ? 138.108 132.561 130.691 1.00 31.49 ?  228 LYS A CE    1 
ATOM   1833  N  NZ    . LYS A 1 228 ? 138.569 132.755 132.093 1.00 27.84 1  228 LYS A NZ    1 
ATOM   1834  N  N     . LEU A 1 229 ? 134.386 137.122 128.906 1.00 20.71 ?  229 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 229 ? 133.428 138.204 129.112 1.00 18.79 ?  229 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 229 ? 132.816 138.657 127.793 1.00 20.13 ?  229 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 229 ? 131.600 138.855 127.690 1.00 18.55 ?  229 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 229 ? 134.108 139.378 129.813 1.00 20.16 ?  229 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 229 ? 134.400 139.248 131.306 1.00 18.98 ?  229 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 229 ? 135.268 140.405 131.759 1.00 21.66 ?  229 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 229 ? 133.107 139.210 132.094 1.00 18.33 ?  229 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 230 ? 133.652 138.827 126.767 1.00 24.97 ?  230 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 230 ? 133.164 139.260 125.463 1.00 16.02 ?  230 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 230 ? 132.271 138.204 124.827 1.00 15.64 ?  230 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 230 ? 131.276 138.538 124.179 1.00 30.75 ?  230 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 230 ? 134.339 139.592 124.546 1.00 23.37 ?  230 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 230 ? 135.110 140.868 124.886 1.00 22.41 ?  230 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 230 ? 136.377 140.964 124.050 1.00 23.43 ?  230 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 230 ? 134.233 142.093 124.686 1.00 16.74 ?  230 LEU A CD2   1 
ATOM   1850  N  N     . ASP A 1 231 ? 132.618 136.928 124.987 1.00 23.35 ?  231 ASP A N     1 
ATOM   1851  C  CA    . ASP A 1 231 ? 131.790 135.856 124.451 1.00 23.77 ?  231 ASP A CA    1 
ATOM   1852  C  C     . ASP A 1 231 ? 130.422 135.841 125.116 1.00 22.03 ?  231 ASP A C     1 
ATOM   1853  O  O     . ASP A 1 231 ? 129.401 135.668 124.442 1.00 29.84 ?  231 ASP A O     1 
ATOM   1854  C  CB    . ASP A 1 231 ? 132.497 134.512 124.630 1.00 23.08 ?  231 ASP A CB    1 
ATOM   1855  C  CG    . ASP A 1 231 ? 131.631 133.336 124.232 1.00 36.05 ?  231 ASP A CG    1 
ATOM   1856  O  OD1   . ASP A 1 231 ? 131.153 133.312 123.078 1.00 42.35 ?  231 ASP A OD1   1 
ATOM   1857  O  OD2   . ASP A 1 231 ? 131.433 132.432 125.071 1.00 33.33 -1 231 ASP A OD2   1 
ATOM   1858  N  N     . ASN A 1 232 ? 130.379 136.038 126.435 1.00 27.62 ?  232 ASN A N     1 
ATOM   1859  C  CA    . ASN A 1 232 ? 129.089 136.138 127.113 1.00 25.45 ?  232 ASN A CA    1 
ATOM   1860  C  C     . ASN A 1 232 ? 128.306 137.357 126.636 1.00 21.44 ?  232 ASN A C     1 
ATOM   1861  O  O     . ASN A 1 232 ? 127.087 137.282 126.441 1.00 28.17 ?  232 ASN A O     1 
ATOM   1862  C  CB    . ASN A 1 232 ? 129.287 136.181 128.626 1.00 26.42 ?  232 ASN A CB    1 
ATOM   1863  C  CG    . ASN A 1 232 ? 128.402 135.190 129.351 1.00 32.00 ?  232 ASN A CG    1 
ATOM   1864  O  OD1   . ASN A 1 232 ? 127.180 135.333 129.371 1.00 34.71 ?  232 ASN A OD1   1 
ATOM   1865  N  ND2   . ASN A 1 232 ? 129.010 134.167 129.933 1.00 34.25 ?  232 ASN A ND2   1 
ATOM   1866  N  N     . ALA A 1 233 ? 128.992 138.486 126.446 1.00 17.49 ?  233 ALA A N     1 
ATOM   1867  C  CA    . ALA A 1 233 ? 128.320 139.691 125.971 1.00 19.25 ?  233 ALA A CA    1 
ATOM   1868  C  C     . ALA A 1 233 ? 127.740 139.491 124.576 1.00 27.61 ?  233 ALA A C     1 
ATOM   1869  O  O     . ALA A 1 233 ? 126.636 139.963 124.281 1.00 27.48 ?  233 ALA A O     1 
ATOM   1870  C  CB    . ALA A 1 233 ? 129.291 140.870 125.987 1.00 19.50 ?  233 ALA A CB    1 
ATOM   1871  N  N     . PHE A 1 234 ? 128.475 138.803 123.701 1.00 25.88 ?  234 PHE A N     1 
ATOM   1872  C  CA    . PHE A 1 234 ? 127.998 138.572 122.344 1.00 18.99 ?  234 PHE A CA    1 
ATOM   1873  C  C     . PHE A 1 234 ? 126.888 137.531 122.307 1.00 22.17 ?  234 PHE A C     1 
ATOM   1874  O  O     . PHE A 1 234 ? 125.989 137.619 121.464 1.00 29.06 ?  234 PHE A O     1 
ATOM   1875  C  CB    . PHE A 1 234 ? 129.155 138.152 121.439 1.00 24.21 ?  234 PHE A CB    1 
ATOM   1876  C  CG    . PHE A 1 234 ? 130.045 139.289 121.027 1.00 22.59 ?  234 PHE A CG    1 
ATOM   1877  C  CD1   . PHE A 1 234 ? 129.528 140.380 120.352 1.00 21.43 ?  234 PHE A CD1   1 
ATOM   1878  C  CD2   . PHE A 1 234 ? 131.397 139.267 121.311 1.00 21.36 ?  234 PHE A CD2   1 
ATOM   1879  C  CE1   . PHE A 1 234 ? 130.344 141.428 119.976 1.00 20.43 ?  234 PHE A CE1   1 
ATOM   1880  C  CE2   . PHE A 1 234 ? 132.217 140.311 120.939 1.00 22.33 ?  234 PHE A CE2   1 
ATOM   1881  C  CZ    . PHE A 1 234 ? 131.690 141.392 120.269 1.00 22.81 ?  234 PHE A CZ    1 
ATOM   1882  N  N     . ARG A 1 235 ? 126.934 136.539 123.198 1.00 24.66 ?  235 ARG A N     1 
ATOM   1883  C  CA    . ARG A 1 235 ? 125.817 135.609 123.310 1.00 25.84 ?  235 ARG A CA    1 
ATOM   1884  C  C     . ARG A 1 235 ? 124.561 136.326 123.785 1.00 31.07 ?  235 ARG A C     1 
ATOM   1885  O  O     . ARG A 1 235 ? 123.458 136.050 123.301 1.00 39.35 ?  235 ARG A O     1 
ATOM   1886  C  CB    . ARG A 1 235 ? 126.171 134.464 124.258 1.00 26.56 ?  235 ARG A CB    1 
ATOM   1887  C  CG    . ARG A 1 235 ? 127.223 133.515 123.720 1.00 32.06 ?  235 ARG A CG    1 
ATOM   1888  C  CD    . ARG A 1 235 ? 127.238 132.210 124.493 1.00 31.55 ?  235 ARG A CD    1 
ATOM   1889  N  NE    . ARG A 1 235 ? 128.491 132.027 125.216 1.00 33.93 ?  235 ARG A NE    1 
ATOM   1890  C  CZ    . ARG A 1 235 ? 128.694 132.417 126.466 1.00 35.96 ?  235 ARG A CZ    1 
ATOM   1891  N  NH1   . ARG A 1 235 ? 127.743 133.010 127.168 1.00 35.78 1  235 ARG A NH1   1 
ATOM   1892  N  NH2   . ARG A 1 235 ? 129.883 132.208 127.026 1.00 33.53 ?  235 ARG A NH2   1 
ATOM   1893  N  N     . TYR A 1 236 ? 124.711 137.252 124.734 1.00 25.37 ?  236 TYR A N     1 
ATOM   1894  C  CA    . TYR A 1 236 ? 123.556 137.980 125.246 1.00 21.11 ?  236 TYR A CA    1 
ATOM   1895  C  C     . TYR A 1 236 ? 122.958 138.895 124.182 1.00 24.21 ?  236 TYR A C     1 
ATOM   1896  O  O     . TYR A 1 236 ? 121.737 138.926 123.990 1.00 24.55 ?  236 TYR A O     1 
ATOM   1897  C  CB    . TYR A 1 236 ? 123.951 138.784 126.483 1.00 19.94 ?  236 TYR A CB    1 
ATOM   1898  C  CG    . TYR A 1 236 ? 122.780 139.429 127.178 1.00 23.99 ?  236 TYR A CG    1 
ATOM   1899  C  CD1   . TYR A 1 236 ? 121.905 138.671 127.941 1.00 21.35 ?  236 TYR A CD1   1 
ATOM   1900  C  CD2   . TYR A 1 236 ? 122.546 140.793 127.068 1.00 24.85 ?  236 TYR A CD2   1 
ATOM   1901  C  CE1   . TYR A 1 236 ? 120.832 139.250 128.578 1.00 24.71 ?  236 TYR A CE1   1 
ATOM   1902  C  CE2   . TYR A 1 236 ? 121.473 141.382 127.703 1.00 16.98 ?  236 TYR A CE2   1 
ATOM   1903  C  CZ    . TYR A 1 236 ? 120.621 140.604 128.456 1.00 21.52 ?  236 TYR A CZ    1 
ATOM   1904  O  OH    . TYR A 1 236 ? 119.550 141.177 129.093 1.00 25.78 ?  236 TYR A OH    1 
ATOM   1905  N  N     . ALA A 1 237 ? 123.803 139.646 123.480 1.00 30.61 ?  237 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 237 ? 123.358 140.591 122.456 1.00 30.91 ?  237 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 237 ? 123.379 139.868 121.113 1.00 35.59 ?  237 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 237 ? 124.411 139.779 120.448 1.00 39.55 ?  237 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 237 ? 124.238 141.835 122.446 1.00 30.89 ?  237 ALA A CB    1 
ATOM   1910  N  N     . ASP A 1 238 ? 122.220 139.355 120.709 1.00 50.35 ?  238 ASP A N     1 
ATOM   1911  C  CA    . ASP A 1 238 ? 122.091 138.525 119.515 1.00 54.69 ?  238 ASP A CA    1 
ATOM   1912  C  C     . ASP A 1 238 ? 120.966 139.038 118.621 1.00 59.58 ?  238 ASP A C     1 
ATOM   1913  O  O     . ASP A 1 238 ? 120.114 138.279 118.153 1.00 59.96 ?  238 ASP A O     1 
ATOM   1914  C  CB    . ASP A 1 238 ? 121.864 137.067 119.901 1.00 52.63 ?  238 ASP A CB    1 
ATOM   1915  C  CG    . ASP A 1 238 ? 120.720 136.894 120.876 1.00 55.48 ?  238 ASP A CG    1 
ATOM   1916  O  OD1   . ASP A 1 238 ? 120.248 137.909 121.429 1.00 55.79 ?  238 ASP A OD1   1 
ATOM   1917  O  OD2   . ASP A 1 238 ? 120.291 135.741 121.095 1.00 56.24 -1 238 ASP A OD2   1 
ATOM   1918  N  N     . GLN A 1 239 ? 120.958 140.352 118.376 1.00 65.05 ?  239 GLN A N     1 
ATOM   1919  C  CA    . GLN A 1 239 ? 119.997 140.992 117.472 1.00 64.51 ?  239 GLN A CA    1 
ATOM   1920  C  C     . GLN A 1 239 ? 118.555 140.678 117.863 1.00 64.87 ?  239 GLN A C     1 
ATOM   1921  O  O     . GLN A 1 239 ? 117.729 140.307 117.025 1.00 64.37 ?  239 GLN A O     1 
ATOM   1922  C  CB    . GLN A 1 239 ? 120.259 140.596 116.017 1.00 64.27 ?  239 GLN A CB    1 
ATOM   1923  C  CG    . GLN A 1 239 ? 121.298 141.441 115.309 1.00 63.60 ?  239 GLN A CG    1 
ATOM   1924  C  CD    . GLN A 1 239 ? 120.995 141.607 113.831 1.00 65.72 ?  239 GLN A CD    1 
ATOM   1925  O  OE1   . GLN A 1 239 ? 119.862 141.895 113.448 1.00 65.94 ?  239 GLN A OE1   1 
ATOM   1926  N  NE2   . GLN A 1 239 ? 122.008 141.417 112.994 1.00 64.99 ?  239 GLN A NE2   1 
ATOM   1927  N  N     . MET A 1 240 ? 118.252 140.835 119.153 1.00 68.51 ?  240 MET A N     1 
ATOM   1928  C  CA    . MET A 1 240 ? 116.913 140.575 119.683 1.00 68.14 ?  240 MET A CA    1 
ATOM   1929  C  C     . MET A 1 240 ? 116.467 139.144 119.386 1.00 69.94 ?  240 MET A C     1 
ATOM   1930  O  O     . MET A 1 240 ? 115.312 138.894 119.035 1.00 68.89 ?  240 MET A O     1 
ATOM   1931  C  CB    . MET A 1 240 ? 115.897 141.584 119.140 1.00 66.92 ?  240 MET A CB    1 
ATOM   1932  C  CG    . MET A 1 240 ? 116.062 142.997 119.673 1.00 68.38 ?  240 MET A CG    1 
ATOM   1933  S  SD    . MET A 1 240 ? 117.760 143.595 119.599 1.00 73.97 ?  240 MET A SD    1 
ATOM   1934  C  CE    . MET A 1 240 ? 117.483 145.363 119.588 1.00 65.29 ?  240 MET A CE    1 
ATOM   1935  N  N     . GLY A 1 241 ? 117.390 138.200 119.524 1.00 69.79 ?  241 GLY A N     1 
ATOM   1936  C  CA    . GLY A 1 241 ? 117.083 136.801 119.279 1.00 68.54 ?  241 GLY A CA    1 
ATOM   1937  C  C     . GLY A 1 241 ? 116.765 136.464 117.837 1.00 70.57 ?  241 GLY A C     1 
ATOM   1938  O  O     . GLY A 1 241 ? 115.846 135.678 117.578 1.00 71.99 ?  241 GLY A O     1 
ATOM   1939  N  N     . GLN A 1 242 ? 117.506 137.037 116.889 1.00 72.20 ?  242 GLN A N     1 
ATOM   1940  C  CA    . GLN A 1 242 ? 117.330 136.743 115.473 1.00 72.85 ?  242 GLN A CA    1 
ATOM   1941  C  C     . GLN A 1 242 ? 118.533 136.011 114.892 1.00 73.98 ?  242 GLN A C     1 
ATOM   1942  O  O     . GLN A 1 242 ? 118.380 134.943 114.294 1.00 74.28 ?  242 GLN A O     1 
ATOM   1943  C  CB    . GLN A 1 242 ? 117.060 138.039 114.695 1.00 72.37 ?  242 GLN A CB    1 
ATOM   1944  C  CG    . GLN A 1 242 ? 115.749 138.717 115.061 1.00 73.86 ?  242 GLN A CG    1 
ATOM   1945  C  CD    . GLN A 1 242 ? 115.305 139.726 114.022 1.00 75.01 ?  242 GLN A CD    1 
ATOM   1946  O  OE1   . GLN A 1 242 ? 115.870 139.801 112.931 1.00 75.76 ?  242 GLN A OE1   1 
ATOM   1947  N  NE2   . GLN A 1 242 ? 114.289 140.511 114.358 1.00 73.28 ?  242 GLN A NE2   1 
ATOM   1948  N  N     . ARG A 1 243 ? 119.734 136.560 115.058 1.00 64.01 ?  243 ARG A N     1 
ATOM   1949  C  CA    . ARG A 1 243 ? 120.962 135.925 114.609 1.00 63.58 ?  243 ARG A CA    1 
ATOM   1950  C  C     . ARG A 1 243 ? 121.889 135.723 115.800 1.00 62.97 ?  243 ARG A C     1 
ATOM   1951  O  O     . ARG A 1 243 ? 121.803 136.441 116.800 1.00 61.17 ?  243 ARG A O     1 
ATOM   1952  C  CB    . ARG A 1 243 ? 121.648 136.757 113.495 1.00 62.81 ?  243 ARG A CB    1 
ATOM   1953  C  CG    . ARG A 1 243 ? 122.137 138.170 113.877 1.00 63.98 ?  243 ARG A CG    1 
ATOM   1954  C  CD    . ARG A 1 243 ? 123.459 138.168 114.640 1.00 64.32 ?  243 ARG A CD    1 
ATOM   1955  N  NE    . ARG A 1 243 ? 123.892 139.500 115.044 1.00 65.06 ?  243 ARG A NE    1 
ATOM   1956  C  CZ    . ARG A 1 243 ? 124.835 140.200 114.430 1.00 64.23 ?  243 ARG A CZ    1 
ATOM   1957  N  NH1   . ARG A 1 243 ? 125.462 139.730 113.363 1.00 63.32 1  243 ARG A NH1   1 
ATOM   1958  N  NH2   . ARG A 1 243 ? 125.163 141.400 114.901 1.00 60.04 ?  243 ARG A NH2   1 
ATOM   1959  N  N     . GLN A 1 244 ? 122.778 134.740 115.687 1.00 64.35 ?  244 GLN A N     1 
ATOM   1960  C  CA    . GLN A 1 244 ? 123.744 134.487 116.747 1.00 62.85 ?  244 GLN A CA    1 
ATOM   1961  C  C     . GLN A 1 244 ? 124.760 135.621 116.811 1.00 62.96 ?  244 GLN A C     1 
ATOM   1962  O  O     . GLN A 1 244 ? 125.361 135.985 115.796 1.00 60.03 ?  244 GLN A O     1 
ATOM   1963  C  CB    . GLN A 1 244 ? 124.457 133.156 116.514 1.00 60.75 ?  244 GLN A CB    1 
ATOM   1964  C  CG    . GLN A 1 244 ? 123.633 131.932 116.875 1.00 62.26 ?  244 GLN A CG    1 
ATOM   1965  C  CD    . GLN A 1 244 ? 124.497 130.725 117.184 1.00 64.17 ?  244 GLN A CD    1 
ATOM   1966  O  OE1   . GLN A 1 244 ? 125.494 130.470 116.508 1.00 64.37 ?  244 GLN A OE1   1 
ATOM   1967  N  NE2   . GLN A 1 244 ? 124.120 129.975 118.213 1.00 61.33 ?  244 GLN A NE2   1 
ATOM   1968  N  N     . GLY A 1 245 ? 124.957 136.171 118.008 1.00 50.20 ?  245 GLY A N     1 
ATOM   1969  C  CA    . GLY A 1 245 ? 125.894 137.263 118.194 1.00 46.90 ?  245 GLY A CA    1 
ATOM   1970  C  C     . GLY A 1 245 ? 127.301 136.899 117.770 1.00 45.73 ?  245 GLY A C     1 
ATOM   1971  O  O     . GLY A 1 245 ? 127.883 135.940 118.282 1.00 43.83 ?  245 GLY A O     1 
ATOM   1972  N  N     . SER A 1 246 ? 127.857 137.664 116.836 1.00 40.73 ?  246 SER A N     1 
ATOM   1973  C  CA    . SER A 1 246 ? 129.142 137.358 116.224 1.00 32.62 ?  246 SER A CA    1 
ATOM   1974  C  C     . SER A 1 246 ? 130.166 138.397 116.656 1.00 31.43 ?  246 SER A C     1 
ATOM   1975  O  O     . SER A 1 246 ? 129.955 139.600 116.467 1.00 30.78 ?  246 SER A O     1 
ATOM   1976  C  CB    . SER A 1 246 ? 129.026 137.320 114.701 1.00 32.71 ?  246 SER A CB    1 
ATOM   1977  O  OG    . SER A 1 246 ? 128.184 136.262 114.279 1.00 44.32 ?  246 SER A OG    1 
ATOM   1978  N  N     . GLY A 1 247 ? 131.272 137.929 117.229 1.00 28.96 ?  247 GLY A N     1 
ATOM   1979  C  CA    . GLY A 1 247 ? 132.348 138.810 117.621 1.00 13.13 ?  247 GLY A CA    1 
ATOM   1980  C  C     . GLY A 1 247 ? 133.688 138.184 117.295 1.00 15.41 ?  247 GLY A C     1 
ATOM   1981  O  O     . GLY A 1 247 ? 133.817 136.966 117.156 1.00 23.68 ?  247 GLY A O     1 
ATOM   1982  N  N     . ALA A 1 248 ? 134.689 139.048 117.172 1.00 17.67 ?  248 ALA A N     1 
ATOM   1983  C  CA    . ALA A 1 248 ? 136.049 138.632 116.878 1.00 14.46 ?  248 ALA A CA    1 
ATOM   1984  C  C     . ALA A 1 248 ? 137.000 139.278 117.870 1.00 12.56 ?  248 ALA A C     1 
ATOM   1985  O  O     . ALA A 1 248 ? 136.792 140.411 118.308 1.00 16.39 ?  248 ALA A O     1 
ATOM   1986  C  CB    . ALA A 1 248 ? 136.459 139.000 115.445 1.00 8.12  ?  248 ALA A CB    1 
ATOM   1987  N  N     . ALA A 1 249 ? 138.048 138.542 118.223 1.00 16.30 ?  249 ALA A N     1 
ATOM   1988  C  CA    . ALA A 1 249 ? 139.106 139.037 119.091 1.00 5.45  ?  249 ALA A CA    1 
ATOM   1989  C  C     . ALA A 1 249 ? 140.438 138.852 118.384 1.00 11.13 ?  249 ALA A C     1 
ATOM   1990  O  O     . ALA A 1 249 ? 140.725 137.769 117.869 1.00 19.26 ?  249 ALA A O     1 
ATOM   1991  C  CB    . ALA A 1 249 ? 139.107 138.308 120.438 1.00 13.03 ?  249 ALA A CB    1 
ATOM   1992  N  N     . TYR A 1 250 ? 141.242 139.907 118.352 1.00 15.80 ?  250 TYR A N     1 
ATOM   1993  C  CA    . TYR A 1 250 ? 142.548 139.872 117.713 1.00 9.77  ?  250 TYR A CA    1 
ATOM   1994  C  C     . TYR A 1 250 ? 143.634 140.049 118.761 1.00 6.64  ?  250 TYR A C     1 
ATOM   1995  O  O     . TYR A 1 250 ? 143.542 140.935 119.616 1.00 17.12 ?  250 TYR A O     1 
ATOM   1996  C  CB    . TYR A 1 250 ? 142.665 140.952 116.640 1.00 10.64 ?  250 TYR A CB    1 
ATOM   1997  C  CG    . TYR A 1 250 ? 142.093 140.545 115.303 1.00 17.03 ?  250 TYR A CG    1 
ATOM   1998  C  CD1   . TYR A 1 250 ? 140.724 140.565 115.080 1.00 11.39 ?  250 TYR A CD1   1 
ATOM   1999  C  CD2   . TYR A 1 250 ? 142.920 140.135 114.267 1.00 13.62 ?  250 TYR A CD2   1 
ATOM   2000  C  CE1   . TYR A 1 250 ? 140.195 140.194 113.865 1.00 5.03  ?  250 TYR A CE1   1 
ATOM   2001  C  CE2   . TYR A 1 250 ? 142.398 139.759 113.047 1.00 9.66  ?  250 TYR A CE2   1 
ATOM   2002  C  CZ    . TYR A 1 250 ? 141.035 139.791 112.851 1.00 8.96  ?  250 TYR A CZ    1 
ATOM   2003  O  OH    . TYR A 1 250 ? 140.509 139.423 111.637 1.00 16.52 ?  250 TYR A OH    1 
ATOM   2004  N  N     . LEU A 1 251 ? 144.652 139.201 118.692 1.00 11.05 ?  251 LEU A N     1 
ATOM   2005  C  CA    . LEU A 1 251 ? 145.795 139.270 119.584 1.00 13.94 ?  251 LEU A CA    1 
ATOM   2006  C  C     . LEU A 1 251 ? 147.072 139.214 118.764 1.00 11.63 ?  251 LEU A C     1 
ATOM   2007  O  O     . LEU A 1 251 ? 147.172 138.439 117.810 1.00 16.73 ?  251 LEU A O     1 
ATOM   2008  C  CB    . LEU A 1 251 ? 145.783 138.128 120.602 1.00 17.48 ?  251 LEU A CB    1 
ATOM   2009  C  CG    . LEU A 1 251 ? 146.639 138.342 121.849 1.00 12.99 ?  251 LEU A CG    1 
ATOM   2010  C  CD1   . LEU A 1 251 ? 145.958 139.307 122.799 1.00 18.08 ?  251 LEU A CD1   1 
ATOM   2011  C  CD2   . LEU A 1 251 ? 146.925 137.021 122.535 1.00 13.39 ?  251 LEU A CD2   1 
ATOM   2012  N  N     . ASN A 1 252 ? 148.042 140.043 119.134 1.00 15.94 ?  252 ASN A N     1 
ATOM   2013  C  CA    . ASN A 1 252 ? 149.351 139.973 118.506 1.00 12.87 ?  252 ASN A CA    1 
ATOM   2014  C  C     . ASN A 1 252 ? 150.033 138.664 118.876 1.00 14.42 ?  252 ASN A C     1 
ATOM   2015  O  O     . ASN A 1 252 ? 149.895 138.167 119.997 1.00 25.53 ?  252 ASN A O     1 
ATOM   2016  C  CB    . ASN A 1 252 ? 150.210 141.162 118.928 1.00 15.10 ?  252 ASN A CB    1 
ATOM   2017  C  CG    . ASN A 1 252 ? 151.302 141.471 117.928 1.00 20.40 ?  252 ASN A CG    1 
ATOM   2018  O  OD1   . ASN A 1 252 ? 152.326 140.792 117.881 1.00 25.03 ?  252 ASN A OD1   1 
ATOM   2019  N  ND2   . ASN A 1 252 ? 151.082 142.493 117.112 1.00 17.33 ?  252 ASN A ND2   1 
ATOM   2020  N  N     . ILE A 1 253 ? 150.772 138.095 117.920 1.00 13.59 ?  253 ILE A N     1 
ATOM   2021  C  CA    . ILE A 1 253 ? 151.410 136.807 118.152 1.00 20.79 ?  253 ILE A CA    1 
ATOM   2022  C  C     . ILE A 1 253 ? 152.539 136.907 119.172 1.00 23.63 ?  253 ILE A C     1 
ATOM   2023  O  O     . ILE A 1 253 ? 152.960 135.884 119.722 1.00 25.79 ?  253 ILE A O     1 
ATOM   2024  C  CB    . ILE A 1 253 ? 151.913 136.213 116.822 1.00 19.47 ?  253 ILE A CB    1 
ATOM   2025  C  CG1   . ILE A 1 253 ? 152.027 134.692 116.929 1.00 23.14 ?  253 ILE A CG1   1 
ATOM   2026  C  CG2   . ILE A 1 253 ? 153.238 136.838 116.416 1.00 13.69 ?  253 ILE A CG2   1 
ATOM   2027  C  CD1   . ILE A 1 253 ? 151.842 133.970 115.622 1.00 21.73 ?  253 ILE A CD1   1 
ATOM   2028  N  N     . PHE A 1 254 ? 153.035 138.110 119.448 1.00 22.21 ?  254 PHE A N     1 
ATOM   2029  C  CA    . PHE A 1 254 ? 154.064 138.304 120.460 1.00 15.92 ?  254 PHE A CA    1 
ATOM   2030  C  C     . PHE A 1 254 ? 153.484 138.567 121.843 1.00 21.42 ?  254 PHE A C     1 
ATOM   2031  O  O     . PHE A 1 254 ? 154.245 138.656 122.813 1.00 29.46 ?  254 PHE A O     1 
ATOM   2032  C  CB    . PHE A 1 254 ? 154.996 139.448 120.047 1.00 22.92 ?  254 PHE A CB    1 
ATOM   2033  C  CG    . PHE A 1 254 ? 156.004 139.053 119.005 1.00 26.00 ?  254 PHE A CG    1 
ATOM   2034  C  CD1   . PHE A 1 254 ? 157.020 138.162 119.308 1.00 25.65 ?  254 PHE A CD1   1 
ATOM   2035  C  CD2   . PHE A 1 254 ? 155.924 139.554 117.718 1.00 23.77 ?  254 PHE A CD2   1 
ATOM   2036  C  CE1   . PHE A 1 254 ? 157.945 137.791 118.352 1.00 28.02 ?  254 PHE A CE1   1 
ATOM   2037  C  CE2   . PHE A 1 254 ? 156.845 139.184 116.756 1.00 26.10 ?  254 PHE A CE2   1 
ATOM   2038  C  CZ    . PHE A 1 254 ? 157.857 138.303 117.075 1.00 27.05 ?  254 PHE A CZ    1 
ATOM   2039  N  N     . HIS A 1 255 ? 152.166 138.705 121.952 1.00 26.58 ?  255 HIS A N     1 
ATOM   2040  C  CA    . HIS A 1 255 ? 151.514 138.694 123.254 1.00 17.25 ?  255 HIS A CA    1 
ATOM   2041  C  C     . HIS A 1 255 ? 151.708 137.328 123.898 1.00 19.54 ?  255 HIS A C     1 
ATOM   2042  O  O     . HIS A 1 255 ? 151.671 136.298 123.220 1.00 28.90 ?  255 HIS A O     1 
ATOM   2043  C  CB    . HIS A 1 255 ? 150.027 139.006 123.094 1.00 19.06 ?  255 HIS A CB    1 
ATOM   2044  C  CG    . HIS A 1 255 ? 149.333 139.366 124.371 1.00 23.16 ?  255 HIS A CG    1 
ATOM   2045  N  ND1   . HIS A 1 255 ? 149.064 138.447 125.361 1.00 21.46 ?  255 HIS A ND1   1 
ATOM   2046  C  CD2   . HIS A 1 255 ? 148.830 140.544 124.806 1.00 15.99 ?  255 HIS A CD2   1 
ATOM   2047  C  CE1   . HIS A 1 255 ? 148.439 139.047 126.358 1.00 16.84 ?  255 HIS A CE1   1 
ATOM   2048  N  NE2   . HIS A 1 255 ? 148.283 140.320 126.046 1.00 13.24 ?  255 HIS A NE2   1 
ATOM   2049  N  N     . ARG A 1 256 ? 151.925 137.316 125.214 1.00 21.55 ?  256 ARG A N     1 
ATOM   2050  C  CA    . ARG A 1 256 ? 152.263 136.059 125.871 1.00 21.81 ?  256 ARG A CA    1 
ATOM   2051  C  C     . ARG A 1 256 ? 151.073 135.110 125.897 1.00 27.23 ?  256 ARG A C     1 
ATOM   2052  O  O     . ARG A 1 256 ? 151.246 133.887 125.838 1.00 30.87 ?  256 ARG A O     1 
ATOM   2053  C  CB    . ARG A 1 256 ? 152.757 136.314 127.288 1.00 24.98 ?  256 ARG A CB    1 
ATOM   2054  C  CG    . ARG A 1 256 ? 153.417 135.100 127.896 1.00 29.78 ?  256 ARG A CG    1 
ATOM   2055  C  CD    . ARG A 1 256 ? 152.952 134.854 129.307 1.00 30.42 ?  256 ARG A CD    1 
ATOM   2056  N  NE    . ARG A 1 256 ? 151.503 134.931 129.440 1.00 29.67 ?  256 ARG A NE    1 
ATOM   2057  C  CZ    . ARG A 1 256 ? 150.731 133.882 129.686 1.00 31.62 ?  256 ARG A CZ    1 
ATOM   2058  N  NH1   . ARG A 1 256 ? 151.240 132.671 129.840 1.00 32.60 1  256 ARG A NH1   1 
ATOM   2059  N  NH2   . ARG A 1 256 ? 149.418 134.053 129.791 1.00 33.08 ?  256 ARG A NH2   1 
ATOM   2060  N  N     . ASP A 1 257 ? 149.861 135.649 125.979 1.00 22.54 ?  257 ASP A N     1 
ATOM   2061  C  CA    . ASP A 1 257 ? 148.639 134.848 126.008 1.00 19.25 ?  257 ASP A CA    1 
ATOM   2062  C  C     . ASP A 1 257 ? 148.341 134.168 124.693 1.00 24.96 ?  257 ASP A C     1 
ATOM   2063  O  O     . ASP A 1 257 ? 147.305 133.491 124.633 1.00 32.70 ?  257 ASP A O     1 
ATOM   2064  C  CB    . ASP A 1 257 ? 147.446 135.719 126.400 1.00 21.68 ?  257 ASP A CB    1 
ATOM   2065  C  CG    . ASP A 1 257 ? 147.413 136.042 127.876 1.00 30.64 ?  257 ASP A CG    1 
ATOM   2066  O  OD1   . ASP A 1 257 ? 148.052 135.314 128.661 1.00 28.10 ?  257 ASP A OD1   1 
ATOM   2067  O  OD2   . ASP A 1 257 ? 146.736 137.018 128.252 1.00 34.69 -1 257 ASP A OD2   1 
ATOM   2068  N  N     . ILE A 1 258 ? 149.212 134.308 123.690 1.00 26.12 ?  258 ILE A N     1 
ATOM   2069  C  CA    . ILE A 1 258 ? 148.882 133.874 122.335 1.00 25.64 ?  258 ILE A CA    1 
ATOM   2070  C  C     . ILE A 1 258 ? 148.520 132.394 122.315 1.00 23.84 ?  258 ILE A C     1 
ATOM   2071  O  O     . ILE A 1 258 ? 147.601 131.979 121.603 1.00 32.27 ?  258 ILE A O     1 
ATOM   2072  C  CB    . ILE A 1 258 ? 150.038 134.199 121.367 1.00 22.86 ?  258 ILE A CB    1 
ATOM   2073  C  CG1   . ILE A 1 258 ? 149.630 133.895 119.924 1.00 25.32 ?  258 ILE A CG1   1 
ATOM   2074  C  CG2   . ILE A 1 258 ? 151.314 133.457 121.750 1.00 19.03 ?  258 ILE A CG2   1 
ATOM   2075  C  CD1   . ILE A 1 258 ? 148.423 134.678 119.465 1.00 18.76 ?  258 ILE A CD1   1 
ATOM   2076  N  N     . ASN A 1 259 ? 149.222 131.578 123.104 1.00 23.42 ?  259 ASN A N     1 
ATOM   2077  C  CA    . ASN A 1 259 ? 148.877 130.163 123.173 1.00 23.87 ?  259 ASN A CA    1 
ATOM   2078  C  C     . ASN A 1 259 ? 147.510 129.969 123.816 1.00 27.63 ?  259 ASN A C     1 
ATOM   2079  O  O     . ASN A 1 259 ? 146.632 129.311 123.242 1.00 29.97 ?  259 ASN A O     1 
ATOM   2080  C  CB    . ASN A 1 259 ? 149.955 129.402 123.944 1.00 25.62 ?  259 ASN A CB    1 
ATOM   2081  C  CG    . ASN A 1 259 ? 151.225 129.221 123.138 1.00 30.57 ?  259 ASN A CG    1 
ATOM   2082  O  OD1   . ASN A 1 259 ? 151.247 128.496 122.144 1.00 31.68 ?  259 ASN A OD1   1 
ATOM   2083  N  ND2   . ASN A 1 259 ? 152.293 129.887 123.562 1.00 27.56 ?  259 ASN A ND2   1 
ATOM   2084  N  N     . ASP A 1 260 ? 147.294 130.579 124.984 1.00 26.94 ?  260 ASP A N     1 
ATOM   2085  C  CA    . ASP A 1 260 ? 146.005 130.452 125.658 1.00 26.40 ?  260 ASP A CA    1 
ATOM   2086  C  C     . ASP A 1 260 ? 144.888 131.010 124.788 1.00 21.16 ?  260 ASP A C     1 
ATOM   2087  O  O     . ASP A 1 260 ? 143.824 130.395 124.652 1.00 27.71 ?  260 ASP A O     1 
ATOM   2088  C  CB    . ASP A 1 260 ? 146.047 131.163 127.011 1.00 26.24 ?  260 ASP A CB    1 
ATOM   2089  C  CG    . ASP A 1 260 ? 147.318 130.876 127.783 1.00 36.42 ?  260 ASP A CG    1 
ATOM   2090  O  OD1   . ASP A 1 260 ? 147.775 131.768 128.529 1.00 35.80 ?  260 ASP A OD1   1 
ATOM   2091  O  OD2   . ASP A 1 260 ? 147.858 129.759 127.648 1.00 35.91 -1 260 ASP A OD2   1 
ATOM   2092  N  N     . PHE A 1 261 ? 145.124 132.179 124.189 1.00 26.31 ?  261 PHE A N     1 
ATOM   2093  C  CA    . PHE A 1 261 ? 144.282 132.705 123.123 1.00 23.74 ?  261 PHE A CA    1 
ATOM   2094  C  C     . PHE A 1 261 ? 143.917 131.608 122.130 1.00 20.08 ?  261 PHE A C     1 
ATOM   2095  O  O     . PHE A 1 261 ? 142.741 131.267 121.955 1.00 21.56 ?  261 PHE A O     1 
ATOM   2096  C  CB    . PHE A 1 261 ? 145.029 133.853 122.433 1.00 16.16 ?  261 PHE A CB    1 
ATOM   2097  C  CG    . PHE A 1 261 ? 144.218 134.600 121.415 1.00 22.45 ?  261 PHE A CG    1 
ATOM   2098  C  CD1   . PHE A 1 261 ? 143.288 135.544 121.807 1.00 18.74 ?  261 PHE A CD1   1 
ATOM   2099  C  CD2   . PHE A 1 261 ? 144.419 134.387 120.063 1.00 23.64 ?  261 PHE A CD2   1 
ATOM   2100  C  CE1   . PHE A 1 261 ? 142.552 136.241 120.872 1.00 13.75 ?  261 PHE A CE1   1 
ATOM   2101  C  CE2   . PHE A 1 261 ? 143.689 135.083 119.124 1.00 15.00 ?  261 PHE A CE2   1 
ATOM   2102  C  CZ    . PHE A 1 261 ? 142.755 136.012 119.529 1.00 18.00 ?  261 PHE A CZ    1 
ATOM   2103  N  N     . LEU A 1 262 ? 144.938 131.003 121.516 1.00 26.08 ?  262 LEU A N     1 
ATOM   2104  C  CA    . LEU A 1 262 ? 144.693 129.934 120.556 1.00 23.94 ?  262 LEU A CA    1 
ATOM   2105  C  C     . LEU A 1 262 ? 144.011 128.749 121.223 1.00 29.96 ?  262 LEU A C     1 
ATOM   2106  O  O     . LEU A 1 262 ? 143.151 128.094 120.620 1.00 28.96 ?  262 LEU A O     1 
ATOM   2107  C  CB    . LEU A 1 262 ? 146.008 129.507 119.906 1.00 23.93 ?  262 LEU A CB    1 
ATOM   2108  C  CG    . LEU A 1 262 ? 146.690 130.542 119.014 1.00 25.30 ?  262 LEU A CG    1 
ATOM   2109  C  CD1   . LEU A 1 262 ? 147.994 129.991 118.468 1.00 27.68 ?  262 LEU A CD1   1 
ATOM   2110  C  CD2   . LEU A 1 262 ? 145.769 130.976 117.890 1.00 23.46 ?  262 LEU A CD2   1 
ATOM   2111  N  N     . ASP A 1 263 ? 144.355 128.481 122.485 1.00 35.28 ?  263 ASP A N     1 
ATOM   2112  C  CA    . ASP A 1 263 ? 143.750 127.365 123.198 1.00 29.88 ?  263 ASP A CA    1 
ATOM   2113  C  C     . ASP A 1 263 ? 142.252 127.551 123.381 1.00 31.41 ?  263 ASP A C     1 
ATOM   2114  O  O     . ASP A 1 263 ? 141.556 126.584 123.706 1.00 39.37 ?  263 ASP A O     1 
ATOM   2115  C  CB    . ASP A 1 263 ? 144.422 127.181 124.559 1.00 33.59 ?  263 ASP A CB    1 
ATOM   2116  C  CG    . ASP A 1 263 ? 145.804 126.570 124.445 1.00 38.24 ?  263 ASP A CG    1 
ATOM   2117  O  OD1   . ASP A 1 263 ? 146.108 125.977 123.390 1.00 38.59 ?  263 ASP A OD1   1 
ATOM   2118  O  OD2   . ASP A 1 263 ? 146.584 126.680 125.414 1.00 38.50 -1 263 ASP A OD2   1 
ATOM   2119  N  N     . THR A 1 264 ? 141.739 128.767 123.182 1.00 34.25 ?  264 THR A N     1 
ATOM   2120  C  CA    . THR A 1 264 ? 140.300 128.969 123.270 1.00 32.61 ?  264 THR A CA    1 
ATOM   2121  C  C     . THR A 1 264 ? 139.551 128.312 122.119 1.00 37.29 ?  264 THR A C     1 
ATOM   2122  O  O     . THR A 1 264 ? 138.334 128.130 122.215 1.00 40.05 ?  264 THR A O     1 
ATOM   2123  C  CB    . THR A 1 264 ? 139.976 130.462 123.311 1.00 35.07 ?  264 THR A CB    1 
ATOM   2124  O  OG1   . THR A 1 264 ? 140.492 131.096 122.135 1.00 39.96 ?  264 THR A OG1   1 
ATOM   2125  C  CG2   . THR A 1 264 ? 140.592 131.103 124.544 1.00 31.28 ?  264 THR A CG2   1 
ATOM   2126  N  N     . LYS A 1 265 ? 140.242 127.950 121.037 1.00 36.99 ?  265 LYS A N     1 
ATOM   2127  C  CA    . LYS A 1 265 ? 139.596 127.337 119.884 1.00 36.97 ?  265 LYS A CA    1 
ATOM   2128  C  C     . LYS A 1 265 ? 139.848 125.842 119.769 1.00 39.83 ?  265 LYS A C     1 
ATOM   2129  O  O     . LYS A 1 265 ? 139.325 125.212 118.844 1.00 43.53 ?  265 LYS A O     1 
ATOM   2130  C  CB    . LYS A 1 265 ? 140.041 128.033 118.593 1.00 37.82 ?  265 LYS A CB    1 
ATOM   2131  C  CG    . LYS A 1 265 ? 139.298 129.320 118.305 1.00 37.62 ?  265 LYS A CG    1 
ATOM   2132  C  CD    . LYS A 1 265 ? 137.805 129.148 118.498 1.00 39.31 ?  265 LYS A CD    1 
ATOM   2133  C  CE    . LYS A 1 265 ? 137.070 130.456 118.285 1.00 36.10 ?  265 LYS A CE    1 
ATOM   2134  N  NZ    . LYS A 1 265 ? 135.645 130.359 118.699 1.00 37.78 1  265 LYS A NZ    1 
ATOM   2135  N  N     . LYS A 1 266 ? 140.628 125.256 120.672 1.00 45.49 ?  266 LYS A N     1 
ATOM   2136  C  CA    . LYS A 1 266 ? 140.840 123.817 120.636 1.00 46.34 ?  266 LYS A CA    1 
ATOM   2137  C  C     . LYS A 1 266 ? 139.594 123.082 121.115 1.00 50.98 ?  266 LYS A C     1 
ATOM   2138  O  O     . LYS A 1 266 ? 138.872 123.543 122.003 1.00 50.36 ?  266 LYS A O     1 
ATOM   2139  C  CB    . LYS A 1 266 ? 142.045 123.430 121.492 1.00 44.07 ?  266 LYS A CB    1 
ATOM   2140  C  CG    . LYS A 1 266 ? 143.379 123.642 120.798 1.00 47.04 ?  266 LYS A CG    1 
ATOM   2141  C  CD    . LYS A 1 266 ? 144.537 123.129 121.636 1.00 48.02 ?  266 LYS A CD    1 
ATOM   2142  C  CE    . LYS A 1 266 ? 145.835 123.150 120.843 1.00 48.71 ?  266 LYS A CE    1 
ATOM   2143  N  NZ    . LYS A 1 266 ? 147.025 122.930 121.709 1.00 47.04 1  266 LYS A NZ    1 
ATOM   2144  N  N     . ILE A 1 267 ? 139.338 121.925 120.500 1.00 57.94 ?  267 ILE A N     1 
ATOM   2145  C  CA    . ILE A 1 267 ? 138.183 121.120 120.886 1.00 59.55 ?  267 ILE A CA    1 
ATOM   2146  C  C     . ILE A 1 267 ? 138.371 120.555 122.288 1.00 59.12 ?  267 ILE A C     1 
ATOM   2147  O  O     . ILE A 1 267 ? 137.410 120.433 123.058 1.00 57.17 ?  267 ILE A O     1 
ATOM   2148  C  CB    . ILE A 1 267 ? 137.939 120.006 119.853 1.00 59.00 ?  267 ILE A CB    1 
ATOM   2149  C  CG1   . ILE A 1 267 ? 137.551 120.607 118.499 1.00 59.81 ?  267 ILE A CG1   1 
ATOM   2150  C  CG2   . ILE A 1 267 ? 136.863 119.052 120.347 1.00 57.14 ?  267 ILE A CG2   1 
ATOM   2151  C  CD1   . ILE A 1 267 ? 138.692 120.671 117.507 1.00 59.86 ?  267 ILE A CD1   1 
ATOM   2152  N  N     . SER A 1 268 ? 139.608 120.201 122.644 1.00 60.20 ?  268 SER A N     1 
ATOM   2153  C  CA    . SER A 1 268 ? 139.895 119.641 123.959 1.00 63.53 ?  268 SER A CA    1 
ATOM   2154  C  C     . SER A 1 268 ? 139.833 120.676 125.075 1.00 64.19 ?  268 SER A C     1 
ATOM   2155  O  O     . SER A 1 268 ? 139.926 120.297 126.248 1.00 63.68 ?  268 SER A O     1 
ATOM   2156  C  CB    . SER A 1 268 ? 141.274 118.977 123.953 1.00 63.60 ?  268 SER A CB    1 
ATOM   2157  O  OG    . SER A 1 268 ? 142.285 119.906 123.604 1.00 62.10 ?  268 SER A OG    1 
ATOM   2158  N  N     . ALA A 1 269 ? 139.689 121.957 124.745 1.00 66.10 ?  269 ALA A N     1 
ATOM   2159  C  CA    . ALA A 1 269 ? 139.646 122.997 125.763 1.00 65.74 ?  269 ALA A CA    1 
ATOM   2160  C  C     . ALA A 1 269 ? 138.432 122.822 126.668 1.00 66.79 ?  269 ALA A C     1 
ATOM   2161  O  O     . ALA A 1 269 ? 137.357 122.401 126.233 1.00 64.71 ?  269 ALA A O     1 
ATOM   2162  C  CB    . ALA A 1 269 ? 139.616 124.381 125.111 1.00 61.65 ?  269 ALA A CB    1 
ATOM   2163  N  N     . ASP A 1 270 ? 138.616 123.153 127.944 1.00 73.17 ?  270 ASP A N     1 
ATOM   2164  C  CA    . ASP A 1 270 ? 137.548 123.022 128.921 1.00 73.06 ?  270 ASP A CA    1 
ATOM   2165  C  C     . ASP A 1 270 ? 136.503 124.121 128.725 1.00 73.22 ?  270 ASP A C     1 
ATOM   2166  O  O     . ASP A 1 270 ? 136.667 125.043 127.921 1.00 73.93 ?  270 ASP A O     1 
ATOM   2167  C  CB    . ASP A 1 270 ? 138.111 123.071 130.340 1.00 73.27 ?  270 ASP A CB    1 
ATOM   2168  C  CG    . ASP A 1 270 ? 139.380 122.256 130.492 1.00 74.95 ?  270 ASP A CG    1 
ATOM   2169  O  OD1   . ASP A 1 270 ? 139.524 121.240 129.782 1.00 74.46 ?  270 ASP A OD1   1 
ATOM   2170  O  OD2   . ASP A 1 270 ? 140.234 122.633 131.323 1.00 73.37 -1 270 ASP A OD2   1 
ATOM   2171  N  N     . GLU A 1 271 ? 135.411 124.010 129.485 1.00 74.54 ?  271 GLU A N     1 
ATOM   2172  C  CA    . GLU A 1 271 ? 134.320 124.973 129.364 1.00 75.66 ?  271 GLU A CA    1 
ATOM   2173  C  C     . GLU A 1 271 ? 134.723 126.355 129.862 1.00 75.28 ?  271 GLU A C     1 
ATOM   2174  O  O     . GLU A 1 271 ? 134.174 127.361 129.400 1.00 74.37 ?  271 GLU A O     1 
ATOM   2175  C  CB    . GLU A 1 271 ? 133.092 124.472 130.123 1.00 74.59 ?  271 GLU A CB    1 
ATOM   2176  C  CG    . GLU A 1 271 ? 132.585 123.114 129.659 1.00 75.40 ?  271 GLU A CG    1 
ATOM   2177  C  CD    . GLU A 1 271 ? 132.510 123.001 128.148 1.00 76.58 ?  271 GLU A CD    1 
ATOM   2178  O  OE1   . GLU A 1 271 ? 131.917 123.897 127.509 1.00 75.75 ?  271 GLU A OE1   1 
ATOM   2179  O  OE2   . GLU A 1 271 ? 133.045 122.017 127.597 1.00 74.84 -1 271 GLU A OE2   1 
ATOM   2180  N  N     . ASP A 1 272 ? 135.669 126.428 130.795 1.00 69.39 ?  272 ASP A N     1 
ATOM   2181  C  CA    . ASP A 1 272 ? 136.156 127.703 131.304 1.00 70.33 ?  272 ASP A CA    1 
ATOM   2182  C  C     . ASP A 1 272 ? 137.279 128.284 130.455 1.00 70.67 ?  272 ASP A C     1 
ATOM   2183  O  O     . ASP A 1 272 ? 137.821 129.336 130.806 1.00 68.52 ?  272 ASP A O     1 
ATOM   2184  C  CB    . ASP A 1 272 ? 136.628 127.552 132.754 1.00 70.43 ?  272 ASP A CB    1 
ATOM   2185  C  CG    . ASP A 1 272 ? 137.849 126.662 132.883 1.00 71.48 ?  272 ASP A CG    1 
ATOM   2186  O  OD1   . ASP A 1 272 ? 138.057 125.800 132.005 1.00 70.47 ?  272 ASP A OD1   1 
ATOM   2187  O  OD2   . ASP A 1 272 ? 138.604 126.826 133.865 1.00 70.07 -1 272 ASP A OD2   1 
ATOM   2188  N  N     . VAL A 1 273 ? 137.646 127.620 129.357 1.00 65.21 ?  273 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 273 ? 138.700 128.083 128.468 1.00 64.67 ?  273 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 273 ? 138.166 128.409 127.079 1.00 62.53 ?  273 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 273 ? 138.550 129.422 126.482 1.00 65.25 ?  273 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 273 ? 139.843 127.048 128.379 1.00 66.28 ?  273 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 273 ? 140.805 127.393 127.252 1.00 63.57 ?  273 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 273 ? 140.578 126.955 129.706 1.00 64.79 ?  273 VAL A CG2   1 
ATOM   2195  N  N     . ARG A 1 274 ? 137.263 127.584 126.556 1.00 60.44 ?  274 ARG A N     1 
ATOM   2196  C  CA    . ARG A 1 274 ? 136.806 127.719 125.180 1.00 59.82 ?  274 ARG A CA    1 
ATOM   2197  C  C     . ARG A 1 274 ? 135.733 128.795 125.063 1.00 58.10 ?  274 ARG A C     1 
ATOM   2198  O  O     . ARG A 1 274 ? 134.806 128.854 125.877 1.00 58.12 ?  274 ARG A O     1 
ATOM   2199  C  CB    . ARG A 1 274 ? 136.264 126.381 124.674 1.00 59.95 ?  274 ARG A CB    1 
ATOM   2200  C  CG    . ARG A 1 274 ? 135.324 126.495 123.486 1.00 58.60 ?  274 ARG A CG    1 
ATOM   2201  C  CD    . ARG A 1 274 ? 135.333 125.229 122.644 1.00 58.80 ?  274 ARG A CD    1 
ATOM   2202  N  NE    . ARG A 1 274 ? 135.267 124.024 123.462 1.00 62.16 ?  274 ARG A NE    1 
ATOM   2203  C  CZ    . ARG A 1 274 ? 134.167 123.574 124.052 1.00 63.53 ?  274 ARG A CZ    1 
ATOM   2204  N  NH1   . ARG A 1 274 ? 133.010 124.207 123.931 1.00 62.50 1  274 ARG A NH1   1 
ATOM   2205  N  NH2   . ARG A 1 274 ? 134.227 122.461 124.776 1.00 63.03 ?  274 ARG A NH2   1 
ATOM   2206  N  N     . VAL A 1 275 ? 135.864 129.646 124.047 1.00 47.64 ?  275 VAL A N     1 
ATOM   2207  C  CA    . VAL A 1 275 ? 134.840 130.615 123.673 1.00 44.89 ?  275 VAL A CA    1 
ATOM   2208  C  C     . VAL A 1 275 ? 134.243 130.171 122.345 1.00 45.72 ?  275 VAL A C     1 
ATOM   2209  O  O     . VAL A 1 275 ? 134.976 129.902 121.386 1.00 47.61 ?  275 VAL A O     1 
ATOM   2210  C  CB    . VAL A 1 275 ? 135.413 132.042 123.587 1.00 44.54 ?  275 VAL A CB    1 
ATOM   2211  C  CG1   . VAL A 1 275 ? 135.660 132.596 124.980 1.00 42.69 ?  275 VAL A CG1   1 
ATOM   2212  C  CG2   . VAL A 1 275 ? 136.702 132.061 122.782 1.00 44.81 ?  275 VAL A CG2   1 
ATOM   2213  N  N     . LYS A 1 276 ? 132.916 130.077 122.292 1.00 46.73 ?  276 LYS A N     1 
ATOM   2214  C  CA    . LYS A 1 276 ? 132.242 129.474 121.149 1.00 47.97 ?  276 LYS A CA    1 
ATOM   2215  C  C     . LYS A 1 276 ? 131.731 130.483 120.131 1.00 47.05 ?  276 LYS A C     1 
ATOM   2216  O  O     . LYS A 1 276 ? 131.789 130.210 118.928 1.00 52.80 ?  276 LYS A O     1 
ATOM   2217  C  CB    . LYS A 1 276 ? 131.071 128.605 121.624 1.00 49.01 ?  276 LYS A CB    1 
ATOM   2218  C  CG    . LYS A 1 276 ? 130.130 129.300 122.597 1.00 52.48 ?  276 LYS A CG    1 
ATOM   2219  C  CD    . LYS A 1 276 ? 129.169 128.315 123.245 1.00 50.48 ?  276 LYS A CD    1 
ATOM   2220  C  CE    . LYS A 1 276 ? 129.897 127.080 123.755 1.00 49.46 ?  276 LYS A CE    1 
ATOM   2221  N  NZ    . LYS A 1 276 ? 130.969 127.429 124.729 1.00 48.12 1  276 LYS A NZ    1 
ATOM   2222  N  N     . THR A 1 277 ? 131.234 131.637 120.571 1.00 38.15 ?  277 THR A N     1 
ATOM   2223  C  CA    . THR A 1 277 ? 130.705 132.648 119.667 1.00 38.69 ?  277 THR A CA    1 
ATOM   2224  C  C     . THR A 1 277 ? 131.678 133.793 119.430 1.00 42.36 ?  277 THR A C     1 
ATOM   2225  O  O     . THR A 1 277 ? 131.280 134.828 118.887 1.00 41.83 ?  277 THR A O     1 
ATOM   2226  C  CB    . THR A 1 277 ? 129.377 133.191 120.197 1.00 41.43 ?  277 THR A CB    1 
ATOM   2227  O  OG1   . THR A 1 277 ? 129.625 134.096 121.281 1.00 35.00 ?  277 THR A OG1   1 
ATOM   2228  C  CG2   . THR A 1 277 ? 128.492 132.052 120.677 1.00 41.22 ?  277 THR A CG2   1 
ATOM   2229  N  N     . LEU A 1 278 ? 132.936 133.636 119.827 1.00 33.87 ?  278 LEU A N     1 
ATOM   2230  C  CA    . LEU A 1 278 ? 133.955 134.665 119.655 1.00 31.20 ?  278 LEU A CA    1 
ATOM   2231  C  C     . LEU A 1 278 ? 135.007 134.153 118.681 1.00 25.43 ?  278 LEU A C     1 
ATOM   2232  O  O     . LEU A 1 278 ? 135.811 133.283 119.029 1.00 34.43 ?  278 LEU A O     1 
ATOM   2233  C  CB    . LEU A 1 278 ? 134.589 135.035 120.994 1.00 28.77 ?  278 LEU A CB    1 
ATOM   2234  C  CG    . LEU A 1 278 ? 135.389 136.337 121.027 1.00 25.02 ?  278 LEU A CG    1 
ATOM   2235  C  CD1   . LEU A 1 278 ? 134.462 137.533 121.128 1.00 24.11 ?  278 LEU A CD1   1 
ATOM   2236  C  CD2   . LEU A 1 278 ? 136.379 136.326 122.177 1.00 31.95 ?  278 LEU A CD2   1 
ATOM   2237  N  N     . SER A 1 279 ? 134.996 134.689 117.465 1.00 26.11 ?  279 SER A N     1 
ATOM   2238  C  CA    . SER A 1 279 ? 136.061 134.406 116.517 1.00 21.19 ?  279 SER A CA    1 
ATOM   2239  C  C     . SER A 1 279 ? 137.374 134.992 117.020 1.00 20.60 ?  279 SER A C     1 
ATOM   2240  O  O     . SER A 1 279 ? 137.394 135.963 117.779 1.00 33.10 ?  279 SER A O     1 
ATOM   2241  C  CB    . SER A 1 279 ? 135.722 134.983 115.144 1.00 17.65 ?  279 SER A CB    1 
ATOM   2242  O  OG    . SER A 1 279 ? 134.648 134.280 114.546 1.00 25.68 ?  279 SER A OG    1 
ATOM   2243  N  N     . ILE A 1 280 ? 138.481 134.385 116.606 1.00 18.70 ?  280 ILE A N     1 
ATOM   2244  C  CA    . ILE A 1 280 ? 139.800 134.835 117.027 1.00 22.67 ?  280 ILE A CA    1 
ATOM   2245  C  C     . ILE A 1 280 ? 140.658 135.086 115.798 1.00 23.14 ?  280 ILE A C     1 
ATOM   2246  O  O     . ILE A 1 280 ? 140.568 134.360 114.802 1.00 26.18 ?  280 ILE A O     1 
ATOM   2247  C  CB    . ILE A 1 280 ? 140.486 133.831 117.979 1.00 17.83 ?  280 ILE A CB    1 
ATOM   2248  C  CG1   . ILE A 1 280 ? 140.729 132.490 117.291 1.00 23.84 ?  280 ILE A CG1   1 
ATOM   2249  C  CG2   . ILE A 1 280 ? 139.661 133.649 119.240 1.00 20.13 ?  280 ILE A CG2   1 
ATOM   2250  C  CD1   . ILE A 1 280 ? 141.893 131.721 117.879 1.00 18.96 ?  280 ILE A CD1   1 
ATOM   2251  N  N     . GLY A 1 281 ? 141.462 136.137 115.861 1.00 13.73 ?  281 GLY A N     1 
ATOM   2252  C  CA    . GLY A 1 281 ? 142.449 136.404 114.838 1.00 4.47  ?  281 GLY A CA    1 
ATOM   2253  C  C     . GLY A 1 281 ? 143.790 136.700 115.474 1.00 10.46 ?  281 GLY A C     1 
ATOM   2254  O  O     . GLY A 1 281 ? 143.872 137.239 116.576 1.00 18.34 ?  281 GLY A O     1 
ATOM   2255  N  N     . VAL A 1 282 ? 144.848 136.330 114.762 1.00 15.23 ?  282 VAL A N     1 
ATOM   2256  C  CA    . VAL A 1 282 ? 146.215 136.504 115.236 1.00 12.71 ?  282 VAL A CA    1 
ATOM   2257  C  C     . VAL A 1 282 ? 146.928 137.473 114.307 1.00 13.55 ?  282 VAL A C     1 
ATOM   2258  O  O     . VAL A 1 282 ? 146.881 137.319 113.080 1.00 17.64 ?  282 VAL A O     1 
ATOM   2259  C  CB    . VAL A 1 282 ? 146.961 135.160 115.317 1.00 14.51 ?  282 VAL A CB    1 
ATOM   2260  C  CG1   . VAL A 1 282 ? 148.446 135.387 115.520 1.00 19.00 ?  282 VAL A CG1   1 
ATOM   2261  C  CG2   . VAL A 1 282 ? 146.402 134.328 116.452 1.00 19.47 ?  282 VAL A CG2   1 
ATOM   2262  N  N     . VAL A 1 283 ? 147.573 138.476 114.892 1.00 12.13 ?  283 VAL A N     1 
ATOM   2263  C  CA    . VAL A 1 283 ? 148.364 139.444 114.144 1.00 11.66 ?  283 VAL A CA    1 
ATOM   2264  C  C     . VAL A 1 283 ? 149.816 138.990 114.174 1.00 16.58 ?  283 VAL A C     1 
ATOM   2265  O  O     . VAL A 1 283 ? 150.407 138.841 115.248 1.00 25.42 ?  283 VAL A O     1 
ATOM   2266  C  CB    . VAL A 1 283 ? 148.211 140.854 114.733 1.00 11.36 ?  283 VAL A CB    1 
ATOM   2267  C  CG1   . VAL A 1 283 ? 148.850 141.879 113.820 1.00 9.15  ?  283 VAL A CG1   1 
ATOM   2268  C  CG2   . VAL A 1 283 ? 146.741 141.167 114.953 1.00 14.54 ?  283 VAL A CG2   1 
ATOM   2269  N  N     . ILE A 1 284 ? 150.391 138.770 113.000 1.00 14.52 ?  284 ILE A N     1 
ATOM   2270  C  CA    . ILE A 1 284 ? 151.726 138.208 112.861 1.00 14.52 ?  284 ILE A CA    1 
ATOM   2271  C  C     . ILE A 1 284 ? 152.628 139.254 112.220 1.00 18.20 ?  284 ILE A C     1 
ATOM   2272  O  O     . ILE A 1 284 ? 152.574 139.479 111.011 1.00 20.15 ?  284 ILE A O     1 
ATOM   2273  C  CB    . ILE A 1 284 ? 151.709 136.910 112.035 1.00 16.43 ?  284 ILE A CB    1 
ATOM   2274  C  CG1   . ILE A 1 284 ? 150.779 135.882 112.683 1.00 16.93 ?  284 ILE A CG1   1 
ATOM   2275  C  CG2   . ILE A 1 284 ? 153.113 136.347 111.895 1.00 17.23 ?  284 ILE A CG2   1 
ATOM   2276  C  CD1   . ILE A 1 284 ? 150.819 134.523 112.025 1.00 19.37 ?  284 ILE A CD1   1 
ATOM   2277  N  N     . PRO A 1 285 ? 153.471 139.921 113.004 1.00 27.08 ?  285 PRO A N     1 
ATOM   2278  C  CA    . PRO A 1 285 ? 154.456 140.836 112.420 1.00 25.81 ?  285 PRO A CA    1 
ATOM   2279  C  C     . PRO A 1 285 ? 155.522 140.075 111.646 1.00 23.52 ?  285 PRO A C     1 
ATOM   2280  O  O     . PRO A 1 285 ? 155.683 138.860 111.778 1.00 25.24 ?  285 PRO A O     1 
ATOM   2281  C  CB    . PRO A 1 285 ? 155.055 141.547 113.639 1.00 19.49 ?  285 PRO A CB    1 
ATOM   2282  C  CG    . PRO A 1 285 ? 154.088 141.301 114.754 1.00 17.59 ?  285 PRO A CG    1 
ATOM   2283  C  CD    . PRO A 1 285 ? 153.484 139.965 114.474 1.00 21.54 ?  285 PRO A CD    1 
ATOM   2284  N  N     . ASP A 1 286 ? 156.255 140.820 110.814 1.00 26.51 ?  286 ASP A N     1 
ATOM   2285  C  CA    . ASP A 1 286 ? 157.325 140.211 110.030 1.00 24.40 ?  286 ASP A CA    1 
ATOM   2286  C  C     . ASP A 1 286 ? 158.407 139.616 110.919 1.00 29.80 ?  286 ASP A C     1 
ATOM   2287  O  O     . ASP A 1 286 ? 159.107 138.687 110.502 1.00 32.08 ?  286 ASP A O     1 
ATOM   2288  C  CB    . ASP A 1 286 ? 157.937 141.238 109.078 1.00 24.91 ?  286 ASP A CB    1 
ATOM   2289  C  CG    . ASP A 1 286 ? 157.364 141.150 107.681 1.00 36.92 ?  286 ASP A CG    1 
ATOM   2290  O  OD1   . ASP A 1 286 ? 156.312 140.502 107.510 1.00 36.04 ?  286 ASP A OD1   1 
ATOM   2291  O  OD2   . ASP A 1 286 ? 157.964 141.733 106.753 1.00 39.10 -1 286 ASP A OD2   1 
ATOM   2292  N  N     . LYS A 1 287 ? 158.566 140.138 112.138 1.00 30.46 ?  287 LYS A N     1 
ATOM   2293  C  CA    . LYS A 1 287 ? 159.591 139.620 113.037 1.00 28.00 ?  287 LYS A CA    1 
ATOM   2294  C  C     . LYS A 1 287 ? 159.327 138.164 113.397 1.00 29.31 ?  287 LYS A C     1 
ATOM   2295  O  O     . LYS A 1 287 ? 160.261 137.356 113.465 1.00 36.10 ?  287 LYS A O     1 
ATOM   2296  C  CB    . LYS A 1 287 ? 159.667 140.479 114.299 1.00 31.50 ?  287 LYS A CB    1 
ATOM   2297  C  CG    . LYS A 1 287 ? 160.878 140.185 115.164 1.00 27.46 ?  287 LYS A CG    1 
ATOM   2298  C  CD    . LYS A 1 287 ? 162.147 140.176 114.330 1.00 30.56 ?  287 LYS A CD    1 
ATOM   2299  C  CE    . LYS A 1 287 ? 163.385 140.085 115.200 1.00 31.46 ?  287 LYS A CE    1 
ATOM   2300  N  NZ    . LYS A 1 287 ? 164.633 140.189 114.396 1.00 34.93 1  287 LYS A NZ    1 
ATOM   2301  N  N     . PHE A 1 288 ? 158.063 137.809 113.635 1.00 24.06 ?  288 PHE A N     1 
ATOM   2302  C  CA    . PHE A 1 288 ? 157.733 136.419 113.937 1.00 24.02 ?  288 PHE A CA    1 
ATOM   2303  C  C     . PHE A 1 288 ? 158.056 135.509 112.760 1.00 24.75 ?  288 PHE A C     1 
ATOM   2304  O  O     . PHE A 1 288 ? 158.569 134.398 112.944 1.00 36.24 ?  288 PHE A O     1 
ATOM   2305  C  CB    . PHE A 1 288 ? 156.258 136.299 114.319 1.00 25.06 ?  288 PHE A CB    1 
ATOM   2306  C  CG    . PHE A 1 288 ? 155.849 134.911 114.721 1.00 26.56 ?  288 PHE A CG    1 
ATOM   2307  C  CD1   . PHE A 1 288 ? 156.059 134.461 116.013 1.00 27.58 ?  288 PHE A CD1   1 
ATOM   2308  C  CD2   . PHE A 1 288 ? 155.255 134.057 113.807 1.00 22.72 ?  288 PHE A CD2   1 
ATOM   2309  C  CE1   . PHE A 1 288 ? 155.686 133.185 116.385 1.00 26.22 ?  288 PHE A CE1   1 
ATOM   2310  C  CE2   . PHE A 1 288 ? 154.880 132.781 114.174 1.00 24.98 ?  288 PHE A CE2   1 
ATOM   2311  C  CZ    . PHE A 1 288 ? 155.095 132.344 115.465 1.00 29.33 ?  288 PHE A CZ    1 
ATOM   2312  N  N     . VAL A 1 289 ? 157.761 135.962 111.540 1.00 24.93 ?  289 VAL A N     1 
ATOM   2313  C  CA    . VAL A 1 289 ? 158.046 135.152 110.362 1.00 28.22 ?  289 VAL A CA    1 
ATOM   2314  C  C     . VAL A 1 289 ? 159.549 135.000 110.169 1.00 29.88 ?  289 VAL A C     1 
ATOM   2315  O  O     . VAL A 1 289 ? 160.031 133.935 109.772 1.00 33.12 ?  289 VAL A O     1 
ATOM   2316  C  CB    . VAL A 1 289 ? 157.369 135.757 109.120 1.00 31.83 ?  289 VAL A CB    1 
ATOM   2317  C  CG1   . VAL A 1 289 ? 157.431 134.785 107.954 1.00 25.97 ?  289 VAL A CG1   1 
ATOM   2318  C  CG2   . VAL A 1 289 ? 155.929 136.132 109.432 1.00 26.24 ?  289 VAL A CG2   1 
ATOM   2319  N  N     . GLU A 1 290 ? 160.314 136.061 110.443 1.00 33.29 ?  290 GLU A N     1 
ATOM   2320  C  CA    . GLU A 1 290 ? 161.769 135.963 110.359 1.00 32.38 ?  290 GLU A CA    1 
ATOM   2321  C  C     . GLU A 1 290 ? 162.317 134.996 111.400 1.00 35.00 ?  290 GLU A C     1 
ATOM   2322  O  O     . GLU A 1 290 ? 163.227 134.211 111.110 1.00 41.47 ?  290 GLU A O     1 
ATOM   2323  C  CB    . GLU A 1 290 ? 162.405 137.343 110.524 1.00 33.41 ?  290 GLU A CB    1 
ATOM   2324  C  CG    . GLU A 1 290 ? 162.379 138.203 109.272 1.00 38.34 ?  290 GLU A CG    1 
ATOM   2325  C  CD    . GLU A 1 290 ? 161.789 139.577 109.515 1.00 39.81 ?  290 GLU A CD    1 
ATOM   2326  O  OE1   . GLU A 1 290 ? 161.026 140.059 108.652 1.00 38.86 ?  290 GLU A OE1   1 
ATOM   2327  O  OE2   . GLU A 1 290 ? 162.086 140.176 110.570 1.00 40.07 -1 290 GLU A OE2   1 
ATOM   2328  N  N     . LEU A 1 291 ? 161.783 135.045 112.622 1.00 32.62 ?  291 LEU A N     1 
ATOM   2329  C  CA    . LEU A 1 291 ? 162.241 134.138 113.669 1.00 29.33 ?  291 LEU A CA    1 
ATOM   2330  C  C     . LEU A 1 291 ? 161.918 132.689 113.328 1.00 32.32 ?  291 LEU A C     1 
ATOM   2331  O  O     . LEU A 1 291 ? 162.748 131.797 113.540 1.00 39.75 ?  291 LEU A O     1 
ATOM   2332  C  CB    . LEU A 1 291 ? 161.617 134.527 115.010 1.00 31.03 ?  291 LEU A CB    1 
ATOM   2333  C  CG    . LEU A 1 291 ? 162.101 135.845 115.613 1.00 32.77 ?  291 LEU A CG    1 
ATOM   2334  C  CD1   . LEU A 1 291 ? 161.104 136.367 116.632 1.00 27.11 ?  291 LEU A CD1   1 
ATOM   2335  C  CD2   . LEU A 1 291 ? 163.475 135.676 116.235 1.00 32.96 ?  291 LEU A CD2   1 
ATOM   2336  N  N     . ALA A 1 292 ? 160.717 132.434 112.806 1.00 33.22 ?  292 ALA A N     1 
ATOM   2337  C  CA    . ALA A 1 292 ? 160.360 131.077 112.404 1.00 31.63 ?  292 ALA A CA    1 
ATOM   2338  C  C     . ALA A 1 292 ? 161.208 130.607 111.228 1.00 32.39 ?  292 ALA A C     1 
ATOM   2339  O  O     . ALA A 1 292 ? 161.609 129.439 111.171 1.00 37.80 ?  292 ALA A O     1 
ATOM   2340  C  CB    . ALA A 1 292 ? 158.874 131.006 112.059 1.00 30.62 ?  292 ALA A CB    1 
ATOM   2341  N  N     . ARG A 1 293 ? 161.486 131.504 110.280 1.00 34.05 ?  293 ARG A N     1 
ATOM   2342  C  CA    . ARG A 1 293 ? 162.273 131.142 109.105 1.00 33.45 ?  293 ARG A CA    1 
ATOM   2343  C  C     . ARG A 1 293 ? 163.688 130.732 109.486 1.00 39.26 ?  293 ARG A C     1 
ATOM   2344  O  O     . ARG A 1 293 ? 164.222 129.750 108.956 1.00 43.88 ?  293 ARG A O     1 
ATOM   2345  C  CB    . ARG A 1 293 ? 162.294 132.314 108.124 1.00 34.13 ?  293 ARG A CB    1 
ATOM   2346  C  CG    . ARG A 1 293 ? 163.142 132.096 106.887 1.00 34.36 ?  293 ARG A CG    1 
ATOM   2347  C  CD    . ARG A 1 293 ? 163.304 133.395 106.118 1.00 38.71 ?  293 ARG A CD    1 
ATOM   2348  N  NE    . ARG A 1 293 ? 162.045 134.123 106.030 1.00 40.23 ?  293 ARG A NE    1 
ATOM   2349  C  CZ    . ARG A 1 293 ? 161.905 135.413 106.305 1.00 39.33 ?  293 ARG A CZ    1 
ATOM   2350  N  NH1   . ARG A 1 293 ? 162.935 136.157 106.675 1.00 37.97 1  293 ARG A NH1   1 
ATOM   2351  N  NH2   . ARG A 1 293 ? 160.701 135.970 106.207 1.00 35.71 ?  293 ARG A NH2   1 
ATOM   2352  N  N     . GLU A 1 294 ? 164.312 131.468 110.401 1.00 41.45 ?  294 GLU A N     1 
ATOM   2353  C  CA    . GLU A 1 294 ? 165.664 131.160 110.847 1.00 39.06 ?  294 GLU A CA    1 
ATOM   2354  C  C     . GLU A 1 294 ? 165.696 130.130 111.967 1.00 40.16 ?  294 GLU A C     1 
ATOM   2355  O  O     . GLU A 1 294 ? 166.787 129.787 112.437 1.00 42.64 ?  294 GLU A O     1 
ATOM   2356  C  CB    . GLU A 1 294 ? 166.368 132.440 111.304 1.00 39.21 ?  294 GLU A CB    1 
ATOM   2357  C  CG    . GLU A 1 294 ? 166.811 133.344 110.167 1.00 41.33 ?  294 GLU A CG    1 
ATOM   2358  C  CD    . GLU A 1 294 ? 166.273 134.753 110.304 1.00 44.89 ?  294 GLU A CD    1 
ATOM   2359  O  OE1   . GLU A 1 294 ? 166.108 135.220 111.451 1.00 45.92 ?  294 GLU A OE1   1 
ATOM   2360  O  OE2   . GLU A 1 294 ? 166.014 135.396 109.265 1.00 46.51 -1 294 GLU A OE2   1 
ATOM   2361  N  N     . ASP A 1 295 ? 164.535 129.650 112.410 1.00 38.72 ?  295 ASP A N     1 
ATOM   2362  C  CA    . ASP A 1 295 ? 164.384 128.661 113.474 1.00 37.97 ?  295 ASP A CA    1 
ATOM   2363  C  C     . ASP A 1 295 ? 164.891 129.155 114.823 1.00 44.50 ?  295 ASP A C     1 
ATOM   2364  O  O     . ASP A 1 295 ? 165.005 128.361 115.763 1.00 44.19 ?  295 ASP A O     1 
ATOM   2365  C  CB    . ASP A 1 295 ? 165.070 127.334 113.117 1.00 40.78 ?  295 ASP A CB    1 
ATOM   2366  C  CG    . ASP A 1 295 ? 164.232 126.127 113.488 1.00 44.89 ?  295 ASP A CG    1 
ATOM   2367  O  OD1   . ASP A 1 295 ? 163.268 126.287 114.265 1.00 46.03 ?  295 ASP A OD1   1 
ATOM   2368  O  OD2   . ASP A 1 295 ? 164.539 125.018 113.004 1.00 42.65 -1 295 ASP A OD2   1 
ATOM   2369  N  N     . LYS A 1 296 ? 165.201 130.444 114.946 1.00 43.47 ?  296 LYS A N     1 
ATOM   2370  C  CA    . LYS A 1 296 ? 165.570 130.998 116.240 1.00 41.60 ?  296 LYS A CA    1 
ATOM   2371  C  C     . LYS A 1 296 ? 164.367 130.994 117.171 1.00 41.53 ?  296 LYS A C     1 
ATOM   2372  O  O     . LYS A 1 296 ? 163.244 131.295 116.759 1.00 45.89 ?  296 LYS A O     1 
ATOM   2373  C  CB    . LYS A 1 296 ? 166.104 132.422 116.087 1.00 42.27 ?  296 LYS A CB    1 
ATOM   2374  C  CG    . LYS A 1 296 ? 167.191 132.584 115.043 1.00 44.14 ?  296 LYS A CG    1 
ATOM   2375  C  CD    . LYS A 1 296 ? 167.158 133.979 114.441 1.00 42.91 ?  296 LYS A CD    1 
ATOM   2376  C  CE    . LYS A 1 296 ? 168.554 134.561 114.319 1.00 43.56 ?  296 LYS A CE    1 
ATOM   2377  N  NZ    . LYS A 1 296 ? 169.409 133.766 113.396 1.00 44.16 1  296 LYS A NZ    1 
ATOM   2378  N  N     . ALA A 1 297 ? 164.604 130.645 118.431 1.00 40.88 ?  297 ALA A N     1 
ATOM   2379  C  CA    . ALA A 1 297 ? 163.532 130.662 119.415 1.00 42.43 ?  297 ALA A CA    1 
ATOM   2380  C  C     . ALA A 1 297 ? 163.064 132.090 119.660 1.00 40.42 ?  297 ALA A C     1 
ATOM   2381  O  O     . ALA A 1 297 ? 163.872 133.009 119.814 1.00 41.09 ?  297 ALA A O     1 
ATOM   2382  C  CB    . ALA A 1 297 ? 164.000 130.027 120.721 1.00 37.53 ?  297 ALA A CB    1 
ATOM   2383  N  N     . ALA A 1 298 ? 161.748 132.272 119.695 1.00 35.05 ?  298 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 298 ? 161.154 133.588 119.843 1.00 34.96 ?  298 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 298 ? 160.766 133.827 121.298 1.00 35.60 ?  298 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 298 ? 160.830 132.935 122.146 1.00 39.04 ?  298 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 298 ? 159.944 133.735 118.919 1.00 33.74 ?  298 ALA A CB    1 
ATOM   2388  N  N     . TYR A 1 299 ? 160.347 135.055 121.585 1.00 33.59 ?  299 TYR A N     1 
ATOM   2389  C  CA    . TYR A 1 299 ? 159.907 135.435 122.919 1.00 27.91 ?  299 TYR A CA    1 
ATOM   2390  C  C     . TYR A 1 299 ? 158.536 136.082 122.823 1.00 29.08 ?  299 TYR A C     1 
ATOM   2391  O  O     . TYR A 1 299 ? 158.324 136.976 121.999 1.00 30.35 ?  299 TYR A O     1 
ATOM   2392  C  CB    . TYR A 1 299 ? 160.901 136.397 123.577 1.00 29.77 ?  299 TYR A CB    1 
ATOM   2393  C  CG    . TYR A 1 299 ? 162.168 135.729 124.055 1.00 31.98 ?  299 TYR A CG    1 
ATOM   2394  C  CD1   . TYR A 1 299 ? 162.206 135.057 125.270 1.00 34.99 ?  299 TYR A CD1   1 
ATOM   2395  C  CD2   . TYR A 1 299 ? 163.324 135.765 123.289 1.00 32.52 ?  299 TYR A CD2   1 
ATOM   2396  C  CE1   . TYR A 1 299 ? 163.363 134.443 125.708 1.00 35.03 ?  299 TYR A CE1   1 
ATOM   2397  C  CE2   . TYR A 1 299 ? 164.484 135.155 123.718 1.00 33.28 ?  299 TYR A CE2   1 
ATOM   2398  C  CZ    . TYR A 1 299 ? 164.498 134.495 124.928 1.00 35.74 ?  299 TYR A CZ    1 
ATOM   2399  O  OH    . TYR A 1 299 ? 165.653 133.885 125.361 1.00 39.40 ?  299 TYR A OH    1 
ATOM   2400  N  N     . VAL A 1 300 ? 157.611 135.624 123.659 1.00 32.74 ?  300 VAL A N     1 
ATOM   2401  C  CA    . VAL A 1 300 ? 156.311 136.265 123.818 1.00 27.48 ?  300 VAL A CA    1 
ATOM   2402  C  C     . VAL A 1 300 ? 156.377 137.138 125.061 1.00 28.99 ?  300 VAL A C     1 
ATOM   2403  O  O     . VAL A 1 300 ? 156.792 136.678 126.131 1.00 35.40 ?  300 VAL A O     1 
ATOM   2404  C  CB    . VAL A 1 300 ? 155.177 135.230 123.914 1.00 25.59 ?  300 VAL A CB    1 
ATOM   2405  C  CG1   . VAL A 1 300 ? 154.818 134.710 122.531 1.00 26.29 ?  300 VAL A CG1   1 
ATOM   2406  C  CG2   . VAL A 1 300 ? 155.565 134.086 124.836 1.00 28.34 ?  300 VAL A CG2   1 
ATOM   2407  N  N     . PHE A 1 301 ? 155.988 138.398 124.922 1.00 22.22 ?  301 PHE A N     1 
ATOM   2408  C  CA    . PHE A 1 301 ? 156.245 139.398 125.946 1.00 24.64 ?  301 PHE A CA    1 
ATOM   2409  C  C     . PHE A 1 301 ? 155.003 139.703 126.772 1.00 29.79 ?  301 PHE A C     1 
ATOM   2410  O  O     . PHE A 1 301 ? 153.869 139.582 126.303 1.00 32.59 ?  301 PHE A O     1 
ATOM   2411  C  CB    . PHE A 1 301 ? 156.775 140.685 125.314 1.00 23.17 ?  301 PHE A CB    1 
ATOM   2412  C  CG    . PHE A 1 301 ? 157.957 140.471 124.419 1.00 28.71 ?  301 PHE A CG    1 
ATOM   2413  C  CD1   . PHE A 1 301 ? 159.221 140.319 124.959 1.00 27.45 ?  301 PHE A CD1   1 
ATOM   2414  C  CD2   . PHE A 1 301 ? 157.807 140.404 123.045 1.00 27.89 ?  301 PHE A CD2   1 
ATOM   2415  C  CE1   . PHE A 1 301 ? 160.315 140.113 124.149 1.00 27.89 ?  301 PHE A CE1   1 
ATOM   2416  C  CE2   . PHE A 1 301 ? 158.900 140.199 122.229 1.00 26.73 ?  301 PHE A CE2   1 
ATOM   2417  C  CZ    . PHE A 1 301 ? 160.157 140.053 122.784 1.00 29.84 ?  301 PHE A CZ    1 
ATOM   2418  N  N     . TYR A 1 302 ? 155.241 140.092 128.022 1.00 27.90 ?  302 TYR A N     1 
ATOM   2419  C  CA    . TYR A 1 302 ? 154.193 140.596 128.895 1.00 24.69 ?  302 TYR A CA    1 
ATOM   2420  C  C     . TYR A 1 302 ? 153.952 142.061 128.562 1.00 28.70 ?  302 TYR A C     1 
ATOM   2421  O  O     . TYR A 1 302 ? 154.848 142.897 128.737 1.00 30.11 ?  302 TYR A O     1 
ATOM   2422  C  CB    . TYR A 1 302 ? 154.576 140.426 130.364 1.00 25.69 ?  302 TYR A CB    1 
ATOM   2423  C  CG    . TYR A 1 302 ? 154.539 138.997 130.852 1.00 28.28 ?  302 TYR A CG    1 
ATOM   2424  C  CD1   . TYR A 1 302 ? 155.502 138.080 130.457 1.00 27.90 ?  302 TYR A CD1   1 
ATOM   2425  C  CD2   . TYR A 1 302 ? 153.538 138.566 131.709 1.00 29.97 ?  302 TYR A CD2   1 
ATOM   2426  C  CE1   . TYR A 1 302 ? 155.468 136.775 130.904 1.00 26.48 ?  302 TYR A CE1   1 
ATOM   2427  C  CE2   . TYR A 1 302 ? 153.496 137.265 132.163 1.00 30.24 ?  302 TYR A CE2   1 
ATOM   2428  C  CZ    . TYR A 1 302 ? 154.465 136.374 131.762 1.00 33.79 ?  302 TYR A CZ    1 
ATOM   2429  O  OH    . TYR A 1 302 ? 154.423 135.074 132.208 1.00 34.01 ?  302 TYR A OH    1 
ATOM   2430  N  N     . PRO A 1 303 ? 152.764 142.404 128.062 1.00 24.50 ?  303 PRO A N     1 
ATOM   2431  C  CA    . PRO A 1 303 ? 152.536 143.778 127.583 1.00 21.46 ?  303 PRO A CA    1 
ATOM   2432  C  C     . PRO A 1 303 ? 152.677 144.843 128.653 1.00 28.11 ?  303 PRO A C     1 
ATOM   2433  O  O     . PRO A 1 303 ? 153.149 145.946 128.352 1.00 32.36 ?  303 PRO A O     1 
ATOM   2434  C  CB    . PRO A 1 303 ? 151.102 143.718 127.041 1.00 24.61 ?  303 PRO A CB    1 
ATOM   2435  C  CG    . PRO A 1 303 ? 150.863 142.278 126.762 1.00 26.14 ?  303 PRO A CG    1 
ATOM   2436  C  CD    . PRO A 1 303 ? 151.605 141.534 127.816 1.00 25.81 ?  303 PRO A CD    1 
ATOM   2437  N  N     . HIS A 1 304 ? 152.282 144.554 129.895 1.00 29.80 ?  304 HIS A N     1 
ATOM   2438  C  CA    . HIS A 1 304 ? 152.311 145.585 130.924 1.00 24.97 ?  304 HIS A CA    1 
ATOM   2439  C  C     . HIS A 1 304 ? 153.736 145.945 131.318 1.00 28.58 ?  304 HIS A C     1 
ATOM   2440  O  O     . HIS A 1 304 ? 154.014 147.107 131.622 1.00 36.19 ?  304 HIS A O     1 
ATOM   2441  C  CB    . HIS A 1 304 ? 151.518 145.140 132.151 1.00 28.66 ?  304 HIS A CB    1 
ATOM   2442  C  CG    . HIS A 1 304 ? 151.314 146.225 133.160 1.00 30.65 ?  304 HIS A CG    1 
ATOM   2443  N  ND1   . HIS A 1 304 ? 151.500 146.031 134.512 1.00 33.01 ?  304 HIS A ND1   1 
ATOM   2444  C  CD2   . HIS A 1 304 ? 150.943 147.520 133.014 1.00 29.10 ?  304 HIS A CD2   1 
ATOM   2445  C  CE1   . HIS A 1 304 ? 151.249 147.158 135.155 1.00 32.39 ?  304 HIS A CE1   1 
ATOM   2446  N  NE2   . HIS A 1 304 ? 150.910 148.077 134.269 1.00 30.65 ?  304 HIS A NE2   1 
ATOM   2447  N  N     . THR A 1 305 ? 154.647 144.968 131.326 1.00 29.10 ?  305 THR A N     1 
ATOM   2448  C  CA    . THR A 1 305 ? 156.046 145.274 131.608 1.00 32.57 ?  305 THR A CA    1 
ATOM   2449  C  C     . THR A 1 305 ? 156.640 146.167 130.524 1.00 27.80 ?  305 THR A C     1 
ATOM   2450  O  O     . THR A 1 305 ? 157.385 147.108 130.822 1.00 33.42 ?  305 THR A O     1 
ATOM   2451  C  CB    . THR A 1 305 ? 156.854 143.984 131.750 1.00 31.42 ?  305 THR A CB    1 
ATOM   2452  O  OG1   . THR A 1 305 ? 157.056 143.391 130.461 1.00 31.84 ?  305 THR A OG1   1 
ATOM   2453  C  CG2   . THR A 1 305 ? 156.122 142.999 132.644 1.00 29.19 ?  305 THR A CG2   1 
ATOM   2454  N  N     . ILE A 1 306 ? 156.309 145.892 129.261 1.00 32.77 ?  306 ILE A N     1 
ATOM   2455  C  CA    . ILE A 1 306 ? 156.764 146.747 128.169 1.00 32.57 ?  306 ILE A CA    1 
ATOM   2456  C  C     . ILE A 1 306 ? 156.183 148.148 128.314 1.00 31.32 ?  306 ILE A C     1 
ATOM   2457  O  O     . ILE A 1 306 ? 156.878 149.150 128.105 1.00 32.80 ?  306 ILE A O     1 
ATOM   2458  C  CB    . ILE A 1 306 ? 156.400 146.114 126.814 1.00 28.41 ?  306 ILE A CB    1 
ATOM   2459  C  CG1   . ILE A 1 306 ? 157.386 144.997 126.471 1.00 32.43 ?  306 ILE A CG1   1 
ATOM   2460  C  CG2   . ILE A 1 306 ? 156.362 147.164 125.716 1.00 31.73 ?  306 ILE A CG2   1 
ATOM   2461  C  CD1   . ILE A 1 306 ? 157.086 144.296 125.175 1.00 31.27 ?  306 ILE A CD1   1 
ATOM   2462  N  N     . TYR A 1 307 ? 154.900 148.242 128.671 1.00 31.91 ?  307 TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 307 ? 154.276 149.548 128.851 1.00 31.01 ?  307 TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 307 ? 154.927 150.321 129.991 1.00 33.45 ?  307 TYR A C     1 
ATOM   2465  O  O     . TYR A 1 307 ? 155.138 151.534 129.888 1.00 36.52 ?  307 TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 307 ? 152.776 149.386 129.100 1.00 28.97 ?  307 TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 307 ? 152.035 150.696 129.198 1.00 30.60 ?  307 TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 307 ? 151.681 151.399 128.055 1.00 30.65 ?  307 TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 307 ? 151.695 151.235 130.430 1.00 33.18 ?  307 TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 307 ? 151.010 152.596 128.136 1.00 33.00 ?  307 TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 307 ? 151.023 152.433 130.522 1.00 33.13 ?  307 TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 307 ? 150.683 153.108 129.370 1.00 34.63 ?  307 TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 307 ? 150.012 154.304 129.446 1.00 36.39 ?  307 TYR A OH    1 
ATOM   2474  N  N     . LYS A 1 308 ? 155.240 149.637 131.091 1.00 34.52 ?  308 LYS A N     1 
ATOM   2475  C  CA    . LYS A 1 308 ? 155.899 150.293 132.215 1.00 32.72 ?  308 LYS A CA    1 
ATOM   2476  C  C     . LYS A 1 308 ? 157.303 150.753 131.842 1.00 32.52 ?  308 LYS A C     1 
ATOM   2477  O  O     . LYS A 1 308 ? 157.738 151.833 132.255 1.00 38.35 ?  308 LYS A O     1 
ATOM   2478  C  CB    . LYS A 1 308 ? 155.945 149.351 133.416 1.00 33.87 ?  308 LYS A CB    1 
ATOM   2479  C  CG    . LYS A 1 308 ? 154.604 149.160 134.105 1.00 33.26 ?  308 LYS A CG    1 
ATOM   2480  C  CD    . LYS A 1 308 ? 154.751 148.359 135.388 1.00 36.34 ?  308 LYS A CD    1 
ATOM   2481  C  CE    . LYS A 1 308 ? 155.395 147.009 135.126 1.00 37.36 ?  308 LYS A CE    1 
ATOM   2482  N  NZ    . LYS A 1 308 ? 154.433 145.888 135.306 1.00 37.78 1  308 LYS A NZ    1 
ATOM   2483  N  N     . GLU A 1 309 ? 158.026 149.945 131.063 1.00 32.39 ?  309 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 309 ? 159.404 150.287 130.728 1.00 33.46 ?  309 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 309 ? 159.477 151.413 129.704 1.00 36.40 ?  309 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 309 ? 160.310 152.319 129.830 1.00 37.54 ?  309 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 309 ? 160.138 149.049 130.216 1.00 31.64 ?  309 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 309 ? 161.537 149.331 129.698 1.00 37.48 ?  309 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 309 ? 162.498 149.748 130.791 1.00 42.65 ?  309 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 309 ? 162.195 149.507 131.978 1.00 41.25 ?  309 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 309 ? 163.559 150.319 130.464 1.00 41.78 -1 309 GLU A OE2   1 
ATOM   2492  N  N     . TYR A 1 310 ? 158.615 151.382 128.687 1.00 37.05 ?  310 TYR A N     1 
ATOM   2493  C  CA    . TYR A 1 310 ? 158.726 152.294 127.558 1.00 36.10 ?  310 TYR A CA    1 
ATOM   2494  C  C     . TYR A 1 310 ? 157.619 153.336 127.489 1.00 33.12 ?  310 TYR A C     1 
ATOM   2495  O  O     . TYR A 1 310 ? 157.740 154.287 126.709 1.00 38.26 ?  310 TYR A O     1 
ATOM   2496  C  CB    . TYR A 1 310 ? 158.752 151.500 126.243 1.00 37.36 ?  310 TYR A CB    1 
ATOM   2497  C  CG    . TYR A 1 310 ? 159.890 150.507 126.159 1.00 33.85 ?  310 TYR A CG    1 
ATOM   2498  C  CD1   . TYR A 1 310 ? 161.143 150.896 125.709 1.00 34.94 ?  310 TYR A CD1   1 
ATOM   2499  C  CD2   . TYR A 1 310 ? 159.711 149.183 126.533 1.00 32.11 ?  310 TYR A CD2   1 
ATOM   2500  C  CE1   . TYR A 1 310 ? 162.187 149.996 125.633 1.00 36.55 ?  310 TYR A CE1   1 
ATOM   2501  C  CE2   . TYR A 1 310 ? 160.749 148.275 126.462 1.00 33.23 ?  310 TYR A CE2   1 
ATOM   2502  C  CZ    . TYR A 1 310 ? 161.983 148.687 126.009 1.00 37.01 ?  310 TYR A CZ    1 
ATOM   2503  O  OH    . TYR A 1 310 ? 163.019 147.785 125.936 1.00 41.12 ?  310 TYR A OH    1 
ATOM   2504  N  N     . GLY A 1 311 ? 156.555 153.196 128.275 1.00 27.93 ?  311 GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 311 ? 155.462 154.144 128.230 1.00 31.03 ?  311 GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 311 ? 154.508 153.967 127.072 1.00 36.06 ?  311 GLY A C     1 
ATOM   2507  O  O     . GLY A 1 311 ? 153.580 154.773 126.928 1.00 39.00 ?  311 GLY A O     1 
ATOM   2508  N  N     . GLN A 1 312 ? 154.708 152.946 126.241 1.00 35.59 ?  312 GLN A N     1 
ATOM   2509  C  CA    . GLN A 1 312 ? 153.838 152.660 125.113 1.00 32.40 ?  312 GLN A CA    1 
ATOM   2510  C  C     . GLN A 1 312 ? 153.487 151.179 125.119 1.00 34.00 ?  312 GLN A C     1 
ATOM   2511  O  O     . GLN A 1 312 ? 154.229 150.347 125.646 1.00 38.82 ?  312 GLN A O     1 
ATOM   2512  C  CB    . GLN A 1 312 ? 154.491 153.034 123.774 1.00 31.89 ?  312 GLN A CB    1 
ATOM   2513  C  CG    . GLN A 1 312 ? 155.591 154.076 123.875 1.00 34.46 ?  312 GLN A CG    1 
ATOM   2514  C  CD    . GLN A 1 312 ? 156.329 154.272 122.567 1.00 39.73 ?  312 GLN A CD    1 
ATOM   2515  O  OE1   . GLN A 1 312 ? 155.715 154.421 121.511 1.00 38.64 ?  312 GLN A OE1   1 
ATOM   2516  N  NE2   . GLN A 1 312 ? 157.655 154.271 122.629 1.00 38.75 ?  312 GLN A NE2   1 
ATOM   2517  N  N     . HIS A 1 313 ? 152.343 150.859 124.522 1.00 31.83 ?  313 HIS A N     1 
ATOM   2518  C  CA    . HIS A 1 313 ? 151.904 149.477 124.452 1.00 28.38 ?  313 HIS A CA    1 
ATOM   2519  C  C     . HIS A 1 313 ? 152.771 148.689 123.472 1.00 33.15 ?  313 HIS A C     1 
ATOM   2520  O  O     . HIS A 1 313 ? 153.394 149.244 122.564 1.00 35.26 ?  313 HIS A O     1 
ATOM   2521  C  CB    . HIS A 1 313 ? 150.435 149.399 124.039 1.00 28.95 ?  313 HIS A CB    1 
ATOM   2522  C  CG    . HIS A 1 313 ? 149.507 150.108 124.975 1.00 33.95 ?  313 HIS A CG    1 
ATOM   2523  N  ND1   . HIS A 1 313 ? 149.051 149.539 126.145 1.00 30.64 ?  313 HIS A ND1   1 
ATOM   2524  C  CD2   . HIS A 1 313 ? 148.945 151.338 124.912 1.00 32.84 ?  313 HIS A CD2   1 
ATOM   2525  C  CE1   . HIS A 1 313 ? 148.250 150.388 126.762 1.00 28.85 ?  313 HIS A CE1   1 
ATOM   2526  N  NE2   . HIS A 1 313 ? 148.169 151.487 126.035 1.00 30.06 ?  313 HIS A NE2   1 
ATOM   2527  N  N     . MET A 1 314 ? 152.806 147.369 123.676 1.00 34.61 ?  314 MET A N     1 
ATOM   2528  C  CA    . MET A 1 314 ? 153.632 146.509 122.837 1.00 27.28 ?  314 MET A CA    1 
ATOM   2529  C  C     . MET A 1 314 ? 153.184 146.552 121.381 1.00 31.93 ?  314 MET A C     1 
ATOM   2530  O  O     . MET A 1 314 ? 154.016 146.546 120.467 1.00 36.58 ?  314 MET A O     1 
ATOM   2531  C  CB    . MET A 1 314 ? 153.601 145.076 123.369 1.00 27.70 ?  314 MET A CB    1 
ATOM   2532  C  CG    . MET A 1 314 ? 154.514 144.115 122.628 1.00 28.99 ?  314 MET A CG    1 
ATOM   2533  S  SD    . MET A 1 314 ? 154.119 142.389 122.960 1.00 41.60 ?  314 MET A SD    1 
ATOM   2534  C  CE    . MET A 1 314 ? 152.331 142.450 122.972 1.00 30.84 ?  314 MET A CE    1 
ATOM   2535  N  N     . ASP A 1 315 ? 151.875 146.593 121.143 1.00 33.57 ?  315 ASP A N     1 
ATOM   2536  C  CA    . ASP A 1 315 ? 151.352 146.625 119.784 1.00 36.36 ?  315 ASP A CA    1 
ATOM   2537  C  C     . ASP A 1 315 ? 151.383 148.016 119.161 1.00 33.16 ?  315 ASP A C     1 
ATOM   2538  O  O     . ASP A 1 315 ? 151.044 148.152 117.980 1.00 35.57 ?  315 ASP A O     1 
ATOM   2539  C  CB    . ASP A 1 315 ? 149.923 146.072 119.758 1.00 27.80 ?  315 ASP A CB    1 
ATOM   2540  C  CG    . ASP A 1 315 ? 148.933 146.986 120.447 1.00 34.50 ?  315 ASP A CG    1 
ATOM   2541  O  OD1   . ASP A 1 315 ? 149.348 147.737 121.354 1.00 36.88 ?  315 ASP A OD1   1 
ATOM   2542  O  OD2   . ASP A 1 315 ? 147.739 146.954 120.081 1.00 31.81 -1 315 ASP A OD2   1 
ATOM   2543  N  N     . GLU A 1 316 ? 151.775 149.042 119.910 1.00 30.94 ?  316 GLU A N     1 
ATOM   2544  C  CA    . GLU A 1 316 ? 151.839 150.402 119.393 1.00 31.82 ?  316 GLU A CA    1 
ATOM   2545  C  C     . GLU A 1 316 ? 153.192 150.761 118.795 1.00 34.22 ?  316 GLU A C     1 
ATOM   2546  O  O     . GLU A 1 316 ? 153.320 151.833 118.195 1.00 36.40 ?  316 GLU A O     1 
ATOM   2547  C  CB    . GLU A 1 316 ? 151.494 151.403 120.499 1.00 34.66 ?  316 GLU A CB    1 
ATOM   2548  C  CG    . GLU A 1 316 ? 150.067 151.312 120.996 1.00 35.61 ?  316 GLU A CG    1 
ATOM   2549  C  CD    . GLU A 1 316 ? 149.158 152.315 120.321 1.00 39.42 ?  316 GLU A CD    1 
ATOM   2550  O  OE1   . GLU A 1 316 ? 149.294 152.512 119.096 1.00 36.52 ?  316 GLU A OE1   1 
ATOM   2551  O  OE2   . GLU A 1 316 ? 148.313 152.914 121.018 1.00 45.88 -1 316 GLU A OE2   1 
ATOM   2552  N  N     . MET A 1 317 ? 154.198 149.904 118.938 1.00 40.57 ?  317 MET A N     1 
ATOM   2553  C  CA    . MET A 1 317 ? 155.518 150.153 118.381 1.00 41.21 ?  317 MET A CA    1 
ATOM   2554  C  C     . MET A 1 317 ? 155.888 149.049 117.399 1.00 42.05 ?  317 MET A C     1 
ATOM   2555  O  O     . MET A 1 317 ? 155.322 147.953 117.419 1.00 38.59 ?  317 MET A O     1 
ATOM   2556  C  CB    . MET A 1 317 ? 156.587 150.255 119.476 1.00 40.57 ?  317 MET A CB    1 
ATOM   2557  C  CG    . MET A 1 317 ? 156.095 150.847 120.780 1.00 42.12 ?  317 MET A CG    1 
ATOM   2558  S  SD    . MET A 1 317 ? 157.367 150.811 122.054 1.00 51.18 ?  317 MET A SD    1 
ATOM   2559  C  CE    . MET A 1 317 ? 156.540 149.869 123.326 1.00 35.61 ?  317 MET A CE    1 
ATOM   2560  N  N     . ASP A 1 318 ? 156.859 149.353 116.541 1.00 43.69 ?  318 ASP A N     1 
ATOM   2561  C  CA    . ASP A 1 318 ? 157.301 148.424 115.507 1.00 41.03 ?  318 ASP A CA    1 
ATOM   2562  C  C     . ASP A 1 318 ? 158.120 147.316 116.154 1.00 40.87 ?  318 ASP A C     1 
ATOM   2563  O  O     . ASP A 1 318 ? 159.216 147.563 116.667 1.00 43.57 ?  318 ASP A O     1 
ATOM   2564  C  CB    . ASP A 1 318 ? 158.113 149.157 114.444 1.00 41.27 ?  318 ASP A CB    1 
ATOM   2565  C  CG    . ASP A 1 318 ? 158.721 148.214 113.425 1.00 47.77 ?  318 ASP A CG    1 
ATOM   2566  O  OD1   . ASP A 1 318 ? 158.023 147.271 112.997 1.00 46.74 ?  318 ASP A OD1   1 
ATOM   2567  O  OD2   . ASP A 1 318 ? 159.896 148.417 113.052 1.00 49.13 -1 318 ASP A OD2   1 
ATOM   2568  N  N     . MET A 1 319 ? 157.591 146.092 116.128 1.00 42.96 ?  319 MET A N     1 
ATOM   2569  C  CA    . MET A 1 319 ? 158.287 144.959 116.725 1.00 36.29 ?  319 MET A CA    1 
ATOM   2570  C  C     . MET A 1 319 ? 159.573 144.614 115.984 1.00 36.71 ?  319 MET A C     1 
ATOM   2571  O  O     . MET A 1 319 ? 160.482 144.040 116.588 1.00 41.37 ?  319 MET A O     1 
ATOM   2572  C  CB    . MET A 1 319 ? 157.351 143.746 116.774 1.00 33.84 ?  319 MET A CB    1 
ATOM   2573  C  CG    . MET A 1 319 ? 158.011 142.444 117.201 1.00 38.01 ?  319 MET A CG    1 
ATOM   2574  S  SD    . MET A 1 319 ? 158.049 142.193 118.988 1.00 45.80 ?  319 MET A SD    1 
ATOM   2575  C  CE    . MET A 1 319 ? 156.668 143.199 119.523 1.00 34.85 ?  319 MET A CE    1 
ATOM   2576  N  N     . ASN A 1 320 ? 159.687 144.979 114.706 1.00 38.02 ?  320 ASN A N     1 
ATOM   2577  C  CA    . ASN A 1 320 ? 160.903 144.671 113.963 1.00 41.12 ?  320 ASN A CA    1 
ATOM   2578  C  C     . ASN A 1 320 ? 162.118 145.357 114.576 1.00 41.90 ?  320 ASN A C     1 
ATOM   2579  O  O     . ASN A 1 320 ? 163.195 144.758 114.675 1.00 41.32 ?  320 ASN A O     1 
ATOM   2580  C  CB    . ASN A 1 320 ? 160.739 145.073 112.497 1.00 41.65 ?  320 ASN A CB    1 
ATOM   2581  C  CG    . ASN A 1 320 ? 160.099 143.981 111.666 1.00 43.37 ?  320 ASN A CG    1 
ATOM   2582  O  OD1   . ASN A 1 320 ? 158.888 143.772 111.721 1.00 38.61 ?  320 ASN A OD1   1 
ATOM   2583  N  ND2   . ASN A 1 320 ? 160.913 143.275 110.889 1.00 40.60 ?  320 ASN A ND2   1 
ATOM   2584  N  N     . GLU A 1 321 ? 161.964 146.610 114.998 1.00 42.91 ?  321 GLU A N     1 
ATOM   2585  C  CA    . GLU A 1 321 ? 163.046 147.343 115.640 1.00 44.57 ?  321 GLU A CA    1 
ATOM   2586  C  C     . GLU A 1 321 ? 163.002 147.268 117.161 1.00 42.96 ?  321 GLU A C     1 
ATOM   2587  O  O     . GLU A 1 321 ? 163.977 147.660 117.812 1.00 44.36 ?  321 GLU A O     1 
ATOM   2588  C  CB    . GLU A 1 321 ? 163.018 148.812 115.205 1.00 44.39 ?  321 GLU A CB    1 
ATOM   2589  C  CG    . GLU A 1 321 ? 161.813 149.583 115.715 1.00 47.17 ?  321 GLU A CG    1 
ATOM   2590  C  CD    . GLU A 1 321 ? 162.152 151.011 116.095 1.00 49.00 ?  321 GLU A CD    1 
ATOM   2591  O  OE1   . GLU A 1 321 ? 163.249 151.237 116.645 1.00 46.69 ?  321 GLU A OE1   1 
ATOM   2592  O  OE2   . GLU A 1 321 ? 161.319 151.907 115.842 1.00 47.46 -1 321 GLU A OE2   1 
ATOM   2593  N  N     . MET A 1 322 ? 161.909 146.775 117.740 1.00 41.35 ?  322 MET A N     1 
ATOM   2594  C  CA    . MET A 1 322 ? 161.742 146.743 119.186 1.00 35.79 ?  322 MET A CA    1 
ATOM   2595  C  C     . MET A 1 322 ? 161.982 145.369 119.798 1.00 33.07 ?  322 MET A C     1 
ATOM   2596  O  O     . MET A 1 322 ? 162.117 145.275 121.020 1.00 41.00 ?  322 MET A O     1 
ATOM   2597  C  CB    . MET A 1 322 ? 160.330 147.209 119.566 1.00 34.29 ?  322 MET A CB    1 
ATOM   2598  C  CG    . MET A 1 322 ? 160.204 148.693 119.871 1.00 39.93 ?  322 MET A CG    1 
ATOM   2599  S  SD    . MET A 1 322 ? 161.535 149.335 120.898 1.00 48.26 ?  322 MET A SD    1 
ATOM   2600  C  CE    . MET A 1 322 ? 162.318 150.463 119.749 1.00 39.75 ?  322 MET A CE    1 
ATOM   2601  N  N     . TYR A 1 323 ? 162.024 144.308 118.988 1.00 31.27 ?  323 TYR A N     1 
ATOM   2602  C  CA    . TYR A 1 323 ? 162.088 142.954 119.530 1.00 32.27 ?  323 TYR A CA    1 
ATOM   2603  C  C     . TYR A 1 323 ? 163.407 142.704 120.250 1.00 36.70 ?  323 TYR A C     1 
ATOM   2604  O  O     . TYR A 1 323 ? 163.429 142.136 121.348 1.00 38.05 ?  323 TYR A O     1 
ATOM   2605  C  CB    . TYR A 1 323 ? 161.884 141.936 118.408 1.00 30.02 ?  323 TYR A CB    1 
ATOM   2606  C  CG    . TYR A 1 323 ? 162.026 140.499 118.849 1.00 35.95 ?  323 TYR A CG    1 
ATOM   2607  C  CD1   . TYR A 1 323 ? 160.960 139.821 119.422 1.00 31.23 ?  323 TYR A CD1   1 
ATOM   2608  C  CD2   . TYR A 1 323 ? 163.226 139.818 118.691 1.00 33.51 ?  323 TYR A CD2   1 
ATOM   2609  C  CE1   . TYR A 1 323 ? 161.085 138.509 119.826 1.00 28.78 ?  323 TYR A CE1   1 
ATOM   2610  C  CE2   . TYR A 1 323 ? 163.360 138.508 119.091 1.00 26.53 ?  323 TYR A CE2   1 
ATOM   2611  C  CZ    . TYR A 1 323 ? 162.287 137.857 119.659 1.00 31.76 ?  323 TYR A CZ    1 
ATOM   2612  O  OH    . TYR A 1 323 ? 162.419 136.550 120.060 1.00 34.72 ?  323 TYR A OH    1 
ATOM   2613  N  N     . ASP A 1 324 ? 164.521 143.113 119.638 1.00 38.06 ?  324 ASP A N     1 
ATOM   2614  C  CA    . ASP A 1 324 ? 165.820 142.914 120.269 1.00 37.16 ?  324 ASP A CA    1 
ATOM   2615  C  C     . ASP A 1 324 ? 165.930 143.712 121.559 1.00 39.55 ?  324 ASP A C     1 
ATOM   2616  O  O     . ASP A 1 324 ? 166.488 143.230 122.552 1.00 45.08 ?  324 ASP A O     1 
ATOM   2617  C  CB    . ASP A 1 324 ? 166.938 143.297 119.300 1.00 40.36 ?  324 ASP A CB    1 
ATOM   2618  C  CG    . ASP A 1 324 ? 167.032 142.355 118.119 1.00 43.01 ?  324 ASP A CG    1 
ATOM   2619  O  OD1   . ASP A 1 324 ? 166.841 141.136 118.312 1.00 43.21 ?  324 ASP A OD1   1 
ATOM   2620  O  OD2   . ASP A 1 324 ? 167.299 142.832 116.996 1.00 43.38 -1 324 ASP A OD2   1 
ATOM   2621  N  N     . LYS A 1 325 ? 165.402 144.937 121.566 1.00 37.78 ?  325 LYS A N     1 
ATOM   2622  C  CA    . LYS A 1 325 ? 165.439 145.749 122.777 1.00 37.22 ?  325 LYS A CA    1 
ATOM   2623  C  C     . LYS A 1 325 ? 164.563 145.151 123.871 1.00 37.32 ?  325 LYS A C     1 
ATOM   2624  O  O     . LYS A 1 325 ? 164.922 145.200 125.052 1.00 44.63 ?  325 LYS A O     1 
ATOM   2625  C  CB    . LYS A 1 325 ? 165.013 147.182 122.459 1.00 40.71 ?  325 LYS A CB    1 
ATOM   2626  C  CG    . LYS A 1 325 ? 165.953 147.892 121.500 1.00 40.43 ?  325 LYS A CG    1 
ATOM   2627  C  CD    . LYS A 1 325 ? 165.450 149.280 121.150 1.00 40.26 ?  325 LYS A CD    1 
ATOM   2628  C  CE    . LYS A 1 325 ? 166.296 149.913 120.058 1.00 41.23 ?  325 LYS A CE    1 
ATOM   2629  N  NZ    . LYS A 1 325 ? 165.610 151.072 119.425 1.00 45.47 1  325 LYS A NZ    1 
ATOM   2630  N  N     . PHE A 1 326 ? 163.411 144.590 123.501 1.00 37.17 ?  326 PHE A N     1 
ATOM   2631  C  CA    . PHE A 1 326 ? 162.572 143.906 124.480 1.00 36.58 ?  326 PHE A CA    1 
ATOM   2632  C  C     . PHE A 1 326 ? 163.296 142.700 125.067 1.00 34.61 ?  326 PHE A C     1 
ATOM   2633  O  O     . PHE A 1 326 ? 163.274 142.480 126.283 1.00 41.38 ?  326 PHE A O     1 
ATOM   2634  C  CB    . PHE A 1 326 ? 161.255 143.467 123.838 1.00 34.54 ?  326 PHE A CB    1 
ATOM   2635  C  CG    . PHE A 1 326 ? 160.362 144.601 123.423 1.00 34.95 ?  326 PHE A CG    1 
ATOM   2636  C  CD1   . PHE A 1 326 ? 160.497 145.857 123.987 1.00 36.22 ?  326 PHE A CD1   1 
ATOM   2637  C  CD2   . PHE A 1 326 ? 159.382 144.406 122.465 1.00 34.82 ?  326 PHE A CD2   1 
ATOM   2638  C  CE1   . PHE A 1 326 ? 159.670 146.896 123.601 1.00 36.18 ?  326 PHE A CE1   1 
ATOM   2639  C  CE2   . PHE A 1 326 ? 158.554 145.440 122.078 1.00 36.20 ?  326 PHE A CE2   1 
ATOM   2640  C  CZ    . PHE A 1 326 ? 158.698 146.686 122.648 1.00 38.81 ?  326 PHE A CZ    1 
ATOM   2641  N  N     . VAL A 1 327 ? 163.941 141.907 124.210 1.00 38.25 ?  327 VAL A N     1 
ATOM   2642  C  CA    . VAL A 1 327 ? 164.626 140.704 124.673 1.00 39.48 ?  327 VAL A CA    1 
ATOM   2643  C  C     . VAL A 1 327 ? 165.796 141.067 125.581 1.00 42.72 ?  327 VAL A C     1 
ATOM   2644  O  O     . VAL A 1 327 ? 166.005 140.440 126.627 1.00 44.58 ?  327 VAL A O     1 
ATOM   2645  C  CB    . VAL A 1 327 ? 165.078 139.854 123.472 1.00 37.45 ?  327 VAL A CB    1 
ATOM   2646  C  CG1   . VAL A 1 327 ? 165.997 138.732 123.927 1.00 40.17 ?  327 VAL A CG1   1 
ATOM   2647  C  CG2   . VAL A 1 327 ? 163.871 139.289 122.743 1.00 32.45 ?  327 VAL A CG2   1 
ATOM   2648  N  N     . ASP A 1 328 ? 166.569 142.084 125.205 1.00 40.53 ?  328 ASP A N     1 
ATOM   2649  C  CA    . ASP A 1 328 ? 167.736 142.485 125.981 1.00 39.72 ?  328 ASP A CA    1 
ATOM   2650  C  C     . ASP A 1 328 ? 167.385 143.314 127.208 1.00 43.46 ?  328 ASP A C     1 
ATOM   2651  O  O     . ASP A 1 328 ? 168.275 143.599 128.015 1.00 47.01 ?  328 ASP A O     1 
ATOM   2652  C  CB    . ASP A 1 328 ? 168.708 143.269 125.096 1.00 41.20 ?  328 ASP A CB    1 
ATOM   2653  C  CG    . ASP A 1 328 ? 169.313 142.418 123.997 1.00 48.04 ?  328 ASP A CG    1 
ATOM   2654  O  OD1   . ASP A 1 328 ? 168.869 141.263 123.826 1.00 46.00 ?  328 ASP A OD1   1 
ATOM   2655  O  OD2   . ASP A 1 328 ? 170.231 142.904 123.305 1.00 47.87 -1 328 ASP A OD2   1 
ATOM   2656  N  N     . ASN A 1 329 ? 166.123 143.707 127.371 1.00 40.52 ?  329 ASN A N     1 
ATOM   2657  C  CA    . ASN A 1 329 ? 165.722 144.513 128.516 1.00 40.00 ?  329 ASN A CA    1 
ATOM   2658  C  C     . ASN A 1 329 ? 165.377 143.604 129.687 1.00 43.33 ?  329 ASN A C     1 
ATOM   2659  O  O     . ASN A 1 329 ? 164.433 142.810 129.581 1.00 43.25 ?  329 ASN A O     1 
ATOM   2660  C  CB    . ASN A 1 329 ? 164.528 145.385 128.167 1.00 36.36 ?  329 ASN A CB    1 
ATOM   2661  C  CG    . ASN A 1 329 ? 164.370 146.561 129.108 1.00 38.87 ?  329 ASN A CG    1 
ATOM   2662  O  OD1   . ASN A 1 329 ? 164.417 146.406 130.328 1.00 45.50 ?  329 ASN A OD1   1 
ATOM   2663  N  ND2   . ASN A 1 329 ? 164.187 147.747 128.544 1.00 36.20 ?  329 ASN A ND2   1 
ATOM   2664  N  N     . PRO A 1 330 ? 166.105 143.675 130.805 1.00 43.62 ?  330 PRO A N     1 
ATOM   2665  C  CA    . PRO A 1 330 ? 165.754 142.828 131.954 1.00 38.70 ?  330 PRO A CA    1 
ATOM   2666  C  C     . PRO A 1 330 ? 164.420 143.187 132.583 1.00 38.18 ?  330 PRO A C     1 
ATOM   2667  O  O     . PRO A 1 330 ? 163.776 142.315 133.179 1.00 41.07 ?  330 PRO A O     1 
ATOM   2668  C  CB    . PRO A 1 330 ? 166.919 143.059 132.927 1.00 40.51 ?  330 PRO A CB    1 
ATOM   2669  C  CG    . PRO A 1 330 ? 167.438 144.410 132.570 1.00 38.95 ?  330 PRO A CG    1 
ATOM   2670  C  CD    . PRO A 1 330 ? 167.268 144.535 131.082 1.00 40.23 ?  330 PRO A CD    1 
ATOM   2671  N  N     . ARG A 1 331 ? 163.983 144.441 132.469 1.00 37.03 ?  331 ARG A N     1 
ATOM   2672  C  CA    . ARG A 1 331 ? 162.724 144.868 133.065 1.00 38.27 ?  331 ARG A CA    1 
ATOM   2673  C  C     . ARG A 1 331 ? 161.512 144.486 132.228 1.00 39.55 ?  331 ARG A C     1 
ATOM   2674  O  O     . ARG A 1 331 ? 160.379 144.703 132.673 1.00 38.55 ?  331 ARG A O     1 
ATOM   2675  C  CB    . ARG A 1 331 ? 162.741 146.381 133.295 1.00 36.84 ?  331 ARG A CB    1 
ATOM   2676  C  CG    . ARG A 1 331 ? 163.665 146.813 134.422 1.00 38.30 ?  331 ARG A CG    1 
ATOM   2677  C  CD    . ARG A 1 331 ? 163.945 148.305 134.378 1.00 38.69 ?  331 ARG A CD    1 
ATOM   2678  N  NE    . ARG A 1 331 ? 164.480 148.729 133.090 1.00 41.16 ?  331 ARG A NE    1 
ATOM   2679  C  CZ    . ARG A 1 331 ? 165.711 148.479 132.667 1.00 40.35 ?  331 ARG A CZ    1 
ATOM   2680  N  NH1   . ARG A 1 331 ? 166.578 147.812 133.412 1.00 42.22 1  331 ARG A NH1   1 
ATOM   2681  N  NH2   . ARG A 1 331 ? 166.085 148.912 131.466 1.00 35.96 ?  331 ARG A NH2   1 
ATOM   2682  N  N     . VAL A 1 332 ? 161.717 143.931 131.039 1.00 35.93 ?  332 VAL A N     1 
ATOM   2683  C  CA    . VAL A 1 332 ? 160.638 143.407 130.211 1.00 34.17 ?  332 VAL A CA    1 
ATOM   2684  C  C     . VAL A 1 332 ? 160.571 141.904 130.437 1.00 37.50 ?  332 VAL A C     1 
ATOM   2685  O  O     . VAL A 1 332 ? 161.553 141.189 130.205 1.00 37.78 ?  332 VAL A O     1 
ATOM   2686  C  CB    . VAL A 1 332 ? 160.858 143.737 128.727 1.00 34.74 ?  332 VAL A CB    1 
ATOM   2687  C  CG1   . VAL A 1 332 ? 159.987 142.850 127.851 1.00 34.04 ?  332 VAL A CG1   1 
ATOM   2688  C  CG2   . VAL A 1 332 ? 160.571 145.204 128.460 1.00 35.22 ?  332 VAL A CG2   1 
ATOM   2689  N  N     . LYS A 1 333 ? 159.422 141.423 130.899 1.00 33.45 ?  333 LYS A N     1 
ATOM   2690  C  CA    . LYS A 1 333 ? 159.235 140.006 131.168 1.00 31.89 ?  333 LYS A CA    1 
ATOM   2691  C  C     . LYS A 1 333 ? 158.768 139.297 129.905 1.00 32.22 ?  333 LYS A C     1 
ATOM   2692  O  O     . LYS A 1 333 ? 157.901 139.795 129.182 1.00 36.70 ?  333 LYS A O     1 
ATOM   2693  C  CB    . LYS A 1 333 ? 158.226 139.801 132.299 1.00 29.77 ?  333 LYS A CB    1 
ATOM   2694  C  CG    . LYS A 1 333 ? 158.078 138.358 132.750 1.00 32.83 ?  333 LYS A CG    1 
ATOM   2695  C  CD    . LYS A 1 333 ? 157.288 138.266 134.043 1.00 33.72 ?  333 LYS A CD    1 
ATOM   2696  C  CE    . LYS A 1 333 ? 157.365 136.871 134.639 1.00 36.46 ?  333 LYS A CE    1 
ATOM   2697  N  NZ    . LYS A 1 333 ? 156.030 136.387 135.086 1.00 38.82 1  333 LYS A NZ    1 
ATOM   2698  N  N     . LYS A 1 334 ? 159.352 138.130 129.642 1.00 35.19 ?  334 LYS A N     1 
ATOM   2699  C  CA    . LYS A 1 334 ? 159.081 137.403 128.412 1.00 33.26 ?  334 LYS A CA    1 
ATOM   2700  C  C     . LYS A 1 334 ? 159.189 135.909 128.670 1.00 37.91 ?  334 LYS A C     1 
ATOM   2701  O  O     . LYS A 1 334 ? 159.808 135.467 129.642 1.00 40.87 ?  334 LYS A O     1 
ATOM   2702  C  CB    . LYS A 1 334 ? 160.046 137.817 127.296 1.00 31.87 ?  334 LYS A CB    1 
ATOM   2703  C  CG    . LYS A 1 334 ? 161.506 137.613 127.649 1.00 34.69 ?  334 LYS A CG    1 
ATOM   2704  C  CD    . LYS A 1 334 ? 162.399 138.555 126.869 1.00 33.81 ?  334 LYS A CD    1 
ATOM   2705  C  CE    . LYS A 1 334 ? 162.913 139.676 127.754 1.00 35.60 ?  334 LYS A CE    1 
ATOM   2706  N  NZ    . LYS A 1 334 ? 163.820 139.175 128.820 1.00 37.49 1  334 LYS A NZ    1 
ATOM   2707  N  N     . GLU A 1 335 ? 158.571 135.133 127.783 1.00 35.08 ?  335 GLU A N     1 
ATOM   2708  C  CA    . GLU A 1 335 ? 158.614 133.680 127.834 1.00 35.23 ?  335 GLU A CA    1 
ATOM   2709  C  C     . GLU A 1 335 ? 159.127 133.130 126.511 1.00 39.41 ?  335 GLU A C     1 
ATOM   2710  O  O     . GLU A 1 335 ? 158.768 133.624 125.437 1.00 44.34 ?  335 GLU A O     1 
ATOM   2711  C  CB    . GLU A 1 335 ? 157.236 133.089 128.149 1.00 34.11 ?  335 GLU A CB    1 
ATOM   2712  C  CG    . GLU A 1 335 ? 156.539 133.745 129.328 1.00 43.30 ?  335 GLU A CG    1 
ATOM   2713  C  CD    . GLU A 1 335 ? 156.347 132.796 130.494 1.00 43.64 ?  335 GLU A CD    1 
ATOM   2714  O  OE1   . GLU A 1 335 ? 157.331 132.139 130.895 1.00 40.96 ?  335 GLU A OE1   1 
ATOM   2715  O  OE2   . GLU A 1 335 ? 155.215 132.708 131.013 1.00 38.15 -1 335 GLU A OE2   1 
ATOM   2716  N  N     . LYS A 1 336 ? 159.972 132.107 126.605 1.00 38.66 ?  336 LYS A N     1 
ATOM   2717  C  CA    . LYS A 1 336 ? 160.553 131.462 125.436 1.00 34.38 ?  336 LYS A CA    1 
ATOM   2718  C  C     . LYS A 1 336 ? 159.511 130.603 124.729 1.00 38.68 ?  336 LYS A C     1 
ATOM   2719  O  O     . LYS A 1 336 ? 158.783 129.840 125.372 1.00 41.63 ?  336 LYS A O     1 
ATOM   2720  C  CB    . LYS A 1 336 ? 161.744 130.605 125.861 1.00 40.52 ?  336 LYS A CB    1 
ATOM   2721  C  CG    . LYS A 1 336 ? 162.918 130.593 124.900 1.00 42.05 ?  336 LYS A CG    1 
ATOM   2722  C  CD    . LYS A 1 336 ? 163.853 129.440 125.238 1.00 41.51 ?  336 LYS A CD    1 
ATOM   2723  C  CE    . LYS A 1 336 ? 164.684 129.016 124.042 1.00 40.22 ?  336 LYS A CE    1 
ATOM   2724  N  NZ    . LYS A 1 336 ? 165.322 127.687 124.248 1.00 41.73 1  336 LYS A NZ    1 
ATOM   2725  N  N     . ILE A 1 337 ? 159.439 130.728 123.401 1.00 36.69 ?  337 ILE A N     1 
ATOM   2726  C  CA    . ILE A 1 337 ? 158.562 129.907 122.577 1.00 33.68 ?  337 ILE A CA    1 
ATOM   2727  C  C     . ILE A 1 337 ? 159.316 129.501 121.319 1.00 32.64 ?  337 ILE A C     1 
ATOM   2728  O  O     . ILE A 1 337 ? 160.348 130.078 120.970 1.00 36.49 ?  337 ILE A O     1 
ATOM   2729  C  CB    . ILE A 1 337 ? 157.252 130.632 122.192 1.00 34.61 ?  337 ILE A CB    1 
ATOM   2730  C  CG1   . ILE A 1 337 ? 157.564 131.964 121.507 1.00 33.71 ?  337 ILE A CG1   1 
ATOM   2731  C  CG2   . ILE A 1 337 ? 156.364 130.833 123.411 1.00 35.33 ?  337 ILE A CG2   1 
ATOM   2732  C  CD1   . ILE A 1 337 ? 156.670 132.266 120.329 1.00 31.06 ?  337 ILE A CD1   1 
ATOM   2733  N  N     . ASN A 1 338 ? 158.784 128.490 120.634 1.00 33.74 ?  338 ASN A N     1 
ATOM   2734  C  CA    . ASN A 1 338 ? 159.313 128.095 119.340 1.00 35.16 ?  338 ASN A CA    1 
ATOM   2735  C  C     . ASN A 1 338 ? 158.396 128.640 118.257 1.00 32.98 ?  338 ASN A C     1 
ATOM   2736  O  O     . ASN A 1 338 ? 157.248 128.183 118.148 1.00 34.04 ?  338 ASN A O     1 
ATOM   2737  C  CB    . ASN A 1 338 ? 159.424 126.577 119.234 1.00 35.34 ?  338 ASN A CB    1 
ATOM   2738  C  CG    . ASN A 1 338 ? 160.167 126.134 117.989 1.00 36.98 ?  338 ASN A CG    1 
ATOM   2739  O  OD1   . ASN A 1 338 ? 159.787 125.165 117.335 1.00 37.66 ?  338 ASN A OD1   1 
ATOM   2740  N  ND2   . ASN A 1 338 ? 161.235 126.849 117.653 1.00 37.68 ?  338 ASN A ND2   1 
ATOM   2741  N  N     . PRO A 1 339 ? 158.834 129.614 117.456 1.00 35.25 ?  339 PRO A N     1 
ATOM   2742  C  CA    . PRO A 1 339 ? 157.937 130.183 116.437 1.00 31.07 ?  339 PRO A CA    1 
ATOM   2743  C  C     . PRO A 1 339 ? 157.453 129.174 115.412 1.00 32.75 ?  339 PRO A C     1 
ATOM   2744  O  O     . PRO A 1 339 ? 156.321 129.294 114.932 1.00 37.31 ?  339 PRO A O     1 
ATOM   2745  C  CB    . PRO A 1 339 ? 158.793 131.282 115.791 1.00 31.83 ?  339 PRO A CB    1 
ATOM   2746  C  CG    . PRO A 1 339 ? 160.198 130.912 116.105 1.00 34.70 ?  339 PRO A CG    1 
ATOM   2747  C  CD    . PRO A 1 339 ? 160.164 130.243 117.440 1.00 33.83 ?  339 PRO A CD    1 
ATOM   2748  N  N     . ARG A 1 340 ? 158.274 128.185 115.053 1.00 32.40 ?  340 ARG A N     1 
ATOM   2749  C  CA    . ARG A 1 340 ? 157.817 127.158 114.123 1.00 27.98 ?  340 ARG A CA    1 
ATOM   2750  C  C     . ARG A 1 340 ? 156.742 126.284 114.755 1.00 31.44 ?  340 ARG A C     1 
ATOM   2751  O  O     . ARG A 1 340 ? 155.772 125.902 114.089 1.00 37.96 ?  340 ARG A O     1 
ATOM   2752  C  CB    . ARG A 1 340 ? 158.998 126.313 113.648 1.00 30.71 ?  340 ARG A CB    1 
ATOM   2753  C  CG    . ARG A 1 340 ? 159.878 127.023 112.636 1.00 30.19 ?  340 ARG A CG    1 
ATOM   2754  C  CD    . ARG A 1 340 ? 160.761 126.054 111.876 1.00 27.86 ?  340 ARG A CD    1 
ATOM   2755  N  NE    . ARG A 1 340 ? 161.635 126.755 110.943 1.00 30.37 ?  340 ARG A NE    1 
ATOM   2756  C  CZ    . ARG A 1 340 ? 162.565 126.170 110.203 1.00 32.54 ?  340 ARG A CZ    1 
ATOM   2757  N  NH1   . ARG A 1 340 ? 162.773 124.865 110.258 1.00 32.83 1  340 ARG A NH1   1 
ATOM   2758  N  NH2   . ARG A 1 340 ? 163.306 126.913 109.385 1.00 32.68 ?  340 ARG A NH2   1 
ATOM   2759  N  N     . LYS A 1 341 ? 156.891 125.963 116.041 1.00 33.69 ?  341 LYS A N     1 
ATOM   2760  C  CA    . LYS A 1 341 ? 155.836 125.243 116.746 1.00 32.33 ?  341 LYS A CA    1 
ATOM   2761  C  C     . LYS A 1 341 ? 154.555 126.065 116.799 1.00 31.94 ?  341 LYS A C     1 
ATOM   2762  O  O     . LYS A 1 341 ? 153.455 125.521 116.663 1.00 35.86 ?  341 LYS A O     1 
ATOM   2763  C  CB    . LYS A 1 341 ? 156.297 124.876 118.157 1.00 35.30 ?  341 LYS A CB    1 
ATOM   2764  C  CG    . LYS A 1 341 ? 157.138 123.614 118.229 1.00 37.81 ?  341 LYS A CG    1 
ATOM   2765  C  CD    . LYS A 1 341 ? 156.483 122.464 117.483 1.00 36.37 ?  341 LYS A CD    1 
ATOM   2766  C  CE    . LYS A 1 341 ? 157.520 121.578 116.816 1.00 38.19 ?  341 LYS A CE    1 
ATOM   2767  N  NZ    . LYS A 1 341 ? 158.380 122.346 115.874 1.00 38.23 1  341 LYS A NZ    1 
ATOM   2768  N  N     . LEU A 1 342 ? 154.678 127.378 116.998 1.00 29.81 ?  342 LEU A N     1 
ATOM   2769  C  CA    . LEU A 1 342 ? 153.498 128.237 117.013 1.00 27.23 ?  342 LEU A CA    1 
ATOM   2770  C  C     . LEU A 1 342 ? 152.831 128.283 115.642 1.00 29.81 ?  342 LEU A C     1 
ATOM   2771  O  O     . LEU A 1 342 ? 151.599 128.283 115.545 1.00 36.01 ?  342 LEU A O     1 
ATOM   2772  C  CB    . LEU A 1 342 ? 153.881 129.640 117.482 1.00 28.01 ?  342 LEU A CB    1 
ATOM   2773  C  CG    . LEU A 1 342 ? 152.745 130.579 117.884 1.00 27.34 ?  342 LEU A CG    1 
ATOM   2774  C  CD1   . LEU A 1 342 ? 151.676 129.829 118.657 1.00 26.87 ?  342 LEU A CD1   1 
ATOM   2775  C  CD2   . LEU A 1 342 ? 153.288 131.733 118.709 1.00 28.36 ?  342 LEU A CD2   1 
ATOM   2776  N  N     . LEU A 1 343 ? 153.628 128.326 114.571 1.00 28.68 ?  343 LEU A N     1 
ATOM   2777  C  CA    . LEU A 1 343 ? 153.065 128.288 113.223 1.00 24.60 ?  343 LEU A CA    1 
ATOM   2778  C  C     . LEU A 1 343 ? 152.351 126.969 112.961 1.00 31.50 ?  343 LEU A C     1 
ATOM   2779  O  O     . LEU A 1 343 ? 151.273 126.945 112.354 1.00 36.23 ?  343 LEU A O     1 
ATOM   2780  C  CB    . LEU A 1 343 ? 154.168 128.513 112.190 1.00 28.60 ?  343 LEU A CB    1 
ATOM   2781  C  CG    . LEU A 1 343 ? 154.537 129.962 111.879 1.00 31.05 ?  343 LEU A CG    1 
ATOM   2782  C  CD1   . LEU A 1 343 ? 155.519 130.023 110.722 1.00 27.29 ?  343 LEU A CD1   1 
ATOM   2783  C  CD2   . LEU A 1 343 ? 153.293 130.778 111.570 1.00 30.62 ?  343 LEU A CD2   1 
ATOM   2784  N  N     . GLU A 1 344 ? 152.944 125.858 113.403 1.00 34.59 ?  344 GLU A N     1 
ATOM   2785  C  CA    . GLU A 1 344 ? 152.293 124.562 113.244 1.00 30.94 ?  344 GLU A CA    1 
ATOM   2786  C  C     . GLU A 1 344 ? 151.003 124.497 114.051 1.00 30.40 ?  344 GLU A C     1 
ATOM   2787  O  O     . GLU A 1 344 ? 150.016 123.902 113.607 1.00 39.33 ?  344 GLU A O     1 
ATOM   2788  C  CB    . GLU A 1 344 ? 153.245 123.439 113.654 1.00 31.41 ?  344 GLU A CB    1 
ATOM   2789  C  CG    . GLU A 1 344 ? 154.454 123.297 112.745 1.00 33.61 ?  344 GLU A CG    1 
ATOM   2790  C  CD    . GLU A 1 344 ? 155.571 122.497 113.383 1.00 40.44 ?  344 GLU A CD    1 
ATOM   2791  O  OE1   . GLU A 1 344 ? 155.308 121.802 114.387 1.00 41.47 ?  344 GLU A OE1   1 
ATOM   2792  O  OE2   . GLU A 1 344 ? 156.714 122.565 112.884 1.00 40.14 -1 344 GLU A OE2   1 
ATOM   2793  N  N     . LYS A 1 345 ? 150.992 125.100 115.240 1.00 29.13 ?  345 LYS A N     1 
ATOM   2794  C  CA    . LYS A 1 345 ? 149.768 125.166 116.033 1.00 29.09 ?  345 LYS A CA    1 
ATOM   2795  C  C     . LYS A 1 345 ? 148.697 125.988 115.326 1.00 29.83 ?  345 LYS A C     1 
ATOM   2796  O  O     . LYS A 1 345 ? 147.519 125.615 115.333 1.00 31.83 ?  345 LYS A O     1 
ATOM   2797  C  CB    . LYS A 1 345 ? 150.068 125.747 117.414 1.00 26.73 ?  345 LYS A CB    1 
ATOM   2798  C  CG    . LYS A 1 345 ? 148.860 125.808 118.332 1.00 29.26 ?  345 LYS A CG    1 
ATOM   2799  C  CD    . LYS A 1 345 ? 149.225 126.362 119.697 1.00 30.18 ?  345 LYS A CD    1 
ATOM   2800  C  CE    . LYS A 1 345 ? 148.001 126.455 120.593 1.00 32.03 ?  345 LYS A CE    1 
ATOM   2801  N  NZ    . LYS A 1 345 ? 148.322 127.046 121.919 1.00 31.82 1  345 LYS A NZ    1 
ATOM   2802  N  N     . LEU A 1 346 ? 149.087 127.109 114.715 1.00 32.88 ?  346 LEU A N     1 
ATOM   2803  C  CA    . LEU A 1 346 ? 148.137 127.904 113.943 1.00 25.13 ?  346 LEU A CA    1 
ATOM   2804  C  C     . LEU A 1 346 ? 147.560 127.098 112.788 1.00 26.69 ?  346 LEU A C     1 
ATOM   2805  O  O     . LEU A 1 346 ? 146.347 127.122 112.548 1.00 32.19 ?  346 LEU A O     1 
ATOM   2806  C  CB    . LEU A 1 346 ? 148.810 129.171 113.412 1.00 24.17 ?  346 LEU A CB    1 
ATOM   2807  C  CG    . LEU A 1 346 ? 149.329 130.214 114.402 1.00 26.88 ?  346 LEU A CG    1 
ATOM   2808  C  CD1   . LEU A 1 346 ? 150.304 131.149 113.710 1.00 27.67 ?  346 LEU A CD1   1 
ATOM   2809  C  CD2   . LEU A 1 346 ? 148.183 130.998 114.999 1.00 28.49 ?  346 LEU A CD2   1 
ATOM   2810  N  N     . ALA A 1 347 ? 148.417 126.377 112.062 1.00 25.65 ?  347 ALA A N     1 
ATOM   2811  C  CA    . ALA A 1 347 ? 147.945 125.571 110.941 1.00 26.16 ?  347 ALA A CA    1 
ATOM   2812  C  C     . ALA A 1 347 ? 147.020 124.453 111.408 1.00 29.62 ?  347 ALA A C     1 
ATOM   2813  O  O     . ALA A 1 347 ? 145.994 124.184 110.774 1.00 35.76 ?  347 ALA A O     1 
ATOM   2814  C  CB    . ALA A 1 347 ? 149.133 124.999 110.169 1.00 26.21 ?  347 ALA A CB    1 
ATOM   2815  N  N     . MET A 1 348 ? 147.364 123.795 112.518 1.00 31.30 ?  348 MET A N     1 
ATOM   2816  C  CA    . MET A 1 348 ? 146.515 122.733 113.046 1.00 34.50 ?  348 MET A CA    1 
ATOM   2817  C  C     . MET A 1 348 ? 145.161 123.276 113.480 1.00 31.34 ?  348 MET A C     1 
ATOM   2818  O  O     . MET A 1 348 ? 144.120 122.671 113.199 1.00 36.47 ?  348 MET A O     1 
ATOM   2819  C  CB    . MET A 1 348 ? 147.218 122.037 114.211 1.00 32.72 ?  348 MET A CB    1 
ATOM   2820  C  CG    . MET A 1 348 ? 146.305 121.195 115.085 1.00 37.45 ?  348 MET A CG    1 
ATOM   2821  S  SD    . MET A 1 348 ? 146.057 121.908 116.724 1.00 55.87 ?  348 MET A SD    1 
ATOM   2822  C  CE    . MET A 1 348 ? 147.731 121.899 117.356 1.00 38.89 ?  348 MET A CE    1 
ATOM   2823  N  N     . LEU A 1 349 ? 145.153 124.425 114.160 1.00 27.73 ?  349 LEU A N     1 
ATOM   2824  C  CA    . LEU A 1 349 ? 143.895 125.018 114.597 1.00 22.99 ?  349 LEU A CA    1 
ATOM   2825  C  C     . LEU A 1 349 ? 143.043 125.442 113.409 1.00 28.25 ?  349 LEU A C     1 
ATOM   2826  O  O     . LEU A 1 349 ? 141.816 125.293 113.432 1.00 30.06 ?  349 LEU A O     1 
ATOM   2827  C  CB    . LEU A 1 349 ? 144.170 126.207 115.514 1.00 26.16 ?  349 LEU A CB    1 
ATOM   2828  C  CG    . LEU A 1 349 ? 144.218 125.876 117.003 1.00 32.55 ?  349 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A 1 349 ? 145.036 126.915 117.736 1.00 30.67 ?  349 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A 1 349 ? 142.817 125.787 117.581 1.00 34.59 ?  349 LEU A CD2   1 
ATOM   2831  N  N     . ARG A 1 350 ? 143.672 125.985 112.365 1.00 29.88 ?  350 ARG A N     1 
ATOM   2832  C  CA    . ARG A 1 350 ? 142.925 126.344 111.166 1.00 24.31 ?  350 ARG A CA    1 
ATOM   2833  C  C     . ARG A 1 350 ? 142.376 125.113 110.459 1.00 30.19 ?  350 ARG A C     1 
ATOM   2834  O  O     . ARG A 1 350 ? 141.286 125.167 109.879 1.00 34.35 ?  350 ARG A O     1 
ATOM   2835  C  CB    . ARG A 1 350 ? 143.806 127.160 110.222 1.00 26.02 ?  350 ARG A CB    1 
ATOM   2836  C  CG    . ARG A 1 350 ? 144.030 128.592 110.679 1.00 24.05 ?  350 ARG A CG    1 
ATOM   2837  C  CD    . ARG A 1 350 ? 145.157 129.252 109.907 1.00 23.05 ?  350 ARG A CD    1 
ATOM   2838  N  NE    . ARG A 1 350 ? 144.803 129.448 108.508 1.00 34.27 ?  350 ARG A NE    1 
ATOM   2839  C  CZ    . ARG A 1 350 ? 144.007 130.410 108.061 1.00 31.39 ?  350 ARG A CZ    1 
ATOM   2840  N  NH1   . ARG A 1 350 ? 143.471 131.302 108.880 1.00 24.59 1  350 ARG A NH1   1 
ATOM   2841  N  NH2   . ARG A 1 350 ? 143.738 130.478 106.761 1.00 28.80 ?  350 ARG A NH2   1 
ATOM   2842  N  N     . SER A 1 351 ? 143.115 124.003 110.483 1.00 33.50 ?  351 SER A N     1 
ATOM   2843  C  CA    . SER A 1 351 ? 142.592 122.761 109.925 1.00 30.16 ?  351 SER A CA    1 
ATOM   2844  C  C     . SER A 1 351 ? 141.384 122.268 110.713 1.00 31.45 ?  351 SER A C     1 
ATOM   2845  O  O     . SER A 1 351 ? 140.392 121.821 110.127 1.00 38.80 ?  351 SER A O     1 
ATOM   2846  C  CB    . SER A 1 351 ? 143.687 121.696 109.899 1.00 30.96 ?  351 SER A CB    1 
ATOM   2847  O  OG    . SER A 1 351 ? 144.630 121.958 108.875 1.00 39.77 ?  351 SER A OG    1 
ATOM   2848  N  N     . GLU A 1 352 ? 141.450 122.344 112.044 1.00 29.70 ?  352 GLU A N     1 
ATOM   2849  C  CA    . GLU A 1 352 ? 140.351 121.843 112.866 1.00 30.98 ?  352 GLU A CA    1 
ATOM   2850  C  C     . GLU A 1 352 ? 139.110 122.724 112.751 1.00 34.19 ?  352 GLU A C     1 
ATOM   2851  O  O     . GLU A 1 352 ? 137.996 122.219 112.573 1.00 39.10 ?  352 GLU A O     1 
ATOM   2852  C  CB    . GLU A 1 352 ? 140.786 121.724 114.328 1.00 33.49 ?  352 GLU A CB    1 
ATOM   2853  C  CG    . GLU A 1 352 ? 142.044 120.905 114.553 1.00 33.65 ?  352 GLU A CG    1 
ATOM   2854  C  CD    . GLU A 1 352 ? 142.552 121.000 115.979 1.00 42.38 ?  352 GLU A CD    1 
ATOM   2855  O  OE1   . GLU A 1 352 ? 143.288 120.089 116.411 1.00 41.46 ?  352 GLU A OE1   1 
ATOM   2856  O  OE2   . GLU A 1 352 ? 142.215 121.986 116.667 1.00 41.70 -1 352 GLU A OE2   1 
ATOM   2857  N  N     . SER A 1 353 ? 139.277 124.045 112.853 1.00 34.69 ?  353 SER A N     1 
ATOM   2858  C  CA    . SER A 1 353 ? 138.135 124.942 112.975 1.00 34.74 ?  353 SER A CA    1 
ATOM   2859  C  C     . SER A 1 353 ? 138.177 126.160 112.062 1.00 30.47 ?  353 SER A C     1 
ATOM   2860  O  O     . SER A 1 353 ? 137.224 126.946 112.074 1.00 31.06 ?  353 SER A O     1 
ATOM   2861  C  CB    . SER A 1 353 ? 137.994 125.421 114.428 1.00 34.34 ?  353 SER A CB    1 
ATOM   2862  O  OG    . SER A 1 353 ? 139.117 126.189 114.824 1.00 32.37 ?  353 SER A OG    1 
ATOM   2863  N  N     . GLY A 1 354 ? 139.236 126.347 111.280 1.00 27.70 ?  354 GLY A N     1 
ATOM   2864  C  CA    . GLY A 1 354 ? 139.350 127.523 110.445 1.00 27.40 ?  354 GLY A CA    1 
ATOM   2865  C  C     . GLY A 1 354 ? 139.856 128.758 111.151 1.00 21.81 ?  354 GLY A C     1 
ATOM   2866  O  O     . GLY A 1 354 ? 139.988 129.808 110.510 1.00 25.58 ?  354 GLY A O     1 
ATOM   2867  N  N     . TYR A 1 355 ? 140.147 128.670 112.444 1.00 22.77 ?  355 TYR A N     1 
ATOM   2868  C  CA    . TYR A 1 355 ? 140.644 129.762 113.255 1.00 17.75 ?  355 TYR A CA    1 
ATOM   2869  C  C     . TYR A 1 355 ? 142.118 129.547 113.585 1.00 22.19 ?  355 TYR A C     1 
ATOM   2870  O  O     . TYR A 1 355 ? 142.585 128.406 113.633 1.00 28.86 ?  355 TYR A O     1 
ATOM   2871  C  CB    . TYR A 1 355 ? 139.843 129.883 114.557 1.00 23.82 ?  355 TYR A CB    1 
ATOM   2872  C  CG    . TYR A 1 355 ? 138.433 130.385 114.363 1.00 26.78 ?  355 TYR A CG    1 
ATOM   2873  C  CD1   . TYR A 1 355 ? 138.189 131.600 113.740 1.00 20.43 ?  355 TYR A CD1   1 
ATOM   2874  C  CD2   . TYR A 1 355 ? 137.345 129.642 114.801 1.00 25.91 ?  355 TYR A CD2   1 
ATOM   2875  C  CE1   . TYR A 1 355 ? 136.902 132.062 113.560 1.00 27.50 ?  355 TYR A CE1   1 
ATOM   2876  C  CE2   . TYR A 1 355 ? 136.054 130.096 114.625 1.00 26.03 ?  355 TYR A CE2   1 
ATOM   2877  C  CZ    . TYR A 1 355 ? 135.838 131.306 114.004 1.00 30.59 ?  355 TYR A CZ    1 
ATOM   2878  O  OH    . TYR A 1 355 ? 134.553 131.763 113.826 1.00 31.21 ?  355 TYR A OH    1 
ATOM   2879  N  N     . PRO A 1 356 ? 142.880 130.617 113.826 1.00 22.84 ?  356 PRO A N     1 
ATOM   2880  C  CA    . PRO A 1 356 ? 142.496 132.034 113.830 1.00 17.73 ?  356 PRO A CA    1 
ATOM   2881  C  C     . PRO A 1 356 ? 142.601 132.698 112.467 1.00 15.52 ?  356 PRO A C     1 
ATOM   2882  O  O     . PRO A 1 356 ? 143.189 132.148 111.541 1.00 19.50 ?  356 PRO A O     1 
ATOM   2883  C  CB    . PRO A 1 356 ? 143.501 132.639 114.811 1.00 18.27 ?  356 PRO A CB    1 
ATOM   2884  C  CG    . PRO A 1 356 ? 144.749 131.851 114.542 1.00 17.73 ?  356 PRO A CG    1 
ATOM   2885  C  CD    . PRO A 1 356 ? 144.286 130.445 114.235 1.00 13.52 ?  356 PRO A CD    1 
ATOM   2886  N  N     . TYR A 1 357 ? 142.031 133.889 112.316 1.00 18.54 ?  357 TYR A N     1 
ATOM   2887  C  CA    . TYR A 1 357 ? 142.379 134.730 111.183 1.00 11.30 ?  357 TYR A CA    1 
ATOM   2888  C  C     . TYR A 1 357 ? 143.828 135.180 111.316 1.00 16.15 ?  357 TYR A C     1 
ATOM   2889  O  O     . TYR A 1 357 ? 144.333 135.408 112.418 1.00 25.34 ?  357 TYR A O     1 
ATOM   2890  C  CB    . TYR A 1 357 ? 141.461 135.951 111.101 1.00 15.07 ?  357 TYR A CB    1 
ATOM   2891  C  CG    . TYR A 1 357 ? 139.992 135.677 111.339 1.00 18.99 ?  357 TYR A CG    1 
ATOM   2892  C  CD1   . TYR A 1 357 ? 139.403 134.498 110.908 1.00 14.29 ?  357 TYR A CD1   1 
ATOM   2893  C  CD2   . TYR A 1 357 ? 139.193 136.602 111.993 1.00 18.46 ?  357 TYR A CD2   1 
ATOM   2894  C  CE1   . TYR A 1 357 ? 138.066 134.247 111.117 1.00 14.64 ?  357 TYR A CE1   1 
ATOM   2895  C  CE2   . TYR A 1 357 ? 137.852 136.361 112.211 1.00 17.60 ?  357 TYR A CE2   1 
ATOM   2896  C  CZ    . TYR A 1 357 ? 137.294 135.181 111.771 1.00 21.97 ?  357 TYR A CZ    1 
ATOM   2897  O  OH    . TYR A 1 357 ? 135.959 134.930 111.982 1.00 26.52 ?  357 TYR A OH    1 
ATOM   2898  N  N     . ILE A 1 358 ? 144.505 135.298 110.180 1.00 14.85 ?  358 ILE A N     1 
ATOM   2899  C  CA    . ILE A 1 358 ? 145.912 135.675 110.141 1.00 13.71 ?  358 ILE A CA    1 
ATOM   2900  C  C     . ILE A 1 358 ? 146.018 137.082 109.575 1.00 16.73 ?  358 ILE A C     1 
ATOM   2901  O  O     . ILE A 1 358 ? 145.541 137.349 108.465 1.00 25.12 ?  358 ILE A O     1 
ATOM   2902  C  CB    . ILE A 1 358 ? 146.741 134.685 109.306 1.00 18.73 ?  358 ILE A CB    1 
ATOM   2903  C  CG1   . ILE A 1 358 ? 146.478 133.248 109.759 1.00 21.88 ?  358 ILE A CG1   1 
ATOM   2904  C  CG2   . ILE A 1 358 ? 148.220 135.018 109.406 1.00 17.24 ?  358 ILE A CG2   1 
ATOM   2905  C  CD1   . ILE A 1 358 ? 146.949 132.952 111.162 1.00 18.48 ?  358 ILE A CD1   1 
ATOM   2906  N  N     . MET A 1 359 ? 146.635 137.979 110.336 1.00 10.67 ?  359 MET A N     1 
ATOM   2907  C  CA    . MET A 1 359 ? 146.940 139.326 109.874 1.00 8.82  ?  359 MET A CA    1 
ATOM   2908  C  C     . MET A 1 359 ? 148.451 139.476 109.802 1.00 10.43 ?  359 MET A C     1 
ATOM   2909  O  O     . MET A 1 359 ? 149.138 139.369 110.823 1.00 21.36 ?  359 MET A O     1 
ATOM   2910  C  CB    . MET A 1 359 ? 146.341 140.386 110.797 1.00 11.87 ?  359 MET A CB    1 
ATOM   2911  C  CG    . MET A 1 359 ? 145.727 141.559 110.054 1.00 12.10 ?  359 MET A CG    1 
ATOM   2912  S  SD    . MET A 1 359 ? 145.750 143.122 110.947 1.00 33.65 ?  359 MET A SD    1 
ATOM   2913  C  CE    . MET A 1 359 ? 147.491 143.518 110.915 1.00 12.22 ?  359 MET A CE    1 
ATOM   2914  N  N     . PHE A 1 360 ? 148.964 139.714 108.600 1.00 10.78 ?  360 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 360 ? 150.385 139.978 108.401 1.00 11.58 ?  360 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 360 ? 150.594 141.476 108.577 1.00 15.89 ?  360 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 360 ? 150.347 142.261 107.660 1.00 25.75 ?  360 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 360 ? 150.835 139.483 107.032 1.00 9.13  ?  360 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 360 ? 150.721 137.994 106.868 1.00 17.71 ?  360 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 360 ? 151.397 137.140 107.721 1.00 16.06 ?  360 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 360 ? 149.930 137.450 105.872 1.00 13.68 ?  360 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 360 ? 151.291 135.770 107.581 1.00 11.57 ?  360 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 360 ? 149.821 136.084 105.726 1.00 17.28 ?  360 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 360 ? 150.503 135.242 106.581 1.00 15.05 ?  360 PHE A CZ    1 
ATOM   2925  N  N     . GLN A 1 361 ? 151.050 141.866 109.770 1.00 11.68 ?  361 GLN A N     1 
ATOM   2926  C  CA    . GLN A 1 361 ? 151.062 143.274 110.157 1.00 11.92 ?  361 GLN A CA    1 
ATOM   2927  C  C     . GLN A 1 361 ? 151.900 144.114 109.201 1.00 15.94 ?  361 GLN A C     1 
ATOM   2928  O  O     . GLN A 1 361 ? 151.477 145.194 108.770 1.00 20.44 ?  361 GLN A O     1 
ATOM   2929  C  CB    . GLN A 1 361 ? 151.587 143.412 111.586 1.00 23.22 ?  361 GLN A CB    1 
ATOM   2930  C  CG    . GLN A 1 361 ? 151.341 144.773 112.207 1.00 17.97 ?  361 GLN A CG    1 
ATOM   2931  C  CD    . GLN A 1 361 ? 151.000 144.688 113.678 1.00 20.29 ?  361 GLN A CD    1 
ATOM   2932  O  OE1   . GLN A 1 361 ? 151.480 143.806 114.387 1.00 24.15 ?  361 GLN A OE1   1 
ATOM   2933  N  NE2   . GLN A 1 361 ? 150.172 145.613 114.145 1.00 23.91 ?  361 GLN A NE2   1 
ATOM   2934  N  N     . ASP A 1 362 ? 153.098 143.637 108.861 1.00 18.11 ?  362 ASP A N     1 
ATOM   2935  C  CA    . ASP A 1 362 ? 153.973 144.427 108.003 1.00 17.14 ?  362 ASP A CA    1 
ATOM   2936  C  C     . ASP A 1 362 ? 153.475 144.464 106.566 1.00 18.27 ?  362 ASP A C     1 
ATOM   2937  O  O     . ASP A 1 362 ? 153.669 145.470 105.877 1.00 19.69 ?  362 ASP A O     1 
ATOM   2938  C  CB    . ASP A 1 362 ? 155.399 143.890 108.071 1.00 18.97 ?  362 ASP A CB    1 
ATOM   2939  C  CG    . ASP A 1 362 ? 155.960 143.919 109.476 1.00 30.49 ?  362 ASP A CG    1 
ATOM   2940  O  OD1   . ASP A 1 362 ? 155.268 143.452 110.405 1.00 27.74 ?  362 ASP A OD1   1 
ATOM   2941  O  OD2   . ASP A 1 362 ? 157.093 144.412 109.654 1.00 34.52 -1 362 ASP A OD2   1 
ATOM   2942  N  N     . ASN A 1 363 ? 152.820 143.398 106.103 1.00 18.08 ?  363 ASN A N     1 
ATOM   2943  C  CA    . ASN A 1 363 ? 152.204 143.436 104.780 1.00 10.98 ?  363 ASN A CA    1 
ATOM   2944  C  C     . ASN A 1 363 ? 151.120 144.504 104.714 1.00 13.44 ?  363 ASN A C     1 
ATOM   2945  O  O     . ASN A 1 363 ? 150.952 145.169 103.685 1.00 21.41 ?  363 ASN A O     1 
ATOM   2946  C  CB    . ASN A 1 363 ? 151.631 142.064 104.426 1.00 11.67 ?  363 ASN A CB    1 
ATOM   2947  C  CG    . ASN A 1 363 ? 152.689 141.101 103.934 1.00 18.13 ?  363 ASN A CG    1 
ATOM   2948  O  OD1   . ASN A 1 363 ? 153.823 141.492 103.663 1.00 19.36 ?  363 ASN A OD1   1 
ATOM   2949  N  ND2   . ASN A 1 363 ? 152.322 139.832 103.813 1.00 18.77 ?  363 ASN A ND2   1 
ATOM   2950  N  N     . VAL A 1 364 ? 150.368 144.677 105.801 1.00 9.09  ?  364 VAL A N     1 
ATOM   2951  C  CA    . VAL A 1 364 ? 149.351 145.722 105.846 1.00 10.59 ?  364 VAL A CA    1 
ATOM   2952  C  C     . VAL A 1 364 ? 150.001 147.099 105.915 1.00 17.38 ?  364 VAL A C     1 
ATOM   2953  O  O     . VAL A 1 364 ? 149.595 148.032 105.212 1.00 16.12 ?  364 VAL A O     1 
ATOM   2954  C  CB    . VAL A 1 364 ? 148.401 145.495 107.035 1.00 1.48  ?  364 VAL A CB    1 
ATOM   2955  C  CG1   . VAL A 1 364 ? 147.296 146.535 107.030 1.00 4.43  ?  364 VAL A CG1   1 
ATOM   2956  C  CG2   . VAL A 1 364 ? 147.826 144.094 107.001 1.00 8.10  ?  364 VAL A CG2   1 
ATOM   2957  N  N     . ASN A 1 365 ? 151.021 147.246 106.758 1.00 21.00 ?  365 ASN A N     1 
ATOM   2958  C  CA    . ASN A 1 365 ? 151.539 148.562 107.109 1.00 11.91 ?  365 ASN A CA    1 
ATOM   2959  C  C     . ASN A 1 365 ? 152.615 149.080 106.163 1.00 15.26 ?  365 ASN A C     1 
ATOM   2960  O  O     . ASN A 1 365 ? 152.936 150.272 106.222 1.00 21.76 ?  365 ASN A O     1 
ATOM   2961  C  CB    . ASN A 1 365 ? 152.083 148.542 108.540 1.00 13.85 ?  365 ASN A CB    1 
ATOM   2962  C  CG    . ASN A 1 365 ? 150.981 148.510 109.576 1.00 15.71 ?  365 ASN A CG    1 
ATOM   2963  O  OD1   . ASN A 1 365 ? 150.094 149.363 109.581 1.00 12.41 ?  365 ASN A OD1   1 
ATOM   2964  N  ND2   . ASN A 1 365 ? 151.026 147.520 110.458 1.00 18.99 ?  365 ASN A ND2   1 
ATOM   2965  N  N     . LYS A 1 366 ? 153.176 148.239 105.294 1.00 19.00 ?  366 LYS A N     1 
ATOM   2966  C  CA    . LYS A 1 366 ? 154.127 148.728 104.307 1.00 15.84 ?  366 LYS A CA    1 
ATOM   2967  C  C     . LYS A 1 366 ? 153.447 149.439 103.148 1.00 19.99 ?  366 LYS A C     1 
ATOM   2968  O  O     . LYS A 1 366 ? 154.117 150.159 102.402 1.00 29.30 ?  366 LYS A O     1 
ATOM   2969  C  CB    . LYS A 1 366 ? 154.983 147.572 103.782 1.00 13.23 ?  366 LYS A CB    1 
ATOM   2970  C  CG    . LYS A 1 366 ? 154.336 146.761 102.675 1.00 19.82 ?  366 LYS A CG    1 
ATOM   2971  C  CD    . LYS A 1 366 ? 154.886 145.344 102.647 1.00 23.35 ?  366 LYS A CD    1 
ATOM   2972  C  CE    . LYS A 1 366 ? 154.145 144.480 101.640 1.00 26.32 ?  366 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A 1 366 ? 152.684 144.768 101.619 1.00 25.54 1  366 LYS A NZ    1 
ATOM   2974  N  N     . VAL A 1 367 ? 152.138 149.253 102.988 1.00 25.26 ?  367 VAL A N     1 
ATOM   2975  C  CA    . VAL A 1 367 ? 151.342 149.976 102.007 1.00 15.02 ?  367 VAL A CA    1 
ATOM   2976  C  C     . VAL A 1 367 ? 150.247 150.803 102.655 1.00 14.05 ?  367 VAL A C     1 
ATOM   2977  O  O     . VAL A 1 367 ? 149.442 151.410 101.944 1.00 18.32 ?  367 VAL A O     1 
ATOM   2978  C  CB    . VAL A 1 367 ? 150.740 149.017 100.961 1.00 13.12 ?  367 VAL A CB    1 
ATOM   2979  C  CG1   . VAL A 1 367 ? 151.798 148.608 99.951  1.00 17.27 ?  367 VAL A CG1   1 
ATOM   2980  C  CG2   . VAL A 1 367 ? 150.161 147.796 101.646 1.00 4.98  ?  367 VAL A CG2   1 
ATOM   2981  N  N     . HIS A 1 368 ? 150.193 150.844 103.984 1.00 14.46 ?  368 HIS A N     1 
ATOM   2982  C  CA    . HIS A 1 368 ? 149.196 151.642 104.683 1.00 6.03  ?  368 HIS A CA    1 
ATOM   2983  C  C     . HIS A 1 368 ? 149.463 153.125 104.459 1.00 15.52 ?  368 HIS A C     1 
ATOM   2984  O  O     . HIS A 1 368 ? 150.582 153.604 104.659 1.00 25.03 ?  368 HIS A O     1 
ATOM   2985  C  CB    . HIS A 1 368 ? 149.218 151.316 106.174 1.00 12.53 ?  368 HIS A CB    1 
ATOM   2986  C  CG    . HIS A 1 368 ? 148.093 151.930 106.945 1.00 8.17  ?  368 HIS A CG    1 
ATOM   2987  N  ND1   . HIS A 1 368 ? 148.248 152.408 108.229 1.00 13.52 ?  368 HIS A ND1   1 
ATOM   2988  C  CD2   . HIS A 1 368 ? 146.798 152.144 106.619 1.00 10.74 ?  368 HIS A CD2   1 
ATOM   2989  C  CE1   . HIS A 1 368 ? 147.096 152.889 108.658 1.00 15.09 ?  368 HIS A CE1   1 
ATOM   2990  N  NE2   . HIS A 1 368 ? 146.199 152.741 107.700 1.00 7.25  ?  368 HIS A NE2   1 
ATOM   2991  N  N     . ALA A 1 369 ? 148.426 153.852 104.042 1.00 18.25 ?  369 ALA A N     1 
ATOM   2992  C  CA    . ALA A 1 369 ? 148.580 155.265 103.735 1.00 12.50 ?  369 ALA A CA    1 
ATOM   2993  C  C     . ALA A 1 369 ? 148.495 156.157 104.965 1.00 17.79 ?  369 ALA A C     1 
ATOM   2994  O  O     . ALA A 1 369 ? 148.916 157.315 104.900 1.00 25.01 ?  369 ALA A O     1 
ATOM   2995  C  CB    . ALA A 1 369 ? 147.522 155.698 102.720 1.00 8.96  ?  369 ALA A CB    1 
ATOM   2996  N  N     . ASN A 1 370 ? 147.977 155.649 106.079 1.00 17.23 ?  370 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 370 ? 147.734 156.450 107.270 1.00 12.34 ?  370 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 370 ? 148.508 155.913 108.466 1.00 12.14 ?  370 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 370 ? 147.980 155.810 109.575 1.00 21.21 ?  370 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 370 ? 146.241 156.515 107.581 1.00 12.21 ?  370 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 370 ? 145.436 157.082 106.433 1.00 10.47 ?  370 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 370 ? 145.654 158.215 106.007 1.00 26.58 ?  370 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 370 ? 144.500 156.295 105.921 1.00 12.40 ?  370 ASN A ND2   1 
ATOM   3004  N  N     . ASN A 1 371 ? 149.778 155.562 108.254 1.00 14.37 ?  371 ASN A N     1 
ATOM   3005  C  CA    . ASN A 1 371 ? 150.621 155.124 109.360 1.00 11.15 ?  371 ASN A CA    1 
ATOM   3006  C  C     . ASN A 1 371 ? 150.912 156.248 110.343 1.00 16.52 ?  371 ASN A C     1 
ATOM   3007  O  O     . ASN A 1 371 ? 151.206 155.972 111.510 1.00 19.08 ?  371 ASN A O     1 
ATOM   3008  C  CB    . ASN A 1 371 ? 151.932 154.545 108.829 1.00 8.50  ?  371 ASN A CB    1 
ATOM   3009  C  CG    . ASN A 1 371 ? 151.813 153.082 108.463 1.00 16.56 ?  371 ASN A CG    1 
ATOM   3010  O  OD1   . ASN A 1 371 ? 150.947 152.372 108.973 1.00 20.95 ?  371 ASN A OD1   1 
ATOM   3011  N  ND2   . ASN A 1 371 ? 152.685 152.621 107.575 1.00 18.37 ?  371 ASN A ND2   1 
ATOM   3012  N  N     . HIS A 1 372 ? 150.849 157.505 109.895 1.00 19.53 ?  372 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 372 ? 151.050 158.628 110.805 1.00 15.92 ?  372 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 372 ? 149.962 158.676 111.869 1.00 16.49 ?  372 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 372 ? 150.244 158.943 113.043 1.00 25.78 ?  372 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 372 ? 151.094 159.937 110.017 1.00 18.05 ?  372 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 372 ? 149.792 160.294 109.370 1.00 18.35 ?  372 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 372 ? 149.200 159.508 108.407 1.00 23.68 ?  372 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 372 ? 148.964 161.348 109.557 1.00 18.43 ?  372 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 372 ? 148.064 160.063 108.026 1.00 17.06 ?  372 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 372 ? 147.899 161.182 108.705 1.00 17.38 ?  372 HIS A NE2   1 
ATOM   3022  N  N     . ILE A 1 373 ? 148.710 158.434 111.476 1.00 16.32 ?  373 ILE A N     1 
ATOM   3023  C  CA    . ILE A 1 373 ? 147.627 158.359 112.453 1.00 18.68 ?  373 ILE A CA    1 
ATOM   3024  C  C     . ILE A 1 373 ? 147.851 157.184 113.391 1.00 15.16 ?  373 ILE A C     1 
ATOM   3025  O  O     . ILE A 1 373 ? 147.837 157.330 114.620 1.00 28.13 ?  373 ILE A O     1 
ATOM   3026  C  CB    . ILE A 1 373 ? 146.268 158.248 111.738 1.00 19.22 ?  373 ILE A CB    1 
ATOM   3027  C  CG1   . ILE A 1 373 ? 146.041 159.450 110.825 1.00 15.45 ?  373 ILE A CG1   1 
ATOM   3028  C  CG2   . ILE A 1 373 ? 145.140 158.114 112.749 1.00 19.60 ?  373 ILE A CG2   1 
ATOM   3029  C  CD1   . ILE A 1 373 ? 144.888 159.278 109.868 1.00 15.20 ?  373 ILE A CD1   1 
ATOM   3030  N  N     . SER A 1 374 ? 148.089 156.006 112.818 1.00 16.92 ?  374 SER A N     1 
ATOM   3031  C  CA    . SER A 1 374 ? 148.333 154.780 113.564 1.00 12.66 ?  374 SER A CA    1 
ATOM   3032  C  C     . SER A 1 374 ? 148.670 153.661 112.591 1.00 14.27 ?  374 SER A C     1 
ATOM   3033  O  O     . SER A 1 374 ? 148.268 153.707 111.425 1.00 21.20 ?  374 SER A O     1 
ATOM   3034  C  CB    . SER A 1 374 ? 147.115 154.398 114.405 1.00 19.05 ?  374 SER A CB    1 
ATOM   3035  O  OG    . SER A 1 374 ? 147.437 153.375 115.328 1.00 24.05 ?  374 SER A OG    1 
ATOM   3036  N  N     . LYS A 1 375 ? 149.406 152.658 113.048 1.00 22.39 ?  375 LYS A N     1 
ATOM   3037  C  CA    . LYS A 1 375 ? 149.576 151.456 112.251 1.00 19.34 ?  375 LYS A CA    1 
ATOM   3038  C  C     . LYS A 1 375 ? 148.387 150.529 112.460 1.00 15.28 ?  375 LYS A C     1 
ATOM   3039  O  O     . LYS A 1 375 ? 147.779 150.496 113.534 1.00 22.44 ?  375 LYS A O     1 
ATOM   3040  C  CB    . LYS A 1 375 ? 150.879 150.744 112.611 1.00 12.06 ?  375 LYS A CB    1 
ATOM   3041  C  CG    . LYS A 1 375 ? 152.112 151.409 112.025 1.00 16.85 ?  375 LYS A CG    1 
ATOM   3042  C  CD    . LYS A 1 375 ? 153.296 150.462 111.995 1.00 24.65 ?  375 LYS A CD    1 
ATOM   3043  C  CE    . LYS A 1 375 ? 154.464 151.077 111.246 1.00 24.19 ?  375 LYS A CE    1 
ATOM   3044  N  NZ    . LYS A 1 375 ? 155.578 150.110 111.056 1.00 29.43 1  375 LYS A NZ    1 
ATOM   3045  N  N     . VAL A 1 376 ? 148.042 149.786 111.413 1.00 15.10 ?  376 VAL A N     1 
ATOM   3046  C  CA    . VAL A 1 376 ? 146.928 148.847 111.489 1.00 15.74 ?  376 VAL A CA    1 
ATOM   3047  C  C     . VAL A 1 376 ? 147.339 147.705 112.414 1.00 13.96 ?  376 VAL A C     1 
ATOM   3048  O  O     . VAL A 1 376 ? 148.235 146.922 112.088 1.00 20.44 ?  376 VAL A O     1 
ATOM   3049  C  CB    . VAL A 1 376 ? 146.529 148.331 110.104 1.00 10.94 ?  376 VAL A CB    1 
ATOM   3050  C  CG1   . VAL A 1 376 ? 145.324 147.416 110.209 1.00 8.26  ?  376 VAL A CG1   1 
ATOM   3051  C  CG2   . VAL A 1 376 ? 146.243 149.494 109.170 1.00 3.91  ?  376 VAL A CG2   1 
ATOM   3052  N  N     . LYS A 1 377 ? 146.689 147.612 113.573 1.00 12.77 ?  377 LYS A N     1 
ATOM   3053  C  CA    . LYS A 1 377 ? 147.045 146.617 114.572 1.00 11.43 ?  377 LYS A CA    1 
ATOM   3054  C  C     . LYS A 1 377 ? 146.186 145.364 114.513 1.00 10.48 ?  377 LYS A C     1 
ATOM   3055  O  O     . LYS A 1 377 ? 146.609 144.324 115.022 1.00 24.90 ?  377 LYS A O     1 
ATOM   3056  C  CB    . LYS A 1 377 ? 146.943 147.211 115.981 1.00 15.92 ?  377 LYS A CB    1 
ATOM   3057  C  CG    . LYS A 1 377 ? 147.708 148.501 116.178 1.00 12.28 ?  377 LYS A CG    1 
ATOM   3058  C  CD    . LYS A 1 377 ? 147.016 149.361 117.214 1.00 21.26 ?  377 LYS A CD    1 
ATOM   3059  C  CE    . LYS A 1 377 ? 147.443 150.806 117.110 1.00 23.69 ?  377 LYS A CE    1 
ATOM   3060  N  NZ    . LYS A 1 377 ? 146.462 151.715 117.763 1.00 26.00 1  377 LYS A NZ    1 
ATOM   3061  N  N     . PHE A 1 378 ? 144.999 145.439 113.918 1.00 8.60  ?  378 PHE A N     1 
ATOM   3062  C  CA    . PHE A 1 378 ? 144.098 144.297 113.869 1.00 7.85  ?  378 PHE A CA    1 
ATOM   3063  C  C     . PHE A 1 378 ? 143.079 144.527 112.764 1.00 8.00  ?  378 PHE A C     1 
ATOM   3064  O  O     . PHE A 1 378 ? 143.021 145.598 112.157 1.00 15.64 ?  378 PHE A O     1 
ATOM   3065  C  CB    . PHE A 1 378 ? 143.420 144.059 115.225 1.00 6.52  ?  378 PHE A CB    1 
ATOM   3066  C  CG    . PHE A 1 378 ? 142.399 145.098 115.598 1.00 8.31  ?  378 PHE A CG    1 
ATOM   3067  C  CD1   . PHE A 1 378 ? 142.754 146.431 115.730 1.00 9.59  ?  378 PHE A CD1   1 
ATOM   3068  C  CD2   . PHE A 1 378 ? 141.086 144.735 115.843 1.00 5.15  ?  378 PHE A CD2   1 
ATOM   3069  C  CE1   . PHE A 1 378 ? 141.819 147.380 116.080 1.00 4.02  ?  378 PHE A CE1   1 
ATOM   3070  C  CE2   . PHE A 1 378 ? 140.148 145.682 116.192 1.00 9.56  ?  378 PHE A CE2   1 
ATOM   3071  C  CZ    . PHE A 1 378 ? 140.516 147.005 116.313 1.00 11.53 ?  378 PHE A CZ    1 
ATOM   3072  N  N     . SER A 1 379 ? 142.279 143.500 112.508 1.00 3.31  ?  379 SER A N     1 
ATOM   3073  C  CA    . SER A 1 379 ? 141.290 143.507 111.439 1.00 4.14  ?  379 SER A CA    1 
ATOM   3074  C  C     . SER A 1 379 ? 139.896 143.309 112.032 1.00 5.96  ?  379 SER A C     1 
ATOM   3075  O  O     . SER A 1 379 ? 139.709 143.311 113.250 1.00 12.37 ?  379 SER A O     1 
ATOM   3076  C  CB    . SER A 1 379 ? 141.621 142.436 110.398 1.00 5.03  ?  379 SER A CB    1 
ATOM   3077  O  OG    . SER A 1 379 ? 141.084 142.778 109.134 1.00 8.38  ?  379 SER A OG    1 
ATOM   3078  N  N     . ASN A 1 380 ? 138.914 143.142 111.153 1.00 11.92 ?  380 ASN A N     1 
ATOM   3079  C  CA    . ASN A 1 380 ? 137.523 143.024 111.551 1.00 9.17  ?  380 ASN A CA    1 
ATOM   3080  C  C     . ASN A 1 380 ? 137.136 141.554 111.697 1.00 9.46  ?  380 ASN A C     1 
ATOM   3081  O  O     . ASN A 1 380 ? 137.976 140.652 111.634 1.00 9.92  ?  380 ASN A O     1 
ATOM   3082  C  CB    . ASN A 1 380 ? 136.625 143.746 110.546 1.00 2.71  ?  380 ASN A CB    1 
ATOM   3083  C  CG    . ASN A 1 380 ? 136.563 143.044 109.209 1.00 3.90  ?  380 ASN A CG    1 
ATOM   3084  O  OD1   . ASN A 1 380 ? 137.590 142.722 108.614 1.00 12.64 ?  380 ASN A OD1   1 
ATOM   3085  N  ND2   . ASN A 1 380 ? 135.352 142.800 108.726 1.00 10.73 ?  380 ASN A ND2   1 
ATOM   3086  N  N     . LEU A 1 381 ? 135.840 141.311 111.902 1.00 17.84 ?  381 LEU A N     1 
ATOM   3087  C  CA    . LEU A 1 381 ? 135.328 139.951 112.016 1.00 6.52  ?  381 LEU A CA    1 
ATOM   3088  C  C     . LEU A 1 381 ? 135.484 139.165 110.720 1.00 6.70  ?  381 LEU A C     1 
ATOM   3089  O  O     . LEU A 1 381 ? 135.600 137.936 110.766 1.00 15.30 ?  381 LEU A O     1 
ATOM   3090  C  CB    . LEU A 1 381 ? 133.860 139.996 112.443 1.00 11.71 ?  381 LEU A CB    1 
ATOM   3091  C  CG    . LEU A 1 381 ? 133.038 138.707 112.489 1.00 20.37 ?  381 LEU A CG    1 
ATOM   3092  C  CD1   . LEU A 1 381 ? 133.565 137.755 113.547 1.00 14.47 ?  381 LEU A CD1   1 
ATOM   3093  C  CD2   . LEU A 1 381 ? 131.576 139.031 112.735 1.00 15.89 ?  381 LEU A CD2   1 
ATOM   3094  N  N     . CYS A 1 382 ? 135.498 139.839 109.574 1.00 8.83  ?  382 CYS A N     1 
ATOM   3095  C  CA    . CYS A 1 382 ? 135.693 139.190 108.286 1.00 6.39  ?  382 CYS A CA    1 
ATOM   3096  C  C     . CYS A 1 382 ? 137.120 139.319 107.771 1.00 10.63 ?  382 CYS A C     1 
ATOM   3097  O  O     . CYS A 1 382 ? 137.413 138.836 106.672 1.00 17.01 ?  382 CYS A O     1 
ATOM   3098  C  CB    . CYS A 1 382 ? 134.714 139.760 107.255 1.00 15.57 ?  382 CYS A CB    1 
ATOM   3099  S  SG    . CYS A 1 382 ? 132.976 139.666 107.748 1.00 35.34 ?  382 CYS A SG    1 
ATOM   3100  N  N     . SER A 1 383 ? 138.007 139.955 108.538 1.00 11.05 ?  383 SER A N     1 
ATOM   3101  C  CA    . SER A 1 383 ? 139.433 140.050 108.218 1.00 8.94  ?  383 SER A CA    1 
ATOM   3102  C  C     . SER A 1 383 ? 139.674 140.709 106.861 1.00 12.51 ?  383 SER A C     1 
ATOM   3103  O  O     . SER A 1 383 ? 140.472 140.232 106.054 1.00 22.80 ?  383 SER A O     1 
ATOM   3104  C  CB    . SER A 1 383 ? 140.104 138.677 108.278 1.00 12.13 ?  383 SER A CB    1 
ATOM   3105  O  OG    . SER A 1 383 ? 139.788 137.910 107.131 1.00 20.92 ?  383 SER A OG    1 
ATOM   3106  N  N     . GLU A 1 384 ? 138.977 141.814 106.600 1.00 8.02  ?  384 GLU A N     1 
ATOM   3107  C  CA    . GLU A 1 384 ? 139.247 142.612 105.412 1.00 11.46 ?  384 GLU A CA    1 
ATOM   3108  C  C     . GLU A 1 384 ? 139.334 144.106 105.686 1.00 13.32 ?  384 GLU A C     1 
ATOM   3109  O  O     . GLU A 1 384 ? 139.836 144.840 104.827 1.00 22.51 ?  384 GLU A O     1 
ATOM   3110  C  CB    . GLU A 1 384 ? 138.188 142.348 104.327 1.00 6.55  ?  384 GLU A CB    1 
ATOM   3111  C  CG    . GLU A 1 384 ? 137.146 143.437 104.124 1.00 7.25  ?  384 GLU A CG    1 
ATOM   3112  C  CD    . GLU A 1 384 ? 136.016 143.365 105.125 1.00 16.76 ?  384 GLU A CD    1 
ATOM   3113  O  OE1   . GLU A 1 384 ? 135.865 142.313 105.777 1.00 19.97 ?  384 GLU A OE1   1 
ATOM   3114  O  OE2   . GLU A 1 384 ? 135.264 144.353 105.245 1.00 21.02 -1 384 GLU A OE2   1 
ATOM   3115  N  N     . VAL A 1 385 ? 138.890 144.576 106.845 1.00 13.29 ?  385 VAL A N     1 
ATOM   3116  C  CA    . VAL A 1 385 ? 139.012 145.982 107.211 1.00 3.12  ?  385 VAL A CA    1 
ATOM   3117  C  C     . VAL A 1 385 ? 140.363 146.185 107.881 1.00 15.14 ?  385 VAL A C     1 
ATOM   3118  O  O     . VAL A 1 385 ? 140.651 145.575 108.916 1.00 19.40 ?  385 VAL A O     1 
ATOM   3119  C  CB    . VAL A 1 385 ? 137.869 146.420 108.136 1.00 3.77  ?  385 VAL A CB    1 
ATOM   3120  C  CG1   . VAL A 1 385 ? 137.998 147.889 108.455 1.00 10.14 ?  385 VAL A CG1   1 
ATOM   3121  C  CG2   . VAL A 1 385 ? 136.532 146.138 107.493 1.00 8.54  ?  385 VAL A CG2   1 
ATOM   3122  N  N     . LEU A 1 386 ? 141.195 147.040 107.290 1.00 16.86 ?  386 LEU A N     1 
ATOM   3123  C  CA    . LEU A 1 386 ? 142.540 147.310 107.789 1.00 3.54  ?  386 LEU A CA    1 
ATOM   3124  C  C     . LEU A 1 386 ? 142.739 148.821 107.821 1.00 7.34  ?  386 LEU A C     1 
ATOM   3125  O  O     . LEU A 1 386 ? 143.068 149.433 106.801 1.00 8.00  ?  386 LEU A O     1 
ATOM   3126  C  CB    . LEU A 1 386 ? 143.590 146.626 106.924 1.00 3.17  ?  386 LEU A CB    1 
ATOM   3127  C  CG    . LEU A 1 386 ? 143.492 145.103 106.929 1.00 7.86  ?  386 LEU A CG    1 
ATOM   3128  C  CD1   . LEU A 1 386 ? 144.419 144.521 105.901 1.00 9.37  ?  386 LEU A CD1   1 
ATOM   3129  C  CD2   . LEU A 1 386 ? 143.808 144.559 108.309 1.00 6.77  ?  386 LEU A CD2   1 
ATOM   3130  N  N     . GLN A 1 387 ? 142.541 149.417 108.994 1.00 14.69 ?  387 GLN A N     1 
ATOM   3131  C  CA    . GLN A 1 387 ? 142.572 150.862 109.139 1.00 4.40  ?  387 GLN A CA    1 
ATOM   3132  C  C     . GLN A 1 387 ? 143.345 151.242 110.391 1.00 6.85  ?  387 GLN A C     1 
ATOM   3133  O  O     . GLN A 1 387 ? 143.536 150.435 111.303 1.00 18.95 ?  387 GLN A O     1 
ATOM   3134  C  CB    . GLN A 1 387 ? 141.158 151.451 109.204 1.00 6.31  ?  387 GLN A CB    1 
ATOM   3135  C  CG    . GLN A 1 387 ? 140.288 151.087 108.024 1.00 8.48  ?  387 GLN A CG    1 
ATOM   3136  C  CD    . GLN A 1 387 ? 138.995 151.857 108.009 1.00 6.84  ?  387 GLN A CD    1 
ATOM   3137  O  OE1   . GLN A 1 387 ? 138.806 152.789 108.787 1.00 19.59 ?  387 GLN A OE1   1 
ATOM   3138  N  NE2   . GLN A 1 387 ? 138.098 151.480 107.113 1.00 8.43  ?  387 GLN A NE2   1 
ATOM   3139  N  N     . ALA A 1 388 ? 143.804 152.489 110.413 1.00 10.17 ?  388 ALA A N     1 
ATOM   3140  C  CA    . ALA A 1 388 ? 144.445 153.033 111.601 1.00 9.47  ?  388 ALA A CA    1 
ATOM   3141  C  C     . ALA A 1 388 ? 143.425 153.208 112.717 1.00 14.32 ?  388 ALA A C     1 
ATOM   3142  O  O     . ALA A 1 388 ? 142.307 153.678 112.492 1.00 25.46 ?  388 ALA A O     1 
ATOM   3143  C  CB    . ALA A 1 388 ? 145.108 154.371 111.280 1.00 12.02 ?  388 ALA A CB    1 
ATOM   3144  N  N     . SER A 1 389 ? 143.813 152.819 113.928 1.00 17.96 ?  389 SER A N     1 
ATOM   3145  C  CA    . SER A 1 389 ? 142.954 152.959 115.093 1.00 8.83  ?  389 SER A CA    1 
ATOM   3146  C  C     . SER A 1 389 ? 143.772 153.479 116.263 1.00 13.12 ?  389 SER A C     1 
ATOM   3147  O  O     . SER A 1 389 ? 144.930 153.094 116.441 1.00 24.46 ?  389 SER A O     1 
ATOM   3148  C  CB    . SER A 1 389 ? 142.293 151.628 115.468 1.00 16.70 ?  389 SER A CB    1 
ATOM   3149  O  OG    . SER A 1 389 ? 143.219 150.559 115.395 1.00 21.83 ?  389 SER A OG    1 
ATOM   3150  N  N     . GLN A 1 390 ? 143.162 154.353 117.057 1.00 17.64 ?  390 GLN A N     1 
ATOM   3151  C  CA    . GLN A 1 390 ? 143.772 154.880 118.269 1.00 14.92 ?  390 GLN A CA    1 
ATOM   3152  C  C     . GLN A 1 390 ? 142.949 154.429 119.464 1.00 13.36 ?  390 GLN A C     1 
ATOM   3153  O  O     . GLN A 1 390 ? 141.724 154.577 119.468 1.00 17.32 ?  390 GLN A O     1 
ATOM   3154  C  CB    . GLN A 1 390 ? 143.865 156.407 118.226 1.00 10.33 ?  390 GLN A CB    1 
ATOM   3155  C  CG    . GLN A 1 390 ? 144.922 156.933 117.271 1.00 15.85 ?  390 GLN A CG    1 
ATOM   3156  C  CD    . GLN A 1 390 ? 144.794 158.421 117.020 1.00 25.93 ?  390 GLN A CD    1 
ATOM   3157  O  OE1   . GLN A 1 390 ? 143.835 159.056 117.457 1.00 24.72 ?  390 GLN A OE1   1 
ATOM   3158  N  NE2   . GLN A 1 390 ? 145.762 158.985 116.307 1.00 21.61 ?  390 GLN A NE2   1 
ATOM   3159  N  N     . VAL A 1 391 ? 143.624 153.874 120.471 1.00 24.05 ?  391 VAL A N     1 
ATOM   3160  C  CA    . VAL A 1 391 ? 142.926 153.375 121.647 1.00 20.62 ?  391 VAL A CA    1 
ATOM   3161  C  C     . VAL A 1 391 ? 142.345 154.541 122.438 1.00 22.62 ?  391 VAL A C     1 
ATOM   3162  O  O     . VAL A 1 391 ? 142.861 155.667 122.413 1.00 24.03 ?  391 VAL A O     1 
ATOM   3163  C  CB    . VAL A 1 391 ? 143.865 152.516 122.515 1.00 19.09 ?  391 VAL A CB    1 
ATOM   3164  C  CG1   . VAL A 1 391 ? 144.769 153.392 123.371 1.00 20.19 ?  391 VAL A CG1   1 
ATOM   3165  C  CG2   . VAL A 1 391 ? 143.064 151.554 123.378 1.00 17.61 ?  391 VAL A CG2   1 
ATOM   3166  N  N     . SER A 1 392 ? 141.244 154.276 123.130 1.00 27.56 ?  392 SER A N     1 
ATOM   3167  C  CA    . SER A 1 392 ? 140.590 155.264 123.972 1.00 19.89 ?  392 SER A CA    1 
ATOM   3168  C  C     . SER A 1 392 ? 140.894 154.983 125.436 1.00 29.15 ?  392 SER A C     1 
ATOM   3169  O  O     . SER A 1 392 ? 141.039 153.831 125.852 1.00 29.80 ?  392 SER A O     1 
ATOM   3170  C  CB    . SER A 1 392 ? 139.078 155.263 123.745 1.00 20.67 ?  392 SER A CB    1 
ATOM   3171  O  OG    . SER A 1 392 ? 138.762 155.516 122.388 1.00 27.89 ?  392 SER A OG    1 
ATOM   3172  N  N     . SER A 1 393 ? 140.996 156.053 126.216 1.00 31.70 ?  393 SER A N     1 
ATOM   3173  C  CA    . SER A 1 393 ? 141.233 155.965 127.654 1.00 28.10 ?  393 SER A CA    1 
ATOM   3174  C  C     . SER A 1 393 ? 139.910 156.264 128.352 1.00 30.16 ?  393 SER A C     1 
ATOM   3175  O  O     . SER A 1 393 ? 139.592 157.417 128.649 1.00 34.98 ?  393 SER A O     1 
ATOM   3176  C  CB    . SER A 1 393 ? 142.331 156.927 128.093 1.00 30.37 ?  393 SER A CB    1 
ATOM   3177  O  OG    . SER A 1 393 ? 143.610 156.434 127.740 1.00 36.82 ?  393 SER A OG    1 
ATOM   3178  N  N     . TYR A 1 394 ? 139.135 155.214 128.604 1.00 29.20 ?  394 TYR A N     1 
ATOM   3179  C  CA    . TYR A 1 394 ? 137.877 155.346 129.326 1.00 28.90 ?  394 TYR A CA    1 
ATOM   3180  C  C     . TYR A 1 394 ? 138.178 155.347 130.819 1.00 28.85 ?  394 TYR A C     1 
ATOM   3181  O  O     . TYR A 1 394 ? 138.531 154.311 131.389 1.00 33.55 ?  394 TYR A O     1 
ATOM   3182  C  CB    . TYR A 1 394 ? 136.924 154.217 128.949 1.00 24.98 ?  394 TYR A CB    1 
ATOM   3183  C  CG    . TYR A 1 394 ? 136.410 154.307 127.531 1.00 28.24 ?  394 TYR A CG    1 
ATOM   3184  C  CD1   . TYR A 1 394 ? 135.459 155.254 127.175 1.00 29.50 ?  394 TYR A CD1   1 
ATOM   3185  C  CD2   . TYR A 1 394 ? 136.883 153.450 126.545 1.00 26.55 ?  394 TYR A CD2   1 
ATOM   3186  C  CE1   . TYR A 1 394 ? 134.987 155.339 125.881 1.00 28.34 ?  394 TYR A CE1   1 
ATOM   3187  C  CE2   . TYR A 1 394 ? 136.416 153.528 125.249 1.00 27.08 ?  394 TYR A CE2   1 
ATOM   3188  C  CZ    . TYR A 1 394 ? 135.469 154.475 124.922 1.00 36.10 ?  394 TYR A CZ    1 
ATOM   3189  O  OH    . TYR A 1 394 ? 135.004 154.557 123.630 1.00 38.36 ?  394 TYR A OH    1 
ATOM   3190  N  N     . THR A 1 395 ? 138.043 156.508 131.448 1.00 35.82 ?  395 THR A N     1 
ATOM   3191  C  CA    . THR A 1 395 ? 138.409 156.684 132.844 1.00 37.45 ?  395 THR A CA    1 
ATOM   3192  C  C     . THR A 1 395 ? 137.239 156.292 133.745 1.00 38.54 ?  395 THR A C     1 
ATOM   3193  O  O     . THR A 1 395 ? 136.254 155.695 133.303 1.00 38.57 ?  395 THR A O     1 
ATOM   3194  C  CB    . THR A 1 395 ? 138.856 158.123 133.089 1.00 36.92 ?  395 THR A CB    1 
ATOM   3195  O  OG1   . THR A 1 395 ? 137.801 159.020 132.721 1.00 38.62 ?  395 THR A OG1   1 
ATOM   3196  C  CG2   . THR A 1 395 ? 140.092 158.441 132.264 1.00 35.25 ?  395 THR A CG2   1 
ATOM   3197  N  N     . ASP A 1 396 ? 137.342 156.623 135.030 1.00 36.30 ?  396 ASP A N     1 
ATOM   3198  C  CA    . ASP A 1 396 ? 136.278 156.340 135.979 1.00 36.61 ?  396 ASP A CA    1 
ATOM   3199  C  C     . ASP A 1 396 ? 135.057 157.207 135.673 1.00 38.06 ?  396 ASP A C     1 
ATOM   3200  O  O     . ASP A 1 396 ? 135.049 158.018 134.742 1.00 42.28 ?  396 ASP A O     1 
ATOM   3201  C  CB    . ASP A 1 396 ? 136.761 156.579 137.408 1.00 38.06 ?  396 ASP A CB    1 
ATOM   3202  C  CG    . ASP A 1 396 ? 138.014 155.795 137.743 1.00 42.51 ?  396 ASP A CG    1 
ATOM   3203  O  OD1   . ASP A 1 396 ? 138.250 154.743 137.113 1.00 43.52 ?  396 ASP A OD1   1 
ATOM   3204  O  OD2   . ASP A 1 396 ? 138.761 156.230 138.643 1.00 44.02 -1 396 ASP A OD2   1 
ATOM   3205  N  N     . TYR A 1 397 ? 134.008 157.028 136.471 1.00 37.44 ?  397 TYR A N     1 
ATOM   3206  C  CA    . TYR A 1 397 ? 132.844 157.889 136.358 1.00 34.06 ?  397 TYR A CA    1 
ATOM   3207  C  C     . TYR A 1 397 ? 133.231 159.329 136.697 1.00 37.34 ?  397 TYR A C     1 
ATOM   3208  O  O     . TYR A 1 397 ? 134.326 159.602 137.185 1.00 39.74 ?  397 TYR A O     1 
ATOM   3209  C  CB    . TYR A 1 397 ? 131.721 157.395 137.268 1.00 33.65 ?  397 TYR A CB    1 
ATOM   3210  C  CG    . TYR A 1 397 ? 130.339 157.798 136.803 1.00 33.80 ?  397 TYR A CG    1 
ATOM   3211  C  CD1   . TYR A 1 397 ? 129.664 157.050 135.849 1.00 36.07 ?  397 TYR A CD1   1 
ATOM   3212  C  CD2   . TYR A 1 397 ? 129.710 158.924 137.320 1.00 34.56 ?  397 TYR A CD2   1 
ATOM   3213  C  CE1   . TYR A 1 397 ? 128.403 157.413 135.420 1.00 33.88 ?  397 TYR A CE1   1 
ATOM   3214  C  CE2   . TYR A 1 397 ? 128.452 159.294 136.897 1.00 31.84 ?  397 TYR A CE2   1 
ATOM   3215  C  CZ    . TYR A 1 397 ? 127.802 158.536 135.949 1.00 34.09 ?  397 TYR A CZ    1 
ATOM   3216  O  OH    . TYR A 1 397 ? 126.546 158.901 135.526 1.00 39.73 ?  397 TYR A OH    1 
ATOM   3217  N  N     . ASP A 1 398 ? 132.325 160.253 136.360 1.00 41.00 ?  398 ASP A N     1 
ATOM   3218  C  CA    . ASP A 1 398 ? 132.439 161.704 136.523 1.00 42.01 ?  398 ASP A CA    1 
ATOM   3219  C  C     . ASP A 1 398 ? 133.850 162.197 136.203 1.00 44.08 ?  398 ASP A C     1 
ATOM   3220  O  O     . ASP A 1 398 ? 134.347 163.153 136.807 1.00 41.83 ?  398 ASP A O     1 
ATOM   3221  C  CB    . ASP A 1 398 ? 131.944 162.157 137.917 1.00 41.67 ?  398 ASP A CB    1 
ATOM   3222  C  CG    . ASP A 1 398 ? 132.954 161.959 139.058 1.00 44.94 ?  398 ASP A CG    1 
ATOM   3223  O  OD1   . ASP A 1 398 ? 132.684 162.503 140.149 1.00 45.96 ?  398 ASP A OD1   1 
ATOM   3224  O  OD2   . ASP A 1 398 ? 133.998 161.306 138.908 1.00 42.18 -1 398 ASP A OD2   1 
ATOM   3225  N  N     . GLU A 1 399 ? 134.477 161.560 135.216 1.00 48.02 ?  399 GLU A N     1 
ATOM   3226  C  CA    . GLU A 1 399 ? 135.802 161.911 134.735 1.00 43.95 ?  399 GLU A CA    1 
ATOM   3227  C  C     . GLU A 1 399 ? 135.793 161.822 133.217 1.00 44.55 ?  399 GLU A C     1 
ATOM   3228  O  O     . GLU A 1 399 ? 135.239 160.876 132.648 1.00 42.49 ?  399 GLU A O     1 
ATOM   3229  C  CB    . GLU A 1 399 ? 136.874 160.982 135.319 1.00 39.19 ?  399 GLU A CB    1 
ATOM   3230  C  CG    . GLU A 1 399 ? 138.215 161.651 135.561 1.00 42.93 ?  399 GLU A CG    1 
ATOM   3231  C  CD    . GLU A 1 399 ? 139.344 160.652 135.722 1.00 48.39 ?  399 GLU A CD    1 
ATOM   3232  O  OE1   . GLU A 1 399 ? 139.105 159.567 136.291 1.00 47.56 ?  399 GLU A OE1   1 
ATOM   3233  O  OE2   . GLU A 1 399 ? 140.473 160.953 135.279 1.00 47.06 -1 399 GLU A OE2   1 
ATOM   3234  N  N     . GLU A 1 400 ? 136.401 162.808 132.566 1.00 44.73 ?  400 GLU A N     1 
ATOM   3235  C  CA    . GLU A 1 400 ? 136.340 162.888 131.113 1.00 40.43 ?  400 GLU A CA    1 
ATOM   3236  C  C     . GLU A 1 400 ? 137.162 161.776 130.476 1.00 43.83 ?  400 GLU A C     1 
ATOM   3237  O  O     . GLU A 1 400 ? 138.330 161.574 130.821 1.00 43.14 ?  400 GLU A O     1 
ATOM   3238  C  CB    . GLU A 1 400 ? 136.835 164.253 130.638 1.00 40.22 ?  400 GLU A CB    1 
ATOM   3239  C  CG    . GLU A 1 400 ? 135.989 164.871 129.536 1.00 45.83 ?  400 GLU A CG    1 
ATOM   3240  C  CD    . GLU A 1 400 ? 134.532 165.030 129.933 1.00 48.85 ?  400 GLU A CD    1 
ATOM   3241  O  OE1   . GLU A 1 400 ? 134.266 165.379 131.102 1.00 46.49 ?  400 GLU A OE1   1 
ATOM   3242  O  OE2   . GLU A 1 400 ? 133.653 164.807 129.075 1.00 47.21 -1 400 GLU A OE2   1 
ATOM   3243  N  N     . ASP A 1 401 ? 136.547 161.056 129.542 1.00 35.69 ?  401 ASP A N     1 
ATOM   3244  C  CA    . ASP A 1 401 ? 137.242 160.015 128.801 1.00 33.74 ?  401 ASP A CA    1 
ATOM   3245  C  C     . ASP A 1 401 ? 138.055 160.623 127.667 1.00 34.42 ?  401 ASP A C     1 
ATOM   3246  O  O     . ASP A 1 401 ? 137.712 161.677 127.122 1.00 38.08 ?  401 ASP A O     1 
ATOM   3247  C  CB    . ASP A 1 401 ? 136.249 159.000 128.234 1.00 32.53 ?  401 ASP A CB    1 
ATOM   3248  C  CG    . ASP A 1 401 ? 135.325 158.431 129.290 1.00 37.68 ?  401 ASP A CG    1 
ATOM   3249  O  OD1   . ASP A 1 401 ? 135.827 157.850 130.273 1.00 42.07 ?  401 ASP A OD1   1 
ATOM   3250  O  OD2   . ASP A 1 401 ? 134.094 158.563 129.133 1.00 38.40 -1 401 ASP A OD2   1 
ATOM   3251  N  N     . GLU A 1 402 ? 139.143 159.947 127.311 1.00 31.60 ?  402 GLU A N     1 
ATOM   3252  C  CA    . GLU A 1 402 ? 139.947 160.316 126.149 1.00 29.37 ?  402 GLU A CA    1 
ATOM   3253  C  C     . GLU A 1 402 ? 139.469 159.427 125.006 1.00 24.85 ?  402 GLU A C     1 
ATOM   3254  O  O     . GLU A 1 402 ? 139.778 158.235 124.959 1.00 30.34 ?  402 GLU A O     1 
ATOM   3255  C  CB    . GLU A 1 402 ? 141.439 160.154 126.435 1.00 31.18 ?  402 GLU A CB    1 
ATOM   3256  C  CG    . GLU A 1 402 ? 142.350 160.200 125.206 1.00 36.78 ?  402 GLU A CG    1 
ATOM   3257  C  CD    . GLU A 1 402 ? 142.622 158.836 124.596 1.00 40.42 ?  402 GLU A CD    1 
ATOM   3258  O  OE1   . GLU A 1 402 ? 143.295 158.012 125.248 1.00 35.31 ?  402 GLU A OE1   1 
ATOM   3259  O  OE2   . GLU A 1 402 ? 142.167 158.591 123.460 1.00 34.93 -1 402 GLU A OE2   1 
ATOM   3260  N  N     . ILE A 1 403 ? 138.683 160.003 124.104 1.00 27.50 ?  403 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 403 ? 138.073 159.238 123.025 1.00 26.57 ?  403 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 403 ? 139.063 159.117 121.874 1.00 28.07 ?  403 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 403 ? 139.577 160.123 121.372 1.00 28.44 ?  403 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 403 ? 136.761 159.893 122.567 1.00 24.55 ?  403 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 403 ? 135.766 159.962 123.726 1.00 24.49 ?  403 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 403 ? 136.163 159.129 121.398 1.00 20.31 ?  403 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 403 ? 135.565 158.647 124.443 1.00 26.84 ?  403 ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 404 ? 139.334 157.888 121.461 1.00 23.34 ?  404 GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 404 ? 140.222 157.595 120.358 1.00 9.27  ?  404 GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 404 ? 139.474 157.358 119.064 1.00 19.17 ?  404 GLY A C     1 
ATOM   3271  O  O     . GLY A 1 404 ? 138.409 157.937 118.817 1.00 31.31 ?  404 GLY A O     1 
ATOM   3272  N  N     . LEU A 1 405 ? 140.035 156.493 118.224 1.00 22.22 ?  405 LEU A N     1 
ATOM   3273  C  CA    . LEU A 1 405 ? 139.450 156.155 116.933 1.00 7.02  ?  405 LEU A CA    1 
ATOM   3274  C  C     . LEU A 1 405 ? 139.182 154.658 116.890 1.00 8.34  ?  405 LEU A C     1 
ATOM   3275  O  O     . LEU A 1 405 ? 140.109 153.854 117.028 1.00 18.34 ?  405 LEU A O     1 
ATOM   3276  C  CB    . LEU A 1 405 ? 140.376 156.566 115.786 1.00 17.23 ?  405 LEU A CB    1 
ATOM   3277  C  CG    . LEU A 1 405 ? 140.723 158.052 115.684 1.00 18.22 ?  405 LEU A CG    1 
ATOM   3278  C  CD1   . LEU A 1 405 ? 141.770 158.286 114.609 1.00 21.75 ?  405 LEU A CD1   1 
ATOM   3279  C  CD2   . LEU A 1 405 ? 139.478 158.879 115.413 1.00 15.48 ?  405 LEU A CD2   1 
ATOM   3280  N  N     . ASP A 1 406 ? 137.920 154.290 116.695 1.00 22.38 ?  406 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 406 ? 137.517 152.902 116.516 1.00 17.43 ?  406 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 406 ? 136.957 152.731 115.112 1.00 19.13 ?  406 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 406 ? 136.068 153.480 114.697 1.00 31.28 ?  406 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 406 ? 136.480 152.488 117.561 1.00 18.37 ?  406 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 406 ? 137.112 152.039 118.865 1.00 29.15 ?  406 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 406 ? 138.352 152.115 118.988 1.00 32.47 ?  406 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 406 ? 136.365 151.615 119.770 1.00 28.37 -1 406 ASP A OD2   1 
ATOM   3288  N  N     . ILE A 1 407 ? 137.465 151.739 114.397 1.00 21.24 ?  407 ILE A N     1 
ATOM   3289  C  CA    . ILE A 1 407 ? 137.200 151.605 112.971 1.00 15.66 ?  407 ILE A CA    1 
ATOM   3290  C  C     . ILE A 1 407 ? 135.774 151.129 112.741 1.00 14.81 ?  407 ILE A C     1 
ATOM   3291  O  O     . ILE A 1 407 ? 135.282 150.220 113.420 1.00 21.70 ?  407 ILE A O     1 
ATOM   3292  C  CB    . ILE A 1 407 ? 138.215 150.643 112.330 1.00 10.60 ?  407 ILE A CB    1 
ATOM   3293  C  CG1   . ILE A 1 407 ? 139.637 151.166 112.513 1.00 6.69  ?  407 ILE A CG1   1 
ATOM   3294  C  CG2   . ILE A 1 407 ? 137.899 150.443 110.870 1.00 16.52 ?  407 ILE A CG2   1 
ATOM   3295  C  CD1   . ILE A 1 407 ? 140.654 150.073 112.689 1.00 10.78 ?  407 ILE A CD1   1 
ATOM   3296  N  N     . SER A 1 408 ? 135.104 151.754 111.775 1.00 25.69 ?  408 SER A N     1 
ATOM   3297  C  CA    . SER A 1 408 ? 133.804 151.291 111.301 1.00 21.75 ?  408 SER A CA    1 
ATOM   3298  C  C     . SER A 1 408 ? 133.670 151.743 109.855 1.00 24.54 ?  408 SER A C     1 
ATOM   3299  O  O     . SER A 1 408 ? 133.307 152.895 109.600 1.00 30.62 ?  408 SER A O     1 
ATOM   3300  C  CB    . SER A 1 408 ? 132.671 151.846 112.157 1.00 26.05 ?  408 SER A CB    1 
ATOM   3301  O  OG    . SER A 1 408 ? 132.624 153.260 112.079 1.00 29.29 ?  408 SER A OG    1 
ATOM   3302  N  N     . CYS A 1 409 ? 133.957 150.850 108.915 1.00 20.52 ?  409 CYS A N     1 
ATOM   3303  C  CA    . CYS A 1 409 ? 133.916 151.203 107.505 1.00 26.32 ?  409 CYS A CA    1 
ATOM   3304  C  C     . CYS A 1 409 ? 132.585 150.795 106.886 1.00 30.59 ?  409 CYS A C     1 
ATOM   3305  O  O     . CYS A 1 409 ? 131.823 149.999 107.440 1.00 25.65 ?  409 CYS A O     1 
ATOM   3306  C  CB    . CYS A 1 409 ? 135.077 150.564 106.739 1.00 23.24 ?  409 CYS A CB    1 
ATOM   3307  S  SG    . CYS A 1 409 ? 134.741 148.955 106.013 1.00 41.88 ?  409 CYS A SG    1 
ATOM   3308  N  N     . ASN A 1 410 ? 132.320 151.360 105.716 1.00 30.01 ?  410 ASN A N     1 
ATOM   3309  C  CA    . ASN A 1 410 ? 131.031 151.268 105.047 1.00 18.67 ?  410 ASN A CA    1 
ATOM   3310  C  C     . ASN A 1 410 ? 131.164 150.334 103.852 1.00 21.72 ?  410 ASN A C     1 
ATOM   3311  O  O     . ASN A 1 410 ? 131.960 150.597 102.947 1.00 29.59 ?  410 ASN A O     1 
ATOM   3312  C  CB    . ASN A 1 410 ? 130.580 152.657 104.607 1.00 26.98 ?  410 ASN A CB    1 
ATOM   3313  C  CG    . ASN A 1 410 ? 129.119 152.719 104.279 1.00 32.40 ?  410 ASN A CG    1 
ATOM   3314  O  OD1   . ASN A 1 410 ? 128.380 151.754 104.463 1.00 35.72 ?  410 ASN A OD1   1 
ATOM   3315  N  ND2   . ASN A 1 410 ? 128.691 153.862 103.781 1.00 34.49 ?  410 ASN A ND2   1 
ATOM   3316  N  N     . LEU A 1 411 ? 130.377 149.262 103.842 1.00 21.50 ?  411 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 411 ? 130.537 148.200 102.858 1.00 11.76 ?  411 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 411 ? 129.641 148.412 101.642 1.00 16.12 ?  411 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 411 ? 128.534 148.948 101.741 1.00 26.82 ?  411 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 411 ? 130.233 146.837 103.481 1.00 19.14 ?  411 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 411 ? 131.400 145.934 103.884 1.00 20.45 ?  411 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 411 ? 132.473 146.726 104.598 1.00 19.01 ?  411 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 411 ? 130.907 144.788 104.752 1.00 18.70 ?  411 LEU A CD2   1 
ATOM   3324  N  N     . GLY A 1 412 ? 130.139 147.970 100.490 1.00 22.65 ?  412 GLY A N     1 
ATOM   3325  C  CA    . GLY A 1 412 ? 129.415 148.000 99.232  1.00 13.61 ?  412 GLY A CA    1 
ATOM   3326  C  C     . GLY A 1 412 ? 130.243 147.337 98.151  1.00 13.30 ?  412 GLY A C     1 
ATOM   3327  O  O     . GLY A 1 412 ? 131.456 147.556 98.094  1.00 23.34 ?  412 GLY A O     1 
ATOM   3328  N  N     . SER A 1 413 ? 129.627 146.530 97.289  1.00 14.80 ?  413 SER A N     1 
ATOM   3329  C  CA    . SER A 1 413 ? 130.372 145.676 96.372  1.00 10.91 ?  413 SER A CA    1 
ATOM   3330  C  C     . SER A 1 413 ? 129.997 145.960 94.927  1.00 17.65 ?  413 SER A C     1 
ATOM   3331  O  O     . SER A 1 413 ? 128.813 146.033 94.588  1.00 21.51 ?  413 SER A O     1 
ATOM   3332  C  CB    . SER A 1 413 ? 130.133 144.200 96.689  1.00 9.74  ?  413 SER A CB    1 
ATOM   3333  O  OG    . SER A 1 413 ? 130.648 143.872 97.965  1.00 32.49 ?  413 SER A OG    1 
ATOM   3334  N  N     . LEU A 1 414 ? 131.008 146.103 94.077  1.00 18.32 ?  414 LEU A N     1 
ATOM   3335  C  CA    . LEU A 1 414 ? 130.789 146.150 92.641  1.00 12.54 ?  414 LEU A CA    1 
ATOM   3336  C  C     . LEU A 1 414 ? 130.600 144.741 92.099  1.00 19.08 ?  414 LEU A C     1 
ATOM   3337  O  O     . LEU A 1 414 ? 131.290 143.806 92.511  1.00 24.42 ?  414 LEU A O     1 
ATOM   3338  C  CB    . LEU A 1 414 ? 131.971 146.818 91.939  1.00 17.56 ?  414 LEU A CB    1 
ATOM   3339  C  CG    . LEU A 1 414 ? 132.494 148.123 92.536  1.00 20.23 ?  414 LEU A CG    1 
ATOM   3340  C  CD1   . LEU A 1 414 ? 133.843 148.470 91.936  1.00 22.49 ?  414 LEU A CD1   1 
ATOM   3341  C  CD2   . LEU A 1 414 ? 131.501 149.246 92.310  1.00 20.11 ?  414 LEU A CD2   1 
ATOM   3342  N  N     . ASN A 1 415 ? 129.656 144.588 91.177  1.00 25.67 ?  415 ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 415 ? 129.478 143.330 90.456  1.00 24.25 ?  415 ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 415 ? 130.348 143.407 89.210  1.00 22.60 ?  415 ASN A C     1 
ATOM   3345  O  O     . ASN A 1 415 ? 130.006 144.087 88.241  1.00 27.33 ?  415 ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 415 ? 128.010 143.101 90.121  1.00 20.70 ?  415 ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 415 ? 127.715 141.664 89.733  1.00 25.69 ?  415 ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 415 ? 128.369 141.095 88.862  1.00 33.28 ?  415 ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 415 ? 126.723 141.070 90.386  1.00 29.90 ?  415 ASN A ND2   1 
ATOM   3350  N  N     . ILE A 1 416 ? 131.482 142.701 89.237  1.00 21.84 ?  416 ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 416 ? 132.494 142.853 88.194  1.00 24.00 ?  416 ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 416 ? 131.927 142.486 86.831  1.00 26.98 ?  416 ILE A C     1 
ATOM   3353  O  O     . ILE A 1 416 ? 132.196 143.160 85.830  1.00 29.35 ?  416 ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 416 ? 133.741 142.017 88.535  1.00 20.69 ?  416 ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 416 ? 134.394 142.535 89.814  1.00 18.38 ?  416 ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 416 ? 134.731 142.035 87.384  1.00 14.34 ?  416 ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 416 ? 135.481 141.639 90.349  1.00 19.31 ?  416 ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 417 ? 131.128 141.420 86.768  1.00 20.94 ?  417 LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 417 ? 130.532 141.022 85.498  1.00 22.96 ?  417 LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 417 ? 129.612 142.112 84.961  1.00 23.58 ?  417 LEU A C     1 
ATOM   3361  O  O     . LEU A 1 417 ? 129.752 142.550 83.812  1.00 34.84 ?  417 LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 417 ? 129.777 139.703 85.668  1.00 25.83 ?  417 LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 417 ? 129.048 139.144 84.445  1.00 28.56 ?  417 LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 417 ? 129.441 137.698 84.220  1.00 25.37 ?  417 LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 417 ? 127.545 139.265 84.615  1.00 28.76 ?  417 LEU A CD2   1 
ATOM   3366  N  N     . ASN A 1 418 ? 128.678 142.581 85.792  1.00 25.55 ?  418 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 418 ? 127.727 143.595 85.349  1.00 25.79 ?  418 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 418 ? 128.414 144.931 85.094  1.00 27.32 ?  418 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 418 ? 128.051 145.650 84.156  1.00 29.87 ?  418 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 418 ? 126.610 143.749 86.380  1.00 25.54 ?  418 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 418 ? 125.747 142.508 86.488  1.00 29.11 ?  418 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 418 ? 125.461 141.853 85.488  1.00 29.68 ?  418 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 418 ? 125.330 142.177 87.703  1.00 29.21 ?  418 ASN A ND2   1 
ATOM   3374  N  N     . VAL A 1 419 ? 129.402 145.282 85.920  1.00 31.03 ?  419 VAL A N     1 
ATOM   3375  C  CA    . VAL A 1 419 ? 130.123 146.537 85.724  1.00 28.81 ?  419 VAL A CA    1 
ATOM   3376  C  C     . VAL A 1 419 ? 130.892 146.516 84.410  1.00 29.87 ?  419 VAL A C     1 
ATOM   3377  O  O     . VAL A 1 419 ? 130.874 147.490 83.648  1.00 32.16 ?  419 VAL A O     1 
ATOM   3378  C  CB    . VAL A 1 419 ? 131.052 146.814 86.922  1.00 26.42 ?  419 VAL A CB    1 
ATOM   3379  C  CG1   . VAL A 1 419 ? 132.074 147.873 86.571  1.00 27.47 ?  419 VAL A CG1   1 
ATOM   3380  C  CG2   . VAL A 1 419 ? 130.244 147.265 88.118  1.00 28.81 ?  419 VAL A CG2   1 
ATOM   3381  N  N     . MET A 1 420 ? 131.572 145.407 84.114  1.00 32.84 ?  420 MET A N     1 
ATOM   3382  C  CA    . MET A 1 420 ? 132.421 145.383 82.930  1.00 33.42 ?  420 MET A CA    1 
ATOM   3383  C  C     . MET A 1 420 ? 131.622 145.171 81.650  1.00 30.71 ?  420 MET A C     1 
ATOM   3384  O  O     . MET A 1 420 ? 132.027 145.664 80.591  1.00 35.76 ?  420 MET A O     1 
ATOM   3385  C  CB    . MET A 1 420 ? 133.503 144.313 83.068  1.00 31.20 ?  420 MET A CB    1 
ATOM   3386  C  CG    . MET A 1 420 ? 134.750 144.831 83.773  1.00 26.08 ?  420 MET A CG    1 
ATOM   3387  S  SD    . MET A 1 420 ? 136.070 145.403 82.689  1.00 47.11 ?  420 MET A SD    1 
ATOM   3388  C  CE    . MET A 1 420 ? 136.202 144.060 81.522  1.00 33.81 ?  420 MET A CE    1 
ATOM   3389  N  N     . GLU A 1 421 ? 130.498 144.450 81.709  1.00 32.30 ?  421 GLU A N     1 
ATOM   3390  C  CA    . GLU A 1 421 ? 129.684 144.305 80.506  1.00 37.53 ?  421 GLU A CA    1 
ATOM   3391  C  C     . GLU A 1 421 ? 128.978 145.603 80.140  1.00 37.35 ?  421 GLU A C     1 
ATOM   3392  O  O     . GLU A 1 421 ? 128.627 145.796 78.972  1.00 40.20 ?  421 GLU A O     1 
ATOM   3393  C  CB    . GLU A 1 421 ? 128.654 143.185 80.673  1.00 34.43 ?  421 GLU A CB    1 
ATOM   3394  C  CG    . GLU A 1 421 ? 127.612 143.437 81.743  1.00 39.15 ?  421 GLU A CG    1 
ATOM   3395  C  CD    . GLU A 1 421 ? 126.519 142.387 81.746  1.00 43.34 ?  421 GLU A CD    1 
ATOM   3396  O  OE1   . GLU A 1 421 ? 126.385 141.666 80.735  1.00 44.06 ?  421 GLU A OE1   1 
ATOM   3397  O  OE2   . GLU A 1 421 ? 125.794 142.281 82.756  1.00 40.29 -1 421 GLU A OE2   1 
ATOM   3398  N  N     . HIS A 1 422 ? 128.766 146.491 81.108  1.00 35.77 ?  422 HIS A N     1 
ATOM   3399  C  CA    . HIS A 1 422 ? 128.212 147.813 80.857  1.00 35.28 ?  422 HIS A CA    1 
ATOM   3400  C  C     . HIS A 1 422 ? 129.285 148.851 80.561  1.00 39.14 ?  422 HIS A C     1 
ATOM   3401  O  O     . HIS A 1 422 ? 128.945 149.997 80.254  1.00 39.84 ?  422 HIS A O     1 
ATOM   3402  C  CB    . HIS A 1 422 ? 127.377 148.273 82.057  1.00 32.46 ?  422 HIS A CB    1 
ATOM   3403  C  CG    . HIS A 1 422 ? 126.042 147.606 82.156  1.00 36.58 ?  422 HIS A CG    1 
ATOM   3404  N  ND1   . HIS A 1 422 ? 125.834 146.466 82.902  1.00 36.83 ?  422 HIS A ND1   1 
ATOM   3405  C  CD2   . HIS A 1 422 ? 124.846 147.917 81.604  1.00 36.85 ?  422 HIS A CD2   1 
ATOM   3406  C  CE1   . HIS A 1 422 ? 124.568 146.104 82.806  1.00 38.65 ?  422 HIS A CE1   1 
ATOM   3407  N  NE2   . HIS A 1 422 ? 123.946 146.966 82.023  1.00 39.61 ?  422 HIS A NE2   1 
ATOM   3408  N  N     . LYS A 1 423 ? 130.561 148.472 80.643  1.00 40.10 ?  423 LYS A N     1 
ATOM   3409  C  CA    . LYS A 1 423 ? 131.684 149.375 80.389  1.00 39.49 ?  423 LYS A CA    1 
ATOM   3410  C  C     . LYS A 1 423 ? 131.578 150.636 81.241  1.00 42.48 ?  423 LYS A C     1 
ATOM   3411  O  O     . LYS A 1 423 ? 131.781 151.759 80.773  1.00 42.19 ?  423 LYS A O     1 
ATOM   3412  C  CB    . LYS A 1 423 ? 131.782 149.719 78.902  1.00 37.95 ?  423 LYS A CB    1 
ATOM   3413  C  CG    . LYS A 1 423 ? 132.066 148.523 78.010  1.00 38.37 ?  423 LYS A CG    1 
ATOM   3414  C  CD    . LYS A 1 423 ? 131.938 148.887 76.540  1.00 40.56 ?  423 LYS A CD    1 
ATOM   3415  C  CE    . LYS A 1 423 ? 131.970 147.650 75.662  1.00 40.10 ?  423 LYS A CE    1 
ATOM   3416  N  NZ    . LYS A 1 423 ? 133.082 146.734 76.037  1.00 43.35 1  423 LYS A NZ    1 
ATOM   3417  N  N     . SER A 1 424 ? 131.255 150.441 82.517  1.00 32.26 ?  424 SER A N     1 
ATOM   3418  C  CA    . SER A 1 424 ? 130.948 151.533 83.433  1.00 29.82 ?  424 SER A CA    1 
ATOM   3419  C  C     . SER A 1 424 ? 131.706 151.374 84.742  1.00 32.67 ?  424 SER A C     1 
ATOM   3420  O  O     . SER A 1 424 ? 131.136 151.463 85.830  1.00 32.96 ?  424 SER A O     1 
ATOM   3421  C  CB    . SER A 1 424 ? 129.446 151.606 83.693  1.00 34.00 ?  424 SER A CB    1 
ATOM   3422  O  OG    . SER A 1 424 ? 129.020 150.526 84.503  1.00 31.39 ?  424 SER A OG    1 
ATOM   3423  N  N     . ILE A 1 425 ? 133.014 151.126 84.659  1.00 31.72 ?  425 ILE A N     1 
ATOM   3424  C  CA    . ILE A 1 425 ? 133.824 151.061 85.873  1.00 23.87 ?  425 ILE A CA    1 
ATOM   3425  C  C     . ILE A 1 425 ? 133.838 152.414 86.574  1.00 29.13 ?  425 ILE A C     1 
ATOM   3426  O  O     . ILE A 1 425 ? 133.601 152.507 87.783  1.00 37.02 ?  425 ILE A O     1 
ATOM   3427  C  CB    . ILE A 1 425 ? 135.250 150.580 85.552  1.00 26.96 ?  425 ILE A CB    1 
ATOM   3428  C  CG1   . ILE A 1 425 ? 135.260 149.083 85.243  1.00 31.42 ?  425 ILE A CG1   1 
ATOM   3429  C  CG2   . ILE A 1 425 ? 136.190 150.878 86.710  1.00 27.22 ?  425 ILE A CG2   1 
ATOM   3430  C  CD1   . ILE A 1 425 ? 136.610 148.567 84.798  1.00 29.41 ?  425 ILE A CD1   1 
ATOM   3431  N  N     . GLU A 1 426 ? 134.093 153.485 85.818  1.00 25.95 ?  426 GLU A N     1 
ATOM   3432  C  CA    . GLU A 1 426 ? 134.211 154.812 86.416  1.00 26.36 ?  426 GLU A CA    1 
ATOM   3433  C  C     . GLU A 1 426 ? 132.903 155.254 87.060  1.00 27.33 ?  426 GLU A C     1 
ATOM   3434  O  O     . GLU A 1 426 ? 132.877 155.655 88.230  1.00 32.66 ?  426 GLU A O     1 
ATOM   3435  C  CB    . GLU A 1 426 ? 134.650 155.821 85.356  1.00 26.18 ?  426 GLU A CB    1 
ATOM   3436  C  CG    . GLU A 1 426 ? 134.388 157.267 85.732  1.00 28.32 ?  426 GLU A CG    1 
ATOM   3437  C  CD    . GLU A 1 426 ? 134.862 158.238 84.671  1.00 36.93 ?  426 GLU A CD    1 
ATOM   3438  O  OE1   . GLU A 1 426 ? 135.291 157.777 83.592  1.00 34.16 ?  426 GLU A OE1   1 
ATOM   3439  O  OE2   . GLU A 1 426 ? 134.805 159.461 84.914  1.00 37.58 -1 426 GLU A OE2   1 
ATOM   3440  N  N     . LYS A 1 427 ? 131.804 155.194 86.303  1.00 27.52 ?  427 LYS A N     1 
ATOM   3441  C  CA    . LYS A 1 427 ? 130.525 155.671 86.815  1.00 24.47 ?  427 LYS A CA    1 
ATOM   3442  C  C     . LYS A 1 427 ? 130.066 154.848 88.010  1.00 26.33 ?  427 LYS A C     1 
ATOM   3443  O  O     . LYS A 1 427 ? 129.603 155.403 89.014  1.00 31.77 ?  427 LYS A O     1 
ATOM   3444  C  CB    . LYS A 1 427 ? 129.477 155.646 85.702  1.00 31.26 ?  427 LYS A CB    1 
ATOM   3445  C  CG    . LYS A 1 427 ? 128.037 155.683 86.190  1.00 28.72 ?  427 LYS A CG    1 
ATOM   3446  C  CD    . LYS A 1 427 ? 127.126 154.878 85.278  1.00 32.81 ?  427 LYS A CD    1 
ATOM   3447  C  CE    . LYS A 1 427 ? 127.061 153.422 85.706  1.00 32.53 ?  427 LYS A CE    1 
ATOM   3448  N  NZ    . LYS A 1 427 ? 126.058 152.651 84.919  1.00 29.00 1  427 LYS A NZ    1 
ATOM   3449  N  N     . THR A 1 428 ? 130.197 153.523 87.927  1.00 26.39 ?  428 THR A N     1 
ATOM   3450  C  CA    . THR A 1 428 ? 129.782 152.674 89.037  1.00 21.30 ?  428 THR A CA    1 
ATOM   3451  C  C     . THR A 1 428 ? 130.628 152.929 90.275  1.00 23.90 ?  428 THR A C     1 
ATOM   3452  O  O     . THR A 1 428 ? 130.094 153.023 91.384  1.00 31.41 ?  428 THR A O     1 
ATOM   3453  C  CB    . THR A 1 428 ? 129.854 151.201 88.641  1.00 25.35 ?  428 THR A CB    1 
ATOM   3454  O  OG1   . THR A 1 428 ? 129.177 151.008 87.394  1.00 29.04 ?  428 THR A OG1   1 
ATOM   3455  C  CG2   . THR A 1 428 ? 129.202 150.336 89.704  1.00 24.41 ?  428 THR A CG2   1 
ATOM   3456  N  N     . VAL A 1 429 ? 131.947 153.052 90.108  1.00 24.51 ?  429 VAL A N     1 
ATOM   3457  C  CA    . VAL A 1 429 ? 132.815 153.286 91.258  1.00 24.24 ?  429 VAL A CA    1 
ATOM   3458  C  C     . VAL A 1 429 ? 132.489 154.623 91.908  1.00 23.22 ?  429 VAL A C     1 
ATOM   3459  O  O     . VAL A 1 429 ? 132.394 154.724 93.136  1.00 26.22 ?  429 VAL A O     1 
ATOM   3460  C  CB    . VAL A 1 429 ? 134.296 153.201 90.843  1.00 21.22 ?  429 VAL A CB    1 
ATOM   3461  C  CG1   . VAL A 1 429 ? 135.179 153.852 91.892  1.00 18.94 ?  429 VAL A CG1   1 
ATOM   3462  C  CG2   . VAL A 1 429 ? 134.705 151.755 90.641  1.00 23.02 ?  429 VAL A CG2   1 
ATOM   3463  N  N     . LYS A 1 430 ? 132.295 155.669 91.099  1.00 22.34 ?  430 LYS A N     1 
ATOM   3464  C  CA    . LYS A 1 430 ? 132.017 156.985 91.667  1.00 20.97 ?  430 LYS A CA    1 
ATOM   3465  C  C     . LYS A 1 430 ? 130.656 157.027 92.352  1.00 23.22 ?  430 LYS A C     1 
ATOM   3466  O  O     . LYS A 1 430 ? 130.521 157.605 93.438  1.00 30.05 ?  430 LYS A O     1 
ATOM   3467  C  CB    . LYS A 1 430 ? 132.117 158.054 90.581  1.00 19.83 ?  430 LYS A CB    1 
ATOM   3468  C  CG    . LYS A 1 430 ? 133.517 158.199 90.010  1.00 23.31 ?  430 LYS A CG    1 
ATOM   3469  C  CD    . LYS A 1 430 ? 133.722 159.550 89.357  1.00 27.87 ?  430 LYS A CD    1 
ATOM   3470  C  CE    . LYS A 1 430 ? 135.185 159.771 89.018  1.00 28.43 ?  430 LYS A CE    1 
ATOM   3471  N  NZ    . LYS A 1 430 ? 135.426 161.133 88.470  1.00 30.72 1  430 LYS A NZ    1 
ATOM   3472  N  N     . LEU A 1 431 ? 129.635 156.412 91.750  1.00 26.98 ?  431 LEU A N     1 
ATOM   3473  C  CA    . LEU A 1 431 ? 128.319 156.398 92.379  1.00 22.52 ?  431 LEU A CA    1 
ATOM   3474  C  C     . LEU A 1 431 ? 128.324 155.568 93.657  1.00 21.71 ?  431 LEU A C     1 
ATOM   3475  O  O     . LEU A 1 431 ? 127.684 155.940 94.648  1.00 28.12 ?  431 LEU A O     1 
ATOM   3476  C  CB    . LEU A 1 431 ? 127.273 155.877 91.396  1.00 27.33 ?  431 LEU A CB    1 
ATOM   3477  C  CG    . LEU A 1 431 ? 126.552 156.932 90.555  1.00 30.18 ?  431 LEU A CG    1 
ATOM   3478  C  CD1   . LEU A 1 431 ? 125.817 156.279 89.397  1.00 26.87 ?  431 LEU A CD1   1 
ATOM   3479  C  CD2   . LEU A 1 431 ? 125.591 157.734 91.416  1.00 28.35 ?  431 LEU A CD2   1 
ATOM   3480  N  N     . ALA A 1 432 ? 129.040 154.441 93.655  1.00 20.35 ?  432 ALA A N     1 
ATOM   3481  C  CA    . ALA A 1 432 ? 129.160 153.636 94.864  1.00 19.22 ?  432 ALA A CA    1 
ATOM   3482  C  C     . ALA A 1 432 ? 129.899 154.396 95.955  1.00 24.76 ?  432 ALA A C     1 
ATOM   3483  O  O     . ALA A 1 432 ? 129.538 154.310 97.133  1.00 26.67 ?  432 ALA A O     1 
ATOM   3484  C  CB    . ALA A 1 432 ? 129.871 152.323 94.547  1.00 26.31 ?  432 ALA A CB    1 
ATOM   3485  N  N     . THR A 1 433 ? 130.940 155.143 95.581  1.00 22.76 ?  433 THR A N     1 
ATOM   3486  C  CA    . THR A 1 433 ? 131.651 155.968 96.550  1.00 17.94 ?  433 THR A CA    1 
ATOM   3487  C  C     . THR A 1 433 ? 130.737 157.035 97.137  1.00 22.72 ?  433 THR A C     1 
ATOM   3488  O  O     . THR A 1 433 ? 130.768 157.292 98.344  1.00 27.81 ?  433 THR A O     1 
ATOM   3489  C  CB    . THR A 1 433 ? 132.871 156.613 95.891  1.00 20.26 ?  433 THR A CB    1 
ATOM   3490  O  OG1   . THR A 1 433 ? 133.669 155.601 95.264  1.00 25.56 ?  433 THR A OG1   1 
ATOM   3491  C  CG2   . THR A 1 433 ? 133.713 157.348 96.921  1.00 24.42 ?  433 THR A CG2   1 
ATOM   3492  N  N     . ASP A 1 434 ? 129.916 157.666 96.295  1.00 20.19 ?  434 ASP A N     1 
ATOM   3493  C  CA    . ASP A 1 434 ? 128.978 158.669 96.792  1.00 15.86 ?  434 ASP A CA    1 
ATOM   3494  C  C     . ASP A 1 434 ? 127.957 158.055 97.745  1.00 19.40 ?  434 ASP A C     1 
ATOM   3495  O  O     . ASP A 1 434 ? 127.643 158.637 98.790  1.00 25.70 ?  434 ASP A O     1 
ATOM   3496  C  CB    . ASP A 1 434 ? 128.274 159.353 95.620  1.00 23.42 ?  434 ASP A CB    1 
ATOM   3497  C  CG    . ASP A 1 434 ? 129.218 160.182 94.778  1.00 31.37 ?  434 ASP A CG    1 
ATOM   3498  O  OD1   . ASP A 1 434 ? 130.234 160.661 95.322  1.00 29.06 ?  434 ASP A OD1   1 
ATOM   3499  O  OD2   . ASP A 1 434 ? 128.944 160.354 93.573  1.00 30.81 -1 434 ASP A OD2   1 
ATOM   3500  N  N     . SER A 1 435 ? 127.427 156.879 97.401  1.00 20.41 ?  435 SER A N     1 
ATOM   3501  C  CA    . SER A 1 435 ? 126.465 156.215 98.277  1.00 17.04 ?  435 SER A CA    1 
ATOM   3502  C  C     . SER A 1 435 ? 127.104 155.812 99.601  1.00 25.13 ?  435 SER A C     1 
ATOM   3503  O  O     . SER A 1 435 ? 126.489 155.956 100.666 1.00 34.54 ?  435 SER A O     1 
ATOM   3504  C  CB    . SER A 1 435 ? 125.875 154.993 97.575  1.00 19.28 ?  435 SER A CB    1 
ATOM   3505  O  OG    . SER A 1 435 ? 126.827 153.950 97.481  1.00 23.37 ?  435 SER A OG    1 
ATOM   3506  N  N     . LEU A 1 436 ? 128.335 155.300 99.554  1.00 18.68 ?  436 LEU A N     1 
ATOM   3507  C  CA    . LEU A 1 436 ? 129.033 154.927 100.778 1.00 13.11 ?  436 LEU A CA    1 
ATOM   3508  C  C     . LEU A 1 436 ? 129.328 156.149 101.636 1.00 15.45 ?  436 LEU A C     1 
ATOM   3509  O  O     . LEU A 1 436 ? 129.222 156.090 102.866 1.00 27.01 ?  436 LEU A O     1 
ATOM   3510  C  CB    . LEU A 1 436 ? 130.320 154.178 100.438 1.00 20.26 ?  436 LEU A CB    1 
ATOM   3511  C  CG    . LEU A 1 436 ? 130.130 152.776 99.863  1.00 17.84 ?  436 LEU A CG    1 
ATOM   3512  C  CD1   . LEU A 1 436 ? 131.456 152.184 99.421  1.00 17.53 ?  436 LEU A CD1   1 
ATOM   3513  C  CD2   . LEU A 1 436 ? 129.450 151.882 100.878 1.00 18.63 ?  436 LEU A CD2   1 
ATOM   3514  N  N     . THR A 1 437 ? 129.696 157.266 101.005 1.00 19.99 ?  437 THR A N     1 
ATOM   3515  C  CA    . THR A 1 437 ? 129.895 158.508 101.741 1.00 20.52 ?  437 THR A CA    1 
ATOM   3516  C  C     . THR A 1 437 ? 128.604 158.962 102.406 1.00 23.63 ?  437 THR A C     1 
ATOM   3517  O  O     . THR A 1 437 ? 128.612 159.392 103.564 1.00 25.90 ?  437 THR A O     1 
ATOM   3518  C  CB    . THR A 1 437 ? 130.420 159.592 100.800 1.00 18.17 ?  437 THR A CB    1 
ATOM   3519  O  OG1   . THR A 1 437 ? 131.612 159.129 100.156 1.00 17.98 ?  437 THR A OG1   1 
ATOM   3520  C  CG2   . THR A 1 437 ? 130.725 160.863 101.569 1.00 22.56 ?  437 THR A CG2   1 
ATOM   3521  N  N     . HIS A 1 438 ? 127.480 158.868 101.691 1.00 22.47 ?  438 HIS A N     1 
ATOM   3522  C  CA    . HIS A 1 438 ? 126.202 159.257 102.274 1.00 23.06 ?  438 HIS A CA    1 
ATOM   3523  C  C     . HIS A 1 438 ? 125.849 158.383 103.470 1.00 22.61 ?  438 HIS A C     1 
ATOM   3524  O  O     . HIS A 1 438 ? 125.403 158.888 104.507 1.00 26.43 ?  438 HIS A O     1 
ATOM   3525  C  CB    . HIS A 1 438 ? 125.098 159.188 101.222 1.00 26.74 ?  438 HIS A CB    1 
ATOM   3526  C  CG    . HIS A 1 438 ? 123.720 159.323 101.790 1.00 27.35 ?  438 HIS A CG    1 
ATOM   3527  N  ND1   . HIS A 1 438 ? 123.158 160.544 102.095 1.00 25.41 ?  438 HIS A ND1   1 
ATOM   3528  C  CD2   . HIS A 1 438 ? 122.796 158.391 102.120 1.00 23.58 ?  438 HIS A CD2   1 
ATOM   3529  C  CE1   . HIS A 1 438 ? 121.945 160.357 102.584 1.00 30.51 ?  438 HIS A CE1   1 
ATOM   3530  N  NE2   . HIS A 1 438 ? 121.701 159.060 102.609 1.00 29.10 ?  438 HIS A NE2   1 
ATOM   3531  N  N     . VAL A 1 439 ? 126.043 157.069 103.346 1.00 24.67 ?  439 VAL A N     1 
ATOM   3532  C  CA    . VAL A 1 439 ? 125.707 156.177 104.453 1.00 20.20 ?  439 VAL A CA    1 
ATOM   3533  C  C     . VAL A 1 439 ? 126.637 156.409 105.638 1.00 27.85 ?  439 VAL A C     1 
ATOM   3534  O  O     . VAL A 1 439 ? 126.203 156.354 106.796 1.00 36.63 ?  439 VAL A O     1 
ATOM   3535  C  CB    . VAL A 1 439 ? 125.727 154.712 103.983 1.00 20.52 ?  439 VAL A CB    1 
ATOM   3536  C  CG1   . VAL A 1 439 ? 125.722 153.760 105.169 1.00 21.99 ?  439 VAL A CG1   1 
ATOM   3537  C  CG2   . VAL A 1 439 ? 124.551 154.435 103.079 1.00 30.53 ?  439 VAL A CG2   1 
ATOM   3538  N  N     . SER A 1 440 ? 127.919 156.682 105.381 1.00 21.50 ?  440 SER A N     1 
ATOM   3539  C  CA    . SER A 1 440 ? 128.841 156.997 106.467 1.00 20.63 ?  440 SER A CA    1 
ATOM   3540  C  C     . SER A 1 440 ? 128.458 158.300 107.159 1.00 24.45 ?  440 SER A C     1 
ATOM   3541  O  O     . SER A 1 440 ? 128.569 158.413 108.385 1.00 26.57 ?  440 SER A O     1 
ATOM   3542  C  CB    . SER A 1 440 ? 130.271 157.069 105.932 1.00 25.67 ?  440 SER A CB    1 
ATOM   3543  O  OG    . SER A 1 440 ? 131.190 157.381 106.964 1.00 24.86 ?  440 SER A OG    1 
ATOM   3544  N  N     . GLU A 1 441 ? 128.012 159.295 106.389 1.00 26.21 ?  441 GLU A N     1 
ATOM   3545  C  CA    . GLU A 1 441 ? 127.621 160.571 106.978 1.00 23.41 ?  441 GLU A CA    1 
ATOM   3546  C  C     . GLU A 1 441 ? 126.318 160.460 107.756 1.00 30.31 ?  441 GLU A C     1 
ATOM   3547  O  O     . GLU A 1 441 ? 126.123 161.185 108.738 1.00 38.74 ?  441 GLU A O     1 
ATOM   3548  C  CB    . GLU A 1 441 ? 127.493 161.636 105.889 1.00 25.90 ?  441 GLU A CB    1 
ATOM   3549  C  CG    . GLU A 1 441 ? 128.816 162.124 105.331 1.00 29.16 ?  441 GLU A CG    1 
ATOM   3550  C  CD    . GLU A 1 441 ? 128.683 162.664 103.922 1.00 36.38 ?  441 GLU A CD    1 
ATOM   3551  O  OE1   . GLU A 1 441 ? 127.657 162.380 103.268 1.00 34.67 ?  441 GLU A OE1   1 
ATOM   3552  O  OE2   . GLU A 1 441 ? 129.603 163.377 103.466 1.00 36.67 -1 441 GLU A OE2   1 
ATOM   3553  N  N     . THR A 1 442 ? 125.418 159.574 107.339 1.00 30.88 ?  442 THR A N     1 
ATOM   3554  C  CA    . THR A 1 442 ? 124.138 159.406 108.014 1.00 29.96 ?  442 THR A CA    1 
ATOM   3555  C  C     . THR A 1 442 ? 124.201 158.417 109.169 1.00 30.74 ?  442 THR A C     1 
ATOM   3556  O  O     . THR A 1 442 ? 123.173 158.167 109.807 1.00 38.69 ?  442 THR A O     1 
ATOM   3557  C  CB    . THR A 1 442 ? 123.063 158.958 107.019 1.00 29.97 ?  442 THR A CB    1 
ATOM   3558  O  OG1   . THR A 1 442 ? 123.515 157.795 106.314 1.00 33.39 ?  442 THR A OG1   1 
ATOM   3559  C  CG2   . THR A 1 442 ? 122.762 160.066 106.024 1.00 29.67 ?  442 THR A CG2   1 
ATOM   3560  N  N     . THR A 1 443 ? 125.371 157.852 109.453 1.00 29.39 ?  443 THR A N     1 
ATOM   3561  C  CA    . THR A 1 443 ? 125.534 156.938 110.575 1.00 32.14 ?  443 THR A CA    1 
ATOM   3562  C  C     . THR A 1 443 ? 125.893 157.728 111.826 1.00 37.04 ?  443 THR A C     1 
ATOM   3563  O  O     . THR A 1 443 ? 126.859 158.499 111.825 1.00 39.75 ?  443 THR A O     1 
ATOM   3564  C  CB    . THR A 1 443 ? 126.612 155.897 110.278 1.00 32.36 ?  443 THR A CB    1 
ATOM   3565  O  OG1   . THR A 1 443 ? 126.182 155.056 109.200 1.00 36.65 ?  443 THR A OG1   1 
ATOM   3566  C  CG2   . THR A 1 443 ? 126.879 155.042 111.505 1.00 26.65 ?  443 THR A CG2   1 
ATOM   3567  N  N     . ASP A 1 444 ? 125.113 157.536 112.888 1.00 43.45 ?  444 ASP A N     1 
ATOM   3568  C  CA    . ASP A 1 444 ? 125.331 158.229 114.158 1.00 42.13 ?  444 ASP A CA    1 
ATOM   3569  C  C     . ASP A 1 444 ? 125.060 157.232 115.280 1.00 41.49 ?  444 ASP A C     1 
ATOM   3570  O  O     . ASP A 1 444 ? 123.902 156.929 115.583 1.00 42.15 ?  444 ASP A O     1 
ATOM   3571  C  CB    . ASP A 1 444 ? 124.439 159.459 114.277 1.00 43.52 ?  444 ASP A CB    1 
ATOM   3572  C  CG    . ASP A 1 444 ? 125.202 160.690 114.721 1.00 47.76 ?  444 ASP A CG    1 
ATOM   3573  O  OD1   . ASP A 1 444 ? 126.448 160.634 114.765 1.00 46.38 ?  444 ASP A OD1   1 
ATOM   3574  O  OD2   . ASP A 1 444 ? 124.554 161.714 115.023 1.00 47.26 -1 444 ASP A OD2   1 
ATOM   3575  N  N     . ILE A 1 445 ? 126.127 156.731 115.893 1.00 34.72 ?  445 ILE A N     1 
ATOM   3576  C  CA    . ILE A 1 445 ? 126.034 155.748 116.964 1.00 37.80 ?  445 ILE A CA    1 
ATOM   3577  C  C     . ILE A 1 445 ? 126.298 156.457 118.284 1.00 38.51 ?  445 ILE A C     1 
ATOM   3578  O  O     . ILE A 1 445 ? 127.392 156.990 118.506 1.00 39.84 ?  445 ILE A O     1 
ATOM   3579  C  CB    . ILE A 1 445 ? 127.016 154.587 116.747 1.00 36.80 ?  445 ILE A CB    1 
ATOM   3580  C  CG1   . ILE A 1 445 ? 126.654 153.833 115.466 1.00 34.86 ?  445 ILE A CG1   1 
ATOM   3581  C  CG2   . ILE A 1 445 ? 127.004 153.649 117.939 1.00 37.90 ?  445 ILE A CG2   1 
ATOM   3582  C  CD1   . ILE A 1 445 ? 127.696 152.843 115.028 1.00 34.17 ?  445 ILE A CD1   1 
ATOM   3583  N  N     . ARG A 1 446 ? 125.297 156.464 119.160 1.00 40.85 ?  446 ARG A N     1 
ATOM   3584  C  CA    . ARG A 1 446 ? 125.336 157.236 120.393 1.00 46.28 ?  446 ARG A CA    1 
ATOM   3585  C  C     . ARG A 1 446 ? 125.861 156.444 121.583 1.00 44.95 ?  446 ARG A C     1 
ATOM   3586  O  O     . ARG A 1 446 ? 125.920 156.988 122.690 1.00 41.08 ?  446 ARG A O     1 
ATOM   3587  C  CB    . ARG A 1 446 ? 123.939 157.780 120.714 1.00 44.76 ?  446 ARG A CB    1 
ATOM   3588  C  CG    . ARG A 1 446 ? 123.021 157.894 119.505 1.00 43.05 ?  446 ARG A CG    1 
ATOM   3589  C  CD    . ARG A 1 446 ? 123.463 159.003 118.556 1.00 45.48 ?  446 ARG A CD    1 
ATOM   3590  N  NE    . ARG A 1 446 ? 123.041 160.322 119.010 1.00 47.02 ?  446 ARG A NE    1 
ATOM   3591  C  CZ    . ARG A 1 446 ? 121.805 160.791 118.901 1.00 47.76 ?  446 ARG A CZ    1 
ATOM   3592  N  NH1   . ARG A 1 446 ? 120.836 160.068 118.364 1.00 43.40 1  446 ARG A NH1   1 
ATOM   3593  N  NH2   . ARG A 1 446 ? 121.535 162.017 119.341 1.00 47.17 ?  446 ARG A NH2   1 
ATOM   3594  N  N     . ASN A 1 447 ? 126.242 155.182 121.388 1.00 34.40 ?  447 ASN A N     1 
ATOM   3595  C  CA    . ASN A 1 447 ? 126.768 154.357 122.463 1.00 29.03 ?  447 ASN A CA    1 
ATOM   3596  C  C     . ASN A 1 447 ? 128.188 153.876 122.205 1.00 32.18 ?  447 ASN A C     1 
ATOM   3597  O  O     . ASN A 1 447 ? 128.753 153.174 123.051 1.00 35.53 ?  447 ASN A O     1 
ATOM   3598  C  CB    . ASN A 1 447 ? 125.853 153.150 122.703 1.00 32.55 ?  447 ASN A CB    1 
ATOM   3599  C  CG    . ASN A 1 447 ? 124.758 153.442 123.705 1.00 29.77 ?  447 ASN A CG    1 
ATOM   3600  O  OD1   . ASN A 1 447 ? 124.945 154.225 124.634 1.00 28.36 ?  447 ASN A OD1   1 
ATOM   3601  N  ND2   . ASN A 1 447 ? 123.602 152.820 123.514 1.00 32.26 ?  447 ASN A ND2   1 
ATOM   3602  N  N     . ALA A 1 448 ? 128.776 154.229 121.062 1.00 34.16 ?  448 ALA A N     1 
ATOM   3603  C  CA    . ALA A 1 448 ? 130.165 153.911 120.736 1.00 29.31 ?  448 ALA A CA    1 
ATOM   3604  C  C     . ALA A 1 448 ? 130.870 155.226 120.428 1.00 29.15 ?  448 ALA A C     1 
ATOM   3605  O  O     . ALA A 1 448 ? 130.846 155.700 119.281 1.00 29.10 ?  448 ALA A O     1 
ATOM   3606  C  CB    . ALA A 1 448 ? 130.252 152.940 119.563 1.00 24.41 ?  448 ALA A CB    1 
ATOM   3607  N  N     . PRO A 1 449 ? 131.501 155.854 121.423 1.00 28.77 ?  449 PRO A N     1 
ATOM   3608  C  CA    . PRO A 1 449 ? 132.070 157.192 121.185 1.00 22.93 ?  449 PRO A CA    1 
ATOM   3609  C  C     . PRO A 1 449 ? 133.226 157.185 120.203 1.00 27.34 ?  449 PRO A C     1 
ATOM   3610  O  O     . PRO A 1 449 ? 133.297 158.061 119.333 1.00 22.25 ?  449 PRO A O     1 
ATOM   3611  C  CB    . PRO A 1 449 ? 132.519 157.642 122.585 1.00 19.14 ?  449 PRO A CB    1 
ATOM   3612  C  CG    . PRO A 1 449 ? 131.967 156.629 123.543 1.00 25.18 ?  449 PRO A CG    1 
ATOM   3613  C  CD    . PRO A 1 449 ? 131.771 155.369 122.784 1.00 23.69 ?  449 PRO A CD    1 
ATOM   3614  N  N     . ALA A 1 450 ? 134.136 156.215 120.315 1.00 25.81 ?  450 ALA A N     1 
ATOM   3615  C  CA    . ALA A 1 450 ? 135.275 156.170 119.407 1.00 16.45 ?  450 ALA A CA    1 
ATOM   3616  C  C     . ALA A 1 450 ? 134.854 155.774 117.997 1.00 22.90 ?  450 ALA A C     1 
ATOM   3617  O  O     . ALA A 1 450 ? 135.418 156.283 117.024 1.00 26.91 ?  450 ALA A O     1 
ATOM   3618  C  CB    . ALA A 1 450 ? 136.337 155.211 119.942 1.00 19.28 ?  450 ALA A CB    1 
ATOM   3619  N  N     . VAL A 1 451 ? 133.862 154.891 117.867 1.00 28.04 ?  451 VAL A N     1 
ATOM   3620  C  CA    . VAL A 1 451 ? 133.346 154.539 116.546 1.00 18.02 ?  451 VAL A CA    1 
ATOM   3621  C  C     . VAL A 1 451 ? 132.754 155.768 115.867 1.00 21.83 ?  451 VAL A C     1 
ATOM   3622  O  O     . VAL A 1 451 ? 133.019 156.040 114.692 1.00 30.56 ?  451 VAL A O     1 
ATOM   3623  C  CB    . VAL A 1 451 ? 132.313 153.404 116.656 1.00 21.98 ?  451 VAL A CB    1 
ATOM   3624  C  CG1   . VAL A 1 451 ? 131.478 153.315 115.389 1.00 23.76 ?  451 VAL A CG1   1 
ATOM   3625  C  CG2   . VAL A 1 451 ? 133.000 152.080 116.934 1.00 22.51 ?  451 VAL A CG2   1 
ATOM   3626  N  N     . ARG A 1 452 ? 131.946 156.533 116.605 1.00 20.50 ?  452 ARG A N     1 
ATOM   3627  C  CA    . ARG A 1 452 ? 131.344 157.738 116.046 1.00 22.77 ?  452 ARG A CA    1 
ATOM   3628  C  C     . ARG A 1 452 ? 132.403 158.776 115.692 1.00 23.83 ?  452 ARG A C     1 
ATOM   3629  O  O     . ARG A 1 452 ? 132.336 159.408 114.629 1.00 33.52 ?  452 ARG A O     1 
ATOM   3630  C  CB    . ARG A 1 452 ? 130.333 158.316 117.036 1.00 21.08 ?  452 ARG A CB    1 
ATOM   3631  C  CG    . ARG A 1 452 ? 129.829 159.701 116.689 1.00 26.53 ?  452 ARG A CG    1 
ATOM   3632  C  CD    . ARG A 1 452 ? 128.769 160.153 117.676 1.00 27.26 ?  452 ARG A CD    1 
ATOM   3633  N  NE    . ARG A 1 452 ? 129.173 159.894 119.053 1.00 38.94 ?  452 ARG A NE    1 
ATOM   3634  C  CZ    . ARG A 1 452 ? 128.429 160.165 120.116 1.00 41.10 ?  452 ARG A CZ    1 
ATOM   3635  N  NH1   . ARG A 1 452 ? 127.225 160.703 120.000 1.00 34.44 1  452 ARG A NH1   1 
ATOM   3636  N  NH2   . ARG A 1 452 ? 128.904 159.889 121.328 1.00 29.62 ?  452 ARG A NH2   1 
ATOM   3637  N  N     . ARG A 1 453 ? 133.393 158.961 116.569 1.00 21.78 ?  453 ARG A N     1 
ATOM   3638  C  CA    . ARG A 1 453 ? 134.443 159.940 116.302 1.00 20.91 ?  453 ARG A CA    1 
ATOM   3639  C  C     . ARG A 1 453 ? 135.254 159.555 115.073 1.00 25.75 ?  453 ARG A C     1 
ATOM   3640  O  O     . ARG A 1 453 ? 135.565 160.409 114.235 1.00 29.91 ?  453 ARG A O     1 
ATOM   3641  C  CB    . ARG A 1 453 ? 135.349 160.083 117.526 1.00 20.33 ?  453 ARG A CB    1 
ATOM   3642  C  CG    . ARG A 1 453 ? 136.692 160.727 117.230 1.00 23.78 ?  453 ARG A CG    1 
ATOM   3643  C  CD    . ARG A 1 453 ? 137.315 161.331 118.476 1.00 21.86 ?  453 ARG A CD    1 
ATOM   3644  N  NE    . ARG A 1 453 ? 138.649 160.798 118.727 1.00 21.77 ?  453 ARG A NE    1 
ATOM   3645  C  CZ    . ARG A 1 453 ? 139.760 161.277 118.184 1.00 23.79 ?  453 ARG A CZ    1 
ATOM   3646  N  NH1   . ARG A 1 453 ? 139.736 162.303 117.350 1.00 24.12 1  453 ARG A NH1   1 
ATOM   3647  N  NH2   . ARG A 1 453 ? 140.924 160.710 118.484 1.00 25.71 ?  453 ARG A NH2   1 
ATOM   3648  N  N     . ALA A 1 454 ? 135.592 158.270 114.937 1.00 23.64 ?  454 ALA A N     1 
ATOM   3649  C  CA    . ALA A 1 454 ? 136.356 157.827 113.778 1.00 18.39 ?  454 ALA A CA    1 
ATOM   3650  C  C     . ALA A 1 454 ? 135.523 157.865 112.505 1.00 18.15 ?  454 ALA A C     1 
ATOM   3651  O  O     . ALA A 1 454 ? 136.066 158.105 111.424 1.00 23.75 ?  454 ALA A O     1 
ATOM   3652  C  CB    . ALA A 1 454 ? 136.905 156.423 114.014 1.00 20.65 ?  454 ALA A CB    1 
ATOM   3653  N  N     . ASN A 1 455 ? 134.214 157.629 112.602 1.00 20.68 ?  455 ASN A N     1 
ATOM   3654  C  CA    . ASN A 1 455 ? 133.361 157.772 111.429 1.00 21.99 ?  455 ASN A CA    1 
ATOM   3655  C  C     . ASN A 1 455 ? 133.300 159.224 110.973 1.00 25.45 ?  455 ASN A C     1 
ATOM   3656  O  O     . ASN A 1 455 ? 133.337 159.506 109.770 1.00 30.27 ?  455 ASN A O     1 
ATOM   3657  C  CB    . ASN A 1 455 ? 131.961 157.239 111.725 1.00 19.31 ?  455 ASN A CB    1 
ATOM   3658  C  CG    . ASN A 1 455 ? 131.044 157.311 110.522 1.00 27.04 ?  455 ASN A CG    1 
ATOM   3659  O  OD1   . ASN A 1 455 ? 131.341 156.753 109.467 1.00 31.25 ?  455 ASN A OD1   1 
ATOM   3660  N  ND2   . ASN A 1 455 ? 129.920 158.002 110.674 1.00 26.78 ?  455 ASN A ND2   1 
ATOM   3661  N  N     . LYS A 1 456 ? 133.205 160.159 111.922 1.00 24.12 ?  456 LYS A N     1 
ATOM   3662  C  CA    . LYS A 1 456 ? 133.179 161.573 111.561 1.00 25.23 ?  456 LYS A CA    1 
ATOM   3663  C  C     . LYS A 1 456 ? 134.521 162.035 111.003 1.00 23.97 ?  456 LYS A C     1 
ATOM   3664  O  O     . LYS A 1 456 ? 134.564 162.828 110.056 1.00 29.54 ?  456 LYS A O     1 
ATOM   3665  C  CB    . LYS A 1 456 ? 132.786 162.416 112.773 1.00 27.55 ?  456 LYS A CB    1 
ATOM   3666  C  CG    . LYS A 1 456 ? 131.342 162.892 112.761 1.00 30.26 ?  456 LYS A CG    1 
ATOM   3667  C  CD    . LYS A 1 456 ? 130.701 162.806 114.143 1.00 33.55 ?  456 LYS A CD    1 
ATOM   3668  C  CE    . LYS A 1 456 ? 131.722 163.003 115.255 1.00 33.77 ?  456 LYS A CE    1 
ATOM   3669  N  NZ    . LYS A 1 456 ? 131.126 162.819 116.607 1.00 31.84 1  456 LYS A NZ    1 
ATOM   3670  N  N     . ALA A 1 457 ? 135.625 161.552 111.576 1.00 19.17 ?  457 ALA A N     1 
ATOM   3671  C  CA    . ALA A 1 457 ? 136.945 162.055 111.212 1.00 17.96 ?  457 ALA A CA    1 
ATOM   3672  C  C     . ALA A 1 457 ? 137.497 161.362 109.970 1.00 24.71 ?  457 ALA A C     1 
ATOM   3673  O  O     . ALA A 1 457 ? 137.797 162.011 108.963 1.00 29.05 ?  457 ALA A O     1 
ATOM   3674  C  CB    . ALA A 1 457 ? 137.906 161.883 112.391 1.00 15.33 ?  457 ALA A CB    1 
ATOM   3675  N  N     . MET A 1 458 ? 137.643 160.039 110.034 1.00 23.82 ?  458 MET A N     1 
ATOM   3676  C  CA    . MET A 1 458 ? 138.277 159.285 108.961 1.00 19.43 ?  458 MET A CA    1 
ATOM   3677  C  C     . MET A 1 458 ? 137.425 159.230 107.699 1.00 23.77 ?  458 MET A C     1 
ATOM   3678  O  O     . MET A 1 458 ? 137.975 159.234 106.593 1.00 30.03 ?  458 MET A O     1 
ATOM   3679  C  CB    . MET A 1 458 ? 138.590 157.869 109.444 1.00 22.61 ?  458 MET A CB    1 
ATOM   3680  C  CG    . MET A 1 458 ? 139.484 157.820 110.670 1.00 14.51 ?  458 MET A CG    1 
ATOM   3681  S  SD    . MET A 1 458 ? 141.163 158.370 110.320 1.00 33.37 ?  458 MET A SD    1 
ATOM   3682  C  CE    . MET A 1 458 ? 142.013 156.797 110.212 1.00 22.54 ?  458 MET A CE    1 
ATOM   3683  N  N     . LYS A 1 459 ? 136.100 159.170 107.843 1.00 18.14 ?  459 LYS A N     1 
ATOM   3684  C  CA    . LYS A 1 459 ? 135.188 159.049 106.704 1.00 21.43 ?  459 LYS A CA    1 
ATOM   3685  C  C     . LYS A 1 459 ? 135.558 157.851 105.835 1.00 21.56 ?  459 LYS A C     1 
ATOM   3686  O  O     . LYS A 1 459 ? 135.506 157.905 104.604 1.00 27.81 ?  459 LYS A O     1 
ATOM   3687  C  CB    . LYS A 1 459 ? 135.159 160.333 105.872 1.00 22.37 ?  459 LYS A CB    1 
ATOM   3688  C  CG    . LYS A 1 459 ? 134.783 161.579 106.649 1.00 24.94 ?  459 LYS A CG    1 
ATOM   3689  C  CD    . LYS A 1 459 ? 135.791 162.690 106.418 1.00 25.12 ?  459 LYS A CD    1 
ATOM   3690  C  CE    . LYS A 1 459 ? 135.163 164.054 106.636 1.00 27.52 ?  459 LYS A CE    1 
ATOM   3691  N  NZ    . LYS A 1 459 ? 133.978 163.982 107.534 1.00 30.30 1  459 LYS A NZ    1 
ATOM   3692  N  N     . SER A 1 460 ? 135.939 156.757 106.485 1.00 20.55 ?  460 SER A N     1 
ATOM   3693  C  CA    . SER A 1 460 ? 136.419 155.584 105.774 1.00 11.16 ?  460 SER A CA    1 
ATOM   3694  C  C     . SER A 1 460 ? 135.254 154.748 105.265 1.00 15.54 ?  460 SER A C     1 
ATOM   3695  O  O     . SER A 1 460 ? 134.281 154.505 105.983 1.00 26.00 ?  460 SER A O     1 
ATOM   3696  C  CB    . SER A 1 460 ? 137.311 154.741 106.683 1.00 13.25 ?  460 SER A CB    1 
ATOM   3697  O  OG    . SER A 1 460 ? 136.591 153.656 107.236 1.00 13.78 ?  460 SER A OG    1 
ATOM   3698  N  N     . ILE A 1 461 ? 135.362 154.313 104.012 1.00 17.07 ?  461 ILE A N     1 
ATOM   3699  C  CA    . ILE A 1 461 ? 134.368 153.461 103.380 1.00 11.44 ?  461 ILE A CA    1 
ATOM   3700  C  C     . ILE A 1 461 ? 135.080 152.245 102.806 1.00 18.03 ?  461 ILE A C     1 
ATOM   3701  O  O     . ILE A 1 461 ? 136.284 152.266 102.545 1.00 18.23 ?  461 ILE A O     1 
ATOM   3702  C  CB    . ILE A 1 461 ? 133.585 154.197 102.272 1.00 13.11 ?  461 ILE A CB    1 
ATOM   3703  C  CG1   . ILE A 1 461 ? 134.544 154.696 101.191 1.00 8.92  ?  461 ILE A CG1   1 
ATOM   3704  C  CG2   . ILE A 1 461 ? 132.790 155.353 102.860 1.00 13.75 ?  461 ILE A CG2   1 
ATOM   3705  C  CD1   . ILE A 1 461 ? 133.858 155.215 99.956  1.00 8.18  ?  461 ILE A CD1   1 
ATOM   3706  N  N     . GLY A 1 462 ? 134.326 151.165 102.639 1.00 17.97 ?  462 GLY A N     1 
ATOM   3707  C  CA    . GLY A 1 462 ? 134.858 150.001 101.965 1.00 8.19  ?  462 GLY A CA    1 
ATOM   3708  C  C     . GLY A 1 462 ? 134.092 149.655 100.708 1.00 5.51  ?  462 GLY A C     1 
ATOM   3709  O  O     . GLY A 1 462 ? 132.961 149.169 100.779 1.00 19.62 ?  462 GLY A O     1 
ATOM   3710  N  N     . LEU A 1 463 ? 134.700 149.880 99.550  1.00 11.37 ?  463 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 463 ? 134.098 149.536 98.268  1.00 9.14  ?  463 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 463 ? 134.716 148.228 97.793  1.00 11.19 ?  463 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 463 ? 135.894 148.188 97.424  1.00 20.03 ?  463 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 463 ? 134.306 150.650 97.247  1.00 18.61 ?  463 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 463 ? 133.713 150.404 95.857  1.00 18.85 ?  463 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 463 ? 132.262 149.970 95.963  1.00 9.23  ?  463 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 463 ? 133.842 151.646 94.993  1.00 15.50 ?  463 LEU A CD2   1 
ATOM   3718  N  N     . GLY A 1 464 ? 133.922 147.158 97.807  1.00 12.27 ?  464 GLY A N     1 
ATOM   3719  C  CA    . GLY A 1 464 ? 134.385 145.850 97.410  1.00 8.91  ?  464 GLY A CA    1 
ATOM   3720  C  C     . GLY A 1 464 ? 133.961 145.479 95.997  1.00 14.99 ?  464 GLY A C     1 
ATOM   3721  O  O     . GLY A 1 464 ? 133.337 146.247 95.269  1.00 21.90 ?  464 GLY A O     1 
ATOM   3722  N  N     . ALA A 1 465 ? 134.329 144.261 95.617  1.00 14.56 ?  465 ALA A N     1 
ATOM   3723  C  CA    . ALA A 1 465 ? 133.966 143.709 94.324  1.00 10.65 ?  465 ALA A CA    1 
ATOM   3724  C  C     . ALA A 1 465 ? 133.549 142.258 94.506  1.00 13.06 ?  465 ALA A C     1 
ATOM   3725  O  O     . ALA A 1 465 ? 133.971 141.589 95.452  1.00 22.50 ?  465 ALA A O     1 
ATOM   3726  C  CB    . ALA A 1 465 ? 135.121 143.807 93.321  1.00 16.40 ?  465 ALA A CB    1 
ATOM   3727  N  N     . MET A 1 466 ? 132.708 141.784 93.593  1.00 13.84 ?  466 MET A N     1 
ATOM   3728  C  CA    . MET A 1 466 ? 132.257 140.402 93.608  1.00 20.15 ?  466 MET A CA    1 
ATOM   3729  C  C     . MET A 1 466 ? 132.053 139.944 92.172  1.00 20.70 ?  466 MET A C     1 
ATOM   3730  O  O     . MET A 1 466 ? 132.182 140.725 91.227  1.00 27.41 ?  466 MET A O     1 
ATOM   3731  C  CB    . MET A 1 466 ? 130.972 140.239 94.425  1.00 25.63 ?  466 MET A CB    1 
ATOM   3732  C  CG    . MET A 1 466 ? 129.787 140.974 93.841  1.00 21.84 ?  466 MET A CG    1 
ATOM   3733  S  SD    . MET A 1 466 ? 128.353 140.973 94.924  1.00 34.17 ?  466 MET A SD    1 
ATOM   3734  C  CE    . MET A 1 466 ? 127.338 142.178 94.085  1.00 25.31 ?  466 MET A CE    1 
ATOM   3735  N  N     . ASN A 1 467 ? 131.733 138.658 92.025  1.00 13.45 ?  467 ASN A N     1 
ATOM   3736  C  CA    . ASN A 1 467 ? 131.531 138.025 90.721  1.00 16.31 ?  467 ASN A CA    1 
ATOM   3737  C  C     . ASN A 1 467 ? 132.802 138.041 89.879  1.00 18.38 ?  467 ASN A C     1 
ATOM   3738  O  O     . ASN A 1 467 ? 132.740 138.082 88.648  1.00 23.98 ?  467 ASN A O     1 
ATOM   3739  C  CB    . ASN A 1 467 ? 130.378 138.675 89.950  1.00 20.54 ?  467 ASN A CB    1 
ATOM   3740  C  CG    . ASN A 1 467 ? 129.555 137.667 89.177  1.00 23.54 ?  467 ASN A CG    1 
ATOM   3741  O  OD1   . ASN A 1 467 ? 129.759 136.460 89.298  1.00 31.27 ?  467 ASN A OD1   1 
ATOM   3742  N  ND2   . ASN A 1 467 ? 128.618 138.157 88.377  1.00 23.37 ?  467 ASN A ND2   1 
ATOM   3743  N  N     . LEU A 1 468 ? 133.965 138.016 90.530  1.00 18.69 ?  468 LEU A N     1 
ATOM   3744  C  CA    . LEU A 1 468 ? 135.217 137.923 89.787  1.00 13.32 ?  468 LEU A CA    1 
ATOM   3745  C  C     . LEU A 1 468 ? 135.336 136.575 89.093  1.00 20.58 ?  468 LEU A C     1 
ATOM   3746  O  O     . LEU A 1 468 ? 135.591 136.504 87.885  1.00 21.33 ?  468 LEU A O     1 
ATOM   3747  C  CB    . LEU A 1 468 ? 136.404 138.151 90.721  1.00 22.42 ?  468 LEU A CB    1 
ATOM   3748  C  CG    . LEU A 1 468 ? 137.784 137.885 90.118  1.00 19.10 ?  468 LEU A CG    1 
ATOM   3749  C  CD1   . LEU A 1 468 ? 138.128 138.928 89.068  1.00 16.67 ?  468 LEU A CD1   1 
ATOM   3750  C  CD2   . LEU A 1 468 ? 138.848 137.834 91.198  1.00 14.68 ?  468 LEU A CD2   1 
ATOM   3751  N  N     . HIS A 1 469 ? 135.132 135.489 89.842  1.00 25.22 ?  469 HIS A N     1 
ATOM   3752  C  CA    . HIS A 1 469 ? 135.206 134.162 89.245  1.00 16.21 ?  469 HIS A CA    1 
ATOM   3753  C  C     . HIS A 1 469 ? 134.071 133.941 88.259  1.00 25.21 ?  469 HIS A C     1 
ATOM   3754  O  O     . HIS A 1 469 ? 134.265 133.307 87.219  1.00 33.67 ?  469 HIS A O     1 
ATOM   3755  C  CB    . HIS A 1 469 ? 135.190 133.085 90.326  1.00 17.64 ?  469 HIS A CB    1 
ATOM   3756  C  CG    . HIS A 1 469 ? 135.565 131.727 89.821  1.00 22.56 ?  469 HIS A CG    1 
ATOM   3757  N  ND1   . HIS A 1 469 ? 135.434 130.586 90.580  1.00 27.87 ?  469 HIS A ND1   1 
ATOM   3758  C  CD2   . HIS A 1 469 ? 136.071 131.329 88.629  1.00 23.49 ?  469 HIS A CD2   1 
ATOM   3759  C  CE1   . HIS A 1 469 ? 135.840 129.543 89.879  1.00 23.94 ?  469 HIS A CE1   1 
ATOM   3760  N  NE2   . HIS A 1 469 ? 136.232 129.967 88.692  1.00 28.10 ?  469 HIS A NE2   1 
ATOM   3761  N  N     . GLY A 1 470 ? 132.877 134.446 88.570  1.00 24.88 ?  470 GLY A N     1 
ATOM   3762  C  CA    . GLY A 1 470 ? 131.785 134.355 87.616  1.00 20.72 ?  470 GLY A CA    1 
ATOM   3763  C  C     . GLY A 1 470 ? 132.108 135.051 86.310  1.00 18.09 ?  470 GLY A C     1 
ATOM   3764  O  O     . GLY A 1 470 ? 131.919 134.490 85.229  1.00 35.24 ?  470 GLY A O     1 
ATOM   3765  N  N     . TYR A 1 471 ? 132.628 136.277 86.396  1.00 17.42 ?  471 TYR A N     1 
ATOM   3766  C  CA    . TYR A 1 471 ? 132.980 137.013 85.187  1.00 21.95 ?  471 TYR A CA    1 
ATOM   3767  C  C     . TYR A 1 471 ? 134.067 136.288 84.401  1.00 25.73 ?  471 TYR A C     1 
ATOM   3768  O  O     . TYR A 1 471 ? 134.006 136.202 83.171  1.00 28.80 ?  471 TYR A O     1 
ATOM   3769  C  CB    . TYR A 1 471 ? 133.439 138.429 85.534  1.00 22.09 ?  471 TYR A CB    1 
ATOM   3770  C  CG    . TYR A 1 471 ? 133.974 139.172 84.334  1.00 19.48 ?  471 TYR A CG    1 
ATOM   3771  C  CD1   . TYR A 1 471 ? 133.109 139.760 83.422  1.00 23.38 ?  471 TYR A CD1   1 
ATOM   3772  C  CD2   . TYR A 1 471 ? 135.338 139.256 84.090  1.00 18.44 ?  471 TYR A CD2   1 
ATOM   3773  C  CE1   . TYR A 1 471 ? 133.586 140.429 82.316  1.00 25.73 ?  471 TYR A CE1   1 
ATOM   3774  C  CE2   . TYR A 1 471 ? 135.824 139.919 82.982  1.00 22.96 ?  471 TYR A CE2   1 
ATOM   3775  C  CZ    . TYR A 1 471 ? 134.943 140.504 82.100  1.00 25.21 ?  471 TYR A CZ    1 
ATOM   3776  O  OH    . TYR A 1 471 ? 135.417 141.166 80.994  1.00 31.66 ?  471 TYR A OH    1 
ATOM   3777  N  N     . LEU A 1 472 ? 135.084 135.778 85.099  1.00 27.82 ?  472 LEU A N     1 
ATOM   3778  C  CA    . LEU A 1 472 ? 136.181 135.098 84.417  1.00 24.74 ?  472 LEU A CA    1 
ATOM   3779  C  C     . LEU A 1 472 ? 135.715 133.804 83.759  1.00 27.35 ?  472 LEU A C     1 
ATOM   3780  O  O     . LEU A 1 472 ? 136.142 133.481 82.646  1.00 32.46 ?  472 LEU A O     1 
ATOM   3781  C  CB    . LEU A 1 472 ? 137.321 134.825 85.399  1.00 25.71 ?  472 LEU A CB    1 
ATOM   3782  C  CG    . LEU A 1 472 ? 138.062 136.048 85.942  1.00 24.59 ?  472 LEU A CG    1 
ATOM   3783  C  CD1   . LEU A 1 472 ? 138.926 135.669 87.133  1.00 23.05 ?  472 LEU A CD1   1 
ATOM   3784  C  CD2   . LEU A 1 472 ? 138.900 136.694 84.851  1.00 23.35 ?  472 LEU A CD2   1 
ATOM   3785  N  N     . ALA A 1 473 ? 134.845 133.049 84.433  1.00 26.73 ?  473 ALA A N     1 
ATOM   3786  C  CA    . ALA A 1 473 ? 134.375 131.784 83.884  1.00 24.56 ?  473 ALA A CA    1 
ATOM   3787  C  C     . ALA A 1 473 ? 133.437 132.002 82.702  1.00 35.21 ?  473 ALA A C     1 
ATOM   3788  O  O     . ALA A 1 473 ? 133.504 131.268 81.710  1.00 42.98 ?  473 ALA A O     1 
ATOM   3789  C  CB    . ALA A 1 473 ? 133.689 130.965 84.975  1.00 27.08 ?  473 ALA A CB    1 
ATOM   3790  N  N     . GLN A 1 474 ? 132.558 133.005 82.784  1.00 29.14 ?  474 GLN A N     1 
ATOM   3791  C  CA    . GLN A 1 474 ? 131.684 133.310 81.657  1.00 29.13 ?  474 GLN A CA    1 
ATOM   3792  C  C     . GLN A 1 474 ? 132.424 133.947 80.489  1.00 32.16 ?  474 GLN A C     1 
ATOM   3793  O  O     . GLN A 1 474 ? 131.830 134.111 79.419  1.00 36.34 ?  474 GLN A O     1 
ATOM   3794  C  CB    . GLN A 1 474 ? 130.538 134.221 82.097  1.00 28.84 ?  474 GLN A CB    1 
ATOM   3795  C  CG    . GLN A 1 474 ? 129.745 133.704 83.281  1.00 30.82 ?  474 GLN A CG    1 
ATOM   3796  C  CD    . GLN A 1 474 ? 128.322 134.213 83.292  1.00 32.74 ?  474 GLN A CD    1 
ATOM   3797  O  OE1   . GLN A 1 474 ? 127.676 134.307 82.249  1.00 37.49 ?  474 GLN A OE1   1 
ATOM   3798  N  NE2   . GLN A 1 474 ? 127.823 134.553 84.475  1.00 31.46 ?  474 GLN A NE2   1 
ATOM   3799  N  N     . ASN A 1 475 ? 133.695 134.310 80.664  1.00 33.08 ?  475 ASN A N     1 
ATOM   3800  C  CA    . ASN A 1 475 ? 134.512 134.856 79.589  1.00 35.90 ?  475 ASN A CA    1 
ATOM   3801  C  C     . ASN A 1 475 ? 135.617 133.897 79.163  1.00 35.04 ?  475 ASN A C     1 
ATOM   3802  O  O     . ASN A 1 475 ? 136.561 134.306 78.480  1.00 33.44 ?  475 ASN A O     1 
ATOM   3803  C  CB    . ASN A 1 475 ? 135.103 136.202 80.008  1.00 32.28 ?  475 ASN A CB    1 
ATOM   3804  C  CG    . ASN A 1 475 ? 134.077 137.314 79.995  1.00 31.54 ?  475 ASN A CG    1 
ATOM   3805  O  OD1   . ASN A 1 475 ? 133.882 137.982 78.981  1.00 33.91 ?  475 ASN A OD1   1 
ATOM   3806  N  ND2   . ASN A 1 475 ? 133.403 137.507 81.121  1.00 29.10 ?  475 ASN A ND2   1 
ATOM   3807  N  N     . GLY A 1 476 ? 135.514 132.629 79.550  1.00 29.82 ?  476 GLY A N     1 
ATOM   3808  C  CA    . GLY A 1 476 ? 136.502 131.636 79.158  1.00 29.15 ?  476 GLY A CA    1 
ATOM   3809  C  C     . GLY A 1 476 ? 137.885 131.882 79.718  1.00 35.07 ?  476 GLY A C     1 
ATOM   3810  O  O     . GLY A 1 476 ? 138.879 131.733 78.998  1.00 37.01 ?  476 GLY A O     1 
ATOM   3811  N  N     . ILE A 1 477 ? 137.974 132.259 80.991  1.00 31.50 ?  477 ILE A N     1 
ATOM   3812  C  CA    . ILE A 1 477 ? 139.247 132.523 81.649  1.00 26.83 ?  477 ILE A CA    1 
ATOM   3813  C  C     . ILE A 1 477 ? 139.297 131.732 82.947  1.00 31.18 ?  477 ILE A C     1 
ATOM   3814  O  O     . ILE A 1 477 ? 138.399 131.854 83.788  1.00 34.93 ?  477 ILE A O     1 
ATOM   3815  C  CB    . ILE A 1 477 ? 139.449 134.025 81.924  1.00 27.36 ?  477 ILE A CB    1 
ATOM   3816  C  CG1   . ILE A 1 477 ? 139.491 134.805 80.611  1.00 30.88 ?  477 ILE A CG1   1 
ATOM   3817  C  CG2   . ILE A 1 477 ? 140.724 134.251 82.713  1.00 28.51 ?  477 ILE A CG2   1 
ATOM   3818  C  CD1   . ILE A 1 477 ? 139.278 136.283 80.782  1.00 30.35 ?  477 ILE A CD1   1 
ATOM   3819  N  N     . ALA A 1 478 ? 140.341 130.925 83.108  1.00 31.04 ?  478 ALA A N     1 
ATOM   3820  C  CA    . ALA A 1 478 ? 140.530 130.184 84.345  1.00 27.78 ?  478 ALA A CA    1 
ATOM   3821  C  C     . ALA A 1 478 ? 140.958 131.126 85.463  1.00 30.47 ?  478 ALA A C     1 
ATOM   3822  O  O     . ALA A 1 478 ? 141.747 132.049 85.249  1.00 31.20 ?  478 ALA A O     1 
ATOM   3823  C  CB    . ALA A 1 478 ? 141.572 129.084 84.155  1.00 28.28 ?  478 ALA A CB    1 
ATOM   3824  N  N     . TYR A 1 479 ? 140.430 130.883 86.666  1.00 29.75 ?  479 TYR A N     1 
ATOM   3825  C  CA    . TYR A 1 479 ? 140.736 131.749 87.801  1.00 22.93 ?  479 TYR A CA    1 
ATOM   3826  C  C     . TYR A 1 479 ? 142.222 131.745 88.130  1.00 27.34 ?  479 TYR A C     1 
ATOM   3827  O  O     . TYR A 1 479 ? 142.760 132.764 88.579  1.00 33.22 ?  479 TYR A O     1 
ATOM   3828  C  CB    . TYR A 1 479 ? 139.916 131.312 89.016  1.00 21.32 ?  479 TYR A CB    1 
ATOM   3829  C  CG    . TYR A 1 479 ? 140.023 132.223 90.220  1.00 28.50 ?  479 TYR A CG    1 
ATOM   3830  C  CD1   . TYR A 1 479 ? 141.007 132.027 91.180  1.00 26.50 ?  479 TYR A CD1   1 
ATOM   3831  C  CD2   . TYR A 1 479 ? 139.128 133.268 90.404  1.00 22.04 ?  479 TYR A CD2   1 
ATOM   3832  C  CE1   . TYR A 1 479 ? 141.103 132.852 92.282  1.00 22.41 ?  479 TYR A CE1   1 
ATOM   3833  C  CE2   . TYR A 1 479 ? 139.216 134.097 91.503  1.00 22.90 ?  479 TYR A CE2   1 
ATOM   3834  C  CZ    . TYR A 1 479 ? 140.205 133.885 92.438  1.00 29.54 ?  479 TYR A CZ    1 
ATOM   3835  O  OH    . TYR A 1 479 ? 140.295 134.710 93.536  1.00 31.36 ?  479 TYR A OH    1 
ATOM   3836  N  N     . GLU A 1 480 ? 142.901 130.623 87.916  1.00 30.91 ?  480 GLU A N     1 
ATOM   3837  C  CA    . GLU A 1 480 ? 144.324 130.511 88.203  1.00 29.89 ?  480 GLU A CA    1 
ATOM   3838  C  C     . GLU A 1 480 ? 145.204 130.926 87.034  1.00 32.47 ?  480 GLU A C     1 
ATOM   3839  O  O     . GLU A 1 480 ? 146.432 130.918 87.170  1.00 37.66 ?  480 GLU A O     1 
ATOM   3840  C  CB    . GLU A 1 480 ? 144.667 129.077 88.609  1.00 29.48 ?  480 GLU A CB    1 
ATOM   3841  C  CG    . GLU A 1 480 ? 143.875 128.549 89.787  1.00 30.62 ?  480 GLU A CG    1 
ATOM   3842  C  CD    . GLU A 1 480 ? 143.741 127.042 89.754  1.00 37.66 ?  480 GLU A CD    1 
ATOM   3843  O  OE1   . GLU A 1 480 ? 142.875 126.538 89.009  1.00 38.85 ?  480 GLU A OE1   1 
ATOM   3844  O  OE2   . GLU A 1 480 ? 144.506 126.361 90.467  1.00 38.05 -1 480 GLU A OE2   1 
ATOM   3845  N  N     . SER A 1 481 ? 144.617 131.283 85.897  1.00 30.10 ?  481 SER A N     1 
ATOM   3846  C  CA    . SER A 1 481 ? 145.407 131.631 84.730  1.00 27.49 ?  481 SER A CA    1 
ATOM   3847  C  C     . SER A 1 481 ? 146.070 132.996 84.913  1.00 31.91 ?  481 SER A C     1 
ATOM   3848  O  O     . SER A 1 481 ? 145.555 133.854 85.634  1.00 32.24 ?  481 SER A O     1 
ATOM   3849  C  CB    . SER A 1 481 ? 144.533 131.643 83.480  1.00 29.10 ?  481 SER A CB    1 
ATOM   3850  O  OG    . SER A 1 481 ? 143.909 132.901 83.309  1.00 33.68 ?  481 SER A OG    1 
ATOM   3851  N  N     . PRO A 1 482 ? 147.224 133.215 84.277  1.00 37.78 ?  482 PRO A N     1 
ATOM   3852  C  CA    . PRO A 1 482 ? 147.826 134.559 84.305  1.00 30.91 ?  482 PRO A CA    1 
ATOM   3853  C  C     . PRO A 1 482 ? 146.939 135.622 83.683  1.00 29.86 ?  482 PRO A C     1 
ATOM   3854  O  O     . PRO A 1 482 ? 147.044 136.797 84.055  1.00 34.98 ?  482 PRO A O     1 
ATOM   3855  C  CB    . PRO A 1 482 ? 149.129 134.375 83.517  1.00 30.41 ?  482 PRO A CB    1 
ATOM   3856  C  CG    . PRO A 1 482 ? 149.415 132.913 83.580  1.00 32.89 ?  482 PRO A CG    1 
ATOM   3857  C  CD    . PRO A 1 482 ? 148.080 132.240 83.584  1.00 31.72 ?  482 PRO A CD    1 
ATOM   3858  N  N     . GLU A 1 483 ? 146.072 135.245 82.741  1.00 36.10 ?  483 GLU A N     1 
ATOM   3859  C  CA    . GLU A 1 483 ? 145.136 136.203 82.162  1.00 32.70 ?  483 GLU A CA    1 
ATOM   3860  C  C     . GLU A 1 483 ? 144.140 136.699 83.202  1.00 31.18 ?  483 GLU A C     1 
ATOM   3861  O  O     . GLU A 1 483 ? 143.768 137.878 83.201  1.00 35.55 ?  483 GLU A O     1 
ATOM   3862  C  CB    . GLU A 1 483 ? 144.404 135.573 80.977  1.00 33.67 ?  483 GLU A CB    1 
ATOM   3863  C  CG    . GLU A 1 483 ? 145.257 135.423 79.731  1.00 36.84 ?  483 GLU A CG    1 
ATOM   3864  C  CD    . GLU A 1 483 ? 146.033 134.120 79.706  1.00 39.71 ?  483 GLU A CD    1 
ATOM   3865  O  OE1   . GLU A 1 483 ? 146.113 133.452 80.758  1.00 37.12 ?  483 GLU A OE1   1 
ATOM   3866  O  OE2   . GLU A 1 483 ? 146.565 133.766 78.634  1.00 41.10 -1 483 GLU A OE2   1 
ATOM   3867  N  N     . ALA A 1 484 ? 143.689 135.811 84.090  1.00 26.19 ?  484 ALA A N     1 
ATOM   3868  C  CA    . ALA A 1 484 ? 142.787 136.229 85.158  1.00 25.77 ?  484 ALA A CA    1 
ATOM   3869  C  C     . ALA A 1 484 ? 143.459 137.233 86.085  1.00 25.99 ?  484 ALA A C     1 
ATOM   3870  O  O     . ALA A 1 484 ? 142.843 138.225 86.489  1.00 25.65 ?  484 ALA A O     1 
ATOM   3871  C  CB    . ALA A 1 484 ? 142.306 135.014 85.946  1.00 20.79 ?  484 ALA A CB    1 
ATOM   3872  N  N     . ARG A 1 485 ? 144.723 136.990 86.436  1.00 27.55 ?  485 ARG A N     1 
ATOM   3873  C  CA    . ARG A 1 485 ? 145.446 137.938 87.275  1.00 21.77 ?  485 ARG A CA    1 
ATOM   3874  C  C     . ARG A 1 485 ? 145.692 139.253 86.549  1.00 22.14 ?  485 ARG A C     1 
ATOM   3875  O  O     . ARG A 1 485 ? 145.647 140.317 87.172  1.00 30.74 ?  485 ARG A O     1 
ATOM   3876  C  CB    . ARG A 1 485 ? 146.768 137.330 87.741  1.00 24.49 ?  485 ARG A CB    1 
ATOM   3877  C  CG    . ARG A 1 485 ? 146.604 136.247 88.789  1.00 25.08 ?  485 ARG A CG    1 
ATOM   3878  C  CD    . ARG A 1 485 ? 147.941 135.846 89.377  1.00 26.67 ?  485 ARG A CD    1 
ATOM   3879  N  NE    . ARG A 1 485 ? 148.840 135.295 88.369  1.00 27.79 ?  485 ARG A NE    1 
ATOM   3880  C  CZ    . ARG A 1 485 ? 148.831 134.031 87.972  1.00 29.59 ?  485 ARG A CZ    1 
ATOM   3881  N  NH1   . ARG A 1 485 ? 147.973 133.156 88.468  1.00 27.74 1  485 ARG A NH1   1 
ATOM   3882  N  NH2   . ARG A 1 485 ? 149.707 133.635 87.053  1.00 25.12 ?  485 ARG A NH2   1 
ATOM   3883  N  N     . ASP A 1 486 ? 145.952 139.202 85.242  1.00 29.60 ?  486 ASP A N     1 
ATOM   3884  C  CA    . ASP A 1 486 ? 146.088 140.424 84.457  1.00 28.93 ?  486 ASP A CA    1 
ATOM   3885  C  C     . ASP A 1 486 ? 144.795 141.232 84.477  1.00 29.97 ?  486 ASP A C     1 
ATOM   3886  O  O     . ASP A 1 486 ? 144.812 142.459 84.662  1.00 35.68 ?  486 ASP A O     1 
ATOM   3887  C  CB    . ASP A 1 486 ? 146.485 140.069 83.025  1.00 33.99 ?  486 ASP A CB    1 
ATOM   3888  C  CG    . ASP A 1 486 ? 146.831 141.282 82.198  1.00 39.53 ?  486 ASP A CG    1 
ATOM   3889  O  OD1   . ASP A 1 486 ? 147.734 142.046 82.601  1.00 38.33 ?  486 ASP A OD1   1 
ATOM   3890  O  OD2   . ASP A 1 486 ? 146.201 141.467 81.136  1.00 40.45 -1 486 ASP A OD2   1 
ATOM   3891  N  N     . PHE A 1 487 ? 143.661 140.556 84.292  1.00 27.52 ?  487 PHE A N     1 
ATOM   3892  C  CA    . PHE A 1 487 ? 142.380 141.246 84.350  1.00 24.06 ?  487 PHE A CA    1 
ATOM   3893  C  C     . PHE A 1 487 ? 142.130 141.833 85.729  1.00 23.48 ?  487 PHE A C     1 
ATOM   3894  O  O     . PHE A 1 487 ? 141.640 142.959 85.847  1.00 28.50 ?  487 PHE A O     1 
ATOM   3895  C  CB    . PHE A 1 487 ? 141.230 140.312 83.981  1.00 23.47 ?  487 PHE A CB    1 
ATOM   3896  C  CG    . PHE A 1 487 ? 139.892 140.837 84.407  1.00 24.82 ?  487 PHE A CG    1 
ATOM   3897  C  CD1   . PHE A 1 487 ? 139.271 141.838 83.682  1.00 22.38 ?  487 PHE A CD1   1 
ATOM   3898  C  CD2   . PHE A 1 487 ? 139.271 140.359 85.550  1.00 24.88 ?  487 PHE A CD2   1 
ATOM   3899  C  CE1   . PHE A 1 487 ? 138.051 142.342 84.077  1.00 24.63 ?  487 PHE A CE1   1 
ATOM   3900  C  CE2   . PHE A 1 487 ? 138.052 140.861 85.949  1.00 25.98 ?  487 PHE A CE2   1 
ATOM   3901  C  CZ    . PHE A 1 487 ? 137.441 141.853 85.211  1.00 24.61 ?  487 PHE A CZ    1 
ATOM   3902  N  N     . ALA A 1 488 ? 142.420 141.071 86.784  1.00 20.43 ?  488 ALA A N     1 
ATOM   3903  C  CA    . ALA A 1 488 ? 142.214 141.582 88.133  1.00 16.31 ?  488 ALA A CA    1 
ATOM   3904  C  C     . ALA A 1 488 ? 143.085 142.803 88.386  1.00 23.39 ?  488 ALA A C     1 
ATOM   3905  O  O     . ALA A 1 488 ? 142.617 143.806 88.937  1.00 28.14 ?  488 ALA A O     1 
ATOM   3906  C  CB    . ALA A 1 488 ? 142.503 140.490 89.161  1.00 22.74 ?  488 ALA A CB    1 
ATOM   3907  N  N     . ASN A 1 489 ? 144.348 142.745 87.959  1.00 25.91 ?  489 ASN A N     1 
ATOM   3908  C  CA    . ASN A 1 489 ? 145.245 143.885 88.096  1.00 21.39 ?  489 ASN A CA    1 
ATOM   3909  C  C     . ASN A 1 489 ? 144.665 145.118 87.422  1.00 20.60 ?  489 ASN A C     1 
ATOM   3910  O  O     . ASN A 1 489 ? 144.530 146.175 88.049  1.00 23.98 ?  489 ASN A O     1 
ATOM   3911  C  CB    . ASN A 1 489 ? 146.610 143.539 87.498  1.00 17.63 ?  489 ASN A CB    1 
ATOM   3912  C  CG    . ASN A 1 489 ? 147.658 144.586 87.789  1.00 25.69 ?  489 ASN A CG    1 
ATOM   3913  O  OD1   . ASN A 1 489 ? 147.768 145.076 88.911  1.00 31.29 ?  489 ASN A OD1   1 
ATOM   3914  N  ND2   . ASN A 1 489 ? 148.442 144.931 86.776  1.00 28.39 ?  489 ASN A ND2   1 
ATOM   3915  N  N     . THR A 1 490 ? 144.283 144.992 86.149  1.00 22.74 ?  490 THR A N     1 
ATOM   3916  C  CA    . THR A 1 490 ? 143.780 146.154 85.422  1.00 21.31 ?  490 THR A CA    1 
ATOM   3917  C  C     . THR A 1 490 ? 142.474 146.664 86.024  1.00 22.67 ?  490 THR A C     1 
ATOM   3918  O  O     . THR A 1 490 ? 142.320 147.868 86.268  1.00 24.89 ?  490 THR A O     1 
ATOM   3919  C  CB    . THR A 1 490 ? 143.592 145.816 83.945  1.00 28.93 ?  490 THR A CB    1 
ATOM   3920  O  OG1   . THR A 1 490 ? 144.796 145.235 83.431  1.00 33.78 ?  490 THR A OG1   1 
ATOM   3921  C  CG2   . THR A 1 490 ? 143.262 147.074 83.158  1.00 22.59 ?  490 THR A CG2   1 
ATOM   3922  N  N     . PHE A 1 491 ? 141.528 145.760 86.282  1.00 19.82 ?  491 PHE A N     1 
ATOM   3923  C  CA    . PHE A 1 491 ? 140.211 146.159 86.766  1.00 17.95 ?  491 PHE A CA    1 
ATOM   3924  C  C     . PHE A 1 491 ? 140.311 146.852 88.115  1.00 22.82 ?  491 PHE A C     1 
ATOM   3925  O  O     . PHE A 1 491 ? 139.706 147.906 88.330  1.00 22.93 ?  491 PHE A O     1 
ATOM   3926  C  CB    . PHE A 1 491 ? 139.297 144.935 86.852  1.00 22.92 ?  491 PHE A CB    1 
ATOM   3927  C  CG    . PHE A 1 491 ? 137.964 145.214 87.490  1.00 19.23 ?  491 PHE A CG    1 
ATOM   3928  C  CD1   . PHE A 1 491 ? 136.901 145.667 86.730  1.00 17.23 ?  491 PHE A CD1   1 
ATOM   3929  C  CD2   . PHE A 1 491 ? 137.770 145.014 88.849  1.00 17.98 ?  491 PHE A CD2   1 
ATOM   3930  C  CE1   . PHE A 1 491 ? 135.677 145.927 87.309  1.00 15.75 ?  491 PHE A CE1   1 
ATOM   3931  C  CE2   . PHE A 1 491 ? 136.549 145.273 89.433  1.00 17.31 ?  491 PHE A CE2   1 
ATOM   3932  C  CZ    . PHE A 1 491 ? 135.500 145.730 88.661  1.00 19.56 ?  491 PHE A CZ    1 
ATOM   3933  N  N     . PHE A 1 492 ? 141.086 146.283 89.039  1.00 23.17 ?  492 PHE A N     1 
ATOM   3934  C  CA    . PHE A 1 492 ? 141.184 146.886 90.357  1.00 12.41 ?  492 PHE A CA    1 
ATOM   3935  C  C     . PHE A 1 492 ? 142.084 148.110 90.374  1.00 14.90 ?  492 PHE A C     1 
ATOM   3936  O  O     . PHE A 1 492 ? 141.894 148.978 91.229  1.00 20.08 ?  492 PHE A O     1 
ATOM   3937  C  CB    . PHE A 1 492 ? 141.650 145.840 91.368  1.00 19.66 ?  492 PHE A CB    1 
ATOM   3938  C  CG    . PHE A 1 492 ? 140.572 144.868 91.752  1.00 16.33 ?  492 PHE A CG    1 
ATOM   3939  C  CD1   . PHE A 1 492 ? 139.593 145.231 92.660  1.00 11.74 ?  492 PHE A CD1   1 
ATOM   3940  C  CD2   . PHE A 1 492 ? 140.517 143.608 91.184  1.00 16.15 ?  492 PHE A CD2   1 
ATOM   3941  C  CE1   . PHE A 1 492 ? 138.593 144.348 93.009  1.00 12.40 ?  492 PHE A CE1   1 
ATOM   3942  C  CE2   . PHE A 1 492 ? 139.517 142.720 91.529  1.00 14.11 ?  492 PHE A CE2   1 
ATOM   3943  C  CZ    . PHE A 1 492 ? 138.555 143.091 92.443  1.00 16.69 ?  492 PHE A CZ    1 
ATOM   3944  N  N     . MET A 1 493 ? 143.018 148.242 89.427  1.00 19.05 ?  493 MET A N     1 
ATOM   3945  C  CA    . MET A 1 493 ? 143.727 149.509 89.307  1.00 16.78 ?  493 MET A CA    1 
ATOM   3946  C  C     . MET A 1 493 ? 142.783 150.606 88.838  1.00 16.20 ?  493 MET A C     1 
ATOM   3947  O  O     . MET A 1 493 ? 142.846 151.733 89.335  1.00 22.30 ?  493 MET A O     1 
ATOM   3948  C  CB    . MET A 1 493 ? 144.941 149.346 88.381  1.00 17.19 ?  493 MET A CB    1 
ATOM   3949  C  CG    . MET A 1 493 ? 145.548 150.600 87.704  1.00 17.53 ?  493 MET A CG    1 
ATOM   3950  S  SD    . MET A 1 493 ? 144.568 151.693 86.647  1.00 32.83 ?  493 MET A SD    1 
ATOM   3951  C  CE    . MET A 1 493 ? 144.533 150.733 85.142  1.00 21.93 ?  493 MET A CE    1 
ATOM   3952  N  N     . MET A 1 494 ? 141.896 150.300 87.883  1.00 20.52 ?  494 MET A N     1 
ATOM   3953  C  CA    . MET A 1 494 ? 140.893 151.288 87.487  1.00 19.50 ?  494 MET A CA    1 
ATOM   3954  C  C     . MET A 1 494 ? 139.940 151.603 88.634  1.00 21.79 ?  494 MET A C     1 
ATOM   3955  O  O     . MET A 1 494 ? 139.542 152.760 88.818  1.00 24.82 ?  494 MET A O     1 
ATOM   3956  C  CB    . MET A 1 494 ? 140.105 150.817 86.263  1.00 17.94 ?  494 MET A CB    1 
ATOM   3957  C  CG    . MET A 1 494 ? 140.940 150.249 85.136  1.00 22.98 ?  494 MET A CG    1 
ATOM   3958  S  SD    . MET A 1 494 ? 140.069 150.196 83.559  1.00 39.60 ?  494 MET A SD    1 
ATOM   3959  C  CE    . MET A 1 494 ? 138.835 151.469 83.799  1.00 24.17 ?  494 MET A CE    1 
ATOM   3960  N  N     . VAL A 1 495 ? 139.554 150.587 89.407  1.00 19.25 ?  495 VAL A N     1 
ATOM   3961  C  CA    . VAL A 1 495 ? 138.679 150.818 90.554  1.00 14.86 ?  495 VAL A CA    1 
ATOM   3962  C  C     . VAL A 1 495 ? 139.355 151.744 91.556  1.00 21.00 ?  495 VAL A C     1 
ATOM   3963  O  O     . VAL A 1 495 ? 138.744 152.693 92.058  1.00 32.06 ?  495 VAL A O     1 
ATOM   3964  C  CB    . VAL A 1 495 ? 138.274 149.482 91.204  1.00 19.73 ?  495 VAL A CB    1 
ATOM   3965  C  CG1   . VAL A 1 495 ? 137.615 149.726 92.552  1.00 13.65 ?  495 VAL A CG1   1 
ATOM   3966  C  CG2   . VAL A 1 495 ? 137.336 148.713 90.294  1.00 14.21 ?  495 VAL A CG2   1 
ATOM   3967  N  N     . ASN A 1 496 ? 140.632 151.489 91.852  1.00 18.39 ?  496 ASN A N     1 
ATOM   3968  C  CA    . ASN A 1 496 ? 141.375 152.355 92.760  1.00 11.72 ?  496 ASN A CA    1 
ATOM   3969  C  C     . ASN A 1 496 ? 141.508 153.764 92.197  1.00 16.27 ?  496 ASN A C     1 
ATOM   3970  O  O     . ASN A 1 496 ? 141.367 154.748 92.930  1.00 26.76 ?  496 ASN A O     1 
ATOM   3971  C  CB    . ASN A 1 496 ? 142.754 151.756 93.039  1.00 17.45 ?  496 ASN A CB    1 
ATOM   3972  C  CG    . ASN A 1 496 ? 143.391 152.318 94.290  1.00 18.49 ?  496 ASN A CG    1 
ATOM   3973  O  OD1   . ASN A 1 496 ? 142.701 152.714 95.227  1.00 24.08 ?  496 ASN A OD1   1 
ATOM   3974  N  ND2   . ASN A 1 496 ? 144.716 152.356 94.312  1.00 18.71 ?  496 ASN A ND2   1 
ATOM   3975  N  N     . PHE A 1 497 ? 141.777 153.879 90.895  1.00 18.94 ?  497 PHE A N     1 
ATOM   3976  C  CA    . PHE A 1 497 ? 141.924 155.188 90.270  1.00 14.12 ?  497 PHE A CA    1 
ATOM   3977  C  C     . PHE A 1 497 ? 140.645 156.001 90.403  1.00 19.38 ?  497 PHE A C     1 
ATOM   3978  O  O     . PHE A 1 497 ? 140.673 157.163 90.826  1.00 24.23 ?  497 PHE A O     1 
ATOM   3979  C  CB    . PHE A 1 497 ? 142.305 155.017 88.797  1.00 17.00 ?  497 PHE A CB    1 
ATOM   3980  C  CG    . PHE A 1 497 ? 142.478 156.312 88.053  1.00 20.91 ?  497 PHE A CG    1 
ATOM   3981  C  CD1   . PHE A 1 497 ? 141.404 156.909 87.415  1.00 20.09 ?  497 PHE A CD1   1 
ATOM   3982  C  CD2   . PHE A 1 497 ? 143.718 156.922 87.976  1.00 25.45 ?  497 PHE A CD2   1 
ATOM   3983  C  CE1   . PHE A 1 497 ? 141.561 158.097 86.729  1.00 22.74 ?  497 PHE A CE1   1 
ATOM   3984  C  CE2   . PHE A 1 497 ? 143.880 158.110 87.290  1.00 23.32 ?  497 PHE A CE2   1 
ATOM   3985  C  CZ    . PHE A 1 497 ? 142.800 158.696 86.666  1.00 22.22 ?  497 PHE A CZ    1 
ATOM   3986  N  N     . TYR A 1 498 ? 139.506 155.399 90.064  1.00 25.25 ?  498 TYR A N     1 
ATOM   3987  C  CA    . TYR A 1 498 ? 138.255 156.145 90.105  1.00 18.22 ?  498 TYR A CA    1 
ATOM   3988  C  C     . TYR A 1 498 ? 137.773 156.361 91.533  1.00 23.26 ?  498 TYR A C     1 
ATOM   3989  O  O     . TYR A 1 498 ? 137.123 157.371 91.813  1.00 29.58 ?  498 TYR A O     1 
ATOM   3990  C  CB    . TYR A 1 498 ? 137.198 155.438 89.260  1.00 19.42 ?  498 TYR A CB    1 
ATOM   3991  C  CG    . TYR A 1 498 ? 137.517 155.494 87.785  1.00 22.71 ?  498 TYR A CG    1 
ATOM   3992  C  CD1   . TYR A 1 498 ? 137.724 156.713 87.151  1.00 23.96 ?  498 TYR A CD1   1 
ATOM   3993  C  CD2   . TYR A 1 498 ? 137.635 154.335 87.032  1.00 23.81 ?  498 TYR A CD2   1 
ATOM   3994  C  CE1   . TYR A 1 498 ? 138.026 156.775 85.806  1.00 19.02 ?  498 TYR A CE1   1 
ATOM   3995  C  CE2   . TYR A 1 498 ? 137.938 154.388 85.686  1.00 26.18 ?  498 TYR A CE2   1 
ATOM   3996  C  CZ    . TYR A 1 498 ? 138.131 155.610 85.079  1.00 27.69 ?  498 TYR A CZ    1 
ATOM   3997  O  OH    . TYR A 1 498 ? 138.431 155.667 83.738  1.00 33.10 ?  498 TYR A OH    1 
ATOM   3998  N  N     . SER A 1 499 ? 138.112 155.458 92.456  1.00 21.40 ?  499 SER A N     1 
ATOM   3999  C  CA    . SER A 1 499 ? 137.789 155.681 93.860  1.00 7.93  ?  499 SER A CA    1 
ATOM   4000  C  C     . SER A 1 499 ? 138.578 156.858 94.419  1.00 13.95 ?  499 SER A C     1 
ATOM   4001  O  O     . SER A 1 499 ? 138.024 157.710 95.123  1.00 20.78 ?  499 SER A O     1 
ATOM   4002  C  CB    . SER A 1 499 ? 138.063 154.411 94.665  1.00 10.95 ?  499 SER A CB    1 
ATOM   4003  O  OG    . SER A 1 499 ? 137.351 154.416 95.887  1.00 23.91 ?  499 SER A OG    1 
ATOM   4004  N  N     . ILE A 1 500 ? 139.873 156.929 94.103  1.00 13.96 ?  500 ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 500 ? 140.686 158.062 94.533  1.00 17.91 ?  500 ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 500 ? 140.193 159.347 93.886  1.00 18.43 ?  500 ILE A C     1 
ATOM   4007  O  O     . ILE A 1 500 ? 140.133 160.400 94.530  1.00 27.23 ?  500 ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 500 ? 142.172 157.805 94.219  1.00 20.89 ?  500 ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 500 ? 142.716 156.671 95.083  1.00 17.96 ?  500 ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 500 ? 142.992 159.058 94.448  1.00 14.38 ?  500 ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 500 ? 143.990 156.066 94.553  1.00 17.65 ?  500 ILE A CD1   1 
ATOM   4012  N  N     . GLN A 1 501 ? 139.833 159.284 92.602  1.00 21.74 ?  501 GLN A N     1 
ATOM   4013  C  CA    . GLN A 1 501 ? 139.328 160.466 91.916  1.00 21.17 ?  501 GLN A CA    1 
ATOM   4014  C  C     . GLN A 1 501 ? 138.031 160.958 92.542  1.00 23.95 ?  501 GLN A C     1 
ATOM   4015  O  O     . GLN A 1 501 ? 137.854 162.161 92.749  1.00 33.02 ?  501 GLN A O     1 
ATOM   4016  C  CB    . GLN A 1 501 ? 139.130 160.164 90.431  1.00 26.40 ?  501 GLN A CB    1 
ATOM   4017  C  CG    . GLN A 1 501 ? 139.356 161.357 89.521  1.00 26.12 ?  501 GLN A CG    1 
ATOM   4018  C  CD    . GLN A 1 501 ? 139.131 161.023 88.062  1.00 29.50 ?  501 GLN A CD    1 
ATOM   4019  O  OE1   . GLN A 1 501 ? 138.094 160.473 87.693  1.00 30.35 ?  501 GLN A OE1   1 
ATOM   4020  N  NE2   . GLN A 1 501 ? 140.104 161.353 87.223  1.00 31.13 ?  501 GLN A NE2   1 
ATOM   4021  N  N     . ARG A 1 502 ? 137.115 160.041 92.863  1.00 22.64 ?  502 ARG A N     1 
ATOM   4022  C  CA    . ARG A 1 502 ? 135.863 160.434 93.499  1.00 21.00 ?  502 ARG A CA    1 
ATOM   4023  C  C     . ARG A 1 502 ? 136.100 160.981 94.901  1.00 21.54 ?  502 ARG A C     1 
ATOM   4024  O  O     . ARG A 1 502 ? 135.447 161.945 95.311  1.00 25.89 ?  502 ARG A O     1 
ATOM   4025  C  CB    . ARG A 1 502 ? 134.898 159.251 93.539  1.00 19.91 ?  502 ARG A CB    1 
ATOM   4026  C  CG    . ARG A 1 502 ? 133.480 159.636 93.917  1.00 22.74 ?  502 ARG A CG    1 
ATOM   4027  C  CD    . ARG A 1 502 ? 132.957 160.746 93.025  1.00 23.43 ?  502 ARG A CD    1 
ATOM   4028  N  NE    . ARG A 1 502 ? 131.864 161.477 93.653  1.00 26.60 ?  502 ARG A NE    1 
ATOM   4029  C  CZ    . ARG A 1 502 ? 131.643 162.775 93.494  1.00 25.59 ?  502 ARG A CZ    1 
ATOM   4030  N  NH1   . ARG A 1 502 ? 132.416 163.518 92.721  1.00 29.04 1  502 ARG A NH1   1 
ATOM   4031  N  NH2   . ARG A 1 502 ? 130.620 163.340 94.128  1.00 26.36 ?  502 ARG A NH2   1 
ATOM   4032  N  N     . SER A 1 503 ? 137.022 160.376 95.654  1.00 19.21 ?  503 SER A N     1 
ATOM   4033  C  CA    . SER A 1 503 ? 137.336 160.888 96.984  1.00 20.41 ?  503 SER A CA    1 
ATOM   4034  C  C     . SER A 1 503 ? 137.903 162.299 96.908  1.00 23.19 ?  503 SER A C     1 
ATOM   4035  O  O     . SER A 1 503 ? 137.519 163.176 97.691  1.00 26.02 ?  503 SER A O     1 
ATOM   4036  C  CB    . SER A 1 503 ? 138.319 159.948 97.684  1.00 19.03 ?  503 SER A CB    1 
ATOM   4037  O  OG    . SER A 1 503 ? 138.321 160.157 99.084  1.00 23.30 ?  503 SER A OG    1 
ATOM   4038  N  N     . ALA A 1 504 ? 138.804 162.544 95.955  1.00 24.12 ?  504 ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 504 ? 139.369 163.877 95.788  1.00 21.09 ?  504 ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 504 ? 138.318 164.870 95.311  1.00 28.52 ?  504 ALA A C     1 
ATOM   4041  O  O     . ALA A 1 504 ? 138.323 166.034 95.726  1.00 37.22 ?  504 ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 504 ? 140.546 163.827 94.816  1.00 24.49 ?  504 ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 505 ? 137.404 164.430 94.444  1.00 26.33 ?  505 GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 505 ? 136.332 165.307 93.985  1.00 26.93 ?  505 GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 505 ? 135.394 165.676 95.127  1.00 29.67 ?  505 GLU A C     1 
ATOM   4046  O  O     . GLU A 1 505 ? 134.960 166.827 95.231  1.00 35.60 ?  505 GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 505 ? 135.559 164.639 92.848  1.00 26.49 ?  505 GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 505 ? 136.282 164.647 91.513  1.00 27.33 ?  505 GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 505 ? 135.844 163.512 90.607  1.00 33.62 ?  505 GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 505 ? 134.958 162.733 91.015  1.00 34.56 ?  505 GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 505 ? 136.387 163.399 89.488  1.00 35.30 -1 505 GLU A OE2   1 
ATOM   4052  N  N     . ILE A 1 506 ? 135.070 164.714 95.992  1.00 26.44 ?  506 ILE A N     1 
ATOM   4053  C  CA    . ILE A 1 506 ? 134.231 165.004 97.150  1.00 24.78 ?  506 ILE A CA    1 
ATOM   4054  C  C     . ILE A 1 506 ? 134.953 165.942 98.109  1.00 28.62 ?  506 ILE A C     1 
ATOM   4055  O  O     . ILE A 1 506 ? 134.346 166.858 98.676  1.00 34.21 ?  506 ILE A O     1 
ATOM   4056  C  CB    . ILE A 1 506 ? 133.803 163.696 97.842  1.00 23.01 ?  506 ILE A CB    1 
ATOM   4057  C  CG1   . ILE A 1 506 ? 132.892 162.880 96.924  1.00 26.55 ?  506 ILE A CG1   1 
ATOM   4058  C  CG2   . ILE A 1 506 ? 133.096 163.987 99.155  1.00 23.61 ?  506 ILE A CG2   1 
ATOM   4059  C  CD1   . ILE A 1 506 ? 132.709 161.446 97.366  1.00 21.55 ?  506 ILE A CD1   1 
ATOM   4060  N  N     . ALA A 1 507 ? 136.259 165.735 98.302  1.00 30.57 ?  507 ALA A N     1 
ATOM   4061  C  CA    . ALA A 1 507 ? 137.032 166.638 99.149  1.00 28.17 ?  507 ALA A CA    1 
ATOM   4062  C  C     . ALA A 1 507 ? 137.037 168.055 98.588  1.00 30.16 ?  507 ALA A C     1 
ATOM   4063  O  O     . ALA A 1 507 ? 136.916 169.029 99.340  1.00 33.75 ?  507 ALA A O     1 
ATOM   4064  C  CB    . ALA A 1 507 ? 138.461 166.118 99.302  1.00 24.00 ?  507 ALA A CB    1 
ATOM   4065  N  N     . LYS A 1 508 ? 137.182 168.188 97.269  1.00 34.66 ?  508 LYS A N     1 
ATOM   4066  C  CA    . LYS A 1 508 ? 137.156 169.505 96.641  1.00 32.34 ?  508 LYS A CA    1 
ATOM   4067  C  C     . LYS A 1 508 ? 135.780 170.152 96.758  1.00 37.17 ?  508 LYS A C     1 
ATOM   4068  O  O     . LYS A 1 508 ? 135.674 171.353 97.034  1.00 43.61 ?  508 LYS A O     1 
ATOM   4069  C  CB    . LYS A 1 508 ? 137.575 169.387 95.175  1.00 34.75 ?  508 LYS A CB    1 
ATOM   4070  C  CG    . LYS A 1 508 ? 137.338 170.638 94.350  1.00 36.97 ?  508 LYS A CG    1 
ATOM   4071  C  CD    . LYS A 1 508 ? 137.502 170.353 92.868  1.00 38.51 ?  508 LYS A CD    1 
ATOM   4072  C  CE    . LYS A 1 508 ? 137.306 171.610 92.039  1.00 37.16 ?  508 LYS A CE    1 
ATOM   4073  N  NZ    . LYS A 1 508 ? 138.139 171.596 90.804  1.00 40.86 1  508 LYS A NZ    1 
ATOM   4074  N  N     . GLU A 1 509 ? 134.716 169.375 96.545  1.00 35.71 ?  509 GLU A N     1 
ATOM   4075  C  CA    . GLU A 1 509 ? 133.364 169.922 96.607  1.00 34.30 ?  509 GLU A CA    1 
ATOM   4076  C  C     . GLU A 1 509 ? 133.017 170.379 98.018  1.00 37.22 ?  509 GLU A C     1 
ATOM   4077  O  O     . GLU A 1 509 ? 132.541 171.503 98.218  1.00 41.97 ?  509 GLU A O     1 
ATOM   4078  C  CB    . GLU A 1 509 ? 132.356 168.882 96.118  1.00 33.13 ?  509 GLU A CB    1 
ATOM   4079  C  CG    . GLU A 1 509 ? 132.377 168.653 94.616  1.00 40.38 ?  509 GLU A CG    1 
ATOM   4080  C  CD    . GLU A 1 509 ? 131.937 167.252 94.234  1.00 43.69 ?  509 GLU A CD    1 
ATOM   4081  O  OE1   . GLU A 1 509 ? 131.434 166.524 95.116  1.00 42.01 ?  509 GLU A OE1   1 
ATOM   4082  O  OE2   . GLU A 1 509 ? 132.097 166.879 93.053  1.00 40.06 -1 509 GLU A OE2   1 
ATOM   4083  N  N     . LYS A 1 510 ? 133.248 169.521 99.009  1.00 33.73 ?  510 LYS A N     1 
ATOM   4084  C  CA    . LYS A 1 510 ? 132.943 169.857 100.393 1.00 30.44 ?  510 LYS A CA    1 
ATOM   4085  C  C     . LYS A 1 510 ? 134.018 170.713 101.047 1.00 32.19 ?  510 LYS A C     1 
ATOM   4086  O  O     . LYS A 1 510 ? 133.776 171.259 102.129 1.00 38.71 ?  510 LYS A O     1 
ATOM   4087  C  CB    . LYS A 1 510 ? 132.736 168.578 101.208 1.00 29.73 ?  510 LYS A CB    1 
ATOM   4088  C  CG    . LYS A 1 510 ? 131.690 167.643 100.625 1.00 29.83 ?  510 LYS A CG    1 
ATOM   4089  C  CD    . LYS A 1 510 ? 131.439 166.454 101.534 1.00 30.57 ?  510 LYS A CD    1 
ATOM   4090  C  CE    . LYS A 1 510 ? 129.995 165.992 101.451 1.00 35.93 ?  510 LYS A CE    1 
ATOM   4091  N  NZ    . LYS A 1 510 ? 129.889 164.512 101.318 1.00 35.29 1  510 LYS A NZ    1 
ATOM   4092  N  N     . GLY A 1 511 ? 135.188 170.844 100.427 1.00 31.46 ?  511 GLY A N     1 
ATOM   4093  C  CA    . GLY A 1 511 ? 136.248 171.649 100.993 1.00 28.76 ?  511 GLY A CA    1 
ATOM   4094  C  C     . GLY A 1 511 ? 136.947 171.041 102.185 1.00 36.85 ?  511 GLY A C     1 
ATOM   4095  O  O     . GLY A 1 511 ? 137.702 171.743 102.865 1.00 40.96 ?  511 GLY A O     1 
ATOM   4096  N  N     . GLU A 1 512 ? 136.722 169.759 102.463 1.00 29.37 ?  512 GLU A N     1 
ATOM   4097  C  CA    . GLU A 1 512 ? 137.308 169.105 103.622 1.00 27.23 ?  512 GLU A CA    1 
ATOM   4098  C  C     . GLU A 1 512 ? 137.819 167.726 103.236 1.00 29.79 ?  512 GLU A C     1 
ATOM   4099  O  O     . GLU A 1 512 ? 137.230 167.039 102.398 1.00 29.31 ?  512 GLU A O     1 
ATOM   4100  C  CB    . GLU A 1 512 ? 136.296 168.983 104.769 1.00 29.38 ?  512 GLU A CB    1 
ATOM   4101  C  CG    . GLU A 1 512 ? 135.008 168.276 104.386 1.00 31.17 ?  512 GLU A CG    1 
ATOM   4102  C  CD    . GLU A 1 512 ? 134.295 167.673 105.579 1.00 33.54 ?  512 GLU A CD    1 
ATOM   4103  O  OE1   . GLU A 1 512 ? 134.981 167.303 106.554 1.00 31.95 ?  512 GLU A OE1   1 
ATOM   4104  O  OE2   . GLU A 1 512 ? 133.052 167.570 105.542 1.00 30.20 -1 512 GLU A OE2   1 
ATOM   4105  N  N     . THR A 1 513 ? 138.925 167.333 103.856 1.00 31.54 ?  513 THR A N     1 
ATOM   4106  C  CA    . THR A 1 513 ? 139.495 166.003 103.734 1.00 24.41 ?  513 THR A CA    1 
ATOM   4107  C  C     . THR A 1 513 ? 139.232 165.234 105.026 1.00 26.94 ?  513 THR A C     1 
ATOM   4108  O  O     . THR A 1 513 ? 138.558 165.726 105.938 1.00 31.85 ?  513 THR A O     1 
ATOM   4109  C  CB    . THR A 1 513 ? 140.988 166.097 103.420 1.00 26.12 ?  513 THR A CB    1 
ATOM   4110  O  OG1   . THR A 1 513 ? 141.698 166.520 104.589 1.00 35.94 ?  513 THR A OG1   1 
ATOM   4111  C  CG2   . THR A 1 513 ? 141.231 167.096 102.302 1.00 25.68 ?  513 THR A CG2   1 
ATOM   4112  N  N     . PHE A 1 514 ? 139.763 164.019 105.110 1.00 23.23 ?  514 PHE A N     1 
ATOM   4113  C  CA    . PHE A 1 514 ? 139.667 163.278 106.356 1.00 23.53 ?  514 PHE A CA    1 
ATOM   4114  C  C     . PHE A 1 514 ? 140.707 163.790 107.344 1.00 19.94 ?  514 PHE A C     1 
ATOM   4115  O  O     . PHE A 1 514 ? 141.727 164.368 106.960 1.00 28.21 ?  514 PHE A O     1 
ATOM   4116  C  CB    . PHE A 1 514 ? 139.828 161.774 106.125 1.00 16.82 ?  514 PHE A CB    1 
ATOM   4117  C  CG    . PHE A 1 514 ? 141.183 161.362 105.618 1.00 18.74 ?  514 PHE A CG    1 
ATOM   4118  C  CD1   . PHE A 1 514 ? 141.453 161.340 104.262 1.00 18.81 ?  514 PHE A CD1   1 
ATOM   4119  C  CD2   . PHE A 1 514 ? 142.174 160.960 106.497 1.00 19.05 ?  514 PHE A CD2   1 
ATOM   4120  C  CE1   . PHE A 1 514 ? 142.690 160.946 103.794 1.00 12.80 ?  514 PHE A CE1   1 
ATOM   4121  C  CE2   . PHE A 1 514 ? 143.412 160.568 106.035 1.00 16.19 ?  514 PHE A CE2   1 
ATOM   4122  C  CZ    . PHE A 1 514 ? 143.670 160.561 104.681 1.00 15.17 ?  514 PHE A CZ    1 
ATOM   4123  N  N     . ASP A 1 515 ? 140.425 163.594 108.630 1.00 22.86 ?  515 ASP A N     1 
ATOM   4124  C  CA    . ASP A 1 515 ? 141.301 164.117 109.669 1.00 26.17 ?  515 ASP A CA    1 
ATOM   4125  C  C     . ASP A 1 515 ? 142.694 163.513 109.553 1.00 27.64 ?  515 ASP A C     1 
ATOM   4126  O  O     . ASP A 1 515 ? 142.853 162.313 109.311 1.00 32.62 ?  515 ASP A O     1 
ATOM   4127  C  CB    . ASP A 1 515 ? 140.714 163.834 111.051 1.00 27.91 ?  515 ASP A CB    1 
ATOM   4128  C  CG    . ASP A 1 515 ? 139.564 164.759 111.394 1.00 30.13 ?  515 ASP A CG    1 
ATOM   4129  O  OD1   . ASP A 1 515 ? 138.969 165.341 110.462 1.00 30.97 ?  515 ASP A OD1   1 
ATOM   4130  O  OD2   . ASP A 1 515 ? 139.255 164.909 112.595 1.00 31.63 -1 515 ASP A OD2   1 
ATOM   4131  N  N     . GLN A 1 516 ? 143.706 164.365 109.722 1.00 29.29 ?  516 GLN A N     1 
ATOM   4132  C  CA    . GLN A 1 516 ? 145.112 163.982 109.595 1.00 27.02 ?  516 GLN A CA    1 
ATOM   4133  C  C     . GLN A 1 516 ? 145.432 163.453 108.201 1.00 24.74 ?  516 GLN A C     1 
ATOM   4134  O  O     . GLN A 1 516 ? 146.245 162.541 108.045 1.00 31.63 ?  516 GLN A O     1 
ATOM   4135  C  CB    . GLN A 1 516 ? 145.511 162.956 110.659 1.00 23.58 ?  516 GLN A CB    1 
ATOM   4136  C  CG    . GLN A 1 516 ? 145.298 163.418 112.089 1.00 27.32 ?  516 GLN A CG    1 
ATOM   4137  C  CD    . GLN A 1 516 ? 145.535 162.310 113.096 1.00 28.96 ?  516 GLN A CD    1 
ATOM   4138  O  OE1   . GLN A 1 516 ? 146.676 161.934 113.365 1.00 24.45 ?  516 GLN A OE1   1 
ATOM   4139  N  NE2   . GLN A 1 516 ? 144.455 161.779 113.657 1.00 30.70 ?  516 GLN A NE2   1 
ATOM   4140  N  N     . TYR A 1 517 ? 144.794 164.015 107.172 1.00 21.14 ?  517 TYR A N     1 
ATOM   4141  C  CA    . TYR A 1 517 ? 145.131 163.631 105.805 1.00 19.39 ?  517 TYR A CA    1 
ATOM   4142  C  C     . TYR A 1 517 ? 146.506 164.144 105.401 1.00 29.46 ?  517 TYR A C     1 
ATOM   4143  O  O     . TYR A 1 517 ? 147.202 163.494 104.614 1.00 36.04 ?  517 TYR A O     1 
ATOM   4144  C  CB    . TYR A 1 517 ? 144.072 164.141 104.828 1.00 18.68 ?  517 TYR A CB    1 
ATOM   4145  C  CG    . TYR A 1 517 ? 144.612 164.413 103.440 1.00 27.03 ?  517 TYR A CG    1 
ATOM   4146  C  CD1   . TYR A 1 517 ? 144.791 163.380 102.530 1.00 23.94 ?  517 TYR A CD1   1 
ATOM   4147  C  CD2   . TYR A 1 517 ? 144.946 165.702 103.042 1.00 29.69 ?  517 TYR A CD2   1 
ATOM   4148  C  CE1   . TYR A 1 517 ? 145.289 163.621 101.265 1.00 27.36 ?  517 TYR A CE1   1 
ATOM   4149  C  CE2   . TYR A 1 517 ? 145.447 165.951 101.782 1.00 25.86 ?  517 TYR A CE2   1 
ATOM   4150  C  CZ    . TYR A 1 517 ? 145.616 164.908 100.898 1.00 29.69 ?  517 TYR A CZ    1 
ATOM   4151  O  OH    . TYR A 1 517 ? 146.109 165.154 99.639  1.00 34.33 ?  517 TYR A OH    1 
ATOM   4152  N  N     . GLU A 1 518 ? 146.910 165.304 105.926 1.00 31.48 ?  518 GLU A N     1 
ATOM   4153  C  CA    . GLU A 1 518 ? 148.156 165.931 105.499 1.00 33.30 ?  518 GLU A CA    1 
ATOM   4154  C  C     . GLU A 1 518 ? 149.360 165.038 105.762 1.00 37.36 ?  518 GLU A C     1 
ATOM   4155  O  O     . GLU A 1 518 ? 150.354 165.104 105.028 1.00 39.66 ?  518 GLU A O     1 
ATOM   4156  C  CB    . GLU A 1 518 ? 148.341 167.285 106.193 1.00 32.58 ?  518 GLU A CB    1 
ATOM   4157  C  CG    . GLU A 1 518 ? 147.173 168.272 106.067 1.00 34.94 ?  518 GLU A CG    1 
ATOM   4158  C  CD    . GLU A 1 518 ? 145.927 167.847 106.825 1.00 42.69 ?  518 GLU A CD    1 
ATOM   4159  O  OE1   . GLU A 1 518 ? 144.813 168.217 106.397 1.00 41.60 ?  518 GLU A OE1   1 
ATOM   4160  O  OE2   . GLU A 1 518 ? 146.062 167.141 107.847 1.00 40.31 -1 518 GLU A OE2   1 
ATOM   4161  N  N     . GLY A 1 519 ? 149.299 164.202 106.796 1.00 26.93 ?  519 GLY A N     1 
ATOM   4162  C  CA    . GLY A 1 519 ? 150.373 163.266 107.055 1.00 23.56 ?  519 GLY A CA    1 
ATOM   4163  C  C     . GLY A 1 519 ? 150.308 161.978 106.267 1.00 23.79 ?  519 GLY A C     1 
ATOM   4164  O  O     . GLY A 1 519 ? 151.248 161.180 106.333 1.00 28.85 ?  519 GLY A O     1 
ATOM   4165  N  N     . SER A 1 520 ? 149.228 161.758 105.521 1.00 22.77 ?  520 SER A N     1 
ATOM   4166  C  CA    . SER A 1 520 ? 149.059 160.514 104.790 1.00 24.37 ?  520 SER A CA    1 
ATOM   4167  C  C     . SER A 1 520 ? 149.935 160.488 103.542 1.00 22.49 ?  520 SER A C     1 
ATOM   4168  O  O     . SER A 1 520 ? 150.417 161.516 103.061 1.00 31.54 ?  520 SER A O     1 
ATOM   4169  C  CB    . SER A 1 520 ? 147.593 160.314 104.404 1.00 19.01 ?  520 SER A CB    1 
ATOM   4170  O  OG    . SER A 1 520 ? 147.153 161.333 103.525 1.00 21.50 ?  520 SER A OG    1 
ATOM   4171  N  N     . THR A 1 521 ? 150.141 159.278 103.018 1.00 20.34 ?  521 THR A N     1 
ATOM   4172  C  CA    . THR A 1 521 ? 150.915 159.117 101.794 1.00 21.16 ?  521 THR A CA    1 
ATOM   4173  C  C     . THR A 1 521 ? 150.188 159.672 100.576 1.00 23.54 ?  521 THR A C     1 
ATOM   4174  O  O     . THR A 1 521 ? 150.829 159.925 99.552  1.00 24.52 ?  521 THR A O     1 
ATOM   4175  C  CB    . THR A 1 521 ? 151.256 157.643 101.572 1.00 22.76 ?  521 THR A CB    1 
ATOM   4176  O  OG1   . THR A 1 521 ? 150.067 156.921 101.229 1.00 23.73 ?  521 THR A OG1   1 
ATOM   4177  C  CG2   . THR A 1 521 ? 151.859 157.043 102.831 1.00 19.65 ?  521 THR A CG2   1 
ATOM   4178  N  N     . TYR A 1 522 ? 148.866 159.850 100.659 1.00 26.55 ?  522 TYR A N     1 
ATOM   4179  C  CA    . TYR A 1 522 ? 148.149 160.552 99.600  1.00 18.97 ?  522 TYR A CA    1 
ATOM   4180  C  C     . TYR A 1 522 ? 148.623 161.995 99.494  1.00 23.87 ?  522 TYR A C     1 
ATOM   4181  O  O     . TYR A 1 522 ? 148.864 162.507 98.395  1.00 25.62 ?  522 TYR A O     1 
ATOM   4182  C  CB    . TYR A 1 522 ? 146.643 160.508 99.860  1.00 17.28 ?  522 TYR A CB    1 
ATOM   4183  C  CG    . TYR A 1 522 ? 146.042 159.122 99.898  1.00 17.83 ?  522 TYR A CG    1 
ATOM   4184  C  CD1   . TYR A 1 522 ? 145.994 158.332 98.758  1.00 19.28 ?  522 TYR A CD1   1 
ATOM   4185  C  CD2   . TYR A 1 522 ? 145.503 158.613 101.071 1.00 21.38 ?  522 TYR A CD2   1 
ATOM   4186  C  CE1   . TYR A 1 522 ? 145.439 157.070 98.790  1.00 18.02 ?  522 TYR A CE1   1 
ATOM   4187  C  CE2   . TYR A 1 522 ? 144.943 157.353 101.111 1.00 18.03 ?  522 TYR A CE2   1 
ATOM   4188  C  CZ    . TYR A 1 522 ? 144.916 156.584 99.969  1.00 19.92 ?  522 TYR A CZ    1 
ATOM   4189  O  OH    . TYR A 1 522 ? 144.362 155.328 100.006 1.00 25.93 ?  522 TYR A OH    1 
ATOM   4190  N  N     . ALA A 1 523 ? 148.765 162.668 100.639 1.00 25.50 ?  523 ALA A N     1 
ATOM   4191  C  CA    . ALA A 1 523 ? 149.189 164.064 100.638 1.00 26.43 ?  523 ALA A CA    1 
ATOM   4192  C  C     . ALA A 1 523 ? 150.627 164.207 100.158 1.00 31.21 ?  523 ALA A C     1 
ATOM   4193  O  O     . ALA A 1 523 ? 150.947 165.135 99.406  1.00 32.89 ?  523 ALA A O     1 
ATOM   4194  C  CB    . ALA A 1 523 ? 149.025 164.661 102.034 1.00 25.19 ?  523 ALA A CB    1 
ATOM   4195  N  N     . THR A 1 524 ? 151.508 163.302 100.582 1.00 24.86 ?  524 THR A N     1 
ATOM   4196  C  CA    . THR A 1 524 ? 152.905 163.353 100.179 1.00 24.67 ?  524 THR A CA    1 
ATOM   4197  C  C     . THR A 1 524 ? 153.141 162.794 98.783  1.00 30.74 ?  524 THR A C     1 
ATOM   4198  O  O     . THR A 1 524 ? 154.248 162.947 98.254  1.00 36.80 ?  524 THR A O     1 
ATOM   4199  C  CB    . THR A 1 524 ? 153.773 162.590 101.184 1.00 28.88 ?  524 THR A CB    1 
ATOM   4200  O  OG1   . THR A 1 524 ? 153.599 161.181 100.999 1.00 30.78 ?  524 THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1 524 ? 153.387 162.959 102.607 1.00 26.81 ?  524 THR A CG2   1 
ATOM   4202  N  N     . GLY A 1 525 ? 152.142 162.156 98.178  1.00 26.63 ?  525 GLY A N     1 
ATOM   4203  C  CA    . GLY A 1 525 ? 152.283 161.589 96.855  1.00 24.39 ?  525 GLY A CA    1 
ATOM   4204  C  C     . GLY A 1 525 ? 152.981 160.250 96.800  1.00 29.59 ?  525 GLY A C     1 
ATOM   4205  O  O     . GLY A 1 525 ? 153.161 159.711 95.701  1.00 32.79 ?  525 GLY A O     1 
ATOM   4206  N  N     . GLU A 1 526 ? 153.384 159.696 97.946  1.00 29.06 ?  526 GLU A N     1 
ATOM   4207  C  CA    . GLU A 1 526 ? 154.054 158.400 97.952  1.00 29.80 ?  526 GLU A CA    1 
ATOM   4208  C  C     . GLU A 1 526 ? 153.119 157.294 97.479  1.00 31.92 ?  526 GLU A C     1 
ATOM   4209  O  O     . GLU A 1 526 ? 153.545 156.370 96.774  1.00 37.13 ?  526 GLU A O     1 
ATOM   4210  C  CB    . GLU A 1 526 ? 154.587 158.099 99.353  1.00 30.68 ?  526 GLU A CB    1 
ATOM   4211  C  CG    . GLU A 1 526 ? 154.973 156.648 99.583  1.00 31.72 ?  526 GLU A CG    1 
ATOM   4212  C  CD    . GLU A 1 526 ? 155.079 156.302 101.056 1.00 36.24 ?  526 GLU A CD    1 
ATOM   4213  O  OE1   . GLU A 1 526 ? 155.161 157.235 101.881 1.00 35.08 ?  526 GLU A OE1   1 
ATOM   4214  O  OE2   . GLU A 1 526 ? 155.079 155.098 101.387 1.00 34.53 -1 526 GLU A OE2   1 
ATOM   4215  N  N     . TYR A 1 527 ? 151.838 157.380 97.850  1.00 31.75 ?  527 TYR A N     1 
ATOM   4216  C  CA    . TYR A 1 527 ? 150.869 156.353 97.478  1.00 22.45 ?  527 TYR A CA    1 
ATOM   4217  C  C     . TYR A 1 527 ? 150.833 156.134 95.971  1.00 24.31 ?  527 TYR A C     1 
ATOM   4218  O  O     . TYR A 1 527 ? 150.657 155.004 95.503  1.00 30.71 ?  527 TYR A O     1 
ATOM   4219  C  CB    . TYR A 1 527 ? 149.481 156.741 97.993  1.00 18.46 ?  527 TYR A CB    1 
ATOM   4220  C  CG    . TYR A 1 527 ? 148.412 155.704 97.732  1.00 25.45 ?  527 TYR A CG    1 
ATOM   4221  C  CD1   . TYR A 1 527 ? 147.696 155.696 96.541  1.00 23.33 ?  527 TYR A CD1   1 
ATOM   4222  C  CD2   . TYR A 1 527 ? 148.116 154.735 98.679  1.00 24.14 ?  527 TYR A CD2   1 
ATOM   4223  C  CE1   . TYR A 1 527 ? 146.724 154.750 96.302  1.00 20.19 ?  527 TYR A CE1   1 
ATOM   4224  C  CE2   . TYR A 1 527 ? 147.143 153.787 98.448  1.00 22.64 ?  527 TYR A CE2   1 
ATOM   4225  C  CZ    . TYR A 1 527 ? 146.450 153.800 97.259  1.00 23.29 ?  527 TYR A CZ    1 
ATOM   4226  O  OH    . TYR A 1 527 ? 145.478 152.854 97.026  1.00 29.93 ?  527 TYR A OH    1 
ATOM   4227  N  N     . PHE A 1 528 ? 151.002 157.202 95.198  1.00 26.54 ?  528 PHE A N     1 
ATOM   4228  C  CA    . PHE A 1 528 ? 150.916 157.139 93.747  1.00 27.56 ?  528 PHE A CA    1 
ATOM   4229  C  C     . PHE A 1 528 ? 152.223 156.725 93.086  1.00 31.65 ?  528 PHE A C     1 
ATOM   4230  O  O     . PHE A 1 528 ? 152.269 156.640 91.855  1.00 37.05 ?  528 PHE A O     1 
ATOM   4231  C  CB    . PHE A 1 528 ? 150.469 158.494 93.191  1.00 28.67 ?  528 PHE A CB    1 
ATOM   4232  C  CG    . PHE A 1 528 ? 149.177 158.989 93.772  1.00 31.81 ?  528 PHE A CG    1 
ATOM   4233  C  CD1   . PHE A 1 528 ? 147.968 158.653 93.186  1.00 27.01 ?  528 PHE A CD1   1 
ATOM   4234  C  CD2   . PHE A 1 528 ? 149.168 159.786 94.904  1.00 29.35 ?  528 PHE A CD2   1 
ATOM   4235  C  CE1   . PHE A 1 528 ? 146.777 159.103 93.717  1.00 27.38 ?  528 PHE A CE1   1 
ATOM   4236  C  CE2   . PHE A 1 528 ? 147.980 160.239 95.439  1.00 29.22 ?  528 PHE A CE2   1 
ATOM   4237  C  CZ    . PHE A 1 528 ? 146.783 159.896 94.844  1.00 28.09 ?  528 PHE A CZ    1 
ATOM   4238  N  N     . ASP A 1 529 ? 153.275 156.464 93.868  1.00 30.61 ?  529 ASP A N     1 
ATOM   4239  C  CA    . ASP A 1 529 ? 154.580 156.138 93.297  1.00 29.55 ?  529 ASP A CA    1 
ATOM   4240  C  C     . ASP A 1 529 ? 154.481 154.983 92.307  1.00 33.50 ?  529 ASP A C     1 
ATOM   4241  O  O     . ASP A 1 529 ? 154.753 155.144 91.110  1.00 35.83 ?  529 ASP A O     1 
ATOM   4242  C  CB    . ASP A 1 529 ? 155.566 155.806 94.419  1.00 32.37 ?  529 ASP A CB    1 
ATOM   4243  C  CG    . ASP A 1 529 ? 156.135 157.045 95.079  1.00 39.19 ?  529 ASP A CG    1 
ATOM   4244  O  OD1   . ASP A 1 529 ? 155.841 158.163 94.604  1.00 36.61 ?  529 ASP A OD1   1 
ATOM   4245  O  OD2   . ASP A 1 529 ? 156.876 156.902 96.075  1.00 39.06 -1 529 ASP A OD2   1 
ATOM   4246  N  N     . LYS A 1 530 ? 154.045 153.815 92.785  1.00 34.90 ?  530 LYS A N     1 
ATOM   4247  C  CA    . LYS A 1 530 ? 153.915 152.655 91.911  1.00 32.53 ?  530 LYS A CA    1 
ATOM   4248  C  C     . LYS A 1 530 ? 152.933 152.899 90.776  1.00 32.70 ?  530 LYS A C     1 
ATOM   4249  O  O     . LYS A 1 530 ? 152.976 152.188 89.768  1.00 34.96 ?  530 LYS A O     1 
ATOM   4250  C  CB    . LYS A 1 530 ? 153.478 151.433 92.718  1.00 31.49 ?  530 LYS A CB    1 
ATOM   4251  C  CG    . LYS A 1 530 ? 151.985 151.168 92.669  1.00 29.76 ?  530 LYS A CG    1 
ATOM   4252  C  CD    . LYS A 1 530 ? 151.567 150.132 93.686  1.00 31.93 ?  530 LYS A CD    1 
ATOM   4253  C  CE    . LYS A 1 530 ? 150.111 149.763 93.506  1.00 27.82 ?  530 LYS A CE    1 
ATOM   4254  N  NZ    . LYS A 1 530 ? 149.367 149.842 94.790  1.00 33.29 1  530 LYS A NZ    1 
ATOM   4255  N  N     . TYR A 1 531 ? 152.053 153.887 90.915  1.00 30.64 ?  531 TYR A N     1 
ATOM   4256  C  CA    . TYR A 1 531 ? 151.101 154.208 89.864  1.00 28.11 ?  531 TYR A CA    1 
ATOM   4257  C  C     . TYR A 1 531 ? 151.653 155.189 88.842  1.00 26.93 ?  531 TYR A C     1 
ATOM   4258  O  O     . TYR A 1 531 ? 151.164 155.215 87.708  1.00 32.56 ?  531 TYR A O     1 
ATOM   4259  C  CB    . TYR A 1 531 ? 149.818 154.769 90.477  1.00 27.82 ?  531 TYR A CB    1 
ATOM   4260  C  CG    . TYR A 1 531 ? 148.959 153.719 91.138  1.00 28.79 ?  531 TYR A CG    1 
ATOM   4261  C  CD1   . TYR A 1 531 ? 148.538 152.599 90.437  1.00 23.74 ?  531 TYR A CD1   1 
ATOM   4262  C  CD2   . TYR A 1 531 ? 148.568 153.847 92.464  1.00 25.66 ?  531 TYR A CD2   1 
ATOM   4263  C  CE1   . TYR A 1 531 ? 147.752 151.636 91.034  1.00 29.88 ?  531 TYR A CE1   1 
ATOM   4264  C  CE2   . TYR A 1 531 ? 147.781 152.889 93.070  1.00 25.40 ?  531 TYR A CE2   1 
ATOM   4265  C  CZ    . TYR A 1 531 ? 147.377 151.786 92.350  1.00 28.75 ?  531 TYR A CZ    1 
ATOM   4266  O  OH    . TYR A 1 531 ? 146.593 150.829 92.950  1.00 26.64 ?  531 TYR A OH    1 
ATOM   4267  N  N     . VAL A 1 532 ? 152.657 155.993 89.210  1.00 36.73 ?  532 VAL A N     1 
ATOM   4268  C  CA    . VAL A 1 532 ? 153.250 156.927 88.259  1.00 35.08 ?  532 VAL A CA    1 
ATOM   4269  C  C     . VAL A 1 532 ? 154.477 156.347 87.573  1.00 36.69 ?  532 VAL A C     1 
ATOM   4270  O  O     . VAL A 1 532 ? 155.080 157.020 86.727  1.00 41.15 ?  532 VAL A O     1 
ATOM   4271  C  CB    . VAL A 1 532 ? 153.612 158.265 88.937  1.00 35.29 ?  532 VAL A CB    1 
ATOM   4272  C  CG1   . VAL A 1 532 ? 152.378 158.894 89.563  1.00 34.97 ?  532 VAL A CG1   1 
ATOM   4273  C  CG2   . VAL A 1 532 ? 154.702 158.067 89.972  1.00 33.74 ?  532 VAL A CG2   1 
ATOM   4274  N  N     . SER A 1 533 ? 154.863 155.118 87.906  1.00 37.31 ?  533 SER A N     1 
ATOM   4275  C  CA    . SER A 1 533 ? 156.011 154.463 87.298  1.00 39.93 ?  533 SER A CA    1 
ATOM   4276  C  C     . SER A 1 533 ? 155.676 153.147 86.614  1.00 40.94 ?  533 SER A C     1 
ATOM   4277  O  O     . SER A 1 533 ? 156.326 152.804 85.624  1.00 43.31 ?  533 SER A O     1 
ATOM   4278  C  CB    . SER A 1 533 ? 157.099 154.209 88.352  1.00 41.14 ?  533 SER A CB    1 
ATOM   4279  O  OG    . SER A 1 533 ? 156.717 153.171 89.237  1.00 44.41 ?  533 SER A OG    1 
ATOM   4280  N  N     . THR A 1 534 ? 154.687 152.408 87.107  1.00 40.28 ?  534 THR A N     1 
ATOM   4281  C  CA    . THR A 1 534 ? 154.305 151.121 86.544  1.00 38.86 ?  534 THR A CA    1 
ATOM   4282  C  C     . THR A 1 534 ? 152.988 151.264 85.796  1.00 38.19 ?  534 THR A C     1 
ATOM   4283  O  O     . THR A 1 534 ? 152.013 151.790 86.343  1.00 43.56 ?  534 THR A O     1 
ATOM   4284  C  CB    . THR A 1 534 ? 154.175 150.059 87.640  1.00 39.36 ?  534 THR A CB    1 
ATOM   4285  O  OG1   . THR A 1 534 ? 155.458 149.816 88.229  1.00 42.76 ?  534 THR A OG1   1 
ATOM   4286  C  CG2   . THR A 1 534 ? 153.632 148.759 87.064  1.00 38.66 ?  534 THR A CG2   1 
ATOM   4287  N  N     . ASP A 1 535 ? 152.965 150.800 84.551  1.00 40.64 ?  535 ASP A N     1 
ATOM   4288  C  CA    . ASP A 1 535 ? 151.753 150.799 83.747  1.00 39.74 ?  535 ASP A CA    1 
ATOM   4289  C  C     . ASP A 1 535 ? 150.970 149.521 84.020  1.00 41.84 ?  535 ASP A C     1 
ATOM   4290  O  O     . ASP A 1 535 ? 151.516 148.418 83.919  1.00 42.89 ?  535 ASP A O     1 
ATOM   4291  C  CB    . ASP A 1 535 ? 152.090 150.914 82.261  1.00 38.68 ?  535 ASP A CB    1 
ATOM   4292  C  CG    . ASP A 1 535 ? 150.909 151.363 81.428  1.00 44.50 ?  535 ASP A CG    1 
ATOM   4293  O  OD1   . ASP A 1 535 ? 150.480 152.526 81.578  1.00 45.74 ?  535 ASP A OD1   1 
ATOM   4294  O  OD2   . ASP A 1 535 ? 150.410 150.553 80.620  1.00 45.92 -1 535 ASP A OD2   1 
ATOM   4295  N  N     . PHE A 1 536 ? 149.692 149.674 84.367  1.00 34.20 ?  536 PHE A N     1 
ATOM   4296  C  CA    . PHE A 1 536 ? 148.844 148.546 84.729  1.00 26.98 ?  536 PHE A CA    1 
ATOM   4297  C  C     . PHE A 1 536 ? 147.854 148.190 83.627  1.00 31.33 ?  536 PHE A C     1 
ATOM   4298  O  O     . PHE A 1 536 ? 146.824 147.563 83.899  1.00 37.66 ?  536 PHE A O     1 
ATOM   4299  C  CB    . PHE A 1 536 ? 148.112 148.839 86.039  1.00 29.06 ?  536 PHE A CB    1 
ATOM   4300  C  CG    . PHE A 1 536 ? 149.017 148.892 87.237  1.00 27.91 ?  536 PHE A CG    1 
ATOM   4301  C  CD1   . PHE A 1 536 ? 149.354 147.737 87.919  1.00 27.98 ?  536 PHE A CD1   1 
ATOM   4302  C  CD2   . PHE A 1 536 ? 149.537 150.096 87.676  1.00 27.54 ?  536 PHE A CD2   1 
ATOM   4303  C  CE1   . PHE A 1 536 ? 150.189 147.782 89.019  1.00 28.05 ?  536 PHE A CE1   1 
ATOM   4304  C  CE2   . PHE A 1 536 ? 150.372 150.147 88.776  1.00 32.24 ?  536 PHE A CE2   1 
ATOM   4305  C  CZ    . PHE A 1 536 ? 150.697 148.989 89.448  1.00 28.77 ?  536 PHE A CZ    1 
ATOM   4306  N  N     . SER A 1 537 ? 148.143 148.584 82.390  1.00 37.02 ?  537 SER A N     1 
ATOM   4307  C  CA    . SER A 1 537 ? 147.338 148.160 81.259  1.00 33.64 ?  537 SER A CA    1 
ATOM   4308  C  C     . SER A 1 537 ? 147.484 146.653 81.056  1.00 38.82 ?  537 SER A C     1 
ATOM   4309  O  O     . SER A 1 537 ? 148.517 146.072 81.400  1.00 39.19 ?  537 SER A O     1 
ATOM   4310  C  CB    . SER A 1 537 ? 147.763 148.910 79.999  1.00 37.25 ?  537 SER A CB    1 
ATOM   4311  O  OG    . SER A 1 537 ? 147.360 148.236 78.821  1.00 44.12 ?  537 SER A OG    1 
ATOM   4312  N  N     . PRO A 1 538 ? 146.455 145.993 80.523  1.00 37.27 ?  538 PRO A N     1 
ATOM   4313  C  CA    . PRO A 1 538 ? 146.530 144.538 80.347  1.00 34.32 ?  538 PRO A CA    1 
ATOM   4314  C  C     . PRO A 1 538 ? 147.690 144.132 79.449  1.00 39.19 ?  538 PRO A C     1 
ATOM   4315  O  O     . PRO A 1 538 ? 147.965 144.767 78.429  1.00 39.38 ?  538 PRO A O     1 
ATOM   4316  C  CB    . PRO A 1 538 ? 145.181 144.190 79.710  1.00 37.31 ?  538 PRO A CB    1 
ATOM   4317  C  CG    . PRO A 1 538 ? 144.277 145.299 80.111  1.00 34.46 ?  538 PRO A CG    1 
ATOM   4318  C  CD    . PRO A 1 538 ? 145.137 146.523 80.136  1.00 33.65 ?  538 PRO A CD    1 
ATOM   4319  N  N     . LYS A 1 539 ? 148.370 143.058 79.845  1.00 44.39 ?  539 LYS A N     1 
ATOM   4320  C  CA    . LYS A 1 539 ? 149.469 142.503 79.068  1.00 44.62 ?  539 LYS A CA    1 
ATOM   4321  C  C     . LYS A 1 539 ? 149.015 141.433 78.087  1.00 44.99 ?  539 LYS A C     1 
ATOM   4322  O  O     . LYS A 1 539 ? 149.824 140.978 77.271  1.00 47.43 ?  539 LYS A O     1 
ATOM   4323  C  CB    . LYS A 1 539 ? 150.533 141.918 80.002  1.00 43.77 ?  539 LYS A CB    1 
ATOM   4324  C  CG    . LYS A 1 539 ? 150.945 142.847 81.130  1.00 42.84 ?  539 LYS A CG    1 
ATOM   4325  C  CD    . LYS A 1 539 ? 152.048 143.795 80.691  1.00 45.68 ?  539 LYS A CD    1 
ATOM   4326  C  CE    . LYS A 1 539 ? 152.269 144.895 81.717  1.00 45.50 ?  539 LYS A CE    1 
ATOM   4327  N  NZ    . LYS A 1 539 ? 151.538 146.142 81.359  1.00 44.13 1  539 LYS A NZ    1 
ATOM   4328  N  N     . TYR A 1 540 ? 147.751 141.026 78.144  1.00 42.49 ?  540 TYR A N     1 
ATOM   4329  C  CA    . TYR A 1 540 ? 147.200 140.014 77.257  1.00 41.58 ?  540 TYR A CA    1 
ATOM   4330  C  C     . TYR A 1 540 ? 146.145 140.644 76.359  1.00 42.99 ?  540 TYR A C     1 
ATOM   4331  O  O     . TYR A 1 540 ? 145.384 141.515 76.794  1.00 44.81 ?  540 TYR A O     1 
ATOM   4332  C  CB    . TYR A 1 540 ? 146.594 138.855 78.054  1.00 42.66 ?  540 TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1 540 ? 147.614 138.054 78.826  1.00 44.40 ?  540 TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1 540 ? 147.976 138.413 80.117  1.00 42.75 ?  540 TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1 540 ? 148.222 136.941 78.261  1.00 45.61 ?  540 TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1 540 ? 148.911 137.685 80.826  1.00 45.50 ?  540 TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1 540 ? 149.158 136.207 78.963  1.00 40.60 ?  540 TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1 540 ? 149.499 136.583 80.244  1.00 45.33 ?  540 TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1 540 ? 150.430 135.852 80.942  1.00 46.48 ?  540 TYR A OH    1 
ATOM   4340  N  N     . GLU A 1 541 ? 146.110 140.202 75.099  1.00 47.04 ?  541 GLU A N     1 
ATOM   4341  C  CA    . GLU A 1 541 ? 145.171 140.771 74.138  1.00 47.04 ?  541 GLU A CA    1 
ATOM   4342  C  C     . GLU A 1 541 ? 143.728 140.483 74.533  1.00 47.07 ?  541 GLU A C     1 
ATOM   4343  O  O     . GLU A 1 541 ? 142.840 141.314 74.313  1.00 44.24 ?  541 GLU A O     1 
ATOM   4344  C  CB    . GLU A 1 541 ? 145.460 140.230 72.738  1.00 45.13 ?  541 GLU A CB    1 
ATOM   4345  C  CG    . GLU A 1 541 ? 144.991 141.134 71.612  1.00 46.40 ?  541 GLU A CG    1 
ATOM   4346  C  CD    . GLU A 1 541 ? 144.920 140.414 70.281  1.00 52.19 ?  541 GLU A CD    1 
ATOM   4347  O  OE1   . GLU A 1 541 ? 144.926 139.165 70.279  1.00 52.67 ?  541 GLU A OE1   1 
ATOM   4348  O  OE2   . GLU A 1 541 ? 144.860 141.096 69.235  1.00 50.07 -1 541 GLU A OE2   1 
ATOM   4349  N  N     . LYS A 1 542 ? 143.473 139.305 75.107  1.00 42.45 ?  542 LYS A N     1 
ATOM   4350  C  CA    . LYS A 1 542 ? 142.115 138.955 75.510  1.00 41.73 ?  542 LYS A CA    1 
ATOM   4351  C  C     . LYS A 1 542 ? 141.594 139.904 76.583  1.00 43.05 ?  542 LYS A C     1 
ATOM   4352  O  O     . LYS A 1 542 ? 140.448 140.364 76.515  1.00 41.93 ?  542 LYS A O     1 
ATOM   4353  C  CB    . LYS A 1 542 ? 142.076 137.510 76.004  1.00 40.93 ?  542 LYS A CB    1 
ATOM   4354  C  CG    . LYS A 1 542 ? 140.687 136.993 76.325  1.00 43.00 ?  542 LYS A CG    1 
ATOM   4355  C  CD    . LYS A 1 542 ? 140.740 135.550 76.796  1.00 39.38 ?  542 LYS A CD    1 
ATOM   4356  C  CE    . LYS A 1 542 ? 139.347 134.971 76.962  1.00 41.15 ?  542 LYS A CE    1 
ATOM   4357  N  NZ    . LYS A 1 542 ? 139.389 133.518 77.282  1.00 42.60 1  542 LYS A NZ    1 
ATOM   4358  N  N     . ILE A 1 543 ? 142.429 140.226 77.572  1.00 38.22 ?  543 ILE A N     1 
ATOM   4359  C  CA    . ILE A 1 543 ? 142.003 141.133 78.632  1.00 36.34 ?  543 ILE A CA    1 
ATOM   4360  C  C     . ILE A 1 543 ? 141.808 142.542 78.081  1.00 38.94 ?  543 ILE A C     1 
ATOM   4361  O  O     . ILE A 1 543 ? 140.875 143.255 78.474  1.00 41.41 ?  543 ILE A O     1 
ATOM   4362  C  CB    . ILE A 1 543 ? 143.012 141.108 79.794  1.00 35.88 ?  543 ILE A CB    1 
ATOM   4363  C  CG1   . ILE A 1 543 ? 143.133 139.702 80.390  1.00 39.31 ?  543 ILE A CG1   1 
ATOM   4364  C  CG2   . ILE A 1 543 ? 142.589 142.075 80.879  1.00 37.77 ?  543 ILE A CG2   1 
ATOM   4365  C  CD1   . ILE A 1 543 ? 141.839 138.914 80.420  1.00 37.09 ?  543 ILE A CD1   1 
ATOM   4366  N  N     . ALA A 1 544 ? 142.680 142.963 77.162  1.00 37.81 ?  544 ALA A N     1 
ATOM   4367  C  CA    . ALA A 1 544 ? 142.524 144.273 76.540  1.00 40.47 ?  544 ALA A CA    1 
ATOM   4368  C  C     . ALA A 1 544 ? 141.219 144.362 75.760  1.00 42.32 ?  544 ALA A C     1 
ATOM   4369  O  O     . ALA A 1 544 ? 140.535 145.391 75.793  1.00 42.94 ?  544 ALA A O     1 
ATOM   4370  C  CB    . ALA A 1 544 ? 143.717 144.567 75.630  1.00 40.60 ?  544 ALA A CB    1 
ATOM   4371  N  N     . ASN A 1 545 ? 140.858 143.292 75.047  1.00 43.74 ?  545 ASN A N     1 
ATOM   4372  C  CA    . ASN A 1 545 ? 139.570 143.261 74.362  1.00 44.64 ?  545 ASN A CA    1 
ATOM   4373  C  C     . ASN A 1 545 ? 138.415 143.245 75.353  1.00 44.81 ?  545 ASN A C     1 
ATOM   4374  O  O     . ASN A 1 545 ? 137.342 143.787 75.062  1.00 47.71 ?  545 ASN A O     1 
ATOM   4375  C  CB    . ASN A 1 545 ? 139.494 142.049 73.434  1.00 44.57 ?  545 ASN A CB    1 
ATOM   4376  C  CG    . ASN A 1 545 ? 140.573 142.060 72.373  1.00 47.93 ?  545 ASN A CG    1 
ATOM   4377  O  OD1   . ASN A 1 545 ? 141.102 143.114 72.021  1.00 47.94 ?  545 ASN A OD1   1 
ATOM   4378  N  ND2   . ASN A 1 545 ? 140.909 140.883 71.857  1.00 47.29 ?  545 ASN A ND2   1 
ATOM   4379  N  N     . LEU A 1 546 ? 138.609 142.621 76.516  1.00 40.52 ?  546 LEU A N     1 
ATOM   4380  C  CA    . LEU A 1 546 ? 137.600 142.697 77.569  1.00 38.34 ?  546 LEU A CA    1 
ATOM   4381  C  C     . LEU A 1 546 ? 137.394 144.135 78.025  1.00 38.77 ?  546 LEU A C     1 
ATOM   4382  O  O     . LEU A 1 546 ? 136.259 144.562 78.268  1.00 40.95 ?  546 LEU A O     1 
ATOM   4383  C  CB    . LEU A 1 546 ? 138.003 141.816 78.751  1.00 35.29 ?  546 LEU A CB    1 
ATOM   4384  C  CG    . LEU A 1 546 ? 137.837 140.309 78.577  1.00 38.57 ?  546 LEU A CG    1 
ATOM   4385  C  CD1   . LEU A 1 546 ? 138.163 139.600 79.876  1.00 36.37 ?  546 LEU A CD1   1 
ATOM   4386  C  CD2   . LEU A 1 546 ? 136.428 139.977 78.119  1.00 34.75 ?  546 LEU A CD2   1 
ATOM   4387  N  N     . PHE A 1 547 ? 138.478 144.898 78.144  1.00 37.80 ?  547 PHE A N     1 
ATOM   4388  C  CA    . PHE A 1 547 ? 138.409 146.292 78.561  1.00 36.82 ?  547 PHE A CA    1 
ATOM   4389  C  C     . PHE A 1 547 ? 138.116 147.244 77.409  1.00 37.34 ?  547 PHE A C     1 
ATOM   4390  O  O     . PHE A 1 547 ? 138.204 148.462 77.594  1.00 38.01 ?  547 PHE A O     1 
ATOM   4391  C  CB    . PHE A 1 547 ? 139.711 146.703 79.250  1.00 35.38 ?  547 PHE A CB    1 
ATOM   4392  C  CG    . PHE A 1 547 ? 139.815 146.240 80.670  1.00 35.44 ?  547 PHE A CG    1 
ATOM   4393  C  CD1   . PHE A 1 547 ? 139.214 146.955 81.690  1.00 34.89 ?  547 PHE A CD1   1 
ATOM   4394  C  CD2   . PHE A 1 547 ? 140.514 145.089 80.986  1.00 32.16 ?  547 PHE A CD2   1 
ATOM   4395  C  CE1   . PHE A 1 547 ? 139.309 146.530 83.000  1.00 31.83 ?  547 PHE A CE1   1 
ATOM   4396  C  CE2   . PHE A 1 547 ? 140.610 144.661 82.293  1.00 34.52 ?  547 PHE A CE2   1 
ATOM   4397  C  CZ    . PHE A 1 547 ? 140.006 145.381 83.300  1.00 33.71 ?  547 PHE A CZ    1 
ATOM   4398  N  N     . GLU A 1 548 ? 137.776 146.724 76.231  1.00 43.65 ?  548 GLU A N     1 
ATOM   4399  C  CA    . GLU A 1 548 ? 137.479 147.583 75.093  1.00 46.68 ?  548 GLU A CA    1 
ATOM   4400  C  C     . GLU A 1 548 ? 136.251 148.441 75.373  1.00 47.86 ?  548 GLU A C     1 
ATOM   4401  O  O     . GLU A 1 548 ? 135.284 147.990 75.993  1.00 47.21 ?  548 GLU A O     1 
ATOM   4402  C  CB    . GLU A 1 548 ? 137.259 146.743 73.835  1.00 45.30 ?  548 GLU A CB    1 
ATOM   4403  C  CG    . GLU A 1 548 ? 137.985 147.268 72.610  1.00 46.87 ?  548 GLU A CG    1 
ATOM   4404  C  CD    . GLU A 1 548 ? 139.491 147.234 72.769  1.00 49.11 ?  548 GLU A CD    1 
ATOM   4405  O  OE1   . GLU A 1 548 ? 140.091 146.163 72.541  1.00 48.26 ?  548 GLU A OE1   1 
ATOM   4406  O  OE2   . GLU A 1 548 ? 140.077 148.279 73.124  1.00 47.53 -1 548 GLU A OE2   1 
ATOM   4407  N  N     . GLY A 1 549 ? 136.295 149.687 74.906  1.00 44.32 ?  549 GLY A N     1 
ATOM   4408  C  CA    . GLY A 1 549 ? 135.238 150.641 75.157  1.00 40.96 ?  549 GLY A CA    1 
ATOM   4409  C  C     . GLY A 1 549 ? 135.367 151.410 76.452  1.00 43.69 ?  549 GLY A C     1 
ATOM   4410  O  O     . GLY A 1 549 ? 134.511 152.256 76.737  1.00 44.76 ?  549 GLY A O     1 
ATOM   4411  N  N     . MET A 1 550 ? 136.405 151.145 77.242  1.00 43.09 ?  550 MET A N     1 
ATOM   4412  C  CA    . MET A 1 550 ? 136.624 151.808 78.519  1.00 40.92 ?  550 MET A CA    1 
ATOM   4413  C  C     . MET A 1 550 ? 138.035 152.371 78.547  1.00 41.67 ?  550 MET A C     1 
ATOM   4414  O  O     . MET A 1 550 ? 138.986 151.685 78.157  1.00 42.25 ?  550 MET A O     1 
ATOM   4415  C  CB    . MET A 1 550 ? 136.427 150.837 79.685  1.00 38.56 ?  550 MET A CB    1 
ATOM   4416  C  CG    . MET A 1 550 ? 135.171 151.074 80.494  1.00 42.56 ?  550 MET A CG    1 
ATOM   4417  S  SD    . MET A 1 550 ? 135.033 149.891 81.839  1.00 55.69 ?  550 MET A SD    1 
ATOM   4418  C  CE    . MET A 1 550 ? 135.090 148.347 80.935  1.00 41.52 ?  550 MET A CE    1 
ATOM   4419  N  N     . HIS A 1 551 ? 138.173 153.610 79.009  1.00 38.98 ?  551 HIS A N     1 
ATOM   4420  C  CA    . HIS A 1 551 ? 139.490 154.224 79.106  1.00 38.16 ?  551 HIS A CA    1 
ATOM   4421  C  C     . HIS A 1 551 ? 140.243 153.639 80.295  1.00 38.90 ?  551 HIS A C     1 
ATOM   4422  O  O     . HIS A 1 551 ? 139.769 153.702 81.433  1.00 40.01 ?  551 HIS A O     1 
ATOM   4423  C  CB    . HIS A 1 551 ? 139.365 155.739 79.242  1.00 39.46 ?  551 HIS A CB    1 
ATOM   4424  C  CG    . HIS A 1 551 ? 140.661 156.424 79.542  1.00 41.61 ?  551 HIS A CG    1 
ATOM   4425  N  ND1   . HIS A 1 551 ? 141.747 156.367 78.694  1.00 42.78 ?  551 HIS A ND1   1 
ATOM   4426  C  CD2   . HIS A 1 551 ? 141.048 157.181 80.597  1.00 42.39 ?  551 HIS A CD2   1 
ATOM   4427  C  CE1   . HIS A 1 551 ? 142.745 157.059 79.213  1.00 40.85 ?  551 HIS A CE1   1 
ATOM   4428  N  NE2   . HIS A 1 551 ? 142.347 157.562 80.367  1.00 41.74 ?  551 HIS A NE2   1 
ATOM   4429  N  N     . ILE A 1 552 ? 141.412 153.070 80.028  1.00 35.62 ?  552 ILE A N     1 
ATOM   4430  C  CA    . ILE A 1 552 ? 142.256 152.485 81.065  1.00 31.64 ?  552 ILE A CA    1 
ATOM   4431  C  C     . ILE A 1 552 ? 143.245 153.554 81.523  1.00 33.24 ?  552 ILE A C     1 
ATOM   4432  O  O     . ILE A 1 552 ? 144.027 154.047 80.696  1.00 36.10 ?  552 ILE A O     1 
ATOM   4433  C  CB    . ILE A 1 552 ? 142.990 151.240 80.554  1.00 33.70 ?  552 ILE A CB    1 
ATOM   4434  C  CG1   . ILE A 1 552 ? 141.983 150.150 80.184  1.00 32.99 ?  552 ILE A CG1   1 
ATOM   4435  C  CG2   . ILE A 1 552 ? 143.974 150.735 81.592  1.00 34.38 ?  552 ILE A CG2   1 
ATOM   4436  C  CD1   . ILE A 1 552 ? 142.599 148.972 79.473  1.00 34.55 ?  552 ILE A CD1   1 
ATOM   4437  N  N     . PRO A 1 553 ? 143.235 153.944 82.797  1.00 38.28 ?  553 PRO A N     1 
ATOM   4438  C  CA    . PRO A 1 553 ? 144.146 155.002 83.253  1.00 32.24 ?  553 PRO A CA    1 
ATOM   4439  C  C     . PRO A 1 553 ? 145.603 154.606 83.060  1.00 35.19 ?  553 PRO A C     1 
ATOM   4440  O  O     . PRO A 1 553 ? 146.024 153.509 83.432  1.00 36.48 ?  553 PRO A O     1 
ATOM   4441  C  CB    . PRO A 1 553 ? 143.794 155.156 84.737  1.00 31.02 ?  553 PRO A CB    1 
ATOM   4442  C  CG    . PRO A 1 553 ? 142.401 154.621 84.853  1.00 30.52 ?  553 PRO A CG    1 
ATOM   4443  C  CD    . PRO A 1 553 ? 142.320 153.503 83.861  1.00 32.28 ?  553 PRO A CD    1 
ATOM   4444  N  N     . THR A 1 554 ? 146.371 155.515 82.472  1.00 39.01 ?  554 THR A N     1 
ATOM   4445  C  CA    . THR A 1 554 ? 147.783 155.309 82.208  1.00 38.97 ?  554 THR A CA    1 
ATOM   4446  C  C     . THR A 1 554 ? 148.613 155.959 83.312  1.00 37.81 ?  554 THR A C     1 
ATOM   4447  O  O     . THR A 1 554 ? 148.087 156.423 84.327  1.00 39.91 ?  554 THR A O     1 
ATOM   4448  C  CB    . THR A 1 554 ? 148.146 155.861 80.829  1.00 37.93 ?  554 THR A CB    1 
ATOM   4449  O  OG1   . THR A 1 554 ? 148.035 157.289 80.840  1.00 40.49 ?  554 THR A OG1   1 
ATOM   4450  C  CG2   . THR A 1 554 ? 147.215 155.296 79.768  1.00 35.01 ?  554 THR A CG2   1 
ATOM   4451  N  N     . THR A 1 555 ? 149.933 155.991 83.116  1.00 38.74 ?  555 THR A N     1 
ATOM   4452  C  CA    . THR A 1 555 ? 150.800 156.654 84.083  1.00 36.20 ?  555 THR A CA    1 
ATOM   4453  C  C     . THR A 1 555 ? 150.592 158.162 84.083  1.00 38.34 ?  555 THR A C     1 
ATOM   4454  O  O     . THR A 1 555 ? 150.696 158.799 85.135  1.00 40.28 ?  555 THR A O     1 
ATOM   4455  C  CB    . THR A 1 555 ? 152.264 156.320 83.799  1.00 38.61 ?  555 THR A CB    1 
ATOM   4456  O  OG1   . THR A 1 555 ? 152.531 156.477 82.399  1.00 41.79 ?  555 THR A OG1   1 
ATOM   4457  C  CG2   . THR A 1 555 ? 152.573 154.888 84.213  1.00 37.28 ?  555 THR A CG2   1 
ATOM   4458  N  N     . GLU A 1 556 ? 150.306 158.751 82.918  1.00 39.91 ?  556 GLU A N     1 
ATOM   4459  C  CA    . GLU A 1 556 ? 150.009 160.179 82.866  1.00 39.82 ?  556 GLU A CA    1 
ATOM   4460  C  C     . GLU A 1 556 ? 148.705 160.498 83.589  1.00 38.55 ?  556 GLU A C     1 
ATOM   4461  O  O     . GLU A 1 556 ? 148.610 161.506 84.301  1.00 40.13 ?  556 GLU A O     1 
ATOM   4462  C  CB    . GLU A 1 556 ? 149.947 160.649 81.413  1.00 40.74 ?  556 GLU A CB    1 
ATOM   4463  C  CG    . GLU A 1 556 ? 149.923 162.158 81.251  1.00 43.25 ?  556 GLU A CG    1 
ATOM   4464  C  CD    . GLU A 1 556 ? 151.120 162.832 81.894  1.00 44.78 ?  556 GLU A CD    1 
ATOM   4465  O  OE1   . GLU A 1 556 ? 152.242 162.294 81.778  1.00 41.96 ?  556 GLU A OE1   1 
ATOM   4466  O  OE2   . GLU A 1 556 ? 150.939 163.899 82.517  1.00 44.90 -1 556 GLU A OE2   1 
ATOM   4467  N  N     . ASP A 1 557 ? 147.688 159.651 83.415  1.00 40.02 ?  557 ASP A N     1 
ATOM   4468  C  CA    . ASP A 1 557 ? 146.438 159.836 84.142  1.00 36.22 ?  557 ASP A CA    1 
ATOM   4469  C  C     . ASP A 1 557 ? 146.658 159.717 85.643  1.00 36.15 ?  557 ASP A C     1 
ATOM   4470  O  O     . ASP A 1 557 ? 146.070 160.469 86.428  1.00 37.41 ?  557 ASP A O     1 
ATOM   4471  C  CB    . ASP A 1 557 ? 145.399 158.821 83.668  1.00 35.10 ?  557 ASP A CB    1 
ATOM   4472  C  CG    . ASP A 1 557 ? 144.770 159.208 82.345  1.00 40.32 ?  557 ASP A CG    1 
ATOM   4473  O  OD1   . ASP A 1 557 ? 144.612 160.420 82.093  1.00 43.55 ?  557 ASP A OD1   1 
ATOM   4474  O  OD2   . ASP A 1 557 ? 144.436 158.299 81.557  1.00 42.22 -1 557 ASP A OD2   1 
ATOM   4475  N  N     . TRP A 1 558 ? 147.508 158.777 86.062  1.00 29.19 ?  558 TRP A N     1 
ATOM   4476  C  CA    . TRP A 1 558 ? 147.815 158.643 87.481  1.00 27.33 ?  558 TRP A CA    1 
ATOM   4477  C  C     . TRP A 1 558 ? 148.598 159.839 88.005  1.00 29.30 ?  558 TRP A C     1 
ATOM   4478  O  O     . TRP A 1 558 ? 148.400 160.247 89.152  1.00 33.21 ?  558 TRP A O     1 
ATOM   4479  C  CB    . TRP A 1 558 ? 148.582 157.348 87.730  1.00 29.55 ?  558 TRP A CB    1 
ATOM   4480  C  CG    . TRP A 1 558 ? 147.695 156.174 87.993  1.00 27.37 ?  558 TRP A CG    1 
ATOM   4481  C  CD1   . TRP A 1 558 ? 147.433 155.138 87.148  1.00 27.28 ?  558 TRP A CD1   1 
ATOM   4482  C  CD2   . TRP A 1 558 ? 146.948 155.916 89.188  1.00 28.16 ?  558 TRP A CD2   1 
ATOM   4483  N  NE1   . TRP A 1 558 ? 146.573 154.248 87.742  1.00 30.85 ?  558 TRP A NE1   1 
ATOM   4484  C  CE2   . TRP A 1 558 ? 146.263 154.701 88.997  1.00 28.47 ?  558 TRP A CE2   1 
ATOM   4485  C  CE3   . TRP A 1 558 ? 146.799 156.590 90.404  1.00 30.88 ?  558 TRP A CE3   1 
ATOM   4486  C  CZ2   . TRP A 1 558 ? 145.439 154.149 89.973  1.00 26.24 ?  558 TRP A CZ2   1 
ATOM   4487  C  CZ3   . TRP A 1 558 ? 145.981 156.040 91.371  1.00 26.03 ?  558 TRP A CZ3   1 
ATOM   4488  C  CH2   . TRP A 1 558 ? 145.311 154.832 91.150  1.00 22.82 ?  558 TRP A CH2   1 
ATOM   4489  N  N     . LYS A 1 559 ? 149.486 160.413 87.190  1.00 36.33 ?  559 LYS A N     1 
ATOM   4490  C  CA    . LYS A 1 559 ? 150.181 161.632 87.597  1.00 32.59 ?  559 LYS A CA    1 
ATOM   4491  C  C     . LYS A 1 559 ? 149.204 162.790 87.760  1.00 31.12 ?  559 LYS A C     1 
ATOM   4492  O  O     . LYS A 1 559 ? 149.308 163.576 88.711  1.00 34.31 ?  559 LYS A O     1 
ATOM   4493  C  CB    . LYS A 1 559 ? 151.259 161.987 86.572  1.00 36.36 ?  559 LYS A CB    1 
ATOM   4494  C  CG    . LYS A 1 559 ? 152.571 161.249 86.760  1.00 38.00 ?  559 LYS A CG    1 
ATOM   4495  C  CD    . LYS A 1 559 ? 153.263 161.021 85.428  1.00 39.16 ?  559 LYS A CD    1 
ATOM   4496  C  CE    . LYS A 1 559 ? 154.438 160.071 85.568  1.00 37.84 ?  559 LYS A CE    1 
ATOM   4497  N  NZ    . LYS A 1 559 ? 155.547 160.423 84.640  1.00 39.17 1  559 LYS A NZ    1 
ATOM   4498  N  N     . LYS A 1 560 ? 148.250 162.910 86.836  1.00 33.31 ?  560 LYS A N     1 
ATOM   4499  C  CA    . LYS A 1 560 ? 147.227 163.945 86.955  1.00 32.75 ?  560 LYS A CA    1 
ATOM   4500  C  C     . LYS A 1 560 ? 146.381 163.737 88.204  1.00 36.91 ?  560 LYS A C     1 
ATOM   4501  O  O     . LYS A 1 560 ? 146.043 164.700 88.900  1.00 36.57 ?  560 LYS A O     1 
ATOM   4502  C  CB    . LYS A 1 560 ? 146.347 163.961 85.707  1.00 32.44 ?  560 LYS A CB    1 
ATOM   4503  C  CG    . LYS A 1 560 ? 147.062 164.415 84.448  1.00 37.98 ?  560 LYS A CG    1 
ATOM   4504  C  CD    . LYS A 1 560 ? 146.159 164.291 83.232  1.00 38.81 ?  560 LYS A CD    1 
ATOM   4505  C  CE    . LYS A 1 560 ? 146.943 164.455 81.942  1.00 35.97 ?  560 LYS A CE    1 
ATOM   4506  N  NZ    . LYS A 1 560 ? 146.180 163.955 80.766  1.00 38.72 1  560 LYS A NZ    1 
ATOM   4507  N  N     . LEU A 1 561 ? 146.028 162.485 88.503  1.00 35.84 ?  561 LEU A N     1 
ATOM   4508  C  CA    . LEU A 1 561 ? 145.272 162.196 89.718  1.00 28.48 ?  561 LEU A CA    1 
ATOM   4509  C  C     . LEU A 1 561 ? 146.085 162.514 90.967  1.00 28.17 ?  561 LEU A C     1 
ATOM   4510  O  O     . LEU A 1 561 ? 145.541 163.008 91.959  1.00 30.26 ?  561 LEU A O     1 
ATOM   4511  C  CB    . LEU A 1 561 ? 144.824 160.736 89.728  1.00 28.29 ?  561 LEU A CB    1 
ATOM   4512  C  CG    . LEU A 1 561 ? 143.992 160.326 90.945  1.00 29.77 ?  561 LEU A CG    1 
ATOM   4513  C  CD1   . LEU A 1 561 ? 142.764 161.210 91.060  1.00 26.57 ?  561 LEU A CD1   1 
ATOM   4514  C  CD2   . LEU A 1 561 ? 143.597 158.864 90.874  1.00 24.71 ?  561 LEU A CD2   1 
ATOM   4515  N  N     . LYS A 1 562 ? 147.387 162.223 90.941  1.00 29.68 ?  562 LYS A N     1 
ATOM   4516  C  CA    . LYS A 1 562 ? 148.251 162.559 92.068  1.00 30.82 ?  562 LYS A CA    1 
ATOM   4517  C  C     . LYS A 1 562 ? 148.304 164.064 92.290  1.00 35.47 ?  562 LYS A C     1 
ATOM   4518  O  O     . LYS A 1 562 ? 148.225 164.536 93.429  1.00 35.60 ?  562 LYS A O     1 
ATOM   4519  C  CB    . LYS A 1 562 ? 149.652 161.998 91.830  1.00 28.95 ?  562 LYS A CB    1 
ATOM   4520  C  CG    . LYS A 1 562 ? 150.692 162.428 92.845  1.00 29.87 ?  562 LYS A CG    1 
ATOM   4521  C  CD    . LYS A 1 562 ? 152.082 162.010 92.397  1.00 30.17 ?  562 LYS A CD    1 
ATOM   4522  C  CE    . LYS A 1 562 ? 153.139 162.408 93.409  1.00 32.22 ?  562 LYS A CE    1 
ATOM   4523  N  NZ    . LYS A 1 562 ? 154.390 161.622 93.229  1.00 34.97 1  562 LYS A NZ    1 
ATOM   4524  N  N     . ALA A 1 563 ? 148.428 164.835 91.206  1.00 34.18 ?  563 ALA A N     1 
ATOM   4525  C  CA    . ALA A 1 563 ? 148.412 166.290 91.330  1.00 31.91 ?  563 ALA A CA    1 
ATOM   4526  C  C     . ALA A 1 563 ? 147.064 166.785 91.845  1.00 31.32 ?  563 ALA A C     1 
ATOM   4527  O  O     . ALA A 1 563 ? 147.005 167.708 92.666  1.00 37.17 ?  563 ALA A O     1 
ATOM   4528  C  CB    . ALA A 1 563 ? 148.744 166.935 89.984  1.00 33.30 ?  563 ALA A CB    1 
ATOM   4529  N  N     . PHE A 1 564 ? 145.972 166.181 91.371  1.00 33.10 ?  564 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 564 ? 144.642 166.564 91.832  1.00 30.55 ?  564 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 564 ? 144.472 166.288 93.321  1.00 31.17 ?  564 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 564 ? 143.888 167.098 94.049  1.00 35.80 ?  564 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 564 ? 143.584 165.820 91.019  1.00 30.41 ?  564 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 564 ? 142.200 166.380 91.157  1.00 30.40 ?  564 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 564 ? 141.782 167.435 90.364  1.00 32.82 ?  564 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 564 ? 141.309 165.842 92.069  1.00 33.53 ?  564 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 564 ? 140.506 167.948 90.487  1.00 38.30 ?  564 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 564 ? 140.033 166.351 92.196  1.00 34.07 ?  564 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 564 ? 139.630 167.405 91.405  1.00 36.68 ?  564 PHE A CZ    1 
ATOM   4540  N  N     . VAL A 1 565 ? 144.973 165.144 93.789  1.00 32.53 ?  565 VAL A N     1 
ATOM   4541  C  CA    . VAL A 1 565 ? 144.898 164.816 95.209  1.00 27.22 ?  565 VAL A CA    1 
ATOM   4542  C  C     . VAL A 1 565 ? 145.768 165.765 96.022  1.00 31.96 ?  565 VAL A C     1 
ATOM   4543  O  O     . VAL A 1 565 ? 145.389 166.190 97.120  1.00 36.49 ?  565 VAL A O     1 
ATOM   4544  C  CB    . VAL A 1 565 ? 145.292 163.344 95.433  1.00 26.89 ?  565 VAL A CB    1 
ATOM   4545  C  CG1   . VAL A 1 565 ? 145.567 163.072 96.903  1.00 28.44 ?  565 VAL A CG1   1 
ATOM   4546  C  CG2   . VAL A 1 565 ? 144.201 162.429 94.920  1.00 30.95 ?  565 VAL A CG2   1 
ATOM   4547  N  N     . ALA A 1 566 ? 146.941 166.122 95.498  1.00 35.27 ?  566 ALA A N     1 
ATOM   4548  C  CA    . ALA A 1 566 ? 147.800 167.075 96.192  1.00 33.21 ?  566 ALA A CA    1 
ATOM   4549  C  C     . ALA A 1 566 ? 147.120 168.432 96.325  1.00 36.36 ?  566 ALA A C     1 
ATOM   4550  O  O     . ALA A 1 566 ? 147.217 169.085 97.372  1.00 36.75 ?  566 ALA A O     1 
ATOM   4551  C  CB    . ALA A 1 566 ? 149.133 167.211 95.459  1.00 32.08 ?  566 ALA A CB    1 
ATOM   4552  N  N     . GLU A 1 567 ? 146.427 168.875 95.275  1.00 36.78 ?  567 GLU A N     1 
ATOM   4553  C  CA    . GLU A 1 567 ? 145.785 170.185 95.313  1.00 35.42 ?  567 GLU A CA    1 
ATOM   4554  C  C     . GLU A 1 567 ? 144.532 170.180 96.186  1.00 38.61 ?  567 GLU A C     1 
ATOM   4555  O  O     . GLU A 1 567 ? 144.296 171.131 96.940  1.00 41.33 ?  567 GLU A O     1 
ATOM   4556  C  CB    . GLU A 1 567 ? 145.447 170.645 93.896  1.00 37.27 ?  567 GLU A CB    1 
ATOM   4557  C  CG    . GLU A 1 567 ? 146.468 171.599 93.293  1.00 42.63 ?  567 GLU A CG    1 
ATOM   4558  C  CD    . GLU A 1 567 ? 147.826 170.956 93.092  1.00 45.29 ?  567 GLU A CD    1 
ATOM   4559  O  OE1   . GLU A 1 567 ? 148.723 171.183 93.930  1.00 42.73 ?  567 GLU A OE1   1 
ATOM   4560  O  OE2   . GLU A 1 567 ? 148.000 170.232 92.089  1.00 42.47 -1 567 GLU A OE2   1 
ATOM   4561  N  N     . HIS A 1 568 ? 143.721 169.124 96.103  1.00 39.00 ?  568 HIS A N     1 
ATOM   4562  C  CA    . HIS A 1 568 ? 142.400 169.122 96.716  1.00 36.41 ?  568 HIS A CA    1 
ATOM   4563  C  C     . HIS A 1 568 ? 142.262 168.186 97.909  1.00 35.41 ?  568 HIS A C     1 
ATOM   4564  O  O     . HIS A 1 568 ? 141.292 168.317 98.661  1.00 41.18 ?  568 HIS A O     1 
ATOM   4565  C  CB    . HIS A 1 568 ? 141.338 168.754 95.671  1.00 33.87 ?  568 HIS A CB    1 
ATOM   4566  C  CG    . HIS A 1 568 ? 141.134 169.802 94.623  1.00 38.50 ?  568 HIS A CG    1 
ATOM   4567  N  ND1   . HIS A 1 568 ? 140.801 171.104 94.928  1.00 36.84 ?  568 HIS A ND1   1 
ATOM   4568  C  CD2   . HIS A 1 568 ? 141.221 169.743 93.273  1.00 37.26 ?  568 HIS A CD2   1 
ATOM   4569  C  CE1   . HIS A 1 568 ? 140.689 171.801 93.811  1.00 40.24 ?  568 HIS A CE1   1 
ATOM   4570  N  NE2   . HIS A 1 568 ? 140.938 170.999 92.793  1.00 40.01 ?  568 HIS A NE2   1 
ATOM   4571  N  N     . GLY A 1 569 ? 143.190 167.258 98.107  1.00 28.17 ?  569 GLY A N     1 
ATOM   4572  C  CA    . GLY A 1 569 ? 143.063 166.315 99.194  1.00 28.04 ?  569 GLY A CA    1 
ATOM   4573  C  C     . GLY A 1 569 ? 142.186 165.131 98.835  1.00 28.41 ?  569 GLY A C     1 
ATOM   4574  O  O     . GLY A 1 569 ? 141.759 164.947 97.693  1.00 34.15 ?  569 GLY A O     1 
ATOM   4575  N  N     . MET A 1 570 ? 141.920 164.309 99.846  1.00 25.27 ?  570 MET A N     1 
ATOM   4576  C  CA    . MET A 1 570 ? 141.094 163.119 99.694  1.00 25.78 ?  570 MET A CA    1 
ATOM   4577  C  C     . MET A 1 570 ? 140.096 163.064 100.839 1.00 24.58 ?  570 MET A C     1 
ATOM   4578  O  O     . MET A 1 570 ? 140.475 163.217 102.003 1.00 27.32 ?  570 MET A O     1 
ATOM   4579  C  CB    . MET A 1 570 ? 141.955 161.852 99.663  1.00 24.02 ?  570 MET A CB    1 
ATOM   4580  C  CG    . MET A 1 570 ? 142.466 161.494 98.276  1.00 20.26 ?  570 MET A CG    1 
ATOM   4581  S  SD    . MET A 1 570 ? 142.818 159.741 98.063  1.00 39.13 ?  570 MET A SD    1 
ATOM   4582  C  CE    . MET A 1 570 ? 141.727 159.023 99.282  1.00 25.71 ?  570 MET A CE    1 
ATOM   4583  N  N     . TYR A 1 571 ? 138.823 162.847 100.506 1.00 21.91 ?  571 TYR A N     1 
ATOM   4584  C  CA    . TYR A 1 571 ? 137.771 162.881 101.516 1.00 14.14 ?  571 TYR A CA    1 
ATOM   4585  C  C     . TYR A 1 571 ? 137.772 161.645 102.405 1.00 20.21 ?  571 TYR A C     1 
ATOM   4586  O  O     . TYR A 1 571 ? 137.483 161.751 103.602 1.00 24.53 ?  571 TYR A O     1 
ATOM   4587  C  CB    . TYR A 1 571 ? 136.405 163.036 100.848 1.00 22.96 ?  571 TYR A CB    1 
ATOM   4588  C  CG    . TYR A 1 571 ? 135.283 163.314 101.821 1.00 24.15 ?  571 TYR A CG    1 
ATOM   4589  C  CD1   . TYR A 1 571 ? 135.094 164.585 102.344 1.00 23.12 ?  571 TYR A CD1   1 
ATOM   4590  C  CD2   . TYR A 1 571 ? 134.416 162.306 102.219 1.00 18.53 ?  571 TYR A CD2   1 
ATOM   4591  C  CE1   . TYR A 1 571 ? 134.073 164.845 103.234 1.00 22.43 ?  571 TYR A CE1   1 
ATOM   4592  C  CE2   . TYR A 1 571 ? 133.393 162.557 103.109 1.00 19.81 ?  571 TYR A CE2   1 
ATOM   4593  C  CZ    . TYR A 1 571 ? 133.224 163.828 103.611 1.00 25.46 ?  571 TYR A CZ    1 
ATOM   4594  O  OH    . TYR A 1 571 ? 132.205 164.084 104.498 1.00 28.14 ?  571 TYR A OH    1 
ATOM   4595  N  N     . HIS A 1 572 ? 138.088 160.478 101.854 1.00 22.73 ?  572 HIS A N     1 
ATOM   4596  C  CA    . HIS A 1 572 ? 138.030 159.224 102.592 1.00 13.70 ?  572 HIS A CA    1 
ATOM   4597  C  C     . HIS A 1 572 ? 139.434 158.774 102.966 1.00 10.41 ?  572 HIS A C     1 
ATOM   4598  O  O     . HIS A 1 572 ? 140.328 158.744 102.116 1.00 22.35 ?  572 HIS A O     1 
ATOM   4599  C  CB    . HIS A 1 572 ? 137.337 158.135 101.772 1.00 14.68 ?  572 HIS A CB    1 
ATOM   4600  C  CG    . HIS A 1 572 ? 136.034 158.562 101.174 1.00 15.57 ?  572 HIS A CG    1 
ATOM   4601  N  ND1   . HIS A 1 572 ? 135.938 159.109 99.913  1.00 16.85 ?  572 HIS A ND1   1 
ATOM   4602  C  CD2   . HIS A 1 572 ? 134.771 158.520 101.662 1.00 9.72  ?  572 HIS A CD2   1 
ATOM   4603  C  CE1   . HIS A 1 572 ? 134.674 159.388 99.651  1.00 16.23 ?  572 HIS A CE1   1 
ATOM   4604  N  NE2   . HIS A 1 572 ? 133.946 159.040 100.696 1.00 23.78 ?  572 HIS A NE2   1 
ATOM   4605  N  N     . SER A 1 573 ? 139.623 158.433 104.241 1.00 5.57  ?  573 SER A N     1 
ATOM   4606  C  CA    . SER A 1 573 ? 140.885 157.835 104.661 1.00 7.60  ?  573 SER A CA    1 
ATOM   4607  C  C     . SER A 1 573 ? 141.079 156.469 104.019 1.00 11.79 ?  573 SER A C     1 
ATOM   4608  O  O     . SER A 1 573 ? 142.199 156.107 103.640 1.00 19.77 ?  573 SER A O     1 
ATOM   4609  C  CB    . SER A 1 573 ? 140.931 157.727 106.183 1.00 15.52 ?  573 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 573 ? 139.809 157.017 106.669 1.00 22.99 ?  573 SER A OG    1 
ATOM   4611  N  N     . TYR A 1 574 ? 140.002 155.697 103.899 1.00 12.39 ?  574 TYR A N     1 
ATOM   4612  C  CA    . TYR A 1 574 ? 140.029 154.394 103.253 1.00 1.15  ?  574 TYR A CA    1 
ATOM   4613  C  C     . TYR A 1 574 ? 138.821 154.284 102.338 1.00 8.90  ?  574 TYR A C     1 
ATOM   4614  O  O     . TYR A 1 574 ? 137.743 154.788 102.663 1.00 16.56 ?  574 TYR A O     1 
ATOM   4615  C  CB    . TYR A 1 574 ? 140.034 153.262 104.287 1.00 11.68 ?  574 TYR A CB    1 
ATOM   4616  C  CG    . TYR A 1 574 ? 141.140 153.400 105.307 1.00 8.23  ?  574 TYR A CG    1 
ATOM   4617  C  CD1   . TYR A 1 574 ? 140.954 154.151 106.459 1.00 10.27 ?  574 TYR A CD1   1 
ATOM   4618  C  CD2   . TYR A 1 574 ? 142.370 152.790 105.115 1.00 8.46  ?  574 TYR A CD2   1 
ATOM   4619  C  CE1   . TYR A 1 574 ? 141.958 154.292 107.388 1.00 6.62  ?  574 TYR A CE1   1 
ATOM   4620  C  CE2   . TYR A 1 574 ? 143.381 152.923 106.043 1.00 11.12 ?  574 TYR A CE2   1 
ATOM   4621  C  CZ    . TYR A 1 574 ? 143.168 153.675 107.178 1.00 5.82  ?  574 TYR A CZ    1 
ATOM   4622  O  OH    . TYR A 1 574 ? 144.169 153.811 108.108 1.00 18.04 ?  574 TYR A OH    1 
ATOM   4623  N  N     . ARG A 1 575 ? 139.006 153.634 101.195 1.00 11.09 ?  575 ARG A N     1 
ATOM   4624  C  CA    . ARG A 1 575 ? 137.973 153.576 100.169 1.00 4.65  ?  575 ARG A CA    1 
ATOM   4625  C  C     . ARG A 1 575 ? 137.567 152.163 99.787  1.00 9.69  ?  575 ARG A C     1 
ATOM   4626  O  O     . ARG A 1 575 ? 136.378 151.904 99.591  1.00 19.78 ?  575 ARG A O     1 
ATOM   4627  C  CB    . ARG A 1 575 ? 138.443 154.312 98.909  1.00 17.10 ?  575 ARG A CB    1 
ATOM   4628  C  CG    . ARG A 1 575 ? 138.715 155.789 99.105  1.00 11.51 ?  575 ARG A CG    1 
ATOM   4629  C  CD    . ARG A 1 575 ? 139.722 156.283 98.084  1.00 11.59 ?  575 ARG A CD    1 
ATOM   4630  N  NE    . ARG A 1 575 ? 141.052 155.741 98.334  1.00 16.30 ?  575 ARG A NE    1 
ATOM   4631  C  CZ    . ARG A 1 575 ? 141.603 154.751 97.643  1.00 14.92 ?  575 ARG A CZ    1 
ATOM   4632  N  NH1   . ARG A 1 575 ? 140.967 154.174 96.638  1.00 12.79 1  575 ARG A NH1   1 
ATOM   4633  N  NH2   . ARG A 1 575 ? 142.821 154.333 97.969  1.00 14.91 ?  575 ARG A NH2   1 
ATOM   4634  N  N     . LEU A 1 576 ? 138.519 151.241 99.671  1.00 19.64 ?  576 LEU A N     1 
ATOM   4635  C  CA    . LEU A 1 576 ? 138.270 149.929 99.093  1.00 12.26 ?  576 LEU A CA    1 
ATOM   4636  C  C     . LEU A 1 576 ? 138.568 148.841 100.112 1.00 3.41  ?  576 LEU A C     1 
ATOM   4637  O  O     . LEU A 1 576 ? 139.650 148.821 100.706 1.00 19.60 ?  576 LEU A O     1 
ATOM   4638  C  CB    . LEU A 1 576 ? 139.126 149.716 97.842  1.00 4.91  ?  576 LEU A CB    1 
ATOM   4639  C  CG    . LEU A 1 576 ? 139.108 150.824 96.789  1.00 8.38  ?  576 LEU A CG    1 
ATOM   4640  C  CD1   . LEU A 1 576 ? 140.148 150.548 95.719  1.00 11.87 ?  576 LEU A CD1   1 
ATOM   4641  C  CD2   . LEU A 1 576 ? 137.729 150.966 96.172  1.00 10.83 ?  576 LEU A CD2   1 
ATOM   4642  N  N     . CYS A 1 577 ? 137.607 147.943 100.311 1.00 1.85  ?  577 CYS A N     1 
ATOM   4643  C  CA    . CYS A 1 577 ? 137.829 146.713 101.058 1.00 6.52  ?  577 CYS A CA    1 
ATOM   4644  C  C     . CYS A 1 577 ? 136.882 145.664 100.499 1.00 16.04 ?  577 CYS A C     1 
ATOM   4645  O  O     . CYS A 1 577 ? 135.708 145.956 100.255 1.00 21.38 ?  577 CYS A O     1 
ATOM   4646  C  CB    . CYS A 1 577 ? 137.615 146.908 102.566 1.00 5.82  ?  577 CYS A CB    1 
ATOM   4647  S  SG    . CYS A 1 577 ? 135.904 146.839 103.152 1.00 27.63 ?  577 CYS A SG    1 
ATOM   4648  N  N     . ILE A 1 578 ? 137.393 144.459 100.277 1.00 8.13  ?  578 ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 578 ? 136.635 143.395 99.630  1.00 11.51 ?  578 ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 578 ? 136.100 142.481 100.726 1.00 8.57  ?  578 ILE A C     1 
ATOM   4651  O  O     . ILE A 1 578 ? 136.832 141.664 101.289 1.00 10.89 ?  578 ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 578 ? 137.484 142.634 98.610  1.00 12.84 ?  578 ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 578 ? 138.091 143.612 97.602  1.00 0.32  ?  578 ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 578 ? 136.643 141.596 97.892  1.00 8.42  ?  578 ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 578 ? 138.661 142.948 96.379  1.00 9.81  ?  578 ILE A CD1   1 
ATOM   4656  N  N     . ALA A 1 579 ? 134.814 142.621 101.024 1.00 16.56 ?  579 ALA A N     1 
ATOM   4657  C  CA    . ALA A 1 579 ? 134.086 141.845 102.014 1.00 8.89  ?  579 ALA A CA    1 
ATOM   4658  C  C     . ALA A 1 579 ? 133.650 140.507 101.430 1.00 16.81 ?  579 ALA A C     1 
ATOM   4659  O  O     . ALA A 1 579 ? 133.612 140.334 100.209 1.00 21.14 ?  579 ALA A O     1 
ATOM   4660  C  CB    . ALA A 1 579 ? 132.872 142.634 102.499 1.00 13.01 ?  579 ALA A CB    1 
ATOM   4661  N  N     . PRO A 1 580 ? 133.339 139.523 102.281 1.00 24.08 ?  580 PRO A N     1 
ATOM   4662  C  CA    . PRO A 1 580 ? 132.908 138.215 101.757 1.00 20.95 ?  580 PRO A CA    1 
ATOM   4663  C  C     . PRO A 1 580 ? 131.644 138.263 100.910 1.00 25.56 ?  580 PRO A C     1 
ATOM   4664  O  O     . PRO A 1 580 ? 131.508 137.445 99.990  1.00 31.34 ?  580 PRO A O     1 
ATOM   4665  C  CB    . PRO A 1 580 ? 132.702 137.376 103.029 1.00 17.28 ?  580 PRO A CB    1 
ATOM   4666  C  CG    . PRO A 1 580 ? 132.680 138.353 104.159 1.00 20.67 ?  580 PRO A CG    1 
ATOM   4667  C  CD    . PRO A 1 580 ? 133.549 139.483 103.737 1.00 20.22 ?  580 PRO A CD    1 
ATOM   4668  N  N     . THR A 1 581 ? 130.718 139.181 101.189 1.00 21.90 ?  581 THR A N     1 
ATOM   4669  C  CA    . THR A 1 581 ? 129.461 139.315 100.447 1.00 27.67 ?  581 THR A CA    1 
ATOM   4670  C  C     . THR A 1 581 ? 128.679 137.998 100.453 1.00 31.22 ?  581 THR A C     1 
ATOM   4671  O  O     . THR A 1 581 ? 128.480 137.346 99.429  1.00 32.14 ?  581 THR A O     1 
ATOM   4672  C  CB    . THR A 1 581 ? 129.701 139.795 99.011  1.00 27.73 ?  581 THR A CB    1 
ATOM   4673  O  OG1   . THR A 1 581 ? 130.125 138.695 98.197  1.00 23.00 ?  581 THR A OG1   1 
ATOM   4674  C  CG2   . THR A 1 581 ? 130.750 140.890 98.973  1.00 28.64 ?  581 THR A CG2   1 
ATOM   4675  N  N     . GLY A 1 582 ? 128.240 137.626 101.652 1.00 28.49 ?  582 GLY A N     1 
ATOM   4676  C  CA    . GLY A 1 582 ? 127.602 136.341 101.867 1.00 31.03 ?  582 GLY A CA    1 
ATOM   4677  C  C     . GLY A 1 582 ? 126.315 136.103 101.101 1.00 34.80 ?  582 GLY A C     1 
ATOM   4678  O  O     . GLY A 1 582 ? 126.276 135.258 100.202 1.00 33.60 ?  582 GLY A O     1 
ATOM   4679  N  N     . SER A 1 583 ? 125.255 136.837 101.438 1.00 34.42 ?  583 SER A N     1 
ATOM   4680  C  CA    . SER A 1 583 ? 123.939 136.580 100.866 1.00 38.66 ?  583 SER A CA    1 
ATOM   4681  C  C     . SER A 1 583 ? 123.566 137.524 99.733  1.00 35.70 ?  583 SER A C     1 
ATOM   4682  O  O     . SER A 1 583 ? 122.710 137.175 98.915  1.00 34.27 ?  583 SER A O     1 
ATOM   4683  C  CB    . SER A 1 583 ? 122.861 136.660 101.954 1.00 40.58 ?  583 SER A CB    1 
ATOM   4684  O  OG    . SER A 1 583 ? 122.903 135.520 102.794 1.00 41.67 ?  583 SER A OG    1 
ATOM   4685  N  N     . ILE A 1 584 ? 124.176 138.710 99.661  1.00 32.67 ?  584 ILE A N     1 
ATOM   4686  C  CA    . ILE A 1 584 ? 123.879 139.621 98.563  1.00 26.88 ?  584 ILE A CA    1 
ATOM   4687  C  C     . ILE A 1 584 ? 124.378 139.079 97.231  1.00 29.09 ?  584 ILE A C     1 
ATOM   4688  O  O     . ILE A 1 584 ? 123.884 139.491 96.177  1.00 36.37 ?  584 ILE A O     1 
ATOM   4689  C  CB    . ILE A 1 584 ? 124.471 141.018 98.832  1.00 33.33 ?  584 ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1 584 ? 125.978 140.926 99.082  1.00 34.20 ?  584 ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1 584 ? 123.753 141.687 99.994  1.00 34.09 ?  584 ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1 584 ? 126.571 142.160 99.727  1.00 28.91 ?  584 ILE A CD1   1 
ATOM   4693  N  N     . SER A 1 585 ? 125.351 138.166 97.251  1.00 30.54 ?  585 SER A N     1 
ATOM   4694  C  CA    . SER A 1 585 ? 125.815 137.557 96.008  1.00 27.64 ?  585 SER A CA    1 
ATOM   4695  C  C     . SER A 1 585 ? 124.736 136.690 95.375  1.00 26.77 ?  585 SER A C     1 
ATOM   4696  O  O     . SER A 1 585 ? 124.707 136.537 94.149  1.00 27.43 ?  585 SER A O     1 
ATOM   4697  C  CB    . SER A 1 585 ? 127.077 136.736 96.265  1.00 24.39 ?  585 SER A CB    1 
ATOM   4698  O  OG    . SER A 1 585 ? 126.842 135.728 97.231  1.00 31.13 ?  585 SER A OG    1 
ATOM   4699  N  N     . TYR A 1 586 ? 123.852 136.109 96.189  1.00 34.80 ?  586 TYR A N     1 
ATOM   4700  C  CA    . TYR A 1 586 ? 122.725 135.357 95.647  1.00 33.30 ?  586 TYR A CA    1 
ATOM   4701  C  C     . TYR A 1 586 ? 121.763 136.277 94.909  1.00 31.89 ?  586 TYR A C     1 
ATOM   4702  O  O     . TYR A 1 586 ? 121.392 136.011 93.761  1.00 35.40 ?  586 TYR A O     1 
ATOM   4703  C  CB    . TYR A 1 586 ? 121.995 134.624 96.771  1.00 32.22 ?  586 TYR A CB    1 
ATOM   4704  C  CG    . TYR A 1 586 ? 122.726 133.425 97.325  1.00 30.72 ?  586 TYR A CG    1 
ATOM   4705  C  CD1   . TYR A 1 586 ? 123.127 133.390 98.653  1.00 33.44 ?  586 TYR A CD1   1 
ATOM   4706  C  CD2   . TYR A 1 586 ? 123.004 132.325 96.527  1.00 34.07 ?  586 TYR A CD2   1 
ATOM   4707  C  CE1   . TYR A 1 586 ? 123.793 132.298 99.169  1.00 35.12 ?  586 TYR A CE1   1 
ATOM   4708  C  CE2   . TYR A 1 586 ? 123.670 131.226 97.036  1.00 34.78 ?  586 TYR A CE2   1 
ATOM   4709  C  CZ    . TYR A 1 586 ? 124.061 131.218 98.357  1.00 36.82 ?  586 TYR A CZ    1 
ATOM   4710  O  OH    . TYR A 1 586 ? 124.725 130.128 98.870  1.00 38.57 ?  586 TYR A OH    1 
ATOM   4711  N  N     . VAL A 1 587 ? 121.361 137.375 95.554  1.00 29.42 ?  587 VAL A N     1 
ATOM   4712  C  CA    . VAL A 1 587 ? 120.386 138.291 94.966  1.00 27.19 ?  587 VAL A CA    1 
ATOM   4713  C  C     . VAL A 1 587 ? 120.925 138.894 93.678  1.00 29.12 ?  587 VAL A C     1 
ATOM   4714  O  O     . VAL A 1 587 ? 120.182 139.099 92.710  1.00 34.89 ?  587 VAL A O     1 
ATOM   4715  C  CB    . VAL A 1 587 ? 120.002 139.380 95.985  1.00 31.21 ?  587 VAL A CB    1 
ATOM   4716  C  CG1   . VAL A 1 587 ? 118.944 140.300 95.408  1.00 31.59 ?  587 VAL A CG1   1 
ATOM   4717  C  CG2   . VAL A 1 587 ? 119.519 138.747 97.279  1.00 33.64 ?  587 VAL A CG2   1 
ATOM   4718  N  N     . GLN A 1 588 ? 122.222 139.182 93.640  1.00 31.49 ?  588 GLN A N     1 
ATOM   4719  C  CA    . GLN A 1 588 ? 122.850 139.742 92.453  1.00 26.60 ?  588 GLN A CA    1 
ATOM   4720  C  C     . GLN A 1 588 ? 123.210 138.683 91.423  1.00 28.18 ?  588 GLN A C     1 
ATOM   4721  O  O     . GLN A 1 588 ? 123.729 139.038 90.357  1.00 29.80 ?  588 GLN A O     1 
ATOM   4722  C  CB    . GLN A 1 588 ? 124.103 140.526 92.845  1.00 24.80 ?  588 GLN A CB    1 
ATOM   4723  C  CG    . GLN A 1 588 ? 123.815 141.800 93.613  1.00 23.53 ?  588 GLN A CG    1 
ATOM   4724  C  CD    . GLN A 1 588 ? 123.805 143.021 92.719  1.00 26.75 ?  588 GLN A CD    1 
ATOM   4725  O  OE1   . GLN A 1 588 ? 124.603 143.128 91.790  1.00 24.74 ?  588 GLN A OE1   1 
ATOM   4726  N  NE2   . GLN A 1 588 ? 122.900 143.950 92.998  1.00 32.10 ?  588 GLN A NE2   1 
ATOM   4727  N  N     . SER A 1 589 ? 122.938 137.411 91.708  1.00 29.68 ?  589 SER A N     1 
ATOM   4728  C  CA    . SER A 1 589 ? 123.328 136.293 90.852  1.00 26.27 ?  589 SER A CA    1 
ATOM   4729  C  C     . SER A 1 589 ? 124.814 136.385 90.510  1.00 28.13 ?  589 SER A C     1 
ATOM   4730  O  O     . SER A 1 589 ? 125.218 136.508 89.352  1.00 30.35 ?  589 SER A O     1 
ATOM   4731  C  CB    . SER A 1 589 ? 122.462 136.236 89.591  1.00 28.07 ?  589 SER A CB    1 
ATOM   4732  O  OG    . SER A 1 589 ? 122.891 137.179 88.626  1.00 34.21 ?  589 SER A OG    1 
ATOM   4733  N  N     . SER A 1 590 ? 125.628 136.332 91.560  1.00 27.77 ?  590 SER A N     1 
ATOM   4734  C  CA    . SER A 1 590 ? 127.060 136.538 91.445  1.00 22.98 ?  590 SER A CA    1 
ATOM   4735  C  C     . SER A 1 590 ? 127.785 135.568 92.362  1.00 24.82 ?  590 SER A C     1 
ATOM   4736  O  O     . SER A 1 590 ? 127.230 135.077 93.348  1.00 29.39 ?  590 SER A O     1 
ATOM   4737  C  CB    . SER A 1 590 ? 127.442 137.982 91.797  1.00 22.09 ?  590 SER A CB    1 
ATOM   4738  O  OG    . SER A 1 590 ? 127.788 138.097 93.164  1.00 29.32 ?  590 SER A OG    1 
ATOM   4739  N  N     . THR A 1 591 ? 129.038 135.285 92.019  1.00 23.96 ?  591 THR A N     1 
ATOM   4740  C  CA    . THR A 1 591 ? 129.900 134.523 92.906  1.00 24.18 ?  591 THR A CA    1 
ATOM   4741  C  C     . THR A 1 591 ? 130.366 135.406 94.057  1.00 23.05 ?  591 THR A C     1 
ATOM   4742  O  O     . THR A 1 591 ? 130.523 136.621 93.911  1.00 17.67 ?  591 THR A O     1 
ATOM   4743  C  CB    . THR A 1 591 ? 131.100 133.958 92.145  1.00 26.23 ?  591 THR A CB    1 
ATOM   4744  O  OG1   . THR A 1 591 ? 132.005 135.018 91.814  1.00 30.00 ?  591 THR A OG1   1 
ATOM   4745  C  CG2   . THR A 1 591 ? 130.639 133.280 90.866  1.00 25.88 ?  591 THR A CG2   1 
ATOM   4746  N  N     . ALA A 1 592 ? 130.580 134.783 95.212  1.00 22.30 ?  592 ALA A N     1 
ATOM   4747  C  CA    . ALA A 1 592 ? 130.844 135.540 96.427  1.00 22.38 ?  592 ALA A CA    1 
ATOM   4748  C  C     . ALA A 1 592 ? 132.237 136.153 96.395  1.00 22.73 ?  592 ALA A C     1 
ATOM   4749  O  O     . ALA A 1 592 ? 133.234 135.446 96.226  1.00 27.19 ?  592 ALA A O     1 
ATOM   4750  C  CB    . ALA A 1 592 ? 130.691 134.641 97.653  1.00 24.34 ?  592 ALA A CB    1 
ATOM   4751  N  N     . SER A 1 593 ? 132.295 137.468 96.562  1.00 24.21 ?  593 SER A N     1 
ATOM   4752  C  CA    . SER A 1 593 ? 133.539 138.230 96.701  1.00 16.30 ?  593 SER A CA    1 
ATOM   4753  C  C     . SER A 1 593 ? 134.431 137.976 95.485  1.00 15.94 ?  593 SER A C     1 
ATOM   4754  O  O     . SER A 1 593 ? 133.947 137.661 94.393  1.00 23.75 ?  593 SER A O     1 
ATOM   4755  C  CB    . SER A 1 593 ? 134.175 137.889 98.037  1.00 25.18 ?  593 SER A CB    1 
ATOM   4756  O  OG    . SER A 1 593 ? 135.214 138.793 98.358  1.00 24.78 ?  593 SER A OG    1 
ATOM   4757  N  N     . VAL A 1 594 ? 135.744 138.122 95.661  1.00 21.63 ?  594 VAL A N     1 
ATOM   4758  C  CA    . VAL A 1 594 ? 136.713 137.747 94.642  1.00 19.48 ?  594 VAL A CA    1 
ATOM   4759  C  C     . VAL A 1 594 ? 137.200 136.317 94.834  1.00 18.95 ?  594 VAL A C     1 
ATOM   4760  O  O     . VAL A 1 594 ? 138.138 135.885 94.158  1.00 18.36 ?  594 VAL A O     1 
ATOM   4761  C  CB    . VAL A 1 594 ? 137.896 138.728 94.615  1.00 21.54 ?  594 VAL A CB    1 
ATOM   4762  C  CG1   . VAL A 1 594 ? 137.430 140.103 94.164  1.00 9.11  ?  594 VAL A CG1   1 
ATOM   4763  C  CG2   . VAL A 1 594 ? 138.552 138.802 95.982  1.00 17.90 ?  594 VAL A CG2   1 
ATOM   4764  N  N     . MET A 1 595 ? 136.583 135.574 95.748  1.00 25.45 ?  595 MET A N     1 
ATOM   4765  C  CA    . MET A 1 595 ? 136.958 134.192 95.980  1.00 18.76 ?  595 MET A CA    1 
ATOM   4766  C  C     . MET A 1 595 ? 136.522 133.319 94.806  1.00 24.58 ?  595 MET A C     1 
ATOM   4767  O  O     . MET A 1 595 ? 135.534 133.618 94.130  1.00 32.18 ?  595 MET A O     1 
ATOM   4768  C  CB    . MET A 1 595 ? 136.313 133.674 97.263  1.00 22.37 ?  595 MET A CB    1 
ATOM   4769  C  CG    . MET A 1 595 ? 136.989 134.003 98.612  1.00 25.47 ?  595 MET A CG    1 
ATOM   4770  S  SD    . MET A 1 595 ? 138.789 133.919 98.815  1.00 31.61 ?  595 MET A SD    1 
ATOM   4771  C  CE    . MET A 1 595 ? 139.371 135.393 97.983  1.00 18.71 ?  595 MET A CE    1 
ATOM   4772  N  N     . PRO A 1 596 ? 137.246 132.236 94.539  1.00 27.55 ?  596 PRO A N     1 
ATOM   4773  C  CA    . PRO A 1 596 ? 136.741 131.227 93.605  1.00 22.18 ?  596 PRO A CA    1 
ATOM   4774  C  C     . PRO A 1 596 ? 135.569 130.469 94.209  1.00 27.22 ?  596 PRO A C     1 
ATOM   4775  O  O     . PRO A 1 596 ? 135.405 130.387 95.428  1.00 31.05 ?  596 PRO A O     1 
ATOM   4776  C  CB    . PRO A 1 596 ? 137.947 130.310 93.381  1.00 23.92 ?  596 PRO A CB    1 
ATOM   4777  C  CG    . PRO A 1 596 ? 138.794 130.497 94.593  1.00 28.34 ?  596 PRO A CG    1 
ATOM   4778  C  CD    . PRO A 1 596 ? 138.597 131.916 95.031  1.00 28.46 ?  596 PRO A CD    1 
ATOM   4779  N  N     . ILE A 1 597 ? 134.739 129.912 93.326  1.00 29.21 ?  597 ILE A N     1 
ATOM   4780  C  CA    . ILE A 1 597 ? 133.537 129.221 93.773  1.00 31.33 ?  597 ILE A CA    1 
ATOM   4781  C  C     . ILE A 1 597 ? 133.913 127.941 94.511  1.00 34.65 ?  597 ILE A C     1 
ATOM   4782  O  O     . ILE A 1 597 ? 134.864 127.236 94.149  1.00 36.12 ?  597 ILE A O     1 
ATOM   4783  C  CB    . ILE A 1 597 ? 132.603 128.925 92.585  1.00 32.00 ?  597 ILE A CB    1 
ATOM   4784  C  CG1   . ILE A 1 597 ? 133.258 127.945 91.609  1.00 31.16 ?  597 ILE A CG1   1 
ATOM   4785  C  CG2   . ILE A 1 597 ? 132.234 130.210 91.872  1.00 31.63 ?  597 ILE A CG2   1 
ATOM   4786  C  CD1   . ILE A 1 597 ? 132.272 127.161 90.779  1.00 31.93 ?  597 ILE A CD1   1 
ATOM   4787  N  N     . MET A 1 598 ? 133.163 127.644 95.572  1.00 39.86 ?  598 MET A N     1 
ATOM   4788  C  CA    . MET A 1 598 ? 133.396 126.417 96.323  1.00 38.55 ?  598 MET A CA    1 
ATOM   4789  C  C     . MET A 1 598 ? 132.805 125.208 95.610  1.00 38.59 ?  598 MET A C     1 
ATOM   4790  O  O     . MET A 1 598 ? 133.443 124.154 95.533  1.00 44.29 ?  598 MET A O     1 
ATOM   4791  C  CB    . MET A 1 598 ? 132.813 126.545 97.729  1.00 37.06 ?  598 MET A CB    1 
ATOM   4792  C  CG    . MET A 1 598 ? 133.737 127.219 98.723  1.00 35.00 ?  598 MET A CG    1 
ATOM   4793  S  SD    . MET A 1 598 ? 132.927 127.577 100.292 1.00 53.18 ?  598 MET A SD    1 
ATOM   4794  C  CE    . MET A 1 598 ? 131.729 128.803 99.778  1.00 39.51 ?  598 MET A CE    1 
ATOM   4795  N  N     . GLU A 1 599 ? 131.586 125.345 95.092  1.00 38.15 ?  599 GLU A N     1 
ATOM   4796  C  CA    . GLU A 1 599 ? 130.911 124.289 94.356  1.00 37.01 ?  599 GLU A CA    1 
ATOM   4797  C  C     . GLU A 1 599 ? 130.311 124.872 93.087  1.00 36.30 ?  599 GLU A C     1 
ATOM   4798  O  O     . GLU A 1 599 ? 129.923 126.041 93.048  1.00 40.49 ?  599 GLU A O     1 
ATOM   4799  C  CB    . GLU A 1 599 ? 129.804 123.631 95.196  1.00 38.85 ?  599 GLU A CB    1 
ATOM   4800  C  CG    . GLU A 1 599 ? 130.178 123.377 96.647  1.00 39.53 ?  599 GLU A CG    1 
ATOM   4801  C  CD    . GLU A 1 599 ? 128.973 123.366 97.567  1.00 43.17 ?  599 GLU A CD    1 
ATOM   4802  O  OE1   . GLU A 1 599 ? 128.486 124.458 97.926  1.00 40.97 ?  599 GLU A OE1   1 
ATOM   4803  O  OE2   . GLU A 1 599 ? 128.512 122.264 97.932  1.00 45.94 -1 599 GLU A OE2   1 
ATOM   4804  N  N     . ARG A 1 600 ? 130.244 124.049 92.039  1.00 38.66 ?  600 ARG A N     1 
ATOM   4805  C  CA    . ARG A 1 600 ? 129.590 124.490 90.812  1.00 35.38 ?  600 ARG A CA    1 
ATOM   4806  C  C     . ARG A 1 600 ? 128.085 124.608 91.013  1.00 34.16 ?  600 ARG A C     1 
ATOM   4807  O  O     . ARG A 1 600 ? 127.470 125.607 90.624  1.00 37.87 ?  600 ARG A O     1 
ATOM   4808  C  CB    . ARG A 1 600 ? 129.909 123.529 89.670  1.00 34.71 ?  600 ARG A CB    1 
ATOM   4809  C  CG    . ARG A 1 600 ? 131.272 123.748 89.057  1.00 35.12 ?  600 ARG A CG    1 
ATOM   4810  C  CD    . ARG A 1 600 ? 131.472 122.865 87.848  1.00 34.48 ?  600 ARG A CD    1 
ATOM   4811  N  NE    . ARG A 1 600 ? 132.787 123.045 87.246  1.00 34.15 ?  600 ARG A NE    1 
ATOM   4812  C  CZ    . ARG A 1 600 ? 133.883 122.418 87.648  1.00 37.48 ?  600 ARG A CZ    1 
ATOM   4813  N  NH1   . ARG A 1 600 ? 133.861 121.568 88.661  1.00 36.61 1  600 ARG A NH1   1 
ATOM   4814  N  NH2   . ARG A 1 600 ? 135.031 122.651 87.018  1.00 37.83 ?  600 ARG A NH2   1 
ATOM   4815  N  N     . ILE A 1 601 ? 127.478 123.592 91.616  1.00 39.12 ?  601 ILE A N     1 
ATOM   4816  C  CA    . ILE A 1 601 ? 126.080 123.622 92.024  1.00 41.28 ?  601 ILE A CA    1 
ATOM   4817  C  C     . ILE A 1 601 ? 126.042 123.316 93.513  1.00 40.35 ?  601 ILE A C     1 
ATOM   4818  O  O     . ILE A 1 601 ? 126.566 122.285 93.954  1.00 41.59 ?  601 ILE A O     1 
ATOM   4819  C  CB    . ILE A 1 601 ? 125.226 122.618 91.236  1.00 40.71 ?  601 ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1 601 ? 125.412 122.821 89.732  1.00 41.03 ?  601 ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1 601 ? 123.761 122.758 91.612  1.00 37.03 ?  601 ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1 601 ? 124.815 121.719 88.891  1.00 39.55 ?  601 ILE A CD1   1 
ATOM   4823  N  N     . GLU A 1 602 ? 125.430 124.206 94.286  1.00 45.16 ?  602 GLU A N     1 
ATOM   4824  C  CA    . GLU A 1 602 ? 125.348 124.048 95.729  1.00 47.44 ?  602 GLU A CA    1 
ATOM   4825  C  C     . GLU A 1 602 ? 123.965 123.556 96.132  1.00 48.63 ?  602 GLU A C     1 
ATOM   4826  O  O     . GLU A 1 602 ? 122.944 124.044 95.637  1.00 48.67 ?  602 GLU A O     1 
ATOM   4827  C  CB    . GLU A 1 602 ? 125.675 125.360 96.448  1.00 45.19 ?  602 GLU A CB    1 
ATOM   4828  C  CG    . GLU A 1 602 ? 124.878 126.558 95.975  1.00 47.09 ?  602 GLU A CG    1 
ATOM   4829  C  CD    . GLU A 1 602 ? 125.087 127.774 96.854  1.00 50.58 ?  602 GLU A CD    1 
ATOM   4830  O  OE1   . GLU A 1 602 ? 126.146 128.424 96.731  1.00 50.27 ?  602 GLU A OE1   1 
ATOM   4831  O  OE2   . GLU A 1 602 ? 124.191 128.082 97.668  1.00 51.85 -1 602 GLU A OE2   1 
ATOM   4832  N  N     . GLU A 1 603 ? 123.945 122.573 97.026  1.00 56.87 ?  603 GLU A N     1 
ATOM   4833  C  CA    . GLU A 1 603 ? 122.719 121.987 97.547  1.00 57.73 ?  603 GLU A CA    1 
ATOM   4834  C  C     . GLU A 1 603 ? 122.430 122.565 98.924  1.00 57.59 ?  603 GLU A C     1 
ATOM   4835  O  O     . GLU A 1 603 ? 123.282 122.510 99.816  1.00 57.50 ?  603 GLU A O     1 
ATOM   4836  C  CB    . GLU A 1 603 ? 122.843 120.465 97.627  1.00 57.17 ?  603 GLU A CB    1 
ATOM   4837  C  CG    . GLU A 1 603 ? 121.608 119.761 98.153  1.00 58.95 ?  603 GLU A CG    1 
ATOM   4838  C  CD    . GLU A 1 603 ? 121.945 118.497 98.917  1.00 60.15 ?  603 GLU A CD    1 
ATOM   4839  O  OE1   . GLU A 1 603 ? 122.277 118.598 100.117 1.00 60.48 ?  603 GLU A OE1   1 
ATOM   4840  O  OE2   . GLU A 1 603 ? 121.879 117.405 98.320  1.00 59.56 -1 603 GLU A OE2   1 
ATOM   4841  N  N     . ARG A 1 604 ? 121.231 123.116 99.096  1.00 58.62 ?  604 ARG A N     1 
ATOM   4842  C  CA    . ARG A 1 604 ? 120.833 123.713 100.360 1.00 59.06 ?  604 ARG A CA    1 
ATOM   4843  C  C     . ARG A 1 604 ? 119.517 123.105 100.824 1.00 59.92 ?  604 ARG A C     1 
ATOM   4844  O  O     . ARG A 1 604 ? 118.729 122.602 100.022 1.00 59.33 ?  604 ARG A O     1 
ATOM   4845  C  CB    . ARG A 1 604 ? 120.699 125.236 100.250 1.00 58.99 ?  604 ARG A CB    1 
ATOM   4846  C  CG    . ARG A 1 604 ? 121.965 125.933 99.784  1.00 58.38 ?  604 ARG A CG    1 
ATOM   4847  C  CD    . ARG A 1 604 ? 122.820 126.366 100.962 1.00 58.50 ?  604 ARG A CD    1 
ATOM   4848  N  NE    . ARG A 1 604 ? 123.920 125.441 101.205 1.00 58.72 ?  604 ARG A NE    1 
ATOM   4849  C  CZ    . ARG A 1 604 ? 125.128 125.556 100.670 1.00 59.29 ?  604 ARG A CZ    1 
ATOM   4850  N  NH1   . ARG A 1 604 ? 125.430 126.550 99.852  1.00 57.85 1  604 ARG A NH1   1 
ATOM   4851  N  NH2   . ARG A 1 604 ? 126.056 124.648 100.962 1.00 57.26 ?  604 ARG A NH2   1 
ATOM   4852  N  N     . THR A 1 605 ? 119.298 123.143 102.135 1.00 65.73 ?  605 THR A N     1 
ATOM   4853  C  CA    . THR A 1 605 ? 118.082 122.619 102.750 1.00 66.61 ?  605 THR A CA    1 
ATOM   4854  C  C     . THR A 1 605 ? 117.374 123.763 103.463 1.00 66.54 ?  605 THR A C     1 
ATOM   4855  O  O     . THR A 1 605 ? 117.874 124.277 104.469 1.00 65.70 ?  605 THR A O     1 
ATOM   4856  C  CB    . THR A 1 605 ? 118.401 121.484 103.723 1.00 66.19 ?  605 THR A CB    1 
ATOM   4857  O  OG1   . THR A 1 605 ? 119.157 120.471 103.049 1.00 66.36 ?  605 THR A OG1   1 
ATOM   4858  C  CG2   . THR A 1 605 ? 117.118 120.874 104.266 1.00 66.87 ?  605 THR A CG2   1 
ATOM   4859  N  N     . TYR A 1 606 ? 116.216 124.160 102.945 1.00 66.48 ?  606 TYR A N     1 
ATOM   4860  C  CA    . TYR A 1 606 ? 115.384 125.177 103.571 1.00 68.28 ?  606 TYR A CA    1 
ATOM   4861  C  C     . TYR A 1 606 ? 114.090 124.531 104.042 1.00 70.28 ?  606 TYR A C     1 
ATOM   4862  O  O     . TYR A 1 606 ? 113.384 123.896 103.249 1.00 69.13 ?  606 TYR A O     1 
ATOM   4863  C  CB    . TYR A 1 606 ? 115.092 126.330 102.607 1.00 66.57 ?  606 TYR A CB    1 
ATOM   4864  C  CG    . TYR A 1 606 ? 116.321 127.118 102.214 1.00 68.29 ?  606 TYR A CG    1 
ATOM   4865  C  CD1   . TYR A 1 606 ? 117.021 127.865 103.153 1.00 66.92 ?  606 TYR A CD1   1 
ATOM   4866  C  CD2   . TYR A 1 606 ? 116.779 127.118 100.906 1.00 67.97 ?  606 TYR A CD2   1 
ATOM   4867  C  CE1   . TYR A 1 606 ? 118.145 128.587 102.797 1.00 66.54 ?  606 TYR A CE1   1 
ATOM   4868  C  CE2   . TYR A 1 606 ? 117.901 127.837 100.541 1.00 65.78 ?  606 TYR A CE2   1 
ATOM   4869  C  CZ    . TYR A 1 606 ? 118.580 128.569 101.489 1.00 67.46 ?  606 TYR A CZ    1 
ATOM   4870  O  OH    . TYR A 1 606 ? 119.697 129.285 101.126 1.00 66.96 ?  606 TYR A OH    1 
ATOM   4871  N  N     . GLY A 1 607 ? 113.781 124.700 105.324 1.00 75.36 ?  607 GLY A N     1 
ATOM   4872  C  CA    . GLY A 1 607 ? 112.665 123.967 105.900 1.00 74.97 ?  607 GLY A CA    1 
ATOM   4873  C  C     . GLY A 1 607 ? 112.917 122.479 105.780 1.00 75.53 ?  607 GLY A C     1 
ATOM   4874  O  O     . GLY A 1 607 ? 113.962 121.966 106.196 1.00 75.04 ?  607 GLY A O     1 
ATOM   4875  N  N     . ASN A 1 608 ? 111.950 121.769 105.201 1.00 78.59 ?  608 ASN A N     1 
ATOM   4876  C  CA    . ASN A 1 608 ? 112.099 120.354 104.891 1.00 80.29 ?  608 ASN A CA    1 
ATOM   4877  C  C     . ASN A 1 608 ? 112.269 120.114 103.395 1.00 79.21 ?  608 ASN A C     1 
ATOM   4878  O  O     . ASN A 1 608 ? 112.024 119.003 102.915 1.00 78.37 ?  608 ASN A O     1 
ATOM   4879  C  CB    . ASN A 1 608 ? 110.905 119.563 105.427 1.00 79.45 ?  608 ASN A CB    1 
ATOM   4880  C  CG    . ASN A 1 608 ? 110.966 119.367 106.930 1.00 79.47 ?  608 ASN A CG    1 
ATOM   4881  O  OD1   . ASN A 1 608 ? 111.993 119.622 107.560 1.00 79.06 ?  608 ASN A OD1   1 
ATOM   4882  N  ND2   . ASN A 1 608 ? 109.864 118.911 107.513 1.00 78.01 ?  608 ASN A ND2   1 
ATOM   4883  N  N     . SER A 1 609 ? 112.686 121.136 102.651 1.00 73.08 ?  609 SER A N     1 
ATOM   4884  C  CA    . SER A 1 609 ? 112.805 121.061 101.205 1.00 72.48 ?  609 SER A CA    1 
ATOM   4885  C  C     . SER A 1 609 ? 114.253 121.267 100.781 1.00 73.03 ?  609 SER A C     1 
ATOM   4886  O  O     . SER A 1 609 ? 115.025 121.962 101.449 1.00 72.83 ?  609 SER A O     1 
ATOM   4887  C  CB    . SER A 1 609 ? 111.912 122.103 100.524 1.00 71.53 ?  609 SER A CB    1 
ATOM   4888  O  OG    . SER A 1 609 ? 112.292 123.418 100.891 1.00 70.80 ?  609 SER A OG    1 
ATOM   4889  N  N     . LYS A 1 610 ? 114.614 120.642 99.664  1.00 65.08 ?  610 LYS A N     1 
ATOM   4890  C  CA    . LYS A 1 610 ? 115.950 120.747 99.099  1.00 62.96 ?  610 LYS A CA    1 
ATOM   4891  C  C     . LYS A 1 610 ? 115.925 121.682 97.897  1.00 63.45 ?  610 LYS A C     1 
ATOM   4892  O  O     . LYS A 1 610 ? 114.949 121.714 97.142  1.00 64.05 ?  610 LYS A O     1 
ATOM   4893  C  CB    . LYS A 1 610 ? 116.476 119.372 98.683  1.00 62.17 ?  610 LYS A CB    1 
ATOM   4894  C  CG    . LYS A 1 610 ? 117.990 119.283 98.600  1.00 63.41 ?  610 LYS A CG    1 
ATOM   4895  C  CD    . LYS A 1 610 ? 118.497 118.004 99.251  1.00 64.78 ?  610 LYS A CD    1 
ATOM   4896  C  CE    . LYS A 1 610 ? 118.610 118.152 100.761 1.00 64.27 ?  610 LYS A CE    1 
ATOM   4897  N  NZ    . LYS A 1 610 ? 119.820 118.915 101.169 1.00 62.54 1  610 LYS A NZ    1 
ATOM   4898  N  N     . THR A 1 611 ? 117.003 122.443 97.725  1.00 61.72 ?  611 THR A N     1 
ATOM   4899  C  CA    . THR A 1 611 ? 117.107 123.396 96.633  1.00 58.73 ?  611 THR A CA    1 
ATOM   4900  C  C     . THR A 1 611 ? 118.519 123.358 96.068  1.00 57.57 ?  611 THR A C     1 
ATOM   4901  O  O     . THR A 1 611 ? 119.481 122.997 96.753  1.00 56.69 ?  611 THR A O     1 
ATOM   4902  C  CB    . THR A 1 611 ? 116.750 124.817 97.085  1.00 58.99 ?  611 THR A CB    1 
ATOM   4903  O  OG1   . THR A 1 611 ? 116.794 125.702 95.960  1.00 61.87 ?  611 THR A OG1   1 
ATOM   4904  C  CG2   . THR A 1 611 ? 117.727 125.294 98.139  1.00 59.35 ?  611 THR A CG2   1 
ATOM   4905  N  N     . TYR A 1 612 ? 118.628 123.747 94.800  1.00 53.41 ?  612 TYR A N     1 
ATOM   4906  C  CA    . TYR A 1 612 ? 119.855 123.602 94.029  1.00 51.64 ?  612 TYR A CA    1 
ATOM   4907  C  C     . TYR A 1 612 ? 120.174 124.936 93.373  1.00 54.03 ?  612 TYR A C     1 
ATOM   4908  O  O     . TYR A 1 612 ? 119.361 125.460 92.605  1.00 56.09 ?  612 TYR A O     1 
ATOM   4909  C  CB    . TYR A 1 612 ? 119.688 122.507 92.973  1.00 53.90 ?  612 TYR A CB    1 
ATOM   4910  C  CG    . TYR A 1 612 ? 119.637 121.115 93.557  1.00 55.12 ?  612 TYR A CG    1 
ATOM   4911  C  CD1   . TYR A 1 612 ? 120.631 120.659 94.410  1.00 54.59 ?  612 TYR A CD1   1 
ATOM   4912  C  CD2   . TYR A 1 612 ? 118.562 120.276 93.300  1.00 54.58 ?  612 TYR A CD2   1 
ATOM   4913  C  CE1   . TYR A 1 612 ? 120.578 119.391 94.951  1.00 55.95 ?  612 TYR A CE1   1 
ATOM   4914  C  CE2   . TYR A 1 612 ? 118.494 119.009 93.846  1.00 55.96 ?  612 TYR A CE2   1 
ATOM   4915  C  CZ    . TYR A 1 612 ? 119.507 118.571 94.670  1.00 57.43 ?  612 TYR A CZ    1 
ATOM   4916  O  OH    . TYR A 1 612 ? 119.451 117.310 95.217  1.00 58.99 ?  612 TYR A OH    1 
ATOM   4917  N  N     . TYR A 1 613 ? 121.348 125.486 93.675  1.00 46.07 ?  613 TYR A N     1 
ATOM   4918  C  CA    . TYR A 1 613 ? 121.796 126.741 93.073  1.00 40.41 ?  613 TYR A CA    1 
ATOM   4919  C  C     . TYR A 1 613 ? 123.044 126.506 92.239  1.00 39.86 ?  613 TYR A C     1 
ATOM   4920  O  O     . TYR A 1 613 ? 124.138 126.314 92.796  1.00 39.39 ?  613 TYR A O     1 
ATOM   4921  C  CB    . TYR A 1 613 ? 122.065 127.799 94.140  1.00 40.96 ?  613 TYR A CB    1 
ATOM   4922  C  CG    . TYR A 1 613 ? 122.526 129.123 93.570  1.00 37.21 ?  613 TYR A CG    1 
ATOM   4923  C  CD1   . TYR A 1 613 ? 121.777 129.784 92.606  1.00 37.85 ?  613 TYR A CD1   1 
ATOM   4924  C  CD2   . TYR A 1 613 ? 123.712 129.709 93.992  1.00 37.53 ?  613 TYR A CD2   1 
ATOM   4925  C  CE1   . TYR A 1 613 ? 122.192 130.992 92.083  1.00 41.31 ?  613 TYR A CE1   1 
ATOM   4926  C  CE2   . TYR A 1 613 ? 124.135 130.917 93.474  1.00 39.98 ?  613 TYR A CE2   1 
ATOM   4927  C  CZ    . TYR A 1 613 ? 123.372 131.554 92.519  1.00 44.91 ?  613 TYR A CZ    1 
ATOM   4928  O  OH    . TYR A 1 613 ? 123.788 132.757 91.999  1.00 41.53 ?  613 TYR A OH    1 
ATOM   4929  N  N     . PRO A 1 614 ? 122.933 126.471 90.915  1.00 41.29 ?  614 PRO A N     1 
ATOM   4930  C  CA    . PRO A 1 614 ? 124.138 126.499 90.083  1.00 38.89 ?  614 PRO A CA    1 
ATOM   4931  C  C     . PRO A 1 614 ? 124.789 127.870 90.140  1.00 39.14 ?  614 PRO A C     1 
ATOM   4932  O  O     . PRO A 1 614 ? 124.132 128.887 90.372  1.00 37.77 ?  614 PRO A O     1 
ATOM   4933  C  CB    . PRO A 1 614 ? 123.614 126.187 88.675  1.00 35.09 ?  614 PRO A CB    1 
ATOM   4934  C  CG    . PRO A 1 614 ? 122.208 125.694 88.866  1.00 39.46 ?  614 PRO A CG    1 
ATOM   4935  C  CD    . PRO A 1 614 ? 121.709 126.345 90.110  1.00 39.99 ?  614 PRO A CD    1 
ATOM   4936  N  N     . MET A 1 615 ? 126.101 127.890 89.932  1.00 37.84 ?  615 MET A N     1 
ATOM   4937  C  CA    . MET A 1 615 ? 126.807 129.157 89.879  1.00 35.62 ?  615 MET A CA    1 
ATOM   4938  C  C     . MET A 1 615 ? 126.328 129.971 88.679  1.00 38.19 ?  615 MET A C     1 
ATOM   4939  O  O     . MET A 1 615 ? 125.947 129.408 87.649  1.00 40.78 ?  615 MET A O     1 
ATOM   4940  C  CB    . MET A 1 615 ? 128.315 128.928 89.820  1.00 36.41 ?  615 MET A CB    1 
ATOM   4941  C  CG    . MET A 1 615 ? 128.925 128.694 91.192  1.00 37.79 ?  615 MET A CG    1 
ATOM   4942  S  SD    . MET A 1 615 ? 127.971 129.539 92.470  1.00 44.79 ?  615 MET A SD    1 
ATOM   4943  C  CE    . MET A 1 615 ? 128.470 128.653 93.940  1.00 37.65 ?  615 MET A CE    1 
ATOM   4944  N  N     . PRO A 1 616 ? 126.305 131.298 88.798  1.00 38.31 ?  616 PRO A N     1 
ATOM   4945  C  CA    . PRO A 1 616 ? 125.701 132.127 87.746  1.00 35.48 ?  616 PRO A CA    1 
ATOM   4946  C  C     . PRO A 1 616 ? 126.400 131.941 86.408  1.00 36.21 ?  616 PRO A C     1 
ATOM   4947  O  O     . PRO A 1 616 ? 127.628 131.967 86.319  1.00 38.12 ?  616 PRO A O     1 
ATOM   4948  C  CB    . PRO A 1 616 ? 125.874 133.553 88.280  1.00 36.48 ?  616 PRO A CB    1 
ATOM   4949  C  CG    . PRO A 1 616 ? 126.061 133.387 89.754  1.00 35.50 ?  616 PRO A CG    1 
ATOM   4950  C  CD    . PRO A 1 616 ? 126.791 132.104 89.929  1.00 35.95 ?  616 PRO A CD    1 
ATOM   4951  N  N     . GLY A 1 617 ? 125.600 131.759 85.361  1.00 37.13 ?  617 GLY A N     1 
ATOM   4952  C  CA    . GLY A 1 617 ? 126.139 131.547 84.034  1.00 36.09 ?  617 GLY A CA    1 
ATOM   4953  C  C     . GLY A 1 617 ? 126.744 130.185 83.797  1.00 40.13 ?  617 GLY A C     1 
ATOM   4954  O  O     . GLY A 1 617 ? 127.402 129.988 82.771  1.00 42.08 ?  617 GLY A O     1 
ATOM   4955  N  N     . LEU A 1 618 ? 126.548 129.236 84.710  1.00 41.11 ?  618 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 618 ? 127.118 127.907 84.542  1.00 37.11 ?  618 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 618 ? 126.394 127.156 83.433  1.00 39.55 ?  618 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 618 ? 125.161 127.119 83.391  1.00 44.58 ?  618 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 618 ? 127.041 127.122 85.850  1.00 37.34 ?  618 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 618 ? 127.634 125.713 85.834  1.00 38.46 ?  618 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 618 ? 129.101 125.750 85.444  1.00 38.88 ?  618 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 618 ? 127.456 125.042 87.186  1.00 39.00 ?  618 LEU A CD2   1 
ATOM   4963  N  N     . ALA A 1 619 ? 127.168 126.556 82.534  1.00 45.15 ?  619 ALA A N     1 
ATOM   4964  C  CA    . ALA A 1 619 ? 126.627 125.769 81.438  1.00 45.77 ?  619 ALA A CA    1 
ATOM   4965  C  C     . ALA A 1 619 ? 127.641 124.689 81.087  1.00 49.12 ?  619 ALA A C     1 
ATOM   4966  O  O     . ALA A 1 619 ? 128.649 124.509 81.775  1.00 51.63 ?  619 ALA A O     1 
ATOM   4967  C  CB    . ALA A 1 619 ? 126.298 126.651 80.231  1.00 44.64 ?  619 ALA A CB    1 
ATOM   4968  N  N     . SER A 1 620 ? 127.365 123.964 80.002  1.00 50.10 ?  620 SER A N     1 
ATOM   4969  C  CA    . SER A 1 620 ? 128.293 122.929 79.561  1.00 49.28 ?  620 SER A CA    1 
ATOM   4970  C  C     . SER A 1 620 ? 129.574 123.536 79.003  1.00 49.15 ?  620 SER A C     1 
ATOM   4971  O  O     . SER A 1 620 ? 130.660 122.967 79.166  1.00 51.61 ?  620 SER A O     1 
ATOM   4972  C  CB    . SER A 1 620 ? 127.621 122.035 78.520  1.00 52.72 ?  620 SER A CB    1 
ATOM   4973  O  OG    . SER A 1 620 ? 126.395 121.518 79.008  1.00 54.05 ?  620 SER A OG    1 
ATOM   4974  N  N     . ASN A 1 621 ? 129.469 124.691 78.341  1.00 47.90 ?  621 ASN A N     1 
ATOM   4975  C  CA    . ASN A 1 621 ? 130.644 125.299 77.725  1.00 50.30 ?  621 ASN A CA    1 
ATOM   4976  C  C     . ASN A 1 621 ? 131.610 125.842 78.772  1.00 50.21 ?  621 ASN A C     1 
ATOM   4977  O  O     . ASN A 1 621 ? 132.831 125.735 78.610  1.00 50.40 ?  621 ASN A O     1 
ATOM   4978  C  CB    . ASN A 1 621 ? 130.216 126.406 76.763  1.00 49.26 ?  621 ASN A CB    1 
ATOM   4979  C  CG    . ASN A 1 621 ? 128.967 127.127 77.224  1.00 51.92 ?  621 ASN A CG    1 
ATOM   4980  O  OD1   . ASN A 1 621 ? 128.932 127.697 78.314  1.00 50.98 ?  621 ASN A OD1   1 
ATOM   4981  N  ND2   . ASN A 1 621 ? 127.930 127.104 76.394  1.00 51.57 ?  621 ASN A ND2   1 
ATOM   4982  N  N     . ASN A 1 622 ? 131.087 126.428 79.850  1.00 40.26 ?  622 ASN A N     1 
ATOM   4983  C  CA    . ASN A 1 622 ? 131.918 127.018 80.892  1.00 39.73 ?  622 ASN A CA    1 
ATOM   4984  C  C     . ASN A 1 622 ? 131.948 126.173 82.162  1.00 43.21 ?  622 ASN A C     1 
ATOM   4985  O  O     . ASN A 1 622 ? 132.299 126.681 83.231  1.00 47.91 ?  622 ASN A O     1 
ATOM   4986  C  CB    . ASN A 1 622 ? 131.452 128.442 81.204  1.00 40.12 ?  622 ASN A CB    1 
ATOM   4987  C  CG    . ASN A 1 622 ? 129.980 128.515 81.566  1.00 41.94 ?  622 ASN A CG    1 
ATOM   4988  O  OD1   . ASN A 1 622 ? 129.347 127.503 81.865  1.00 47.40 ?  622 ASN A OD1   1 
ATOM   4989  N  ND2   . ASN A 1 622 ? 129.427 129.721 81.538  1.00 38.35 ?  622 ASN A ND2   1 
ATOM   4990  N  N     . TRP A 1 623 ? 131.581 124.893 82.067  1.00 40.70 ?  623 TRP A N     1 
ATOM   4991  C  CA    . TRP A 1 623 ? 131.656 124.014 83.229  1.00 40.55 ?  623 TRP A CA    1 
ATOM   4992  C  C     . TRP A 1 623 ? 133.097 123.839 83.690  1.00 41.55 ?  623 TRP A C     1 
ATOM   4993  O  O     . TRP A 1 623 ? 133.375 123.816 84.894  1.00 40.00 ?  623 TRP A O     1 
ATOM   4994  C  CB    . TRP A 1 623 ? 131.024 122.660 82.903  1.00 41.25 ?  623 TRP A CB    1 
ATOM   4995  C  CG    . TRP A 1 623 ? 131.150 121.641 83.996  1.00 40.04 ?  623 TRP A CG    1 
ATOM   4996  C  CD1   . TRP A 1 623 ? 132.208 120.808 84.226  1.00 37.86 ?  623 TRP A CD1   1 
ATOM   4997  C  CD2   . TRP A 1 623 ? 130.180 121.341 85.007  1.00 39.38 ?  623 TRP A CD2   1 
ATOM   4998  N  NE1   . TRP A 1 623 ? 131.957 120.013 85.316  1.00 37.74 ?  623 TRP A NE1   1 
ATOM   4999  C  CE2   . TRP A 1 623 ? 130.717 120.319 85.812  1.00 37.65 ?  623 TRP A CE2   1 
ATOM   5000  C  CE3   . TRP A 1 623 ? 128.909 121.839 85.307  1.00 38.03 ?  623 TRP A CE3   1 
ATOM   5001  C  CZ2   . TRP A 1 623 ? 130.030 119.788 86.902  1.00 38.90 ?  623 TRP A CZ2   1 
ATOM   5002  C  CZ3   . TRP A 1 623 ? 128.228 121.310 86.387  1.00 39.91 ?  623 TRP A CZ3   1 
ATOM   5003  C  CH2   . TRP A 1 623 ? 128.789 120.296 87.171  1.00 39.28 ?  623 TRP A CH2   1 
ATOM   5004  N  N     . PHE A 1 624 ? 134.030 123.713 82.744  1.00 43.25 ?  624 PHE A N     1 
ATOM   5005  C  CA    . PHE A 1 624 ? 135.434 123.545 83.097  1.00 43.02 ?  624 PHE A CA    1 
ATOM   5006  C  C     . PHE A 1 624 ? 136.037 124.826 83.657  1.00 41.73 ?  624 PHE A C     1 
ATOM   5007  O  O     . PHE A 1 624 ? 136.879 124.764 84.560  1.00 45.72 ?  624 PHE A O     1 
ATOM   5008  C  CB    . PHE A 1 624 ? 136.217 123.043 81.877  1.00 41.79 ?  624 PHE A CB    1 
ATOM   5009  C  CG    . PHE A 1 624 ? 137.650 123.509 81.823  1.00 45.02 ?  624 PHE A CG    1 
ATOM   5010  C  CD1   . PHE A 1 624 ? 137.987 124.722 81.238  1.00 42.97 ?  624 PHE A CD1   1 
ATOM   5011  C  CD2   . PHE A 1 624 ? 138.660 122.729 82.359  1.00 44.13 ?  624 PHE A CD2   1 
ATOM   5012  C  CE1   . PHE A 1 624 ? 139.302 125.144 81.190  1.00 43.88 ?  624 PHE A CE1   1 
ATOM   5013  C  CE2   . PHE A 1 624 ? 139.977 123.146 82.313  1.00 43.74 ?  624 PHE A CE2   1 
ATOM   5014  C  CZ    . PHE A 1 624 ? 140.297 124.355 81.729  1.00 44.28 ?  624 PHE A CZ    1 
ATOM   5015  N  N     . PHE A 1 625 ? 135.626 125.987 83.142  1.00 35.51 ?  625 PHE A N     1 
ATOM   5016  C  CA    . PHE A 1 625 ? 136.149 127.249 83.652  1.00 34.02 ?  625 PHE A CA    1 
ATOM   5017  C  C     . PHE A 1 625 ? 135.605 127.583 85.034  1.00 33.14 ?  625 PHE A C     1 
ATOM   5018  O  O     . PHE A 1 625 ? 136.221 128.378 85.751  1.00 35.40 ?  625 PHE A O     1 
ATOM   5019  C  CB    . PHE A 1 625 ? 135.836 128.385 82.678  1.00 32.94 ?  625 PHE A CB    1 
ATOM   5020  C  CG    . PHE A 1 625 ? 136.638 128.332 81.412  1.00 34.92 ?  625 PHE A CG    1 
ATOM   5021  C  CD1   . PHE A 1 625 ? 137.984 128.661 81.415  1.00 33.87 ?  625 PHE A CD1   1 
ATOM   5022  C  CD2   . PHE A 1 625 ? 136.050 127.951 80.219  1.00 34.90 ?  625 PHE A CD2   1 
ATOM   5023  C  CE1   . PHE A 1 625 ? 138.726 128.612 80.250  1.00 35.98 ?  625 PHE A CE1   1 
ATOM   5024  C  CE2   . PHE A 1 625 ? 136.786 127.901 79.051  1.00 36.21 ?  625 PHE A CE2   1 
ATOM   5025  C  CZ    . PHE A 1 625 ? 138.126 128.231 79.067  1.00 38.49 ?  625 PHE A CZ    1 
ATOM   5026  N  N     . TYR A 1 626 ? 134.473 126.997 85.424  1.00 29.63 ?  626 TYR A N     1 
ATOM   5027  C  CA    . TYR A 1 626 ? 133.956 127.187 86.772  1.00 32.34 ?  626 TYR A CA    1 
ATOM   5028  C  C     . TYR A 1 626 ? 134.591 126.184 87.724  1.00 31.25 ?  626 TYR A C     1 
ATOM   5029  O  O     . TYR A 1 626 ? 133.889 125.460 88.435  1.00 34.79 ?  626 TYR A O     1 
ATOM   5030  C  CB    . TYR A 1 626 ? 132.433 127.054 86.796  1.00 32.25 ?  626 TYR A CB    1 
ATOM   5031  C  CG    . TYR A 1 626 ? 131.715 128.378 86.713  1.00 31.54 ?  626 TYR A CG    1 
ATOM   5032  C  CD1   . TYR A 1 626 ? 131.733 129.265 87.780  1.00 34.40 ?  626 TYR A CD1   1 
ATOM   5033  C  CD2   . TYR A 1 626 ? 131.017 128.741 85.570  1.00 30.33 ?  626 TYR A CD2   1 
ATOM   5034  C  CE1   . TYR A 1 626 ? 131.082 130.477 87.710  1.00 34.43 ?  626 TYR A CE1   1 
ATOM   5035  C  CE2   . TYR A 1 626 ? 130.360 129.951 85.491  1.00 32.29 ?  626 TYR A CE2   1 
ATOM   5036  C  CZ    . TYR A 1 626 ? 130.397 130.815 86.565  1.00 33.86 ?  626 TYR A CZ    1 
ATOM   5037  O  OH    . TYR A 1 626 ? 129.748 132.023 86.495  1.00 36.02 ?  626 TYR A OH    1 
ATOM   5038  N  N     . LYS A 1 627 ? 135.921 126.143 87.744  1.00 31.15 ?  627 LYS A N     1 
ATOM   5039  C  CA    . LYS A 1 627 ? 136.635 125.209 88.601  1.00 30.24 ?  627 LYS A CA    1 
ATOM   5040  C  C     . LYS A 1 627 ? 136.336 125.493 90.066  1.00 34.65 ?  627 LYS A C     1 
ATOM   5041  O  O     . LYS A 1 627 ? 136.250 126.649 90.487  1.00 40.73 ?  627 LYS A O     1 
ATOM   5042  C  CB    . LYS A 1 627 ? 138.136 125.306 88.334  1.00 35.22 ?  627 LYS A CB    1 
ATOM   5043  C  CG    . LYS A 1 627 ? 138.976 124.252 89.027  1.00 34.08 ?  627 LYS A CG    1 
ATOM   5044  C  CD    . LYS A 1 627 ? 140.406 124.298 88.520  1.00 31.12 ?  627 LYS A CD    1 
ATOM   5045  C  CE    . LYS A 1 627 ? 141.305 123.367 89.310  1.00 36.23 ?  627 LYS A CE    1 
ATOM   5046  N  NZ    . LYS A 1 627 ? 142.737 123.558 88.955  1.00 36.73 1  627 LYS A NZ    1 
ATOM   5047  N  N     . GLU A 1 628 ? 136.159 124.430 90.843  1.00 38.83 ?  628 GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 628 ? 135.891 124.593 92.263  1.00 36.13 ?  628 GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 628 ? 137.145 125.056 92.994  1.00 38.43 ?  628 GLU A C     1 
ATOM   5050  O  O     . GLU A 1 628 ? 138.273 124.759 92.592  1.00 40.81 ?  628 GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 628 ? 135.372 123.288 92.863  1.00 37.33 ?  628 GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 628 ? 133.929 122.982 92.495  1.00 39.57 ?  628 GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 628 ? 133.494 121.601 92.933  1.00 43.19 ?  628 GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 628 ? 134.237 120.956 93.701  1.00 45.12 ?  628 GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 628 ? 132.406 121.159 92.508  1.00 39.83 -1 628 GLU A OE2   1 
ATOM   5056  N  N     . ALA A 1 629 ? 136.932 125.802 94.081  1.00 39.43 ?  629 ALA A N     1 
ATOM   5057  C  CA    . ALA A 1 629 ? 138.049 126.403 94.805  1.00 33.25 ?  629 ALA A CA    1 
ATOM   5058  C  C     . ALA A 1 629 ? 138.961 125.344 95.410  1.00 35.69 ?  629 ALA A C     1 
ATOM   5059  O  O     . ALA A 1 629 ? 140.185 125.514 95.441  1.00 42.03 ?  629 ALA A O     1 
ATOM   5060  C  CB    . ALA A 1 629 ? 137.523 127.340 95.890  1.00 30.29 ?  629 ALA A CB    1 
ATOM   5061  N  N     . TYR A 1 630 ? 138.383 124.249 95.907  1.00 40.56 ?  630 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 630 ? 139.191 123.214 96.543  1.00 36.66 ?  630 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 630 ? 140.109 122.519 95.546  1.00 41.15 ?  630 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 630 ? 141.227 122.133 95.903  1.00 44.81 ?  630 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 630 ? 138.287 122.197 97.235  1.00 35.20 ?  630 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 630 ? 137.368 122.809 98.266  1.00 36.69 ?  630 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 630 ? 137.832 123.127 99.535  1.00 34.53 ?  630 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 630 ? 136.039 123.074 97.969  1.00 37.62 ?  630 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 630 ? 136.997 123.687 100.479 1.00 37.48 ?  630 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 630 ? 135.197 123.634 98.908  1.00 38.03 ?  630 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 630 ? 135.681 123.939 100.161 1.00 44.44 ?  630 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 630 ? 134.844 124.497 101.099 1.00 44.97 ?  630 TYR A OH    1 
ATOM   5073  N  N     . ASP A 1 631 ? 139.664 122.353 94.302  1.00 38.93 ?  631 ASP A N     1 
ATOM   5074  C  CA    . ASP A 1 631 ? 140.493 121.746 93.271  1.00 38.97 ?  631 ASP A CA    1 
ATOM   5075  C  C     . ASP A 1 631 ? 141.607 122.664 92.788  1.00 41.98 ?  631 ASP A C     1 
ATOM   5076  O  O     . ASP A 1 631 ? 142.516 122.196 92.095  1.00 43.81 ?  631 ASP A O     1 
ATOM   5077  C  CB    . ASP A 1 631 ? 139.628 121.328 92.079  1.00 39.94 ?  631 ASP A CB    1 
ATOM   5078  C  CG    . ASP A 1 631 ? 138.502 120.396 92.476  1.00 45.71 ?  631 ASP A CG    1 
ATOM   5079  O  OD1   . ASP A 1 631 ? 138.694 119.592 93.412  1.00 46.44 ?  631 ASP A OD1   1 
ATOM   5080  O  OD2   . ASP A 1 631 ? 137.421 120.468 91.852  1.00 43.66 -1 631 ASP A OD2   1 
ATOM   5081  N  N     . MET A 1 632 ? 141.562 123.946 93.138  1.00 35.51 ?  632 MET A N     1 
ATOM   5082  C  CA    . MET A 1 632 ? 142.530 124.908 92.641  1.00 32.76 ?  632 MET A CA    1 
ATOM   5083  C  C     . MET A 1 632 ? 143.819 124.865 93.456  1.00 37.18 ?  632 MET A C     1 
ATOM   5084  O  O     . MET A 1 632 ? 143.844 124.437 94.613  1.00 35.27 ?  632 MET A O     1 
ATOM   5085  C  CB    . MET A 1 632 ? 141.951 126.321 92.676  1.00 31.39 ?  632 MET A CB    1 
ATOM   5086  C  CG    . MET A 1 632 ? 140.882 126.580 91.639  1.00 35.86 ?  632 MET A CG    1 
ATOM   5087  S  SD    . MET A 1 632 ? 140.325 128.290 91.652  1.00 39.76 ?  632 MET A SD    1 
ATOM   5088  C  CE    . MET A 1 632 ? 139.006 128.209 90.450  1.00 33.94 ?  632 MET A CE    1 
ATOM   5089  N  N     . ASP A 1 633 ? 144.898 125.322 92.829  1.00 33.46 ?  633 ASP A N     1 
ATOM   5090  C  CA    . ASP A 1 633 ? 146.168 125.503 93.519  1.00 31.47 ?  633 ASP A CA    1 
ATOM   5091  C  C     . ASP A 1 633 ? 146.086 126.759 94.375  1.00 31.69 ?  633 ASP A C     1 
ATOM   5092  O  O     . ASP A 1 633 ? 145.857 127.856 93.854  1.00 35.01 ?  633 ASP A O     1 
ATOM   5093  C  CB    . ASP A 1 633 ? 147.312 125.604 92.513  1.00 29.78 ?  633 ASP A CB    1 
ATOM   5094  C  CG    . ASP A 1 633 ? 148.677 125.568 93.172  1.00 36.13 ?  633 ASP A CG    1 
ATOM   5095  O  OD1   . ASP A 1 633 ? 148.747 125.343 94.398  1.00 38.03 ?  633 ASP A OD1   1 
ATOM   5096  O  OD2   . ASP A 1 633 ? 149.683 125.770 92.460  1.00 37.92 -1 633 ASP A OD2   1 
ATOM   5097  N  N     . MET A 1 634 ? 146.268 126.602 95.688  1.00 27.77 ?  634 MET A N     1 
ATOM   5098  C  CA    . MET A 1 634 ? 146.148 127.740 96.590  1.00 25.57 ?  634 MET A CA    1 
ATOM   5099  C  C     . MET A 1 634 ? 147.237 128.780 96.368  1.00 27.47 ?  634 MET A C     1 
ATOM   5100  O  O     . MET A 1 634 ? 147.038 129.945 96.722  1.00 26.26 ?  634 MET A O     1 
ATOM   5101  C  CB    . MET A 1 634 ? 146.164 127.267 98.042  1.00 27.41 ?  634 MET A CB    1 
ATOM   5102  C  CG    . MET A 1 634 ? 144.797 126.872 98.569  1.00 28.92 ?  634 MET A CG    1 
ATOM   5103  S  SD    . MET A 1 634 ? 143.593 128.204 98.409  1.00 43.53 ?  634 MET A SD    1 
ATOM   5104  C  CE    . MET A 1 634 ? 142.444 127.484 97.240  1.00 28.34 ?  634 MET A CE    1 
ATOM   5105  N  N     . PHE A 1 635 ? 148.375 128.393 95.789  1.00 26.68 ?  635 PHE A N     1 
ATOM   5106  C  CA    . PHE A 1 635 ? 149.408 129.374 95.479  1.00 23.26 ?  635 PHE A CA    1 
ATOM   5107  C  C     . PHE A 1 635 ? 148.939 130.347 94.403  1.00 21.66 ?  635 PHE A C     1 
ATOM   5108  O  O     . PHE A 1 635 ? 149.203 131.551 94.489  1.00 25.79 ?  635 PHE A O     1 
ATOM   5109  C  CB    . PHE A 1 635 ? 150.693 128.668 95.048  1.00 23.22 ?  635 PHE A CB    1 
ATOM   5110  C  CG    . PHE A 1 635 ? 151.585 128.282 96.193  1.00 24.30 ?  635 PHE A CG    1 
ATOM   5111  C  CD1   . PHE A 1 635 ? 151.061 127.688 97.328  1.00 23.65 ?  635 PHE A CD1   1 
ATOM   5112  C  CD2   . PHE A 1 635 ? 152.947 128.516 96.135  1.00 27.13 ?  635 PHE A CD2   1 
ATOM   5113  C  CE1   . PHE A 1 635 ? 151.878 127.332 98.382  1.00 22.91 ?  635 PHE A CE1   1 
ATOM   5114  C  CE2   . PHE A 1 635 ? 153.770 128.164 97.186  1.00 29.75 ?  635 PHE A CE2   1 
ATOM   5115  C  CZ    . PHE A 1 635 ? 153.234 127.570 98.311  1.00 26.44 ?  635 PHE A CZ    1 
ATOM   5116  N  N     . LYS A 1 636 ? 148.226 129.849 93.392  1.00 23.36 ?  636 LYS A N     1 
ATOM   5117  C  CA    . LYS A 1 636 ? 147.723 130.735 92.347  1.00 26.62 ?  636 LYS A CA    1 
ATOM   5118  C  C     . LYS A 1 636 ? 146.564 131.591 92.846  1.00 27.24 ?  636 LYS A C     1 
ATOM   5119  O  O     . LYS A 1 636 ? 146.416 132.744 92.421  1.00 32.63 ?  636 LYS A O     1 
ATOM   5120  C  CB    . LYS A 1 636 ? 147.316 129.913 91.126  1.00 28.33 ?  636 LYS A CB    1 
ATOM   5121  C  CG    . LYS A 1 636 ? 148.501 129.264 90.427  1.00 28.04 ?  636 LYS A CG    1 
ATOM   5122  C  CD    . LYS A 1 636 ? 148.073 128.442 89.229  1.00 33.47 ?  636 LYS A CD    1 
ATOM   5123  C  CE    . LYS A 1 636 ? 149.219 127.597 88.699  1.00 32.60 ?  636 LYS A CE    1 
ATOM   5124  N  NZ    . LYS A 1 636 ? 148.752 126.605 87.691  1.00 33.68 1  636 LYS A NZ    1 
ATOM   5125  N  N     . VAL A 1 637 ? 145.746 131.058 93.755  1.00 23.94 ?  637 VAL A N     1 
ATOM   5126  C  CA    . VAL A 1 637 ? 144.724 131.877 94.402  1.00 16.29 ?  637 VAL A CA    1 
ATOM   5127  C  C     . VAL A 1 637 ? 145.378 132.985 95.219  1.00 23.84 ?  637 VAL A C     1 
ATOM   5128  O  O     . VAL A 1 637 ? 144.915 134.132 95.219  1.00 27.23 ?  637 VAL A O     1 
ATOM   5129  C  CB    . VAL A 1 637 ? 143.802 130.999 95.266  1.00 20.35 ?  637 VAL A CB    1 
ATOM   5130  C  CG1   . VAL A 1 637 ? 142.653 131.823 95.824  1.00 21.92 ?  637 VAL A CG1   1 
ATOM   5131  C  CG2   . VAL A 1 637 ? 143.275 129.829 94.455  1.00 25.87 ?  637 VAL A CG2   1 
ATOM   5132  N  N     . VAL A 1 638 ? 146.464 132.660 95.924  1.00 25.45 ?  638 VAL A N     1 
ATOM   5133  C  CA    . VAL A 1 638 ? 147.220 133.674 96.656  1.00 21.79 ?  638 VAL A CA    1 
ATOM   5134  C  C     . VAL A 1 638 ? 147.771 134.719 95.698  1.00 17.02 ?  638 VAL A C     1 
ATOM   5135  O  O     . VAL A 1 638 ? 147.763 135.919 95.993  1.00 25.22 ?  638 VAL A O     1 
ATOM   5136  C  CB    . VAL A 1 638 ? 148.343 133.016 97.481  1.00 20.12 ?  638 VAL A CB    1 
ATOM   5137  C  CG1   . VAL A 1 638 ? 149.387 134.045 97.879  1.00 15.90 ?  638 VAL A CG1   1 
ATOM   5138  C  CG2   . VAL A 1 638 ? 147.778 132.335 98.711  1.00 18.74 ?  638 VAL A CG2   1 
ATOM   5139  N  N     . ASP A 1 639 ? 148.271 134.280 94.542  1.00 20.16 ?  639 ASP A N     1 
ATOM   5140  C  CA    . ASP A 1 639 ? 148.802 135.218 93.556  1.00 17.42 ?  639 ASP A CA    1 
ATOM   5141  C  C     . ASP A 1 639 ? 147.722 136.174 93.064  1.00 23.65 ?  639 ASP A C     1 
ATOM   5142  O  O     . ASP A 1 639 ? 147.954 137.383 92.956  1.00 34.49 ?  639 ASP A O     1 
ATOM   5143  C  CB    . ASP A 1 639 ? 149.413 134.453 92.384  1.00 22.23 ?  639 ASP A CB    1 
ATOM   5144  C  CG    . ASP A 1 639 ? 150.779 133.885 92.706  1.00 30.93 ?  639 ASP A CG    1 
ATOM   5145  O  OD1   . ASP A 1 639 ? 151.547 134.556 93.425  1.00 31.40 ?  639 ASP A OD1   1 
ATOM   5146  O  OD2   . ASP A 1 639 ? 151.083 132.768 92.242  1.00 30.53 -1 639 ASP A OD2   1 
ATOM   5147  N  N     . MET A 1 640 ? 146.531 135.648 92.768  1.00 23.94 ?  640 MET A N     1 
ATOM   5148  C  CA    . MET A 1 640 ? 145.433 136.508 92.338  1.00 17.59 ?  640 MET A CA    1 
ATOM   5149  C  C     . MET A 1 640 ? 145.017 137.475 93.440  1.00 19.97 ?  640 MET A C     1 
ATOM   5150  O  O     . MET A 1 640 ? 144.765 138.661 93.181  1.00 30.73 ?  640 MET A O     1 
ATOM   5151  C  CB    . MET A 1 640 ? 144.240 135.662 91.895  1.00 23.08 ?  640 MET A CB    1 
ATOM   5152  C  CG    . MET A 1 640 ? 142.900 136.358 92.070  1.00 26.44 ?  640 MET A CG    1 
ATOM   5153  S  SD    . MET A 1 640 ? 142.317 137.162 90.568  1.00 31.92 ?  640 MET A SD    1 
ATOM   5154  C  CE    . MET A 1 640 ? 142.218 135.770 89.456  1.00 23.12 ?  640 MET A CE    1 
ATOM   5155  N  N     . ILE A 1 641 ? 144.933 136.988 94.680  1.00 15.77 ?  641 ILE A N     1 
ATOM   5156  C  CA    . ILE A 1 641 ? 144.509 137.855 95.771  1.00 18.94 ?  641 ILE A CA    1 
ATOM   5157  C  C     . ILE A 1 641 ? 145.548 138.936 96.033  1.00 19.32 ?  641 ILE A C     1 
ATOM   5158  O  O     . ILE A 1 641 ? 145.194 140.071 96.354  1.00 24.40 ?  641 ILE A O     1 
ATOM   5159  C  CB    . ILE A 1 641 ? 144.200 137.024 97.030  1.00 20.90 ?  641 ILE A CB    1 
ATOM   5160  C  CG1   . ILE A 1 641 ? 143.013 136.099 96.763  1.00 17.33 ?  641 ILE A CG1   1 
ATOM   5161  C  CG2   . ILE A 1 641 ? 143.871 137.926 98.207  1.00 16.43 ?  641 ILE A CG2   1 
ATOM   5162  C  CD1   . ILE A 1 641 ? 141.910 136.745 95.951  1.00 20.72 ?  641 ILE A CD1   1 
ATOM   5163  N  N     . ALA A 1 642 ? 146.836 138.621 95.880  1.00 15.52 ?  642 ALA A N     1 
ATOM   5164  C  CA    . ALA A 1 642 ? 147.874 139.640 96.019  1.00 16.76 ?  642 ALA A CA    1 
ATOM   5165  C  C     . ALA A 1 642 ? 147.815 140.648 94.879  1.00 19.56 ?  642 ALA A C     1 
ATOM   5166  O  O     . ALA A 1 642 ? 148.024 141.851 95.089  1.00 30.33 ?  642 ALA A O     1 
ATOM   5167  C  CB    . ALA A 1 642 ? 149.250 138.980 96.081  1.00 17.60 ?  642 ALA A CB    1 
ATOM   5168  N  N     . THR A 1 643 ? 147.534 140.172 93.664  1.00 16.40 ?  643 THR A N     1 
ATOM   5169  C  CA    . THR A 1 643 ? 147.370 141.072 92.530  1.00 16.82 ?  643 THR A CA    1 
ATOM   5170  C  C     . THR A 1 643 ? 146.238 142.060 92.779  1.00 20.72 ?  643 THR A C     1 
ATOM   5171  O  O     . THR A 1 643 ? 146.367 143.253 92.486  1.00 23.15 ?  643 THR A O     1 
ATOM   5172  C  CB    . THR A 1 643 ? 147.111 140.260 91.261  1.00 18.01 ?  643 THR A CB    1 
ATOM   5173  O  OG1   . THR A 1 643 ? 148.287 139.516 90.920  1.00 22.20 ?  643 THR A OG1   1 
ATOM   5174  C  CG2   . THR A 1 643 ? 146.745 141.168 90.111  1.00 14.96 ?  643 THR A CG2   1 
ATOM   5175  N  N     . ILE A 1 644 ? 145.122 141.581 93.328  1.00 17.72 ?  644 ILE A N     1 
ATOM   5176  C  CA    . ILE A 1 644 ? 144.031 142.486 93.679  1.00 11.61 ?  644 ILE A CA    1 
ATOM   5177  C  C     . ILE A 1 644 ? 144.434 143.390 94.840  1.00 15.14 ?  644 ILE A C     1 
ATOM   5178  O  O     . ILE A 1 644 ? 144.141 144.592 94.838  1.00 19.99 ?  644 ILE A O     1 
ATOM   5179  C  CB    . ILE A 1 644 ? 142.755 141.688 93.999  1.00 15.27 ?  644 ILE A CB    1 
ATOM   5180  C  CG1   . ILE A 1 644 ? 142.341 140.836 92.799  1.00 18.05 ?  644 ILE A CG1   1 
ATOM   5181  C  CG2   . ILE A 1 644 ? 141.632 142.627 94.394  1.00 9.24  ?  644 ILE A CG2   1 
ATOM   5182  C  CD1   . ILE A 1 644 ? 141.318 139.777 93.135  1.00 21.85 ?  644 ILE A CD1   1 
ATOM   5183  N  N     . GLN A 1 645 ? 145.119 142.831 95.841  1.00 13.04 ?  645 GLN A N     1 
ATOM   5184  C  CA    . GLN A 1 645 ? 145.451 143.565 97.057  1.00 14.10 ?  645 GLN A CA    1 
ATOM   5185  C  C     . GLN A 1 645 ? 146.396 144.722 96.784  1.00 15.57 ?  645 GLN A C     1 
ATOM   5186  O  O     . GLN A 1 645 ? 146.386 145.715 97.521  1.00 19.84 ?  645 GLN A O     1 
ATOM   5187  C  CB    . GLN A 1 645 ? 146.066 142.612 98.081  1.00 12.50 ?  645 GLN A CB    1 
ATOM   5188  C  CG    . GLN A 1 645 ? 146.331 143.231 99.439  1.00 8.73  ?  645 GLN A CG    1 
ATOM   5189  C  CD    . GLN A 1 645 ? 145.058 143.504 100.206 1.00 11.82 ?  645 GLN A CD    1 
ATOM   5190  O  OE1   . GLN A 1 645 ? 144.542 142.632 100.903 1.00 17.05 ?  645 GLN A OE1   1 
ATOM   5191  N  NE2   . GLN A 1 645 ? 144.541 144.720 100.082 1.00 6.56  ?  645 GLN A NE2   1 
ATOM   5192  N  N     . GLN A 1 646 ? 147.214 144.618 95.740  1.00 20.80 ?  646 GLN A N     1 
ATOM   5193  C  CA    . GLN A 1 646 ? 148.096 145.731 95.419  1.00 14.50 ?  646 GLN A CA    1 
ATOM   5194  C  C     . GLN A 1 646 ? 147.329 146.982 95.002  1.00 13.51 ?  646 GLN A C     1 
ATOM   5195  O  O     . GLN A 1 646 ? 147.920 148.065 94.968  1.00 17.75 ?  646 GLN A O     1 
ATOM   5196  C  CB    . GLN A 1 646 ? 149.085 145.325 94.326  1.00 17.94 ?  646 GLN A CB    1 
ATOM   5197  C  CG    . GLN A 1 646 ? 148.558 145.458 92.917  1.00 21.82 ?  646 GLN A CG    1 
ATOM   5198  C  CD    . GLN A 1 646 ? 149.482 144.831 91.894  1.00 26.95 ?  646 GLN A CD    1 
ATOM   5199  O  OE1   . GLN A 1 646 ? 150.608 145.285 91.700  1.00 25.36 ?  646 GLN A OE1   1 
ATOM   5200  N  NE2   . GLN A 1 646 ? 149.011 143.780 91.236  1.00 22.86 ?  646 GLN A NE2   1 
ATOM   5201  N  N     . HIS A 1 647 ? 146.034 146.866 94.703  1.00 21.28 ?  647 HIS A N     1 
ATOM   5202  C  CA    . HIS A 1 647 ? 145.203 148.012 94.353  1.00 14.87 ?  647 HIS A CA    1 
ATOM   5203  C  C     . HIS A 1 647 ? 144.121 148.295 95.387  1.00 11.61 ?  647 HIS A C     1 
ATOM   5204  O  O     . HIS A 1 647 ? 143.286 149.178 95.167  1.00 19.13 ?  647 HIS A O     1 
ATOM   5205  C  CB    . HIS A 1 647 ? 144.563 147.803 92.979  1.00 10.26 ?  647 HIS A CB    1 
ATOM   5206  C  CG    . HIS A 1 647 ? 145.551 147.504 91.898  1.00 15.52 ?  647 HIS A CG    1 
ATOM   5207  N  ND1   . HIS A 1 647 ? 146.517 148.406 91.506  1.00 16.09 ?  647 HIS A ND1   1 
ATOM   5208  C  CD2   . HIS A 1 647 ? 145.729 146.404 91.131  1.00 13.32 ?  647 HIS A CD2   1 
ATOM   5209  C  CE1   . HIS A 1 647 ? 147.246 147.874 90.542  1.00 18.02 ?  647 HIS A CE1   1 
ATOM   5210  N  NE2   . HIS A 1 647 ? 146.788 146.660 90.296  1.00 19.55 ?  647 HIS A NE2   1 
ATOM   5211  N  N     . ILE A 1 648 ? 144.111 147.574 96.504  1.00 11.14 ?  648 ILE A N     1 
ATOM   5212  C  CA    . ILE A 1 648 ? 143.129 147.760 97.566  1.00 13.31 ?  648 ILE A CA    1 
ATOM   5213  C  C     . ILE A 1 648 ? 143.855 148.308 98.786  1.00 13.02 ?  648 ILE A C     1 
ATOM   5214  O  O     . ILE A 1 648 ? 144.831 147.711 99.254  1.00 23.58 ?  648 ILE A O     1 
ATOM   5215  C  CB    . ILE A 1 648 ? 142.401 146.445 97.896  1.00 11.46 ?  648 ILE A CB    1 
ATOM   5216  C  CG1   . ILE A 1 648 ? 141.774 145.842 96.636  1.00 7.66  ?  648 ILE A CG1   1 
ATOM   5217  C  CG2   . ILE A 1 648 ? 141.339 146.673 98.955  1.00 9.21  ?  648 ILE A CG2   1 
ATOM   5218  C  CD1   . ILE A 1 648 ? 140.611 146.635 96.084  1.00 9.58  ?  648 ILE A CD1   1 
ATOM   5219  N  N     . ASP A 1 649 ? 143.386 149.451 99.293  1.00 6.66  ?  649 ASP A N     1 
ATOM   5220  C  CA    . ASP A 1 649 ? 144.054 150.075 100.432 1.00 11.95 ?  649 ASP A CA    1 
ATOM   5221  C  C     . ASP A 1 649 ? 143.829 149.279 101.711 1.00 9.56  ?  649 ASP A C     1 
ATOM   5222  O  O     . ASP A 1 649 ? 144.736 149.160 102.542 1.00 28.87 ?  649 ASP A O     1 
ATOM   5223  C  CB    . ASP A 1 649 ? 143.575 151.517 100.601 1.00 21.67 ?  649 ASP A CB    1 
ATOM   5224  C  CG    . ASP A 1 649 ? 142.085 151.662 100.398 1.00 18.65 ?  649 ASP A CG    1 
ATOM   5225  O  OD1   . ASP A 1 649 ? 141.517 150.891 99.602  1.00 24.11 ?  649 ASP A OD1   1 
ATOM   5226  O  OD2   . ASP A 1 649 ? 141.481 152.549 101.033 1.00 15.97 -1 649 ASP A OD2   1 
ATOM   5227  N  N     . GLN A 1 650 ? 142.633 148.734 101.891 1.00 10.05 ?  650 GLN A N     1 
ATOM   5228  C  CA    . GLN A 1 650 ? 142.347 147.849 103.009 1.00 6.55  ?  650 GLN A CA    1 
ATOM   5229  C  C     . GLN A 1 650 ? 142.605 146.407 102.570 1.00 5.55  ?  650 GLN A C     1 
ATOM   5230  O  O     . GLN A 1 650 ? 143.227 146.164 101.532 1.00 16.73 ?  650 GLN A O     1 
ATOM   5231  C  CB    . GLN A 1 650 ? 140.919 148.081 103.510 1.00 3.48  ?  650 GLN A CB    1 
ATOM   5232  C  CG    . GLN A 1 650 ? 140.653 149.497 103.984 1.00 4.86  ?  650 GLN A CG    1 
ATOM   5233  C  CD    . GLN A 1 650 ? 139.225 149.695 104.436 1.00 10.24 ?  650 GLN A CD    1 
ATOM   5234  O  OE1   . GLN A 1 650 ? 138.825 149.209 105.492 1.00 21.25 ?  650 GLN A OE1   1 
ATOM   5235  N  NE2   . GLN A 1 650 ? 138.446 150.413 103.638 1.00 5.10  ?  650 GLN A NE2   1 
ATOM   5236  N  N     . GLY A 1 651 ? 142.147 145.435 103.355 1.00 6.66  ?  651 GLY A N     1 
ATOM   5237  C  CA    . GLY A 1 651 ? 142.387 144.042 103.053 1.00 8.64  ?  651 GLY A CA    1 
ATOM   5238  C  C     . GLY A 1 651 ? 141.281 143.408 102.232 1.00 6.35  ?  651 GLY A C     1 
ATOM   5239  O  O     . GLY A 1 651 ? 140.277 144.027 101.883 1.00 9.60  ?  651 GLY A O     1 
ATOM   5240  N  N     . ILE A 1 652 ? 141.490 142.133 101.923 1.00 18.34 ?  652 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 652 ? 140.540 141.312 101.187 1.00 8.90  ?  652 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 652 ? 140.222 140.096 102.039 1.00 7.64  ?  652 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 652 ? 141.135 139.450 102.568 1.00 19.66 ?  652 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 652 ? 141.099 140.881 99.819  1.00 6.86  ?  652 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 652 ? 141.497 142.100 98.989  1.00 0.00  ?  652 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 652 ? 140.093 140.023 99.074  1.00 10.78 ?  652 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 652 ? 142.377 141.759 97.817  1.00 4.02  ?  652 ILE A CD1   1 
ATOM   5248  N  N     . SER A 1 653 ? 138.938 139.786 102.181 1.00 15.16 ?  653 SER A N     1 
ATOM   5249  C  CA    . SER A 1 653 ? 138.534 138.573 102.885 1.00 12.99 ?  653 SER A CA    1 
ATOM   5250  C  C     . SER A 1 653 ? 138.994 137.379 102.061 1.00 13.55 ?  653 SER A C     1 
ATOM   5251  O  O     . SER A 1 653 ? 138.386 137.034 101.046 1.00 26.18 ?  653 SER A O     1 
ATOM   5252  C  CB    . SER A 1 653 ? 137.029 138.552 103.109 1.00 12.53 ?  653 SER A CB    1 
ATOM   5253  O  OG    . SER A 1 653 ? 136.714 138.864 104.453 1.00 15.77 ?  653 SER A OG    1 
ATOM   5254  N  N     . PHE A 1 654 ? 140.074 136.746 102.499 1.00 18.67 ?  654 PHE A N     1 
ATOM   5255  C  CA    . PHE A 1 654 ? 140.756 135.702 101.740 1.00 9.68  ?  654 PHE A CA    1 
ATOM   5256  C  C     . PHE A 1 654 ? 140.609 134.390 102.501 1.00 15.65 ?  654 PHE A C     1 
ATOM   5257  O  O     . PHE A 1 654 ? 141.314 134.147 103.484 1.00 24.30 ?  654 PHE A O     1 
ATOM   5258  C  CB    . PHE A 1 654 ? 142.221 136.071 101.527 1.00 9.20  ?  654 PHE A CB    1 
ATOM   5259  C  CG    . PHE A 1 654 ? 142.987 135.094 100.681 1.00 16.73 ?  654 PHE A CG    1 
ATOM   5260  C  CD1   . PHE A 1 654 ? 142.333 134.204 99.845  1.00 22.93 ?  654 PHE A CD1   1 
ATOM   5261  C  CD2   . PHE A 1 654 ? 144.369 135.069 100.722 1.00 18.70 ?  654 PHE A CD2   1 
ATOM   5262  C  CE1   . PHE A 1 654 ? 143.041 133.309 99.073  1.00 14.90 ?  654 PHE A CE1   1 
ATOM   5263  C  CE2   . PHE A 1 654 ? 145.081 134.178 99.951  1.00 20.49 ?  654 PHE A CE2   1 
ATOM   5264  C  CZ    . PHE A 1 654 ? 144.416 133.296 99.126  1.00 15.99 ?  654 PHE A CZ    1 
ATOM   5265  N  N     . THR A 1 655 ? 139.698 133.544 102.034 1.00 20.69 ?  655 THR A N     1 
ATOM   5266  C  CA    . THR A 1 655 ? 139.490 132.227 102.615 1.00 16.46 ?  655 THR A CA    1 
ATOM   5267  C  C     . THR A 1 655 ? 140.342 131.203 101.877 1.00 23.11 ?  655 THR A C     1 
ATOM   5268  O  O     . THR A 1 655 ? 140.331 131.152 100.644 1.00 28.79 ?  655 THR A O     1 
ATOM   5269  C  CB    . THR A 1 655 ? 138.012 131.837 102.546 1.00 23.48 ?  655 THR A CB    1 
ATOM   5270  O  OG1   . THR A 1 655 ? 137.264 132.613 103.490 1.00 23.66 ?  655 THR A OG1   1 
ATOM   5271  C  CG2   . THR A 1 655 ? 137.828 130.359 102.853 1.00 24.36 ?  655 THR A CG2   1 
ATOM   5272  N  N     . LEU A 1 656 ? 141.091 130.406 102.633 1.00 31.95 ?  656 LEU A N     1 
ATOM   5273  C  CA    . LEU A 1 656 ? 141.817 129.286 102.055 1.00 28.61 ?  656 LEU A CA    1 
ATOM   5274  C  C     . LEU A 1 656 ? 140.872 128.112 101.855 1.00 27.54 ?  656 LEU A C     1 
ATOM   5275  O  O     . LEU A 1 656 ? 140.010 127.844 102.694 1.00 31.16 ?  656 LEU A O     1 
ATOM   5276  C  CB    . LEU A 1 656 ? 142.980 128.871 102.956 1.00 29.59 ?  656 LEU A CB    1 
ATOM   5277  C  CG    . LEU A 1 656 ? 144.071 129.915 103.181 1.00 30.46 ?  656 LEU A CG    1 
ATOM   5278  C  CD1   . LEU A 1 656 ? 145.264 129.297 103.891 1.00 26.80 ?  656 LEU A CD1   1 
ATOM   5279  C  CD2   . LEU A 1 656 ? 144.485 130.556 101.867 1.00 27.73 ?  656 LEU A CD2   1 
ATOM   5280  N  N     . PHE A 1 657 ? 141.027 127.418 100.732 1.00 26.53 ?  657 PHE A N     1 
ATOM   5281  C  CA    . PHE A 1 657 ? 140.197 126.265 100.401 1.00 28.20 ?  657 PHE A CA    1 
ATOM   5282  C  C     . PHE A 1 657 ? 141.103 125.048 100.301 1.00 36.33 ?  657 PHE A C     1 
ATOM   5283  O  O     . PHE A 1 657 ? 141.859 124.909 99.333  1.00 37.74 ?  657 PHE A O     1 
ATOM   5284  C  CB    . PHE A 1 657 ? 139.428 126.500 99.104  1.00 29.41 ?  657 PHE A CB    1 
ATOM   5285  C  CG    . PHE A 1 657 ? 138.612 127.758 99.110  1.00 32.69 ?  657 PHE A CG    1 
ATOM   5286  C  CD1   . PHE A 1 657 ? 137.342 127.771 99.657  1.00 30.22 ?  657 PHE A CD1   1 
ATOM   5287  C  CD2   . PHE A 1 657 ? 139.115 128.929 98.569  1.00 33.87 ?  657 PHE A CD2   1 
ATOM   5288  C  CE1   . PHE A 1 657 ? 136.591 128.929 99.666  1.00 32.64 ?  657 PHE A CE1   1 
ATOM   5289  C  CE2   . PHE A 1 657 ? 138.366 130.087 98.570  1.00 29.81 ?  657 PHE A CE2   1 
ATOM   5290  C  CZ    . PHE A 1 657 ? 137.103 130.087 99.121  1.00 32.98 ?  657 PHE A CZ    1 
ATOM   5291  N  N     . LEU A 1 658 ? 141.026 124.170 101.294 1.00 40.31 ?  658 LEU A N     1 
ATOM   5292  C  CA    . LEU A 1 658 ? 141.940 123.050 101.421 1.00 42.67 ?  658 LEU A CA    1 
ATOM   5293  C  C     . LEU A 1 658 ? 141.201 121.732 101.244 1.00 45.45 ?  658 LEU A C     1 
ATOM   5294  O  O     . LEU A 1 658 ? 140.002 121.627 101.520 1.00 46.68 ?  658 LEU A O     1 
ATOM   5295  C  CB    . LEU A 1 658 ? 142.634 123.067 102.785 1.00 40.37 ?  658 LEU A CB    1 
ATOM   5296  C  CG    . LEU A 1 658 ? 142.940 124.450 103.361 1.00 39.41 ?  658 LEU A CG    1 
ATOM   5297  C  CD1   . LEU A 1 658 ? 143.227 124.345 104.846 1.00 41.38 ?  658 LEU A CD1   1 
ATOM   5298  C  CD2   . LEU A 1 658 ? 144.101 125.101 102.628 1.00 42.05 ?  658 LEU A CD2   1 
ATOM   5299  N  N     . LYS A 1 659 ? 141.926 120.736 100.754 1.00 51.27 ?  659 LYS A N     1 
ATOM   5300  C  CA    . LYS A 1 659 ? 141.447 119.365 100.735 1.00 51.78 ?  659 LYS A CA    1 
ATOM   5301  C  C     . LYS A 1 659 ? 141.802 118.678 102.048 1.00 52.89 ?  659 LYS A C     1 
ATOM   5302  O  O     . LYS A 1 659 ? 142.725 119.080 102.758 1.00 54.58 ?  659 LYS A O     1 
ATOM   5303  C  CB    . LYS A 1 659 ? 142.047 118.598 99.556  1.00 54.80 ?  659 LYS A CB    1 
ATOM   5304  C  CG    . LYS A 1 659 ? 141.801 119.244 98.203  1.00 53.58 ?  659 LYS A CG    1 
ATOM   5305  C  CD    . LYS A 1 659 ? 142.229 118.327 97.068  1.00 53.18 ?  659 LYS A CD    1 
ATOM   5306  C  CE    . LYS A 1 659 ? 141.959 118.962 95.713  1.00 53.02 ?  659 LYS A CE    1 
ATOM   5307  N  NZ    . LYS A 1 659 ? 142.025 117.967 94.607  1.00 52.86 1  659 LYS A NZ    1 
ATOM   5308  N  N     . ASP A 1 660 ? 141.043 117.628 102.371 1.00 57.82 ?  660 ASP A N     1 
ATOM   5309  C  CA    . ASP A 1 660 ? 141.327 116.862 103.577 1.00 57.29 ?  660 ASP A CA    1 
ATOM   5310  C  C     . ASP A 1 660 ? 142.660 116.129 103.496 1.00 55.49 ?  660 ASP A C     1 
ATOM   5311  O  O     . ASP A 1 660 ? 143.200 115.733 104.534 1.00 56.14 ?  660 ASP A O     1 
ATOM   5312  C  CB    . ASP A 1 660 ? 140.197 115.868 103.850 1.00 58.51 ?  660 ASP A CB    1 
ATOM   5313  C  CG    . ASP A 1 660 ? 139.629 115.269 102.578 1.00 61.52 ?  660 ASP A CG    1 
ATOM   5314  O  OD1   . ASP A 1 660 ? 140.420 114.827 101.719 1.00 59.08 ?  660 ASP A OD1   1 
ATOM   5315  O  OD2   . ASP A 1 660 ? 138.388 115.242 102.437 1.00 61.60 -1 660 ASP A OD2   1 
ATOM   5316  N  N     . THR A 1 661 ? 143.200 115.944 102.289 1.00 53.18 ?  661 THR A N     1 
ATOM   5317  C  CA    . THR A 1 661 ? 144.455 115.213 102.145 1.00 55.32 ?  661 THR A CA    1 
ATOM   5318  C  C     . THR A 1 661 ? 145.645 116.045 102.606 1.00 54.64 ?  661 THR A C     1 
ATOM   5319  O  O     . THR A 1 661 ? 146.565 115.518 103.243 1.00 55.17 ?  661 THR A O     1 
ATOM   5320  C  CB    . THR A 1 661 ? 144.644 114.773 100.693 1.00 56.55 ?  661 THR A CB    1 
ATOM   5321  O  OG1   . THR A 1 661 ? 145.215 115.849 99.938  1.00 56.41 ?  661 THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1 661 ? 143.311 114.379 100.079 1.00 54.38 ?  661 THR A CG2   1 
ATOM   5323  N  N     . MET A 1 662 ? 145.653 117.340 102.295 1.00 52.78 ?  662 MET A N     1 
ATOM   5324  C  CA    . MET A 1 662 ? 146.796 118.171 102.643 1.00 52.47 ?  662 MET A CA    1 
ATOM   5325  C  C     . MET A 1 662 ? 146.891 118.359 104.153 1.00 51.28 ?  662 MET A C     1 
ATOM   5326  O  O     . MET A 1 662 ? 145.887 118.389 104.870 1.00 49.11 ?  662 MET A O     1 
ATOM   5327  C  CB    . MET A 1 662 ? 146.722 119.524 101.931 1.00 50.11 ?  662 MET A CB    1 
ATOM   5328  C  CG    . MET A 1 662 ? 146.168 120.670 102.757 1.00 51.94 ?  662 MET A CG    1 
ATOM   5329  S  SD    . MET A 1 662 ? 146.052 122.180 101.781 1.00 62.99 ?  662 MET A SD    1 
ATOM   5330  C  CE    . MET A 1 662 ? 145.103 121.605 100.379 1.00 48.13 ?  662 MET A CE    1 
ATOM   5331  N  N     . THR A 1 663 ? 148.125 118.464 104.631 1.00 45.64 ?  663 THR A N     1 
ATOM   5332  C  CA    . THR A 1 663 ? 148.440 118.480 106.048 1.00 44.52 ?  663 THR A CA    1 
ATOM   5333  C  C     . THR A 1 663 ? 148.658 119.915 106.525 1.00 44.92 ?  663 THR A C     1 
ATOM   5334  O  O     . THR A 1 663 ? 148.460 120.879 105.781 1.00 46.43 ?  663 THR A O     1 
ATOM   5335  C  CB    . THR A 1 663 ? 149.664 117.604 106.307 1.00 43.39 ?  663 THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 663 ? 150.854 118.383 106.135 1.00 42.25 ?  663 THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 663 ? 149.688 116.438 105.330 1.00 44.97 ?  663 THR A CG2   1 
ATOM   5338  N  N     . THR A 1 664 ? 149.072 120.062 107.786 1.00 39.16 ?  664 THR A N     1 
ATOM   5339  C  CA    . THR A 1 664 ? 149.354 121.388 108.321 1.00 38.73 ?  664 THR A CA    1 
ATOM   5340  C  C     . THR A 1 664 ? 150.590 122.013 107.692 1.00 37.04 ?  664 THR A C     1 
ATOM   5341  O  O     . THR A 1 664 ? 150.712 123.242 107.692 1.00 40.13 ?  664 THR A O     1 
ATOM   5342  C  CB    . THR A 1 664 ? 149.523 121.333 109.841 1.00 39.50 ?  664 THR A CB    1 
ATOM   5343  O  OG1   . THR A 1 664 ? 150.784 120.734 110.165 1.00 39.06 ?  664 THR A OG1   1 
ATOM   5344  C  CG2   . THR A 1 664 ? 148.397 120.534 110.477 1.00 36.70 ?  664 THR A CG2   1 
ATOM   5345  N  N     . ARG A 1 665 ? 151.509 121.203 107.162 1.00 37.74 ?  665 ARG A N     1 
ATOM   5346  C  CA    . ARG A 1 665 ? 152.648 121.759 106.441 1.00 34.74 ?  665 ARG A CA    1 
ATOM   5347  C  C     . ARG A 1 665 ? 152.191 122.508 105.196 1.00 39.12 ?  665 ARG A C     1 
ATOM   5348  O  O     . ARG A 1 665 ? 152.709 123.585 104.887 1.00 44.89 ?  665 ARG A O     1 
ATOM   5349  C  CB    . ARG A 1 665 ? 153.634 120.655 106.067 1.00 37.03 ?  665 ARG A CB    1 
ATOM   5350  C  CG    . ARG A 1 665 ? 154.614 121.047 104.973 1.00 35.80 ?  665 ARG A CG    1 
ATOM   5351  C  CD    . ARG A 1 665 ? 156.025 120.599 105.302 1.00 37.90 ?  665 ARG A CD    1 
ATOM   5352  N  NE    . ARG A 1 665 ? 156.950 120.873 104.210 1.00 40.76 ?  665 ARG A NE    1 
ATOM   5353  C  CZ    . ARG A 1 665 ? 157.232 120.022 103.233 1.00 42.19 ?  665 ARG A CZ    1 
ATOM   5354  N  NH1   . ARG A 1 665 ? 156.673 118.825 103.178 1.00 41.36 1  665 ARG A NH1   1 
ATOM   5355  N  NH2   . ARG A 1 665 ? 158.096 120.382 102.288 1.00 41.42 ?  665 ARG A NH2   1 
ATOM   5356  N  N     . ASP A 1 666 ? 151.216 121.955 104.472 1.00 37.63 ?  666 ASP A N     1 
ATOM   5357  C  CA    . ASP A 1 666 ? 150.688 122.640 103.297 1.00 36.14 ?  666 ASP A CA    1 
ATOM   5358  C  C     . ASP A 1 666 ? 149.981 123.935 103.681 1.00 39.97 ?  666 ASP A C     1 
ATOM   5359  O  O     . ASP A 1 666 ? 150.121 124.952 102.994 1.00 44.17 ?  666 ASP A O     1 
ATOM   5360  C  CB    . ASP A 1 666 ? 149.746 121.713 102.532 1.00 42.08 ?  666 ASP A CB    1 
ATOM   5361  C  CG    . ASP A 1 666 ? 150.449 120.481 102.003 1.00 46.23 ?  666 ASP A CG    1 
ATOM   5362  O  OD1   . ASP A 1 666 ? 151.491 120.633 101.333 1.00 44.32 ?  666 ASP A OD1   1 
ATOM   5363  O  OD2   . ASP A 1 666 ? 149.962 119.359 102.260 1.00 46.85 -1 666 ASP A OD2   1 
ATOM   5364  N  N     . LEU A 1 667 ? 149.216 123.915 104.775 1.00 33.15 ?  667 LEU A N     1 
ATOM   5365  C  CA    . LEU A 1 667 ? 148.561 125.131 105.243 1.00 30.35 ?  667 LEU A CA    1 
ATOM   5366  C  C     . LEU A 1 667 ? 149.585 126.193 105.622 1.00 30.18 ?  667 LEU A C     1 
ATOM   5367  O  O     . LEU A 1 667 ? 149.432 127.370 105.274 1.00 33.76 ?  667 LEU A O     1 
ATOM   5368  C  CB    . LEU A 1 667 ? 147.659 124.810 106.436 1.00 33.25 ?  667 LEU A CB    1 
ATOM   5369  C  CG    . LEU A 1 667 ? 146.335 125.560 106.571 1.00 35.96 ?  667 LEU A CG    1 
ATOM   5370  C  CD1   . LEU A 1 667 ? 145.464 124.885 107.614 1.00 35.10 ?  667 LEU A CD1   1 
ATOM   5371  C  CD2   . LEU A 1 667 ? 146.551 127.021 106.925 1.00 33.24 ?  667 LEU A CD2   1 
ATOM   5372  N  N     . ASN A 1 668 ? 150.639 125.792 106.336 1.00 30.42 ?  668 ASN A N     1 
ATOM   5373  C  CA    . ASN A 1 668 ? 151.688 126.733 106.705 1.00 27.03 ?  668 ASN A CA    1 
ATOM   5374  C  C     . ASN A 1 668 ? 152.407 127.264 105.474 1.00 27.13 ?  668 ASN A C     1 
ATOM   5375  O  O     . ASN A 1 668 ? 152.785 128.437 105.429 1.00 33.76 ?  668 ASN A O     1 
ATOM   5376  C  CB    . ASN A 1 668 ? 152.679 126.068 107.660 1.00 28.88 ?  668 ASN A CB    1 
ATOM   5377  C  CG    . ASN A 1 668 ? 152.255 126.176 109.108 1.00 31.15 ?  668 ASN A CG    1 
ATOM   5378  O  OD1   . ASN A 1 668 ? 152.517 125.280 109.908 1.00 39.82 ?  668 ASN A OD1   1 
ATOM   5379  N  ND2   . ASN A 1 668 ? 151.595 127.274 109.452 1.00 28.99 ?  668 ASN A ND2   1 
ATOM   5380  N  N     . ARG A 1 669 ? 152.617 126.411 104.469 1.00 29.15 ?  669 ARG A N     1 
ATOM   5381  C  CA    . ARG A 1 669 ? 153.245 126.863 103.232 1.00 30.94 ?  669 ARG A CA    1 
ATOM   5382  C  C     . ARG A 1 669 ? 152.378 127.886 102.514 1.00 28.85 ?  669 ARG A C     1 
ATOM   5383  O  O     . ARG A 1 669 ? 152.891 128.878 101.986 1.00 28.98 ?  669 ARG A O     1 
ATOM   5384  C  CB    . ARG A 1 669 ? 153.532 125.673 102.320 1.00 31.95 ?  669 ARG A CB    1 
ATOM   5385  C  CG    . ARG A 1 669 ? 155.000 125.311 102.219 1.00 29.86 ?  669 ARG A CG    1 
ATOM   5386  C  CD    . ARG A 1 669 ? 155.225 124.188 101.219 1.00 35.06 ?  669 ARG A CD    1 
ATOM   5387  N  NE    . ARG A 1 669 ? 155.331 124.679 99.851  1.00 33.74 ?  669 ARG A NE    1 
ATOM   5388  C  CZ    . ARG A 1 669 ? 156.372 125.343 99.364  1.00 34.89 ?  669 ARG A CZ    1 
ATOM   5389  N  NH1   . ARG A 1 669 ? 157.431 125.611 100.109 1.00 33.74 1  669 ARG A NH1   1 
ATOM   5390  N  NH2   . ARG A 1 669 ? 156.350 125.745 98.097  1.00 37.58 ?  669 ARG A NH2   1 
ATOM   5391  N  N     . ILE A 1 670 ? 151.063 127.661 102.479 1.00 25.18 ?  670 ILE A N     1 
ATOM   5392  C  CA    . ILE A 1 670 ? 150.164 128.640 101.874 1.00 25.57 ?  670 ILE A CA    1 
ATOM   5393  C  C     . ILE A 1 670 ? 150.210 129.953 102.647 1.00 27.89 ?  670 ILE A C     1 
ATOM   5394  O  O     . ILE A 1 670 ? 150.244 131.037 102.052 1.00 32.77 ?  670 ILE A O     1 
ATOM   5395  C  CB    . ILE A 1 670 ? 148.730 128.084 101.790 1.00 28.03 ?  670 ILE A CB    1 
ATOM   5396  C  CG1   . ILE A 1 670 ? 148.693 126.816 100.938 1.00 30.18 ?  670 ILE A CG1   1 
ATOM   5397  C  CG2   . ILE A 1 670 ? 147.791 129.126 101.210 1.00 25.40 ?  670 ILE A CG2   1 
ATOM   5398  C  CD1   . ILE A 1 670 ? 147.500 125.932 101.219 1.00 26.89 ?  670 ILE A CD1   1 
ATOM   5399  N  N     . ASP A 1 671 ? 150.213 129.878 103.980 1.00 24.47 ?  671 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 671 ? 150.282 131.093 104.789 1.00 21.06 ?  671 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 671 ? 151.586 131.848 104.553 1.00 25.88 ?  671 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 671 ? 151.590 133.079 104.441 1.00 27.34 ?  671 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 671 ? 150.128 130.747 106.270 1.00 22.89 ?  671 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 671 ? 148.792 130.104 106.582 1.00 34.47 ?  671 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 671 ? 147.847 130.279 105.786 1.00 34.26 ?  671 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 671 ? 148.689 129.423 107.624 1.00 35.03 -1 671 ASP A OD2   1 
ATOM   5407  N  N     . LEU A 1 672 ? 152.704 131.126 104.472 1.00 23.57 ?  672 LEU A N     1 
ATOM   5408  C  CA    . LEU A 1 672 ? 153.996 131.773 104.268 1.00 19.62 ?  672 LEU A CA    1 
ATOM   5409  C  C     . LEU A 1 672 ? 154.131 132.334 102.860 1.00 18.97 ?  672 LEU A C     1 
ATOM   5410  O  O     . LEU A 1 672 ? 154.788 133.362 102.670 1.00 24.16 ?  672 LEU A O     1 
ATOM   5411  C  CB    . LEU A 1 672 ? 155.126 130.787 104.560 1.00 27.26 ?  672 LEU A CB    1 
ATOM   5412  C  CG    . LEU A 1 672 ? 155.243 130.323 106.012 1.00 23.67 ?  672 LEU A CG    1 
ATOM   5413  C  CD1   . LEU A 1 672 ? 156.142 129.104 106.110 1.00 21.82 ?  672 LEU A CD1   1 
ATOM   5414  C  CD2   . LEU A 1 672 ? 155.750 131.448 106.896 1.00 20.76 ?  672 LEU A CD2   1 
ATOM   5415  N  N     . TYR A 1 673 ? 153.530 131.679 101.865 1.00 21.31 ?  673 TYR A N     1 
ATOM   5416  C  CA    . TYR A 1 673 ? 153.531 132.231 100.516 1.00 18.01 ?  673 TYR A CA    1 
ATOM   5417  C  C     . TYR A 1 673 ? 152.636 133.459 100.430 1.00 21.32 ?  673 TYR A C     1 
ATOM   5418  O  O     . TYR A 1 673 ? 152.937 134.404 99.692  1.00 23.54 ?  673 TYR A O     1 
ATOM   5419  C  CB    . TYR A 1 673 ? 153.087 131.166 99.514  1.00 16.74 ?  673 TYR A CB    1 
ATOM   5420  C  CG    . TYR A 1 673 ? 153.153 131.620 98.076  1.00 22.24 ?  673 TYR A CG    1 
ATOM   5421  C  CD1   . TYR A 1 673 ? 154.369 131.915 97.478  1.00 23.24 ?  673 TYR A CD1   1 
ATOM   5422  C  CD2   . TYR A 1 673 ? 152.000 131.754 97.316  1.00 20.22 ?  673 TYR A CD2   1 
ATOM   5423  C  CE1   . TYR A 1 673 ? 154.437 132.331 96.165  1.00 18.97 ?  673 TYR A CE1   1 
ATOM   5424  C  CE2   . TYR A 1 673 ? 152.056 132.170 96.002  1.00 22.76 ?  673 TYR A CE2   1 
ATOM   5425  C  CZ    . TYR A 1 673 ? 153.277 132.454 95.432  1.00 21.41 ?  673 TYR A CZ    1 
ATOM   5426  O  OH    . TYR A 1 673 ? 153.340 132.870 94.123  1.00 26.15 ?  673 TYR A OH    1 
ATOM   5427  N  N     . ALA A 1 674 ? 151.527 133.459 101.172 1.00 21.02 ?  674 ALA A N     1 
ATOM   5428  C  CA    . ALA A 1 674 ? 150.692 134.650 101.263 1.00 16.37 ?  674 ALA A CA    1 
ATOM   5429  C  C     . ALA A 1 674 ? 151.456 135.801 101.901 1.00 16.90 ?  674 ALA A C     1 
ATOM   5430  O  O     . ALA A 1 674 ? 151.393 136.941 101.427 1.00 25.79 ?  674 ALA A O     1 
ATOM   5431  C  CB    . ALA A 1 674 ? 149.425 134.334 102.056 1.00 18.01 ?  674 ALA A CB    1 
ATOM   5432  N  N     . HIS A 1 675 ? 152.193 135.518 102.975 1.00 15.15 ?  675 HIS A N     1 
ATOM   5433  C  CA    . HIS A 1 675 ? 153.030 136.541 103.592 1.00 15.76 ?  675 HIS A CA    1 
ATOM   5434  C  C     . HIS A 1 675 ? 154.098 137.036 102.624 1.00 20.74 ?  675 HIS A C     1 
ATOM   5435  O  O     . HIS A 1 675 ? 154.384 138.236 102.562 1.00 27.09 ?  675 HIS A O     1 
ATOM   5436  C  CB    . HIS A 1 675 ? 153.669 135.991 104.868 1.00 12.33 ?  675 HIS A CB    1 
ATOM   5437  C  CG    . HIS A 1 675 ? 154.635 136.933 105.512 1.00 21.52 ?  675 HIS A CG    1 
ATOM   5438  N  ND1   . HIS A 1 675 ? 155.999 136.817 105.362 1.00 24.93 ?  675 HIS A ND1   1 
ATOM   5439  C  CD2   . HIS A 1 675 ? 154.433 138.011 106.306 1.00 19.57 ?  675 HIS A CD2   1 
ATOM   5440  C  CE1   . HIS A 1 675 ? 156.598 137.781 106.036 1.00 25.63 ?  675 HIS A CE1   1 
ATOM   5441  N  NE2   . HIS A 1 675 ? 155.670 138.520 106.618 1.00 22.92 ?  675 HIS A NE2   1 
ATOM   5442  N  N     . HIS A 1 676 ? 154.699 136.121 101.863 1.00 19.67 ?  676 HIS A N     1 
ATOM   5443  C  CA    . HIS A 1 676 ? 155.727 136.499 100.898 1.00 20.42 ?  676 HIS A CA    1 
ATOM   5444  C  C     . HIS A 1 676 ? 155.147 137.327 99.758  1.00 24.31 ?  676 HIS A C     1 
ATOM   5445  O  O     . HIS A 1 676 ? 155.784 138.276 99.287  1.00 25.05 ?  676 HIS A O     1 
ATOM   5446  C  CB    . HIS A 1 676 ? 156.413 135.246 100.356 1.00 23.92 ?  676 HIS A CB    1 
ATOM   5447  C  CG    . HIS A 1 676 ? 157.289 135.500 99.170  1.00 25.00 ?  676 HIS A CG    1 
ATOM   5448  N  ND1   . HIS A 1 676 ? 158.478 136.193 99.256  1.00 20.88 ?  676 HIS A ND1   1 
ATOM   5449  C  CD2   . HIS A 1 676 ? 157.150 135.153 97.869  1.00 19.79 ?  676 HIS A CD2   1 
ATOM   5450  C  CE1   . HIS A 1 676 ? 159.032 136.262 98.060  1.00 25.77 ?  676 HIS A CE1   1 
ATOM   5451  N  NE2   . HIS A 1 676 ? 158.247 135.639 97.200  1.00 28.82 ?  676 HIS A NE2   1 
ATOM   5452  N  N     . ARG A 1 677 ? 153.944 136.987 99.303  1.00 21.42 ?  677 ARG A N     1 
ATOM   5453  C  CA    . ARG A 1 677 ? 153.337 137.654 98.158  1.00 20.36 ?  677 ARG A CA    1 
ATOM   5454  C  C     . ARG A 1 677 ? 152.649 138.960 98.525  1.00 24.10 ?  677 ARG A C     1 
ATOM   5455  O  O     . ARG A 1 677 ? 152.105 139.625 97.636  1.00 25.29 ?  677 ARG A O     1 
ATOM   5456  C  CB    . ARG A 1 677 ? 152.336 136.719 97.476  1.00 18.85 ?  677 ARG A CB    1 
ATOM   5457  C  CG    . ARG A 1 677 ? 152.966 135.769 96.473  1.00 20.21 ?  677 ARG A CG    1 
ATOM   5458  C  CD    . ARG A 1 677 ? 153.494 136.515 95.260  1.00 20.22 ?  677 ARG A CD    1 
ATOM   5459  N  NE    . ARG A 1 677 ? 152.471 136.687 94.236  1.00 25.02 ?  677 ARG A NE    1 
ATOM   5460  C  CZ    . ARG A 1 677 ? 151.964 137.857 93.873  1.00 27.26 ?  677 ARG A CZ    1 
ATOM   5461  N  NH1   . ARG A 1 677 ? 152.364 138.987 94.432  1.00 21.21 1  677 ARG A NH1   1 
ATOM   5462  N  NH2   . ARG A 1 677 ? 151.032 137.894 92.925  1.00 22.30 ?  677 ARG A NH2   1 
ATOM   5463  N  N     . GLY A 1 678 ? 152.658 139.346 99.797  1.00 20.70 ?  678 GLY A N     1 
ATOM   5464  C  CA    . GLY A 1 678 ? 152.044 140.589 100.212 1.00 16.08 ?  678 GLY A CA    1 
ATOM   5465  C  C     . GLY A 1 678 ? 150.597 140.487 100.624 1.00 16.22 ?  678 GLY A C     1 
ATOM   5466  O  O     . GLY A 1 678 ? 149.917 141.518 100.696 1.00 23.71 ?  678 GLY A O     1 
ATOM   5467  N  N     . ILE A 1 679 ? 150.096 139.281 100.888 1.00 15.50 ?  679 ILE A N     1 
ATOM   5468  C  CA    . ILE A 1 679 ? 148.729 139.128 101.370 1.00 11.34 ?  679 ILE A CA    1 
ATOM   5469  C  C     . ILE A 1 679 ? 148.620 139.755 102.751 1.00 15.26 ?  679 ILE A C     1 
ATOM   5470  O  O     . ILE A 1 679 ? 149.450 139.505 103.634 1.00 23.09 ?  679 ILE A O     1 
ATOM   5471  C  CB    . ILE A 1 679 ? 148.327 137.647 101.397 1.00 15.65 ?  679 ILE A CB    1 
ATOM   5472  C  CG1   . ILE A 1 679 ? 148.255 137.084 99.978  1.00 15.46 ?  679 ILE A CG1   1 
ATOM   5473  C  CG2   . ILE A 1 679 ? 147.002 137.461 102.116 1.00 15.73 ?  679 ILE A CG2   1 
ATOM   5474  C  CD1   . ILE A 1 679 ? 147.347 137.852 99.077  1.00 13.41 ?  679 ILE A CD1   1 
ATOM   5475  N  N     . LYS A 1 680 ? 147.598 140.585 102.942 1.00 13.20 ?  680 LYS A N     1 
ATOM   5476  C  CA    . LYS A 1 680 ? 147.429 141.297 104.200 1.00 8.26  ?  680 LYS A CA    1 
ATOM   5477  C  C     . LYS A 1 680 ? 146.724 140.444 105.251 1.00 8.16  ?  680 LYS A C     1 
ATOM   5478  O  O     . LYS A 1 680 ? 147.157 140.396 106.406 1.00 16.91 ?  680 LYS A O     1 
ATOM   5479  C  CB    . LYS A 1 680 ? 146.654 142.595 103.963 1.00 8.86  ?  680 LYS A CB    1 
ATOM   5480  C  CG    . LYS A 1 680 ? 147.425 143.649 103.191 1.00 0.00  ?  680 LYS A CG    1 
ATOM   5481  C  CD    . LYS A 1 680 ? 146.599 144.910 103.022 1.00 6.45  ?  680 LYS A CD    1 
ATOM   5482  C  CE    . LYS A 1 680 ? 147.191 145.829 101.975 1.00 13.22 ?  680 LYS A CE    1 
ATOM   5483  N  NZ    . LYS A 1 680 ? 146.429 147.100 101.858 1.00 10.77 1  680 LYS A NZ    1 
ATOM   5484  N  N     . THR A 1 681 ? 145.643 139.770 104.871 1.00 15.71 ?  681 THR A N     1 
ATOM   5485  C  CA    . THR A 1 681 ? 144.862 138.964 105.796 1.00 8.89  ?  681 THR A CA    1 
ATOM   5486  C  C     . THR A 1 681 ? 144.503 137.632 105.156 1.00 15.33 ?  681 THR A C     1 
ATOM   5487  O  O     . THR A 1 681 ? 144.332 137.534 103.939 1.00 22.36 ?  681 THR A O     1 
ATOM   5488  C  CB    . THR A 1 681 ? 143.569 139.675 106.226 1.00 16.05 ?  681 THR A CB    1 
ATOM   5489  O  OG1   . THR A 1 681 ? 142.876 140.156 105.068 1.00 30.21 ?  681 THR A OG1   1 
ATOM   5490  C  CG2   . THR A 1 681 ? 143.870 140.841 107.145 1.00 3.10  ?  681 THR A CG2   1 
ATOM   5491  N  N     . ILE A 1 682 ? 144.387 136.606 105.995 1.00 15.27 ?  682 ILE A N     1 
ATOM   5492  C  CA    . ILE A 1 682 ? 143.852 135.310 105.600 1.00 9.32  ?  682 ILE A CA    1 
ATOM   5493  C  C     . ILE A 1 682 ? 142.625 135.037 106.458 1.00 13.63 ?  682 ILE A C     1 
ATOM   5494  O  O     . ILE A 1 682 ? 142.710 135.056 107.691 1.00 21.07 ?  682 ILE A O     1 
ATOM   5495  C  CB    . ILE A 1 682 ? 144.892 134.187 105.752 1.00 12.93 ?  682 ILE A CB    1 
ATOM   5496  C  CG1   . ILE A 1 682 ? 146.282 134.682 105.354 1.00 17.99 ?  682 ILE A CG1   1 
ATOM   5497  C  CG2   . ILE A 1 682 ? 144.507 133.009 104.894 1.00 20.80 ?  682 ILE A CG2   1 
ATOM   5498  C  CD1   . ILE A 1 682 ? 147.329 133.593 105.327 1.00 19.45 ?  682 ILE A CD1   1 
ATOM   5499  N  N     . TYR A 1 683 ? 141.487 134.797 105.806 1.00 18.77 ?  683 TYR A N     1 
ATOM   5500  C  CA    . TYR A 1 683 ? 140.219 134.735 106.534 1.00 12.07 ?  683 TYR A CA    1 
ATOM   5501  C  C     . TYR A 1 683 ? 139.973 133.354 107.139 1.00 19.43 ?  683 TYR A C     1 
ATOM   5502  O  O     . TYR A 1 683 ? 139.940 133.197 108.361 1.00 32.31 ?  683 TYR A O     1 
ATOM   5503  C  CB    . TYR A 1 683 ? 139.070 135.136 105.603 1.00 18.00 ?  683 TYR A CB    1 
ATOM   5504  C  CG    . TYR A 1 683 ? 137.729 135.281 106.287 1.00 16.18 ?  683 TYR A CG    1 
ATOM   5505  C  CD1   . TYR A 1 683 ? 137.645 135.521 107.652 1.00 12.18 ?  683 TYR A CD1   1 
ATOM   5506  C  CD2   . TYR A 1 683 ? 136.548 135.188 105.565 1.00 9.75  ?  683 TYR A CD2   1 
ATOM   5507  C  CE1   . TYR A 1 683 ? 136.425 135.656 108.278 1.00 15.88 ?  683 TYR A CE1   1 
ATOM   5508  C  CE2   . TYR A 1 683 ? 135.322 135.323 106.185 1.00 18.37 ?  683 TYR A CE2   1 
ATOM   5509  C  CZ    . TYR A 1 683 ? 135.267 135.558 107.541 1.00 19.26 ?  683 TYR A CZ    1 
ATOM   5510  O  OH    . TYR A 1 683 ? 134.049 135.692 108.163 1.00 26.27 ?  683 TYR A OH    1 
ATOM   5511  N  N     . TYR A 1 684 ? 139.818 132.339 106.298 1.00 29.27 ?  684 TYR A N     1 
ATOM   5512  C  CA    . TYR A 1 684 ? 139.358 131.045 106.772 1.00 25.72 ?  684 TYR A CA    1 
ATOM   5513  C  C     . TYR A 1 684 ? 140.119 129.934 106.069 1.00 32.85 ?  684 TYR A C     1 
ATOM   5514  O  O     . TYR A 1 684 ? 140.647 130.118 104.969 1.00 36.53 ?  684 TYR A O     1 
ATOM   5515  C  CB    . TYR A 1 684 ? 137.852 130.867 106.540 1.00 23.92 ?  684 TYR A CB    1 
ATOM   5516  C  CG    . TYR A 1 684 ? 137.002 131.157 107.754 1.00 22.24 ?  684 TYR A CG    1 
ATOM   5517  C  CD1   . TYR A 1 684 ? 137.217 130.490 108.953 1.00 26.54 ?  684 TYR A CD1   1 
ATOM   5518  C  CD2   . TYR A 1 684 ? 135.983 132.098 107.702 1.00 29.36 ?  684 TYR A CD2   1 
ATOM   5519  C  CE1   . TYR A 1 684 ? 136.440 130.752 110.065 1.00 30.37 ?  684 TYR A CE1   1 
ATOM   5520  C  CE2   . TYR A 1 684 ? 135.202 132.369 108.809 1.00 26.07 ?  684 TYR A CE2   1 
ATOM   5521  C  CZ    . TYR A 1 684 ? 135.435 131.694 109.987 1.00 29.63 ?  684 TYR A CZ    1 
ATOM   5522  O  OH    . TYR A 1 684 ? 134.660 131.960 111.091 1.00 32.26 ?  684 TYR A OH    1 
ATOM   5523  N  N     . ALA A 1 685 ? 140.170 128.779 106.723 1.00 31.03 ?  685 ALA A N     1 
ATOM   5524  C  CA    . ALA A 1 685 ? 140.731 127.557 106.158 1.00 32.41 ?  685 ALA A CA    1 
ATOM   5525  C  C     . ALA A 1 685 ? 139.593 126.544 106.092 1.00 36.55 ?  685 ALA A C     1 
ATOM   5526  O  O     . ALA A 1 685 ? 139.399 125.748 107.014 1.00 43.59 ?  685 ALA A O     1 
ATOM   5527  C  CB    . ALA A 1 685 ? 141.903 127.047 106.988 1.00 32.11 ?  685 ALA A CB    1 
ATOM   5528  N  N     . ARG A 1 686 ? 138.835 126.585 105.000 1.00 32.51 ?  686 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 686 ? 137.713 125.679 104.805 1.00 33.05 ?  686 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 686 ? 138.220 124.381 104.191 1.00 38.70 ?  686 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 686 ? 138.751 124.382 103.076 1.00 40.64 ?  686 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 686 ? 136.663 126.325 103.904 1.00 38.13 ?  686 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 686 ? 135.939 127.500 104.535 1.00 38.73 ?  686 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 686 ? 134.660 127.825 103.783 1.00 39.90 ?  686 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 686 ? 133.786 126.665 103.660 1.00 42.70 ?  686 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 686 ? 132.469 126.705 103.801 1.00 42.66 ?  686 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 686 ? 131.835 127.836 104.069 1.00 41.77 1  686 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 686 ? 131.767 125.582 103.669 1.00 42.47 ?  686 ARG A NH2   1 
ATOM   5539  N  N     . THR A 1 687 ? 138.062 123.280 104.919 1.00 48.40 ?  687 THR A N     1 
ATOM   5540  C  CA    . THR A 1 687 ? 138.492 121.969 104.457 1.00 46.64 ?  687 THR A CA    1 
ATOM   5541  C  C     . THR A 1 687 ? 137.310 121.224 103.852 1.00 47.93 ?  687 THR A C     1 
ATOM   5542  O  O     . THR A 1 687 ? 136.233 121.154 104.451 1.00 50.75 ?  687 THR A O     1 
ATOM   5543  C  CB    . THR A 1 687 ? 139.096 121.156 105.606 1.00 46.66 ?  687 THR A CB    1 
ATOM   5544  O  OG1   . THR A 1 687 ? 140.394 121.672 105.930 1.00 48.39 ?  687 THR A OG1   1 
ATOM   5545  C  CG2   . THR A 1 687 ? 139.225 119.689 105.220 1.00 47.30 ?  687 THR A CG2   1 
ATOM   5546  N  N     . LYS A 1 688 ? 137.518 120.673 102.662 1.00 48.04 ?  688 LYS A N     1 
ATOM   5547  C  CA    . LYS A 1 688 ? 136.469 119.940 101.965 1.00 48.98 ?  688 LYS A CA    1 
ATOM   5548  C  C     . LYS A 1 688 ? 136.344 118.521 102.508 1.00 53.36 ?  688 LYS A C     1 
ATOM   5549  O  O     . LYS A 1 688 ? 137.326 117.930 102.959 1.00 55.18 ?  688 LYS A O     1 
ATOM   5550  C  CB    . LYS A 1 688 ? 136.745 119.906 100.461 1.00 49.54 ?  688 LYS A CB    1 
ATOM   5551  C  CG    . LYS A 1 688 ? 135.614 119.315 99.638  1.00 48.07 ?  688 LYS A CG    1 
ATOM   5552  C  CD    . LYS A 1 688 ? 135.924 119.370 98.152  1.00 47.51 ?  688 LYS A CD    1 
ATOM   5553  C  CE    . LYS A 1 688 ? 134.766 118.831 97.330  1.00 51.68 ?  688 LYS A CE    1 
ATOM   5554  N  NZ    . LYS A 1 688 ? 135.042 118.903 95.869  1.00 52.23 ?  688 LYS A NZ    1 
ATOM   5555  N  N     . VAL B 1 6   ? 155.384 118.285 162.543 1.00 57.44 ?  6   VAL B N     1 
ATOM   5556  C  CA    . VAL B 1 6   ? 154.270 119.124 162.967 1.00 58.35 ?  6   VAL B CA    1 
ATOM   5557  C  C     . VAL B 1 6   ? 154.722 120.114 164.035 1.00 60.21 ?  6   VAL B C     1 
ATOM   5558  O  O     . VAL B 1 6   ? 155.559 119.788 164.876 1.00 58.78 ?  6   VAL B O     1 
ATOM   5559  C  CB    . VAL B 1 6   ? 153.093 118.271 163.474 1.00 58.16 ?  6   VAL B CB    1 
ATOM   5560  C  CG1   . VAL B 1 6   ? 152.412 117.566 162.312 1.00 58.66 ?  6   VAL B CG1   1 
ATOM   5561  C  CG2   . VAL B 1 6   ? 153.573 117.262 164.502 1.00 58.25 ?  6   VAL B CG2   1 
ATOM   5562  N  N     . PRO B 1 7   ? 154.175 121.326 163.993 1.00 57.76 ?  7   PRO B N     1 
ATOM   5563  C  CA    . PRO B 1 7   ? 154.556 122.346 164.975 1.00 53.33 ?  7   PRO B CA    1 
ATOM   5564  C  C     . PRO B 1 7   ? 154.102 121.977 166.380 1.00 52.92 ?  7   PRO B C     1 
ATOM   5565  O  O     . PRO B 1 7   ? 153.146 121.224 166.582 1.00 55.02 ?  7   PRO B O     1 
ATOM   5566  C  CB    . PRO B 1 7   ? 153.844 123.609 164.479 1.00 52.57 ?  7   PRO B CB    1 
ATOM   5567  C  CG    . PRO B 1 7   ? 153.485 123.335 163.058 1.00 52.52 ?  7   PRO B CG    1 
ATOM   5568  C  CD    . PRO B 1 7   ? 153.282 121.859 162.952 1.00 54.44 ?  7   PRO B CD    1 
ATOM   5569  N  N     . LYS B 1 8   ? 154.821 122.525 167.362 1.00 50.58 ?  8   LYS B N     1 
ATOM   5570  C  CA    . LYS B 1 8   ? 154.513 122.237 168.760 1.00 49.37 ?  8   LYS B CA    1 
ATOM   5571  C  C     . LYS B 1 8   ? 153.124 122.735 169.140 1.00 52.20 ?  8   LYS B C     1 
ATOM   5572  O  O     . LYS B 1 8   ? 152.371 122.034 169.827 1.00 54.02 ?  8   LYS B O     1 
ATOM   5573  C  CB    . LYS B 1 8   ? 155.574 122.859 169.667 1.00 51.24 ?  8   LYS B CB    1 
ATOM   5574  C  CG    . LYS B 1 8   ? 155.155 122.974 171.123 1.00 52.38 ?  8   LYS B CG    1 
ATOM   5575  C  CD    . LYS B 1 8   ? 156.359 122.987 172.047 1.00 51.18 ?  8   LYS B CD    1 
ATOM   5576  C  CE    . LYS B 1 8   ? 155.935 122.892 173.503 1.00 51.50 ?  8   LYS B CE    1 
ATOM   5577  N  NZ    . LYS B 1 8   ? 155.875 124.230 174.153 1.00 52.01 1  8   LYS B NZ    1 
ATOM   5578  N  N     . TRP B 1 9   ? 152.766 123.946 168.703 1.00 53.51 ?  9   TRP B N     1 
ATOM   5579  C  CA    . TRP B 1 9   ? 151.438 124.465 169.010 1.00 51.21 ?  9   TRP B CA    1 
ATOM   5580  C  C     . TRP B 1 9   ? 150.351 123.640 168.339 1.00 49.73 ?  9   TRP B C     1 
ATOM   5581  O  O     . TRP B 1 9   ? 149.257 123.494 168.894 1.00 51.44 ?  9   TRP B O     1 
ATOM   5582  C  CB    . TRP B 1 9   ? 151.322 125.933 168.595 1.00 51.68 ?  9   TRP B CB    1 
ATOM   5583  C  CG    . TRP B 1 9   ? 151.646 126.204 167.160 1.00 49.36 ?  9   TRP B CG    1 
ATOM   5584  C  CD1   . TRP B 1 9   ? 150.777 126.190 166.109 1.00 48.25 ?  9   TRP B CD1   1 
ATOM   5585  C  CD2   . TRP B 1 9   ? 152.925 126.554 166.618 1.00 49.96 ?  9   TRP B CD2   1 
ATOM   5586  N  NE1   . TRP B 1 9   ? 151.436 126.500 164.945 1.00 47.82 ?  9   TRP B NE1   1 
ATOM   5587  C  CE2   . TRP B 1 9   ? 152.755 126.730 165.231 1.00 49.58 ?  9   TRP B CE2   1 
ATOM   5588  C  CE3   . TRP B 1 9   ? 154.196 126.732 167.169 1.00 47.79 ?  9   TRP B CE3   1 
ATOM   5589  C  CZ2   . TRP B 1 9   ? 153.809 127.072 164.388 1.00 48.99 ?  9   TRP B CZ2   1 
ATOM   5590  C  CZ3   . TRP B 1 9   ? 155.241 127.073 166.332 1.00 49.28 ?  9   TRP B CZ3   1 
ATOM   5591  C  CH2   . TRP B 1 9   ? 155.041 127.236 164.956 1.00 50.26 ?  9   TRP B CH2   1 
ATOM   5592  N  N     . ILE B 1 10  ? 150.631 123.086 167.158 1.00 52.27 ?  10  ILE B N     1 
ATOM   5593  C  CA    . ILE B 1 10  ? 149.665 122.216 166.497 1.00 52.32 ?  10  ILE B CA    1 
ATOM   5594  C  C     . ILE B 1 10  ? 149.423 120.962 167.328 1.00 53.45 ?  10  ILE B C     1 
ATOM   5595  O  O     . ILE B 1 10  ? 148.277 120.527 167.502 1.00 55.24 ?  10  ILE B O     1 
ATOM   5596  C  CB    . ILE B 1 10  ? 150.149 121.875 165.077 1.00 52.71 ?  10  ILE B CB    1 
ATOM   5597  C  CG1   . ILE B 1 10  ? 149.995 123.091 164.158 1.00 52.31 ?  10  ILE B CG1   1 
ATOM   5598  C  CG2   . ILE B 1 10  ? 149.396 120.672 164.526 1.00 53.05 ?  10  ILE B CG2   1 
ATOM   5599  C  CD1   . ILE B 1 10  ? 148.679 123.153 163.424 1.00 53.46 ?  10  ILE B CD1   1 
ATOM   5600  N  N     . GLN B 1 11  ? 150.492 120.365 167.861 1.00 53.92 ?  11  GLN B N     1 
ATOM   5601  C  CA    . GLN B 1 11  ? 150.337 119.200 168.727 1.00 55.14 ?  11  GLN B CA    1 
ATOM   5602  C  C     . GLN B 1 11  ? 149.573 119.553 169.996 1.00 54.84 ?  11  GLN B C     1 
ATOM   5603  O  O     . GLN B 1 11  ? 148.710 118.788 170.444 1.00 57.06 ?  11  GLN B O     1 
ATOM   5604  C  CB    . GLN B 1 11  ? 151.706 118.617 169.077 1.00 56.03 ?  11  GLN B CB    1 
ATOM   5605  C  CG    . GLN B 1 11  ? 152.560 118.264 167.874 1.00 56.59 ?  11  GLN B CG    1 
ATOM   5606  C  CD    . GLN B 1 11  ? 154.040 118.249 168.200 1.00 58.95 ?  11  GLN B CD    1 
ATOM   5607  O  OE1   . GLN B 1 11  ? 154.880 118.506 167.338 1.00 58.89 ?  11  GLN B OE1   1 
ATOM   5608  N  NE2   . GLN B 1 11  ? 154.366 117.950 169.452 1.00 55.94 ?  11  GLN B NE2   1 
ATOM   5609  N  N     . LEU B 1 12  ? 149.875 120.709 170.591 1.00 51.73 ?  12  LEU B N     1 
ATOM   5610  C  CA    . LEU B 1 12  ? 149.170 121.114 171.803 1.00 50.64 ?  12  LEU B CA    1 
ATOM   5611  C  C     . LEU B 1 12  ? 147.688 121.345 171.530 1.00 51.29 ?  12  LEU B C     1 
ATOM   5612  O  O     . LEU B 1 12  ? 146.838 121.010 172.364 1.00 53.55 ?  12  LEU B O     1 
ATOM   5613  C  CB    . LEU B 1 12  ? 149.816 122.367 172.390 1.00 52.10 ?  12  LEU B CB    1 
ATOM   5614  C  CG    . LEU B 1 12  ? 151.066 122.119 173.236 1.00 52.39 ?  12  LEU B CG    1 
ATOM   5615  C  CD1   . LEU B 1 12  ? 151.850 123.407 173.434 1.00 52.91 ?  12  LEU B CD1   1 
ATOM   5616  C  CD2   . LEU B 1 12  ? 150.692 121.502 174.572 1.00 51.76 ?  12  LEU B CD2   1 
ATOM   5617  N  N     . ASN B 1 13  ? 147.360 121.920 170.372 1.00 51.33 ?  13  ASN B N     1 
ATOM   5618  C  CA    . ASN B 1 13  ? 145.961 122.131 170.015 1.00 49.42 ?  13  ASN B CA    1 
ATOM   5619  C  C     . ASN B 1 13  ? 145.257 120.810 169.730 1.00 52.08 ?  13  ASN B C     1 
ATOM   5620  O  O     . ASN B 1 13  ? 144.080 120.644 170.067 1.00 56.58 ?  13  ASN B O     1 
ATOM   5621  C  CB    . ASN B 1 13  ? 145.866 123.066 168.809 1.00 51.33 ?  13  ASN B CB    1 
ATOM   5622  C  CG    . ASN B 1 13  ? 144.442 123.260 168.335 1.00 50.05 ?  13  ASN B CG    1 
ATOM   5623  O  OD1   . ASN B 1 13  ? 144.048 122.742 167.293 1.00 50.41 ?  13  ASN B OD1   1 
ATOM   5624  N  ND2   . ASN B 1 13  ? 143.661 124.010 169.102 1.00 51.28 ?  13  ASN B ND2   1 
ATOM   5625  N  N     . ASN B 1 14  ? 145.953 119.860 169.102 1.00 53.76 ?  14  ASN B N     1 
ATOM   5626  C  CA    . ASN B 1 14  ? 145.366 118.545 168.876 1.00 52.32 ?  14  ASN B CA    1 
ATOM   5627  C  C     . ASN B 1 14  ? 145.233 117.749 170.166 1.00 53.34 ?  14  ASN B C     1 
ATOM   5628  O  O     . ASN B 1 14  ? 144.446 116.798 170.216 1.00 56.59 ?  14  ASN B O     1 
ATOM   5629  C  CB    . ASN B 1 14  ? 146.200 117.760 167.862 1.00 52.91 ?  14  ASN B CB    1 
ATOM   5630  C  CG    . ASN B 1 14  ? 146.127 118.351 166.472 1.00 55.92 ?  14  ASN B CG    1 
ATOM   5631  O  OD1   . ASN B 1 14  ? 145.347 119.268 166.217 1.00 58.01 ?  14  ASN B OD1   1 
ATOM   5632  N  ND2   . ASN B 1 14  ? 146.939 117.828 165.562 1.00 54.69 ?  14  ASN B ND2   1 
ATOM   5633  N  N     . GLU B 1 15  ? 145.986 118.116 171.204 1.00 56.23 ?  15  GLU B N     1 
ATOM   5634  C  CA    . GLU B 1 15  ? 145.869 117.455 172.498 1.00 56.56 ?  15  GLU B CA    1 
ATOM   5635  C  C     . GLU B 1 15  ? 144.536 117.720 173.186 1.00 57.08 ?  15  GLU B C     1 
ATOM   5636  O  O     . GLU B 1 15  ? 144.243 117.065 174.192 1.00 60.06 ?  15  GLU B O     1 
ATOM   5637  C  CB    . GLU B 1 15  ? 147.016 117.890 173.413 1.00 55.53 ?  15  GLU B CB    1 
ATOM   5638  C  CG    . GLU B 1 15  ? 148.186 116.920 173.440 1.00 57.49 ?  15  GLU B CG    1 
ATOM   5639  C  CD    . GLU B 1 15  ? 149.484 117.580 173.861 1.00 61.35 ?  15  GLU B CD    1 
ATOM   5640  O  OE1   . GLU B 1 15  ? 149.617 117.925 175.054 1.00 60.81 ?  15  GLU B OE1   1 
ATOM   5641  O  OE2   . GLU B 1 15  ? 150.373 117.752 173.000 1.00 60.08 -1 15  GLU B OE2   1 
ATOM   5642  N  N     . ILE B 1 16  ? 143.735 118.663 172.685 1.00 56.73 ?  16  ILE B N     1 
ATOM   5643  C  CA    . ILE B 1 16  ? 142.428 118.929 173.284 1.00 56.54 ?  16  ILE B CA    1 
ATOM   5644  C  C     . ILE B 1 16  ? 141.535 117.700 173.174 1.00 56.57 ?  16  ILE B C     1 
ATOM   5645  O  O     . ILE B 1 16  ? 140.882 117.293 174.143 1.00 54.26 ?  16  ILE B O     1 
ATOM   5646  C  CB    . ILE B 1 16  ? 141.769 120.152 172.621 1.00 55.92 ?  16  ILE B CB    1 
ATOM   5647  C  CG1   . ILE B 1 16  ? 142.619 121.405 172.816 1.00 55.42 ?  16  ILE B CG1   1 
ATOM   5648  C  CG2   . ILE B 1 16  ? 140.370 120.371 173.177 1.00 56.40 ?  16  ILE B CG2   1 
ATOM   5649  C  CD1   . ILE B 1 16  ? 142.250 122.519 171.869 1.00 54.74 ?  16  ILE B CD1   1 
ATOM   5650  N  N     . MET B 1 17  ? 141.496 117.088 171.990 1.00 56.33 ?  17  MET B N     1 
ATOM   5651  C  CA    . MET B 1 17  ? 140.599 115.966 171.750 1.00 56.69 ?  17  MET B CA    1 
ATOM   5652  C  C     . MET B 1 17  ? 141.062 114.682 172.421 1.00 57.42 ?  17  MET B C     1 
ATOM   5653  O  O     . MET B 1 17  ? 140.247 113.773 172.611 1.00 56.86 ?  17  MET B O     1 
ATOM   5654  C  CB    . MET B 1 17  ? 140.440 115.734 170.248 1.00 57.47 ?  17  MET B CB    1 
ATOM   5655  C  CG    . MET B 1 17  ? 140.054 116.983 169.487 1.00 57.59 ?  17  MET B CG    1 
ATOM   5656  S  SD    . MET B 1 17  ? 138.470 117.657 170.019 1.00 63.33 ?  17  MET B SD    1 
ATOM   5657  C  CE    . MET B 1 17  ? 137.371 116.965 168.788 1.00 55.92 ?  17  MET B CE    1 
ATOM   5658  N  N     . ILE B 1 18  ? 142.339 114.582 172.781 1.00 59.62 ?  18  ILE B N     1 
ATOM   5659  C  CA    . ILE B 1 18  ? 142.811 113.440 173.550 1.00 58.94 ?  18  ILE B CA    1 
ATOM   5660  C  C     . ILE B 1 18  ? 142.248 113.582 174.957 1.00 60.09 ?  18  ILE B C     1 
ATOM   5661  O  O     . ILE B 1 18  ? 142.717 114.408 175.748 1.00 59.84 ?  18  ILE B O     1 
ATOM   5662  C  CB    . ILE B 1 18  ? 144.348 113.347 173.557 1.00 60.01 ?  18  ILE B CB    1 
ATOM   5663  C  CG1   . ILE B 1 18  ? 144.859 112.969 172.165 1.00 60.22 ?  18  ILE B CG1   1 
ATOM   5664  C  CG2   . ILE B 1 18  ? 144.819 112.326 174.580 1.00 59.20 ?  18  ILE B CG2   1 
ATOM   5665  C  CD1   . ILE B 1 18  ? 145.950 113.875 171.646 1.00 60.47 ?  18  ILE B CD1   1 
ATOM   5666  N  N     . GLN B 1 19  ? 141.226 112.791 175.268 1.00 62.58 ?  19  GLN B N     1 
ATOM   5667  C  CA    . GLN B 1 19  ? 140.512 112.953 176.524 1.00 62.09 ?  19  GLN B CA    1 
ATOM   5668  C  C     . GLN B 1 19  ? 141.341 112.435 177.691 1.00 64.61 ?  19  GLN B C     1 
ATOM   5669  O  O     . GLN B 1 19  ? 142.012 111.404 177.593 1.00 66.56 ?  19  GLN B O     1 
ATOM   5670  C  CB    . GLN B 1 19  ? 139.170 112.224 176.468 1.00 64.69 ?  19  GLN B CB    1 
ATOM   5671  C  CG    . GLN B 1 19  ? 138.578 112.131 175.072 1.00 64.60 ?  19  GLN B CG    1 
ATOM   5672  C  CD    . GLN B 1 19  ? 137.075 112.328 175.059 1.00 64.39 ?  19  GLN B CD    1 
ATOM   5673  O  OE1   . GLN B 1 19  ? 136.380 111.952 176.004 1.00 64.88 ?  19  GLN B OE1   1 
ATOM   5674  N  NE2   . GLN B 1 19  ? 136.564 112.919 173.986 1.00 64.21 ?  19  GLN B NE2   1 
ATOM   5675  N  N     . LYS B 1 20  ? 141.292 113.165 178.802 1.00 67.86 ?  20  LYS B N     1 
ATOM   5676  C  CA    . LYS B 1 20  ? 141.927 112.761 180.050 1.00 69.26 ?  20  LYS B CA    1 
ATOM   5677  C  C     . LYS B 1 20  ? 140.838 112.620 181.102 1.00 69.23 ?  20  LYS B C     1 
ATOM   5678  O  O     . LYS B 1 20  ? 140.116 113.584 181.382 1.00 68.81 ?  20  LYS B O     1 
ATOM   5679  C  CB    . LYS B 1 20  ? 142.985 113.775 180.485 1.00 67.79 ?  20  LYS B CB    1 
ATOM   5680  C  CG    . LYS B 1 20  ? 143.278 113.775 181.976 1.00 68.45 ?  20  LYS B CG    1 
ATOM   5681  C  CD    . LYS B 1 20  ? 144.648 114.366 182.268 1.00 69.24 ?  20  LYS B CD    1 
ATOM   5682  C  CE    . LYS B 1 20  ? 144.537 115.811 182.725 1.00 69.19 ?  20  LYS B CE    1 
ATOM   5683  N  NZ    . LYS B 1 20  ? 145.856 116.501 182.715 1.00 68.51 1  20  LYS B NZ    1 
ATOM   5684  N  N     . ASP B 1 21  ? 140.720 111.422 181.675 1.00 71.38 ?  21  ASP B N     1 
ATOM   5685  C  CA    . ASP B 1 21  ? 139.663 111.101 182.637 1.00 71.25 ?  21  ASP B CA    1 
ATOM   5686  C  C     . ASP B 1 21  ? 138.279 111.352 182.041 1.00 72.08 ?  21  ASP B C     1 
ATOM   5687  O  O     . ASP B 1 21  ? 137.360 111.810 182.725 1.00 71.47 ?  21  ASP B O     1 
ATOM   5688  C  CB    . ASP B 1 21  ? 139.846 111.878 183.942 1.00 71.76 ?  21  ASP B CB    1 
ATOM   5689  C  CG    . ASP B 1 21  ? 141.285 111.882 184.421 1.00 73.48 ?  21  ASP B CG    1 
ATOM   5690  O  OD1   . ASP B 1 21  ? 141.945 110.825 184.334 1.00 72.23 ?  21  ASP B OD1   1 
ATOM   5691  O  OD2   . ASP B 1 21  ? 141.756 112.942 184.885 1.00 72.92 -1 21  ASP B OD2   1 
ATOM   5692  N  N     . GLY B 1 22  ? 138.128 111.050 180.753 1.00 68.63 ?  22  GLY B N     1 
ATOM   5693  C  CA    . GLY B 1 22  ? 136.853 111.185 180.081 1.00 66.05 ?  22  GLY B CA    1 
ATOM   5694  C  C     . GLY B 1 22  ? 136.441 112.598 179.738 1.00 67.44 ?  22  GLY B C     1 
ATOM   5695  O  O     . GLY B 1 22  ? 135.295 112.807 179.326 1.00 67.11 ?  22  GLY B O     1 
ATOM   5696  N  N     . LYS B 1 23  ? 137.332 113.574 179.889 1.00 66.70 ?  23  LYS B N     1 
ATOM   5697  C  CA    . LYS B 1 23  ? 137.019 114.971 179.632 1.00 63.82 ?  23  LYS B CA    1 
ATOM   5698  C  C     . LYS B 1 23  ? 138.005 115.555 178.630 1.00 63.01 ?  23  LYS B C     1 
ATOM   5699  O  O     . LYS B 1 23  ? 139.179 115.173 178.593 1.00 64.84 ?  23  LYS B O     1 
ATOM   5700  C  CB    . LYS B 1 23  ? 137.052 115.796 180.925 1.00 63.78 ?  23  LYS B CB    1 
ATOM   5701  C  CG    . LYS B 1 23  ? 136.435 115.099 182.123 1.00 65.44 ?  23  LYS B CG    1 
ATOM   5702  C  CD    . LYS B 1 23  ? 134.935 114.939 181.952 1.00 65.22 ?  23  LYS B CD    1 
ATOM   5703  C  CE    . LYS B 1 23  ? 134.214 116.248 182.212 1.00 64.91 ?  23  LYS B CE    1 
ATOM   5704  N  NZ    . LYS B 1 23  ? 134.890 117.043 183.273 1.00 63.67 1  23  LYS B NZ    1 
ATOM   5705  N  N     . PHE B 1 24  ? 137.514 116.486 177.815 1.00 59.23 ?  24  PHE B N     1 
ATOM   5706  C  CA    . PHE B 1 24  ? 138.369 117.166 176.852 1.00 57.17 ?  24  PHE B CA    1 
ATOM   5707  C  C     . PHE B 1 24  ? 139.391 118.037 177.571 1.00 56.29 ?  24  PHE B C     1 
ATOM   5708  O  O     . PHE B 1 24  ? 139.107 118.620 178.620 1.00 56.56 ?  24  PHE B O     1 
ATOM   5709  C  CB    . PHE B 1 24  ? 137.530 118.021 175.904 1.00 55.54 ?  24  PHE B CB    1 
ATOM   5710  C  CG    . PHE B 1 24  ? 136.832 117.237 174.830 1.00 55.27 ?  24  PHE B CG    1 
ATOM   5711  C  CD1   . PHE B 1 24  ? 137.525 116.788 173.719 1.00 57.16 ?  24  PHE B CD1   1 
ATOM   5712  C  CD2   . PHE B 1 24  ? 135.479 116.960 174.926 1.00 55.44 ?  24  PHE B CD2   1 
ATOM   5713  C  CE1   . PHE B 1 24  ? 136.884 116.069 172.729 1.00 56.09 ?  24  PHE B CE1   1 
ATOM   5714  C  CE2   . PHE B 1 24  ? 134.834 116.242 173.938 1.00 56.44 ?  24  PHE B CE2   1 
ATOM   5715  C  CZ    . PHE B 1 24  ? 135.537 115.798 172.838 1.00 55.50 ?  24  PHE B CZ    1 
ATOM   5716  N  N     . GLN B 1 25  ? 140.591 118.123 176.996 1.00 57.29 ?  25  GLN B N     1 
ATOM   5717  C  CA    . GLN B 1 25  ? 141.668 118.937 177.564 1.00 57.15 ?  25  GLN B CA    1 
ATOM   5718  C  C     . GLN B 1 25  ? 141.610 120.325 176.933 1.00 57.88 ?  25  GLN B C     1 
ATOM   5719  O  O     . GLN B 1 25  ? 142.411 120.691 176.070 1.00 59.45 ?  25  GLN B O     1 
ATOM   5720  C  CB    . GLN B 1 25  ? 143.019 118.268 177.345 1.00 57.43 ?  25  GLN B CB    1 
ATOM   5721  C  CG    . GLN B 1 25  ? 143.115 116.865 177.918 1.00 57.27 ?  25  GLN B CG    1 
ATOM   5722  C  CD    . GLN B 1 25  ? 144.477 116.241 177.696 1.00 58.27 ?  25  GLN B CD    1 
ATOM   5723  O  OE1   . GLN B 1 25  ? 145.345 116.292 178.568 1.00 58.75 ?  25  GLN B OE1   1 
ATOM   5724  N  NE2   . GLN B 1 25  ? 144.673 115.648 176.524 1.00 58.57 ?  25  GLN B NE2   1 
ATOM   5725  N  N     . PHE B 1 26  ? 140.630 121.111 177.383 1.00 51.55 ?  26  PHE B N     1 
ATOM   5726  C  CA    . PHE B 1 26  ? 140.454 122.458 176.847 1.00 52.93 ?  26  PHE B CA    1 
ATOM   5727  C  C     . PHE B 1 26  ? 141.630 123.358 177.211 1.00 53.51 ?  26  PHE B C     1 
ATOM   5728  O  O     . PHE B 1 26  ? 142.050 124.194 176.402 1.00 52.89 ?  26  PHE B O     1 
ATOM   5729  C  CB    . PHE B 1 26  ? 139.143 123.055 177.354 1.00 50.12 ?  26  PHE B CB    1 
ATOM   5730  C  CG    . PHE B 1 26  ? 137.920 122.327 176.872 1.00 51.96 ?  26  PHE B CG    1 
ATOM   5731  C  CD1   . PHE B 1 26  ? 137.687 122.159 175.518 1.00 51.08 ?  26  PHE B CD1   1 
ATOM   5732  C  CD2   . PHE B 1 26  ? 137.005 121.812 177.774 1.00 50.64 ?  26  PHE B CD2   1 
ATOM   5733  C  CE1   . PHE B 1 26  ? 136.564 121.491 175.071 1.00 49.46 ?  26  PHE B CE1   1 
ATOM   5734  C  CE2   . PHE B 1 26  ? 135.880 121.142 177.332 1.00 49.81 ?  26  PHE B CE2   1 
ATOM   5735  C  CZ    . PHE B 1 26  ? 135.659 120.983 175.980 1.00 49.40 ?  26  PHE B CZ    1 
ATOM   5736  N  N     . ASP B 1 27  ? 142.173 123.200 178.422 1.00 57.05 ?  27  ASP B N     1 
ATOM   5737  C  CA    . ASP B 1 27  ? 143.277 124.048 178.861 1.00 54.92 ?  27  ASP B CA    1 
ATOM   5738  C  C     . ASP B 1 27  ? 144.494 123.907 177.956 1.00 55.84 ?  27  ASP B C     1 
ATOM   5739  O  O     . ASP B 1 27  ? 145.267 124.863 177.806 1.00 55.38 ?  27  ASP B O     1 
ATOM   5740  C  CB    . ASP B 1 27  ? 143.649 123.715 180.306 1.00 55.14 ?  27  ASP B CB    1 
ATOM   5741  C  CG    . ASP B 1 27  ? 143.502 122.239 180.620 1.00 59.58 ?  27  ASP B CG    1 
ATOM   5742  O  OD1   . ASP B 1 27  ? 143.912 121.408 179.784 1.00 58.90 ?  27  ASP B OD1   1 
ATOM   5743  O  OD2   . ASP B 1 27  ? 142.975 121.911 181.704 1.00 60.21 -1 27  ASP B OD2   1 
ATOM   5744  N  N     . LYS B 1 28  ? 144.673 122.735 177.338 1.00 55.09 ?  28  LYS B N     1 
ATOM   5745  C  CA    . LYS B 1 28  ? 145.772 122.552 176.395 1.00 55.69 ?  28  LYS B CA    1 
ATOM   5746  C  C     . LYS B 1 28  ? 145.739 123.614 175.305 1.00 55.91 ?  28  LYS B C     1 
ATOM   5747  O  O     . LYS B 1 28  ? 146.792 124.090 174.860 1.00 58.39 ?  28  LYS B O     1 
ATOM   5748  C  CB    . LYS B 1 28  ? 145.709 121.154 175.781 1.00 56.35 ?  28  LYS B CB    1 
ATOM   5749  C  CG    . LYS B 1 28  ? 146.223 120.046 176.684 1.00 56.47 ?  28  LYS B CG    1 
ATOM   5750  C  CD    . LYS B 1 28  ? 147.730 120.121 176.850 1.00 56.20 ?  28  LYS B CD    1 
ATOM   5751  C  CE    . LYS B 1 28  ? 148.226 119.092 177.852 1.00 56.98 ?  28  LYS B CE    1 
ATOM   5752  N  NZ    . LYS B 1 28  ? 149.037 119.713 178.934 1.00 55.47 1  28  LYS B NZ    1 
ATOM   5753  N  N     . ASP B 1 29  ? 144.534 124.016 174.886 1.00 54.35 ?  29  ASP B N     1 
ATOM   5754  C  CA    . ASP B 1 29  ? 144.394 125.073 173.891 1.00 52.22 ?  29  ASP B CA    1 
ATOM   5755  C  C     . ASP B 1 29  ? 145.188 126.306 174.292 1.00 52.26 ?  29  ASP B C     1 
ATOM   5756  O  O     . ASP B 1 29  ? 145.952 126.854 173.490 1.00 52.34 ?  29  ASP B O     1 
ATOM   5757  C  CB    . ASP B 1 29  ? 142.918 125.426 173.709 1.00 52.42 ?  29  ASP B CB    1 
ATOM   5758  C  CG    . ASP B 1 29  ? 142.626 126.027 172.349 1.00 54.90 ?  29  ASP B CG    1 
ATOM   5759  O  OD1   . ASP B 1 29  ? 143.357 125.711 171.387 1.00 55.08 ?  29  ASP B OD1   1 
ATOM   5760  O  OD2   . ASP B 1 29  ? 141.663 126.814 172.242 1.00 52.90 -1 29  ASP B OD2   1 
ATOM   5761  N  N     . LYS B 1 30  ? 145.046 126.731 175.551 1.00 52.18 ?  30  LYS B N     1 
ATOM   5762  C  CA    . LYS B 1 30  ? 145.795 127.886 176.032 1.00 53.26 ?  30  LYS B CA    1 
ATOM   5763  C  C     . LYS B 1 30  ? 147.288 127.677 175.836 1.00 51.63 ?  30  LYS B C     1 
ATOM   5764  O  O     . LYS B 1 30  ? 147.986 128.544 175.294 1.00 55.03 ?  30  LYS B O     1 
ATOM   5765  C  CB    . LYS B 1 30  ? 145.472 128.143 177.505 1.00 52.12 ?  30  LYS B CB    1 
ATOM   5766  C  CG    . LYS B 1 30  ? 146.175 129.355 178.091 1.00 51.47 ?  30  LYS B CG    1 
ATOM   5767  C  CD    . LYS B 1 30  ? 145.763 129.588 179.535 1.00 53.30 ?  30  LYS B CD    1 
ATOM   5768  C  CE    . LYS B 1 30  ? 146.482 130.791 180.124 1.00 55.90 ?  30  LYS B CE    1 
ATOM   5769  N  NZ    . LYS B 1 30  ? 146.089 131.032 181.539 1.00 55.29 1  30  LYS B NZ    1 
ATOM   5770  N  N     . GLU B 1 31  ? 147.787 126.501 176.231 1.00 53.21 ?  31  GLU B N     1 
ATOM   5771  C  CA    . GLU B 1 31  ? 149.198 126.194 176.034 1.00 52.85 ?  31  GLU B CA    1 
ATOM   5772  C  C     . GLU B 1 31  ? 149.590 126.395 174.578 1.00 52.18 ?  31  GLU B C     1 
ATOM   5773  O  O     . GLU B 1 31  ? 150.620 127.015 174.283 1.00 54.46 ?  31  GLU B O     1 
ATOM   5774  C  CB    . GLU B 1 31  ? 149.490 124.762 176.478 1.00 52.70 ?  31  GLU B CB    1 
ATOM   5775  C  CG    . GLU B 1 31  ? 149.244 124.509 177.957 1.00 54.76 ?  31  GLU B CG    1 
ATOM   5776  C  CD    . GLU B 1 31  ? 149.283 123.035 178.308 1.00 57.88 ?  31  GLU B CD    1 
ATOM   5777  O  OE1   . GLU B 1 31  ? 150.094 122.301 177.708 1.00 59.45 ?  31  GLU B OE1   1 
ATOM   5778  O  OE2   . GLU B 1 31  ? 148.502 122.610 179.185 1.00 56.50 -1 31  GLU B OE2   1 
ATOM   5779  N  N     . ALA B 1 32  ? 148.739 125.933 173.658 1.00 43.56 ?  32  ALA B N     1 
ATOM   5780  C  CA    . ALA B 1 32  ? 149.025 126.079 172.236 1.00 44.58 ?  32  ALA B CA    1 
ATOM   5781  C  C     . ALA B 1 32  ? 149.303 127.532 171.886 1.00 48.74 ?  32  ALA B C     1 
ATOM   5782  O  O     . ALA B 1 32  ? 150.319 127.843 171.250 1.00 50.09 ?  32  ALA B O     1 
ATOM   5783  C  CB    . ALA B 1 32  ? 147.860 125.535 171.408 1.00 44.78 ?  32  ALA B CB    1 
ATOM   5784  N  N     . VAL B 1 33  ? 148.441 128.446 172.349 1.00 49.04 ?  33  VAL B N     1 
ATOM   5785  C  CA    . VAL B 1 33  ? 148.641 129.859 172.038 1.00 47.36 ?  33  VAL B CA    1 
ATOM   5786  C  C     . VAL B 1 33  ? 150.018 130.300 172.506 1.00 47.53 ?  33  VAL B C     1 
ATOM   5787  O  O     . VAL B 1 33  ? 150.777 130.925 171.754 1.00 49.67 ?  33  VAL B O     1 
ATOM   5788  C  CB    . VAL B 1 33  ? 147.532 130.727 172.659 1.00 45.21 ?  33  VAL B CB    1 
ATOM   5789  C  CG1   . VAL B 1 33  ? 147.135 131.835 171.699 1.00 45.04 ?  33  VAL B CG1   1 
ATOM   5790  C  CG2   . VAL B 1 33  ? 146.330 129.890 173.012 1.00 47.96 ?  33  VAL B CG2   1 
ATOM   5791  N  N     . HIS B 1 34  ? 150.380 129.928 173.738 1.00 44.02 ?  34  HIS B N     1 
ATOM   5792  C  CA    . HIS B 1 34  ? 151.705 130.264 174.241 1.00 45.18 ?  34  HIS B CA    1 
ATOM   5793  C  C     . HIS B 1 34  ? 152.776 129.765 173.283 1.00 45.96 ?  34  HIS B C     1 
ATOM   5794  O  O     . HIS B 1 34  ? 153.628 130.540 172.829 1.00 49.13 ?  34  HIS B O     1 
ATOM   5795  C  CB    . HIS B 1 34  ? 151.905 129.676 175.637 1.00 50.39 ?  34  HIS B CB    1 
ATOM   5796  C  CG    . HIS B 1 34  ? 152.878 130.440 176.478 1.00 49.36 ?  34  HIS B CG    1 
ATOM   5797  N  ND1   . HIS B 1 34  ? 154.166 130.006 176.707 1.00 48.47 ?  34  HIS B ND1   1 
ATOM   5798  C  CD2   . HIS B 1 34  ? 152.753 131.613 177.141 1.00 49.42 ?  34  HIS B CD2   1 
ATOM   5799  C  CE1   . HIS B 1 34  ? 154.792 130.878 177.477 1.00 50.02 ?  34  HIS B CE1   1 
ATOM   5800  N  NE2   . HIS B 1 34  ? 153.956 131.863 177.755 1.00 51.44 ?  34  HIS B NE2   1 
ATOM   5801  N  N     . SER B 1 35  ? 152.701 128.486 172.908 1.00 46.26 ?  35  SER B N     1 
ATOM   5802  C  CA    . SER B 1 35  ? 153.642 127.956 171.932 1.00 47.37 ?  35  SER B CA    1 
ATOM   5803  C  C     . SER B 1 35  ? 153.588 128.772 170.651 1.00 46.78 ?  35  SER B C     1 
ATOM   5804  O  O     . SER B 1 35  ? 154.620 129.253 170.163 1.00 50.48 ?  35  SER B O     1 
ATOM   5805  C  CB    . SER B 1 35  ? 153.339 126.483 171.653 1.00 48.20 ?  35  SER B CB    1 
ATOM   5806  O  OG    . SER B 1 35  ? 154.028 126.030 170.503 1.00 48.65 ?  35  SER B OG    1 
ATOM   5807  N  N     . TYR B 1 36  ? 152.374 129.014 170.144 1.00 47.40 ?  36  TYR B N     1 
ATOM   5808  C  CA    . TYR B 1 36  ? 152.219 129.738 168.890 1.00 45.60 ?  36  TYR B CA    1 
ATOM   5809  C  C     . TYR B 1 36  ? 152.864 131.112 168.962 1.00 46.42 ?  36  TYR B C     1 
ATOM   5810  O  O     . TYR B 1 36  ? 153.260 131.666 167.932 1.00 47.08 ?  36  TYR B O     1 
ATOM   5811  C  CB    . TYR B 1 36  ? 150.736 129.863 168.537 1.00 44.83 ?  36  TYR B CB    1 
ATOM   5812  C  CG    . TYR B 1 36  ? 150.471 130.490 167.188 1.00 45.26 ?  36  TYR B CG    1 
ATOM   5813  C  CD1   . TYR B 1 36  ? 150.966 129.918 166.024 1.00 44.63 ?  36  TYR B CD1   1 
ATOM   5814  C  CD2   . TYR B 1 36  ? 149.721 131.653 167.078 1.00 42.99 ?  36  TYR B CD2   1 
ATOM   5815  C  CE1   . TYR B 1 36  ? 150.723 130.485 164.790 1.00 43.22 ?  36  TYR B CE1   1 
ATOM   5816  C  CE2   . TYR B 1 36  ? 149.473 132.228 165.848 1.00 44.18 ?  36  TYR B CE2   1 
ATOM   5817  C  CZ    . TYR B 1 36  ? 149.977 131.640 164.708 1.00 44.46 ?  36  TYR B CZ    1 
ATOM   5818  O  OH    . TYR B 1 36  ? 149.732 132.211 163.479 1.00 43.59 ?  36  TYR B OH    1 
ATOM   5819  N  N     . PHE B 1 37  ? 152.995 131.666 170.165 1.00 49.89 ?  37  PHE B N     1 
ATOM   5820  C  CA    . PHE B 1 37  ? 153.659 132.952 170.308 1.00 49.17 ?  37  PHE B CA    1 
ATOM   5821  C  C     . PHE B 1 37  ? 155.135 132.805 170.645 1.00 51.17 ?  37  PHE B C     1 
ATOM   5822  O  O     . PHE B 1 37  ? 155.952 133.602 170.176 1.00 55.25 ?  37  PHE B O     1 
ATOM   5823  C  CB    . PHE B 1 37  ? 152.950 133.794 171.370 1.00 49.72 ?  37  PHE B CB    1 
ATOM   5824  C  CG    . PHE B 1 37  ? 151.756 134.533 170.846 1.00 50.79 ?  37  PHE B CG    1 
ATOM   5825  C  CD1   . PHE B 1 37  ? 151.906 135.754 170.213 1.00 51.43 ?  37  PHE B CD1   1 
ATOM   5826  C  CD2   . PHE B 1 37  ? 150.486 133.999 170.969 1.00 50.28 ?  37  PHE B CD2   1 
ATOM   5827  C  CE1   . PHE B 1 37  ? 150.810 136.433 169.723 1.00 50.45 ?  37  PHE B CE1   1 
ATOM   5828  C  CE2   . PHE B 1 37  ? 149.387 134.675 170.481 1.00 48.78 ?  37  PHE B CE2   1 
ATOM   5829  C  CZ    . PHE B 1 37  ? 149.550 135.892 169.855 1.00 48.83 ?  37  PHE B CZ    1 
ATOM   5830  N  N     . VAL B 1 38  ? 155.508 131.793 171.435 1.00 52.14 ?  38  VAL B N     1 
ATOM   5831  C  CA    . VAL B 1 38  ? 156.909 131.681 171.842 1.00 51.44 ?  38  VAL B CA    1 
ATOM   5832  C  C     . VAL B 1 38  ? 157.759 130.955 170.815 1.00 53.54 ?  38  VAL B C     1 
ATOM   5833  O  O     . VAL B 1 38  ? 158.983 130.888 170.977 1.00 56.53 ?  38  VAL B O     1 
ATOM   5834  C  CB    . VAL B 1 38  ? 157.065 130.976 173.203 1.00 50.73 ?  38  VAL B CB    1 
ATOM   5835  C  CG1   . VAL B 1 38  ? 156.241 131.687 174.268 1.00 50.91 ?  38  VAL B CG1   1 
ATOM   5836  C  CG2   . VAL B 1 38  ? 156.684 129.511 173.097 1.00 49.68 ?  38  VAL B CG2   1 
ATOM   5837  N  N     . ASP B 1 39  ? 157.151 130.413 169.765 1.00 50.18 ?  39  ASP B N     1 
ATOM   5838  C  CA    . ASP B 1 39  ? 157.884 129.705 168.730 1.00 51.31 ?  39  ASP B CA    1 
ATOM   5839  C  C     . ASP B 1 39  ? 157.678 130.262 167.330 1.00 53.35 ?  39  ASP B C     1 
ATOM   5840  O  O     . ASP B 1 39  ? 158.569 130.113 166.492 1.00 56.10 ?  39  ASP B O     1 
ATOM   5841  C  CB    . ASP B 1 39  ? 157.503 128.215 168.729 1.00 52.76 ?  39  ASP B CB    1 
ATOM   5842  C  CG    . ASP B 1 39  ? 157.606 127.587 170.104 1.00 54.28 ?  39  ASP B CG    1 
ATOM   5843  O  OD1   . ASP B 1 39  ? 158.528 127.955 170.859 1.00 54.59 ?  39  ASP B OD1   1 
ATOM   5844  O  OD2   . ASP B 1 39  ? 156.764 126.723 170.428 1.00 53.25 -1 39  ASP B OD2   1 
ATOM   5845  N  N     . TYR B 1 40  ? 156.537 130.892 167.047 1.00 53.18 ?  40  TYR B N     1 
ATOM   5846  C  CA    . TYR B 1 40  ? 156.267 131.406 165.708 1.00 53.04 ?  40  TYR B CA    1 
ATOM   5847  C  C     . TYR B 1 40  ? 156.086 132.918 165.679 1.00 55.10 ?  40  TYR B C     1 
ATOM   5848  O  O     . TYR B 1 40  ? 156.786 133.596 164.921 1.00 55.56 ?  40  TYR B O     1 
ATOM   5849  C  CB    . TYR B 1 40  ? 155.032 130.714 165.119 1.00 52.98 ?  40  TYR B CB    1 
ATOM   5850  C  CG    . TYR B 1 40  ? 154.892 130.896 163.625 1.00 52.53 ?  40  TYR B CG    1 
ATOM   5851  C  CD1   . TYR B 1 40  ? 155.647 130.136 162.741 1.00 53.26 ?  40  TYR B CD1   1 
ATOM   5852  C  CD2   . TYR B 1 40  ? 154.010 131.830 163.098 1.00 51.96 ?  40  TYR B CD2   1 
ATOM   5853  C  CE1   . TYR B 1 40  ? 155.524 130.299 161.375 1.00 55.40 ?  40  TYR B CE1   1 
ATOM   5854  C  CE2   . TYR B 1 40  ? 153.881 132.001 161.733 1.00 52.85 ?  40  TYR B CE2   1 
ATOM   5855  C  CZ    . TYR B 1 40  ? 154.641 131.232 160.876 1.00 56.50 ?  40  TYR B CZ    1 
ATOM   5856  O  OH    . TYR B 1 40  ? 154.516 131.396 159.515 1.00 57.66 ?  40  TYR B OH    1 
ATOM   5857  N  N     . ILE B 1 41  ? 155.171 133.472 166.476 1.00 55.05 ?  41  ILE B N     1 
ATOM   5858  C  CA    . ILE B 1 41  ? 154.795 134.874 166.305 1.00 53.28 ?  41  ILE B CA    1 
ATOM   5859  C  C     . ILE B 1 41  ? 155.927 135.796 166.739 1.00 52.04 ?  41  ILE B C     1 
ATOM   5860  O  O     . ILE B 1 41  ? 156.274 136.749 166.031 1.00 54.19 ?  41  ILE B O     1 
ATOM   5861  C  CB    . ILE B 1 41  ? 153.493 135.181 167.065 1.00 50.85 ?  41  ILE B CB    1 
ATOM   5862  C  CG1   . ILE B 1 41  ? 152.346 134.326 166.524 1.00 48.55 ?  41  ILE B CG1   1 
ATOM   5863  C  CG2   . ILE B 1 41  ? 153.146 136.657 166.951 1.00 49.09 ?  41  ILE B CG2   1 
ATOM   5864  C  CD1   . ILE B 1 41  ? 152.199 134.386 165.022 1.00 49.11 ?  41  ILE B CD1   1 
ATOM   5865  N  N     . ASN B 1 42  ? 156.524 135.531 167.904 1.00 50.52 ?  42  ASN B N     1 
ATOM   5866  C  CA    . ASN B 1 42  ? 157.594 136.399 168.385 1.00 51.96 ?  42  ASN B CA    1 
ATOM   5867  C  C     . ASN B 1 42  ? 158.837 136.298 167.513 1.00 54.31 ?  42  ASN B C     1 
ATOM   5868  O  O     . ASN B 1 42  ? 159.572 137.281 167.367 1.00 54.08 ?  42  ASN B O     1 
ATOM   5869  C  CB    . ASN B 1 42  ? 157.932 136.068 169.837 1.00 53.11 ?  42  ASN B CB    1 
ATOM   5870  C  CG    . ASN B 1 42  ? 156.803 136.407 170.790 1.00 53.45 ?  42  ASN B CG    1 
ATOM   5871  O  OD1   . ASN B 1 42  ? 155.832 137.061 170.411 1.00 56.58 ?  42  ASN B OD1   1 
ATOM   5872  N  ND2   . ASN B 1 42  ? 156.925 135.962 172.035 1.00 53.35 ?  42  ASN B ND2   1 
ATOM   5873  N  N     . GLN B 1 43  ? 159.094 135.125 166.931 1.00 58.65 ?  43  GLN B N     1 
ATOM   5874  C  CA    . GLN B 1 43  ? 160.234 134.978 166.034 1.00 57.83 ?  43  GLN B CA    1 
ATOM   5875  C  C     . GLN B 1 43  ? 159.961 135.596 164.668 1.00 56.26 ?  43  GLN B C     1 
ATOM   5876  O  O     . GLN B 1 43  ? 160.867 136.167 164.052 1.00 58.13 ?  43  GLN B O     1 
ATOM   5877  C  CB    . GLN B 1 43  ? 160.602 133.501 165.890 1.00 58.46 ?  43  GLN B CB    1 
ATOM   5878  C  CG    . GLN B 1 43  ? 161.638 133.024 166.893 1.00 58.98 ?  43  GLN B CG    1 
ATOM   5879  C  CD    . GLN B 1 43  ? 161.028 132.636 168.225 1.00 60.06 ?  43  GLN B CD    1 
ATOM   5880  O  OE1   . GLN B 1 43  ? 160.604 131.498 168.417 1.00 59.73 ?  43  GLN B OE1   1 
ATOM   5881  N  NE2   . GLN B 1 43  ? 160.983 133.583 169.154 1.00 59.72 ?  43  GLN B NE2   1 
ATOM   5882  N  N     . ASN B 1 44  ? 158.727 135.495 164.180 1.00 56.45 ?  44  ASN B N     1 
ATOM   5883  C  CA    . ASN B 1 44  ? 158.369 136.022 162.871 1.00 56.94 ?  44  ASN B CA    1 
ATOM   5884  C  C     . ASN B 1 44  ? 157.962 137.488 162.909 1.00 55.64 ?  44  ASN B C     1 
ATOM   5885  O  O     . ASN B 1 44  ? 157.738 138.081 161.849 1.00 56.35 ?  44  ASN B O     1 
ATOM   5886  C  CB    . ASN B 1 44  ? 157.235 135.193 162.258 1.00 55.57 ?  44  ASN B CB    1 
ATOM   5887  C  CG    . ASN B 1 44  ? 157.746 134.051 161.404 1.00 56.91 ?  44  ASN B CG    1 
ATOM   5888  O  OD1   . ASN B 1 44  ? 158.705 133.370 161.769 1.00 58.79 ?  44  ASN B OD1   1 
ATOM   5889  N  ND2   . ASN B 1 44  ? 157.106 133.833 160.262 1.00 58.76 ?  44  ASN B ND2   1 
ATOM   5890  N  N     . THR B 1 45  ? 157.856 138.086 164.091 1.00 55.50 ?  45  THR B N     1 
ATOM   5891  C  CA    . THR B 1 45  ? 157.536 139.501 164.182 1.00 56.66 ?  45  THR B CA    1 
ATOM   5892  C  C     . THR B 1 45  ? 158.772 140.343 163.890 1.00 57.37 ?  45  THR B C     1 
ATOM   5893  O  O     . THR B 1 45  ? 159.911 139.908 164.086 1.00 60.83 ?  45  THR B O     1 
ATOM   5894  C  CB    . THR B 1 45  ? 156.966 139.845 165.564 1.00 56.50 ?  45  THR B CB    1 
ATOM   5895  O  OG1   . THR B 1 45  ? 156.467 141.187 165.557 1.00 56.05 ?  45  THR B OG1   1 
ATOM   5896  C  CG2   . THR B 1 45  ? 158.025 139.707 166.650 1.00 55.69 ?  45  THR B CG2   1 
ATOM   5897  N  N     . VAL B 1 46  ? 158.537 141.549 163.384 1.00 56.32 ?  46  VAL B N     1 
ATOM   5898  C  CA    . VAL B 1 46  ? 159.602 142.496 163.079 1.00 57.35 ?  46  VAL B CA    1 
ATOM   5899  C  C     . VAL B 1 46  ? 159.593 143.572 164.155 1.00 57.06 ?  46  VAL B C     1 
ATOM   5900  O  O     . VAL B 1 46  ? 158.621 144.327 164.283 1.00 58.31 ?  46  VAL B O     1 
ATOM   5901  C  CB    . VAL B 1 46  ? 159.429 143.108 161.680 1.00 56.58 ?  46  VAL B CB    1 
ATOM   5902  C  CG1   . VAL B 1 46  ? 160.316 144.330 161.523 1.00 55.16 ?  46  VAL B CG1   1 
ATOM   5903  C  CG2   . VAL B 1 46  ? 159.746 142.080 160.612 1.00 55.55 ?  46  VAL B CG2   1 
ATOM   5904  N  N     . PHE B 1 47  ? 160.669 143.642 164.930 1.00 58.54 ?  47  PHE B N     1 
ATOM   5905  C  CA    . PHE B 1 47  ? 160.782 144.603 166.014 1.00 60.28 ?  47  PHE B CA    1 
ATOM   5906  C  C     . PHE B 1 47  ? 161.699 145.751 165.616 1.00 60.60 ?  47  PHE B C     1 
ATOM   5907  O  O     . PHE B 1 47  ? 162.709 145.560 164.934 1.00 61.43 ?  47  PHE B O     1 
ATOM   5908  C  CB    . PHE B 1 47  ? 161.307 143.937 167.287 1.00 60.54 ?  47  PHE B CB    1 
ATOM   5909  C  CG    . PHE B 1 47  ? 161.006 144.707 168.541 1.00 60.62 ?  47  PHE B CG    1 
ATOM   5910  C  CD1   . PHE B 1 47  ? 159.700 145.010 168.887 1.00 59.97 ?  47  PHE B CD1   1 
ATOM   5911  C  CD2   . PHE B 1 47  ? 162.031 145.132 169.372 1.00 60.05 ?  47  PHE B CD2   1 
ATOM   5912  C  CE1   . PHE B 1 47  ? 159.420 145.718 170.041 1.00 60.86 ?  47  PHE B CE1   1 
ATOM   5913  C  CE2   . PHE B 1 47  ? 161.757 145.840 170.526 1.00 60.57 ?  47  PHE B CE2   1 
ATOM   5914  C  CZ    . PHE B 1 47  ? 160.451 146.135 170.860 1.00 61.43 ?  47  PHE B CZ    1 
ATOM   5915  N  N     . PHE B 1 48  ? 161.332 146.951 166.051 1.00 56.81 ?  48  PHE B N     1 
ATOM   5916  C  CA    . PHE B 1 48  ? 162.108 148.155 165.807 1.00 56.47 ?  48  PHE B CA    1 
ATOM   5917  C  C     . PHE B 1 48  ? 162.608 148.707 167.134 1.00 59.30 ?  48  PHE B C     1 
ATOM   5918  O  O     . PHE B 1 48  ? 162.174 148.283 168.209 1.00 59.94 ?  48  PHE B O     1 
ATOM   5919  C  CB    . PHE B 1 48  ? 161.280 149.217 165.069 1.00 56.72 ?  48  PHE B CB    1 
ATOM   5920  C  CG    . PHE B 1 48  ? 160.770 148.770 163.727 1.00 57.71 ?  48  PHE B CG    1 
ATOM   5921  C  CD1   . PHE B 1 48  ? 159.672 147.930 163.629 1.00 56.37 ?  48  PHE B CD1   1 
ATOM   5922  C  CD2   . PHE B 1 48  ? 161.386 149.194 162.563 1.00 57.45 ?  48  PHE B CD2   1 
ATOM   5923  C  CE1   . PHE B 1 48  ? 159.201 147.523 162.396 1.00 56.89 ?  48  PHE B CE1   1 
ATOM   5924  C  CE2   . PHE B 1 48  ? 160.920 148.788 161.328 1.00 56.57 ?  48  PHE B CE2   1 
ATOM   5925  C  CZ    . PHE B 1 48  ? 159.827 147.952 161.244 1.00 56.22 ?  48  PHE B CZ    1 
ATOM   5926  N  N     . HIS B 1 49  ? 163.541 149.659 167.049 1.00 62.05 ?  49  HIS B N     1 
ATOM   5927  C  CA    . HIS B 1 49  ? 164.099 150.248 168.262 1.00 62.83 ?  49  HIS B CA    1 
ATOM   5928  C  C     . HIS B 1 49  ? 163.023 150.964 169.071 1.00 63.07 ?  49  HIS B C     1 
ATOM   5929  O  O     . HIS B 1 49  ? 162.977 150.842 170.300 1.00 64.37 ?  49  HIS B O     1 
ATOM   5930  C  CB    . HIS B 1 49  ? 165.236 151.206 167.909 1.00 64.35 ?  49  HIS B CB    1 
ATOM   5931  C  CG    . HIS B 1 49  ? 165.935 151.775 169.104 1.00 65.21 ?  49  HIS B CG    1 
ATOM   5932  N  ND1   . HIS B 1 49  ? 166.457 150.985 170.105 1.00 63.91 ?  49  HIS B ND1   1 
ATOM   5933  C  CD2   . HIS B 1 49  ? 166.195 153.056 169.460 1.00 63.74 ?  49  HIS B CD2   1 
ATOM   5934  C  CE1   . HIS B 1 49  ? 167.012 151.755 171.026 1.00 63.98 ?  49  HIS B CE1   1 
ATOM   5935  N  NE2   . HIS B 1 49  ? 166.865 153.015 170.658 1.00 63.41 ?  49  HIS B NE2   1 
ATOM   5936  N  N     . ASN B 1 50  ? 162.151 151.710 168.398 1.00 61.05 ?  50  ASN B N     1 
ATOM   5937  C  CA    . ASN B 1 50  ? 161.005 152.330 169.044 1.00 62.50 ?  50  ASN B CA    1 
ATOM   5938  C  C     . ASN B 1 50  ? 159.878 152.438 168.024 1.00 60.99 ?  50  ASN B C     1 
ATOM   5939  O  O     . ASN B 1 50  ? 160.004 151.993 166.880 1.00 58.84 ?  50  ASN B O     1 
ATOM   5940  C  CB    . ASN B 1 50  ? 161.365 153.694 169.644 1.00 61.56 ?  50  ASN B CB    1 
ATOM   5941  C  CG    . ASN B 1 50  ? 162.045 154.609 168.648 1.00 62.99 ?  50  ASN B CG    1 
ATOM   5942  O  OD1   . ASN B 1 50  ? 162.282 154.232 167.503 1.00 62.27 ?  50  ASN B OD1   1 
ATOM   5943  N  ND2   . ASN B 1 50  ? 162.360 155.824 169.080 1.00 63.03 ?  50  ASN B ND2   1 
ATOM   5944  N  N     . LEU B 1 51  ? 158.765 153.036 168.453 1.00 55.35 ?  51  LEU B N     1 
ATOM   5945  C  CA    . LEU B 1 51  ? 157.600 153.145 167.582 1.00 54.03 ?  51  LEU B CA    1 
ATOM   5946  C  C     . LEU B 1 51  ? 157.859 154.075 166.403 1.00 56.24 ?  51  LEU B C     1 
ATOM   5947  O  O     . LEU B 1 51  ? 157.236 153.921 165.346 1.00 56.85 ?  51  LEU B O     1 
ATOM   5948  C  CB    . LEU B 1 51  ? 156.393 153.625 168.387 1.00 55.44 ?  51  LEU B CB    1 
ATOM   5949  C  CG    . LEU B 1 51  ? 155.042 153.650 167.672 1.00 53.80 ?  51  LEU B CG    1 
ATOM   5950  C  CD1   . LEU B 1 51  ? 154.630 152.248 167.250 1.00 51.80 ?  51  LEU B CD1   1 
ATOM   5951  C  CD2   . LEU B 1 51  ? 153.987 154.279 168.561 1.00 53.40 ?  51  LEU B CD2   1 
ATOM   5952  N  N     . LYS B 1 52  ? 158.764 155.044 166.565 1.00 56.71 ?  52  LYS B N     1 
ATOM   5953  C  CA    . LYS B 1 52  ? 159.041 155.987 165.484 1.00 55.26 ?  52  LYS B CA    1 
ATOM   5954  C  C     . LYS B 1 52  ? 159.605 155.274 164.262 1.00 56.32 ?  52  LYS B C     1 
ATOM   5955  O  O     . LYS B 1 52  ? 159.165 155.513 163.132 1.00 57.80 ?  52  LYS B O     1 
ATOM   5956  C  CB    . LYS B 1 52  ? 160.007 157.069 165.968 1.00 56.33 ?  52  LYS B CB    1 
ATOM   5957  C  CG    . LYS B 1 52  ? 159.475 158.486 165.822 1.00 57.26 ?  52  LYS B CG    1 
ATOM   5958  C  CD    . LYS B 1 52  ? 159.357 158.889 164.363 1.00 58.35 ?  52  LYS B CD    1 
ATOM   5959  C  CE    . LYS B 1 52  ? 158.535 160.160 164.210 1.00 58.29 ?  52  LYS B CE    1 
ATOM   5960  N  NZ    . LYS B 1 52  ? 158.279 160.488 162.780 1.00 58.58 1  52  LYS B NZ    1 
ATOM   5961  N  N     . GLU B 1 53  ? 160.584 154.389 164.472 1.00 59.10 ?  53  GLU B N     1 
ATOM   5962  C  CA    . GLU B 1 53  ? 161.167 153.656 163.353 1.00 59.32 ?  53  GLU B CA    1 
ATOM   5963  C  C     . GLU B 1 53  ? 160.139 152.744 162.698 1.00 57.39 ?  53  GLU B C     1 
ATOM   5964  O  O     . GLU B 1 53  ? 160.107 152.618 161.470 1.00 59.82 ?  53  GLU B O     1 
ATOM   5965  C  CB    . GLU B 1 53  ? 162.380 152.852 163.819 1.00 59.95 ?  53  GLU B CB    1 
ATOM   5966  C  CG    . GLU B 1 53  ? 163.375 153.651 164.637 1.00 60.72 ?  53  GLU B CG    1 
ATOM   5967  C  CD    . GLU B 1 53  ? 164.812 153.317 164.294 1.00 62.00 ?  53  GLU B CD    1 
ATOM   5968  O  OE1   . GLU B 1 53  ? 165.214 152.150 164.487 1.00 62.82 ?  53  GLU B OE1   1 
ATOM   5969  O  OE2   . GLU B 1 53  ? 165.538 154.220 163.830 1.00 61.66 -1 53  GLU B OE2   1 
ATOM   5970  N  N     . LYS B 1 54  ? 159.291 152.099 163.501 1.00 54.54 ?  54  LYS B N     1 
ATOM   5971  C  CA    . LYS B 1 54  ? 158.254 151.235 162.947 1.00 54.20 ?  54  LYS B CA    1 
ATOM   5972  C  C     . LYS B 1 54  ? 157.294 152.026 162.069 1.00 52.54 ?  54  LYS B C     1 
ATOM   5973  O  O     . LYS B 1 54  ? 156.984 151.618 160.942 1.00 52.90 ?  54  LYS B O     1 
ATOM   5974  C  CB    . LYS B 1 54  ? 157.496 150.540 164.077 1.00 53.29 ?  54  LYS B CB    1 
ATOM   5975  C  CG    . LYS B 1 54  ? 156.267 149.782 163.615 1.00 54.25 ?  54  LYS B CG    1 
ATOM   5976  C  CD    . LYS B 1 54  ? 155.875 148.717 164.616 1.00 53.22 ?  54  LYS B CD    1 
ATOM   5977  C  CE    . LYS B 1 54  ? 154.676 147.924 164.137 1.00 53.86 ?  54  LYS B CE    1 
ATOM   5978  N  NZ    . LYS B 1 54  ? 154.623 146.576 164.765 1.00 54.25 1  54  LYS B NZ    1 
ATOM   5979  N  N     . LEU B 1 55  ? 156.815 153.165 162.572 1.00 52.77 ?  55  LEU B N     1 
ATOM   5980  C  CA    . LEU B 1 55  ? 155.880 153.976 161.800 1.00 53.11 ?  55  LEU B CA    1 
ATOM   5981  C  C     . LEU B 1 55  ? 156.531 154.517 160.535 1.00 56.57 ?  55  LEU B C     1 
ATOM   5982  O  O     . LEU B 1 55  ? 155.907 154.527 159.469 1.00 60.90 ?  55  LEU B O     1 
ATOM   5983  C  CB    . LEU B 1 55  ? 155.340 155.117 162.659 1.00 55.67 ?  55  LEU B CB    1 
ATOM   5984  C  CG    . LEU B 1 55  ? 154.174 154.770 163.585 1.00 55.50 ?  55  LEU B CG    1 
ATOM   5985  C  CD1   . LEU B 1 55  ? 153.389 156.024 163.914 1.00 56.44 ?  55  LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B 1 55  ? 153.270 153.718 162.960 1.00 54.78 ?  55  LEU B CD2   1 
ATOM   5987  N  N     . ASP B 1 56  ? 157.785 154.968 160.628 1.00 56.68 ?  56  ASP B N     1 
ATOM   5988  C  CA    . ASP B 1 56  ? 158.474 155.466 159.443 1.00 56.24 ?  56  ASP B CA    1 
ATOM   5989  C  C     . ASP B 1 56  ? 158.653 154.363 158.406 1.00 57.03 ?  56  ASP B C     1 
ATOM   5990  O  O     . ASP B 1 56  ? 158.417 154.580 157.213 1.00 57.75 ?  56  ASP B O     1 
ATOM   5991  C  CB    . ASP B 1 56  ? 159.825 156.063 159.833 1.00 59.58 ?  56  ASP B CB    1 
ATOM   5992  C  CG    . ASP B 1 56  ? 159.687 157.280 160.726 1.00 60.61 ?  56  ASP B CG    1 
ATOM   5993  O  OD1   . ASP B 1 56  ? 158.546 157.748 160.924 1.00 61.48 ?  56  ASP B OD1   1 
ATOM   5994  O  OD2   . ASP B 1 56  ? 160.719 157.768 161.232 1.00 59.36 -1 56  ASP B OD2   1 
ATOM   5995  N  N     . TYR B 1 57  ? 159.060 153.169 158.844 1.00 55.74 ?  57  TYR B N     1 
ATOM   5996  C  CA    . TYR B 1 57  ? 159.241 152.062 157.912 1.00 56.06 ?  57  TYR B CA    1 
ATOM   5997  C  C     . TYR B 1 57  ? 157.923 151.684 157.251 1.00 56.30 ?  57  TYR B C     1 
ATOM   5998  O  O     . TYR B 1 57  ? 157.883 151.403 156.048 1.00 60.11 ?  57  TYR B O     1 
ATOM   5999  C  CB    . TYR B 1 57  ? 159.846 150.859 158.638 1.00 55.53 ?  57  TYR B CB    1 
ATOM   6000  C  CG    . TYR B 1 57  ? 159.895 149.591 157.814 1.00 56.81 ?  57  TYR B CG    1 
ATOM   6001  C  CD1   . TYR B 1 57  ? 160.966 149.331 156.971 1.00 57.13 ?  57  TYR B CD1   1 
ATOM   6002  C  CD2   . TYR B 1 57  ? 158.876 148.648 157.886 1.00 59.01 ?  57  TYR B CD2   1 
ATOM   6003  C  CE1   . TYR B 1 57  ? 161.019 148.175 156.216 1.00 57.09 ?  57  TYR B CE1   1 
ATOM   6004  C  CE2   . TYR B 1 57  ? 158.920 147.491 157.135 1.00 59.36 ?  57  TYR B CE2   1 
ATOM   6005  C  CZ    . TYR B 1 57  ? 159.994 147.257 156.303 1.00 59.35 ?  57  TYR B CZ    1 
ATOM   6006  O  OH    . TYR B 1 57  ? 160.040 146.104 155.554 1.00 59.74 ?  57  TYR B OH    1 
ATOM   6007  N  N     . LEU B 1 58  ? 156.833 151.672 158.018 1.00 53.38 ?  58  LEU B N     1 
ATOM   6008  C  CA    . LEU B 1 58  ? 155.540 151.320 157.442 1.00 52.61 ?  58  LEU B CA    1 
ATOM   6009  C  C     . LEU B 1 58  ? 155.006 152.421 156.532 1.00 51.55 ?  58  LEU B C     1 
ATOM   6010  O  O     . LEU B 1 58  ? 154.215 152.141 155.626 1.00 53.00 ?  58  LEU B O     1 
ATOM   6011  C  CB    . LEU B 1 58  ? 154.541 151.006 158.555 1.00 52.55 ?  58  LEU B CB    1 
ATOM   6012  C  CG    . LEU B 1 58  ? 154.868 149.749 159.366 1.00 52.17 ?  58  LEU B CG    1 
ATOM   6013  C  CD1   . LEU B 1 58  ? 154.103 149.727 160.677 1.00 52.11 ?  58  LEU B CD1   1 
ATOM   6014  C  CD2   . LEU B 1 58  ? 154.582 148.496 158.555 1.00 53.03 ?  58  LEU B CD2   1 
ATOM   6015  N  N     . VAL B 1 59  ? 155.421 153.668 156.750 1.00 55.47 ?  59  VAL B N     1 
ATOM   6016  C  CA    . VAL B 1 59  ? 154.924 154.764 155.926 1.00 56.82 ?  59  VAL B CA    1 
ATOM   6017  C  C     . VAL B 1 59  ? 155.686 154.844 154.608 1.00 57.98 ?  59  VAL B C     1 
ATOM   6018  O  O     . VAL B 1 59  ? 155.081 154.913 153.531 1.00 56.51 ?  59  VAL B O     1 
ATOM   6019  C  CB    . VAL B 1 59  ? 154.992 156.090 156.705 1.00 56.13 ?  59  VAL B CB    1 
ATOM   6020  C  CG1   . VAL B 1 59  ? 155.053 157.273 155.750 1.00 55.82 ?  59  VAL B CG1   1 
ATOM   6021  C  CG2   . VAL B 1 59  ? 153.798 156.216 157.638 1.00 55.43 ?  59  VAL B CG2   1 
ATOM   6022  N  N     . GLU B 1 60  ? 157.022 154.834 154.665 1.00 59.74 ?  60  GLU B N     1 
ATOM   6023  C  CA    . GLU B 1 60  ? 157.801 154.974 153.436 1.00 59.69 ?  60  GLU B CA    1 
ATOM   6024  C  C     . GLU B 1 60  ? 157.702 153.740 152.547 1.00 59.71 ?  60  GLU B C     1 
ATOM   6025  O  O     . GLU B 1 60  ? 157.800 153.858 151.320 1.00 61.21 ?  60  GLU B O     1 
ATOM   6026  C  CB    . GLU B 1 60  ? 159.267 155.279 153.750 1.00 59.21 ?  60  GLU B CB    1 
ATOM   6027  C  CG    . GLU B 1 60  ? 159.487 156.263 154.884 1.00 60.66 ?  60  GLU B CG    1 
ATOM   6028  C  CD    . GLU B 1 60  ? 160.689 155.905 155.738 1.00 62.93 ?  60  GLU B CD    1 
ATOM   6029  O  OE1   . GLU B 1 60  ? 161.127 156.758 156.538 1.00 59.92 ?  60  GLU B OE1   1 
ATOM   6030  O  OE2   . GLU B 1 60  ? 161.196 154.771 155.608 1.00 61.95 -1 60  GLU B OE2   1 
ATOM   6031  N  N     . ASN B 1 61  ? 157.516 152.558 153.132 1.00 55.81 ?  61  ASN B N     1 
ATOM   6032  C  CA    . ASN B 1 61  ? 157.405 151.327 152.362 1.00 56.10 ?  61  ASN B CA    1 
ATOM   6033  C  C     . ASN B 1 61  ? 155.990 151.077 151.853 1.00 56.29 ?  61  ASN B C     1 
ATOM   6034  O  O     . ASN B 1 61  ? 155.672 149.948 151.463 1.00 58.43 ?  61  ASN B O     1 
ATOM   6035  C  CB    . ASN B 1 61  ? 157.885 150.137 153.193 1.00 56.83 ?  61  ASN B CB    1 
ATOM   6036  C  CG    . ASN B 1 61  ? 159.389 150.128 153.378 1.00 58.89 ?  61  ASN B CG    1 
ATOM   6037  O  OD1   . ASN B 1 61  ? 160.111 149.453 152.646 1.00 58.92 ?  61  ASN B OD1   1 
ATOM   6038  N  ND2   . ASN B 1 61  ? 159.868 150.886 154.357 1.00 58.89 ?  61  ASN B ND2   1 
ATOM   6039  N  N     . GLN B 1 62  ? 155.142 152.108 151.851 1.00 55.77 ?  62  GLN B N     1 
ATOM   6040  C  CA    . GLN B 1 62  ? 153.788 152.037 151.298 1.00 57.06 ?  62  GLN B CA    1 
ATOM   6041  C  C     . GLN B 1 62  ? 152.953 150.953 151.976 1.00 55.48 ?  62  GLN B C     1 
ATOM   6042  O  O     . GLN B 1 62  ? 152.140 150.279 151.340 1.00 56.00 ?  62  GLN B O     1 
ATOM   6043  C  CB    . GLN B 1 62  ? 153.821 151.829 149.781 1.00 54.59 ?  62  GLN B CB    1 
ATOM   6044  C  CG    . GLN B 1 62  ? 154.759 152.773 149.046 1.00 55.59 ?  62  GLN B CG    1 
ATOM   6045  C  CD    . GLN B 1 62  ? 154.588 154.219 149.471 1.00 58.59 ?  62  GLN B CD    1 
ATOM   6046  O  OE1   . GLN B 1 62  ? 153.573 154.850 149.175 1.00 58.31 ?  62  GLN B OE1   1 
ATOM   6047  N  NE2   . GLN B 1 62  ? 155.583 154.753 150.170 1.00 57.60 ?  62  GLN B NE2   1 
ATOM   6048  N  N     . TYR B 1 63  ? 153.154 150.781 153.281 1.00 52.92 ?  63  TYR B N     1 
ATOM   6049  C  CA    . TYR B 1 63  ? 152.282 149.924 154.075 1.00 52.23 ?  63  TYR B CA    1 
ATOM   6050  C  C     . TYR B 1 63  ? 151.132 150.709 154.690 1.00 52.08 ?  63  TYR B C     1 
ATOM   6051  O  O     . TYR B 1 63  ? 150.006 150.206 154.763 1.00 51.06 ?  63  TYR B O     1 
ATOM   6052  C  CB    . TYR B 1 63  ? 153.075 149.228 155.184 1.00 51.41 ?  63  TYR B CB    1 
ATOM   6053  C  CG    . TYR B 1 63  ? 153.993 148.132 154.702 1.00 53.74 ?  63  TYR B CG    1 
ATOM   6054  C  CD1   . TYR B 1 63  ? 153.486 146.993 154.094 1.00 51.61 ?  63  TYR B CD1   1 
ATOM   6055  C  CD2   . TYR B 1 63  ? 155.367 148.232 154.865 1.00 53.83 ?  63  TYR B CD2   1 
ATOM   6056  C  CE1   . TYR B 1 63  ? 154.323 145.987 153.656 1.00 54.06 ?  63  TYR B CE1   1 
ATOM   6057  C  CE2   . TYR B 1 63  ? 156.212 147.233 154.431 1.00 52.91 ?  63  TYR B CE2   1 
ATOM   6058  C  CZ    . TYR B 1 63  ? 155.686 146.113 153.826 1.00 55.02 ?  63  TYR B CZ    1 
ATOM   6059  O  OH    . TYR B 1 63  ? 156.529 145.117 153.392 1.00 55.71 ?  63  TYR B OH    1 
ATOM   6060  N  N     . TYR B 1 64  ? 151.400 151.934 155.131 1.00 49.23 ?  64  TYR B N     1 
ATOM   6061  C  CA    . TYR B 1 64  ? 150.417 152.777 155.791 1.00 46.99 ?  64  TYR B CA    1 
ATOM   6062  C  C     . TYR B 1 64  ? 150.185 154.047 154.987 1.00 48.94 ?  64  TYR B C     1 
ATOM   6063  O  O     . TYR B 1 64  ? 151.098 154.568 154.340 1.00 50.62 ?  64  TYR B O     1 
ATOM   6064  C  CB    . TYR B 1 64  ? 150.869 153.159 157.203 1.00 47.69 ?  64  TYR B CB    1 
ATOM   6065  C  CG    . TYR B 1 64  ? 150.695 152.075 158.235 1.00 47.26 ?  64  TYR B CG    1 
ATOM   6066  C  CD1   . TYR B 1 64  ? 150.086 150.869 157.913 1.00 47.65 ?  64  TYR B CD1   1 
ATOM   6067  C  CD2   . TYR B 1 64  ? 151.143 152.258 159.533 1.00 47.78 ?  64  TYR B CD2   1 
ATOM   6068  C  CE1   . TYR B 1 64  ? 149.928 149.878 158.859 1.00 45.62 ?  64  TYR B CE1   1 
ATOM   6069  C  CE2   . TYR B 1 64  ? 150.991 151.276 160.481 1.00 48.04 ?  64  TYR B CE2   1 
ATOM   6070  C  CZ    . TYR B 1 64  ? 150.385 150.089 160.142 1.00 47.45 ?  64  TYR B CZ    1 
ATOM   6071  O  OH    . TYR B 1 64  ? 150.237 149.113 161.097 1.00 49.14 ?  64  TYR B OH    1 
ATOM   6072  N  N     . GLU B 1 65  ? 148.952 154.539 155.032 1.00 51.99 ?  65  GLU B N     1 
ATOM   6073  C  CA    . GLU B 1 65  ? 148.669 155.875 154.531 1.00 51.96 ?  65  GLU B CA    1 
ATOM   6074  C  C     . GLU B 1 65  ? 149.198 156.905 155.521 1.00 54.39 ?  65  GLU B C     1 
ATOM   6075  O  O     . GLU B 1 65  ? 148.947 156.807 156.726 1.00 55.86 ?  65  GLU B O     1 
ATOM   6076  C  CB    . GLU B 1 65  ? 147.168 156.059 154.316 1.00 50.39 ?  65  GLU B CB    1 
ATOM   6077  C  CG    . GLU B 1 65  ? 146.545 155.026 153.391 1.00 51.97 ?  65  GLU B CG    1 
ATOM   6078  C  CD    . GLU B 1 65  ? 145.042 155.179 153.275 1.00 55.50 ?  65  GLU B CD    1 
ATOM   6079  O  OE1   . GLU B 1 65  ? 144.405 155.592 154.267 1.00 54.42 ?  65  GLU B OE1   1 
ATOM   6080  O  OE2   . GLU B 1 65  ? 144.495 154.888 152.190 1.00 54.21 -1 65  GLU B OE2   1 
ATOM   6081  N  N     . GLU B 1 66  ? 149.943 157.887 155.018 1.00 52.84 ?  66  GLU B N     1 
ATOM   6082  C  CA    . GLU B 1 66  ? 150.540 158.882 155.898 1.00 54.72 ?  66  GLU B CA    1 
ATOM   6083  C  C     . GLU B 1 66  ? 149.560 159.975 156.304 1.00 54.99 ?  66  GLU B C     1 
ATOM   6084  O  O     . GLU B 1 66  ? 149.829 160.700 157.268 1.00 54.13 ?  66  GLU B O     1 
ATOM   6085  C  CB    . GLU B 1 66  ? 151.767 159.507 155.229 1.00 55.88 ?  66  GLU B CB    1 
ATOM   6086  C  CG    . GLU B 1 66  ? 151.446 160.613 154.240 1.00 55.41 ?  66  GLU B CG    1 
ATOM   6087  C  CD    . GLU B 1 66  ? 152.660 161.450 153.893 1.00 56.78 ?  66  GLU B CD    1 
ATOM   6088  O  OE1   . GLU B 1 66  ? 153.764 160.876 153.780 1.00 55.65 ?  66  GLU B OE1   1 
ATOM   6089  O  OE2   . GLU B 1 66  ? 152.511 162.679 153.734 1.00 56.59 -1 66  GLU B OE2   1 
ATOM   6090  N  N     . GLU B 1 67  ? 148.431 160.099 155.606 1.00 53.83 ?  67  GLU B N     1 
ATOM   6091  C  CA    . GLU B 1 67  ? 147.500 161.188 155.886 1.00 53.55 ?  67  GLU B CA    1 
ATOM   6092  C  C     . GLU B 1 67  ? 146.844 161.023 157.252 1.00 55.20 ?  67  GLU B C     1 
ATOM   6093  O  O     . GLU B 1 67  ? 146.773 161.977 158.034 1.00 55.05 ?  67  GLU B O     1 
ATOM   6094  C  CB    . GLU B 1 67  ? 146.437 161.284 154.786 1.00 54.00 ?  67  GLU B CB    1 
ATOM   6095  C  CG    . GLU B 1 67  ? 146.965 161.348 153.350 1.00 55.13 ?  67  GLU B CG    1 
ATOM   6096  C  CD    . GLU B 1 67  ? 147.510 160.025 152.844 1.00 58.09 ?  67  GLU B CD    1 
ATOM   6097  O  OE1   . GLU B 1 67  ? 148.677 159.992 152.402 1.00 57.11 ?  67  GLU B OE1   1 
ATOM   6098  O  OE2   . GLU B 1 67  ? 146.769 159.020 152.886 1.00 56.98 -1 67  GLU B OE2   1 
ATOM   6099  N  N     . PHE B 1 68  ? 146.355 159.818 157.558 1.00 50.07 ?  68  PHE B N     1 
ATOM   6100  C  CA    . PHE B 1 68  ? 145.665 159.619 158.829 1.00 46.19 ?  68  PHE B CA    1 
ATOM   6101  C  C     . PHE B 1 68  ? 146.630 159.671 160.006 1.00 46.50 ?  68  PHE B C     1 
ATOM   6102  O  O     . PHE B 1 68  ? 146.245 160.096 161.102 1.00 50.04 ?  68  PHE B O     1 
ATOM   6103  C  CB    . PHE B 1 68  ? 144.886 158.301 158.811 1.00 47.47 ?  68  PHE B CB    1 
ATOM   6104  C  CG    . PHE B 1 68  ? 145.652 157.121 159.342 1.00 47.17 ?  68  PHE B CG    1 
ATOM   6105  C  CD1   . PHE B 1 68  ? 146.510 156.411 158.525 1.00 45.17 ?  68  PHE B CD1   1 
ATOM   6106  C  CD2   . PHE B 1 68  ? 145.487 156.706 160.653 1.00 43.14 ?  68  PHE B CD2   1 
ATOM   6107  C  CE1   . PHE B 1 68  ? 147.209 155.323 159.009 1.00 44.22 ?  68  PHE B CE1   1 
ATOM   6108  C  CE2   . PHE B 1 68  ? 146.181 155.620 161.143 1.00 42.72 ?  68  PHE B CE2   1 
ATOM   6109  C  CZ    . PHE B 1 68  ? 147.041 154.925 160.319 1.00 44.93 ?  68  PHE B CZ    1 
ATOM   6110  N  N     . LEU B 1 69  ? 147.880 159.250 159.806 1.00 49.73 ?  69  LEU B N     1 
ATOM   6111  C  CA    . LEU B 1 69  ? 148.886 159.365 160.854 1.00 47.63 ?  69  LEU B CA    1 
ATOM   6112  C  C     . LEU B 1 69  ? 149.404 160.787 161.013 1.00 48.62 ?  69  LEU B C     1 
ATOM   6113  O  O     . LEU B 1 69  ? 149.909 161.130 162.087 1.00 52.37 ?  69  LEU B O     1 
ATOM   6114  C  CB    . LEU B 1 69  ? 150.058 158.423 160.569 1.00 47.53 ?  69  LEU B CB    1 
ATOM   6115  C  CG    . LEU B 1 69  ? 149.851 156.949 160.915 1.00 47.12 ?  69  LEU B CG    1 
ATOM   6116  C  CD1   . LEU B 1 69  ? 150.997 156.104 160.381 1.00 48.48 ?  69  LEU B CD1   1 
ATOM   6117  C  CD2   . LEU B 1 69  ? 149.695 156.762 162.415 1.00 47.04 ?  69  LEU B CD2   1 
ATOM   6118  N  N     . SER B 1 70  ? 149.293 161.618 159.974 1.00 48.36 ?  70  SER B N     1 
ATOM   6119  C  CA    . SER B 1 70  ? 149.782 162.989 160.062 1.00 47.28 ?  70  SER B CA    1 
ATOM   6120  C  C     . SER B 1 70  ? 148.875 163.880 160.901 1.00 49.11 ?  70  SER B C     1 
ATOM   6121  O  O     . SER B 1 70  ? 149.297 164.972 161.296 1.00 51.02 ?  70  SER B O     1 
ATOM   6122  C  CB    . SER B 1 70  ? 149.940 163.581 158.662 1.00 49.35 ?  70  SER B CB    1 
ATOM   6123  O  OG    . SER B 1 70  ? 148.688 163.980 158.132 1.00 49.06 ?  70  SER B OG    1 
ATOM   6124  N  N     . LEU B 1 71  ? 147.646 163.446 161.179 1.00 46.46 ?  71  LEU B N     1 
ATOM   6125  C  CA    . LEU B 1 71  ? 146.737 164.229 162.005 1.00 45.72 ?  71  LEU B CA    1 
ATOM   6126  C  C     . LEU B 1 71  ? 147.100 164.194 163.482 1.00 45.67 ?  71  LEU B C     1 
ATOM   6127  O  O     . LEU B 1 71  ? 146.536 164.972 164.259 1.00 46.85 ?  71  LEU B O     1 
ATOM   6128  C  CB    . LEU B 1 71  ? 145.299 163.738 161.823 1.00 44.59 ?  71  LEU B CB    1 
ATOM   6129  C  CG    . LEU B 1 71  ? 144.750 163.740 160.397 1.00 47.01 ?  71  LEU B CG    1 
ATOM   6130  C  CD1   . LEU B 1 71  ? 143.869 162.526 160.165 1.00 49.18 ?  71  LEU B CD1   1 
ATOM   6131  C  CD2   . LEU B 1 71  ? 143.984 165.022 160.122 1.00 45.72 ?  71  LEU B CD2   1 
ATOM   6132  N  N     . TYR B 1 72  ? 148.016 163.320 163.885 1.00 43.56 ?  72  TYR B N     1 
ATOM   6133  C  CA    . TYR B 1 72  ? 148.458 163.212 165.266 1.00 44.85 ?  72  TYR B CA    1 
ATOM   6134  C  C     . TYR B 1 72  ? 149.948 163.505 165.351 1.00 46.70 ?  72  TYR B C     1 
ATOM   6135  O  O     . TYR B 1 72  ? 150.719 163.105 164.473 1.00 48.51 ?  72  TYR B O     1 
ATOM   6136  C  CB    . TYR B 1 72  ? 148.199 161.814 165.844 1.00 45.55 ?  72  TYR B CB    1 
ATOM   6137  C  CG    . TYR B 1 72  ? 146.821 161.250 165.592 1.00 42.98 ?  72  TYR B CG    1 
ATOM   6138  C  CD1   . TYR B 1 72  ? 146.514 160.622 164.392 1.00 42.35 ?  72  TYR B CD1   1 
ATOM   6139  C  CD2   . TYR B 1 72  ? 145.837 161.319 166.566 1.00 42.77 ?  72  TYR B CD2   1 
ATOM   6140  C  CE1   . TYR B 1 72  ? 145.261 160.097 164.164 1.00 40.87 ?  72  TYR B CE1   1 
ATOM   6141  C  CE2   . TYR B 1 72  ? 144.580 160.794 166.348 1.00 42.72 ?  72  TYR B CE2   1 
ATOM   6142  C  CZ    . TYR B 1 72  ? 144.298 160.186 165.144 1.00 42.62 ?  72  TYR B CZ    1 
ATOM   6143  O  OH    . TYR B 1 72  ? 143.048 159.663 164.918 1.00 45.08 ?  72  TYR B OH    1 
ATOM   6144  N  N     . SER B 1 73  ? 150.347 164.203 166.409 1.00 52.19 ?  73  SER B N     1 
ATOM   6145  C  CA    . SER B 1 73  ? 151.758 164.263 166.755 1.00 52.49 ?  73  SER B CA    1 
ATOM   6146  C  C     . SER B 1 73  ? 152.225 162.882 167.198 1.00 51.86 ?  73  SER B C     1 
ATOM   6147  O  O     . SER B 1 73  ? 151.435 162.061 167.668 1.00 54.01 ?  73  SER B O     1 
ATOM   6148  C  CB    . SER B 1 73  ? 152.000 165.289 167.861 1.00 51.38 ?  73  SER B CB    1 
ATOM   6149  O  OG    . SER B 1 73  ? 151.625 164.772 169.125 1.00 50.60 ?  73  SER B OG    1 
ATOM   6150  N  N     . PHE B 1 74  ? 153.525 162.621 167.030 1.00 54.68 ?  74  PHE B N     1 
ATOM   6151  C  CA    . PHE B 1 74  ? 154.033 161.292 167.354 1.00 53.82 ?  74  PHE B CA    1 
ATOM   6152  C  C     . PHE B 1 74  ? 153.853 160.960 168.829 1.00 54.02 ?  74  PHE B C     1 
ATOM   6153  O  O     . PHE B 1 74  ? 153.738 159.783 169.187 1.00 55.52 ?  74  PHE B O     1 
ATOM   6154  C  CB    . PHE B 1 74  ? 155.506 161.158 166.971 1.00 54.59 ?  74  PHE B CB    1 
ATOM   6155  C  CG    . PHE B 1 74  ? 156.119 159.865 167.421 1.00 55.45 ?  74  PHE B CG    1 
ATOM   6156  C  CD1   . PHE B 1 74  ? 155.751 158.670 166.827 1.00 53.33 ?  74  PHE B CD1   1 
ATOM   6157  C  CD2   . PHE B 1 74  ? 157.041 159.838 168.454 1.00 55.41 ?  74  PHE B CD2   1 
ATOM   6158  C  CE1   . PHE B 1 74  ? 156.299 157.474 167.244 1.00 55.48 ?  74  PHE B CE1   1 
ATOM   6159  C  CE2   . PHE B 1 74  ? 157.593 158.644 168.876 1.00 55.10 ?  74  PHE B CE2   1 
ATOM   6160  C  CZ    . PHE B 1 74  ? 157.222 157.461 168.271 1.00 55.55 ?  74  PHE B CZ    1 
ATOM   6161  N  N     . GLU B 1 75  ? 153.825 161.972 169.698 1.00 54.99 ?  75  GLU B N     1 
ATOM   6162  C  CA    . GLU B 1 75  ? 153.559 161.714 171.110 1.00 56.01 ?  75  GLU B CA    1 
ATOM   6163  C  C     . GLU B 1 75  ? 152.167 161.128 171.304 1.00 56.55 ?  75  GLU B C     1 
ATOM   6164  O  O     . GLU B 1 75  ? 151.979 160.201 172.100 1.00 57.06 ?  75  GLU B O     1 
ATOM   6165  C  CB    . GLU B 1 75  ? 153.722 163.001 171.921 1.00 56.12 ?  75  GLU B CB    1 
ATOM   6166  C  CG    . GLU B 1 75  ? 155.121 163.222 172.477 1.00 56.08 ?  75  GLU B CG    1 
ATOM   6167  C  CD    . GLU B 1 75  ? 156.211 162.873 171.482 1.00 59.46 ?  75  GLU B CD    1 
ATOM   6168  O  OE1   . GLU B 1 75  ? 156.382 163.622 170.497 1.00 59.31 ?  75  GLU B OE1   1 
ATOM   6169  O  OE2   . GLU B 1 75  ? 156.899 161.849 171.686 1.00 59.07 -1 75  GLU B OE2   1 
ATOM   6170  N  N     . ASP B 1 76  ? 151.179 161.649 170.573 1.00 52.52 ?  76  ASP B N     1 
ATOM   6171  C  CA    . ASP B 1 76  ? 149.820 161.127 170.676 1.00 51.01 ?  76  ASP B CA    1 
ATOM   6172  C  C     . ASP B 1 76  ? 149.729 159.697 170.153 1.00 49.96 ?  76  ASP B C     1 
ATOM   6173  O  O     . ASP B 1 76  ? 149.047 158.856 170.749 1.00 53.31 ?  76  ASP B O     1 
ATOM   6174  C  CB    . ASP B 1 76  ? 148.860 162.042 169.920 1.00 52.34 ?  76  ASP B CB    1 
ATOM   6175  C  CG    . ASP B 1 76  ? 148.657 163.370 170.620 1.00 54.36 ?  76  ASP B CG    1 
ATOM   6176  O  OD1   . ASP B 1 76  ? 149.121 163.513 171.770 1.00 53.96 ?  76  ASP B OD1   1 
ATOM   6177  O  OD2   . ASP B 1 76  ? 148.032 164.272 170.021 1.00 53.46 -1 76  ASP B OD2   1 
ATOM   6178  N  N     . ILE B 1 77  ? 150.406 159.404 169.041 1.00 47.36 ?  77  ILE B N     1 
ATOM   6179  C  CA    . ILE B 1 77  ? 150.409 158.043 168.509 1.00 47.58 ?  77  ILE B CA    1 
ATOM   6180  C  C     . ILE B 1 77  ? 151.087 157.092 169.484 1.00 48.60 ?  77  ILE B C     1 
ATOM   6181  O  O     . ILE B 1 77  ? 150.636 155.957 169.689 1.00 50.21 ?  77  ILE B O     1 
ATOM   6182  C  CB    . ILE B 1 77  ? 151.085 158.010 167.127 1.00 49.12 ?  77  ILE B CB    1 
ATOM   6183  C  CG1   . ILE B 1 77  ? 150.374 158.958 166.162 1.00 48.20 ?  77  ILE B CG1   1 
ATOM   6184  C  CG2   . ILE B 1 77  ? 151.087 156.597 166.575 1.00 46.74 ?  77  ILE B CG2   1 
ATOM   6185  C  CD1   . ILE B 1 77  ? 151.137 159.208 164.883 1.00 45.94 ?  77  ILE B CD1   1 
ATOM   6186  N  N     . LYS B 1 78  ? 152.192 157.534 170.090 1.00 50.55 ?  78  LYS B N     1 
ATOM   6187  C  CA    . LYS B 1 78  ? 152.864 156.726 171.100 1.00 50.70 ?  78  LYS B CA    1 
ATOM   6188  C  C     . LYS B 1 78  ? 151.950 156.465 172.287 1.00 49.63 ?  78  LYS B C     1 
ATOM   6189  O  O     . LYS B 1 78  ? 151.916 155.352 172.818 1.00 50.68 ?  78  LYS B O     1 
ATOM   6190  C  CB    . LYS B 1 78  ? 154.146 157.422 171.556 1.00 53.57 ?  78  LYS B CB    1 
ATOM   6191  C  CG    . LYS B 1 78  ? 155.197 156.490 172.131 1.00 52.73 ?  78  LYS B CG    1 
ATOM   6192  C  CD    . LYS B 1 78  ? 156.094 157.227 173.112 1.00 53.81 ?  78  LYS B CD    1 
ATOM   6193  C  CE    . LYS B 1 78  ? 157.391 156.478 173.354 1.00 54.50 ?  78  LYS B CE    1 
ATOM   6194  N  NZ    . LYS B 1 78  ? 158.565 157.212 172.808 1.00 52.68 1  78  LYS B NZ    1 
ATOM   6195  N  N     . GLU B 1 79  ? 151.200 157.482 172.715 1.00 51.71 ?  79  GLU B N     1 
ATOM   6196  C  CA    . GLU B 1 79  ? 150.267 157.303 173.823 1.00 51.17 ?  79  GLU B CA    1 
ATOM   6197  C  C     . GLU B 1 79  ? 149.162 156.317 173.461 1.00 49.54 ?  79  GLU B C     1 
ATOM   6198  O  O     . GLU B 1 79  ? 148.760 155.494 174.288 1.00 51.83 ?  79  GLU B O     1 
ATOM   6199  C  CB    . GLU B 1 79  ? 149.681 158.656 174.227 1.00 49.44 ?  79  GLU B CB    1 
ATOM   6200  C  CG    . GLU B 1 79  ? 150.331 159.259 175.462 1.00 52.62 ?  79  GLU B CG    1 
ATOM   6201  C  CD    . GLU B 1 79  ? 149.443 160.269 176.159 1.00 56.12 ?  79  GLU B CD    1 
ATOM   6202  O  OE1   . GLU B 1 79  ? 149.813 160.727 177.261 1.00 54.05 ?  79  GLU B OE1   1 
ATOM   6203  O  OE2   . GLU B 1 79  ? 148.383 160.618 175.600 1.00 56.75 -1 79  GLU B OE2   1 
ATOM   6204  N  N     . VAL B 1 80  ? 148.667 156.380 172.224 1.00 43.97 ?  80  VAL B N     1 
ATOM   6205  C  CA    . VAL B 1 80  ? 147.638 155.443 171.779 1.00 41.94 ?  80  VAL B CA    1 
ATOM   6206  C  C     . VAL B 1 80  ? 148.176 154.015 171.763 1.00 46.28 ?  80  VAL B C     1 
ATOM   6207  O  O     . VAL B 1 80  ? 147.512 153.077 172.225 1.00 48.04 ?  80  VAL B O     1 
ATOM   6208  C  CB    . VAL B 1 80  ? 147.103 155.869 170.399 1.00 43.34 ?  80  VAL B CB    1 
ATOM   6209  C  CG1   . VAL B 1 80  ? 146.306 154.747 169.758 1.00 44.32 ?  80  VAL B CG1   1 
ATOM   6210  C  CG2   . VAL B 1 80  ? 146.255 157.123 170.527 1.00 44.52 ?  80  VAL B CG2   1 
ATOM   6211  N  N     . PHE B 1 81  ? 149.388 153.825 171.234 1.00 46.65 ?  81  PHE B N     1 
ATOM   6212  C  CA    . PHE B 1 81  ? 149.981 152.491 171.203 1.00 43.06 ?  81  PHE B CA    1 
ATOM   6213  C  C     . PHE B 1 81  ? 150.255 151.974 172.612 1.00 45.86 ?  81  PHE B C     1 
ATOM   6214  O  O     . PHE B 1 81  ? 150.079 150.781 172.891 1.00 48.13 ?  81  PHE B O     1 
ATOM   6215  C  CB    . PHE B 1 81  ? 151.265 152.507 170.374 1.00 40.92 ?  81  PHE B CB    1 
ATOM   6216  C  CG    . PHE B 1 81  ? 151.048 152.227 168.914 1.00 40.82 ?  81  PHE B CG    1 
ATOM   6217  C  CD1   . PHE B 1 81  ? 150.634 153.232 168.057 1.00 41.95 ?  81  PHE B CD1   1 
ATOM   6218  C  CD2   . PHE B 1 81  ? 151.256 150.960 168.399 1.00 42.08 ?  81  PHE B CD2   1 
ATOM   6219  C  CE1   . PHE B 1 81  ? 150.435 152.978 166.713 1.00 43.36 ?  81  PHE B CE1   1 
ATOM   6220  C  CE2   . PHE B 1 81  ? 151.058 150.701 167.057 1.00 42.11 ?  81  PHE B CE2   1 
ATOM   6221  C  CZ    . PHE B 1 81  ? 150.646 151.712 166.214 1.00 41.06 ?  81  PHE B CZ    1 
ATOM   6222  N  N     . LYS B 1 82  ? 150.697 152.855 173.511 1.00 47.33 ?  82  LYS B N     1 
ATOM   6223  C  CA    . LYS B 1 82  ? 150.914 152.459 174.897 1.00 46.06 ?  82  LYS B CA    1 
ATOM   6224  C  C     . LYS B 1 82  ? 149.604 152.074 175.569 1.00 44.98 ?  82  LYS B C     1 
ATOM   6225  O  O     . LYS B 1 82  ? 149.563 151.134 176.367 1.00 46.57 ?  82  LYS B O     1 
ATOM   6226  C  CB    . LYS B 1 82  ? 151.601 153.587 175.666 1.00 46.55 ?  82  LYS B CB    1 
ATOM   6227  C  CG    . LYS B 1 82  ? 153.077 153.747 175.346 1.00 47.41 ?  82  LYS B CG    1 
ATOM   6228  C  CD    . LYS B 1 82  ? 153.944 153.135 176.432 1.00 47.76 ?  82  LYS B CD    1 
ATOM   6229  C  CE    . LYS B 1 82  ? 153.629 153.738 177.791 1.00 49.18 ?  82  LYS B CE    1 
ATOM   6230  N  NZ    . LYS B 1 82  ? 154.223 155.093 177.948 1.00 48.24 1  82  LYS B NZ    1 
ATOM   6231  N  N     . THR B 1 83  ? 148.522 152.792 175.261 1.00 42.72 ?  83  THR B N     1 
ATOM   6232  C  CA    . THR B 1 83  ? 147.213 152.412 175.781 1.00 41.20 ?  83  THR B CA    1 
ATOM   6233  C  C     . THR B 1 83  ? 146.799 151.042 175.262 1.00 42.79 ?  83  THR B C     1 
ATOM   6234  O  O     . THR B 1 83  ? 146.221 150.235 175.999 1.00 45.00 ?  83  THR B O     1 
ATOM   6235  C  CB    . THR B 1 83  ? 146.173 153.468 175.405 1.00 41.20 ?  83  THR B CB    1 
ATOM   6236  O  OG1   . THR B 1 83  ? 146.574 154.740 175.928 1.00 46.81 ?  83  THR B OG1   1 
ATOM   6237  C  CG2   . THR B 1 83  ? 144.811 153.105 175.973 1.00 44.21 ?  83  THR B CG2   1 
ATOM   6238  N  N     . ALA B 1 84  ? 147.086 150.763 173.988 1.00 41.52 ?  84  ALA B N     1 
ATOM   6239  C  CA    . ALA B 1 84  ? 146.763 149.454 173.428 1.00 38.00 ?  84  ALA B CA    1 
ATOM   6240  C  C     . ALA B 1 84  ? 147.553 148.344 174.109 1.00 38.28 ?  84  ALA B C     1 
ATOM   6241  O  O     . ALA B 1 84  ? 147.004 147.280 174.417 1.00 43.99 ?  84  ALA B O     1 
ATOM   6242  C  CB    . ALA B 1 84  ? 147.022 149.447 171.924 1.00 39.60 ?  84  ALA B CB    1 
ATOM   6243  N  N     . TYR B 1 85  ? 148.844 148.571 174.349 1.00 45.05 ?  85  TYR B N     1 
ATOM   6244  C  CA    . TYR B 1 85  ? 149.691 147.545 174.948 1.00 43.36 ?  85  TYR B CA    1 
ATOM   6245  C  C     . TYR B 1 85  ? 149.562 147.458 176.464 1.00 44.29 ?  85  TYR B C     1 
ATOM   6246  O  O     . TYR B 1 85  ? 150.030 146.476 177.049 1.00 46.49 ?  85  TYR B O     1 
ATOM   6247  C  CB    . TYR B 1 85  ? 151.153 147.788 174.571 1.00 40.26 ?  85  TYR B CB    1 
ATOM   6248  C  CG    . TYR B 1 85  ? 151.520 147.267 173.201 1.00 41.59 ?  85  TYR B CG    1 
ATOM   6249  C  CD1   . TYR B 1 85  ? 151.953 145.960 173.031 1.00 43.79 ?  85  TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B 1 85  ? 151.427 148.077 172.078 1.00 43.92 ?  85  TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B 1 85  ? 152.289 145.475 171.785 1.00 44.17 ?  85  TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B 1 85  ? 151.760 147.600 170.827 1.00 43.73 ?  85  TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B 1 85  ? 152.190 146.299 170.686 1.00 43.21 ?  85  TYR B CZ    1 
ATOM   6254  O  OH    . TYR B 1 85  ? 152.524 145.818 169.443 1.00 45.29 ?  85  TYR B OH    1 
ATOM   6255  N  N     . ALA B 1 86  ? 148.943 148.447 177.112 1.00 43.66 ?  86  ALA B N     1 
ATOM   6256  C  CA    . ALA B 1 86  ? 148.803 148.403 178.564 1.00 42.01 ?  86  ALA B CA    1 
ATOM   6257  C  C     . ALA B 1 86  ? 147.812 147.338 179.006 1.00 45.48 ?  86  ALA B C     1 
ATOM   6258  O  O     . ALA B 1 86  ? 147.894 146.851 180.139 1.00 47.31 ?  86  ALA B O     1 
ATOM   6259  C  CB    . ALA B 1 86  ? 148.377 149.773 179.091 1.00 42.20 ?  86  ALA B CB    1 
ATOM   6260  N  N     . LYS B 1 87  ? 146.869 146.968 178.138 1.00 44.46 ?  87  LYS B N     1 
ATOM   6261  C  CA    . LYS B 1 87  ? 145.895 145.946 178.495 1.00 45.39 ?  87  LYS B CA    1 
ATOM   6262  C  C     . LYS B 1 87  ? 146.521 144.563 178.616 1.00 44.55 ?  87  LYS B C     1 
ATOM   6263  O  O     . LYS B 1 87  ? 145.931 143.690 179.262 1.00 46.37 ?  87  LYS B O     1 
ATOM   6264  C  CB    . LYS B 1 87  ? 144.765 145.914 177.465 1.00 43.93 ?  87  LYS B CB    1 
ATOM   6265  C  CG    . LYS B 1 87  ? 143.412 145.531 178.040 1.00 43.92 ?  87  LYS B CG    1 
ATOM   6266  C  CD    . LYS B 1 87  ? 142.852 144.295 177.358 1.00 44.50 ?  87  LYS B CD    1 
ATOM   6267  C  CE    . LYS B 1 87  ? 141.730 143.677 178.177 1.00 42.38 ?  87  LYS B CE    1 
ATOM   6268  N  NZ    . LYS B 1 87  ? 141.048 142.574 177.447 1.00 40.62 1  87  LYS B NZ    1 
ATOM   6269  N  N     . LYS B 1 88  ? 147.699 144.353 178.026 1.00 44.68 ?  88  LYS B N     1 
ATOM   6270  C  CA    . LYS B 1 88  ? 148.354 143.047 178.001 1.00 44.57 ?  88  LYS B CA    1 
ATOM   6271  C  C     . LYS B 1 88  ? 147.407 141.977 177.464 1.00 42.41 ?  88  LYS B C     1 
ATOM   6272  O  O     . LYS B 1 88  ? 147.228 140.911 178.057 1.00 43.90 ?  88  LYS B O     1 
ATOM   6273  C  CB    . LYS B 1 88  ? 148.887 142.665 179.383 1.00 45.79 ?  88  LYS B CB    1 
ATOM   6274  C  CG    . LYS B 1 88  ? 150.275 143.202 179.697 1.00 46.36 ?  88  LYS B CG    1 
ATOM   6275  C  CD    . LYS B 1 88  ? 150.218 144.604 180.278 1.00 45.95 ?  88  LYS B CD    1 
ATOM   6276  C  CE    . LYS B 1 88  ? 151.486 145.382 179.961 1.00 46.97 ?  88  LYS B CE    1 
ATOM   6277  N  NZ    . LYS B 1 88  ? 151.307 146.848 180.148 1.00 47.47 1  88  LYS B NZ    1 
ATOM   6278  N  N     . PHE B 1 89  ? 146.783 142.281 176.328 1.00 42.94 ?  89  PHE B N     1 
ATOM   6279  C  CA    . PHE B 1 89  ? 145.797 141.376 175.753 1.00 39.07 ?  89  PHE B CA    1 
ATOM   6280  C  C     . PHE B 1 89  ? 146.442 140.049 175.377 1.00 43.73 ?  89  PHE B C     1 
ATOM   6281  O  O     . PHE B 1 89  ? 147.503 140.013 174.747 1.00 46.25 ?  89  PHE B O     1 
ATOM   6282  C  CB    . PHE B 1 89  ? 145.143 142.009 174.524 1.00 37.31 ?  89  PHE B CB    1 
ATOM   6283  C  CG    . PHE B 1 89  ? 144.212 141.083 173.793 1.00 38.71 ?  89  PHE B CG    1 
ATOM   6284  C  CD1   . PHE B 1 89  ? 142.894 140.951 174.191 1.00 37.31 ?  89  PHE B CD1   1 
ATOM   6285  C  CD2   . PHE B 1 89  ? 144.658 140.337 172.714 1.00 38.40 ?  89  PHE B CD2   1 
ATOM   6286  C  CE1   . PHE B 1 89  ? 142.038 140.098 173.526 1.00 37.73 ?  89  PHE B CE1   1 
ATOM   6287  C  CE2   . PHE B 1 89  ? 143.805 139.480 172.047 1.00 34.60 ?  89  PHE B CE2   1 
ATOM   6288  C  CZ    . PHE B 1 89  ? 142.494 139.362 172.453 1.00 36.67 ?  89  PHE B CZ    1 
ATOM   6289  N  N     . ARG B 1 90  ? 145.789 138.958 175.762 1.00 42.62 ?  90  ARG B N     1 
ATOM   6290  C  CA    . ARG B 1 90  ? 146.234 137.612 175.441 1.00 40.51 ?  90  ARG B CA    1 
ATOM   6291  C  C     . ARG B 1 90  ? 145.118 136.884 174.710 1.00 41.89 ?  90  ARG B C     1 
ATOM   6292  O  O     . ARG B 1 90  ? 143.957 136.937 175.130 1.00 42.84 ?  90  ARG B O     1 
ATOM   6293  C  CB    . ARG B 1 90  ? 146.628 136.845 176.706 1.00 45.34 ?  90  ARG B CB    1 
ATOM   6294  C  CG    . ARG B 1 90  ? 147.766 137.476 177.486 1.00 42.68 ?  90  ARG B CG    1 
ATOM   6295  C  CD    . ARG B 1 90  ? 149.077 137.378 176.727 1.00 45.15 ?  90  ARG B CD    1 
ATOM   6296  N  NE    . ARG B 1 90  ? 150.120 138.197 177.332 1.00 45.79 ?  90  ARG B NE    1 
ATOM   6297  C  CZ    . ARG B 1 90  ? 150.528 139.362 176.852 1.00 44.67 ?  90  ARG B CZ    1 
ATOM   6298  N  NH1   . ARG B 1 90  ? 150.008 139.876 175.749 1.00 46.68 1  90  ARG B NH1   1 
ATOM   6299  N  NH2   . ARG B 1 90  ? 151.483 140.030 177.493 1.00 44.05 ?  90  ARG B NH2   1 
ATOM   6300  N  N     . PHE B 1 91  ? 145.465 136.218 173.621 1.00 39.25 ?  91  PHE B N     1 
ATOM   6301  C  CA    . PHE B 1 91  ? 144.496 135.406 172.904 1.00 38.08 ?  91  PHE B CA    1 
ATOM   6302  C  C     . PHE B 1 91  ? 144.202 134.153 173.719 1.00 43.46 ?  91  PHE B C     1 
ATOM   6303  O  O     . PHE B 1 91  ? 145.126 133.380 174.002 1.00 45.50 ?  91  PHE B O     1 
ATOM   6304  C  CB    . PHE B 1 91  ? 145.026 135.037 171.524 1.00 38.01 ?  91  PHE B CB    1 
ATOM   6305  C  CG    . PHE B 1 91  ? 144.976 136.166 170.534 1.00 39.78 ?  91  PHE B CG    1 
ATOM   6306  C  CD1   . PHE B 1 91  ? 143.785 136.517 169.921 1.00 40.90 ?  91  PHE B CD1   1 
ATOM   6307  C  CD2   . PHE B 1 91  ? 146.121 136.877 170.216 1.00 39.02 ?  91  PHE B CD2   1 
ATOM   6308  C  CE1   . PHE B 1 91  ? 143.738 137.553 169.011 1.00 39.44 ?  91  PHE B CE1   1 
ATOM   6309  C  CE2   . PHE B 1 91  ? 146.078 137.913 169.306 1.00 39.13 ?  91  PHE B CE2   1 
ATOM   6310  C  CZ    . PHE B 1 91  ? 144.885 138.252 168.704 1.00 39.68 ?  91  PHE B CZ    1 
ATOM   6311  N  N     . PRO B 1 92  ? 142.949 133.909 174.116 1.00 42.41 ?  92  PRO B N     1 
ATOM   6312  C  CA    . PRO B 1 92  ? 142.668 132.746 174.969 1.00 42.17 ?  92  PRO B CA    1 
ATOM   6313  C  C     . PRO B 1 92  ? 142.685 131.423 174.227 1.00 42.72 ?  92  PRO B C     1 
ATOM   6314  O  O     . PRO B 1 92  ? 142.765 130.372 174.877 1.00 43.37 ?  92  PRO B O     1 
ATOM   6315  C  CB    . PRO B 1 92  ? 141.271 133.050 175.520 1.00 41.94 ?  92  PRO B CB    1 
ATOM   6316  C  CG    . PRO B 1 92  ? 140.631 133.856 174.445 1.00 41.93 ?  92  PRO B CG    1 
ATOM   6317  C  CD    . PRO B 1 92  ? 141.728 134.670 173.799 1.00 40.90 ?  92  PRO B CD    1 
ATOM   6318  N  N     . SER B 1 93  ? 142.615 131.439 172.899 1.00 42.05 ?  93  SER B N     1 
ATOM   6319  C  CA    . SER B 1 93  ? 142.619 130.227 172.099 1.00 39.78 ?  93  SER B CA    1 
ATOM   6320  C  C     . SER B 1 93  ? 143.646 130.362 170.986 1.00 40.03 ?  93  SER B C     1 
ATOM   6321  O  O     . SER B 1 93  ? 143.951 131.468 170.532 1.00 44.07 ?  93  SER B O     1 
ATOM   6322  C  CB    . SER B 1 93  ? 141.233 129.941 171.504 1.00 42.98 ?  93  SER B CB    1 
ATOM   6323  O  OG    . SER B 1 93  ? 141.040 130.652 170.295 1.00 44.75 ?  93  SER B OG    1 
ATOM   6324  N  N     . PHE B 1 94  ? 144.188 129.219 170.560 1.00 40.58 ?  94  PHE B N     1 
ATOM   6325  C  CA    . PHE B 1 94  ? 145.176 129.229 169.487 1.00 41.09 ?  94  PHE B CA    1 
ATOM   6326  C  C     . PHE B 1 94  ? 144.573 129.743 168.187 1.00 41.10 ?  94  PHE B C     1 
ATOM   6327  O  O     . PHE B 1 94  ? 145.225 130.483 167.442 1.00 43.52 ?  94  PHE B O     1 
ATOM   6328  C  CB    . PHE B 1 94  ? 145.754 127.827 169.289 1.00 42.58 ?  94  PHE B CB    1 
ATOM   6329  C  CG    . PHE B 1 94  ? 146.306 127.590 167.912 1.00 39.39 ?  94  PHE B CG    1 
ATOM   6330  C  CD1   . PHE B 1 94  ? 147.472 128.211 167.503 1.00 41.36 ?  94  PHE B CD1   1 
ATOM   6331  C  CD2   . PHE B 1 94  ? 145.653 126.752 167.024 1.00 41.92 ?  94  PHE B CD2   1 
ATOM   6332  C  CE1   . PHE B 1 94  ? 147.978 128.001 166.236 1.00 41.54 ?  94  PHE B CE1   1 
ATOM   6333  C  CE2   . PHE B 1 94  ? 146.155 126.537 165.756 1.00 44.46 ?  94  PHE B CE2   1 
ATOM   6334  C  CZ    . PHE B 1 94  ? 147.320 127.162 165.362 1.00 41.24 ?  94  PHE B CZ    1 
ATOM   6335  N  N     . MET B 1 95  ? 143.329 129.358 167.897 1.00 38.90 ?  95  MET B N     1 
ATOM   6336  C  CA    . MET B 1 95  ? 142.723 129.720 166.622 1.00 36.29 ?  95  MET B CA    1 
ATOM   6337  C  C     . MET B 1 95  ? 142.481 131.219 166.506 1.00 38.72 ?  95  MET B C     1 
ATOM   6338  O  O     . MET B 1 95  ? 142.552 131.763 165.404 1.00 44.00 ?  95  MET B O     1 
ATOM   6339  C  CB    . MET B 1 95  ? 141.418 128.949 166.421 1.00 39.90 ?  95  MET B CB    1 
ATOM   6340  C  CG    . MET B 1 95  ? 140.725 129.216 165.091 1.00 42.25 ?  95  MET B CG    1 
ATOM   6341  S  SD    . MET B 1 95  ? 141.364 128.295 163.672 1.00 51.03 ?  95  MET B SD    1 
ATOM   6342  C  CE    . MET B 1 95  ? 142.340 127.015 164.459 1.00 43.73 ?  95  MET B CE    1 
ATOM   6343  N  N     . SER B 1 96  ? 142.209 131.905 167.618 1.00 33.31 ?  96  SER B N     1 
ATOM   6344  C  CA    . SER B 1 96  ? 142.033 133.354 167.562 1.00 30.40 ?  96  SER B CA    1 
ATOM   6345  C  C     . SER B 1 96  ? 143.296 134.039 167.051 1.00 32.32 ?  96  SER B C     1 
ATOM   6346  O  O     . SER B 1 96  ? 143.257 134.815 166.085 1.00 34.21 ?  96  SER B O     1 
ATOM   6347  C  CB    . SER B 1 96  ? 141.659 133.882 168.946 1.00 33.47 ?  96  SER B CB    1 
ATOM   6348  O  OG    . SER B 1 96  ? 140.557 133.172 169.482 1.00 38.67 ?  96  SER B OG    1 
ATOM   6349  N  N     . ALA B 1 97  ? 144.433 133.740 167.682 1.00 37.86 ?  97  ALA B N     1 
ATOM   6350  C  CA    . ALA B 1 97  ? 145.699 134.326 167.262 1.00 34.01 ?  97  ALA B CA    1 
ATOM   6351  C  C     . ALA B 1 97  ? 146.076 133.873 165.860 1.00 35.07 ?  97  ALA B C     1 
ATOM   6352  O  O     . ALA B 1 97  ? 146.585 134.667 165.060 1.00 42.03 ?  97  ALA B O     1 
ATOM   6353  C  CB    . ALA B 1 97  ? 146.797 133.962 168.258 1.00 36.35 ?  97  ALA B CB    1 
ATOM   6354  N  N     . PHE B 1 98  ? 145.846 132.597 165.547 1.00 33.42 ?  98  PHE B N     1 
ATOM   6355  C  CA    . PHE B 1 98  ? 146.178 132.091 164.219 1.00 32.89 ?  98  PHE B CA    1 
ATOM   6356  C  C     . PHE B 1 98  ? 145.387 132.826 163.146 1.00 35.95 ?  98  PHE B C     1 
ATOM   6357  O  O     . PHE B 1 98  ? 145.944 133.251 162.128 1.00 43.40 ?  98  PHE B O     1 
ATOM   6358  C  CB    . PHE B 1 98  ? 145.913 130.587 164.154 1.00 37.17 ?  98  PHE B CB    1 
ATOM   6359  C  CG    . PHE B 1 98  ? 146.109 129.996 162.788 1.00 39.18 ?  98  PHE B CG    1 
ATOM   6360  C  CD1   . PHE B 1 98  ? 147.373 129.646 162.348 1.00 39.78 ?  98  PHE B CD1   1 
ATOM   6361  C  CD2   . PHE B 1 98  ? 145.030 129.792 161.944 1.00 41.11 ?  98  PHE B CD2   1 
ATOM   6362  C  CE1   . PHE B 1 98  ? 147.559 129.104 161.094 1.00 37.68 ?  98  PHE B CE1   1 
ATOM   6363  C  CE2   . PHE B 1 98  ? 145.210 129.250 160.687 1.00 43.04 ?  98  PHE B CE2   1 
ATOM   6364  C  CZ    . PHE B 1 98  ? 146.476 128.906 160.261 1.00 40.72 ?  98  PHE B CZ    1 
ATOM   6365  N  N     . LYS B 1 99  ? 144.083 133.000 163.367 1.00 39.14 ?  99  LYS B N     1 
ATOM   6366  C  CA    . LYS B 1 99  ? 143.243 133.683 162.394 1.00 37.77 ?  99  LYS B CA    1 
ATOM   6367  C  C     . LYS B 1 99  ? 143.644 135.141 162.248 1.00 35.59 ?  99  LYS B C     1 
ATOM   6368  O  O     . LYS B 1 99  ? 143.685 135.664 161.129 1.00 41.58 ?  99  LYS B O     1 
ATOM   6369  C  CB    . LYS B 1 99  ? 141.773 133.566 162.795 1.00 36.70 ?  99  LYS B CB    1 
ATOM   6370  C  CG    . LYS B 1 99  ? 141.130 132.248 162.400 1.00 39.01 ?  99  LYS B CG    1 
ATOM   6371  C  CD    . LYS B 1 99  ? 141.444 131.889 160.959 1.00 42.01 ?  99  LYS B CD    1 
ATOM   6372  C  CE    . LYS B 1 99  ? 140.308 131.108 160.325 1.00 40.21 ?  99  LYS B CE    1 
ATOM   6373  N  NZ    . LYS B 1 99  ? 140.081 131.518 158.912 1.00 42.41 1  99  LYS B NZ    1 
ATOM   6374  N  N     . PHE B 1 100 ? 143.954 135.816 163.359 1.00 32.10 ?  100 PHE B N     1 
ATOM   6375  C  CA    . PHE B 1 100 ? 144.387 137.204 163.244 1.00 35.03 ?  100 PHE B CA    1 
ATOM   6376  C  C     . PHE B 1 100 ? 145.690 137.316 162.462 1.00 35.92 ?  100 PHE B C     1 
ATOM   6377  O  O     . PHE B 1 100 ? 145.804 138.125 161.535 1.00 41.09 ?  100 PHE B O     1 
ATOM   6378  C  CB    . PHE B 1 100 ? 144.558 137.851 164.613 1.00 33.33 ?  100 PHE B CB    1 
ATOM   6379  C  CG    . PHE B 1 100 ? 145.183 139.210 164.534 1.00 35.46 ?  100 PHE B CG    1 
ATOM   6380  C  CD1   . PHE B 1 100 ? 144.479 140.275 164.000 1.00 34.60 ?  100 PHE B CD1   1 
ATOM   6381  C  CD2   . PHE B 1 100 ? 146.493 139.409 164.927 1.00 34.53 ?  100 PHE B CD2   1 
ATOM   6382  C  CE1   . PHE B 1 100 ? 145.055 141.523 163.898 1.00 34.60 ?  100 PHE B CE1   1 
ATOM   6383  C  CE2   . PHE B 1 100 ? 147.076 140.652 164.823 1.00 35.28 ?  100 PHE B CE2   1 
ATOM   6384  C  CZ    . PHE B 1 100 ? 146.355 141.712 164.308 1.00 34.72 ?  100 PHE B CZ    1 
ATOM   6385  N  N     . TYR B 1 101 ? 146.687 136.509 162.821 1.00 36.51 ?  101 TYR B N     1 
ATOM   6386  C  CA    . TYR B 1 101 ? 148.006 136.645 162.220 1.00 35.32 ?  101 TYR B CA    1 
ATOM   6387  C  C     . TYR B 1 101 ? 148.097 136.021 160.835 1.00 37.20 ?  101 TYR B C     1 
ATOM   6388  O  O     . TYR B 1 101 ? 149.109 136.216 160.154 1.00 45.47 ?  101 TYR B O     1 
ATOM   6389  C  CB    . TYR B 1 101 ? 149.066 136.044 163.145 1.00 38.28 ?  101 TYR B CB    1 
ATOM   6390  C  CG    . TYR B 1 101 ? 149.344 136.910 164.354 1.00 37.54 ?  101 TYR B CG    1 
ATOM   6391  C  CD1   . TYR B 1 101 ? 150.022 138.114 164.227 1.00 36.80 ?  101 TYR B CD1   1 
ATOM   6392  C  CD2   . TYR B 1 101 ? 148.913 136.533 165.618 1.00 36.97 ?  101 TYR B CD2   1 
ATOM   6393  C  CE1   . TYR B 1 101 ? 150.270 138.914 165.324 1.00 36.63 ?  101 TYR B CE1   1 
ATOM   6394  C  CE2   . TYR B 1 101 ? 149.155 137.326 166.721 1.00 38.05 ?  101 TYR B CE2   1 
ATOM   6395  C  CZ    . TYR B 1 101 ? 149.834 138.515 166.569 1.00 39.59 ?  101 TYR B CZ    1 
ATOM   6396  O  OH    . TYR B 1 101 ? 150.078 139.307 167.666 1.00 42.17 ?  101 TYR B OH    1 
ATOM   6397  N  N     . ASN B 1 102 ? 147.074 135.288 160.400 1.00 40.40 ?  102 ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 102 ? 147.038 134.771 159.041 1.00 41.86 ?  102 ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 102 ? 146.138 135.573 158.114 1.00 43.32 ?  102 ASN B C     1 
ATOM   6400  O  O     . ASN B 1 102 ? 146.403 135.627 156.910 1.00 47.54 ?  102 ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 102 ? 146.576 133.310 159.045 1.00 40.01 ?  102 ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 102 ? 147.673 132.354 159.463 1.00 43.14 ?  102 ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 102 ? 148.296 132.525 160.511 1.00 45.88 ?  102 ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 102 ? 147.918 131.339 158.643 1.00 43.81 ?  102 ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 103 ? 145.084 136.202 158.639 1.00 38.59 ?  103 ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 103 ? 144.125 136.917 157.809 1.00 40.61 ?  103 ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 103 ? 144.144 138.426 157.991 1.00 40.98 ?  103 ASP B C     1 
ATOM   6408  O  O     . ASP B 1 103 ? 143.782 139.144 157.058 1.00 46.47 ?  103 ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 103 ? 142.700 136.418 158.085 1.00 42.23 ?  103 ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 103 ? 142.595 134.905 158.084 1.00 45.37 ?  103 ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 103 ? 143.509 134.237 157.555 1.00 44.78 ?  103 ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 103 ? 141.592 134.382 158.614 1.00 47.06 -1 103 ASP B OD2   1 
ATOM   6413  N  N     . TYR B 1 104 ? 144.549 138.931 159.157 1.00 31.95 ?  104 TYR B N     1 
ATOM   6414  C  CA    . TYR B 1 104 ? 144.402 140.352 159.452 1.00 35.66 ?  104 TYR B CA    1 
ATOM   6415  C  C     . TYR B 1 104 ? 145.686 141.061 159.855 1.00 38.78 ?  104 TYR B C     1 
ATOM   6416  O  O     . TYR B 1 104 ? 145.769 142.280 159.661 1.00 43.88 ?  104 TYR B O     1 
ATOM   6417  C  CB    . TYR B 1 104 ? 143.353 140.565 160.554 1.00 37.44 ?  104 TYR B CB    1 
ATOM   6418  C  CG    . TYR B 1 104 ? 142.030 139.904 160.244 1.00 36.15 ?  104 TYR B CG    1 
ATOM   6419  C  CD1   . TYR B 1 104 ? 141.056 140.570 159.511 1.00 34.65 ?  104 TYR B CD1   1 
ATOM   6420  C  CD2   . TYR B 1 104 ? 141.753 138.617 160.684 1.00 33.99 ?  104 TYR B CD2   1 
ATOM   6421  C  CE1   . TYR B 1 104 ? 139.848 139.968 159.219 1.00 36.14 ?  104 TYR B CE1   1 
ATOM   6422  C  CE2   . TYR B 1 104 ? 140.547 138.008 160.399 1.00 37.33 ?  104 TYR B CE2   1 
ATOM   6423  C  CZ    . TYR B 1 104 ? 139.598 138.688 159.665 1.00 38.90 ?  104 TYR B CZ    1 
ATOM   6424  O  OH    . TYR B 1 104 ? 138.395 138.086 159.381 1.00 38.34 ?  104 TYR B OH    1 
ATOM   6425  N  N     . ALA B 1 105 ? 146.675 140.366 160.408 1.00 40.73 ?  105 ALA B N     1 
ATOM   6426  C  CA    . ALA B 1 105 ? 147.930 141.019 160.751 1.00 40.00 ?  105 ALA B CA    1 
ATOM   6427  C  C     . ALA B 1 105 ? 148.688 141.409 159.488 1.00 43.61 ?  105 ALA B C     1 
ATOM   6428  O  O     . ALA B 1 105 ? 148.757 140.642 158.524 1.00 40.70 ?  105 ALA B O     1 
ATOM   6429  C  CB    . ALA B 1 105 ? 148.791 140.109 161.620 1.00 37.04 ?  105 ALA B CB    1 
ATOM   6430  N  N     . LEU B 1 106 ? 149.255 142.611 159.498 1.00 46.91 ?  106 LEU B N     1 
ATOM   6431  C  CA    . LEU B 1 106 ? 149.997 143.094 158.342 1.00 44.23 ?  106 LEU B CA    1 
ATOM   6432  C  C     . LEU B 1 106 ? 151.335 142.373 158.237 1.00 47.83 ?  106 LEU B C     1 
ATOM   6433  O  O     . LEU B 1 106 ? 152.086 142.285 159.211 1.00 46.99 ?  106 LEU B O     1 
ATOM   6434  C  CB    . LEU B 1 106 ? 150.213 144.602 158.440 1.00 46.87 ?  106 LEU B CB    1 
ATOM   6435  C  CG    . LEU B 1 106 ? 151.051 145.244 157.334 1.00 45.27 ?  106 LEU B CG    1 
ATOM   6436  C  CD1   . LEU B 1 106 ? 150.287 145.252 156.021 1.00 45.59 ?  106 LEU B CD1   1 
ATOM   6437  C  CD2   . LEU B 1 106 ? 151.462 146.654 157.726 1.00 46.37 ?  106 LEU B CD2   1 
ATOM   6438  N  N     . LYS B 1 107 ? 151.627 141.856 157.048 1.00 53.13 ?  107 LYS B N     1 
ATOM   6439  C  CA    . LYS B 1 107 ? 152.877 141.174 156.761 1.00 52.70 ?  107 LYS B CA    1 
ATOM   6440  C  C     . LYS B 1 107 ? 153.665 141.969 155.729 1.00 55.30 ?  107 LYS B C     1 
ATOM   6441  O  O     . LYS B 1 107 ? 153.180 142.949 155.158 1.00 56.79 ?  107 LYS B O     1 
ATOM   6442  C  CB    . LYS B 1 107 ? 152.627 139.746 156.258 1.00 52.84 ?  107 LYS B CB    1 
ATOM   6443  C  CG    . LYS B 1 107 ? 152.054 138.806 157.305 1.00 51.33 ?  107 LYS B CG    1 
ATOM   6444  C  CD    . LYS B 1 107 ? 151.754 137.442 156.706 1.00 54.71 ?  107 LYS B CD    1 
ATOM   6445  C  CE    . LYS B 1 107 ? 151.216 136.484 157.753 1.00 55.56 ?  107 LYS B CE    1 
ATOM   6446  N  NZ    . LYS B 1 107 ? 150.677 135.236 157.142 1.00 52.71 1  107 LYS B NZ    1 
ATOM   6447  N  N     . THR B 1 108 ? 154.898 141.530 155.492 1.00 59.23 ?  108 THR B N     1 
ATOM   6448  C  CA    . THR B 1 108 ? 155.758 142.187 154.520 1.00 59.39 ?  108 THR B CA    1 
ATOM   6449  C  C     . THR B 1 108 ? 155.259 141.907 153.103 1.00 61.88 ?  108 THR B C     1 
ATOM   6450  O  O     . THR B 1 108 ? 154.280 141.187 152.884 1.00 61.58 ?  108 THR B O     1 
ATOM   6451  C  CB    . THR B 1 108 ? 157.203 141.725 154.694 1.00 60.99 ?  108 THR B CB    1 
ATOM   6452  O  OG1   . THR B 1 108 ? 157.231 140.309 154.912 1.00 65.24 ?  108 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 1 108 ? 157.844 142.425 155.882 1.00 58.11 ?  108 THR B CG2   1 
ATOM   6454  N  N     . ASN B 1 109 ? 155.947 142.497 152.121 1.00 63.97 ?  109 ASN B N     1 
ATOM   6455  C  CA    . ASN B 1 109 ? 155.565 142.297 150.726 1.00 61.95 ?  109 ASN B CA    1 
ATOM   6456  C  C     . ASN B 1 109 ? 155.682 140.832 150.324 1.00 64.82 ?  109 ASN B C     1 
ATOM   6457  O  O     . ASN B 1 109 ? 154.819 140.304 149.614 1.00 64.81 ?  109 ASN B O     1 
ATOM   6458  C  CB    . ASN B 1 109 ? 156.426 143.173 149.816 1.00 63.18 ?  109 ASN B CB    1 
ATOM   6459  C  CG    . ASN B 1 109 ? 156.290 144.648 150.129 1.00 63.25 ?  109 ASN B CG    1 
ATOM   6460  O  OD1   . ASN B 1 109 ? 155.419 145.052 150.898 1.00 61.63 ?  109 ASN B OD1   1 
ATOM   6461  N  ND2   . ASN B 1 109 ? 157.151 145.463 149.533 1.00 64.76 ?  109 ASN B ND2   1 
ATOM   6462  N  N     . ASP B 1 110 ? 156.742 140.160 150.770 1.00 66.37 ?  110 ASP B N     1 
ATOM   6463  C  CA    . ASP B 1 110 ? 156.926 138.741 150.496 1.00 66.12 ?  110 ASP B CA    1 
ATOM   6464  C  C     . ASP B 1 110 ? 156.203 137.848 151.497 1.00 66.70 ?  110 ASP B C     1 
ATOM   6465  O  O     . ASP B 1 110 ? 156.271 136.621 151.363 1.00 67.58 ?  110 ASP B O     1 
ATOM   6466  C  CB    . ASP B 1 110 ? 158.419 138.402 150.476 1.00 66.14 ?  110 ASP B CB    1 
ATOM   6467  C  CG    . ASP B 1 110 ? 159.141 138.872 151.721 1.00 67.51 ?  110 ASP B CG    1 
ATOM   6468  O  OD1   . ASP B 1 110 ? 158.542 139.634 152.508 1.00 67.34 ?  110 ASP B OD1   1 
ATOM   6469  O  OD2   . ASP B 1 110 ? 160.313 138.486 151.909 1.00 67.65 -1 110 ASP B OD2   1 
ATOM   6470  N  N     . LYS B 1 111 ? 155.521 138.435 152.484 1.00 62.24 ?  111 LYS B N     1 
ATOM   6471  C  CA    . LYS B 1 111 ? 154.748 137.688 153.480 1.00 63.06 ?  111 LYS B CA    1 
ATOM   6472  C  C     . LYS B 1 111 ? 155.617 136.675 154.223 1.00 64.05 ?  111 LYS B C     1 
ATOM   6473  O  O     . LYS B 1 111 ? 155.193 135.550 154.496 1.00 65.21 ?  111 LYS B O     1 
ATOM   6474  C  CB    . LYS B 1 111 ? 153.536 137.003 152.845 1.00 63.14 ?  111 LYS B CB    1 
ATOM   6475  C  CG    . LYS B 1 111 ? 152.804 137.849 151.814 1.00 63.13 ?  111 LYS B CG    1 
ATOM   6476  C  CD    . LYS B 1 111 ? 151.756 138.735 152.466 1.00 64.53 ?  111 LYS B CD    1 
ATOM   6477  C  CE    . LYS B 1 111 ? 151.487 139.977 151.634 1.00 64.19 ?  111 LYS B CE    1 
ATOM   6478  N  NZ    . LYS B 1 111 ? 151.553 139.692 150.174 1.00 63.59 1  111 LYS B NZ    1 
ATOM   6479  N  N     . LYS B 1 112 ? 156.844 137.075 154.553 1.00 64.60 ?  112 LYS B N     1 
ATOM   6480  C  CA    . LYS B 1 112 ? 157.744 136.227 155.322 1.00 64.95 ?  112 LYS B CA    1 
ATOM   6481  C  C     . LYS B 1 112 ? 157.826 136.618 156.790 1.00 64.12 ?  112 LYS B C     1 
ATOM   6482  O  O     . LYS B 1 112 ? 158.291 135.811 157.603 1.00 64.02 ?  112 LYS B O     1 
ATOM   6483  C  CB    . LYS B 1 112 ? 159.154 136.257 154.721 1.00 64.38 ?  112 LYS B CB    1 
ATOM   6484  C  CG    . LYS B 1 112 ? 159.965 137.484 155.107 1.00 65.17 ?  112 LYS B CG    1 
ATOM   6485  C  CD    . LYS B 1 112 ? 161.416 137.349 154.678 1.00 66.05 ?  112 LYS B CD    1 
ATOM   6486  C  CE    . LYS B 1 112 ? 162.202 138.610 154.998 1.00 64.52 ?  112 LYS B CE    1 
ATOM   6487  N  NZ    . LYS B 1 112 ? 161.381 139.838 154.808 1.00 64.63 1  112 LYS B NZ    1 
ATOM   6488  N  N     . LYS B 1 113 ? 157.390 137.823 157.147 1.00 59.57 ?  113 LYS B N     1 
ATOM   6489  C  CA    . LYS B 1 113 ? 157.488 138.310 158.514 1.00 59.62 ?  113 LYS B CA    1 
ATOM   6490  C  C     . LYS B 1 113 ? 156.206 139.045 158.876 1.00 57.88 ?  113 LYS B C     1 
ATOM   6491  O  O     . LYS B 1 113 ? 155.420 139.432 158.009 1.00 60.09 ?  113 LYS B O     1 
ATOM   6492  C  CB    . LYS B 1 113 ? 158.702 139.232 158.698 1.00 60.10 ?  113 LYS B CB    1 
ATOM   6493  C  CG    . LYS B 1 113 ? 160.043 138.515 158.666 1.00 58.77 ?  113 LYS B CG    1 
ATOM   6494  C  CD    . LYS B 1 113 ? 160.194 137.571 159.846 1.00 60.69 ?  113 LYS B CD    1 
ATOM   6495  C  CE    . LYS B 1 113 ? 161.542 136.873 159.826 1.00 61.41 ?  113 LYS B CE    1 
ATOM   6496  N  NZ    . LYS B 1 113 ? 161.623 135.797 160.850 1.00 60.18 1  113 LYS B NZ    1 
ATOM   6497  N  N     . ILE B 1 114 ? 156.006 139.234 160.177 1.00 52.57 ?  114 ILE B N     1 
ATOM   6498  C  CA    . ILE B 1 114 ? 154.815 139.884 160.711 1.00 52.15 ?  114 ILE B CA    1 
ATOM   6499  C  C     . ILE B 1 114 ? 155.199 141.291 161.145 1.00 53.20 ?  114 ILE B C     1 
ATOM   6500  O  O     . ILE B 1 114 ? 156.065 141.468 162.010 1.00 54.37 ?  114 ILE B O     1 
ATOM   6501  C  CB    . ILE B 1 114 ? 154.215 139.091 161.882 1.00 53.28 ?  114 ILE B CB    1 
ATOM   6502  C  CG1   . ILE B 1 114 ? 153.549 137.812 161.373 1.00 49.72 ?  114 ILE B CG1   1 
ATOM   6503  C  CG2   . ILE B 1 114 ? 153.219 139.943 162.649 1.00 51.69 ?  114 ILE B CG2   1 
ATOM   6504  C  CD1   . ILE B 1 114 ? 153.259 136.808 162.461 1.00 50.40 ?  114 ILE B CD1   1 
ATOM   6505  N  N     . LEU B 1 115 ? 154.556 142.289 160.544 1.00 49.76 ?  115 LEU B N     1 
ATOM   6506  C  CA    . LEU B 1 115 ? 154.816 143.679 160.896 1.00 48.02 ?  115 LEU B CA    1 
ATOM   6507  C  C     . LEU B 1 115 ? 153.844 144.219 161.932 1.00 49.77 ?  115 LEU B C     1 
ATOM   6508  O  O     . LEU B 1 115 ? 154.195 145.144 162.674 1.00 50.66 ?  115 LEU B O     1 
ATOM   6509  C  CB    . LEU B 1 115 ? 154.763 144.562 159.647 1.00 48.78 ?  115 LEU B CB    1 
ATOM   6510  C  CG    . LEU B 1 115 ? 155.957 144.475 158.697 1.00 48.87 ?  115 LEU B CG    1 
ATOM   6511  C  CD1   . LEU B 1 115 ? 155.596 145.056 157.342 1.00 48.97 ?  115 LEU B CD1   1 
ATOM   6512  C  CD2   . LEU B 1 115 ? 157.160 145.190 159.290 1.00 49.55 ?  115 LEU B CD2   1 
ATOM   6513  N  N     . GLU B 1 116 ? 152.635 143.669 162.007 1.00 49.06 ?  116 GLU B N     1 
ATOM   6514  C  CA    . GLU B 1 116 ? 151.592 144.179 162.885 1.00 45.44 ?  116 GLU B CA    1 
ATOM   6515  C  C     . GLU B 1 116 ? 151.228 143.139 163.933 1.00 45.77 ?  116 GLU B C     1 
ATOM   6516  O  O     . GLU B 1 116 ? 150.906 141.996 163.594 1.00 48.91 ?  116 GLU B O     1 
ATOM   6517  C  CB    . GLU B 1 116 ? 150.342 144.563 162.090 1.00 44.67 ?  116 GLU B CB    1 
ATOM   6518  C  CG    . GLU B 1 116 ? 150.169 146.051 161.880 1.00 44.82 ?  116 GLU B CG    1 
ATOM   6519  C  CD    . GLU B 1 116 ? 148.878 146.384 161.163 1.00 45.82 ?  116 GLU B CD    1 
ATOM   6520  O  OE1   . GLU B 1 116 ? 148.147 145.446 160.785 1.00 44.53 ?  116 GLU B OE1   1 
ATOM   6521  O  OE2   . GLU B 1 116 ? 148.591 147.585 160.976 1.00 47.68 -1 116 GLU B OE2   1 
ATOM   6522  N  N     . ARG B 1 117 ? 151.271 143.543 165.199 1.00 40.37 ?  117 ARG B N     1 
ATOM   6523  C  CA    . ARG B 1 117 ? 150.685 142.753 166.267 1.00 41.84 ?  117 ARG B CA    1 
ATOM   6524  C  C     . ARG B 1 117 ? 149.197 143.077 166.372 1.00 42.11 ?  117 ARG B C     1 
ATOM   6525  O  O     . ARG B 1 117 ? 148.665 143.915 165.638 1.00 44.85 ?  117 ARG B O     1 
ATOM   6526  C  CB    . ARG B 1 117 ? 151.410 143.019 167.584 1.00 43.52 ?  117 ARG B CB    1 
ATOM   6527  C  CG    . ARG B 1 117 ? 152.834 142.493 167.630 1.00 43.24 ?  117 ARG B CG    1 
ATOM   6528  C  CD    . ARG B 1 117 ? 152.898 141.033 167.212 1.00 45.76 ?  117 ARG B CD    1 
ATOM   6529  N  NE    . ARG B 1 117 ? 153.888 140.285 167.977 1.00 45.69 ?  117 ARG B NE    1 
ATOM   6530  C  CZ    . ARG B 1 117 ? 153.711 139.855 169.219 1.00 45.62 ?  117 ARG B CZ    1 
ATOM   6531  N  NH1   . ARG B 1 117 ? 152.583 140.078 169.875 1.00 44.83 1  117 ARG B NH1   1 
ATOM   6532  N  NH2   . ARG B 1 117 ? 154.688 139.182 169.819 1.00 48.06 ?  117 ARG B NH2   1 
ATOM   6533  N  N     . TYR B 1 118 ? 148.504 142.400 167.289 1.00 39.73 ?  118 TYR B N     1 
ATOM   6534  C  CA    . TYR B 1 118 ? 147.101 142.727 167.523 1.00 36.21 ?  118 TYR B CA    1 
ATOM   6535  C  C     . TYR B 1 118 ? 146.958 144.144 168.057 1.00 37.83 ?  118 TYR B C     1 
ATOM   6536  O  O     . TYR B 1 118 ? 146.077 144.899 167.622 1.00 41.14 ?  118 TYR B O     1 
ATOM   6537  C  CB    . TYR B 1 118 ? 146.474 141.719 168.483 1.00 34.13 ?  118 TYR B CB    1 
ATOM   6538  C  CG    . TYR B 1 118 ? 144.967 141.806 168.553 1.00 35.58 ?  118 TYR B CG    1 
ATOM   6539  C  CD1   . TYR B 1 118 ? 144.195 141.747 167.401 1.00 34.33 ?  118 TYR B CD1   1 
ATOM   6540  C  CD2   . TYR B 1 118 ? 144.317 141.951 169.769 1.00 35.30 ?  118 TYR B CD2   1 
ATOM   6541  C  CE1   . TYR B 1 118 ? 142.819 141.826 167.460 1.00 34.36 ?  118 TYR B CE1   1 
ATOM   6542  C  CE2   . TYR B 1 118 ? 142.942 142.028 169.839 1.00 30.65 ?  118 TYR B CE2   1 
ATOM   6543  C  CZ    . TYR B 1 118 ? 142.198 141.967 168.681 1.00 36.75 ?  118 TYR B CZ    1 
ATOM   6544  O  OH    . TYR B 1 118 ? 140.826 142.047 168.747 1.00 40.55 ?  118 TYR B OH    1 
ATOM   6545  N  N     . GLU B 1 119 ? 147.831 144.530 168.989 1.00 39.86 ?  119 GLU B N     1 
ATOM   6546  C  CA    . GLU B 1 119 ? 147.793 145.883 169.526 1.00 39.18 ?  119 GLU B CA    1 
ATOM   6547  C  C     . GLU B 1 119 ? 148.144 146.912 168.458 1.00 38.98 ?  119 GLU B C     1 
ATOM   6548  O  O     . GLU B 1 119 ? 147.553 147.994 168.423 1.00 43.90 ?  119 GLU B O     1 
ATOM   6549  C  CB    . GLU B 1 119 ? 148.735 145.999 170.722 1.00 36.58 ?  119 GLU B CB    1 
ATOM   6550  C  CG    . GLU B 1 119 ? 148.200 145.367 171.994 1.00 36.87 ?  119 GLU B CG    1 
ATOM   6551  C  CD    . GLU B 1 119 ? 148.747 143.975 172.229 1.00 44.14 ?  119 GLU B CD    1 
ATOM   6552  O  OE1   . GLU B 1 119 ? 149.066 143.284 171.238 1.00 43.47 ?  119 GLU B OE1   1 
ATOM   6553  O  OE2   . GLU B 1 119 ? 148.857 143.570 173.406 1.00 45.63 -1 119 GLU B OE2   1 
ATOM   6554  N  N     . ASP B 1 120 ? 149.098 146.596 167.579 1.00 40.51 ?  120 ASP B N     1 
ATOM   6555  C  CA    . ASP B 1 120 ? 149.452 147.524 166.508 1.00 37.36 ?  120 ASP B CA    1 
ATOM   6556  C  C     . ASP B 1 120 ? 148.283 147.736 165.555 1.00 35.98 ?  120 ASP B C     1 
ATOM   6557  O  O     . ASP B 1 120 ? 147.967 148.872 165.178 1.00 39.04 ?  120 ASP B O     1 
ATOM   6558  C  CB    . ASP B 1 120 ? 150.672 147.006 165.746 1.00 41.42 ?  120 ASP B CB    1 
ATOM   6559  C  CG    . ASP B 1 120 ? 151.860 146.756 166.647 1.00 45.25 ?  120 ASP B CG    1 
ATOM   6560  O  OD1   . ASP B 1 120 ? 151.985 147.453 167.674 1.00 45.23 ?  120 ASP B OD1   1 
ATOM   6561  O  OD2   . ASP B 1 120 ? 152.670 145.862 166.329 1.00 48.28 -1 120 ASP B OD2   1 
ATOM   6562  N  N     . ARG B 1 121 ? 147.628 146.645 165.153 1.00 33.62 ?  121 ARG B N     1 
ATOM   6563  C  CA    . ARG B 1 121 ? 146.475 146.751 164.266 1.00 33.76 ?  121 ARG B CA    1 
ATOM   6564  C  C     . ARG B 1 121 ? 145.349 147.538 164.924 1.00 36.24 ?  121 ARG B C     1 
ATOM   6565  O  O     . ARG B 1 121 ? 144.729 148.401 164.289 1.00 37.10 ?  121 ARG B O     1 
ATOM   6566  C  CB    . ARG B 1 121 ? 146.001 145.354 163.867 1.00 32.18 ?  121 ARG B CB    1 
ATOM   6567  C  CG    . ARG B 1 121 ? 144.708 145.320 163.074 1.00 30.15 ?  121 ARG B CG    1 
ATOM   6568  C  CD    . ARG B 1 121 ? 144.958 145.512 161.593 1.00 30.70 ?  121 ARG B CD    1 
ATOM   6569  N  NE    . ARG B 1 121 ? 144.460 146.800 161.127 1.00 37.96 ?  121 ARG B NE    1 
ATOM   6570  C  CZ    . ARG B 1 121 ? 145.076 147.566 160.239 1.00 34.88 ?  121 ARG B CZ    1 
ATOM   6571  N  NH1   . ARG B 1 121 ? 146.222 147.204 159.689 1.00 37.95 1  121 ARG B NH1   1 
ATOM   6572  N  NH2   . ARG B 1 121 ? 144.528 148.727 159.895 1.00 31.85 ?  121 ARG B NH2   1 
ATOM   6573  N  N     . ILE B 1 122 ? 145.082 147.263 166.203 1.00 33.71 ?  122 ILE B N     1 
ATOM   6574  C  CA    . ILE B 1 122 ? 144.018 147.968 166.907 1.00 26.54 ?  122 ILE B CA    1 
ATOM   6575  C  C     . ILE B 1 122 ? 144.349 149.449 167.036 1.00 30.87 ?  122 ILE B C     1 
ATOM   6576  O  O     . ILE B 1 122 ? 143.476 150.307 166.868 1.00 37.19 ?  122 ILE B O     1 
ATOM   6577  C  CB    . ILE B 1 122 ? 143.762 147.311 168.274 1.00 33.72 ?  122 ILE B CB    1 
ATOM   6578  C  CG1   . ILE B 1 122 ? 142.905 146.059 168.091 1.00 29.67 ?  122 ILE B CG1   1 
ATOM   6579  C  CG2   . ILE B 1 122 ? 143.091 148.287 169.232 1.00 31.03 ?  122 ILE B CG2   1 
ATOM   6580  C  CD1   . ILE B 1 122 ? 142.446 145.447 169.379 1.00 29.81 ?  122 ILE B CD1   1 
ATOM   6581  N  N     . SER B 1 123 ? 145.610 149.777 167.329 1.00 35.20 ?  123 SER B N     1 
ATOM   6582  C  CA    . SER B 1 123 ? 146.011 151.176 167.432 1.00 30.91 ?  123 SER B CA    1 
ATOM   6583  C  C     . SER B 1 123 ? 145.858 151.895 166.101 1.00 30.80 ?  123 SER B C     1 
ATOM   6584  O  O     . SER B 1 123 ? 145.389 153.036 166.056 1.00 39.32 ?  123 SER B O     1 
ATOM   6585  C  CB    . SER B 1 123 ? 147.456 151.276 167.920 1.00 32.46 ?  123 SER B CB    1 
ATOM   6586  O  OG    . SER B 1 123 ? 147.669 150.469 169.059 1.00 36.41 ?  123 SER B OG    1 
ATOM   6587  N  N     . ILE B 1 124 ? 146.256 151.247 165.004 1.00 30.84 ?  124 ILE B N     1 
ATOM   6588  C  CA    . ILE B 1 124 ? 146.134 151.879 163.694 1.00 31.07 ?  124 ILE B CA    1 
ATOM   6589  C  C     . ILE B 1 124 ? 144.668 152.102 163.344 1.00 34.58 ?  124 ILE B C     1 
ATOM   6590  O  O     . ILE B 1 124 ? 144.287 153.174 162.851 1.00 36.70 ?  124 ILE B O     1 
ATOM   6591  C  CB    . ILE B 1 124 ? 146.858 151.037 162.627 1.00 37.99 ?  124 ILE B CB    1 
ATOM   6592  C  CG1   . ILE B 1 124 ? 148.372 151.155 162.811 1.00 37.08 ?  124 ILE B CG1   1 
ATOM   6593  C  CG2   . ILE B 1 124 ? 146.453 151.471 161.228 1.00 34.09 ?  124 ILE B CG2   1 
ATOM   6594  C  CD1   . ILE B 1 124 ? 148.856 152.578 162.990 1.00 34.28 ?  124 ILE B CD1   1 
ATOM   6595  N  N     . VAL B 1 125 ? 143.820 151.105 163.607 1.00 33.80 ?  125 VAL B N     1 
ATOM   6596  C  CA    . VAL B 1 125 ? 142.396 151.248 163.316 1.00 27.57 ?  125 VAL B CA    1 
ATOM   6597  C  C     . VAL B 1 125 ? 141.783 152.352 164.171 1.00 24.37 ?  125 VAL B C     1 
ATOM   6598  O  O     . VAL B 1 125 ? 140.961 153.142 163.693 1.00 35.89 ?  125 VAL B O     1 
ATOM   6599  C  CB    . VAL B 1 125 ? 141.673 149.902 163.513 1.00 31.00 ?  125 VAL B CB    1 
ATOM   6600  C  CG1   . VAL B 1 125 ? 140.175 150.078 163.387 1.00 31.11 ?  125 VAL B CG1   1 
ATOM   6601  C  CG2   . VAL B 1 125 ? 142.164 148.888 162.496 1.00 28.16 ?  125 VAL B CG2   1 
ATOM   6602  N  N     . ALA B 1 126 ? 142.180 152.434 165.444 1.00 23.02 ?  126 ALA B N     1 
ATOM   6603  C  CA    . ALA B 1 126 ? 141.658 153.473 166.326 1.00 25.33 ?  126 ALA B CA    1 
ATOM   6604  C  C     . ALA B 1 126 ? 142.101 154.860 165.883 1.00 30.57 ?  126 ALA B C     1 
ATOM   6605  O  O     . ALA B 1 126 ? 141.313 155.812 165.923 1.00 35.12 ?  126 ALA B O     1 
ATOM   6606  C  CB    . ALA B 1 126 ? 142.105 153.206 167.760 1.00 31.54 ?  126 ALA B CB    1 
ATOM   6607  N  N     . LEU B 1 127 ? 143.364 154.998 165.474 1.00 33.87 ?  127 LEU B N     1 
ATOM   6608  C  CA    . LEU B 1 127 ? 143.852 156.286 164.999 1.00 29.95 ?  127 LEU B CA    1 
ATOM   6609  C  C     . LEU B 1 127 ? 143.147 156.699 163.716 1.00 30.74 ?  127 LEU B C     1 
ATOM   6610  O  O     . LEU B 1 127 ? 142.866 157.885 163.510 1.00 36.71 ?  127 LEU B O     1 
ATOM   6611  C  CB    . LEU B 1 127 ? 145.365 156.230 164.792 1.00 33.31 ?  127 LEU B CB    1 
ATOM   6612  C  CG    . LEU B 1 127 ? 146.219 156.177 166.060 1.00 32.21 ?  127 LEU B CG    1 
ATOM   6613  C  CD1   . LEU B 1 127 ? 147.616 155.682 165.736 1.00 36.25 ?  127 LEU B CD1   1 
ATOM   6614  C  CD2   . LEU B 1 127 ? 146.271 157.535 166.736 1.00 33.87 ?  127 LEU B CD2   1 
ATOM   6615  N  N     . PHE B 1 128 ? 142.862 155.737 162.836 1.00 29.85 ?  128 PHE B N     1 
ATOM   6616  C  CA    . PHE B 1 128 ? 142.075 156.047 161.647 1.00 29.40 ?  128 PHE B CA    1 
ATOM   6617  C  C     . PHE B 1 128 ? 140.660 156.473 162.021 1.00 28.36 ?  128 PHE B C     1 
ATOM   6618  O  O     . PHE B 1 128 ? 140.109 157.412 161.434 1.00 33.31 ?  128 PHE B O     1 
ATOM   6619  C  CB    . PHE B 1 128 ? 142.041 154.841 160.707 1.00 28.61 ?  128 PHE B CB    1 
ATOM   6620  C  CG    . PHE B 1 128 ? 140.942 154.905 159.688 1.00 33.12 ?  128 PHE B CG    1 
ATOM   6621  C  CD1   . PHE B 1 128 ? 141.067 155.710 158.569 1.00 31.02 ?  128 PHE B CD1   1 
ATOM   6622  C  CD2   . PHE B 1 128 ? 139.782 154.167 159.851 1.00 32.42 ?  128 PHE B CD2   1 
ATOM   6623  C  CE1   . PHE B 1 128 ? 140.059 155.777 157.631 1.00 31.53 ?  128 PHE B CE1   1 
ATOM   6624  C  CE2   . PHE B 1 128 ? 138.770 154.233 158.918 1.00 31.93 ?  128 PHE B CE2   1 
ATOM   6625  C  CZ    . PHE B 1 128 ? 138.909 155.039 157.806 1.00 31.58 ?  128 PHE B CZ    1 
ATOM   6626  N  N     . PHE B 1 129 ? 140.054 155.786 162.992 1.00 29.04 ?  129 PHE B N     1 
ATOM   6627  C  CA    . PHE B 1 129 ? 138.690 156.108 163.403 1.00 26.13 ?  129 PHE B CA    1 
ATOM   6628  C  C     . PHE B 1 129 ? 138.598 157.505 164.002 1.00 28.48 ?  129 PHE B C     1 
ATOM   6629  O  O     . PHE B 1 129 ? 137.662 158.256 163.705 1.00 32.18 ?  129 PHE B O     1 
ATOM   6630  C  CB    . PHE B 1 129 ? 138.191 155.077 164.415 1.00 28.98 ?  129 PHE B CB    1 
ATOM   6631  C  CG    . PHE B 1 129 ? 137.725 153.791 163.803 1.00 26.86 ?  129 PHE B CG    1 
ATOM   6632  C  CD1   . PHE B 1 129 ? 137.499 153.693 162.443 1.00 25.66 ?  129 PHE B CD1   1 
ATOM   6633  C  CD2   . PHE B 1 129 ? 137.500 152.681 164.598 1.00 25.26 ?  129 PHE B CD2   1 
ATOM   6634  C  CE1   . PHE B 1 129 ? 137.066 152.508 161.887 1.00 26.72 ?  129 PHE B CE1   1 
ATOM   6635  C  CE2   . PHE B 1 129 ? 137.064 151.495 164.047 1.00 28.32 ?  129 PHE B CE2   1 
ATOM   6636  C  CZ    . PHE B 1 129 ? 136.847 151.408 162.689 1.00 30.23 ?  129 PHE B CZ    1 
ATOM   6637  N  N     . ALA B 1 130 ? 139.558 157.868 164.854 1.00 33.69 ?  130 ALA B N     1 
ATOM   6638  C  CA    . ALA B 1 130 ? 139.440 159.105 165.620 1.00 35.78 ?  130 ALA B CA    1 
ATOM   6639  C  C     . ALA B 1 130 ? 139.589 160.341 164.744 1.00 40.17 ?  130 ALA B C     1 
ATOM   6640  O  O     . ALA B 1 130 ? 139.016 161.391 165.061 1.00 46.69 ?  130 ALA B O     1 
ATOM   6641  C  CB    . ALA B 1 130 ? 140.472 159.123 166.742 1.00 33.05 ?  130 ALA B CB    1 
ATOM   6642  N  N     . ASN B 1 131 ? 140.352 160.243 163.654 1.00 41.05 ?  131 ASN B N     1 
ATOM   6643  C  CA    . ASN B 1 131 ? 140.541 161.346 162.711 1.00 41.85 ?  131 ASN B CA    1 
ATOM   6644  C  C     . ASN B 1 131 ? 141.132 162.578 163.399 1.00 41.78 ?  131 ASN B C     1 
ATOM   6645  O  O     . ASN B 1 131 ? 140.636 163.697 163.261 1.00 44.86 ?  131 ASN B O     1 
ATOM   6646  C  CB    . ASN B 1 131 ? 139.228 161.692 162.001 1.00 38.10 ?  131 ASN B CB    1 
ATOM   6647  C  CG    . ASN B 1 131 ? 139.449 162.271 160.618 1.00 45.08 ?  131 ASN B CG    1 
ATOM   6648  O  OD1   . ASN B 1 131 ? 140.435 161.959 159.951 1.00 45.24 ?  131 ASN B OD1   1 
ATOM   6649  N  ND2   . ASN B 1 131 ? 138.526 163.118 160.177 1.00 43.88 ?  131 ASN B ND2   1 
ATOM   6650  N  N     . GLY B 1 132 ? 142.209 162.359 164.154 1.00 42.24 ?  132 GLY B N     1 
ATOM   6651  C  CA    . GLY B 1 132 ? 142.943 163.439 164.779 1.00 43.72 ?  132 GLY B CA    1 
ATOM   6652  C  C     . GLY B 1 132 ? 142.652 163.678 166.244 1.00 46.62 ?  132 GLY B C     1 
ATOM   6653  O  O     . GLY B 1 132 ? 143.256 164.582 166.833 1.00 49.36 ?  132 GLY B O     1 
ATOM   6654  N  N     . ASP B 1 133 ? 141.756 162.905 166.853 1.00 42.99 ?  133 ASP B N     1 
ATOM   6655  C  CA    . ASP B 1 133 ? 141.394 163.075 168.257 1.00 43.79 ?  133 ASP B CA    1 
ATOM   6656  C  C     . ASP B 1 133 ? 142.110 162.009 169.081 1.00 46.29 ?  133 ASP B C     1 
ATOM   6657  O  O     . ASP B 1 133 ? 141.793 160.820 168.980 1.00 48.43 ?  133 ASP B O     1 
ATOM   6658  C  CB    . ASP B 1 133 ? 139.881 162.990 168.438 1.00 45.24 ?  133 ASP B CB    1 
ATOM   6659  C  CG    . ASP B 1 133 ? 139.412 163.604 169.744 1.00 48.48 ?  133 ASP B CG    1 
ATOM   6660  O  OD1   . ASP B 1 133 ? 140.242 163.770 170.661 1.00 49.94 ?  133 ASP B OD1   1 
ATOM   6661  O  OD2   . ASP B 1 133 ? 138.208 163.918 169.853 1.00 49.76 -1 133 ASP B OD2   1 
ATOM   6662  N  N     . THR B 1 134 ? 143.076 162.437 169.896 1.00 46.10 ?  134 THR B N     1 
ATOM   6663  C  CA    . THR B 1 134 ? 143.851 161.485 170.686 1.00 45.62 ?  134 THR B CA    1 
ATOM   6664  C  C     . THR B 1 134 ? 142.985 160.783 171.726 1.00 45.11 ?  134 THR B C     1 
ATOM   6665  O  O     . THR B 1 134 ? 143.104 159.569 171.921 1.00 45.77 ?  134 THR B O     1 
ATOM   6666  C  CB    . THR B 1 134 ? 145.022 162.196 171.359 1.00 47.78 ?  134 THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 134 ? 145.725 162.977 170.386 1.00 49.81 ?  134 THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 134 ? 145.975 161.182 171.976 1.00 46.42 ?  134 THR B CG2   1 
ATOM   6669  N  N     . GLU B 1 135 ? 142.113 161.530 172.408 1.00 43.87 ?  135 GLU B N     1 
ATOM   6670  C  CA    . GLU B 1 135 ? 141.238 160.916 173.402 1.00 42.72 ?  135 GLU B CA    1 
ATOM   6671  C  C     . GLU B 1 135 ? 140.259 159.946 172.753 1.00 44.61 ?  135 GLU B C     1 
ATOM   6672  O  O     . GLU B 1 135 ? 140.001 158.863 173.291 1.00 45.08 ?  135 GLU B O     1 
ATOM   6673  C  CB    . GLU B 1 135 ? 140.494 161.996 174.185 1.00 45.96 ?  135 GLU B CB    1 
ATOM   6674  C  CG    . GLU B 1 135 ? 141.399 162.851 175.053 1.00 46.64 ?  135 GLU B CG    1 
ATOM   6675  C  CD    . GLU B 1 135 ? 142.348 162.019 175.895 1.00 50.56 ?  135 GLU B CD    1 
ATOM   6676  O  OE1   . GLU B 1 135 ? 141.866 161.197 176.700 1.00 49.79 ?  135 GLU B OE1   1 
ATOM   6677  O  OE2   . GLU B 1 135 ? 143.578 162.186 175.748 1.00 49.37 -1 135 GLU B OE2   1 
ATOM   6678  N  N     . LYS B 1 136 ? 139.708 160.315 171.596 1.00 40.26 ?  136 LYS B N     1 
ATOM   6679  C  CA    . LYS B 1 136 ? 138.831 159.401 170.872 1.00 37.63 ?  136 LYS B CA    1 
ATOM   6680  C  C     . LYS B 1 136 ? 139.597 158.171 170.400 1.00 37.69 ?  136 LYS B C     1 
ATOM   6681  O  O     . LYS B 1 136 ? 139.061 157.056 170.400 1.00 41.90 ?  136 LYS B O     1 
ATOM   6682  C  CB    . LYS B 1 136 ? 138.184 160.122 169.691 1.00 42.81 ?  136 LYS B CB    1 
ATOM   6683  C  CG    . LYS B 1 136 ? 136.951 159.436 169.135 1.00 41.41 ?  136 LYS B CG    1 
ATOM   6684  C  CD    . LYS B 1 136 ? 135.690 159.913 169.833 1.00 41.96 ?  136 LYS B CD    1 
ATOM   6685  C  CE    . LYS B 1 136 ? 134.454 159.599 169.008 1.00 42.73 ?  136 LYS B CE    1 
ATOM   6686  N  NZ    . LYS B 1 136 ? 133.257 160.329 169.505 1.00 43.51 1  136 LYS B NZ    1 
ATOM   6687  N  N     . ALA B 1 137 ? 140.855 158.354 169.991 1.00 36.90 ?  137 ALA B N     1 
ATOM   6688  C  CA    . ALA B 1 137 ? 141.675 157.215 169.594 1.00 33.48 ?  137 ALA B CA    1 
ATOM   6689  C  C     . ALA B 1 137 ? 141.913 156.274 170.766 1.00 36.36 ?  137 ALA B C     1 
ATOM   6690  O  O     . ALA B 1 137 ? 141.869 155.050 170.608 1.00 39.45 ?  137 ALA B O     1 
ATOM   6691  C  CB    . ALA B 1 137 ? 143.003 157.700 169.013 1.00 33.49 ?  137 ALA B CB    1 
ATOM   6692  N  N     . LYS B 1 138 ? 142.157 156.828 171.956 1.00 38.61 ?  138 LYS B N     1 
ATOM   6693  C  CA    . LYS B 1 138 ? 142.312 155.991 173.142 1.00 36.74 ?  138 LYS B CA    1 
ATOM   6694  C  C     . LYS B 1 138 ? 141.011 155.283 173.495 1.00 37.49 ?  138 LYS B C     1 
ATOM   6695  O  O     . LYS B 1 138 ? 141.026 154.130 173.939 1.00 39.01 ?  138 LYS B O     1 
ATOM   6696  C  CB    . LYS B 1 138 ? 142.801 156.829 174.322 1.00 41.46 ?  138 LYS B CB    1 
ATOM   6697  C  CG    . LYS B 1 138 ? 144.161 157.462 174.111 1.00 41.35 ?  138 LYS B CG    1 
ATOM   6698  C  CD    . LYS B 1 138 ? 144.942 157.505 175.409 1.00 38.39 ?  138 LYS B CD    1 
ATOM   6699  C  CE    . LYS B 1 138 ? 145.915 158.666 175.422 1.00 41.44 ?  138 LYS B CE    1 
ATOM   6700  N  NZ    . LYS B 1 138 ? 145.234 159.961 175.148 1.00 43.43 1  138 LYS B NZ    1 
ATOM   6701  N  N     . GLU B 1 139 ? 139.875 155.962 173.321 1.00 37.44 ?  139 GLU B N     1 
ATOM   6702  C  CA    . GLU B 1 139 ? 138.587 155.318 173.564 1.00 37.33 ?  139 GLU B CA    1 
ATOM   6703  C  C     . GLU B 1 139 ? 138.372 154.144 172.615 1.00 36.11 ?  139 GLU B C     1 
ATOM   6704  O  O     . GLU B 1 139 ? 137.924 153.071 173.033 1.00 41.74 ?  139 GLU B O     1 
ATOM   6705  C  CB    . GLU B 1 139 ? 137.455 156.334 173.426 1.00 34.82 ?  139 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 1 139 ? 137.408 157.366 174.539 1.00 38.00 ?  139 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 1 139 ? 136.294 158.375 174.349 1.00 45.17 ?  139 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 1 139 ? 135.254 158.010 173.762 1.00 43.55 ?  139 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 1 139 ? 136.457 159.533 174.786 1.00 44.22 -1 139 GLU B OE2   1 
ATOM   6710  N  N     . TYR B 1 140 ? 138.699 154.327 171.334 1.00 29.54 ?  140 TYR B N     1 
ATOM   6711  C  CA    . TYR B 1 140 ? 138.588 153.232 170.374 1.00 28.47 ?  140 TYR B CA    1 
ATOM   6712  C  C     . TYR B 1 140 ? 139.550 152.101 170.716 1.00 31.07 ?  140 TYR B C     1 
ATOM   6713  O  O     . TYR B 1 140 ? 139.213 150.919 170.563 1.00 35.49 ?  140 TYR B O     1 
ATOM   6714  C  CB    . TYR B 1 140 ? 138.851 153.741 168.959 1.00 29.36 ?  140 TYR B CB    1 
ATOM   6715  C  CG    . TYR B 1 140 ? 137.717 154.528 168.352 1.00 30.90 ?  140 TYR B CG    1 
ATOM   6716  C  CD1   . TYR B 1 140 ? 136.435 153.999 168.282 1.00 31.12 ?  140 TYR B CD1   1 
ATOM   6717  C  CD2   . TYR B 1 140 ? 137.929 155.800 167.843 1.00 32.00 ?  140 TYR B CD2   1 
ATOM   6718  C  CE1   . TYR B 1 140 ? 135.400 154.718 167.722 1.00 34.65 ?  140 TYR B CE1   1 
ATOM   6719  C  CE2   . TYR B 1 140 ? 136.902 156.524 167.286 1.00 30.75 ?  140 TYR B CE2   1 
ATOM   6720  C  CZ    . TYR B 1 140 ? 135.641 155.981 167.226 1.00 28.98 ?  140 TYR B CZ    1 
ATOM   6721  O  OH    . TYR B 1 140 ? 134.622 156.711 166.667 1.00 37.84 ?  140 TYR B OH    1 
ATOM   6722  N  N     . VAL B 1 141 ? 140.759 152.446 171.161 1.00 32.75 ?  141 VAL B N     1 
ATOM   6723  C  CA    . VAL B 1 141 ? 141.735 151.434 171.557 1.00 32.90 ?  141 VAL B CA    1 
ATOM   6724  C  C     . VAL B 1 141 ? 141.204 150.612 172.722 1.00 32.97 ?  141 VAL B C     1 
ATOM   6725  O  O     . VAL B 1 141 ? 141.307 149.382 172.734 1.00 38.73 ?  141 VAL B O     1 
ATOM   6726  C  CB    . VAL B 1 141 ? 143.082 152.095 171.899 1.00 35.19 ?  141 VAL B CB    1 
ATOM   6727  C  CG1   . VAL B 1 141 ? 143.832 151.267 172.912 1.00 33.55 ?  141 VAL B CG1   1 
ATOM   6728  C  CG2   . VAL B 1 141 ? 143.917 152.248 170.649 1.00 33.99 ?  141 VAL B CG2   1 
ATOM   6729  N  N     . ASN B 1 142 ? 140.635 151.281 173.725 1.00 32.61 ?  142 ASN B N     1 
ATOM   6730  C  CA    . ASN B 1 142 ? 140.076 150.561 174.862 1.00 30.80 ?  142 ASN B CA    1 
ATOM   6731  C  C     . ASN B 1 142 ? 138.866 149.734 174.456 1.00 31.55 ?  142 ASN B C     1 
ATOM   6732  O  O     . ASN B 1 142 ? 138.630 148.661 175.022 1.00 35.97 ?  142 ASN B O     1 
ATOM   6733  C  CB    . ASN B 1 142 ? 139.707 151.541 175.973 1.00 28.16 ?  142 ASN B CB    1 
ATOM   6734  C  CG    . ASN B 1 142 ? 140.922 152.091 176.690 1.00 32.27 ?  142 ASN B CG    1 
ATOM   6735  O  OD1   . ASN B 1 142 ? 141.758 151.337 177.185 1.00 32.50 ?  142 ASN B OD1   1 
ATOM   6736  N  ND2   . ASN B 1 142 ? 141.028 153.412 176.743 1.00 34.28 ?  142 ASN B ND2   1 
ATOM   6737  N  N     . LEU B 1 143 ? 138.092 150.214 173.482 1.00 31.52 ?  143 LEU B N     1 
ATOM   6738  C  CA    . LEU B 1 143 ? 136.918 149.478 173.029 1.00 25.88 ?  143 LEU B CA    1 
ATOM   6739  C  C     . LEU B 1 143 ? 137.307 148.212 172.275 1.00 30.44 ?  143 LEU B C     1 
ATOM   6740  O  O     . LEU B 1 143 ? 136.651 147.174 172.412 1.00 32.84 ?  143 LEU B O     1 
ATOM   6741  C  CB    . LEU B 1 143 ? 136.054 150.383 172.156 1.00 25.23 ?  143 LEU B CB    1 
ATOM   6742  C  CG    . LEU B 1 143 ? 134.571 150.041 172.046 1.00 28.76 ?  143 LEU B CG    1 
ATOM   6743  C  CD1   . LEU B 1 143 ? 133.850 150.468 173.308 1.00 31.58 ?  143 LEU B CD1   1 
ATOM   6744  C  CD2   . LEU B 1 143 ? 133.978 150.727 170.834 1.00 28.42 ?  143 LEU B CD2   1 
ATOM   6745  N  N     . MET B 1 144 ? 138.364 148.279 171.467 1.00 28.96 ?  144 MET B N     1 
ATOM   6746  C  CA    . MET B 1 144 ? 138.763 147.136 170.654 1.00 21.69 ?  144 MET B CA    1 
ATOM   6747  C  C     . MET B 1 144 ? 139.693 146.172 171.381 1.00 26.49 ?  144 MET B C     1 
ATOM   6748  O  O     . MET B 1 144 ? 139.625 144.962 171.137 1.00 30.49 ?  144 MET B O     1 
ATOM   6749  C  CB    . MET B 1 144 ? 139.430 147.614 169.362 1.00 24.86 ?  144 MET B CB    1 
ATOM   6750  C  CG    . MET B 1 144 ? 138.485 148.328 168.413 1.00 25.95 ?  144 MET B CG    1 
ATOM   6751  S  SD    . MET B 1 144 ? 139.239 148.679 166.818 1.00 37.66 ?  144 MET B SD    1 
ATOM   6752  C  CE    . MET B 1 144 ? 139.824 150.347 167.092 1.00 27.90 ?  144 MET B CE    1 
ATOM   6753  N  N     . ILE B 1 145 ? 140.568 146.674 172.254 1.00 29.57 ?  145 ILE B N     1 
ATOM   6754  C  CA    . ILE B 1 145 ? 141.447 145.794 173.016 1.00 30.47 ?  145 ILE B CA    1 
ATOM   6755  C  C     . ILE B 1 145 ? 140.662 145.039 174.086 1.00 31.16 ?  145 ILE B C     1 
ATOM   6756  O  O     . ILE B 1 145 ? 140.990 143.891 174.405 1.00 35.22 ?  145 ILE B O     1 
ATOM   6757  C  CB    . ILE B 1 145 ? 142.627 146.589 173.607 1.00 29.75 ?  145 ILE B CB    1 
ATOM   6758  C  CG1   . ILE B 1 145 ? 143.875 145.709 173.698 1.00 28.07 ?  145 ILE B CG1   1 
ATOM   6759  C  CG2   . ILE B 1 145 ? 142.286 147.187 174.966 1.00 31.72 ?  145 ILE B CG2   1 
ATOM   6760  C  CD1   . ILE B 1 145 ? 144.512 145.409 172.362 1.00 28.63 ?  145 ILE B CD1   1 
ATOM   6761  N  N     . ASN B 1 146 ? 139.620 145.656 174.650 1.00 28.14 ?  146 ASN B N     1 
ATOM   6762  C  CA    . ASN B 1 146 ? 138.672 144.919 175.476 1.00 28.75 ?  146 ASN B CA    1 
ATOM   6763  C  C     . ASN B 1 146 ? 137.790 144.006 174.643 1.00 30.68 ?  146 ASN B C     1 
ATOM   6764  O  O     . ASN B 1 146 ? 137.039 143.206 175.214 1.00 37.17 ?  146 ASN B O     1 
ATOM   6765  C  CB    . ASN B 1 146 ? 137.798 145.882 176.279 1.00 28.50 ?  146 ASN B CB    1 
ATOM   6766  C  CG    . ASN B 1 146 ? 138.580 146.644 177.327 1.00 31.95 ?  146 ASN B CG    1 
ATOM   6767  O  OD1   . ASN B 1 146 ? 139.673 146.238 177.720 1.00 33.23 ?  146 ASN B OD1   1 
ATOM   6768  N  ND2   . ASN B 1 146 ? 138.022 147.758 177.787 1.00 31.99 ?  146 ASN B ND2   1 
ATOM   6769  N  N     . GLN B 1 147 ? 137.857 144.125 173.317 1.00 27.45 ?  147 GLN B N     1 
ATOM   6770  C  CA    . GLN B 1 147 ? 137.070 143.318 172.390 1.00 23.39 ?  147 GLN B CA    1 
ATOM   6771  C  C     . GLN B 1 147 ? 135.575 143.507 172.608 1.00 23.64 ?  147 GLN B C     1 
ATOM   6772  O  O     . GLN B 1 147 ? 134.788 142.583 172.407 1.00 30.53 ?  147 GLN B O     1 
ATOM   6773  C  CB    . GLN B 1 147 ? 137.451 141.838 172.482 1.00 26.93 ?  147 GLN B CB    1 
ATOM   6774  C  CG    . GLN B 1 147 ? 138.881 141.553 172.060 1.00 20.38 ?  147 GLN B CG    1 
ATOM   6775  C  CD    . GLN B 1 147 ? 139.069 140.137 171.568 1.00 27.43 ?  147 GLN B CD    1 
ATOM   6776  O  OE1   . GLN B 1 147 ? 139.759 139.899 170.576 1.00 28.19 ?  147 GLN B OE1   1 
ATOM   6777  N  NE2   . GLN B 1 147 ? 138.459 139.184 172.260 1.00 34.56 ?  147 GLN B NE2   1 
ATOM   6778  N  N     . GLU B 1 148 ? 135.177 144.704 173.038 1.00 26.03 ?  148 GLU B N     1 
ATOM   6779  C  CA    . GLU B 1 148 ? 133.759 145.039 173.109 1.00 23.10 ?  148 GLU B CA    1 
ATOM   6780  C  C     . GLU B 1 148 ? 133.173 145.283 171.727 1.00 26.63 ?  148 GLU B C     1 
ATOM   6781  O  O     . GLU B 1 148 ? 132.018 144.923 171.472 1.00 32.90 ?  148 GLU B O     1 
ATOM   6782  C  CB    . GLU B 1 148 ? 133.553 146.272 173.987 1.00 21.39 ?  148 GLU B CB    1 
ATOM   6783  C  CG    . GLU B 1 148 ? 133.993 146.091 175.426 1.00 26.46 ?  148 GLU B CG    1 
ATOM   6784  C  CD    . GLU B 1 148 ? 134.003 147.395 176.194 1.00 32.26 ?  148 GLU B CD    1 
ATOM   6785  O  OE1   . GLU B 1 148 ? 134.994 148.146 176.083 1.00 33.54 ?  148 GLU B OE1   1 
ATOM   6786  O  OE2   . GLU B 1 148 ? 133.017 147.672 176.908 1.00 37.57 -1 148 GLU B OE2   1 
ATOM   6787  N  N     . TYR B 1 149 ? 133.948 145.885 170.831 1.00 23.60 ?  149 TYR B N     1 
ATOM   6788  C  CA    . TYR B 1 149 ? 133.516 146.177 169.475 1.00 19.15 ?  149 TYR B CA    1 
ATOM   6789  C  C     . TYR B 1 149 ? 134.556 145.671 168.492 1.00 22.53 ?  149 TYR B C     1 
ATOM   6790  O  O     . TYR B 1 149 ? 135.760 145.745 168.751 1.00 28.88 ?  149 TYR B O     1 
ATOM   6791  C  CB    . TYR B 1 149 ? 133.289 147.674 169.270 1.00 21.16 ?  149 TYR B CB    1 
ATOM   6792  C  CG    . TYR B 1 149 ? 133.072 148.069 167.829 1.00 21.61 ?  149 TYR B CG    1 
ATOM   6793  C  CD1   . TYR B 1 149 ? 131.951 147.641 167.131 1.00 13.92 ?  149 TYR B CD1   1 
ATOM   6794  C  CD2   . TYR B 1 149 ? 133.989 148.873 167.167 1.00 19.53 ?  149 TYR B CD2   1 
ATOM   6795  C  CE1   . TYR B 1 149 ? 131.752 148.002 165.814 1.00 17.41 ?  149 TYR B CE1   1 
ATOM   6796  C  CE2   . TYR B 1 149 ? 133.798 149.240 165.853 1.00 20.91 ?  149 TYR B CE2   1 
ATOM   6797  C  CZ    . TYR B 1 149 ? 132.678 148.803 165.180 1.00 20.04 ?  149 TYR B CZ    1 
ATOM   6798  O  OH    . TYR B 1 149 ? 132.487 149.167 163.869 1.00 18.44 ?  149 TYR B OH    1 
ATOM   6799  N  N     . GLN B 1 150 ? 134.083 145.155 167.368 1.00 17.68 ?  150 GLN B N     1 
ATOM   6800  C  CA    . GLN B 1 150 ? 134.946 144.634 166.316 1.00 10.71 ?  150 GLN B CA    1 
ATOM   6801  C  C     . GLN B 1 150 ? 134.542 145.250 164.988 1.00 20.38 ?  150 GLN B C     1 
ATOM   6802  O  O     . GLN B 1 150 ? 133.417 145.003 164.511 1.00 23.27 ?  150 GLN B O     1 
ATOM   6803  C  CB    . GLN B 1 150 ? 134.849 143.111 166.257 1.00 17.41 ?  150 GLN B CB    1 
ATOM   6804  C  CG    . GLN B 1 150 ? 135.676 142.480 165.166 1.00 18.97 ?  150 GLN B CG    1 
ATOM   6805  C  CD    . GLN B 1 150 ? 137.141 142.851 165.251 1.00 17.16 ?  150 GLN B CD    1 
ATOM   6806  O  OE1   . GLN B 1 150 ? 137.820 142.529 166.224 1.00 30.40 ?  150 GLN B OE1   1 
ATOM   6807  N  NE2   . GLN B 1 150 ? 137.637 143.529 164.226 1.00 15.84 ?  150 GLN B NE2   1 
ATOM   6808  N  N     . PRO B 1 151 ? 135.390 146.070 164.371 1.00 26.31 ?  151 PRO B N     1 
ATOM   6809  C  CA    . PRO B 1 151 ? 135.107 146.522 163.007 1.00 16.21 ?  151 PRO B CA    1 
ATOM   6810  C  C     . PRO B 1 151 ? 135.093 145.343 162.049 1.00 16.18 ?  151 PRO B C     1 
ATOM   6811  O  O     . PRO B 1 151 ? 135.743 144.321 162.278 1.00 21.62 ?  151 PRO B O     1 
ATOM   6812  C  CB    . PRO B 1 151 ? 136.262 147.483 162.701 1.00 18.71 ?  151 PRO B CB    1 
ATOM   6813  C  CG    . PRO B 1 151 ? 136.788 147.891 164.039 1.00 18.97 ?  151 PRO B CG    1 
ATOM   6814  C  CD    . PRO B 1 151 ? 136.590 146.710 164.934 1.00 21.62 ?  151 PRO B CD    1 
ATOM   6815  N  N     . SER B 1 152 ? 134.323 145.487 160.975 1.00 21.04 ?  152 SER B N     1 
ATOM   6816  C  CA    . SER B 1 152 ? 134.194 144.418 159.997 1.00 14.61 ?  152 SER B CA    1 
ATOM   6817  C  C     . SER B 1 152 ? 135.554 144.053 159.410 1.00 22.02 ?  152 SER B C     1 
ATOM   6818  O  O     . SER B 1 152 ? 136.535 144.790 159.533 1.00 25.96 ?  152 SER B O     1 
ATOM   6819  C  CB    . SER B 1 152 ? 133.240 144.827 158.878 1.00 20.91 ?  152 SER B CB    1 
ATOM   6820  O  OG    . SER B 1 152 ? 133.788 145.873 158.098 1.00 24.93 ?  152 SER B OG    1 
ATOM   6821  N  N     . THR B 1 153 ? 135.601 142.886 158.769 1.00 28.20 ?  153 THR B N     1 
ATOM   6822  C  CA    . THR B 1 153 ? 136.832 142.426 158.129 1.00 20.89 ?  153 THR B CA    1 
ATOM   6823  C  C     . THR B 1 153 ? 137.422 143.446 157.160 1.00 27.54 ?  153 THR B C     1 
ATOM   6824  O  O     . THR B 1 153 ? 138.636 143.693 157.236 1.00 27.63 ?  153 THR B O     1 
ATOM   6825  C  CB    . THR B 1 153 ? 136.571 141.079 157.438 1.00 25.86 ?  153 THR B CB    1 
ATOM   6826  O  OG1   . THR B 1 153 ? 136.451 140.049 158.426 1.00 29.62 ?  153 THR B OG1   1 
ATOM   6827  C  CG2   . THR B 1 153 ? 137.702 140.732 156.482 1.00 25.78 ?  153 THR B CG2   1 
ATOM   6828  N  N     . PRO B 1 154 ? 136.655 144.079 156.260 1.00 25.81 ?  154 PRO B N     1 
ATOM   6829  C  CA    . PRO B 1 154 ? 137.265 145.133 155.429 1.00 19.80 ?  154 PRO B CA    1 
ATOM   6830  C  C     . PRO B 1 154 ? 137.840 146.278 156.245 1.00 20.96 ?  154 PRO B C     1 
ATOM   6831  O  O     . PRO B 1 154 ? 138.979 146.699 156.006 1.00 26.68 ?  154 PRO B O     1 
ATOM   6832  C  CB    . PRO B 1 154 ? 136.102 145.590 154.539 1.00 21.37 ?  154 PRO B CB    1 
ATOM   6833  C  CG    . PRO B 1 154 ? 135.175 144.442 154.507 1.00 24.97 ?  154 PRO B CG    1 
ATOM   6834  C  CD    . PRO B 1 154 ? 135.259 143.823 155.861 1.00 19.97 ?  154 PRO B CD    1 
ATOM   6835  N  N     . THR B 1 155 ? 137.085 146.783 157.223 1.00 22.65 ?  155 THR B N     1 
ATOM   6836  C  CA    . THR B 1 155 ? 137.556 147.912 158.017 1.00 20.13 ?  155 THR B CA    1 
ATOM   6837  C  C     . THR B 1 155 ? 138.734 147.516 158.899 1.00 24.21 ?  155 THR B C     1 
ATOM   6838  O  O     . THR B 1 155 ? 139.755 148.210 158.935 1.00 29.73 ?  155 THR B O     1 
ATOM   6839  C  CB    . THR B 1 155 ? 136.416 148.472 158.865 1.00 22.59 ?  155 THR B CB    1 
ATOM   6840  O  OG1   . THR B 1 155 ? 135.287 148.753 158.028 1.00 23.45 ?  155 THR B OG1   1 
ATOM   6841  C  CG2   . THR B 1 155 ? 136.851 149.749 159.558 1.00 17.64 ?  155 THR B CG2   1 
ATOM   6842  N  N     . PHE B 1 156 ? 138.612 146.399 159.619 1.00 23.30 ?  156 PHE B N     1 
ATOM   6843  C  CA    . PHE B 1 156 ? 139.687 145.978 160.512 1.00 20.13 ?  156 PHE B CA    1 
ATOM   6844  C  C     . PHE B 1 156 ? 140.961 145.664 159.738 1.00 29.69 ?  156 PHE B C     1 
ATOM   6845  O  O     . PHE B 1 156 ? 142.064 146.010 160.175 1.00 29.95 ?  156 PHE B O     1 
ATOM   6846  C  CB    . PHE B 1 156 ? 139.248 144.766 161.332 1.00 23.60 ?  156 PHE B CB    1 
ATOM   6847  C  CG    . PHE B 1 156 ? 140.099 144.513 162.543 1.00 28.03 ?  156 PHE B CG    1 
ATOM   6848  C  CD1   . PHE B 1 156 ? 140.236 145.482 163.523 1.00 24.88 ?  156 PHE B CD1   1 
ATOM   6849  C  CD2   . PHE B 1 156 ? 140.764 143.310 162.700 1.00 23.77 ?  156 PHE B CD2   1 
ATOM   6850  C  CE1   . PHE B 1 156 ? 141.019 145.253 164.637 1.00 26.16 ?  156 PHE B CE1   1 
ATOM   6851  C  CE2   . PHE B 1 156 ? 141.549 143.077 163.811 1.00 22.91 ?  156 PHE B CE2   1 
ATOM   6852  C  CZ    . PHE B 1 156 ? 141.676 144.049 164.781 1.00 29.01 ?  156 PHE B CZ    1 
ATOM   6853  N  N     . LEU B 1 157 ? 140.828 145.008 158.585 1.00 30.11 ?  157 LEU B N     1 
ATOM   6854  C  CA    . LEU B 1 157 ? 141.996 144.595 157.817 1.00 26.59 ?  157 LEU B CA    1 
ATOM   6855  C  C     . LEU B 1 157 ? 142.633 145.758 157.066 1.00 31.97 ?  157 LEU B C     1 
ATOM   6856  O  O     . LEU B 1 157 ? 143.861 145.817 156.943 1.00 40.37 ?  157 LEU B O     1 
ATOM   6857  C  CB    . LEU B 1 157 ? 141.602 143.482 156.843 1.00 30.79 ?  157 LEU B CB    1 
ATOM   6858  C  CG    . LEU B 1 157 ? 142.624 143.053 155.791 1.00 29.61 ?  157 LEU B CG    1 
ATOM   6859  C  CD1   . LEU B 1 157 ? 143.834 142.414 156.446 1.00 32.68 ?  157 LEU B CD1   1 
ATOM   6860  C  CD2   . LEU B 1 157 ? 141.990 142.102 154.790 1.00 30.30 ?  157 LEU B CD2   1 
ATOM   6861  N  N     . ASN B 1 158 ? 141.829 146.699 156.567 1.00 30.57 ?  158 ASN B N     1 
ATOM   6862  C  CA    . ASN B 1 158 ? 142.312 147.678 155.606 1.00 29.15 ?  158 ASN B CA    1 
ATOM   6863  C  C     . ASN B 1 158 ? 142.443 149.093 156.151 1.00 32.44 ?  158 ASN B C     1 
ATOM   6864  O  O     . ASN B 1 158 ? 142.937 149.963 155.427 1.00 39.63 ?  158 ASN B O     1 
ATOM   6865  C  CB    . ASN B 1 158 ? 141.387 147.701 154.381 1.00 29.82 ?  158 ASN B CB    1 
ATOM   6866  C  CG    . ASN B 1 158 ? 141.349 146.373 153.656 1.00 35.71 ?  158 ASN B CG    1 
ATOM   6867  O  OD1   . ASN B 1 158 ? 142.311 145.607 153.689 1.00 40.03 ?  158 ASN B OD1   1 
ATOM   6868  N  ND2   . ASN B 1 158 ? 140.232 146.090 152.998 1.00 35.98 ?  158 ASN B ND2   1 
ATOM   6869  N  N     . ALA B 1 159 ? 142.018 149.358 157.385 1.00 31.90 ?  159 ALA B N     1 
ATOM   6870  C  CA    . ALA B 1 159 ? 142.078 150.720 157.904 1.00 33.22 ?  159 ALA B CA    1 
ATOM   6871  C  C     . ALA B 1 159 ? 143.522 151.193 158.009 1.00 38.83 ?  159 ALA B C     1 
ATOM   6872  O  O     . ALA B 1 159 ? 144.373 150.511 158.588 1.00 42.87 ?  159 ALA B O     1 
ATOM   6873  C  CB    . ALA B 1 159 ? 141.399 150.805 159.270 1.00 32.12 ?  159 ALA B CB    1 
ATOM   6874  N  N     . GLY B 1 160 ? 143.797 152.364 157.443 1.00 45.42 ?  160 GLY B N     1 
ATOM   6875  C  CA    . GLY B 1 160 ? 145.115 152.954 157.534 1.00 40.42 ?  160 GLY B CA    1 
ATOM   6876  C  C     . GLY B 1 160 ? 146.177 152.316 156.670 1.00 40.71 ?  160 GLY B C     1 
ATOM   6877  O  O     . GLY B 1 160 ? 147.361 152.617 156.856 1.00 45.57 ?  160 GLY B O     1 
ATOM   6878  N  N     . ARG B 1 161 ? 145.803 151.448 155.736 1.00 43.00 ?  161 ARG B N     1 
ATOM   6879  C  CA    . ARG B 1 161 ? 146.755 150.767 154.872 1.00 44.08 ?  161 ARG B CA    1 
ATOM   6880  C  C     . ARG B 1 161 ? 146.797 151.436 153.505 1.00 46.63 ?  161 ARG B C     1 
ATOM   6881  O  O     . ARG B 1 161 ? 145.765 151.852 152.971 1.00 46.53 ?  161 ARG B O     1 
ATOM   6882  C  CB    . ARG B 1 161 ? 146.395 149.289 154.716 1.00 38.66 ?  161 ARG B CB    1 
ATOM   6883  C  CG    . ARG B 1 161 ? 146.646 148.453 155.958 1.00 39.48 ?  161 ARG B CG    1 
ATOM   6884  C  CD    . ARG B 1 161 ? 146.703 146.972 155.626 1.00 40.50 ?  161 ARG B CD    1 
ATOM   6885  N  NE    . ARG B 1 161 ? 146.709 146.144 156.826 1.00 44.00 ?  161 ARG B NE    1 
ATOM   6886  C  CZ    . ARG B 1 161 ? 146.683 144.818 156.824 1.00 44.80 ?  161 ARG B CZ    1 
ATOM   6887  N  NH1   . ARG B 1 161 ? 146.657 144.130 155.696 1.00 44.14 1  161 ARG B NH1   1 
ATOM   6888  N  NH2   . ARG B 1 161 ? 146.681 144.168 157.984 1.00 43.06 ?  161 ARG B NH2   1 
ATOM   6889  N  N     . LYS B 1 162 ? 148.005 151.548 152.944 1.00 53.05 ?  162 LYS B N     1 
ATOM   6890  C  CA    . LYS B 1 162 ? 148.147 152.130 151.613 1.00 52.29 ?  162 LYS B CA    1 
ATOM   6891  C  C     . LYS B 1 162 ? 147.644 151.176 150.536 1.00 52.62 ?  162 LYS B C     1 
ATOM   6892  O  O     . LYS B 1 162 ? 146.930 151.590 149.616 1.00 52.82 ?  162 LYS B O     1 
ATOM   6893  C  CB    . LYS B 1 162 ? 149.605 152.512 151.361 1.00 52.13 ?  162 LYS B CB    1 
ATOM   6894  C  CG    . LYS B 1 162 ? 149.910 152.892 149.922 1.00 52.46 ?  162 LYS B CG    1 
ATOM   6895  C  CD    . LYS B 1 162 ? 149.711 154.382 149.687 1.00 54.30 ?  162 LYS B CD    1 
ATOM   6896  C  CE    . LYS B 1 162 ? 150.542 155.212 150.651 1.00 54.39 ?  162 LYS B CE    1 
ATOM   6897  N  NZ    . LYS B 1 162 ? 149.878 156.505 150.979 1.00 54.64 1  162 LYS B NZ    1 
ATOM   6898  N  N     . ARG B 1 163 ? 147.995 149.893 150.640 1.00 53.33 ?  163 ARG B N     1 
ATOM   6899  C  CA    . ARG B 1 163 ? 147.566 148.873 149.690 1.00 55.14 ?  163 ARG B CA    1 
ATOM   6900  C  C     . ARG B 1 163 ? 146.170 148.342 149.994 1.00 57.86 ?  163 ARG B C     1 
ATOM   6901  O  O     . ARG B 1 163 ? 145.810 147.249 149.539 1.00 56.49 ?  163 ARG B O     1 
ATOM   6902  C  CB    . ARG B 1 163 ? 148.578 147.723 149.665 1.00 56.25 ?  163 ARG B CB    1 
ATOM   6903  C  CG    . ARG B 1 163 ? 148.661 146.986 148.335 1.00 58.12 ?  163 ARG B CG    1 
ATOM   6904  C  CD    . ARG B 1 163 ? 149.054 145.528 148.528 1.00 56.45 ?  163 ARG B CD    1 
ATOM   6905  N  NE    . ARG B 1 163 ? 148.409 144.925 149.689 1.00 59.28 ?  163 ARG B NE    1 
ATOM   6906  C  CZ    . ARG B 1 163 ? 147.165 144.466 149.705 1.00 58.45 ?  163 ARG B CZ    1 
ATOM   6907  N  NH1   . ARG B 1 163 ? 146.392 144.524 148.632 1.00 56.93 1  163 ARG B NH1   1 
ATOM   6908  N  NH2   . ARG B 1 163 ? 146.683 143.933 150.825 1.00 56.83 ?  163 ARG B NH2   1 
ATOM   6909  N  N     . ARG B 1 164 ? 145.381 149.093 150.755 1.00 55.68 ?  164 ARG B N     1 
ATOM   6910  C  CA    . ARG B 1 164 ? 144.063 148.651 151.173 1.00 50.63 ?  164 ARG B CA    1 
ATOM   6911  C  C     . ARG B 1 164 ? 143.080 148.664 150.006 1.00 50.63 ?  164 ARG B C     1 
ATOM   6912  O  O     . ARG B 1 164 ? 143.314 149.274 148.958 1.00 50.44 ?  164 ARG B O     1 
ATOM   6913  C  CB    . ARG B 1 164 ? 143.533 149.545 152.291 1.00 48.84 ?  164 ARG B CB    1 
ATOM   6914  C  CG    . ARG B 1 164 ? 142.963 150.868 151.803 1.00 45.63 ?  164 ARG B CG    1 
ATOM   6915  C  CD    . ARG B 1 164 ? 141.968 151.444 152.794 1.00 48.21 ?  164 ARG B CD    1 
ATOM   6916  N  NE    . ARG B 1 164 ? 141.326 152.651 152.289 1.00 50.38 ?  164 ARG B NE    1 
ATOM   6917  C  CZ    . ARG B 1 164 ? 140.990 153.691 153.041 1.00 53.94 ?  164 ARG B CZ    1 
ATOM   6918  N  NH1   . ARG B 1 164 ? 141.229 153.708 154.342 1.00 51.60 1  164 ARG B NH1   1 
ATOM   6919  N  NH2   . ARG B 1 164 ? 140.401 154.740 152.473 1.00 53.54 ?  164 ARG B NH2   1 
ATOM   6920  N  N     . GLY B 1 165 ? 141.968 147.970 150.203 1.00 49.03 ?  165 GLY B N     1 
ATOM   6921  C  CA    . GLY B 1 165 ? 140.813 148.064 149.333 1.00 45.13 ?  165 GLY B CA    1 
ATOM   6922  C  C     . GLY B 1 165 ? 139.814 149.070 149.859 1.00 48.10 ?  165 GLY B C     1 
ATOM   6923  O  O     . GLY B 1 165 ? 140.171 150.172 150.287 1.00 48.97 ?  165 GLY B O     1 
ATOM   6924  N  N     . GLU B 1 166 ? 138.542 148.690 149.826 1.00 43.00 ?  166 GLU B N     1 
ATOM   6925  C  CA    . GLU B 1 166 ? 137.493 149.510 150.410 1.00 39.82 ?  166 GLU B CA    1 
ATOM   6926  C  C     . GLU B 1 166 ? 137.069 148.946 151.761 1.00 37.59 ?  166 GLU B C     1 
ATOM   6927  O  O     . GLU B 1 166 ? 137.106 147.734 151.991 1.00 33.46 ?  166 GLU B O     1 
ATOM   6928  C  CB    . GLU B 1 166 ? 136.284 149.600 149.478 1.00 36.97 ?  166 GLU B CB    1 
ATOM   6929  C  CG    . GLU B 1 166 ? 136.398 150.697 148.437 1.00 41.28 ?  166 GLU B CG    1 
ATOM   6930  C  CD    . GLU B 1 166 ? 136.447 152.083 149.048 1.00 42.78 ?  166 GLU B CD    1 
ATOM   6931  O  OE1   . GLU B 1 166 ? 135.809 152.293 150.101 1.00 47.42 ?  166 GLU B OE1   1 
ATOM   6932  O  OE2   . GLU B 1 166 ? 137.125 152.961 148.477 1.00 39.22 -1 166 GLU B OE2   1 
ATOM   6933  N  N     . LEU B 1 167 ? 136.670 149.845 152.660 1.00 30.71 ?  167 LEU B N     1 
ATOM   6934  C  CA    . LEU B 1 167 ? 136.228 149.447 153.988 1.00 23.73 ?  167 LEU B CA    1 
ATOM   6935  C  C     . LEU B 1 167 ? 134.784 148.969 154.017 1.00 29.03 ?  167 LEU B C     1 
ATOM   6936  O  O     . LEU B 1 167 ? 134.353 148.417 155.035 1.00 30.76 ?  167 LEU B O     1 
ATOM   6937  C  CB    . LEU B 1 167 ? 136.396 150.608 154.970 1.00 30.06 ?  167 LEU B CB    1 
ATOM   6938  C  CG    . LEU B 1 167 ? 137.793 151.210 155.125 1.00 26.48 ?  167 LEU B CG    1 
ATOM   6939  C  CD1   . LEU B 1 167 ? 137.870 151.996 156.413 1.00 27.89 ?  167 LEU B CD1   1 
ATOM   6940  C  CD2   . LEU B 1 167 ? 138.859 150.133 155.101 1.00 26.02 ?  167 LEU B CD2   1 
ATOM   6941  N  N     . VAL B 1 168 ? 134.032 149.166 152.939 1.00 29.42 ?  168 VAL B N     1 
ATOM   6942  C  CA    . VAL B 1 168 ? 132.643 148.727 152.887 1.00 22.91 ?  168 VAL B CA    1 
ATOM   6943  C  C     . VAL B 1 168 ? 132.601 147.264 152.470 1.00 26.85 ?  168 VAL B C     1 
ATOM   6944  O  O     . VAL B 1 168 ? 133.250 146.863 151.496 1.00 28.67 ?  168 VAL B O     1 
ATOM   6945  C  CB    . VAL B 1 168 ? 131.830 149.604 151.924 1.00 27.41 ?  168 VAL B CB    1 
ATOM   6946  C  CG1   . VAL B 1 168 ? 130.354 149.262 152.022 1.00 28.93 ?  168 VAL B CG1   1 
ATOM   6947  C  CG2   . VAL B 1 168 ? 132.060 151.072 152.227 1.00 27.27 ?  168 VAL B CG2   1 
ATOM   6948  N  N     . SER B 1 169 ? 131.836 146.462 153.211 1.00 35.86 ?  169 SER B N     1 
ATOM   6949  C  CA    . SER B 1 169 ? 131.786 145.028 152.955 1.00 37.59 ?  169 SER B CA    1 
ATOM   6950  C  C     . SER B 1 169 ? 130.843 144.693 151.804 1.00 36.82 ?  169 SER B C     1 
ATOM   6951  O  O     . SER B 1 169 ? 131.213 143.958 150.884 1.00 34.09 ?  169 SER B O     1 
ATOM   6952  C  CB    . SER B 1 169 ? 131.364 144.287 154.225 1.00 31.71 ?  169 SER B CB    1 
ATOM   6953  O  OG    . SER B 1 169 ? 131.387 142.883 154.029 1.00 34.78 ?  169 SER B OG    1 
ATOM   6954  N  N     . CYS B 1 170 ? 129.622 145.219 151.841 1.00 31.77 ?  170 CYS B N     1 
ATOM   6955  C  CA    . CYS B 1 170 ? 128.570 144.817 150.919 1.00 26.64 ?  170 CYS B CA    1 
ATOM   6956  C  C     . CYS B 1 170 ? 128.063 146.011 150.124 1.00 25.35 ?  170 CYS B C     1 
ATOM   6957  O  O     . CYS B 1 170 ? 127.992 147.131 150.639 1.00 24.91 ?  170 CYS B O     1 
ATOM   6958  C  CB    . CYS B 1 170 ? 127.408 144.166 151.674 1.00 34.42 ?  170 CYS B CB    1 
ATOM   6959  S  SG    . CYS B 1 170 ? 126.814 145.129 153.081 1.00 53.61 ?  170 CYS B SG    1 
ATOM   6960  N  N     . PHE B 1 171 ? 127.714 145.758 148.864 1.00 22.77 ?  171 PHE B N     1 
ATOM   6961  C  CA    . PHE B 1 171 ? 127.116 146.752 147.986 1.00 13.83 ?  171 PHE B CA    1 
ATOM   6962  C  C     . PHE B 1 171 ? 125.878 146.160 147.334 1.00 12.90 ?  171 PHE B C     1 
ATOM   6963  O  O     . PHE B 1 171 ? 125.867 144.985 146.956 1.00 24.47 ?  171 PHE B O     1 
ATOM   6964  C  CB    . PHE B 1 171 ? 128.096 147.215 146.907 1.00 16.07 ?  171 PHE B CB    1 
ATOM   6965  C  CG    . PHE B 1 171 ? 129.417 147.667 147.444 1.00 19.04 ?  171 PHE B CG    1 
ATOM   6966  C  CD1   . PHE B 1 171 ? 129.566 148.937 147.970 1.00 15.01 ?  171 PHE B CD1   1 
ATOM   6967  C  CD2   . PHE B 1 171 ? 130.515 146.825 147.416 1.00 18.02 ?  171 PHE B CD2   1 
ATOM   6968  C  CE1   . PHE B 1 171 ? 130.780 149.354 148.464 1.00 13.11 ?  171 PHE B CE1   1 
ATOM   6969  C  CE2   . PHE B 1 171 ? 131.731 147.241 147.907 1.00 15.58 ?  171 PHE B CE2   1 
ATOM   6970  C  CZ    . PHE B 1 171 ? 131.865 148.507 148.431 1.00 15.68 ?  171 PHE B CZ    1 
ATOM   6971  N  N     . LEU B 1 172 ? 124.837 146.976 147.204 1.00 13.06 ?  172 LEU B N     1 
ATOM   6972  C  CA    . LEU B 1 172 ? 123.572 146.556 146.616 1.00 10.19 ?  172 LEU B CA    1 
ATOM   6973  C  C     . LEU B 1 172 ? 123.256 147.470 145.443 1.00 11.41 ?  172 LEU B C     1 
ATOM   6974  O  O     . LEU B 1 172 ? 123.175 148.690 145.612 1.00 17.26 ?  172 LEU B O     1 
ATOM   6975  C  CB    . LEU B 1 172 ? 122.445 146.597 147.648 1.00 13.81 ?  172 LEU B CB    1 
ATOM   6976  C  CG    . LEU B 1 172 ? 122.476 145.597 148.804 1.00 8.92  ?  172 LEU B CG    1 
ATOM   6977  C  CD1   . LEU B 1 172 ? 123.375 146.086 149.927 1.00 10.47 ?  172 LEU B CD1   1 
ATOM   6978  C  CD2   . LEU B 1 172 ? 121.070 145.375 149.311 1.00 10.66 ?  172 LEU B CD2   1 
ATOM   6979  N  N     . LEU B 1 173 ? 123.072 146.882 144.265 1.00 17.95 ?  173 LEU B N     1 
ATOM   6980  C  CA    . LEU B 1 173 ? 122.835 147.633 143.041 1.00 9.04  ?  173 LEU B CA    1 
ATOM   6981  C  C     . LEU B 1 173 ? 121.432 147.371 142.514 1.00 14.71 ?  173 LEU B C     1 
ATOM   6982  O  O     . LEU B 1 173 ? 120.956 146.232 142.523 1.00 20.11 ?  173 LEU B O     1 
ATOM   6983  C  CB    . LEU B 1 173 ? 123.855 147.271 141.961 1.00 13.46 ?  173 LEU B CB    1 
ATOM   6984  C  CG    . LEU B 1 173 ? 125.339 147.313 142.321 1.00 18.36 ?  173 LEU B CG    1 
ATOM   6985  C  CD1   . LEU B 1 173 ? 126.169 146.940 141.106 1.00 21.69 ?  173 LEU B CD1   1 
ATOM   6986  C  CD2   . LEU B 1 173 ? 125.729 148.685 142.844 1.00 20.29 ?  173 LEU B CD2   1 
ATOM   6987  N  N     . GLU B 1 174 ? 120.776 148.434 142.061 1.00 23.41 ?  174 GLU B N     1 
ATOM   6988  C  CA    . GLU B 1 174 ? 119.514 148.324 141.346 1.00 20.21 ?  174 GLU B CA    1 
ATOM   6989  C  C     . GLU B 1 174 ? 119.788 148.385 139.850 1.00 18.27 ?  174 GLU B C     1 
ATOM   6990  O  O     . GLU B 1 174 ? 120.434 149.321 139.371 1.00 27.43 ?  174 GLU B O     1 
ATOM   6991  C  CB    . GLU B 1 174 ? 118.558 149.442 141.759 1.00 23.89 ?  174 GLU B CB    1 
ATOM   6992  C  CG    . GLU B 1 174 ? 117.917 149.249 143.120 1.00 18.30 ?  174 GLU B CG    1 
ATOM   6993  C  CD    . GLU B 1 174 ? 116.412 149.106 143.037 1.00 21.69 ?  174 GLU B CD    1 
ATOM   6994  O  OE1   . GLU B 1 174 ? 115.924 148.497 142.064 1.00 28.18 ?  174 GLU B OE1   1 
ATOM   6995  O  OE2   . GLU B 1 174 ? 115.716 149.605 143.945 1.00 24.53 -1 174 GLU B OE2   1 
ATOM   6996  N  N     . VAL B 1 175 ? 119.299 147.389 139.117 1.00 16.95 ?  175 VAL B N     1 
ATOM   6997  C  CA    . VAL B 1 175 ? 119.529 147.278 137.681 1.00 18.41 ?  175 VAL B CA    1 
ATOM   6998  C  C     . VAL B 1 175 ? 118.234 147.627 136.962 1.00 17.16 ?  175 VAL B C     1 
ATOM   6999  O  O     . VAL B 1 175 ? 117.225 146.926 137.108 1.00 13.81 ?  175 VAL B O     1 
ATOM   7000  C  CB    . VAL B 1 175 ? 120.011 145.872 137.293 1.00 19.90 ?  175 VAL B CB    1 
ATOM   7001  C  CG1   . VAL B 1 175 ? 120.641 145.887 135.908 1.00 14.27 ?  175 VAL B CG1   1 
ATOM   7002  C  CG2   . VAL B 1 175 ? 120.991 145.346 138.327 1.00 14.16 ?  175 VAL B CG2   1 
ATOM   7003  N  N     . ASN B 1 176 ? 118.263 148.707 136.187 1.00 18.38 ?  176 ASN B N     1 
ATOM   7004  C  CA    . ASN B 1 176 ? 117.107 149.096 135.398 1.00 19.52 ?  176 ASN B CA    1 
ATOM   7005  C  C     . ASN B 1 176 ? 117.007 148.236 134.141 1.00 20.93 ?  176 ASN B C     1 
ATOM   7006  O  O     . ASN B 1 176 ? 117.974 147.609 133.704 1.00 19.66 ?  176 ASN B O     1 
ATOM   7007  C  CB    . ASN B 1 176 ? 117.181 150.575 135.021 1.00 18.09 ?  176 ASN B CB    1 
ATOM   7008  C  CG    . ASN B 1 176 ? 115.829 151.251 135.055 1.00 19.52 ?  176 ASN B CG    1 
ATOM   7009  O  OD1   . ASN B 1 176 ? 114.792 150.591 135.055 1.00 27.15 ?  176 ASN B OD1   1 
ATOM   7010  N  ND2   . ASN B 1 176 ? 115.832 152.578 135.082 1.00 21.83 ?  176 ASN B ND2   1 
ATOM   7011  N  N     . ASP B 1 177 ? 115.809 148.222 133.556 1.00 25.27 ?  177 ASP B N     1 
ATOM   7012  C  CA    . ASP B 1 177 ? 115.503 147.355 132.418 1.00 22.19 ?  177 ASP B CA    1 
ATOM   7013  C  C     . ASP B 1 177 ? 115.962 148.036 131.130 1.00 23.70 ?  177 ASP B C     1 
ATOM   7014  O  O     . ASP B 1 177 ? 115.180 148.622 130.377 1.00 26.99 ?  177 ASP B O     1 
ATOM   7015  C  CB    . ASP B 1 177 ? 114.017 147.030 132.386 1.00 18.71 ?  177 ASP B CB    1 
ATOM   7016  C  CG    . ASP B 1 177 ? 113.642 146.125 131.236 1.00 26.22 ?  177 ASP B CG    1 
ATOM   7017  O  OD1   . ASP B 1 177 ? 114.438 145.223 130.905 1.00 30.83 ?  177 ASP B OD1   1 
ATOM   7018  O  OD2   . ASP B 1 177 ? 112.550 146.317 130.664 1.00 29.50 -1 177 ASP B OD2   1 
ATOM   7019  N  N     . SER B 1 178 ? 117.266 147.950 130.877 1.00 19.01 ?  178 SER B N     1 
ATOM   7020  C  CA    . SER B 1 178 ? 117.845 148.479 129.652 1.00 18.37 ?  178 SER B CA    1 
ATOM   7021  C  C     . SER B 1 178 ? 119.230 147.879 129.461 1.00 16.76 ?  178 SER B C     1 
ATOM   7022  O  O     . SER B 1 178 ? 119.878 147.469 130.425 1.00 23.35 ?  178 SER B O     1 
ATOM   7023  C  CB    . SER B 1 178 ? 117.923 150.009 129.674 1.00 14.28 ?  178 SER B CB    1 
ATOM   7024  O  OG    . SER B 1 178 ? 119.161 150.453 130.194 1.00 19.63 ?  178 SER B OG    1 
ATOM   7025  N  N     . LEU B 1 179 ? 119.668 147.826 128.201 1.00 23.99 ?  179 LEU B N     1 
ATOM   7026  C  CA    . LEU B 1 179 ? 121.005 147.320 127.905 1.00 19.15 ?  179 LEU B CA    1 
ATOM   7027  C  C     . LEU B 1 179 ? 122.079 148.224 128.492 1.00 14.42 ?  179 LEU B C     1 
ATOM   7028  O  O     . LEU B 1 179 ? 123.098 147.742 128.999 1.00 18.64 ?  179 LEU B O     1 
ATOM   7029  C  CB    . LEU B 1 179 ? 121.196 147.178 126.395 1.00 20.55 ?  179 LEU B CB    1 
ATOM   7030  C  CG    . LEU B 1 179 ? 122.520 146.553 125.957 1.00 17.53 ?  179 LEU B CG    1 
ATOM   7031  C  CD1   . LEU B 1 179 ? 122.616 145.111 126.437 1.00 14.12 ?  179 LEU B CD1   1 
ATOM   7032  C  CD2   . LEU B 1 179 ? 122.685 146.636 124.450 1.00 15.45 ?  179 LEU B CD2   1 
ATOM   7033  N  N     . ASN B 1 180 ? 121.875 149.542 128.421 1.00 18.45 ?  180 ASN B N     1 
ATOM   7034  C  CA    . ASN B 1 180 ? 122.821 150.471 129.029 1.00 19.17 ?  180 ASN B CA    1 
ATOM   7035  C  C     . ASN B 1 180 ? 122.921 150.240 130.529 1.00 19.71 ?  180 ASN B C     1 
ATOM   7036  O  O     . ASN B 1 180 ? 124.023 150.201 131.089 1.00 23.44 ?  180 ASN B O     1 
ATOM   7037  C  CB    . ASN B 1 180 ? 122.401 151.912 128.740 1.00 18.93 ?  180 ASN B CB    1 
ATOM   7038  C  CG    . ASN B 1 180 ? 122.774 152.361 127.345 1.00 24.64 ?  180 ASN B CG    1 
ATOM   7039  O  OD1   . ASN B 1 180 ? 123.668 151.796 126.716 1.00 31.55 ?  180 ASN B OD1   1 
ATOM   7040  N  ND2   . ASN B 1 180 ? 122.084 153.380 126.849 1.00 25.83 ?  180 ASN B ND2   1 
ATOM   7041  N  N     . ASP B 1 181 ? 121.778 150.065 131.192 1.00 19.83 ?  181 ASP B N     1 
ATOM   7042  C  CA    . ASP B 1 181 ? 121.778 149.830 132.630 1.00 15.41 ?  181 ASP B CA    1 
ATOM   7043  C  C     . ASP B 1 181 ? 122.385 148.477 132.973 1.00 14.51 ?  181 ASP B C     1 
ATOM   7044  O  O     . ASP B 1 181 ? 123.082 148.347 133.983 1.00 25.19 ?  181 ASP B O     1 
ATOM   7045  C  CB    . ASP B 1 181 ? 120.356 149.943 133.175 1.00 21.97 ?  181 ASP B CB    1 
ATOM   7046  C  CG    . ASP B 1 181 ? 119.829 151.363 133.131 1.00 24.91 ?  181 ASP B CG    1 
ATOM   7047  O  OD1   . ASP B 1 181 ? 120.329 152.206 133.904 1.00 24.60 ?  181 ASP B OD1   1 
ATOM   7048  O  OD2   . ASP B 1 181 ? 118.916 151.638 132.326 1.00 29.14 -1 181 ASP B OD2   1 
ATOM   7049  N  N     . ILE B 1 182 ? 122.140 147.459 132.147 1.00 15.82 ?  182 ILE B N     1 
ATOM   7050  C  CA    . ILE B 1 182 ? 122.725 146.142 132.393 1.00 17.64 ?  182 ILE B CA    1 
ATOM   7051  C  C     . ILE B 1 182 ? 124.244 146.201 132.269 1.00 17.43 ?  182 ILE B C     1 
ATOM   7052  O  O     . ILE B 1 182 ? 124.976 145.656 133.105 1.00 21.16 ?  182 ILE B O     1 
ATOM   7053  C  CB    . ILE B 1 182 ? 122.118 145.101 131.435 1.00 18.63 ?  182 ILE B CB    1 
ATOM   7054  C  CG1   . ILE B 1 182 ? 120.736 144.670 131.925 1.00 15.17 ?  182 ILE B CG1   1 
ATOM   7055  C  CG2   . ILE B 1 182 ? 123.031 143.894 131.297 1.00 20.80 ?  182 ILE B CG2   1 
ATOM   7056  C  CD1   . ILE B 1 182 ? 119.937 143.919 130.894 1.00 16.89 ?  182 ILE B CD1   1 
ATOM   7057  N  N     . SER B 1 183 ? 124.740 146.862 131.221 1.00 17.86 ?  183 SER B N     1 
ATOM   7058  C  CA    . SER B 1 183 ? 126.182 146.993 131.043 1.00 18.73 ?  183 SER B CA    1 
ATOM   7059  C  C     . SER B 1 183 ? 126.807 147.808 132.167 1.00 21.57 ?  183 SER B C     1 
ATOM   7060  O  O     . SER B 1 183 ? 127.891 147.472 132.658 1.00 28.03 ?  183 SER B O     1 
ATOM   7061  C  CB    . SER B 1 183 ? 126.484 147.621 129.685 1.00 15.98 ?  183 SER B CB    1 
ATOM   7062  O  OG    . SER B 1 183 ? 125.870 148.890 129.564 1.00 30.83 ?  183 SER B OG    1 
ATOM   7063  N  N     . ARG B 1 184 ? 126.134 148.881 132.594 1.00 18.88 ?  184 ARG B N     1 
ATOM   7064  C  CA    . ARG B 1 184 ? 126.641 149.663 133.715 1.00 16.57 ?  184 ARG B CA    1 
ATOM   7065  C  C     . ARG B 1 184 ? 126.652 148.843 134.999 1.00 25.25 ?  184 ARG B C     1 
ATOM   7066  O  O     . ARG B 1 184 ? 127.568 148.972 135.813 1.00 29.17 ?  184 ARG B O     1 
ATOM   7067  C  CB    . ARG B 1 184 ? 125.810 150.930 133.897 1.00 15.37 ?  184 ARG B CB    1 
ATOM   7068  C  CG    . ARG B 1 184 ? 126.431 151.925 134.860 1.00 24.71 ?  184 ARG B CG    1 
ATOM   7069  C  CD    . ARG B 1 184 ? 127.843 152.288 134.440 1.00 24.41 ?  184 ARG B CD    1 
ATOM   7070  N  NE    . ARG B 1 184 ? 127.853 153.321 133.412 1.00 31.42 ?  184 ARG B NE    1 
ATOM   7071  C  CZ    . ARG B 1 184 ? 128.947 153.916 132.958 1.00 33.23 ?  184 ARG B CZ    1 
ATOM   7072  N  NH1   . ARG B 1 184 ? 130.147 153.587 133.405 1.00 27.36 1  184 ARG B NH1   1 
ATOM   7073  N  NH2   . ARG B 1 184 ? 128.834 154.862 132.031 1.00 28.64 ?  184 ARG B NH2   1 
ATOM   7074  N  N     . ALA B 1 185 ? 125.636 148.002 135.200 1.00 22.10 ?  185 ALA B N     1 
ATOM   7075  C  CA    . ALA B 1 185 ? 125.608 147.141 136.376 1.00 11.35 ?  185 ALA B CA    1 
ATOM   7076  C  C     . ALA B 1 185 ? 126.756 146.143 136.352 1.00 15.81 ?  185 ALA B C     1 
ATOM   7077  O  O     . ALA B 1 185 ? 127.381 145.883 137.384 1.00 20.15 ?  185 ALA B O     1 
ATOM   7078  C  CB    . ALA B 1 185 ? 124.268 146.413 136.466 1.00 15.68 ?  185 ALA B CB    1 
ATOM   7079  N  N     . ILE B 1 186 ? 127.045 145.571 135.181 1.00 24.17 ?  186 ILE B N     1 
ATOM   7080  C  CA    . ILE B 1 186 ? 128.185 144.663 135.060 1.00 21.97 ?  186 ILE B CA    1 
ATOM   7081  C  C     . ILE B 1 186 ? 129.484 145.395 135.379 1.00 20.56 ?  186 ILE B C     1 
ATOM   7082  O  O     . ILE B 1 186 ? 130.344 144.885 136.113 1.00 26.55 ?  186 ILE B O     1 
ATOM   7083  C  CB    . ILE B 1 186 ? 128.221 144.035 133.654 1.00 26.98 ?  186 ILE B CB    1 
ATOM   7084  C  CG1   . ILE B 1 186 ? 127.009 143.130 133.437 1.00 20.24 ?  186 ILE B CG1   1 
ATOM   7085  C  CG2   . ILE B 1 186 ? 129.508 143.255 133.446 1.00 22.94 ?  186 ILE B CG2   1 
ATOM   7086  C  CD1   . ILE B 1 186 ? 126.675 142.915 131.980 1.00 23.18 ?  186 ILE B CD1   1 
ATOM   7087  N  N     . ASP B 1 187 ? 129.642 146.604 134.835 1.00 22.65 ?  187 ASP B N     1 
ATOM   7088  C  CA    . ASP B 1 187 ? 130.847 147.387 135.089 1.00 21.24 ?  187 ASP B CA    1 
ATOM   7089  C  C     . ASP B 1 187 ? 130.999 147.701 136.574 1.00 23.70 ?  187 ASP B C     1 
ATOM   7090  O  O     . ASP B 1 187 ? 132.083 147.548 137.145 1.00 29.52 ?  187 ASP B O     1 
ATOM   7091  C  CB    . ASP B 1 187 ? 130.811 148.676 134.268 1.00 21.82 ?  187 ASP B CB    1 
ATOM   7092  C  CG    . ASP B 1 187 ? 131.798 149.714 134.765 1.00 30.86 ?  187 ASP B CG    1 
ATOM   7093  O  OD1   . ASP B 1 187 ? 132.997 149.389 134.892 1.00 30.90 ?  187 ASP B OD1   1 
ATOM   7094  O  OD2   . ASP B 1 187 ? 131.373 150.858 135.029 1.00 35.86 -1 187 ASP B OD2   1 
ATOM   7095  N  N     . ILE B 1 188 ? 129.913 148.138 137.215 1.00 21.60 ?  188 ILE B N     1 
ATOM   7096  C  CA    . ILE B 1 188 ? 129.969 148.502 138.627 1.00 19.74 ?  188 ILE B CA    1 
ATOM   7097  C  C     . ILE B 1 188 ? 130.218 147.271 139.489 1.00 21.48 ?  188 ILE B C     1 
ATOM   7098  O  O     . ILE B 1 188 ? 130.923 147.340 140.501 1.00 28.68 ?  188 ILE B O     1 
ATOM   7099  C  CB    . ILE B 1 188 ? 128.680 149.239 139.038 1.00 21.13 ?  188 ILE B CB    1 
ATOM   7100  C  CG1   . ILE B 1 188 ? 128.567 150.570 138.296 1.00 22.43 ?  188 ILE B CG1   1 
ATOM   7101  C  CG2   . ILE B 1 188 ? 128.657 149.496 140.530 1.00 23.49 ?  188 ILE B CG2   1 
ATOM   7102  C  CD1   . ILE B 1 188 ? 127.221 151.239 138.449 1.00 18.85 ?  188 ILE B CD1   1 
ATOM   7103  N  N     . SER B 1 189 ? 129.649 146.126 139.104 1.00 17.21 ?  189 SER B N     1 
ATOM   7104  C  CA    . SER B 1 189 ? 129.909 144.892 139.833 1.00 10.40 ?  189 SER B CA    1 
ATOM   7105  C  C     . SER B 1 189 ? 131.381 144.513 139.757 1.00 22.08 ?  189 SER B C     1 
ATOM   7106  O  O     . SER B 1 189 ? 131.984 144.138 140.768 1.00 23.66 ?  189 SER B O     1 
ATOM   7107  C  CB    . SER B 1 189 ? 129.035 143.766 139.284 1.00 18.67 ?  189 SER B CB    1 
ATOM   7108  O  OG    . SER B 1 189 ? 127.667 144.121 139.324 1.00 25.30 ?  189 SER B OG    1 
ATOM   7109  N  N     . MET B 1 190 ? 131.980 144.613 138.566 1.00 27.49 ?  190 MET B N     1 
ATOM   7110  C  CA    . MET B 1 190 ? 133.409 144.336 138.448 1.00 19.93 ?  190 MET B CA    1 
ATOM   7111  C  C     . MET B 1 190 ? 134.234 145.329 139.256 1.00 19.96 ?  190 MET B C     1 
ATOM   7112  O  O     . MET B 1 190 ? 135.218 144.950 139.899 1.00 24.18 ?  190 MET B O     1 
ATOM   7113  C  CB    . MET B 1 190 ? 133.842 144.350 136.983 1.00 20.87 ?  190 MET B CB    1 
ATOM   7114  C  CG    . MET B 1 190 ? 133.242 143.242 136.144 1.00 22.70 ?  190 MET B CG    1 
ATOM   7115  S  SD    . MET B 1 190 ? 133.988 143.141 134.507 1.00 37.29 ?  190 MET B SD    1 
ATOM   7116  C  CE    . MET B 1 190 ? 132.997 144.326 133.604 1.00 24.55 ?  190 MET B CE    1 
ATOM   7117  N  N     . GLN B 1 191 ? 133.848 146.606 139.236 1.00 19.21 ?  191 GLN B N     1 
ATOM   7118  C  CA    . GLN B 1 191 ? 134.595 147.617 139.980 1.00 23.96 ?  191 GLN B CA    1 
ATOM   7119  C  C     . GLN B 1 191 ? 134.534 147.366 141.481 1.00 23.51 ?  191 GLN B C     1 
ATOM   7120  O  O     . GLN B 1 191 ? 135.541 147.507 142.183 1.00 29.80 ?  191 GLN B O     1 
ATOM   7121  C  CB    . GLN B 1 191 ? 134.064 149.013 139.655 1.00 21.47 ?  191 GLN B CB    1 
ATOM   7122  C  CG    . GLN B 1 191 ? 134.283 149.457 138.220 1.00 20.65 ?  191 GLN B CG    1 
ATOM   7123  C  CD    . GLN B 1 191 ? 135.749 149.588 137.861 1.00 26.80 ?  191 GLN B CD    1 
ATOM   7124  O  OE1   . GLN B 1 191 ? 136.600 149.775 138.730 1.00 30.50 ?  191 GLN B OE1   1 
ATOM   7125  N  NE2   . GLN B 1 191 ? 136.050 149.495 136.572 1.00 25.97 ?  191 GLN B NE2   1 
ATOM   7126  N  N     . LEU B 1 192 ? 133.360 146.999 141.994 1.00 23.86 ?  192 LEU B N     1 
ATOM   7127  C  CA    . LEU B 1 192 ? 133.208 146.784 143.427 1.00 18.39 ?  192 LEU B CA    1 
ATOM   7128  C  C     . LEU B 1 192 ? 133.803 145.459 143.880 1.00 22.39 ?  192 LEU B C     1 
ATOM   7129  O  O     . LEU B 1 192 ? 134.276 145.360 145.017 1.00 33.29 ?  192 LEU B O     1 
ATOM   7130  C  CB    . LEU B 1 192 ? 131.733 146.868 143.817 1.00 19.17 ?  192 LEU B CB    1 
ATOM   7131  C  CG    . LEU B 1 192 ? 131.083 148.245 143.666 1.00 20.72 ?  192 LEU B CG    1 
ATOM   7132  C  CD1   . LEU B 1 192 ? 129.574 148.137 143.771 1.00 20.16 ?  192 LEU B CD1   1 
ATOM   7133  C  CD2   . LEU B 1 192 ? 131.630 149.216 144.698 1.00 21.42 ?  192 LEU B CD2   1 
ATOM   7134  N  N     . SER B 1 193 ? 133.786 144.431 143.026 1.00 19.80 ?  193 SER B N     1 
ATOM   7135  C  CA    . SER B 1 193 ? 134.500 143.202 143.350 1.00 22.09 ?  193 SER B CA    1 
ATOM   7136  C  C     . SER B 1 193 ? 136.005 143.414 143.307 1.00 27.73 ?  193 SER B C     1 
ATOM   7137  O  O     . SER B 1 193 ? 136.744 142.774 144.062 1.00 36.62 ?  193 SER B O     1 
ATOM   7138  C  CB    . SER B 1 193 ? 134.091 142.087 142.393 1.00 24.90 ?  193 SER B CB    1 
ATOM   7139  O  OG    . SER B 1 193 ? 132.722 141.778 142.549 1.00 35.01 ?  193 SER B OG    1 
ATOM   7140  N  N     . LYS B 1 194 ? 136.470 144.299 142.425 1.00 29.29 ?  194 LYS B N     1 
ATOM   7141  C  CA    . LYS B 1 194 ? 137.867 144.712 142.448 1.00 29.16 ?  194 LYS B CA    1 
ATOM   7142  C  C     . LYS B 1 194 ? 138.211 145.380 143.772 1.00 35.14 ?  194 LYS B C     1 
ATOM   7143  O  O     . LYS B 1 194 ? 139.293 145.157 144.329 1.00 39.81 ?  194 LYS B O     1 
ATOM   7144  C  CB    . LYS B 1 194 ? 138.140 145.647 141.270 1.00 26.06 ?  194 LYS B CB    1 
ATOM   7145  C  CG    . LYS B 1 194 ? 139.428 146.435 141.360 1.00 33.46 ?  194 LYS B CG    1 
ATOM   7146  C  CD    . LYS B 1 194 ? 139.455 147.528 140.306 1.00 33.37 ?  194 LYS B CD    1 
ATOM   7147  C  CE    . LYS B 1 194 ? 140.821 148.185 140.220 1.00 34.95 ?  194 LYS B CE    1 
ATOM   7148  N  NZ    . LYS B 1 194 ? 140.841 149.287 139.219 1.00 35.12 1  194 LYS B NZ    1 
ATOM   7149  N  N     . LEU B 1 195 ? 137.296 146.198 144.296 1.00 30.45 ?  195 LEU B N     1 
ATOM   7150  C  CA    . LEU B 1 195 ? 137.473 146.812 145.604 1.00 29.84 ?  195 LEU B CA    1 
ATOM   7151  C  C     . LEU B 1 195 ? 137.328 145.817 146.747 1.00 31.64 ?  195 LEU B C     1 
ATOM   7152  O  O     . LEU B 1 195 ? 137.620 146.172 147.895 1.00 35.04 ?  195 LEU B O     1 
ATOM   7153  C  CB    . LEU B 1 195 ? 136.473 147.955 145.780 1.00 31.01 ?  195 LEU B CB    1 
ATOM   7154  C  CG    . LEU B 1 195 ? 136.660 149.135 144.822 1.00 32.60 ?  195 LEU B CG    1 
ATOM   7155  C  CD1   . LEU B 1 195 ? 135.533 150.144 144.973 1.00 32.68 ?  195 LEU B CD1   1 
ATOM   7156  C  CD2   . LEU B 1 195 ? 138.012 149.796 145.045 1.00 30.72 ?  195 LEU B CD2   1 
ATOM   7157  N  N     . GLY B 1 196 ? 136.879 144.592 146.470 1.00 31.68 ?  196 GLY B N     1 
ATOM   7158  C  CA    . GLY B 1 196 ? 136.800 143.547 147.466 1.00 32.64 ?  196 GLY B CA    1 
ATOM   7159  C  C     . GLY B 1 196 ? 135.430 143.333 148.074 1.00 33.71 ?  196 GLY B C     1 
ATOM   7160  O  O     . GLY B 1 196 ? 135.265 142.396 148.866 1.00 35.13 ?  196 GLY B O     1 
ATOM   7161  N  N     . GLY B 1 197 ? 134.447 144.161 147.734 1.00 30.62 ?  197 GLY B N     1 
ATOM   7162  C  CA    . GLY B 1 197 ? 133.145 144.052 148.356 1.00 26.25 ?  197 GLY B CA    1 
ATOM   7163  C  C     . GLY B 1 197 ? 132.219 143.095 147.629 1.00 22.65 ?  197 GLY B C     1 
ATOM   7164  O  O     . GLY B 1 197 ? 132.281 142.925 146.413 1.00 27.65 ?  197 GLY B O     1 
ATOM   7165  N  N     . GLY B 1 198 ? 131.340 142.461 148.403 1.00 19.98 ?  198 GLY B N     1 
ATOM   7166  C  CA    . GLY B 1 198 ? 130.312 141.610 147.829 1.00 16.72 ?  198 GLY B CA    1 
ATOM   7167  C  C     . GLY B 1 198 ? 129.198 142.457 147.244 1.00 17.83 ?  198 GLY B C     1 
ATOM   7168  O  O     . GLY B 1 198 ? 128.702 143.386 147.890 1.00 21.91 ?  198 GLY B O     1 
ATOM   7169  N  N     . VAL B 1 199 ? 128.801 142.137 146.016 1.00 20.11 ?  199 VAL B N     1 
ATOM   7170  C  CA    . VAL B 1 199 ? 127.857 142.943 145.253 1.00 12.78 ?  199 VAL B CA    1 
ATOM   7171  C  C     . VAL B 1 199 ? 126.556 142.171 145.108 1.00 7.15  ?  199 VAL B C     1 
ATOM   7172  O  O     . VAL B 1 199 ? 126.562 141.002 144.707 1.00 15.02 ?  199 VAL B O     1 
ATOM   7173  C  CB    . VAL B 1 199 ? 128.425 143.319 143.874 1.00 13.70 ?  199 VAL B CB    1 
ATOM   7174  C  CG1   . VAL B 1 199 ? 127.491 144.274 143.158 1.00 16.53 ?  199 VAL B CG1   1 
ATOM   7175  C  CG2   . VAL B 1 199 ? 129.810 143.916 144.018 1.00 11.69 ?  199 VAL B CG2   1 
ATOM   7176  N  N     . SER B 1 200 ? 125.444 142.824 145.432 1.00 13.20 ?  200 SER B N     1 
ATOM   7177  C  CA    . SER B 1 200 ? 124.112 142.274 145.241 1.00 3.98  ?  200 SER B CA    1 
ATOM   7178  C  C     . SER B 1 200 ? 123.364 143.126 144.226 1.00 13.16 ?  200 SER B C     1 
ATOM   7179  O  O     . SER B 1 200 ? 123.408 144.357 144.284 1.00 23.38 ?  200 SER B O     1 
ATOM   7180  C  CB    . SER B 1 200 ? 123.338 142.223 146.560 1.00 10.36 ?  200 SER B CB    1 
ATOM   7181  O  OG    . SER B 1 200 ? 122.222 141.359 146.463 1.00 15.93 ?  200 SER B OG    1 
ATOM   7182  N  N     . LEU B 1 201 ? 122.685 142.468 143.291 1.00 15.98 ?  201 LEU B N     1 
ATOM   7183  C  CA    . LEU B 1 201 ? 121.979 143.147 142.215 1.00 8.21  ?  201 LEU B CA    1 
ATOM   7184  C  C     . LEU B 1 201 ? 120.524 142.710 142.197 1.00 7.83  ?  201 LEU B C     1 
ATOM   7185  O  O     . LEU B 1 201 ? 120.230 141.510 142.217 1.00 14.96 ?  201 LEU B O     1 
ATOM   7186  C  CB    . LEU B 1 201 ? 122.632 142.859 140.862 1.00 14.50 ?  201 LEU B CB    1 
ATOM   7187  C  CG    . LEU B 1 201 ? 124.110 143.231 140.750 1.00 19.27 ?  201 LEU B CG    1 
ATOM   7188  C  CD1   . LEU B 1 201 ? 124.979 141.984 140.776 1.00 16.44 ?  201 LEU B CD1   1 
ATOM   7189  C  CD2   . LEU B 1 201 ? 124.361 144.044 139.492 1.00 17.08 ?  201 LEU B CD2   1 
ATOM   7190  N  N     . ASN B 1 202 ? 119.621 143.684 142.148 1.00 13.30 ?  202 ASN B N     1 
ATOM   7191  C  CA    . ASN B 1 202 ? 118.191 143.427 142.031 1.00 4.34  ?  202 ASN B CA    1 
ATOM   7192  C  C     . ASN B 1 202 ? 117.848 143.304 140.551 1.00 19.44 ?  202 ASN B C     1 
ATOM   7193  O  O     . ASN B 1 202 ? 117.940 144.280 139.801 1.00 25.78 ?  202 ASN B O     1 
ATOM   7194  C  CB    . ASN B 1 202 ? 117.386 144.542 142.691 1.00 8.57  ?  202 ASN B CB    1 
ATOM   7195  C  CG    . ASN B 1 202 ? 115.949 144.146 142.954 1.00 9.79  ?  202 ASN B CG    1 
ATOM   7196  O  OD1   . ASN B 1 202 ? 115.626 142.963 143.043 1.00 17.92 ?  202 ASN B OD1   1 
ATOM   7197  N  ND2   . ASN B 1 202 ? 115.076 145.137 143.080 1.00 12.16 ?  202 ASN B ND2   1 
ATOM   7198  N  N     . LEU B 1 203 ? 117.454 142.104 140.132 1.00 12.94 ?  203 LEU B N     1 
ATOM   7199  C  CA    . LEU B 1 203 ? 117.112 141.837 138.744 1.00 9.62  ?  203 LEU B CA    1 
ATOM   7200  C  C     . LEU B 1 203 ? 115.610 141.837 138.501 1.00 12.21 ?  203 LEU B C     1 
ATOM   7201  O  O     . LEU B 1 203 ? 115.166 141.415 137.428 1.00 17.15 ?  203 LEU B O     1 
ATOM   7202  C  CB    . LEU B 1 203 ? 117.715 140.501 138.303 1.00 15.46 ?  203 LEU B CB    1 
ATOM   7203  C  CG    . LEU B 1 203 ? 119.223 140.338 138.506 1.00 15.40 ?  203 LEU B CG    1 
ATOM   7204  C  CD1   . LEU B 1 203 ? 119.720 139.083 137.813 1.00 14.42 ?  203 LEU B CD1   1 
ATOM   7205  C  CD2   . LEU B 1 203 ? 119.976 141.559 138.007 1.00 15.77 ?  203 LEU B CD2   1 
ATOM   7206  N  N     . SER B 1 204 ? 114.818 142.304 139.469 1.00 15.54 ?  204 SER B N     1 
ATOM   7207  C  CA    . SER B 1 204 ? 113.367 142.253 139.349 1.00 10.71 ?  204 SER B CA    1 
ATOM   7208  C  C     . SER B 1 204 ? 112.818 143.258 138.345 1.00 20.34 ?  204 SER B C     1 
ATOM   7209  O  O     . SER B 1 204 ? 111.720 143.048 137.821 1.00 23.52 ?  204 SER B O     1 
ATOM   7210  C  CB    . SER B 1 204 ? 112.721 142.491 140.714 1.00 8.35  ?  204 SER B CB    1 
ATOM   7211  O  OG    . SER B 1 204 ? 113.198 141.561 141.668 1.00 20.64 ?  204 SER B OG    1 
ATOM   7212  N  N     . LYS B 1 205 ? 113.548 144.338 138.070 1.00 22.11 ?  205 LYS B N     1 
ATOM   7213  C  CA    . LYS B 1 205 ? 113.100 145.304 137.077 1.00 16.32 ?  205 LYS B CA    1 
ATOM   7214  C  C     . LYS B 1 205 ? 113.364 144.843 135.652 1.00 15.37 ?  205 LYS B C     1 
ATOM   7215  O  O     . LYS B 1 205 ? 112.663 145.284 134.736 1.00 26.69 ?  205 LYS B O     1 
ATOM   7216  C  CB    . LYS B 1 205 ? 113.771 146.657 137.315 1.00 18.23 ?  205 LYS B CB    1 
ATOM   7217  C  CG    . LYS B 1 205 ? 113.269 147.373 138.552 1.00 15.88 ?  205 LYS B CG    1 
ATOM   7218  C  CD    . LYS B 1 205 ? 113.912 148.735 138.703 1.00 21.18 ?  205 LYS B CD    1 
ATOM   7219  C  CE    . LYS B 1 205 ? 113.200 149.559 139.760 1.00 24.74 ?  205 LYS B CE    1 
ATOM   7220  N  NZ    . LYS B 1 205 ? 113.237 148.903 141.095 1.00 17.90 1  205 LYS B NZ    1 
ATOM   7221  N  N     . LEU B 1 206 ? 114.351 143.975 135.447 1.00 19.58 ?  206 LEU B N     1 
ATOM   7222  C  CA    . LEU B 1 206 ? 114.628 143.449 134.118 1.00 19.72 ?  206 LEU B CA    1 
ATOM   7223  C  C     . LEU B 1 206 ? 113.442 142.642 133.613 1.00 20.06 ?  206 LEU B C     1 
ATOM   7224  O  O     . LEU B 1 206 ? 112.882 141.816 134.340 1.00 24.64 ?  206 LEU B O     1 
ATOM   7225  C  CB    . LEU B 1 206 ? 115.882 142.580 134.146 1.00 19.51 ?  206 LEU B CB    1 
ATOM   7226  C  CG    . LEU B 1 206 ? 117.145 143.237 134.699 1.00 18.70 ?  206 LEU B CG    1 
ATOM   7227  C  CD1   . LEU B 1 206 ? 118.261 142.218 134.799 1.00 19.93 ?  206 LEU B CD1   1 
ATOM   7228  C  CD2   . LEU B 1 206 ? 117.557 144.402 133.825 1.00 22.12 ?  206 LEU B CD2   1 
ATOM   7229  N  N     . ARG B 1 207 ? 113.059 142.880 132.363 1.00 26.04 ?  207 ARG B N     1 
ATOM   7230  C  CA    . ARG B 1 207 ? 111.923 142.170 131.797 1.00 23.84 ?  207 ARG B CA    1 
ATOM   7231  C  C     . ARG B 1 207 ? 112.265 140.703 131.569 1.00 25.07 ?  207 ARG B C     1 
ATOM   7232  O  O     . ARG B 1 207 ? 113.418 140.336 131.327 1.00 30.59 ?  207 ARG B O     1 
ATOM   7233  C  CB    . ARG B 1 207 ? 111.471 142.826 130.493 1.00 22.30 ?  207 ARG B CB    1 
ATOM   7234  C  CG    . ARG B 1 207 ? 112.527 142.938 129.416 1.00 26.52 ?  207 ARG B CG    1 
ATOM   7235  C  CD    . ARG B 1 207 ? 112.023 143.809 128.277 1.00 24.61 ?  207 ARG B CD    1 
ATOM   7236  N  NE    . ARG B 1 207 ? 112.207 145.229 128.547 1.00 25.92 ?  207 ARG B NE    1 
ATOM   7237  C  CZ    . ARG B 1 207 ? 112.286 146.165 127.612 1.00 23.22 ?  207 ARG B CZ    1 
ATOM   7238  N  NH1   . ARG B 1 207 ? 112.181 145.870 126.327 1.00 26.34 1  207 ARG B NH1   1 
ATOM   7239  N  NH2   . ARG B 1 207 ? 112.474 147.430 127.976 1.00 20.80 ?  207 ARG B NH2   1 
ATOM   7240  N  N     . ALA B 1 208 ? 111.241 139.860 131.655 1.00 29.42 ?  208 ALA B N     1 
ATOM   7241  C  CA    . ALA B 1 208 ? 111.432 138.420 131.632 1.00 21.81 ?  208 ALA B CA    1 
ATOM   7242  C  C     . ALA B 1 208 ? 111.779 137.935 130.226 1.00 28.96 ?  208 ALA B C     1 
ATOM   7243  O  O     . ALA B 1 208 ? 111.825 138.700 129.260 1.00 34.82 ?  208 ALA B O     1 
ATOM   7244  C  CB    . ALA B 1 208 ? 110.182 137.711 132.145 1.00 23.95 ?  208 ALA B CB    1 
ATOM   7245  N  N     . LYS B 1 209 ? 112.036 136.634 130.129 1.00 28.19 ?  209 LYS B N     1 
ATOM   7246  C  CA    . LYS B 1 209 ? 112.319 136.016 128.843 1.00 24.45 ?  209 LYS B CA    1 
ATOM   7247  C  C     . LYS B 1 209 ? 111.078 136.041 127.959 1.00 31.93 ?  209 LYS B C     1 
ATOM   7248  O  O     . LYS B 1 209 ? 109.957 135.829 128.428 1.00 34.54 ?  209 LYS B O     1 
ATOM   7249  C  CB    . LYS B 1 209 ? 112.800 134.579 129.039 1.00 27.07 ?  209 LYS B CB    1 
ATOM   7250  C  CG    . LYS B 1 209 ? 113.465 133.975 127.815 1.00 32.28 ?  209 LYS B CG    1 
ATOM   7251  C  CD    . LYS B 1 209 ? 114.306 132.765 128.186 1.00 29.21 ?  209 LYS B CD    1 
ATOM   7252  C  CE    . LYS B 1 209 ? 113.437 131.567 128.528 1.00 32.67 ?  209 LYS B CE    1 
ATOM   7253  N  NZ    . LYS B 1 209 ? 112.204 131.516 127.695 1.00 33.89 1  209 LYS B NZ    1 
ATOM   7254  N  N     . GLY B 1 210 ? 111.287 136.300 126.672 1.00 35.25 ?  210 GLY B N     1 
ATOM   7255  C  CA    . GLY B 1 210 ? 110.180 136.373 125.743 1.00 34.69 ?  210 GLY B CA    1 
ATOM   7256  C  C     . GLY B 1 210 ? 109.455 137.698 125.720 1.00 35.24 ?  210 GLY B C     1 
ATOM   7257  O  O     . GLY B 1 210 ? 108.275 137.743 125.356 1.00 38.95 ?  210 GLY B O     1 
ATOM   7258  N  N     . GLU B 1 211 ? 110.121 138.780 126.103 1.00 33.78 ?  211 GLU B N     1 
ATOM   7259  C  CA    . GLU B 1 211 ? 109.546 140.113 126.036 1.00 33.10 ?  211 GLU B CA    1 
ATOM   7260  C  C     . GLU B 1 211 ? 110.083 140.858 124.817 1.00 37.21 ?  211 GLU B C     1 
ATOM   7261  O  O     . GLU B 1 211 ? 111.019 140.419 124.147 1.00 40.01 ?  211 GLU B O     1 
ATOM   7262  C  CB    . GLU B 1 211 ? 109.833 140.894 127.322 1.00 31.64 ?  211 GLU B CB    1 
ATOM   7263  C  CG    . GLU B 1 211 ? 109.171 140.303 128.551 1.00 33.93 ?  211 GLU B CG    1 
ATOM   7264  C  CD    . GLU B 1 211 ? 108.264 141.288 129.258 1.00 36.00 ?  211 GLU B CD    1 
ATOM   7265  O  OE1   . GLU B 1 211 ? 107.276 141.736 128.639 1.00 39.65 ?  211 GLU B OE1   1 
ATOM   7266  O  OE2   . GLU B 1 211 ? 108.527 141.605 130.435 1.00 32.33 -1 211 GLU B OE2   1 
ATOM   7267  N  N     . ALA B 1 212 ? 109.473 142.005 124.539 1.00 38.34 ?  212 ALA B N     1 
ATOM   7268  C  CA    . ALA B 1 212 ? 109.752 142.753 123.322 1.00 35.63 ?  212 ALA B CA    1 
ATOM   7269  C  C     . ALA B 1 212 ? 110.785 143.843 123.579 1.00 41.57 ?  212 ALA B C     1 
ATOM   7270  O  O     . ALA B 1 212 ? 110.681 144.589 124.558 1.00 44.34 ?  212 ALA B O     1 
ATOM   7271  C  CB    . ALA B 1 212 ? 108.468 143.368 122.766 1.00 38.46 ?  212 ALA B CB    1 
ATOM   7272  N  N     . ILE B 1 213 ? 111.779 143.925 122.700 1.00 40.74 ?  213 ILE B N     1 
ATOM   7273  C  CA    . ILE B 1 213 ? 112.746 145.016 122.689 1.00 43.49 ?  213 ILE B CA    1 
ATOM   7274  C  C     . ILE B 1 213 ? 112.408 145.891 121.488 1.00 41.50 ?  213 ILE B C     1 
ATOM   7275  O  O     . ILE B 1 213 ? 112.871 145.638 120.374 1.00 44.98 ?  213 ILE B O     1 
ATOM   7276  C  CB    . ILE B 1 213 ? 114.186 144.502 122.626 1.00 41.22 ?  213 ILE B CB    1 
ATOM   7277  C  CG1   . ILE B 1 213 ? 114.431 143.458 123.712 1.00 41.47 ?  213 ILE B CG1   1 
ATOM   7278  C  CG2   . ILE B 1 213 ? 115.169 145.655 122.761 1.00 38.15 ?  213 ILE B CG2   1 
ATOM   7279  C  CD1   . ILE B 1 213 ? 115.554 142.503 123.393 1.00 41.34 ?  213 ILE B CD1   1 
ATOM   7280  N  N     . LYS B 1 214 ? 111.607 146.929 121.718 1.00 46.02 ?  214 LYS B N     1 
ATOM   7281  C  CA    . LYS B 1 214 ? 111.143 147.837 120.668 1.00 46.63 ?  214 LYS B CA    1 
ATOM   7282  C  C     . LYS B 1 214 ? 110.369 147.087 119.582 1.00 52.94 ?  214 LYS B C     1 
ATOM   7283  O  O     . LYS B 1 214 ? 110.792 146.984 118.428 1.00 55.44 ?  214 LYS B O     1 
ATOM   7284  C  CB    . LYS B 1 214 ? 112.305 148.631 120.066 1.00 48.06 ?  214 LYS B CB    1 
ATOM   7285  C  CG    . LYS B 1 214 ? 112.417 150.051 120.597 1.00 49.74 ?  214 LYS B CG    1 
ATOM   7286  C  CD    . LYS B 1 214 ? 113.849 150.554 120.567 1.00 49.95 ?  214 LYS B CD    1 
ATOM   7287  C  CE    . LYS B 1 214 ? 114.595 150.057 119.338 1.00 48.13 ?  214 LYS B CE    1 
ATOM   7288  N  NZ    . LYS B 1 214 ? 116.069 150.055 119.544 1.00 51.60 1  214 LYS B NZ    1 
ATOM   7289  N  N     . ASP B 1 215 ? 109.232 146.525 119.999 1.00 54.72 ?  215 ASP B N     1 
ATOM   7290  C  CA    . ASP B 1 215 ? 108.179 146.044 119.106 1.00 56.27 ?  215 ASP B CA    1 
ATOM   7291  C  C     . ASP B 1 215 ? 108.513 144.732 118.401 1.00 55.86 ?  215 ASP B C     1 
ATOM   7292  O  O     . ASP B 1 215 ? 107.675 144.202 117.665 1.00 57.90 ?  215 ASP B O     1 
ATOM   7293  C  CB    . ASP B 1 215 ? 107.830 147.116 118.068 1.00 56.75 ?  215 ASP B CB    1 
ATOM   7294  C  CG    . ASP B 1 215 ? 106.883 148.167 118.612 1.00 58.77 ?  215 ASP B CG    1 
ATOM   7295  O  OD1   . ASP B 1 215 ? 105.700 147.840 118.842 1.00 57.83 ?  215 ASP B OD1   1 
ATOM   7296  O  OD2   . ASP B 1 215 ? 107.322 149.319 118.811 1.00 57.94 -1 215 ASP B OD2   1 
ATOM   7297  N  N     . VAL B 1 216 ? 109.712 144.193 118.608 1.00 49.80 ?  216 VAL B N     1 
ATOM   7298  C  CA    . VAL B 1 216 ? 110.021 142.845 118.132 1.00 49.24 ?  216 VAL B CA    1 
ATOM   7299  C  C     . VAL B 1 216 ? 109.889 141.919 119.339 1.00 51.37 ?  216 VAL B C     1 
ATOM   7300  O  O     . VAL B 1 216 ? 110.579 142.085 120.347 1.00 54.49 ?  216 VAL B O     1 
ATOM   7301  C  CB    . VAL B 1 216 ? 111.404 142.758 117.477 1.00 49.43 ?  216 VAL B CB    1 
ATOM   7302  C  CG1   . VAL B 1 216 ? 112.263 143.945 117.858 1.00 48.26 ?  216 VAL B CG1   1 
ATOM   7303  C  CG2   . VAL B 1 216 ? 112.099 141.434 117.801 1.00 49.08 ?  216 VAL B CG2   1 
ATOM   7304  N  N     . GLU B 1 217 ? 108.974 140.957 119.250 1.00 49.49 ?  217 GLU B N     1 
ATOM   7305  C  CA    . GLU B 1 217 ? 108.570 140.185 120.414 1.00 48.12 ?  217 GLU B CA    1 
ATOM   7306  C  C     . GLU B 1 217 ? 109.446 138.945 120.580 1.00 47.97 ?  217 GLU B C     1 
ATOM   7307  O  O     . GLU B 1 217 ? 110.163 138.522 119.669 1.00 49.55 ?  217 GLU B O     1 
ATOM   7308  C  CB    . GLU B 1 217 ? 107.100 139.785 120.298 1.00 49.89 ?  217 GLU B CB    1 
ATOM   7309  C  CG    . GLU B 1 217 ? 106.182 140.930 119.902 1.00 50.43 ?  217 GLU B CG    1 
ATOM   7310  C  CD    . GLU B 1 217 ? 105.781 141.790 121.082 1.00 53.17 ?  217 GLU B CD    1 
ATOM   7311  O  OE1   . GLU B 1 217 ? 105.880 141.310 122.231 1.00 52.28 ?  217 GLU B OE1   1 
ATOM   7312  O  OE2   . GLU B 1 217 ? 105.367 142.947 120.863 1.00 49.00 -1 217 GLU B OE2   1 
ATOM   7313  N  N     . ASN B 1 218 ? 109.366 138.358 121.775 1.00 43.64 ?  218 ASN B N     1 
ATOM   7314  C  CA    . ASN B 1 218 ? 110.119 137.157 122.138 1.00 41.92 ?  218 ASN B CA    1 
ATOM   7315  C  C     . ASN B 1 218 ? 111.608 137.345 121.870 1.00 45.22 ?  218 ASN B C     1 
ATOM   7316  O  O     . ASN B 1 218 ? 112.287 136.481 121.311 1.00 46.74 ?  218 ASN B O     1 
ATOM   7317  C  CB    . ASN B 1 218 ? 109.575 135.930 121.408 1.00 43.14 ?  218 ASN B CB    1 
ATOM   7318  C  CG    . ASN B 1 218 ? 108.624 135.120 122.264 1.00 46.85 ?  218 ASN B CG    1 
ATOM   7319  O  OD1   . ASN B 1 218 ? 107.592 135.621 122.710 1.00 45.77 ?  218 ASN B OD1   1 
ATOM   7320  N  ND2   . ASN B 1 218 ? 108.972 133.861 122.505 1.00 48.32 ?  218 ASN B ND2   1 
ATOM   7321  N  N     . ALA B 1 219 ? 112.117 138.499 122.289 1.00 37.53 ?  219 ALA B N     1 
ATOM   7322  C  CA    . ALA B 1 219 ? 113.485 138.908 122.001 1.00 35.07 ?  219 ALA B CA    1 
ATOM   7323  C  C     . ALA B 1 219 ? 114.400 138.881 123.214 1.00 37.31 ?  219 ALA B C     1 
ATOM   7324  O  O     . ALA B 1 219 ? 115.597 138.626 123.068 1.00 35.41 ?  219 ALA B O     1 
ATOM   7325  C  CB    . ALA B 1 219 ? 113.488 140.318 121.403 1.00 36.43 ?  219 ALA B CB    1 
ATOM   7326  N  N     . THR B 1 220 ? 113.871 139.137 124.406 1.00 34.97 ?  220 THR B N     1 
ATOM   7327  C  CA    . THR B 1 220 ? 114.702 139.226 125.596 1.00 31.02 ?  220 THR B CA    1 
ATOM   7328  C  C     . THR B 1 220 ? 115.171 137.848 126.046 1.00 34.50 ?  220 THR B C     1 
ATOM   7329  O  O     . THR B 1 220 ? 114.461 136.848 125.909 1.00 35.03 ?  220 THR B O     1 
ATOM   7330  C  CB    . THR B 1 220 ? 113.942 139.902 126.736 1.00 32.28 ?  220 THR B CB    1 
ATOM   7331  O  OG1   . THR B 1 220 ? 112.842 139.076 127.137 1.00 38.26 ?  220 THR B OG1   1 
ATOM   7332  C  CG2   . THR B 1 220 ? 113.413 141.243 126.285 1.00 32.74 ?  220 THR B CG2   1 
ATOM   7333  N  N     . LYS B 1 221 ? 116.387 137.810 126.586 1.00 32.78 ?  221 LYS B N     1 
ATOM   7334  C  CA    . LYS B 1 221 ? 116.924 136.606 127.201 1.00 29.71 ?  221 LYS B CA    1 
ATOM   7335  C  C     . LYS B 1 221 ? 116.468 136.428 128.641 1.00 31.82 ?  221 LYS B C     1 
ATOM   7336  O  O     . LYS B 1 221 ? 116.756 135.387 129.241 1.00 34.84 ?  221 LYS B O     1 
ATOM   7337  C  CB    . LYS B 1 221 ? 118.455 136.625 127.153 1.00 29.40 ?  221 LYS B CB    1 
ATOM   7338  C  CG    . LYS B 1 221 ? 119.027 136.407 125.770 1.00 30.09 ?  221 LYS B CG    1 
ATOM   7339  C  CD    . LYS B 1 221 ? 120.214 135.462 125.816 1.00 32.86 ?  221 LYS B CD    1 
ATOM   7340  C  CE    . LYS B 1 221 ? 120.657 135.081 124.418 1.00 35.04 ?  221 LYS B CE    1 
ATOM   7341  N  NZ    . LYS B 1 221 ? 119.604 135.378 123.409 1.00 32.52 1  221 LYS B NZ    1 
ATOM   7342  N  N     . GLY B 1 222 ? 115.770 137.408 129.202 1.00 31.02 ?  222 GLY B N     1 
ATOM   7343  C  CA    . GLY B 1 222 ? 115.327 137.325 130.571 1.00 27.64 ?  222 GLY B CA    1 
ATOM   7344  C  C     . GLY B 1 222 ? 116.438 137.635 131.555 1.00 28.06 ?  222 GLY B C     1 
ATOM   7345  O  O     . GLY B 1 222 ? 117.520 138.116 131.204 1.00 31.31 ?  222 GLY B O     1 
ATOM   7346  N  N     . VAL B 1 223 ? 116.150 137.349 132.826 1.00 27.28 ?  223 VAL B N     1 
ATOM   7347  C  CA    . VAL B 1 223 ? 117.130 137.598 133.874 1.00 25.17 ?  223 VAL B CA    1 
ATOM   7348  C  C     . VAL B 1 223 ? 118.243 136.563 133.864 1.00 20.16 ?  223 VAL B C     1 
ATOM   7349  O  O     . VAL B 1 223 ? 119.280 136.779 134.495 1.00 26.46 ?  223 VAL B O     1 
ATOM   7350  C  CB    . VAL B 1 223 ? 116.451 137.649 135.256 1.00 21.99 ?  223 VAL B CB    1 
ATOM   7351  C  CG1   . VAL B 1 223 ? 115.196 138.502 135.200 1.00 22.24 ?  223 VAL B CG1   1 
ATOM   7352  C  CG2   . VAL B 1 223 ? 116.134 136.246 135.753 1.00 22.98 ?  223 VAL B CG2   1 
ATOM   7353  N  N     . VAL B 1 224 ? 118.062 135.440 133.169 1.00 24.17 ?  224 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 224 ? 119.096 134.410 133.143 1.00 22.49 ?  224 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 224 ? 120.306 134.852 132.323 1.00 26.27 ?  224 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 224 ? 121.449 134.557 132.690 1.00 30.84 ?  224 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 224 ? 118.509 133.086 132.624 1.00 27.68 ?  224 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 224 ? 119.604 132.052 132.422 1.00 27.23 ?  224 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 224 ? 117.464 132.568 133.594 1.00 26.03 ?  224 VAL B CG2   1 
ATOM   7360  N  N     . GLY B 1 225 ? 120.093 135.558 131.211 1.00 22.82 ?  225 GLY B N     1 
ATOM   7361  C  CA    . GLY B 1 225 ? 121.222 136.077 130.453 1.00 18.39 ?  225 GLY B CA    1 
ATOM   7362  C  C     . GLY B 1 225 ? 122.021 137.103 131.234 1.00 21.88 ?  225 GLY B C     1 
ATOM   7363  O  O     . GLY B 1 225 ? 123.256 137.073 131.241 1.00 34.08 ?  225 GLY B O     1 
ATOM   7364  N  N     . VAL B 1 226 ? 121.327 138.022 131.908 1.00 19.13 ?  226 VAL B N     1 
ATOM   7365  C  CA    . VAL B 1 226 ? 122.002 138.982 132.773 1.00 19.93 ?  226 VAL B CA    1 
ATOM   7366  C  C     . VAL B 1 226 ? 122.701 138.263 133.915 1.00 19.06 ?  226 VAL B C     1 
ATOM   7367  O  O     . VAL B 1 226 ? 123.775 138.681 134.359 1.00 23.03 ?  226 VAL B O     1 
ATOM   7368  C  CB    . VAL B 1 226 ? 121.002 140.030 133.294 1.00 17.08 ?  226 VAL B CB    1 
ATOM   7369  C  CG1   . VAL B 1 226 ? 121.739 141.215 133.899 1.00 22.26 ?  226 VAL B CG1   1 
ATOM   7370  C  CG2   . VAL B 1 226 ? 120.083 140.477 132.177 1.00 16.72 ?  226 VAL B CG2   1 
ATOM   7371  N  N     . MET B 1 227 ? 122.105 137.177 134.409 1.00 22.71 ?  227 MET B N     1 
ATOM   7372  C  CA    . MET B 1 227 ? 122.739 136.379 135.450 1.00 21.23 ?  227 MET B CA    1 
ATOM   7373  C  C     . MET B 1 227 ? 124.046 135.776 134.963 1.00 21.57 ?  227 MET B C     1 
ATOM   7374  O  O     . MET B 1 227 ? 125.041 135.767 135.690 1.00 27.55 ?  227 MET B O     1 
ATOM   7375  C  CB    . MET B 1 227 ? 121.786 135.278 135.907 1.00 20.01 ?  227 MET B CB    1 
ATOM   7376  C  CG    . MET B 1 227 ? 120.858 135.680 137.025 1.00 16.03 ?  227 MET B CG    1 
ATOM   7377  S  SD    . MET B 1 227 ? 119.907 134.270 137.599 1.00 40.04 ?  227 MET B SD    1 
ATOM   7378  C  CE    . MET B 1 227 ? 120.731 133.963 139.149 1.00 24.27 ?  227 MET B CE    1 
ATOM   7379  N  N     . LYS B 1 228 ? 124.057 135.253 133.736 1.00 22.19 ?  228 LYS B N     1 
ATOM   7380  C  CA    . LYS B 1 228 ? 125.288 134.702 133.175 1.00 22.43 ?  228 LYS B CA    1 
ATOM   7381  C  C     . LYS B 1 228 ? 126.341 135.787 132.989 1.00 22.93 ?  228 LYS B C     1 
ATOM   7382  O  O     . LYS B 1 228 ? 127.527 135.573 133.275 1.00 23.93 ?  228 LYS B O     1 
ATOM   7383  C  CB    . LYS B 1 228 ? 124.993 134.009 131.847 1.00 24.69 ?  228 LYS B CB    1 
ATOM   7384  C  CG    . LYS B 1 228 ? 124.774 132.514 131.962 1.00 29.35 ?  228 LYS B CG    1 
ATOM   7385  C  CD    . LYS B 1 228 ? 123.372 132.141 131.518 1.00 29.88 ?  228 LYS B CD    1 
ATOM   7386  C  CE    . LYS B 1 228 ? 123.128 132.554 130.077 1.00 33.12 ?  228 LYS B CE    1 
ATOM   7387  N  NZ    . LYS B 1 228 ? 121.927 131.889 129.502 1.00 34.24 1  228 LYS B NZ    1 
ATOM   7388  N  N     . LEU B 1 229 ? 125.921 136.962 132.511 1.00 22.47 ?  229 LEU B N     1 
ATOM   7389  C  CA    . LEU B 1 229 ? 126.854 138.075 132.358 1.00 20.86 ?  229 LEU B CA    1 
ATOM   7390  C  C     . LEU B 1 229 ? 127.458 138.469 133.699 1.00 19.28 ?  229 LEU B C     1 
ATOM   7391  O  O     . LEU B 1 229 ? 128.672 138.673 133.812 1.00 25.07 ?  229 LEU B O     1 
ATOM   7392  C  CB    . LEU B 1 229 ? 126.146 139.272 131.726 1.00 23.23 ?  229 LEU B CB    1 
ATOM   7393  C  CG    . LEU B 1 229 ? 125.596 139.123 130.314 1.00 19.52 ?  229 LEU B CG    1 
ATOM   7394  C  CD1   . LEU B 1 229 ? 124.435 140.079 130.128 1.00 20.88 ?  229 LEU B CD1   1 
ATOM   7395  C  CD2   . LEU B 1 229 ? 126.686 139.387 129.293 1.00 17.63 ?  229 LEU B CD2   1 
ATOM   7396  N  N     . LEU B 1 230 ? 126.620 138.576 134.731 1.00 21.75 ?  230 LEU B N     1 
ATOM   7397  C  CA    . LEU B 1 230 ? 127.104 138.940 136.057 1.00 17.81 ?  230 LEU B CA    1 
ATOM   7398  C  C     . LEU B 1 230 ? 128.001 137.855 136.634 1.00 17.83 ?  230 LEU B C     1 
ATOM   7399  O  O     . LEU B 1 230 ? 128.986 138.156 137.313 1.00 28.53 ?  230 LEU B O     1 
ATOM   7400  C  CB    . LEU B 1 230 ? 125.924 139.213 136.988 1.00 19.03 ?  230 LEU B CB    1 
ATOM   7401  C  CG    . LEU B 1 230 ? 125.127 140.487 136.714 1.00 23.50 ?  230 LEU B CG    1 
ATOM   7402  C  CD1   . LEU B 1 230 ? 123.825 140.476 137.497 1.00 24.96 ?  230 LEU B CD1   1 
ATOM   7403  C  CD2   . LEU B 1 230 ? 125.951 141.716 137.054 1.00 20.05 ?  230 LEU B CD2   1 
ATOM   7404  N  N     . ASP B 1 231 ? 127.671 136.588 136.385 1.00 21.74 ?  231 ASP B N     1 
ATOM   7405  C  CA    . ASP B 1 231 ? 128.507 135.494 136.859 1.00 24.81 ?  231 ASP B CA    1 
ATOM   7406  C  C     . ASP B 1 231 ? 129.893 135.555 136.235 1.00 26.22 ?  231 ASP B C     1 
ATOM   7407  O  O     . ASP B 1 231 ? 130.903 135.393 136.931 1.00 32.42 ?  231 ASP B O     1 
ATOM   7408  C  CB    . ASP B 1 231 ? 127.834 134.157 136.550 1.00 26.44 ?  231 ASP B CB    1 
ATOM   7409  C  CG    . ASP B 1 231 ? 128.656 132.972 137.002 1.00 35.82 ?  231 ASP B CG    1 
ATOM   7410  O  OD1   . ASP B 1 231 ? 129.096 132.967 138.169 1.00 38.60 ?  231 ASP B OD1   1 
ATOM   7411  O  OD2   . ASP B 1 231 ? 128.864 132.046 136.191 1.00 35.57 -1 231 ASP B OD2   1 
ATOM   7412  N  N     . ASN B 1 232 ? 129.963 135.808 134.927 1.00 29.25 ?  232 ASN B N     1 
ATOM   7413  C  CA    . ASN B 1 232 ? 131.265 135.952 134.283 1.00 26.54 ?  232 ASN B CA    1 
ATOM   7414  C  C     . ASN B 1 232 ? 131.999 137.191 134.778 1.00 23.51 ?  232 ASN B C     1 
ATOM   7415  O  O     . ASN B 1 232 ? 133.227 137.173 134.926 1.00 31.02 ?  232 ASN B O     1 
ATOM   7416  C  CB    . ASN B 1 232 ? 131.105 135.987 132.765 1.00 29.57 ?  232 ASN B CB    1 
ATOM   7417  C  CG    . ASN B 1 232 ? 132.041 135.027 132.065 1.00 31.72 ?  232 ASN B CG    1 
ATOM   7418  O  OD1   . ASN B 1 232 ? 131.600 134.106 131.378 1.00 31.09 ?  232 ASN B OD1   1 
ATOM   7419  N  ND2   . ASN B 1 232 ? 133.339 135.245 132.217 1.00 30.58 ?  232 ASN B ND2   1 
ATOM   7420  N  N     . ALA B 1 233 ? 131.269 138.279 135.034 1.00 22.25 ?  233 ALA B N     1 
ATOM   7421  C  CA    . ALA B 1 233 ? 131.897 139.490 135.552 1.00 19.36 ?  233 ALA B CA    1 
ATOM   7422  C  C     . ALA B 1 233 ? 132.501 139.257 136.931 1.00 30.42 ?  233 ALA B C     1 
ATOM   7423  O  O     . ALA B 1 233 ? 133.611 139.717 137.217 1.00 37.00 ?  233 ALA B O     1 
ATOM   7424  C  CB    . ALA B 1 233 ? 130.877 140.626 135.595 1.00 21.32 ?  233 ALA B CB    1 
ATOM   7425  N  N     . PHE B 1 234 ? 131.780 138.546 137.800 1.00 26.24 ?  234 PHE B N     1 
ATOM   7426  C  CA    . PHE B 1 234 ? 132.294 138.252 139.132 1.00 18.46 ?  234 PHE B CA    1 
ATOM   7427  C  C     . PHE B 1 234 ? 133.429 137.240 139.081 1.00 23.57 ?  234 PHE B C     1 
ATOM   7428  O  O     . PHE B 1 234 ? 134.346 137.299 139.908 1.00 30.29 ?  234 PHE B O     1 
ATOM   7429  C  CB    . PHE B 1 234 ? 131.165 137.751 140.033 1.00 25.09 ?  234 PHE B CB    1 
ATOM   7430  C  CG    . PHE B 1 234 ? 130.250 138.841 140.515 1.00 21.29 ?  234 PHE B CG    1 
ATOM   7431  C  CD1   . PHE B 1 234 ? 130.736 139.876 141.287 1.00 22.20 ?  234 PHE B CD1   1 
ATOM   7432  C  CD2   . PHE B 1 234 ? 128.907 138.831 140.191 1.00 20.87 ?  234 PHE B CD2   1 
ATOM   7433  C  CE1   . PHE B 1 234 ? 129.900 140.881 141.727 1.00 20.21 ?  234 PHE B CE1   1 
ATOM   7434  C  CE2   . PHE B 1 234 ? 128.067 139.836 140.627 1.00 20.94 ?  234 PHE B CE2   1 
ATOM   7435  C  CZ    . PHE B 1 234 ? 128.565 140.859 141.396 1.00 20.90 ?  234 PHE B CZ    1 
ATOM   7436  N  N     . ARG B 1 235 ? 133.384 136.301 138.132 1.00 29.56 ?  235 ARG B N     1 
ATOM   7437  C  CA    . ARG B 1 235 ? 134.511 135.397 137.939 1.00 26.83 ?  235 ARG B CA    1 
ATOM   7438  C  C     . ARG B 1 235 ? 135.757 136.158 137.510 1.00 28.32 ?  235 ARG B C     1 
ATOM   7439  O  O     . ARG B 1 235 ? 136.862 135.872 137.985 1.00 36.66 ?  235 ARG B O     1 
ATOM   7440  C  CB    . ARG B 1 235 ? 134.158 134.328 136.905 1.00 24.84 ?  235 ARG B CB    1 
ATOM   7441  C  CG    . ARG B 1 235 ? 133.796 132.985 137.502 1.00 32.99 ?  235 ARG B CG    1 
ATOM   7442  C  CD    . ARG B 1 235 ? 133.537 131.948 136.422 1.00 30.46 ?  235 ARG B CD    1 
ATOM   7443  N  NE    . ARG B 1 235 ? 132.147 131.949 135.982 1.00 34.53 ?  235 ARG B NE    1 
ATOM   7444  C  CZ    . ARG B 1 235 ? 131.762 132.127 134.725 1.00 36.67 ?  235 ARG B CZ    1 
ATOM   7445  N  NH1   . ARG B 1 235 ? 132.639 132.329 133.756 1.00 35.53 1  235 ARG B NH1   1 
ATOM   7446  N  NH2   . ARG B 1 235 ? 130.465 132.099 134.434 1.00 32.65 ?  235 ARG B NH2   1 
ATOM   7447  N  N     . TYR B 1 236 ? 135.597 137.131 136.613 1.00 24.71 ?  236 TYR B N     1 
ATOM   7448  C  CA    . TYR B 1 236 ? 136.746 137.891 136.132 1.00 25.51 ?  236 TYR B CA    1 
ATOM   7449  C  C     . TYR B 1 236 ? 137.311 138.785 137.229 1.00 27.63 ?  236 TYR B C     1 
ATOM   7450  O  O     . TYR B 1 236 ? 138.527 138.823 137.449 1.00 28.35 ?  236 TYR B O     1 
ATOM   7451  C  CB    . TYR B 1 236 ? 136.347 138.720 134.913 1.00 22.47 ?  236 TYR B CB    1 
ATOM   7452  C  CG    . TYR B 1 236 ? 137.497 139.468 134.289 1.00 23.31 ?  236 TYR B CG    1 
ATOM   7453  C  CD1   . TYR B 1 236 ? 138.453 138.798 133.541 1.00 21.64 ?  236 TYR B CD1   1 
ATOM   7454  C  CD2   . TYR B 1 236 ? 137.629 140.840 134.446 1.00 24.88 ?  236 TYR B CD2   1 
ATOM   7455  C  CE1   . TYR B 1 236 ? 139.506 139.469 132.968 1.00 24.32 ?  236 TYR B CE1   1 
ATOM   7456  C  CE2   . TYR B 1 236 ? 138.683 141.522 133.873 1.00 17.73 ?  236 TYR B CE2   1 
ATOM   7457  C  CZ    . TYR B 1 236 ? 139.617 140.829 133.135 1.00 20.63 ?  236 TYR B CZ    1 
ATOM   7458  O  OH    . TYR B 1 236 ? 140.671 141.492 132.558 1.00 30.59 ?  236 TYR B OH    1 
ATOM   7459  N  N     . ALA B 1 237 ? 136.443 139.517 137.925 1.00 29.98 ?  237 ALA B N     1 
ATOM   7460  C  CA    . ALA B 1 237 ? 136.858 140.394 139.019 1.00 29.43 ?  237 ALA B CA    1 
ATOM   7461  C  C     . ALA B 1 237 ? 136.802 139.588 140.309 1.00 36.88 ?  237 ALA B C     1 
ATOM   7462  O  O     . ALA B 1 237 ? 135.789 139.557 141.008 1.00 39.03 ?  237 ALA B O     1 
ATOM   7463  C  CB    . ALA B 1 237 ? 135.974 141.633 139.083 1.00 30.69 ?  237 ALA B CB    1 
ATOM   7464  N  N     . ASP B 1 238 ? 137.914 138.928 140.630 1.00 50.17 ?  238 ASP B N     1 
ATOM   7465  C  CA    . ASP B 1 238 ? 137.968 138.043 141.788 1.00 53.56 ?  238 ASP B CA    1 
ATOM   7466  C  C     . ASP B 1 238 ? 139.042 138.484 142.776 1.00 57.82 ?  238 ASP B C     1 
ATOM   7467  O  O     . ASP B 1 238 ? 139.847 137.662 143.227 1.00 57.80 ?  238 ASP B O     1 
ATOM   7468  C  CB    . ASP B 1 238 ? 138.210 136.597 141.344 1.00 52.95 ?  238 ASP B CB    1 
ATOM   7469  C  CG    . ASP B 1 238 ? 139.461 136.445 140.500 1.00 57.45 ?  238 ASP B CG    1 
ATOM   7470  O  OD1   . ASP B 1 238 ? 139.922 137.455 139.928 1.00 57.54 ?  238 ASP B OD1   1 
ATOM   7471  O  OD2   . ASP B 1 238 ? 139.986 135.316 140.415 1.00 56.42 -1 238 ASP B OD2   1 
ATOM   7472  N  N     . GLN B 1 239 ? 139.067 139.777 143.103 1.00 63.48 ?  239 GLN B N     1 
ATOM   7473  C  CA    . GLN B 1 239 ? 140.009 140.334 144.077 1.00 64.82 ?  239 GLN B CA    1 
ATOM   7474  C  C     . GLN B 1 239 ? 141.450 139.981 143.720 1.00 67.35 ?  239 GLN B C     1 
ATOM   7475  O  O     . GLN B 1 239 ? 142.239 139.548 144.564 1.00 66.69 ?  239 GLN B O     1 
ATOM   7476  C  CB    . GLN B 1 239 ? 139.674 139.872 145.495 1.00 64.62 ?  239 GLN B CB    1 
ATOM   7477  C  CG    . GLN B 1 239 ? 138.637 140.719 146.205 1.00 63.82 ?  239 GLN B CG    1 
ATOM   7478  C  CD    . GLN B 1 239 ? 138.922 140.855 147.689 1.00 66.05 ?  239 GLN B CD    1 
ATOM   7479  O  OE1   . GLN B 1 239 ? 138.037 140.676 148.524 1.00 65.31 ?  239 GLN B OE1   1 
ATOM   7480  N  NE2   . GLN B 1 239 ? 140.167 141.177 148.023 1.00 65.72 ?  239 GLN B NE2   1 
ATOM   7481  N  N     . MET B 1 240 ? 141.789 140.170 142.443 1.00 69.45 ?  240 MET B N     1 
ATOM   7482  C  CA    . MET B 1 240 ? 143.122 139.866 141.922 1.00 68.65 ?  240 MET B CA    1 
ATOM   7483  C  C     . MET B 1 240 ? 143.504 138.406 142.156 1.00 69.19 ?  240 MET B C     1 
ATOM   7484  O  O     . MET B 1 240 ? 144.674 138.087 142.380 1.00 69.12 ?  240 MET B O     1 
ATOM   7485  C  CB    . MET B 1 240 ? 144.179 140.800 142.518 1.00 68.32 ?  240 MET B CB    1 
ATOM   7486  C  CG    . MET B 1 240 ? 144.016 142.264 142.132 1.00 68.69 ?  240 MET B CG    1 
ATOM   7487  S  SD    . MET B 1 240 ? 142.328 142.878 142.296 1.00 73.09 ?  240 MET B SD    1 
ATOM   7488  C  CE    . MET B 1 240 ? 142.554 144.602 141.869 1.00 67.85 ?  240 MET B CE    1 
ATOM   7489  N  N     . GLY B 1 241 ? 142.520 137.511 142.109 1.00 67.80 ?  241 GLY B N     1 
ATOM   7490  C  CA    . GLY B 1 241 ? 142.772 136.092 142.249 1.00 68.08 ?  241 GLY B CA    1 
ATOM   7491  C  C     . GLY B 1 241 ? 142.973 135.600 143.664 1.00 70.85 ?  241 GLY B C     1 
ATOM   7492  O  O     . GLY B 1 241 ? 143.318 134.427 143.847 1.00 70.98 ?  241 GLY B O     1 
ATOM   7493  N  N     . GLN B 1 242 ? 142.769 136.449 144.671 1.00 75.83 ?  242 GLN B N     1 
ATOM   7494  C  CA    . GLN B 1 242 ? 142.945 136.035 146.058 1.00 75.30 ?  242 GLN B CA    1 
ATOM   7495  C  C     . GLN B 1 242 ? 141.677 135.409 146.631 1.00 76.57 ?  242 GLN B C     1 
ATOM   7496  O  O     . GLN B 1 242 ? 141.704 134.269 147.104 1.00 76.27 ?  242 GLN B O     1 
ATOM   7497  C  CB    . GLN B 1 242 ? 143.379 137.229 146.912 1.00 74.11 ?  242 GLN B CB    1 
ATOM   7498  C  CG    . GLN B 1 242 ? 144.794 137.708 146.630 1.00 76.09 ?  242 GLN B CG    1 
ATOM   7499  C  CD    . GLN B 1 242 ? 145.358 138.557 147.751 1.00 77.11 ?  242 GLN B CD    1 
ATOM   7500  O  OE1   . GLN B 1 242 ? 144.778 138.643 148.834 1.00 76.41 ?  242 GLN B OE1   1 
ATOM   7501  N  NE2   . GLN B 1 242 ? 146.498 139.190 147.497 1.00 75.63 ?  242 GLN B NE2   1 
ATOM   7502  N  N     . ARG B 1 243 ? 140.566 136.139 146.595 1.00 64.77 ?  243 ARG B N     1 
ATOM   7503  C  CA    . ARG B 1 243 ? 139.275 135.644 147.050 1.00 64.67 ?  243 ARG B CA    1 
ATOM   7504  C  C     . ARG B 1 243 ? 138.334 135.575 145.857 1.00 63.62 ?  243 ARG B C     1 
ATOM   7505  O  O     . ARG B 1 243 ? 138.241 136.532 145.083 1.00 62.13 ?  243 ARG B O     1 
ATOM   7506  C  CB    . ARG B 1 243 ? 138.691 136.546 148.145 1.00 63.04 ?  243 ARG B CB    1 
ATOM   7507  C  CG    . ARG B 1 243 ? 137.168 136.591 148.182 1.00 63.91 ?  243 ARG B CG    1 
ATOM   7508  C  CD    . ARG B 1 243 ? 136.634 137.908 147.635 1.00 63.15 ?  243 ARG B CD    1 
ATOM   7509  N  NE    . ARG B 1 243 ? 135.265 138.167 148.066 1.00 65.04 ?  243 ARG B NE    1 
ATOM   7510  C  CZ    . ARG B 1 243 ? 134.511 139.158 147.609 1.00 62.89 ?  243 ARG B CZ    1 
ATOM   7511  N  NH1   . ARG B 1 243 ? 134.962 140.007 146.698 1.00 59.40 1  243 ARG B NH1   1 
ATOM   7512  N  NH2   . ARG B 1 243 ? 133.274 139.299 148.075 1.00 60.40 ?  243 ARG B NH2   1 
ATOM   7513  N  N     . GLN B 1 244 ? 137.645 134.444 145.711 1.00 61.88 ?  244 GLN B N     1 
ATOM   7514  C  CA    . GLN B 1 244 ? 136.728 134.267 144.592 1.00 62.67 ?  244 GLN B CA    1 
ATOM   7515  C  C     . GLN B 1 244 ? 135.669 135.361 144.594 1.00 61.97 ?  244 GLN B C     1 
ATOM   7516  O  O     . GLN B 1 244 ? 135.088 135.678 145.636 1.00 61.07 ?  244 GLN B O     1 
ATOM   7517  C  CB    . GLN B 1 244 ? 136.064 132.891 144.667 1.00 59.38 ?  244 GLN B CB    1 
ATOM   7518  C  CG    . GLN B 1 244 ? 137.002 131.729 144.390 1.00 59.03 ?  244 GLN B CG    1 
ATOM   7519  C  CD    . GLN B 1 244 ? 136.262 130.471 143.979 1.00 60.67 ?  244 GLN B CD    1 
ATOM   7520  O  OE1   . GLN B 1 244 ? 135.224 130.133 144.548 1.00 61.69 ?  244 GLN B OE1   1 
ATOM   7521  N  NE2   . GLN B 1 244 ? 136.794 129.768 142.986 1.00 59.63 ?  244 GLN B NE2   1 
ATOM   7522  N  N     . GLY B 1 245 ? 135.431 135.948 143.423 1.00 50.30 ?  245 GLY B N     1 
ATOM   7523  C  CA    . GLY B 1 245 ? 134.425 136.981 143.291 1.00 47.08 ?  245 GLY B CA    1 
ATOM   7524  C  C     . GLY B 1 245 ? 133.043 136.474 143.641 1.00 46.51 ?  245 GLY B C     1 
ATOM   7525  O  O     . GLY B 1 245 ? 132.553 135.517 143.035 1.00 46.35 ?  245 GLY B O     1 
ATOM   7526  N  N     . SER B 1 246 ? 132.404 137.107 144.620 1.00 41.79 ?  246 SER B N     1 
ATOM   7527  C  CA    . SER B 1 246 ? 131.112 136.671 145.131 1.00 37.18 ?  246 SER B CA    1 
ATOM   7528  C  C     . SER B 1 246 ? 130.057 137.705 144.764 1.00 35.91 ?  246 SER B C     1 
ATOM   7529  O  O     . SER B 1 246 ? 130.195 138.886 145.099 1.00 30.02 ?  246 SER B O     1 
ATOM   7530  C  CB    . SER B 1 246 ? 131.162 136.467 146.644 1.00 37.49 ?  246 SER B CB    1 
ATOM   7531  O  OG    . SER B 1 246 ? 131.969 135.353 146.982 1.00 43.74 ?  246 SER B OG    1 
ATOM   7532  N  N     . GLY B 1 247 ? 129.007 137.254 144.080 1.00 25.68 ?  247 GLY B N     1 
ATOM   7533  C  CA    . GLY B 1 247 ? 127.902 138.116 143.740 1.00 8.74  ?  247 GLY B CA    1 
ATOM   7534  C  C     . GLY B 1 247 ? 126.588 137.481 144.147 1.00 13.22 ?  247 GLY B C     1 
ATOM   7535  O  O     . GLY B 1 247 ? 126.487 136.272 144.354 1.00 20.58 ?  247 GLY B O     1 
ATOM   7536  N  N     . ALA B 1 248 ? 125.577 138.330 144.271 1.00 14.03 ?  248 ALA B N     1 
ATOM   7537  C  CA    . ALA B 1 248 ? 124.229 137.897 144.595 1.00 14.28 ?  248 ALA B CA    1 
ATOM   7538  C  C     . ALA B 1 248 ? 123.258 138.509 143.601 1.00 10.37 ?  248 ALA B C     1 
ATOM   7539  O  O     . ALA B 1 248 ? 123.391 139.677 143.230 1.00 17.81 ?  248 ALA B O     1 
ATOM   7540  C  CB    . ALA B 1 248 ? 123.838 138.285 146.024 1.00 9.00  ?  248 ALA B CB    1 
ATOM   7541  N  N     . ALA B 1 249 ? 122.296 137.710 143.158 1.00 12.61 ?  249 ALA B N     1 
ATOM   7542  C  CA    . ALA B 1 249 ? 121.199 138.181 142.326 1.00 12.36 ?  249 ALA B CA    1 
ATOM   7543  C  C     . ALA B 1 249 ? 119.902 137.978 143.088 1.00 8.88  ?  249 ALA B C     1 
ATOM   7544  O  O     . ALA B 1 249 ? 119.665 136.898 143.639 1.00 16.83 ?  249 ALA B O     1 
ATOM   7545  C  CB    . ALA B 1 249 ? 121.155 137.442 140.986 1.00 14.14 ?  249 ALA B CB    1 
ATOM   7546  N  N     . TYR B 1 250 ? 119.073 139.014 143.135 1.00 8.30  ?  250 TYR B N     1 
ATOM   7547  C  CA    . TYR B 1 250 ? 117.789 138.950 143.813 1.00 8.18  ?  250 TYR B CA    1 
ATOM   7548  C  C     . TYR B 1 250 ? 116.681 139.141 142.792 1.00 7.77  ?  250 TYR B C     1 
ATOM   7549  O  O     . TYR B 1 250 ? 116.749 140.049 141.956 1.00 13.56 ?  250 TYR B O     1 
ATOM   7550  C  CB    . TYR B 1 250 ? 117.691 140.004 144.914 1.00 7.54  ?  250 TYR B CB    1 
ATOM   7551  C  CG    . TYR B 1 250 ? 118.277 139.558 146.230 1.00 15.50 ?  250 TYR B CG    1 
ATOM   7552  C  CD1   . TYR B 1 250 ? 119.651 139.507 146.415 1.00 3.04  ?  250 TYR B CD1   1 
ATOM   7553  C  CD2   . TYR B 1 250 ? 117.461 139.186 147.288 1.00 12.49 ?  250 TYR B CD2   1 
ATOM   7554  C  CE1   . TYR B 1 250 ? 120.195 139.101 147.611 1.00 0.74  ?  250 TYR B CE1   1 
ATOM   7555  C  CE2   . TYR B 1 250 ? 117.997 138.776 148.492 1.00 7.28  ?  250 TYR B CE2   1 
ATOM   7556  C  CZ    . TYR B 1 250 ? 119.365 138.737 148.648 1.00 8.49  ?  250 TYR B CZ    1 
ATOM   7557  O  OH    . TYR B 1 250 ? 119.907 138.330 149.845 1.00 12.85 ?  250 TYR B OH    1 
ATOM   7558  N  N     . LEU B 1 251 ? 115.672 138.282 142.855 1.00 12.99 ?  251 LEU B N     1 
ATOM   7559  C  CA    . LEU B 1 251 ? 114.525 138.359 141.967 1.00 14.29 ?  251 LEU B CA    1 
ATOM   7560  C  C     . LEU B 1 251 ? 113.250 138.236 142.781 1.00 12.54 ?  251 LEU B C     1 
ATOM   7561  O  O     . LEU B 1 251 ? 113.169 137.420 143.704 1.00 15.58 ?  251 LEU B O     1 
ATOM   7562  C  CB    . LEU B 1 251 ? 114.571 137.263 140.899 1.00 15.25 ?  251 LEU B CB    1 
ATOM   7563  C  CG    . LEU B 1 251 ? 113.682 137.508 139.681 1.00 11.75 ?  251 LEU B CG    1 
ATOM   7564  C  CD1   . LEU B 1 251 ? 114.217 138.672 138.872 1.00 12.25 ?  251 LEU B CD1   1 
ATOM   7565  C  CD2   . LEU B 1 251 ? 113.580 136.261 138.828 1.00 7.68  ?  251 LEU B CD2   1 
ATOM   7566  N  N     . ASN B 1 252 ? 112.259 139.052 142.441 1.00 11.64 ?  252 ASN B N     1 
ATOM   7567  C  CA    . ASN B 1 252 ? 110.953 138.928 143.067 1.00 10.65 ?  252 ASN B CA    1 
ATOM   7568  C  C     . ASN B 1 252 ? 110.301 137.616 142.653 1.00 15.17 ?  252 ASN B C     1 
ATOM   7569  O  O     . ASN B 1 252 ? 110.450 137.161 141.515 1.00 23.08 ?  252 ASN B O     1 
ATOM   7570  C  CB    . ASN B 1 252 ? 110.061 140.108 142.688 1.00 12.48 ?  252 ASN B CB    1 
ATOM   7571  C  CG    . ASN B 1 252 ? 109.005 140.395 143.733 1.00 20.70 ?  252 ASN B CG    1 
ATOM   7572  O  OD1   . ASN B 1 252 ? 108.044 139.643 143.883 1.00 30.12 ?  252 ASN B OD1   1 
ATOM   7573  N  ND2   . ASN B 1 252 ? 109.182 141.485 144.469 1.00 20.44 ?  252 ASN B ND2   1 
ATOM   7574  N  N     . ILE B 1 253 ? 109.578 137.000 143.590 1.00 13.68 ?  253 ILE B N     1 
ATOM   7575  C  CA    . ILE B 1 253 ? 108.945 135.718 143.315 1.00 17.48 ?  253 ILE B CA    1 
ATOM   7576  C  C     . ILE B 1 253 ? 107.813 135.847 142.304 1.00 20.96 ?  253 ILE B C     1 
ATOM   7577  O  O     . ILE B 1 253 ? 107.378 134.839 141.734 1.00 23.60 ?  253 ILE B O     1 
ATOM   7578  C  CB    . ILE B 1 253 ? 108.449 135.076 144.625 1.00 16.66 ?  253 ILE B CB    1 
ATOM   7579  C  CG1   . ILE B 1 253 ? 108.340 133.558 144.469 1.00 16.22 ?  253 ILE B CG1   1 
ATOM   7580  C  CG2   . ILE B 1 253 ? 107.121 135.680 145.054 1.00 13.72 ?  253 ILE B CG2   1 
ATOM   7581  C  CD1   . ILE B 1 253 ? 108.561 132.798 145.748 1.00 16.69 ?  253 ILE B CD1   1 
ATOM   7582  N  N     . PHE B 1 254 ? 107.326 137.060 142.057 1.00 19.04 ?  254 PHE B N     1 
ATOM   7583  C  CA    . PHE B 1 254 ? 106.283 137.290 141.069 1.00 16.79 ?  254 PHE B CA    1 
ATOM   7584  C  C     . PHE B 1 254 ? 106.842 137.584 139.683 1.00 18.10 ?  254 PHE B C     1 
ATOM   7585  O  O     . PHE B 1 254 ? 106.065 137.782 138.745 1.00 25.04 ?  254 PHE B O     1 
ATOM   7586  C  CB    . PHE B 1 254 ? 105.374 138.434 141.524 1.00 23.09 ?  254 PHE B CB    1 
ATOM   7587  C  CG    . PHE B 1 254 ? 104.375 138.027 142.565 1.00 22.28 ?  254 PHE B CG    1 
ATOM   7588  C  CD1   . PHE B 1 254 ? 103.334 137.174 142.247 1.00 22.04 ?  254 PHE B CD1   1 
ATOM   7589  C  CD2   . PHE B 1 254 ? 104.488 138.479 143.868 1.00 26.07 ?  254 PHE B CD2   1 
ATOM   7590  C  CE1   . PHE B 1 254 ? 102.416 136.790 143.205 1.00 24.80 ?  254 PHE B CE1   1 
ATOM   7591  C  CE2   . PHE B 1 254 ? 103.575 138.098 144.830 1.00 27.48 ?  254 PHE B CE2   1 
ATOM   7592  C  CZ    . PHE B 1 254 ? 102.537 137.254 144.497 1.00 21.77 ?  254 PHE B CZ    1 
ATOM   7593  N  N     . HIS B 1 255 ? 108.162 137.626 139.540 1.00 25.56 ?  255 HIS B N     1 
ATOM   7594  C  CA    . HIS B 1 255 ? 108.780 137.715 138.225 1.00 14.87 ?  255 HIS B CA    1 
ATOM   7595  C  C     . HIS B 1 255 ? 108.528 136.431 137.447 1.00 18.41 ?  255 HIS B C     1 
ATOM   7596  O  O     . HIS B 1 255 ? 108.530 135.335 138.013 1.00 27.28 ?  255 HIS B O     1 
ATOM   7597  C  CB    . HIS B 1 255 ? 110.281 137.961 138.371 1.00 17.20 ?  255 HIS B CB    1 
ATOM   7598  C  CG    . HIS B 1 255 ? 110.917 138.585 137.171 1.00 19.61 ?  255 HIS B CG    1 
ATOM   7599  N  ND1   . HIS B 1 255 ? 111.122 137.898 135.994 1.00 17.88 ?  255 HIS B ND1   1 
ATOM   7600  C  CD2   . HIS B 1 255 ? 111.415 139.829 136.972 1.00 14.91 ?  255 HIS B CD2   1 
ATOM   7601  C  CE1   . HIS B 1 255 ? 111.708 138.694 135.119 1.00 16.46 ?  255 HIS B CE1   1 
ATOM   7602  N  NE2   . HIS B 1 255 ? 111.899 139.870 135.687 1.00 11.54 ?  255 HIS B NE2   1 
ATOM   7603  N  N     . ARG B 1 256 ? 108.302 136.568 136.138 1.00 21.76 ?  256 ARG B N     1 
ATOM   7604  C  CA    . ARG B 1 256 ? 108.022 135.392 135.320 1.00 22.18 ?  256 ARG B CA    1 
ATOM   7605  C  C     . ARG B 1 256 ? 109.218 134.450 135.261 1.00 23.41 ?  256 ARG B C     1 
ATOM   7606  O  O     . ARG B 1 256 ? 109.044 133.230 135.166 1.00 25.13 ?  256 ARG B O     1 
ATOM   7607  C  CB    . ARG B 1 256 ? 107.610 135.817 133.910 1.00 22.61 ?  256 ARG B CB    1 
ATOM   7608  C  CG    . ARG B 1 256 ? 107.348 134.652 132.970 1.00 23.62 ?  256 ARG B CG    1 
ATOM   7609  C  CD    . ARG B 1 256 ? 108.196 134.745 131.714 1.00 25.89 ?  256 ARG B CD    1 
ATOM   7610  N  NE    . ARG B 1 256 ? 109.462 134.034 131.841 1.00 27.83 ?  256 ARG B NE    1 
ATOM   7611  C  CZ    . ARG B 1 256 ? 109.591 132.716 131.792 1.00 29.95 ?  256 ARG B CZ    1 
ATOM   7612  N  NH1   . ARG B 1 256 ? 108.545 131.923 131.624 1.00 28.67 1  256 ARG B NH1   1 
ATOM   7613  N  NH2   . ARG B 1 256 ? 110.801 132.177 131.918 1.00 27.86 ?  256 ARG B NH2   1 
ATOM   7614  N  N     . ASP B 1 257 ? 110.430 134.990 135.335 1.00 14.82 ?  257 ASP B N     1 
ATOM   7615  C  CA    . ASP B 1 257 ? 111.647 134.195 135.251 1.00 19.17 ?  257 ASP B CA    1 
ATOM   7616  C  C     . ASP B 1 257 ? 111.994 133.491 136.555 1.00 18.74 ?  257 ASP B C     1 
ATOM   7617  O  O     . ASP B 1 257 ? 113.054 132.859 136.627 1.00 24.95 ?  257 ASP B O     1 
ATOM   7618  C  CB    . ASP B 1 257 ? 112.820 135.079 134.828 1.00 23.39 ?  257 ASP B CB    1 
ATOM   7619  C  CG    . ASP B 1 257 ? 112.795 135.412 133.355 1.00 26.85 ?  257 ASP B CG    1 
ATOM   7620  O  OD1   . ASP B 1 257 ? 112.048 134.751 132.604 1.00 27.01 ?  257 ASP B OD1   1 
ATOM   7621  O  OD2   . ASP B 1 257 ? 113.527 136.335 132.948 1.00 31.26 -1 257 ASP B OD2   1 
ATOM   7622  N  N     . ILE B 1 258 ? 111.120 133.560 137.564 1.00 19.61 ?  258 ILE B N     1 
ATOM   7623  C  CA    . ILE B 1 258 ? 111.474 133.086 138.899 1.00 21.87 ?  258 ILE B CA    1 
ATOM   7624  C  C     . ILE B 1 258 ? 111.863 131.614 138.864 1.00 23.00 ?  258 ILE B C     1 
ATOM   7625  O  O     . ILE B 1 258 ? 112.778 131.184 139.574 1.00 32.37 ?  258 ILE B O     1 
ATOM   7626  C  CB    . ILE B 1 258 ? 110.326 133.354 139.892 1.00 23.55 ?  258 ILE B CB    1 
ATOM   7627  C  CG1   . ILE B 1 258 ? 110.756 133.002 141.318 1.00 21.31 ?  258 ILE B CG1   1 
ATOM   7628  C  CG2   . ILE B 1 258 ? 109.067 132.589 139.507 1.00 20.68 ?  258 ILE B CG2   1 
ATOM   7629  C  CD1   . ILE B 1 258 ? 111.926 133.816 141.819 1.00 19.07 ?  258 ILE B CD1   1 
ATOM   7630  N  N     . ASN B 1 259 ? 111.188 130.820 138.032 1.00 26.15 ?  259 ASN B N     1 
ATOM   7631  C  CA    . ASN B 1 259 ? 111.569 129.419 137.896 1.00 24.53 ?  259 ASN B CA    1 
ATOM   7632  C  C     . ASN B 1 259 ? 112.944 129.292 137.254 1.00 23.29 ?  259 ASN B C     1 
ATOM   7633  O  O     . ASN B 1 259 ? 113.832 128.620 137.794 1.00 26.89 ?  259 ASN B O     1 
ATOM   7634  C  CB    . ASN B 1 259 ? 110.515 128.667 137.084 1.00 24.70 ?  259 ASN B CB    1 
ATOM   7635  C  CG    . ASN B 1 259 ? 109.345 128.214 137.932 1.00 24.50 ?  259 ASN B CG    1 
ATOM   7636  O  OD1   . ASN B 1 259 ? 109.480 127.320 138.767 1.00 26.50 ?  259 ASN B OD1   1 
ATOM   7637  N  ND2   . ASN B 1 259 ? 108.190 128.833 137.725 1.00 30.54 ?  259 ASN B ND2   1 
ATOM   7638  N  N     . ASP B 1 260 ? 113.153 129.970 136.121 1.00 27.76 ?  260 ASP B N     1 
ATOM   7639  C  CA    . ASP B 1 260 ? 114.444 129.906 135.446 1.00 24.59 ?  260 ASP B CA    1 
ATOM   7640  C  C     . ASP B 1 260 ? 115.551 130.411 136.360 1.00 19.53 ?  260 ASP B C     1 
ATOM   7641  O  O     . ASP B 1 260 ? 116.622 129.797 136.459 1.00 27.97 ?  260 ASP B O     1 
ATOM   7642  C  CB    . ASP B 1 260 ? 114.400 130.718 134.152 1.00 23.49 ?  260 ASP B CB    1 
ATOM   7643  C  CG    . ASP B 1 260 ? 113.428 130.149 133.139 1.00 32.69 ?  260 ASP B CG    1 
ATOM   7644  O  OD1   . ASP B 1 260 ? 113.230 128.915 133.129 1.00 33.48 ?  260 ASP B OD1   1 
ATOM   7645  O  OD2   . ASP B 1 260 ? 112.861 130.936 132.352 1.00 33.86 -1 260 ASP B OD2   1 
ATOM   7646  N  N     . PHE B 1 261 ? 115.302 131.535 137.036 1.00 26.81 ?  261 PHE B N     1 
ATOM   7647  C  CA    . PHE B 1 261 ? 116.146 132.012 138.122 1.00 22.12 ?  261 PHE B CA    1 
ATOM   7648  C  C     . PHE B 1 261 ? 116.541 130.868 139.050 1.00 16.07 ?  261 PHE B C     1 
ATOM   7649  O  O     . PHE B 1 261 ? 117.728 130.560 139.215 1.00 21.75 ?  261 PHE B O     1 
ATOM   7650  C  CB    . PHE B 1 261 ? 115.387 133.109 138.880 1.00 10.28 ?  261 PHE B CB    1 
ATOM   7651  C  CG    . PHE B 1 261 ? 116.200 133.821 139.921 1.00 22.77 ?  261 PHE B CG    1 
ATOM   7652  C  CD1   . PHE B 1 261 ? 117.107 134.802 139.562 1.00 20.56 ?  261 PHE B CD1   1 
ATOM   7653  C  CD2   . PHE B 1 261 ? 116.025 133.539 141.266 1.00 23.60 ?  261 PHE B CD2   1 
ATOM   7654  C  CE1   . PHE B 1 261 ? 117.842 135.469 140.520 1.00 15.18 ?  261 PHE B CE1   1 
ATOM   7655  C  CE2   . PHE B 1 261 ? 116.756 134.203 142.226 1.00 15.89 ?  261 PHE B CE2   1 
ATOM   7656  C  CZ    . PHE B 1 261 ? 117.667 135.169 141.853 1.00 15.76 ?  261 PHE B CZ    1 
ATOM   7657  N  N     . LEU B 1 262 ? 115.539 130.192 139.619 1.00 23.93 ?  262 LEU B N     1 
ATOM   7658  C  CA    . LEU B 1 262 ? 115.820 129.081 140.520 1.00 23.77 ?  262 LEU B CA    1 
ATOM   7659  C  C     . LEU B 1 262 ? 116.551 127.960 139.795 1.00 28.49 ?  262 LEU B C     1 
ATOM   7660  O  O     . LEU B 1 262 ? 117.430 127.306 140.369 1.00 30.74 ?  262 LEU B O     1 
ATOM   7661  C  CB    . LEU B 1 262 ? 114.524 128.565 141.140 1.00 27.44 ?  262 LEU B CB    1 
ATOM   7662  C  CG    . LEU B 1 262 ? 113.783 129.553 142.040 1.00 24.56 ?  262 LEU B CG    1 
ATOM   7663  C  CD1   . LEU B 1 262 ? 112.461 128.966 142.496 1.00 26.12 ?  262 LEU B CD1   1 
ATOM   7664  C  CD2   . LEU B 1 262 ? 114.645 129.950 143.225 1.00 23.89 ?  262 LEU B CD2   1 
ATOM   7665  N  N     . ASP B 1 263 ? 116.226 127.748 138.519 1.00 34.07 ?  263 ASP B N     1 
ATOM   7666  C  CA    . ASP B 1 263 ? 116.884 126.700 137.755 1.00 25.65 ?  263 ASP B CA    1 
ATOM   7667  C  C     . ASP B 1 263 ? 118.370 126.965 137.571 1.00 29.95 ?  263 ASP B C     1 
ATOM   7668  O  O     . ASP B 1 263 ? 119.099 126.048 137.180 1.00 38.33 ?  263 ASP B O     1 
ATOM   7669  C  CB    . ASP B 1 263 ? 116.208 126.538 136.394 1.00 30.81 ?  263 ASP B CB    1 
ATOM   7670  C  CG    . ASP B 1 263 ? 114.828 125.921 136.499 1.00 37.05 ?  263 ASP B CG    1 
ATOM   7671  O  OD1   . ASP B 1 263 ? 114.538 125.284 137.534 1.00 36.66 ?  263 ASP B OD1   1 
ATOM   7672  O  OD2   . ASP B 1 263 ? 114.034 126.073 135.548 1.00 35.56 -1 263 ASP B OD2   1 
ATOM   7673  N  N     . THR B 1 264 ? 118.835 128.189 137.838 1.00 33.51 ?  264 THR B N     1 
ATOM   7674  C  CA    . THR B 1 264 ? 120.268 128.446 137.799 1.00 32.04 ?  264 THR B CA    1 
ATOM   7675  C  C     . THR B 1 264 ? 121.016 127.709 138.901 1.00 36.16 ?  264 THR B C     1 
ATOM   7676  O  O     . THR B 1 264 ? 122.221 127.474 138.764 1.00 36.90 ?  264 THR B O     1 
ATOM   7677  C  CB    . THR B 1 264 ? 120.542 129.947 137.899 1.00 33.04 ?  264 THR B CB    1 
ATOM   7678  O  OG1   . THR B 1 264 ? 120.001 130.453 139.125 1.00 36.48 ?  264 THR B OG1   1 
ATOM   7679  C  CG2   . THR B 1 264 ? 119.910 130.681 136.727 1.00 30.51 ?  264 THR B CG2   1 
ATOM   7680  N  N     . LYS B 1 265 ? 120.336 127.335 139.986 1.00 32.38 ?  265 LYS B N     1 
ATOM   7681  C  CA    . LYS B 1 265 ? 120.977 126.669 141.111 1.00 34.15 ?  265 LYS B CA    1 
ATOM   7682  C  C     . LYS B 1 265 ? 120.675 125.179 141.190 1.00 36.53 ?  265 LYS B C     1 
ATOM   7683  O  O     . LYS B 1 265 ? 121.183 124.508 142.092 1.00 39.20 ?  265 LYS B O     1 
ATOM   7684  C  CB    . LYS B 1 265 ? 120.576 127.345 142.425 1.00 33.86 ?  265 LYS B CB    1 
ATOM   7685  C  CG    . LYS B 1 265 ? 121.308 128.645 142.692 1.00 32.96 ?  265 LYS B CG    1 
ATOM   7686  C  CD    . LYS B 1 265 ? 122.808 128.465 142.572 1.00 35.96 ?  265 LYS B CD    1 
ATOM   7687  C  CE    . LYS B 1 265 ? 123.528 129.795 142.659 1.00 34.47 ?  265 LYS B CE    1 
ATOM   7688  N  NZ    . LYS B 1 265 ? 124.963 129.673 142.290 1.00 37.38 1  265 LYS B NZ    1 
ATOM   7689  N  N     . LYS B 1 266 ? 119.863 124.646 140.281 1.00 45.03 ?  266 LYS B N     1 
ATOM   7690  C  CA    . LYS B 1 266 ? 119.620 123.210 140.265 1.00 44.08 ?  266 LYS B CA    1 
ATOM   7691  C  C     . LYS B 1 266 ? 120.893 122.467 139.885 1.00 48.90 ?  266 LYS B C     1 
ATOM   7692  O  O     . LYS B 1 266 ? 121.641 122.892 138.999 1.00 50.53 ?  266 LYS B O     1 
ATOM   7693  C  CB    . LYS B 1 266 ? 118.495 122.869 139.289 1.00 44.10 ?  266 LYS B CB    1 
ATOM   7694  C  CG    . LYS B 1 266 ? 117.102 123.035 139.875 1.00 46.71 ?  266 LYS B CG    1 
ATOM   7695  C  CD    . LYS B 1 266 ? 116.034 122.519 138.926 1.00 48.45 ?  266 LYS B CD    1 
ATOM   7696  C  CE    . LYS B 1 266 ? 114.726 122.267 139.660 1.00 47.44 ?  266 LYS B CE    1 
ATOM   7697  N  NZ    . LYS B 1 266 ? 113.608 121.967 138.724 1.00 49.34 1  266 LYS B NZ    1 
ATOM   7698  N  N     . ILE B 1 267 ? 121.144 121.348 140.569 1.00 56.82 ?  267 ILE B N     1 
ATOM   7699  C  CA    . ILE B 1 267 ? 122.368 120.593 140.330 1.00 59.40 ?  267 ILE B CA    1 
ATOM   7700  C  C     . ILE B 1 267 ? 122.352 119.884 138.981 1.00 59.98 ?  267 ILE B C     1 
ATOM   7701  O  O     . ILE B 1 267 ? 123.403 119.440 138.506 1.00 58.71 ?  267 ILE B O     1 
ATOM   7702  C  CB    . ILE B 1 267 ? 122.627 119.613 141.494 1.00 60.41 ?  267 ILE B CB    1 
ATOM   7703  C  CG1   . ILE B 1 267 ? 121.334 118.957 142.010 1.00 59.80 ?  267 ILE B CG1   1 
ATOM   7704  C  CG2   . ILE B 1 267 ? 123.343 120.325 142.634 1.00 58.18 ?  267 ILE B CG2   1 
ATOM   7705  C  CD1   . ILE B 1 267 ? 120.573 118.096 141.018 1.00 57.74 ?  267 ILE B CD1   1 
ATOM   7706  N  N     . SER B 1 268 ? 121.186 119.769 138.347 1.00 62.10 ?  268 SER B N     1 
ATOM   7707  C  CA    . SER B 1 268 ? 121.055 119.150 137.036 1.00 64.31 ?  268 SER B CA    1 
ATOM   7708  C  C     . SER B 1 268 ? 120.981 120.175 135.912 1.00 65.31 ?  268 SER B C     1 
ATOM   7709  O  O     . SER B 1 268 ? 120.722 119.802 134.763 1.00 66.20 ?  268 SER B O     1 
ATOM   7710  C  CB    . SER B 1 268 ? 119.820 118.249 137.003 1.00 67.03 ?  268 SER B CB    1 
ATOM   7711  O  OG    . SER B 1 268 ? 118.659 118.963 137.395 1.00 64.20 ?  268 SER B OG    1 
ATOM   7712  N  N     . ALA B 1 269 ? 121.196 121.451 136.217 1.00 66.97 ?  269 ALA B N     1 
ATOM   7713  C  CA    . ALA B 1 269 ? 121.069 122.501 135.216 1.00 67.58 ?  269 ALA B CA    1 
ATOM   7714  C  C     . ALA B 1 269 ? 122.158 122.386 134.156 1.00 67.63 ?  269 ALA B C     1 
ATOM   7715  O  O     . ALA B 1 269 ? 123.296 121.999 134.436 1.00 65.97 ?  269 ALA B O     1 
ATOM   7716  C  CB    . ALA B 1 269 ? 121.129 123.877 135.877 1.00 65.51 ?  269 ALA B CB    1 
ATOM   7717  N  N     . ASP B 1 270 ? 121.795 122.731 132.924 1.00 73.26 ?  270 ASP B N     1 
ATOM   7718  C  CA    . ASP B 1 270 ? 122.747 122.729 131.826 1.00 73.45 ?  270 ASP B CA    1 
ATOM   7719  C  C     . ASP B 1 270 ? 123.734 123.885 131.977 1.00 73.74 ?  270 ASP B C     1 
ATOM   7720  O  O     . ASP B 1 270 ? 123.492 124.856 132.698 1.00 74.05 ?  270 ASP B O     1 
ATOM   7721  C  CB    . ASP B 1 270 ? 122.018 122.826 130.485 1.00 73.73 ?  270 ASP B CB    1 
ATOM   7722  C  CG    . ASP B 1 270 ? 122.815 122.232 129.342 1.00 75.07 ?  270 ASP B CG    1 
ATOM   7723  O  OD1   . ASP B 1 270 ? 123.934 122.721 129.077 1.00 75.22 ?  270 ASP B OD1   1 
ATOM   7724  O  OD2   . ASP B 1 270 ? 122.324 121.274 128.708 1.00 74.14 -1 270 ASP B OD2   1 
ATOM   7725  N  N     . GLU B 1 271 ? 124.865 123.766 131.277 1.00 73.75 ?  271 GLU B N     1 
ATOM   7726  C  CA    . GLU B 1 271 ? 125.918 124.770 131.397 1.00 73.72 ?  271 GLU B CA    1 
ATOM   7727  C  C     . GLU B 1 271 ? 125.473 126.132 130.873 1.00 72.95 ?  271 GLU B C     1 
ATOM   7728  O  O     . GLU B 1 271 ? 125.950 127.163 131.358 1.00 72.44 ?  271 GLU B O     1 
ATOM   7729  C  CB    . GLU B 1 271 ? 127.174 124.305 130.661 1.00 72.64 ?  271 GLU B CB    1 
ATOM   7730  C  CG    . GLU B 1 271 ? 127.988 123.274 131.425 1.00 73.86 ?  271 GLU B CG    1 
ATOM   7731  C  CD    . GLU B 1 271 ? 128.532 123.814 132.734 1.00 74.42 ?  271 GLU B CD    1 
ATOM   7732  O  OE1   . GLU B 1 271 ? 128.910 125.002 132.777 1.00 73.57 ?  271 GLU B OE1   1 
ATOM   7733  O  OE2   . GLU B 1 271 ? 128.579 123.048 133.719 1.00 73.53 -1 271 GLU B OE2   1 
ATOM   7734  N  N     . ASP B 1 272 ? 124.567 126.160 129.895 1.00 69.22 ?  272 ASP B N     1 
ATOM   7735  C  CA    . ASP B 1 272 ? 124.079 127.430 129.371 1.00 70.00 ?  272 ASP B CA    1 
ATOM   7736  C  C     . ASP B 1 272 ? 123.121 128.132 130.325 1.00 69.56 ?  272 ASP B C     1 
ATOM   7737  O  O     . ASP B 1 272 ? 122.799 129.304 130.099 1.00 68.28 ?  272 ASP B O     1 
ATOM   7738  C  CB    . ASP B 1 272 ? 123.400 127.214 128.016 1.00 69.68 ?  272 ASP B CB    1 
ATOM   7739  C  CG    . ASP B 1 272 ? 122.051 126.532 128.138 1.00 72.04 ?  272 ASP B CG    1 
ATOM   7740  O  OD1   . ASP B 1 272 ? 121.866 125.731 129.078 1.00 71.80 ?  272 ASP B OD1   1 
ATOM   7741  O  OD2   . ASP B 1 272 ? 121.173 126.796 127.289 1.00 69.21 -1 272 ASP B OD2   1 
ATOM   7742  N  N     . VAL B 1 273 ? 122.656 127.450 131.372 1.00 62.08 ?  273 VAL B N     1 
ATOM   7743  C  CA    . VAL B 1 273 ? 121.763 128.030 132.363 1.00 62.78 ?  273 VAL B CA    1 
ATOM   7744  C  C     . VAL B 1 273 ? 122.412 128.098 133.740 1.00 61.16 ?  273 VAL B C     1 
ATOM   7745  O  O     . VAL B 1 273 ? 122.209 129.067 134.479 1.00 60.96 ?  273 VAL B O     1 
ATOM   7746  C  CB    . VAL B 1 273 ? 120.430 127.250 132.429 1.00 63.68 ?  273 VAL B CB    1 
ATOM   7747  C  CG1   . VAL B 1 273 ? 119.541 127.786 133.543 1.00 61.00 ?  273 VAL B CG1   1 
ATOM   7748  C  CG2   . VAL B 1 273 ? 119.712 127.318 131.091 1.00 62.41 ?  273 VAL B CG2   1 
ATOM   7749  N  N     . ARG B 1 274 ? 123.205 127.088 134.096 1.00 61.27 ?  274 ARG B N     1 
ATOM   7750  C  CA    . ARG B 1 274 ? 123.791 127.015 135.428 1.00 60.75 ?  274 ARG B CA    1 
ATOM   7751  C  C     . ARG B 1 274 ? 124.696 128.212 135.698 1.00 59.70 ?  274 ARG B C     1 
ATOM   7752  O  O     . ARG B 1 274 ? 125.500 128.613 134.852 1.00 62.45 ?  274 ARG B O     1 
ATOM   7753  C  CB    . ARG B 1 274 ? 124.582 125.714 135.584 1.00 62.89 ?  274 ARG B CB    1 
ATOM   7754  C  CG    . ARG B 1 274 ? 125.812 125.828 136.473 1.00 58.68 ?  274 ARG B CG    1 
ATOM   7755  C  CD    . ARG B 1 274 ? 126.028 124.572 137.298 1.00 61.77 ?  274 ARG B CD    1 
ATOM   7756  N  NE    . ARG B 1 274 ? 126.328 123.415 136.463 1.00 65.06 ?  274 ARG B NE    1 
ATOM   7757  C  CZ    . ARG B 1 274 ? 125.620 122.295 136.452 1.00 66.11 ?  274 ARG B CZ    1 
ATOM   7758  N  NH1   . ARG B 1 274 ? 124.562 122.138 137.229 1.00 63.75 1  274 ARG B NH1   1 
ATOM   7759  N  NH2   . ARG B 1 274 ? 125.984 121.304 135.642 1.00 63.75 ?  274 ARG B NH2   1 
ATOM   7760  N  N     . VAL B 1 275 ? 124.549 128.785 136.889 1.00 47.00 ?  275 VAL B N     1 
ATOM   7761  C  CA    . VAL B 1 275 ? 125.393 129.868 137.376 1.00 44.89 ?  275 VAL B CA    1 
ATOM   7762  C  C     . VAL B 1 275 ? 125.955 129.438 138.724 1.00 48.71 ?  275 VAL B C     1 
ATOM   7763  O  O     . VAL B 1 275 ? 125.198 129.015 139.606 1.00 51.14 ?  275 VAL B O     1 
ATOM   7764  C  CB    . VAL B 1 275 ? 124.606 131.185 137.498 1.00 45.84 ?  275 VAL B CB    1 
ATOM   7765  C  CG1   . VAL B 1 275 ? 125.370 132.170 138.338 1.00 45.29 ?  275 VAL B CG1   1 
ATOM   7766  C  CG2   . VAL B 1 275 ? 124.317 131.764 136.122 1.00 43.95 ?  275 VAL B CG2   1 
ATOM   7767  N  N     . LYS B 1 276 ? 127.277 129.544 138.887 1.00 46.32 ?  276 LYS B N     1 
ATOM   7768  C  CA    . LYS B 1 276 ? 127.947 128.921 140.020 1.00 47.39 ?  276 LYS B CA    1 
ATOM   7769  C  C     . LYS B 1 276 ? 128.637 129.882 140.980 1.00 45.61 ?  276 LYS B C     1 
ATOM   7770  O  O     . LYS B 1 276 ? 128.842 129.510 142.140 1.00 51.16 ?  276 LYS B O     1 
ATOM   7771  C  CB    . LYS B 1 276 ? 128.973 127.887 139.526 1.00 48.20 ?  276 LYS B CB    1 
ATOM   7772  C  CG    . LYS B 1 276 ? 130.303 128.468 139.087 1.00 47.46 ?  276 LYS B CG    1 
ATOM   7773  C  CD    . LYS B 1 276 ? 131.028 127.529 138.140 1.00 50.60 ?  276 LYS B CD    1 
ATOM   7774  C  CE    . LYS B 1 276 ? 130.246 127.351 136.850 1.00 49.82 ?  276 LYS B CE    1 
ATOM   7775  N  NZ    . LYS B 1 276 ? 129.765 128.656 136.321 1.00 48.35 1  276 LYS B NZ    1 
ATOM   7776  N  N     . THR B 1 277 ? 129.005 131.089 140.550 1.00 37.24 ?  277 THR B N     1 
ATOM   7777  C  CA    . THR B 1 277 ? 129.636 132.056 141.442 1.00 36.87 ?  277 THR B CA    1 
ATOM   7778  C  C     . THR B 1 277 ? 128.710 133.192 141.850 1.00 38.11 ?  277 THR B C     1 
ATOM   7779  O  O     . THR B 1 277 ? 129.167 134.146 142.489 1.00 42.20 ?  277 THR B O     1 
ATOM   7780  C  CB    . THR B 1 277 ? 130.902 132.645 140.804 1.00 39.89 ?  277 THR B CB    1 
ATOM   7781  O  OG1   . THR B 1 277 ? 130.558 133.801 140.029 1.00 37.56 ?  277 THR B OG1   1 
ATOM   7782  C  CG2   . THR B 1 277 ? 131.583 131.624 139.919 1.00 40.45 ?  277 THR B CG2   1 
ATOM   7783  N  N     . LEU B 1 278 ? 127.430 133.120 141.507 1.00 29.21 ?  278 LEU B N     1 
ATOM   7784  C  CA    . LEU B 1 278 ? 126.468 134.174 141.809 1.00 29.10 ?  278 LEU B CA    1 
ATOM   7785  C  C     . LEU B 1 278 ? 125.375 133.592 142.696 1.00 23.31 ?  278 LEU B C     1 
ATOM   7786  O  O     . LEU B 1 278 ? 124.575 132.767 142.243 1.00 29.21 ?  278 LEU B O     1 
ATOM   7787  C  CB    . LEU B 1 278 ? 125.889 134.760 140.524 1.00 26.18 ?  278 LEU B CB    1 
ATOM   7788  C  CG    . LEU B 1 278 ? 124.960 135.967 140.598 1.00 26.72 ?  278 LEU B CG    1 
ATOM   7789  C  CD1   . LEU B 1 278 ? 125.759 137.247 140.708 1.00 23.26 ?  278 LEU B CD1   1 
ATOM   7790  C  CD2   . LEU B 1 278 ? 124.066 136.000 139.371 1.00 23.82 ?  278 LEU B CD2   1 
ATOM   7791  N  N     . SER B 1 279 ? 125.345 134.020 143.953 1.00 23.24 ?  279 SER B N     1 
ATOM   7792  C  CA    . SER B 1 279 ? 124.285 133.608 144.861 1.00 18.49 ?  279 SER B CA    1 
ATOM   7793  C  C     . SER B 1 279 ? 122.948 134.163 144.390 1.00 19.07 ?  279 SER B C     1 
ATOM   7794  O  O     . SER B 1 279 ? 122.879 135.194 143.718 1.00 29.86 ?  279 SER B O     1 
ATOM   7795  C  CB    . SER B 1 279 ? 124.581 134.086 146.280 1.00 17.19 ?  279 SER B CB    1 
ATOM   7796  O  OG    . SER B 1 279 ? 125.810 133.561 146.748 1.00 23.76 ?  279 SER B OG    1 
ATOM   7797  N  N     . ILE B 1 280 ? 121.873 133.463 144.736 1.00 20.84 ?  280 ILE B N     1 
ATOM   7798  C  CA    . ILE B 1 280 ? 120.537 133.847 144.305 1.00 19.36 ?  280 ILE B CA    1 
ATOM   7799  C  C     . ILE B 1 280 ? 119.676 134.101 145.533 1.00 20.82 ?  280 ILE B C     1 
ATOM   7800  O  O     . ILE B 1 280 ? 119.794 133.402 146.546 1.00 24.93 ?  280 ILE B O     1 
ATOM   7801  C  CB    . ILE B 1 280 ? 119.898 132.788 143.381 1.00 16.70 ?  280 ILE B CB    1 
ATOM   7802  C  CG1   . ILE B 1 280 ? 119.541 131.514 144.141 1.00 22.49 ?  280 ILE B CG1   1 
ATOM   7803  C  CG2   . ILE B 1 280 ? 120.846 132.429 142.264 1.00 25.14 ?  280 ILE B CG2   1 
ATOM   7804  C  CD1   . ILE B 1 280 ? 118.491 130.679 143.439 1.00 21.68 ?  280 ILE B CD1   1 
ATOM   7805  N  N     . GLY B 1 281 ? 118.843 135.128 145.450 1.00 11.91 ?  281 GLY B N     1 
ATOM   7806  C  CA    . GLY B 1 281 ? 117.879 135.412 146.491 1.00 6.43  ?  281 GLY B CA    1 
ATOM   7807  C  C     . GLY B 1 281 ? 116.517 135.668 145.886 1.00 8.98  ?  281 GLY B C     1 
ATOM   7808  O  O     . GLY B 1 281 ? 116.392 136.187 144.778 1.00 18.68 ?  281 GLY B O     1 
ATOM   7809  N  N     . VAL B 1 282 ? 115.486 135.286 146.632 1.00 8.40  ?  282 VAL B N     1 
ATOM   7810  C  CA    . VAL B 1 282 ? 114.103 135.420 146.194 1.00 14.89 ?  282 VAL B CA    1 
ATOM   7811  C  C     . VAL B 1 282 ? 113.377 136.332 147.170 1.00 11.81 ?  282 VAL B C     1 
ATOM   7812  O  O     . VAL B 1 282 ? 113.437 136.123 148.387 1.00 18.21 ?  282 VAL B O     1 
ATOM   7813  C  CB    . VAL B 1 282 ? 113.406 134.051 146.089 1.00 13.09 ?  282 VAL B CB    1 
ATOM   7814  C  CG1   . VAL B 1 282 ? 111.906 134.226 145.981 1.00 15.57 ?  282 VAL B CG1   1 
ATOM   7815  C  CG2   . VAL B 1 282 ? 113.932 133.291 144.888 1.00 19.32 ?  282 VAL B CG2   1 
ATOM   7816  N  N     . VAL B 1 283 ? 112.704 137.345 146.636 1.00 7.35  ?  283 VAL B N     1 
ATOM   7817  C  CA    . VAL B 1 283 ? 111.940 138.297 147.431 1.00 10.05 ?  283 VAL B CA    1 
ATOM   7818  C  C     . VAL B 1 283 ? 110.474 137.895 147.361 1.00 12.37 ?  283 VAL B C     1 
ATOM   7819  O  O     . VAL B 1 283 ? 109.869 137.905 146.282 1.00 22.54 ?  283 VAL B O     1 
ATOM   7820  C  CB    . VAL B 1 283 ? 112.151 139.734 146.935 1.00 6.35  ?  283 VAL B CB    1 
ATOM   7821  C  CG1   . VAL B 1 283 ? 111.444 140.716 147.846 1.00 9.67  ?  283 VAL B CG1   1 
ATOM   7822  C  CG2   . VAL B 1 283 ? 113.636 140.041 146.856 1.00 8.67  ?  283 VAL B CG2   1 
ATOM   7823  N  N     . ILE B 1 284 ? 109.904 137.542 148.507 1.00 17.09 ?  284 ILE B N     1 
ATOM   7824  C  CA    . ILE B 1 284 ? 108.557 136.990 148.591 1.00 17.92 ?  284 ILE B CA    1 
ATOM   7825  C  C     . ILE B 1 284 ? 107.668 138.013 149.292 1.00 17.41 ?  284 ILE B C     1 
ATOM   7826  O  O     . ILE B 1 284 ? 107.799 138.219 150.508 1.00 19.60 ?  284 ILE B O     1 
ATOM   7827  C  CB    . ILE B 1 284 ? 108.545 135.646 149.331 1.00 12.85 ?  284 ILE B CB    1 
ATOM   7828  C  CG1   . ILE B 1 284 ? 109.606 134.709 148.754 1.00 13.68 ?  284 ILE B CG1   1 
ATOM   7829  C  CG2   . ILE B 1 284 ? 107.166 135.013 149.257 1.00 17.19 ?  284 ILE B CG2   1 
ATOM   7830  C  CD1   . ILE B 1 284 ? 109.565 133.313 149.326 1.00 15.71 ?  284 ILE B CD1   1 
ATOM   7831  N  N     . PRO B 1 285 ? 106.759 138.674 148.582 1.00 22.30 ?  285 PRO B N     1 
ATOM   7832  C  CA    . PRO B 1 285 ? 105.752 139.497 149.258 1.00 25.67 ?  285 PRO B CA    1 
ATOM   7833  C  C     . PRO B 1 285 ? 104.752 138.631 150.009 1.00 25.21 ?  285 PRO B C     1 
ATOM   7834  O  O     . PRO B 1 285 ? 104.662 137.418 149.812 1.00 24.82 ?  285 PRO B O     1 
ATOM   7835  C  CB    . PRO B 1 285 ? 105.076 140.256 148.110 1.00 23.16 ?  285 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 1 285 ? 106.026 140.153 146.960 1.00 19.61 ?  285 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 1 285 ? 106.712 138.835 147.121 1.00 16.49 ?  285 PRO B CD    1 
ATOM   7838  N  N     . ASP B 1 286 ? 103.994 139.282 150.895 1.00 29.11 ?  286 ASP B N     1 
ATOM   7839  C  CA    . ASP B 1 286 ? 102.955 138.578 151.639 1.00 23.66 ?  286 ASP B CA    1 
ATOM   7840  C  C     . ASP B 1 286 ? 101.871 138.023 150.728 1.00 30.67 ?  286 ASP B C     1 
ATOM   7841  O  O     . ASP B 1 286 ? 101.188 137.065 151.109 1.00 32.81 ?  286 ASP B O     1 
ATOM   7842  C  CB    . ASP B 1 286 ? 102.332 139.507 152.681 1.00 26.22 ?  286 ASP B CB    1 
ATOM   7843  C  CG    . ASP B 1 286 ? 102.857 139.252 154.078 1.00 37.25 ?  286 ASP B CG    1 
ATOM   7844  O  OD1   . ASP B 1 286 ? 104.067 138.977 154.218 1.00 38.58 ?  286 ASP B OD1   1 
ATOM   7845  O  OD2   . ASP B 1 286 ? 102.061 139.331 155.037 1.00 39.34 -1 286 ASP B OD2   1 
ATOM   7846  N  N     . LYS B 1 287 ? 101.697 138.604 149.537 1.00 33.03 ?  287 LYS B N     1 
ATOM   7847  C  CA    . LYS B 1 287 ? 100.696 138.102 148.604 1.00 25.93 ?  287 LYS B CA    1 
ATOM   7848  C  C     . LYS B 1 287 ? 101.000 136.672 148.177 1.00 26.93 ?  287 LYS B C     1 
ATOM   7849  O  O     . LYS B 1 287 ? 100.088 135.844 148.069 1.00 33.99 ?  287 LYS B O     1 
ATOM   7850  C  CB    . LYS B 1 287 ? 100.611 139.018 147.384 1.00 27.63 ?  287 LYS B CB    1 
ATOM   7851  C  CG    . LYS B 1 287 ? 99.424  138.731 146.482 1.00 27.80 ?  287 LYS B CG    1 
ATOM   7852  C  CD    . LYS B 1 287 ? 98.128  138.737 147.273 1.00 32.66 ?  287 LYS B CD    1 
ATOM   7853  C  CE    . LYS B 1 287 ? 96.923  138.584 146.365 1.00 31.91 ?  287 LYS B CE    1 
ATOM   7854  N  NZ    . LYS B 1 287 ? 95.647  138.743 147.114 1.00 33.82 1  287 LYS B NZ    1 
ATOM   7855  N  N     . PHE B 1 288 ? 102.273 136.364 147.919 1.00 26.58 ?  288 PHE B N     1 
ATOM   7856  C  CA    . PHE B 1 288 ? 102.632 135.009 147.512 1.00 23.20 ?  288 PHE B CA    1 
ATOM   7857  C  C     . PHE B 1 288 ? 102.349 134.004 148.620 1.00 22.50 ?  288 PHE B C     1 
ATOM   7858  O  O     . PHE B 1 288 ? 101.837 132.909 148.361 1.00 30.53 ?  288 PHE B O     1 
ATOM   7859  C  CB    . PHE B 1 288 ? 104.103 134.952 147.104 1.00 27.79 ?  288 PHE B CB    1 
ATOM   7860  C  CG    . PHE B 1 288 ? 104.525 133.619 146.559 1.00 26.67 ?  288 PHE B CG    1 
ATOM   7861  C  CD1   . PHE B 1 288 ? 104.306 133.301 145.231 1.00 23.90 ?  288 PHE B CD1   1 
ATOM   7862  C  CD2   . PHE B 1 288 ? 105.131 132.680 147.377 1.00 23.29 ?  288 PHE B CD2   1 
ATOM   7863  C  CE1   . PHE B 1 288 ? 104.687 132.075 144.726 1.00 28.59 ?  288 PHE B CE1   1 
ATOM   7864  C  CE2   . PHE B 1 288 ? 105.513 131.452 146.878 1.00 24.98 ?  288 PHE B CE2   1 
ATOM   7865  C  CZ    . PHE B 1 288 ? 105.293 131.149 145.551 1.00 26.34 ?  288 PHE B CZ    1 
ATOM   7866  N  N     . VAL B 1 289 ? 102.685 134.356 149.862 1.00 25.75 ?  289 VAL B N     1 
ATOM   7867  C  CA    . VAL B 1 289 ? 102.419 133.463 150.985 1.00 26.07 ?  289 VAL B CA    1 
ATOM   7868  C  C     . VAL B 1 289 ? 100.920 133.284 151.177 1.00 26.59 ?  289 VAL B C     1 
ATOM   7869  O  O     . VAL B 1 289 ? 100.450 132.189 151.503 1.00 29.88 ?  289 VAL B O     1 
ATOM   7870  C  CB    . VAL B 1 289 ? 103.097 133.995 152.261 1.00 31.81 ?  289 VAL B CB    1 
ATOM   7871  C  CG1   . VAL B 1 289 ? 102.973 132.985 153.389 1.00 23.07 ?  289 VAL B CG1   1 
ATOM   7872  C  CG2   . VAL B 1 289 ? 104.556 134.324 151.987 1.00 25.12 ?  289 VAL B CG2   1 
ATOM   7873  N  N     . GLU B 1 290 ? 100.147 134.353 150.982 1.00 34.76 ?  290 GLU B N     1 
ATOM   7874  C  CA    . GLU B 1 290 ? 98.695  134.248 151.082 1.00 30.92 ?  290 GLU B CA    1 
ATOM   7875  C  C     . GLU B 1 290 ? 98.129  133.330 150.004 1.00 34.54 ?  290 GLU B C     1 
ATOM   7876  O  O     . GLU B 1 290 ? 97.252  132.503 150.279 1.00 39.59 ?  290 GLU B O     1 
ATOM   7877  C  CB    . GLU B 1 290 ? 98.068  135.640 150.996 1.00 28.23 ?  290 GLU B CB    1 
ATOM   7878  C  CG    . GLU B 1 290 ? 96.683  135.675 150.377 1.00 37.04 ?  290 GLU B CG    1 
ATOM   7879  C  CD    . GLU B 1 290 ? 96.069  137.060 150.407 1.00 41.41 ?  290 GLU B CD    1 
ATOM   7880  O  OE1   . GLU B 1 290 ? 96.095  137.698 151.480 1.00 42.37 ?  290 GLU B OE1   1 
ATOM   7881  O  OE2   . GLU B 1 290 ? 95.563  137.511 149.359 1.00 38.39 -1 290 GLU B OE2   1 
ATOM   7882  N  N     . LEU B 1 291 ? 98.624  133.459 148.771 1.00 27.28 ?  291 LEU B N     1 
ATOM   7883  C  CA    . LEU B 1 291 ? 98.157  132.599 147.685 1.00 25.18 ?  291 LEU B CA    1 
ATOM   7884  C  C     . LEU B 1 291 ? 98.524  131.142 147.935 1.00 32.91 ?  291 LEU B C     1 
ATOM   7885  O  O     . LEU B 1 291 ? 97.713  130.243 147.687 1.00 37.34 ?  291 LEU B O     1 
ATOM   7886  C  CB    . LEU B 1 291 ? 98.735  133.074 146.352 1.00 29.43 ?  291 LEU B CB    1 
ATOM   7887  C  CG    . LEU B 1 291 ? 98.263  134.433 145.835 1.00 29.44 ?  291 LEU B CG    1 
ATOM   7888  C  CD1   . LEU B 1 291 ? 99.261  134.999 144.842 1.00 26.20 ?  291 LEU B CD1   1 
ATOM   7889  C  CD2   . LEU B 1 291 ? 96.885  134.323 145.211 1.00 32.36 ?  291 LEU B CD2   1 
ATOM   7890  N  N     . ALA B 1 292 ? 99.745  130.888 148.411 1.00 32.40 ?  292 ALA B N     1 
ATOM   7891  C  CA    . ALA B 1 292 ? 100.150 129.520 148.716 1.00 27.35 ?  292 ALA B CA    1 
ATOM   7892  C  C     . ALA B 1 292 ? 99.328  128.944 149.864 1.00 29.21 ?  292 ALA B C     1 
ATOM   7893  O  O     . ALA B 1 292 ? 98.967  127.762 149.844 1.00 36.30 ?  292 ALA B O     1 
ATOM   7894  C  CB    . ALA B 1 292 ? 101.641 129.474 149.046 1.00 27.19 ?  292 ALA B CB    1 
ATOM   7895  N  N     . ARG B 1 293 ? 99.031  129.765 150.873 1.00 28.11 ?  293 ARG B N     1 
ATOM   7896  C  CA    . ARG B 1 293 ? 98.239  129.303 152.008 1.00 28.07 ?  293 ARG B CA    1 
ATOM   7897  C  C     . ARG B 1 293 ? 96.836  128.898 151.576 1.00 35.25 ?  293 ARG B C     1 
ATOM   7898  O  O     . ARG B 1 293 ? 96.311  127.874 152.026 1.00 39.63 ?  293 ARG B O     1 
ATOM   7899  C  CB    . ARG B 1 293 ? 98.186  130.397 153.073 1.00 29.39 ?  293 ARG B CB    1 
ATOM   7900  C  CG    . ARG B 1 293 ? 97.108  130.217 154.124 1.00 31.61 ?  293 ARG B CG    1 
ATOM   7901  C  CD    . ARG B 1 293 ? 96.926  131.496 154.920 1.00 32.58 ?  293 ARG B CD    1 
ATOM   7902  N  NE    . ARG B 1 293 ? 98.207  132.058 155.328 1.00 38.76 ?  293 ARG B NE    1 
ATOM   7903  C  CZ    . ARG B 1 293 ? 98.584  133.308 155.097 1.00 37.05 ?  293 ARG B CZ    1 
ATOM   7904  N  NH1   . ARG B 1 293 ? 97.795  134.163 154.469 1.00 36.91 1  293 ARG B NH1   1 
ATOM   7905  N  NH2   . ARG B 1 293 ? 99.786  133.708 155.502 1.00 29.92 ?  293 ARG B NH2   1 
ATOM   7906  N  N     . GLU B 1 294 ? 96.217  129.685 150.700 1.00 44.02 ?  294 GLU B N     1 
ATOM   7907  C  CA    . GLU B 1 294 ? 94.875  129.400 150.213 1.00 41.02 ?  294 GLU B CA    1 
ATOM   7908  C  C     . GLU B 1 294 ? 94.861  128.405 149.061 1.00 42.10 ?  294 GLU B C     1 
ATOM   7909  O  O     . GLU B 1 294 ? 93.776  128.050 148.587 1.00 46.91 ?  294 GLU B O     1 
ATOM   7910  C  CB    . GLU B 1 294 ? 94.192  130.700 149.783 1.00 37.63 ?  294 GLU B CB    1 
ATOM   7911  C  CG    . GLU B 1 294 ? 94.080  131.730 150.894 1.00 42.57 ?  294 GLU B CG    1 
ATOM   7912  C  CD    . GLU B 1 294 ? 93.607  133.081 150.394 1.00 48.77 ?  294 GLU B CD    1 
ATOM   7913  O  OE1   . GLU B 1 294 ? 93.424  133.233 149.169 1.00 48.12 ?  294 GLU B OE1   1 
ATOM   7914  O  OE2   . GLU B 1 294 ? 93.419  133.992 151.228 1.00 45.21 -1 294 GLU B OE2   1 
ATOM   7915  N  N     . ASP B 1 295 ? 96.031  127.961 148.599 1.00 39.29 ?  295 ASP B N     1 
ATOM   7916  C  CA    . ASP B 1 295 ? 96.173  126.999 147.507 1.00 41.69 ?  295 ASP B CA    1 
ATOM   7917  C  C     . ASP B 1 295 ? 95.589  127.514 146.196 1.00 45.58 ?  295 ASP B C     1 
ATOM   7918  O  O     . ASP B 1 295 ? 95.337  126.730 145.274 1.00 46.25 ?  295 ASP B O     1 
ATOM   7919  C  CB    . ASP B 1 295 ? 95.548  125.646 147.867 1.00 45.70 ?  295 ASP B CB    1 
ATOM   7920  C  CG    . ASP B 1 295 ? 96.369  124.474 147.369 1.00 50.22 ?  295 ASP B CG    1 
ATOM   7921  O  OD1   . ASP B 1 295 ? 96.311  123.396 147.995 1.00 47.79 ?  295 ASP B OD1   1 
ATOM   7922  O  OD2   . ASP B 1 295 ? 97.074  124.631 146.350 1.00 47.83 -1 295 ASP B OD2   1 
ATOM   7923  N  N     . LYS B 1 296 ? 95.368  128.822 146.092 1.00 45.81 ?  296 LYS B N     1 
ATOM   7924  C  CA    . LYS B 1 296 ? 94.893  129.417 144.853 1.00 44.99 ?  296 LYS B CA    1 
ATOM   7925  C  C     . LYS B 1 296 ? 96.058  129.591 143.890 1.00 46.34 ?  296 LYS B C     1 
ATOM   7926  O  O     . LYS B 1 296 ? 97.126  130.073 144.279 1.00 48.28 ?  296 LYS B O     1 
ATOM   7927  C  CB    . LYS B 1 296 ? 94.226  130.764 145.131 1.00 45.13 ?  296 LYS B CB    1 
ATOM   7928  C  CG    . LYS B 1 296 ? 92.987  130.673 146.006 1.00 46.13 ?  296 LYS B CG    1 
ATOM   7929  C  CD    . LYS B 1 296 ? 92.408  132.048 146.293 1.00 46.16 ?  296 LYS B CD    1 
ATOM   7930  C  CE    . LYS B 1 296 ? 91.114  131.947 147.086 1.00 47.56 ?  296 LYS B CE    1 
ATOM   7931  N  NZ    . LYS B 1 296 ? 90.679  133.272 147.609 1.00 45.77 1  296 LYS B NZ    1 
ATOM   7932  N  N     . ALA B 1 297 ? 95.856  129.192 142.635 1.00 44.65 ?  297 ALA B N     1 
ATOM   7933  C  CA    . ALA B 1 297 ? 96.912  129.302 141.638 1.00 43.38 ?  297 ALA B CA    1 
ATOM   7934  C  C     . ALA B 1 297 ? 97.319  130.758 141.455 1.00 42.38 ?  297 ALA B C     1 
ATOM   7935  O  O     . ALA B 1 297 ? 96.471  131.639 141.288 1.00 44.72 ?  297 ALA B O     1 
ATOM   7936  C  CB    . ALA B 1 297 ? 96.449  128.708 140.309 1.00 42.71 ?  297 ALA B CB    1 
ATOM   7937  N  N     . ALA B 1 298 ? 98.624  131.007 141.486 1.00 34.57 ?  298 ALA B N     1 
ATOM   7938  C  CA    . ALA B 1 298 ? 99.145  132.360 141.404 1.00 33.18 ?  298 ALA B CA    1 
ATOM   7939  C  C     . ALA B 1 298 ? 99.557  132.685 139.974 1.00 35.87 ?  298 ALA B C     1 
ATOM   7940  O  O     . ALA B 1 298 ? 99.541  131.836 139.082 1.00 40.21 ?  298 ALA B O     1 
ATOM   7941  C  CB    . ALA B 1 298 ? 100.327 132.536 142.357 1.00 34.50 ?  298 ALA B CB    1 
ATOM   7942  N  N     . TYR B 1 299 ? 99.944  133.938 139.761 1.00 36.18 ?  299 TYR B N     1 
ATOM   7943  C  CA    . TYR B 1 299 ? 100.379 134.401 138.452 1.00 25.69 ?  299 TYR B CA    1 
ATOM   7944  C  C     . TYR B 1 299 ? 101.700 135.139 138.592 1.00 27.90 ?  299 TYR B C     1 
ATOM   7945  O  O     . TYR B 1 299 ? 101.811 136.075 139.389 1.00 34.61 ?  299 TYR B O     1 
ATOM   7946  C  CB    . TYR B 1 299 ? 99.330  135.314 137.812 1.00 30.33 ?  299 TYR B CB    1 
ATOM   7947  C  CG    . TYR B 1 299 ? 98.161  134.572 137.205 1.00 31.78 ?  299 TYR B CG    1 
ATOM   7948  C  CD1   . TYR B 1 299 ? 98.284  133.921 135.985 1.00 33.34 ?  299 TYR B CD1   1 
ATOM   7949  C  CD2   . TYR B 1 299 ? 96.930  134.533 137.846 1.00 32.79 ?  299 TYR B CD2   1 
ATOM   7950  C  CE1   . TYR B 1 299 ? 97.219  133.246 135.426 1.00 33.86 ?  299 TYR B CE1   1 
ATOM   7951  C  CE2   . TYR B 1 299 ? 95.857  133.861 137.294 1.00 33.08 ?  299 TYR B CE2   1 
ATOM   7952  C  CZ    . TYR B 1 299 ? 96.008  133.218 136.083 1.00 35.07 ?  299 TYR B CZ    1 
ATOM   7953  O  OH    . TYR B 1 299 ? 94.942  132.548 135.528 1.00 37.22 ?  299 TYR B OH    1 
ATOM   7954  N  N     . VAL B 1 300 ? 102.693 134.715 137.827 1.00 29.64 ?  300 VAL B N     1 
ATOM   7955  C  CA    . VAL B 1 300 ? 103.935 135.465 137.690 1.00 22.32 ?  300 VAL B CA    1 
ATOM   7956  C  C     . VAL B 1 300 ? 103.770 136.412 136.514 1.00 25.64 ?  300 VAL B C     1 
ATOM   7957  O  O     . VAL B 1 300 ? 103.015 136.136 135.580 1.00 30.12 ?  300 VAL B O     1 
ATOM   7958  C  CB    . VAL B 1 300 ? 105.150 134.531 137.511 1.00 24.45 ?  300 VAL B CB    1 
ATOM   7959  C  CG1   . VAL B 1 300 ? 105.506 133.870 138.830 1.00 23.16 ?  300 VAL B CG1   1 
ATOM   7960  C  CG2   . VAL B 1 300 ? 104.867 133.488 136.443 1.00 26.14 ?  300 VAL B CG2   1 
ATOM   7961  N  N     . PHE B 1 301 ? 104.465 137.541 136.552 1.00 25.84 ?  301 PHE B N     1 
ATOM   7962  C  CA    . PHE B 1 301 ? 104.175 138.628 135.635 1.00 20.81 ?  301 PHE B CA    1 
ATOM   7963  C  C     . PHE B 1 301 ? 105.390 138.991 134.795 1.00 28.11 ?  301 PHE B C     1 
ATOM   7964  O  O     . PHE B 1 301 ? 106.540 138.779 135.190 1.00 29.52 ?  301 PHE B O     1 
ATOM   7965  C  CB    . PHE B 1 301 ? 103.681 139.864 136.394 1.00 24.66 ?  301 PHE B CB    1 
ATOM   7966  C  CG    . PHE B 1 301 ? 102.452 139.613 137.210 1.00 27.51 ?  301 PHE B CG    1 
ATOM   7967  C  CD1   . PHE B 1 301 ? 101.222 139.448 136.598 1.00 26.92 ?  301 PHE B CD1   1 
ATOM   7968  C  CD2   . PHE B 1 301 ? 102.524 139.535 138.589 1.00 25.39 ?  301 PHE B CD2   1 
ATOM   7969  C  CE1   . PHE B 1 301 ? 100.090 139.209 137.344 1.00 27.62 ?  301 PHE B CE1   1 
ATOM   7970  C  CE2   . PHE B 1 301 ? 101.394 139.299 139.340 1.00 28.97 ?  301 PHE B CE2   1 
ATOM   7971  C  CZ    . PHE B 1 301 ? 100.175 139.138 138.717 1.00 28.06 ?  301 PHE B CZ    1 
ATOM   7972  N  N     . TYR B 1 302 ? 105.105 139.546 133.617 1.00 25.95 ?  302 TYR B N     1 
ATOM   7973  C  CA    . TYR B 1 302 ? 106.135 140.092 132.747 1.00 26.54 ?  302 TYR B CA    1 
ATOM   7974  C  C     . TYR B 1 302 ? 106.357 141.545 133.140 1.00 29.50 ?  302 TYR B C     1 
ATOM   7975  O  O     . TYR B 1 302 ? 105.430 142.357 133.004 1.00 30.63 ?  302 TYR B O     1 
ATOM   7976  C  CB    . TYR B 1 302 ? 105.716 139.988 131.288 1.00 25.74 ?  302 TYR B CB    1 
ATOM   7977  C  CG    . TYR B 1 302 ? 105.742 138.581 130.738 1.00 27.02 ?  302 TYR B CG    1 
ATOM   7978  C  CD1   . TYR B 1 302 ? 104.761 137.662 131.082 1.00 25.03 ?  302 TYR B CD1   1 
ATOM   7979  C  CD2   . TYR B 1 302 ? 106.746 138.173 129.873 1.00 27.54 ?  302 TYR B CD2   1 
ATOM   7980  C  CE1   . TYR B 1 302 ? 104.780 136.378 130.581 1.00 25.70 ?  302 TYR B CE1   1 
ATOM   7981  C  CE2   . TYR B 1 302 ? 106.773 136.892 129.365 1.00 26.81 ?  302 TYR B CE2   1 
ATOM   7982  C  CZ    . TYR B 1 302 ? 105.788 135.998 129.723 1.00 30.33 ?  302 TYR B CZ    1 
ATOM   7983  O  OH    . TYR B 1 302 ? 105.814 134.718 129.220 1.00 33.17 ?  302 TYR B OH    1 
ATOM   7984  N  N     . PRO B 1 303 ? 107.535 141.914 133.644 1.00 28.05 ?  303 PRO B N     1 
ATOM   7985  C  CA    . PRO B 1 303 ? 107.722 143.285 134.147 1.00 25.48 ?  303 PRO B CA    1 
ATOM   7986  C  C     . PRO B 1 303 ? 107.522 144.365 133.100 1.00 29.88 ?  303 PRO B C     1 
ATOM   7987  O  O     . PRO B 1 303 ? 107.031 145.449 133.435 1.00 30.10 ?  303 PRO B O     1 
ATOM   7988  C  CB    . PRO B 1 303 ? 109.167 143.272 134.665 1.00 23.10 ?  303 PRO B CB    1 
ATOM   7989  C  CG    . PRO B 1 303 ? 109.470 141.843 134.916 1.00 25.78 ?  303 PRO B CG    1 
ATOM   7990  C  CD    . PRO B 1 303 ? 108.717 141.071 133.883 1.00 22.71 ?  303 PRO B CD    1 
ATOM   7991  N  N     . HIS B 1 304 ? 107.889 144.108 131.842 1.00 29.63 ?  304 HIS B N     1 
ATOM   7992  C  CA    . HIS B 1 304 ? 107.833 145.167 130.840 1.00 29.90 ?  304 HIS B CA    1 
ATOM   7993  C  C     . HIS B 1 304 ? 106.396 145.524 130.486 1.00 31.79 ?  304 HIS B C     1 
ATOM   7994  O  O     . HIS B 1 304 ? 106.087 146.695 130.243 1.00 37.64 ?  304 HIS B O     1 
ATOM   7995  C  CB    . HIS B 1 304 ? 108.603 144.761 129.588 1.00 27.70 ?  304 HIS B CB    1 
ATOM   7996  C  CG    . HIS B 1 304 ? 108.731 145.862 128.583 1.00 28.80 ?  304 HIS B CG    1 
ATOM   7997  N  ND1   . HIS B 1 304 ? 109.013 147.162 128.939 1.00 27.07 ?  304 HIS B ND1   1 
ATOM   7998  C  CD2   . HIS B 1 304 ? 108.611 145.858 127.235 1.00 35.59 ?  304 HIS B CD2   1 
ATOM   7999  C  CE1   . HIS B 1 304 ? 109.064 147.912 127.854 1.00 30.15 ?  304 HIS B CE1   1 
ATOM   8000  N  NE2   . HIS B 1 304 ? 108.823 147.146 126.806 1.00 35.61 ?  304 HIS B NE2   1 
ATOM   8001  N  N     . THR B 1 305 ? 105.504 144.533 130.440 1.00 28.56 ?  305 THR B N     1 
ATOM   8002  C  CA    . THR B 1 305 ? 104.097 144.824 130.184 1.00 32.68 ?  305 THR B CA    1 
ATOM   8003  C  C     . THR B 1 305 ? 103.502 145.671 131.300 1.00 29.26 ?  305 THR B C     1 
ATOM   8004  O  O     . THR B 1 305 ? 102.750 146.619 131.041 1.00 34.96 ?  305 THR B O     1 
ATOM   8005  C  CB    . THR B 1 305 ? 103.314 143.522 130.020 1.00 30.45 ?  305 THR B CB    1 
ATOM   8006  O  OG1   . THR B 1 305 ? 103.333 142.793 131.252 1.00 28.12 ?  305 THR B OG1   1 
ATOM   8007  C  CG2   . THR B 1 305 ? 103.928 142.669 128.925 1.00 31.29 ?  305 THR B CG2   1 
ATOM   8008  N  N     . ILE B 1 306 ? 103.839 145.349 132.550 1.00 29.89 ?  306 ILE B N     1 
ATOM   8009  C  CA    . ILE B 1 306 ? 103.360 146.135 133.682 1.00 30.13 ?  306 ILE B CA    1 
ATOM   8010  C  C     . ILE B 1 306 ? 103.912 147.552 133.619 1.00 29.22 ?  306 ILE B C     1 
ATOM   8011  O  O     . ILE B 1 306 ? 103.196 148.525 133.885 1.00 34.03 ?  306 ILE B O     1 
ATOM   8012  C  CB    . ILE B 1 306 ? 103.730 145.436 135.003 1.00 26.76 ?  306 ILE B CB    1 
ATOM   8013  C  CG1   . ILE B 1 306 ? 102.887 144.177 135.189 1.00 26.49 ?  306 ILE B CG1   1 
ATOM   8014  C  CG2   . ILE B 1 306 ? 103.551 146.374 136.177 1.00 29.75 ?  306 ILE B CG2   1 
ATOM   8015  C  CD1   . ILE B 1 306 ? 103.232 143.400 136.425 1.00 28.94 ?  306 ILE B CD1   1 
ATOM   8016  N  N     . TYR B 1 307 ? 105.192 147.693 133.269 1.00 30.63 ?  307 TYR B N     1 
ATOM   8017  C  CA    . TYR B 1 307 ? 105.784 149.021 133.160 1.00 27.67 ?  307 TYR B CA    1 
ATOM   8018  C  C     . TYR B 1 307 ? 105.129 149.827 132.046 1.00 31.63 ?  307 TYR B C     1 
ATOM   8019  O  O     . TYR B 1 307 ? 104.897 151.031 132.196 1.00 35.31 ?  307 TYR B O     1 
ATOM   8020  C  CB    . TYR B 1 307 ? 107.294 148.904 132.941 1.00 24.46 ?  307 TYR B CB    1 
ATOM   8021  C  CG    . TYR B 1 307 ? 108.015 150.231 132.833 1.00 31.21 ?  307 TYR B CG    1 
ATOM   8022  C  CD1   . TYR B 1 307 ? 108.063 150.929 131.631 1.00 31.54 ?  307 TYR B CD1   1 
ATOM   8023  C  CD2   . TYR B 1 307 ? 108.636 150.793 133.940 1.00 26.86 ?  307 TYR B CD2   1 
ATOM   8024  C  CE1   . TYR B 1 307 ? 108.714 152.139 131.536 1.00 31.01 ?  307 TYR B CE1   1 
ATOM   8025  C  CE2   . TYR B 1 307 ? 109.288 152.003 133.854 1.00 29.82 ?  307 TYR B CE2   1 
ATOM   8026  C  CZ    . TYR B 1 307 ? 109.325 152.672 132.650 1.00 34.47 ?  307 TYR B CZ    1 
ATOM   8027  O  OH    . TYR B 1 307 ? 109.977 153.880 132.558 1.00 36.60 ?  307 TYR B OH    1 
ATOM   8028  N  N     . LYS B 1 308 ? 104.836 149.183 130.915 1.00 34.42 ?  308 LYS B N     1 
ATOM   8029  C  CA    . LYS B 1 308 ? 104.159 149.869 129.821 1.00 31.88 ?  308 LYS B CA    1 
ATOM   8030  C  C     . LYS B 1 308 ? 102.763 150.315 130.230 1.00 31.61 ?  308 LYS B C     1 
ATOM   8031  O  O     . LYS B 1 308 ? 102.343 151.436 129.915 1.00 36.40 ?  308 LYS B O     1 
ATOM   8032  C  CB    . LYS B 1 308 ? 104.088 148.955 128.597 1.00 32.36 ?  308 LYS B CB    1 
ATOM   8033  C  CG    . LYS B 1 308 ? 105.351 148.941 127.752 1.00 33.85 ?  308 LYS B CG    1 
ATOM   8034  C  CD    . LYS B 1 308 ? 105.547 147.608 127.036 1.00 35.89 ?  308 LYS B CD    1 
ATOM   8035  C  CE    . LYS B 1 308 ? 104.273 146.774 127.002 1.00 36.98 ?  308 LYS B CE    1 
ATOM   8036  N  NZ    . LYS B 1 308 ? 104.253 145.836 125.847 1.00 35.60 1  308 LYS B NZ    1 
ATOM   8037  N  N     . GLU B 1 309 ? 102.027 149.454 130.936 1.00 29.97 ?  309 GLU B N     1 
ATOM   8038  C  CA    . GLU B 1 309 ? 100.646 149.776 131.277 1.00 34.83 ?  309 GLU B CA    1 
ATOM   8039  C  C     . GLU B 1 309 ? 100.561 150.841 132.364 1.00 35.03 ?  309 GLU B C     1 
ATOM   8040  O  O     . GLU B 1 309 ? 99.743  151.763 132.272 1.00 37.16 ?  309 GLU B O     1 
ATOM   8041  C  CB    . GLU B 1 309 ? 99.906  148.512 131.710 1.00 32.85 ?  309 GLU B CB    1 
ATOM   8042  C  CG    . GLU B 1 309 ? 98.564  148.781 132.365 1.00 35.09 ?  309 GLU B CG    1 
ATOM   8043  C  CD    . GLU B 1 309 ? 97.538  149.349 131.404 1.00 40.22 ?  309 GLU B CD    1 
ATOM   8044  O  OE1   . GLU B 1 309 ? 97.727  149.219 130.177 1.00 40.62 ?  309 GLU B OE1   1 
ATOM   8045  O  OE2   . GLU B 1 309 ? 96.540  149.929 131.880 1.00 39.65 -1 309 GLU B OE2   1 
ATOM   8046  N  N     . TYR B 1 310 ? 101.395 150.738 133.399 1.00 33.44 ?  310 TYR B N     1 
ATOM   8047  C  CA    . TYR B 1 310 ? 101.268 151.590 134.572 1.00 33.04 ?  310 TYR B CA    1 
ATOM   8048  C  C     . TYR B 1 310 ? 102.336 152.668 134.673 1.00 31.90 ?  310 TYR B C     1 
ATOM   8049  O  O     . TYR B 1 310 ? 102.162 153.611 135.453 1.00 31.87 ?  310 TYR B O     1 
ATOM   8050  C  CB    . TYR B 1 310 ? 101.294 150.735 135.847 1.00 31.08 ?  310 TYR B CB    1 
ATOM   8051  C  CG    . TYR B 1 310 ? 100.185 149.711 135.915 1.00 32.59 ?  310 TYR B CG    1 
ATOM   8052  C  CD1   . TYR B 1 310 ? 98.931  150.048 136.407 1.00 31.36 ?  310 TYR B CD1   1 
ATOM   8053  C  CD2   . TYR B 1 310 ? 100.389 148.408 135.480 1.00 32.26 ?  310 TYR B CD2   1 
ATOM   8054  C  CE1   . TYR B 1 310 ? 97.914  149.116 136.469 1.00 33.04 ?  310 TYR B CE1   1 
ATOM   8055  C  CE2   . TYR B 1 310 ? 99.377  147.470 135.536 1.00 32.17 ?  310 TYR B CE2   1 
ATOM   8056  C  CZ    . TYR B 1 310 ? 98.143  147.829 136.033 1.00 33.62 ?  310 TYR B CZ    1 
ATOM   8057  O  OH    . TYR B 1 310 ? 97.133  146.898 136.092 1.00 34.39 ?  310 TYR B OH    1 
ATOM   8058  N  N     . GLY B 1 311 ? 103.423 152.565 133.916 1.00 29.63 ?  311 GLY B N     1 
ATOM   8059  C  CA    . GLY B 1 311 ? 104.504 153.521 134.014 1.00 29.67 ?  311 GLY B CA    1 
ATOM   8060  C  C     . GLY B 1 311 ? 105.474 153.274 135.146 1.00 34.53 ?  311 GLY B C     1 
ATOM   8061  O  O     . GLY B 1 311 ? 106.434 154.039 135.294 1.00 36.90 ?  311 GLY B O     1 
ATOM   8062  N  N     . GLN B 1 312 ? 105.257 152.234 135.947 1.00 31.52 ?  312 GLN B N     1 
ATOM   8063  C  CA    . GLN B 1 312 ? 106.135 151.894 137.054 1.00 29.78 ?  312 GLN B CA    1 
ATOM   8064  C  C     . GLN B 1 312 ? 106.512 150.423 136.965 1.00 32.31 ?  312 GLN B C     1 
ATOM   8065  O  O     . GLN B 1 312 ? 105.799 149.612 136.368 1.00 39.23 ?  312 GLN B O     1 
ATOM   8066  C  CB    . GLN B 1 312 ? 105.481 152.183 138.413 1.00 32.47 ?  312 GLN B CB    1 
ATOM   8067  C  CG    . GLN B 1 312 ? 104.416 153.265 138.381 1.00 31.94 ?  312 GLN B CG    1 
ATOM   8068  C  CD    . GLN B 1 312 ? 103.512 153.226 139.596 1.00 35.90 ?  312 GLN B CD    1 
ATOM   8069  O  OE1   . GLN B 1 312 ? 103.932 153.548 140.707 1.00 38.51 ?  312 GLN B OE1   1 
ATOM   8070  N  NE2   . GLN B 1 312 ? 102.262 152.829 139.391 1.00 33.65 ?  312 GLN B NE2   1 
ATOM   8071  N  N     . HIS B 1 313 ? 107.646 150.088 137.570 1.00 29.23 ?  313 HIS B N     1 
ATOM   8072  C  CA    . HIS B 1 313 ? 108.110 148.711 137.580 1.00 29.45 ?  313 HIS B CA    1 
ATOM   8073  C  C     . HIS B 1 313 ? 107.250 147.862 138.513 1.00 32.07 ?  313 HIS B C     1 
ATOM   8074  O  O     . HIS B 1 313 ? 106.595 148.365 139.431 1.00 32.39 ?  313 HIS B O     1 
ATOM   8075  C  CB    . HIS B 1 313 ? 109.577 148.646 138.001 1.00 26.13 ?  313 HIS B CB    1 
ATOM   8076  C  CG    . HIS B 1 313 ? 110.491 149.432 137.113 1.00 27.87 ?  313 HIS B CG    1 
ATOM   8077  N  ND1   . HIS B 1 313 ? 110.967 148.941 135.916 1.00 30.95 ?  313 HIS B ND1   1 
ATOM   8078  C  CD2   . HIS B 1 313 ? 111.014 150.673 137.244 1.00 29.49 ?  313 HIS B CD2   1 
ATOM   8079  C  CE1   . HIS B 1 313 ? 111.745 149.845 135.350 1.00 28.56 ?  313 HIS B CE1   1 
ATOM   8080  N  NE2   . HIS B 1 313 ? 111.789 150.906 136.135 1.00 30.09 ?  313 HIS B NE2   1 
ATOM   8081  N  N     . MET B 1 314 ? 107.254 146.551 138.259 1.00 35.31 ?  314 MET B N     1 
ATOM   8082  C  CA    . MET B 1 314 ? 106.437 145.639 139.054 1.00 30.43 ?  314 MET B CA    1 
ATOM   8083  C  C     . MET B 1 314 ? 106.870 145.637 140.515 1.00 37.07 ?  314 MET B C     1 
ATOM   8084  O  O     . MET B 1 314 ? 106.027 145.606 141.419 1.00 39.69 ?  314 MET B O     1 
ATOM   8085  C  CB    . MET B 1 314 ? 106.504 144.228 138.473 1.00 28.98 ?  314 MET B CB    1 
ATOM   8086  C  CG    . MET B 1 314 ? 105.580 143.243 139.168 1.00 29.54 ?  314 MET B CG    1 
ATOM   8087  S  SD    . MET B 1 314 ? 106.132 141.530 139.099 1.00 45.32 ?  314 MET B SD    1 
ATOM   8088  C  CE    . MET B 1 314 ? 107.233 141.578 137.692 1.00 30.08 ?  314 MET B CE    1 
ATOM   8089  N  N     . ASP B 1 315 ? 108.176 145.667 140.767 1.00 30.29 ?  315 ASP B N     1 
ATOM   8090  C  CA    . ASP B 1 315 ? 108.687 145.699 142.131 1.00 34.42 ?  315 ASP B CA    1 
ATOM   8091  C  C     . ASP B 1 315 ? 108.698 147.101 142.725 1.00 30.20 ?  315 ASP B C     1 
ATOM   8092  O  O     . ASP B 1 315 ? 109.088 147.261 143.886 1.00 36.93 ?  315 ASP B O     1 
ATOM   8093  C  CB    . ASP B 1 315 ? 110.096 145.103 142.181 1.00 33.18 ?  315 ASP B CB    1 
ATOM   8094  C  CG    . ASP B 1 315 ? 111.100 145.914 141.391 1.00 32.79 ?  315 ASP B CG    1 
ATOM   8095  O  OD1   . ASP B 1 315 ? 110.687 146.590 140.425 1.00 36.65 ?  315 ASP B OD1   1 
ATOM   8096  O  OD2   . ASP B 1 315 ? 112.298 145.878 141.735 1.00 29.78 -1 315 ASP B OD2   1 
ATOM   8097  N  N     . GLU B 1 316 ? 108.284 148.113 141.962 1.00 28.38 ?  316 GLU B N     1 
ATOM   8098  C  CA    . GLU B 1 316 ? 108.224 149.479 142.460 1.00 29.96 ?  316 GLU B CA    1 
ATOM   8099  C  C     . GLU B 1 316 ? 106.942 149.779 143.226 1.00 35.54 ?  316 GLU B C     1 
ATOM   8100  O  O     . GLU B 1 316 ? 106.857 150.834 143.862 1.00 39.07 ?  316 GLU B O     1 
ATOM   8101  C  CB    . GLU B 1 316 ? 108.357 150.467 141.298 1.00 36.44 ?  316 GLU B CB    1 
ATOM   8102  C  CG    . GLU B 1 316 ? 109.774 150.951 141.034 1.00 34.69 ?  316 GLU B CG    1 
ATOM   8103  C  CD    . GLU B 1 316 ? 110.578 151.147 142.302 1.00 36.36 ?  316 GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 1 316 ? 110.143 151.929 143.173 1.00 38.09 ?  316 GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 1 316 ? 111.651 150.522 142.424 1.00 41.39 -1 316 GLU B OE2   1 
ATOM   8106  N  N     . MET B 1 317 ? 105.953 148.892 143.182 1.00 38.06 ?  317 MET B N     1 
ATOM   8107  C  CA    . MET B 1 317 ? 104.678 149.112 143.845 1.00 38.40 ?  317 MET B CA    1 
ATOM   8108  C  C     . MET B 1 317 ? 104.286 147.878 144.646 1.00 37.91 ?  317 MET B C     1 
ATOM   8109  O  O     . MET B 1 317 ? 104.898 146.814 144.541 1.00 37.39 ?  317 MET B O     1 
ATOM   8110  C  CB    . MET B 1 317 ? 103.576 149.475 142.840 1.00 40.05 ?  317 MET B CB    1 
ATOM   8111  C  CG    . MET B 1 317 ? 103.701 148.794 141.492 1.00 34.68 ?  317 MET B CG    1 
ATOM   8112  S  SD    . MET B 1 317 ? 103.021 149.829 140.182 1.00 48.10 ?  317 MET B SD    1 
ATOM   8113  C  CE    . MET B 1 317 ? 103.338 148.814 138.746 1.00 33.99 ?  317 MET B CE    1 
ATOM   8114  N  N     . ASP B 1 318 ? 103.239 148.042 145.454 1.00 40.30 ?  318 ASP B N     1 
ATOM   8115  C  CA    . ASP B 1 318 ? 102.808 147.017 146.399 1.00 38.45 ?  318 ASP B CA    1 
ATOM   8116  C  C     . ASP B 1 318 ? 102.035 145.935 145.658 1.00 38.44 ?  318 ASP B C     1 
ATOM   8117  O  O     . ASP B 1 318 ? 100.987 146.205 145.062 1.00 41.14 ?  318 ASP B O     1 
ATOM   8118  C  CB    . ASP B 1 318 ? 101.957 147.646 147.499 1.00 37.95 ?  318 ASP B CB    1 
ATOM   8119  C  CG    . ASP B 1 318 ? 101.491 146.636 148.527 1.00 46.03 ?  318 ASP B CG    1 
ATOM   8120  O  OD1   . ASP B 1 318 ? 102.332 146.151 149.314 1.00 42.17 ?  318 ASP B OD1   1 
ATOM   8121  O  OD2   . ASP B 1 318 ? 100.282 146.330 148.549 1.00 44.77 -1 318 ASP B OD2   1 
ATOM   8122  N  N     . MET B 1 319 ? 102.552 144.704 145.691 1.00 39.69 ?  319 MET B N     1 
ATOM   8123  C  CA    . MET B 1 319 ? 101.849 143.590 145.066 1.00 35.15 ?  319 MET B CA    1 
ATOM   8124  C  C     . MET B 1 319 ? 100.592 143.209 145.838 1.00 36.04 ?  319 MET B C     1 
ATOM   8125  O  O     . MET B 1 319 ? 99.631  142.719 145.240 1.00 38.25 ?  319 MET B O     1 
ATOM   8126  C  CB    . MET B 1 319 ? 102.776 142.380 144.939 1.00 36.87 ?  319 MET B CB    1 
ATOM   8127  C  CG    . MET B 1 319 ? 102.256 141.294 144.006 1.00 37.09 ?  319 MET B CG    1 
ATOM   8128  S  SD    . MET B 1 319 ? 102.619 141.546 142.255 1.00 44.18 ?  319 MET B SD    1 
ATOM   8129  C  CE    . MET B 1 319 ? 103.939 142.752 142.329 1.00 38.47 ?  319 MET B CE    1 
ATOM   8130  N  N     . ASN B 1 320 ? 100.575 143.435 147.153 1.00 38.47 ?  320 ASN B N     1 
ATOM   8131  C  CA    . ASN B 1 320 ? 99.413  143.060 147.953 1.00 38.98 ?  320 ASN B CA    1 
ATOM   8132  C  C     . ASN B 1 320 ? 98.165  143.819 147.526 1.00 40.89 ?  320 ASN B C     1 
ATOM   8133  O  O     . ASN B 1 320 ? 97.045  143.333 147.721 1.00 41.47 ?  320 ASN B O     1 
ATOM   8134  C  CB    . ASN B 1 320 ? 99.698  143.297 149.435 1.00 37.46 ?  320 ASN B CB    1 
ATOM   8135  C  CG    . ASN B 1 320 ? 100.811 142.417 149.959 1.00 42.30 ?  320 ASN B CG    1 
ATOM   8136  O  OD1   . ASN B 1 320 ? 101.928 142.431 149.440 1.00 37.80 ?  320 ASN B OD1   1 
ATOM   8137  N  ND2   . ASN B 1 320 ? 100.512 141.641 150.993 1.00 41.25 ?  320 ASN B ND2   1 
ATOM   8138  N  N     . GLU B 1 321 ? 98.332  145.005 146.944 1.00 42.19 ?  321 GLU B N     1 
ATOM   8139  C  CA    . GLU B 1 321 ? 97.210  145.808 146.483 1.00 40.34 ?  321 GLU B CA    1 
ATOM   8140  C  C     . GLU B 1 321 ? 97.083  145.864 144.968 1.00 40.01 ?  321 GLU B C     1 
ATOM   8141  O  O     . GLU B 1 321 ? 96.032  146.285 144.470 1.00 46.31 ?  321 GLU B O     1 
ATOM   8142  C  CB    . GLU B 1 321 ? 97.323  147.239 147.032 1.00 42.72 ?  321 GLU B CB    1 
ATOM   8143  C  CG    . GLU B 1 321 ? 98.070  148.197 146.118 1.00 39.85 ?  321 GLU B CG    1 
ATOM   8144  C  CD    . GLU B 1 321 ? 98.763  149.308 146.879 1.00 45.15 ?  321 GLU B CD    1 
ATOM   8145  O  OE1   . GLU B 1 321 ? 98.758  149.269 148.127 1.00 45.47 ?  321 GLU B OE1   1 
ATOM   8146  O  OE2   . GLU B 1 321 ? 99.320  150.218 146.229 1.00 45.61 -1 321 GLU B OE2   1 
ATOM   8147  N  N     . MET B 1 322 ? 98.106  145.450 144.222 1.00 34.71 ?  322 MET B N     1 
ATOM   8148  C  CA    . MET B 1 322 ? 98.095  145.566 142.772 1.00 32.82 ?  322 MET B CA    1 
ATOM   8149  C  C     . MET B 1 322 ? 98.092  144.218 142.063 1.00 33.10 ?  322 MET B C     1 
ATOM   8150  O  O     . MET B 1 322 ? 98.048  144.187 140.830 1.00 39.54 ?  322 MET B O     1 
ATOM   8151  C  CB    . MET B 1 322 ? 99.300  146.388 142.299 1.00 33.39 ?  322 MET B CB    1 
ATOM   8152  C  CG    . MET B 1 322 ? 99.168  147.889 142.536 1.00 35.60 ?  322 MET B CG    1 
ATOM   8153  S  SD    . MET B 1 322 ? 98.251  148.818 141.291 1.00 45.22 ?  322 MET B SD    1 
ATOM   8154  C  CE    . MET B 1 322 ? 98.426  147.772 139.854 1.00 36.56 ?  322 MET B CE    1 
ATOM   8155  N  N     . TYR B 1 323 ? 98.146  143.106 142.803 1.00 32.48 ?  323 TYR B N     1 
ATOM   8156  C  CA    . TYR B 1 323 ? 98.173  141.789 142.172 1.00 28.69 ?  323 TYR B CA    1 
ATOM   8157  C  C     . TYR B 1 323 ? 96.877  141.504 141.424 1.00 29.49 ?  323 TYR B C     1 
ATOM   8158  O  O     . TYR B 1 323 ? 96.902  140.988 140.300 1.00 33.38 ?  323 TYR B O     1 
ATOM   8159  C  CB    . TYR B 1 323 ? 98.434  140.711 143.226 1.00 32.87 ?  323 TYR B CB    1 
ATOM   8160  C  CG    . TYR B 1 323 ? 98.365  139.298 142.692 1.00 30.91 ?  323 TYR B CG    1 
ATOM   8161  C  CD1   . TYR B 1 323 ? 99.473  138.702 142.109 1.00 27.40 ?  323 TYR B CD1   1 
ATOM   8162  C  CD2   . TYR B 1 323 ? 97.193  138.558 142.778 1.00 30.40 ?  323 TYR B CD2   1 
ATOM   8163  C  CE1   . TYR B 1 323 ? 99.413  137.413 141.620 1.00 29.80 ?  323 TYR B CE1   1 
ATOM   8164  C  CE2   . TYR B 1 323 ? 97.124  137.271 142.292 1.00 25.97 ?  323 TYR B CE2   1 
ATOM   8165  C  CZ    . TYR B 1 323 ? 98.237  136.703 141.715 1.00 31.28 ?  323 TYR B CZ    1 
ATOM   8166  O  OH    . TYR B 1 323 ? 98.174  135.420 141.229 1.00 30.96 ?  323 TYR B OH    1 
ATOM   8167  N  N     . ASP B 1 324 ? 95.736  141.823 142.035 1.00 36.10 ?  324 ASP B N     1 
ATOM   8168  C  CA    . ASP B 1 324 ? 94.458  141.601 141.371 1.00 34.38 ?  324 ASP B CA    1 
ATOM   8169  C  C     . ASP B 1 324 ? 94.317  142.484 140.137 1.00 38.34 ?  324 ASP B C     1 
ATOM   8170  O  O     . ASP B 1 324 ? 93.765  142.053 139.118 1.00 41.12 ?  324 ASP B O     1 
ATOM   8171  C  CB    . ASP B 1 324 ? 93.311  141.845 142.349 1.00 38.72 ?  324 ASP B CB    1 
ATOM   8172  C  CG    . ASP B 1 324 ? 93.071  140.662 143.267 1.00 40.69 ?  324 ASP B CG    1 
ATOM   8173  O  OD1   . ASP B 1 324 ? 93.418  139.529 142.876 1.00 40.70 ?  324 ASP B OD1   1 
ATOM   8174  O  OD2   . ASP B 1 324 ? 92.538  140.867 144.378 1.00 42.71 -1 324 ASP B OD2   1 
ATOM   8175  N  N     . LYS B 1 325 ? 94.807  143.723 140.212 1.00 33.53 ?  325 LYS B N     1 
ATOM   8176  C  CA    . LYS B 1 325 ? 94.781  144.600 139.046 1.00 31.34 ?  325 LYS B CA    1 
ATOM   8177  C  C     . LYS B 1 325 ? 95.676  144.067 137.933 1.00 32.90 ?  325 LYS B C     1 
ATOM   8178  O  O     . LYS B 1 325 ? 95.316  144.142 136.753 1.00 40.84 ?  325 LYS B O     1 
ATOM   8179  C  CB    . LYS B 1 325 ? 95.195  146.014 139.446 1.00 36.26 ?  325 LYS B CB    1 
ATOM   8180  C  CG    . LYS B 1 325 ? 94.229  146.675 140.413 1.00 34.78 ?  325 LYS B CG    1 
ATOM   8181  C  CD    . LYS B 1 325 ? 94.838  147.911 141.044 1.00 34.18 ?  325 LYS B CD    1 
ATOM   8182  C  CE    . LYS B 1 325 ? 93.763  148.860 141.542 1.00 36.84 ?  325 LYS B CE    1 
ATOM   8183  N  NZ    . LYS B 1 325 ? 92.450  148.176 141.696 1.00 36.00 1  325 LYS B NZ    1 
ATOM   8184  N  N     . PHE B 1 326 ? 96.845  143.529 138.288 1.00 35.11 ?  326 PHE B N     1 
ATOM   8185  C  CA    . PHE B 1 326 ? 97.701  142.883 137.297 1.00 33.24 ?  326 PHE B CA    1 
ATOM   8186  C  C     . PHE B 1 326 ? 96.996  141.702 136.643 1.00 29.94 ?  326 PHE B C     1 
ATOM   8187  O  O     . PHE B 1 326 ? 97.071  141.521 135.421 1.00 36.57 ?  326 PHE B O     1 
ATOM   8188  C  CB    . PHE B 1 326 ? 99.004  142.413 137.946 1.00 30.23 ?  326 PHE B CB    1 
ATOM   8189  C  CG    . PHE B 1 326 ? 99.922  143.523 138.363 1.00 30.01 ?  326 PHE B CG    1 
ATOM   8190  C  CD1   . PHE B 1 326 ? 99.799  144.790 137.824 1.00 33.25 ?  326 PHE B CD1   1 
ATOM   8191  C  CD2   . PHE B 1 326 ? 100.913 143.293 139.303 1.00 33.29 ?  326 PHE B CD2   1 
ATOM   8192  C  CE1   . PHE B 1 326 ? 100.653 145.804 138.209 1.00 30.86 ?  326 PHE B CE1   1 
ATOM   8193  C  CE2   . PHE B 1 326 ? 101.765 144.305 139.693 1.00 33.97 ?  326 PHE B CE2   1 
ATOM   8194  C  CZ    . PHE B 1 326 ? 101.634 145.562 139.147 1.00 35.34 ?  326 PHE B CZ    1 
ATOM   8195  N  N     . VAL B 1 327 ? 96.315  140.880 137.443 1.00 31.40 ?  327 VAL B N     1 
ATOM   8196  C  CA    . VAL B 1 327 ? 95.685  139.676 136.909 1.00 34.99 ?  327 VAL B CA    1 
ATOM   8197  C  C     . VAL B 1 327 ? 94.509  140.034 136.007 1.00 36.86 ?  327 VAL B C     1 
ATOM   8198  O  O     . VAL B 1 327 ? 94.334  139.450 134.931 1.00 41.34 ?  327 VAL B O     1 
ATOM   8199  C  CB    . VAL B 1 327 ? 95.260  138.745 138.059 1.00 32.98 ?  327 VAL B CB    1 
ATOM   8200  C  CG1   . VAL B 1 327 ? 94.339  137.648 137.549 1.00 35.22 ?  327 VAL B CG1   1 
ATOM   8201  C  CG2   . VAL B 1 327 ? 96.484  138.144 138.730 1.00 29.82 ?  327 VAL B CG2   1 
ATOM   8202  N  N     . ASP B 1 328 ? 93.693  141.003 136.419 1.00 36.62 ?  328 ASP B N     1 
ATOM   8203  C  CA    . ASP B 1 328 ? 92.511  141.382 135.655 1.00 36.77 ?  328 ASP B CA    1 
ATOM   8204  C  C     . ASP B 1 328 ? 92.825  142.289 134.472 1.00 40.53 ?  328 ASP B C     1 
ATOM   8205  O  O     . ASP B 1 328 ? 91.924  142.573 133.678 1.00 43.97 ?  328 ASP B O     1 
ATOM   8206  C  CB    . ASP B 1 328 ? 91.497  142.071 136.570 1.00 38.73 ?  328 ASP B CB    1 
ATOM   8207  C  CG    . ASP B 1 328 ? 91.059  141.188 137.721 1.00 45.21 ?  328 ASP B CG    1 
ATOM   8208  O  OD1   . ASP B 1 328 ? 90.468  141.717 138.686 1.00 46.00 ?  328 ASP B OD1   1 
ATOM   8209  O  OD2   . ASP B 1 328 ? 91.307  139.965 137.661 1.00 44.15 -1 328 ASP B OD2   1 
ATOM   8210  N  N     . ASN B 1 329 ? 94.068  142.744 134.336 1.00 36.19 ?  329 ASN B N     1 
ATOM   8211  C  CA    . ASN B 1 329 ? 94.437  143.645 133.253 1.00 35.52 ?  329 ASN B CA    1 
ATOM   8212  C  C     . ASN B 1 329 ? 94.831  142.826 132.030 1.00 39.38 ?  329 ASN B C     1 
ATOM   8213  O  O     . ASN B 1 329 ? 95.825  142.089 132.089 1.00 39.32 ?  329 ASN B O     1 
ATOM   8214  C  CB    . ASN B 1 329 ? 95.590  144.540 133.680 1.00 35.64 ?  329 ASN B CB    1 
ATOM   8215  C  CG    . ASN B 1 329 ? 95.748  145.770 132.805 1.00 39.66 ?  329 ASN B CG    1 
ATOM   8216  O  OD1   . ASN B 1 329 ? 96.344  146.758 133.225 1.00 37.91 ?  329 ASN B OD1   1 
ATOM   8217  N  ND2   . ASN B 1 329 ? 95.216  145.721 131.593 1.00 42.21 ?  329 ASN B ND2   1 
ATOM   8218  N  N     . PRO B 1 330 ? 94.094  142.914 130.918 1.00 43.55 ?  330 PRO B N     1 
ATOM   8219  C  CA    . PRO B 1 330 ? 94.493  142.152 129.724 1.00 40.99 ?  330 PRO B CA    1 
ATOM   8220  C  C     . PRO B 1 330 ? 95.783  142.647 129.095 1.00 37.31 ?  330 PRO B C     1 
ATOM   8221  O  O     . PRO B 1 330 ? 96.460  141.869 128.411 1.00 39.57 ?  330 PRO B O     1 
ATOM   8222  C  CB    . PRO B 1 330 ? 93.297  142.331 128.781 1.00 41.98 ?  330 PRO B CB    1 
ATOM   8223  C  CG    . PRO B 1 330 ? 92.670  143.613 129.212 1.00 37.44 ?  330 PRO B CG    1 
ATOM   8224  C  CD    . PRO B 1 330 ? 92.854  143.678 130.701 1.00 40.19 ?  330 PRO B CD    1 
ATOM   8225  N  N     . ARG B 1 331 ? 96.149  143.912 129.301 1.00 38.79 ?  331 ARG B N     1 
ATOM   8226  C  CA    . ARG B 1 331 ? 97.381  144.449 128.739 1.00 42.17 ?  331 ARG B CA    1 
ATOM   8227  C  C     . ARG B 1 331 ? 98.617  144.036 129.525 1.00 40.20 ?  331 ARG B C     1 
ATOM   8228  O  O     . ARG B 1 331 ? 99.735  144.337 129.094 1.00 38.14 ?  331 ARG B O     1 
ATOM   8229  C  CB    . ARG B 1 331 ? 97.302  145.975 128.657 1.00 39.65 ?  331 ARG B CB    1 
ATOM   8230  C  CG    . ARG B 1 331 ? 96.337  146.479 127.596 1.00 38.38 ?  331 ARG B CG    1 
ATOM   8231  C  CD    . ARG B 1 331 ? 95.938  147.928 127.837 1.00 40.13 ?  331 ARG B CD    1 
ATOM   8232  N  NE    . ARG B 1 331 ? 95.232  148.112 129.101 1.00 42.43 ?  331 ARG B NE    1 
ATOM   8233  C  CZ    . ARG B 1 331 ? 93.999  147.690 129.345 1.00 42.33 ?  331 ARG B CZ    1 
ATOM   8234  N  NH1   . ARG B 1 331 ? 93.292  147.047 128.429 1.00 41.73 1  331 ARG B NH1   1 
ATOM   8235  N  NH2   . ARG B 1 331 ? 93.458  147.925 130.537 1.00 40.55 ?  331 ARG B NH2   1 
ATOM   8236  N  N     . VAL B 1 332 ? 98.444  143.365 130.659 1.00 38.10 ?  332 VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? 99.548  142.815 131.435 1.00 33.72 ?  332 VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? 99.672  141.337 131.098 1.00 34.64 ?  332 VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? 98.679  140.600 131.136 1.00 37.29 ?  332 VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? 99.327  143.023 132.943 1.00 33.18 ?  332 VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? 100.269 142.143 133.749 1.00 33.55 ?  332 VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? 99.510  144.488 133.308 1.00 33.28 ?  332 VAL B CG2   1 
ATOM   8243  N  N     . LYS B 1 333 ? 100.879 140.906 130.748 1.00 31.25 ?  333 LYS B N     1 
ATOM   8244  C  CA    . LYS B 1 333 ? 101.133 139.512 130.421 1.00 31.37 ?  333 LYS B CA    1 
ATOM   8245  C  C     . LYS B 1 333 ? 101.550 138.753 131.674 1.00 33.26 ?  333 LYS B C     1 
ATOM   8246  O  O     . LYS B 1 333 ? 102.348 139.247 132.476 1.00 34.81 ?  333 LYS B O     1 
ATOM   8247  C  CB    . LYS B 1 333 ? 102.217 139.397 129.348 1.00 26.23 ?  333 LYS B CB    1 
ATOM   8248  C  CG    . LYS B 1 333 ? 102.216 138.077 128.598 1.00 32.17 ?  333 LYS B CG    1 
ATOM   8249  C  CD    . LYS B 1 333 ? 103.377 137.999 127.622 1.00 34.40 ?  333 LYS B CD    1 
ATOM   8250  C  CE    . LYS B 1 333 ? 103.484 136.617 126.999 1.00 35.85 ?  333 LYS B CE    1 
ATOM   8251  N  NZ    . LYS B 1 333 ? 104.620 136.528 126.042 1.00 37.67 1  333 LYS B NZ    1 
ATOM   8252  N  N     . LYS B 1 334 ? 101.005 137.549 131.838 1.00 32.05 ?  334 LYS B N     1 
ATOM   8253  C  CA    . LYS B 1 334 ? 101.274 136.760 133.030 1.00 29.36 ?  334 LYS B CA    1 
ATOM   8254  C  C     . LYS B 1 334 ? 101.211 135.279 132.693 1.00 33.55 ?  334 LYS B C     1 
ATOM   8255  O  O     . LYS B 1 334 ? 100.634 134.871 131.682 1.00 35.10 ?  334 LYS B O     1 
ATOM   8256  C  CB    . LYS B 1 334 ? 100.285 137.085 134.156 1.00 31.14 ?  334 LYS B CB    1 
ATOM   8257  C  CG    . LYS B 1 334 ? 98.869  136.609 133.894 1.00 35.88 ?  334 LYS B CG    1 
ATOM   8258  C  CD    . LYS B 1 334 ? 97.845  137.611 134.390 1.00 32.50 ?  334 LYS B CD    1 
ATOM   8259  C  CE    . LYS B 1 334 ? 97.650  138.730 133.388 1.00 33.97 ?  334 LYS B CE    1 
ATOM   8260  N  NZ    . LYS B 1 334 ? 96.292  139.328 133.472 1.00 34.33 1  334 LYS B NZ    1 
ATOM   8261  N  N     . GLU B 1 335 ? 101.820 134.478 133.563 1.00 33.86 ?  335 GLU B N     1 
ATOM   8262  C  CA    . GLU B 1 335 ? 101.835 133.027 133.449 1.00 33.23 ?  335 GLU B CA    1 
ATOM   8263  C  C     . GLU B 1 335 ? 101.308 132.414 134.737 1.00 34.05 ?  335 GLU B C     1 
ATOM   8264  O  O     . GLU B 1 335 ? 101.591 132.908 135.832 1.00 40.53 ?  335 GLU B O     1 
ATOM   8265  C  CB    . GLU B 1 335 ? 103.246 132.499 133.164 1.00 29.97 ?  335 GLU B CB    1 
ATOM   8266  C  CG    . GLU B 1 335 ? 104.025 133.313 132.151 1.00 37.48 ?  335 GLU B CG    1 
ATOM   8267  C  CD    . GLU B 1 335 ? 104.823 132.448 131.197 1.00 41.55 ?  335 GLU B CD    1 
ATOM   8268  O  OE1   . GLU B 1 335 ? 105.782 131.789 131.651 1.00 36.02 ?  335 GLU B OE1   1 
ATOM   8269  O  OE2   . GLU B 1 335 ? 104.491 132.428 129.993 1.00 36.24 -1 335 GLU B OE2   1 
ATOM   8270  N  N     . LYS B 1 336 ? 100.546 131.334 134.600 1.00 33.34 ?  336 LYS B N     1 
ATOM   8271  C  CA    . LYS B 1 336 ? 99.996  130.642 135.756 1.00 29.33 ?  336 LYS B CA    1 
ATOM   8272  C  C     . LYS B 1 336 ? 101.056 129.767 136.411 1.00 35.73 ?  336 LYS B C     1 
ATOM   8273  O  O     . LYS B 1 336 ? 101.807 129.061 135.734 1.00 37.25 ?  336 LYS B O     1 
ATOM   8274  C  CB    . LYS B 1 336 ? 98.797  129.786 135.345 1.00 37.44 ?  336 LYS B CB    1 
ATOM   8275  C  CG    . LYS B 1 336 ? 97.765  129.594 136.442 1.00 41.25 ?  336 LYS B CG    1 
ATOM   8276  C  CD    . LYS B 1 336 ? 96.614  128.725 135.968 1.00 38.03 ?  336 LYS B CD    1 
ATOM   8277  C  CE    . LYS B 1 336 ? 95.276  129.408 136.188 1.00 39.22 ?  336 LYS B CE    1 
ATOM   8278  N  NZ    . LYS B 1 336 ? 95.209  130.085 137.512 1.00 39.13 1  336 LYS B NZ    1 
ATOM   8279  N  N     . ILE B 1 337 ? 101.116 129.823 137.743 1.00 36.47 ?  337 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 337 ? 102.017 128.997 138.532 1.00 34.68 ?  337 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 337 ? 101.256 128.472 139.741 1.00 35.24 ?  337 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 337 ? 100.201 128.990 140.114 1.00 39.38 ?  337 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 337 ? 103.278 129.760 139.000 1.00 33.50 ?  337 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 337 ? 102.880 131.008 139.793 1.00 33.10 ?  337 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 337 ? 104.161 130.125 137.817 1.00 35.27 ?  337 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 337 ? 103.791 131.302 140.961 1.00 31.75 ?  337 ILE B CD1   1 
ATOM   8287  N  N     . ASN B 1 338 ? 101.804 127.426 140.352 1.00 35.06 ?  338 ASN B N     1 
ATOM   8288  C  CA    . ASN B 1 338 ? 101.283 126.930 141.614 1.00 34.44 ?  338 ASN B CA    1 
ATOM   8289  C  C     . ASN B 1 338 ? 102.156 127.470 142.734 1.00 34.15 ?  338 ASN B C     1 
ATOM   8290  O  O     . ASN B 1 338 ? 103.319 127.057 142.850 1.00 37.77 ?  338 ASN B O     1 
ATOM   8291  C  CB    . ASN B 1 338 ? 101.267 125.404 141.634 1.00 32.16 ?  338 ASN B CB    1 
ATOM   8292  C  CG    . ASN B 1 338 ? 100.360 124.843 142.714 1.00 35.79 ?  338 ASN B CG    1 
ATOM   8293  O  OD1   . ASN B 1 338 ? 100.308 123.632 142.929 1.00 38.49 ?  338 ASN B OD1   1 
ATOM   8294  N  ND2   . ASN B 1 338 ? 99.636  125.722 143.394 1.00 37.38 ?  338 ASN B ND2   1 
ATOM   8295  N  N     . PRO B 1 339 ? 101.662 128.395 143.562 1.00 33.80 ?  339 PRO B N     1 
ATOM   8296  C  CA    . PRO B 1 339 ? 102.515 128.953 144.624 1.00 28.56 ?  339 PRO B CA    1 
ATOM   8297  C  C     . PRO B 1 339 ? 103.018 127.914 145.608 1.00 32.53 ?  339 PRO B C     1 
ATOM   8298  O  O     . PRO B 1 339 ? 104.144 128.043 146.105 1.00 35.56 ?  339 PRO B O     1 
ATOM   8299  C  CB    . PRO B 1 339 ? 101.600 129.983 145.303 1.00 29.85 ?  339 PRO B CB    1 
ATOM   8300  C  CG    . PRO B 1 339 ? 100.215 129.580 144.929 1.00 33.77 ?  339 PRO B CG    1 
ATOM   8301  C  CD    . PRO B 1 339 ? 100.316 128.988 143.562 1.00 33.82 ?  339 PRO B CD    1 
ATOM   8302  N  N     . ARG B 1 340 ? 102.224 126.882 145.907 1.00 31.45 ?  340 ARG B N     1 
ATOM   8303  C  CA    . ARG B 1 340 ? 102.705 125.820 146.784 1.00 28.07 ?  340 ARG B CA    1 
ATOM   8304  C  C     . ARG B 1 340 ? 103.806 125.009 146.114 1.00 31.70 ?  340 ARG B C     1 
ATOM   8305  O  O     . ARG B 1 340 ? 104.781 124.620 146.766 1.00 34.63 ?  340 ARG B O     1 
ATOM   8306  C  CB    . ARG B 1 340 ? 101.546 124.920 147.206 1.00 31.53 ?  340 ARG B CB    1 
ATOM   8307  C  CG    . ARG B 1 340 ? 100.651 125.548 148.255 1.00 29.55 ?  340 ARG B CG    1 
ATOM   8308  C  CD    . ARG B 1 340 ? 99.897  124.508 149.060 1.00 28.13 ?  340 ARG B CD    1 
ATOM   8309  N  NE    . ARG B 1 340 ? 98.950  125.137 149.975 1.00 31.78 ?  340 ARG B NE    1 
ATOM   8310  C  CZ    . ARG B 1 340 ? 98.138  124.476 150.787 1.00 34.23 ?  340 ARG B CZ    1 
ATOM   8311  N  NH1   . ARG B 1 340 ? 98.130  123.154 150.832 1.00 34.73 1  340 ARG B NH1   1 
ATOM   8312  N  NH2   . ARG B 1 340 ? 97.311  125.159 151.573 1.00 34.57 ?  340 ARG B NH2   1 
ATOM   8313  N  N     . LYS B 1 341 ? 103.672 124.749 144.811 1.00 30.60 ?  341 LYS B N     1 
ATOM   8314  C  CA    . LYS B 1 341 ? 104.746 124.077 144.088 1.00 27.34 ?  341 LYS B CA    1 
ATOM   8315  C  C     . LYS B 1 341 ? 106.003 124.933 144.041 1.00 30.08 ?  341 LYS B C     1 
ATOM   8316  O  O     . LYS B 1 341 ? 107.114 124.405 144.132 1.00 29.73 ?  341 LYS B O     1 
ATOM   8317  C  CB    . LYS B 1 341 ? 104.295 123.719 142.671 1.00 35.91 ?  341 LYS B CB    1 
ATOM   8318  C  CG    . LYS B 1 341 ? 103.337 122.535 142.577 1.00 37.10 ?  341 LYS B CG    1 
ATOM   8319  C  CD    . LYS B 1 341 ? 103.371 121.658 143.819 1.00 34.20 ?  341 LYS B CD    1 
ATOM   8320  C  CE    . LYS B 1 341 ? 102.971 120.227 143.494 1.00 36.14 ?  341 LYS B CE    1 
ATOM   8321  N  NZ    . LYS B 1 341 ? 101.616 120.152 142.881 1.00 33.97 1  341 LYS B NZ    1 
ATOM   8322  N  N     . LEU B 1 342 ? 105.850 126.252 143.905 1.00 29.26 ?  342 LEU B N     1 
ATOM   8323  C  CA    . LEU B 1 342 ? 107.011 127.135 143.934 1.00 26.52 ?  342 LEU B CA    1 
ATOM   8324  C  C     . LEU B 1 342 ? 107.671 127.133 145.308 1.00 30.91 ?  342 LEU B C     1 
ATOM   8325  O  O     . LEU B 1 342 ? 108.903 127.149 145.410 1.00 37.75 ?  342 LEU B O     1 
ATOM   8326  C  CB    . LEU B 1 342 ? 106.604 128.550 143.530 1.00 30.07 ?  342 LEU B CB    1 
ATOM   8327  C  CG    . LEU B 1 342 ? 107.739 129.499 143.141 1.00 27.23 ?  342 LEU B CG    1 
ATOM   8328  C  CD1   . LEU B 1 342 ? 108.760 128.787 142.270 1.00 25.62 ?  342 LEU B CD1   1 
ATOM   8329  C  CD2   . LEU B 1 342 ? 107.188 130.723 142.430 1.00 26.81 ?  342 LEU B CD2   1 
ATOM   8330  N  N     . LEU B 1 343 ? 106.871 127.111 146.377 1.00 29.53 ?  343 LEU B N     1 
ATOM   8331  C  CA    . LEU B 1 343 ? 107.428 127.010 147.722 1.00 26.59 ?  343 LEU B CA    1 
ATOM   8332  C  C     . LEU B 1 343 ? 108.178 125.697 147.913 1.00 28.70 ?  343 LEU B C     1 
ATOM   8333  O  O     . LEU B 1 343 ? 109.258 125.669 148.516 1.00 33.74 ?  343 LEU B O     1 
ATOM   8334  C  CB    . LEU B 1 343 ? 106.317 127.143 148.761 1.00 30.61 ?  343 LEU B CB    1 
ATOM   8335  C  CG    . LEU B 1 343 ? 106.087 128.532 149.350 1.00 30.70 ?  343 LEU B CG    1 
ATOM   8336  C  CD1   . LEU B 1 343 ? 105.065 128.464 150.472 1.00 27.27 ?  343 LEU B CD1   1 
ATOM   8337  C  CD2   . LEU B 1 343 ? 107.396 129.126 149.843 1.00 30.33 ?  343 LEU B CD2   1 
ATOM   8338  N  N     . GLU B 1 344 ? 107.611 124.595 147.418 1.00 30.95 ?  344 GLU B N     1 
ATOM   8339  C  CA    . GLU B 1 344 ? 108.290 123.308 147.515 1.00 28.52 ?  344 GLU B CA    1 
ATOM   8340  C  C     . GLU B 1 344 ? 109.579 123.303 146.703 1.00 29.40 ?  344 GLU B C     1 
ATOM   8341  O  O     . GLU B 1 344 ? 110.574 122.700 147.115 1.00 34.84 ?  344 GLU B O     1 
ATOM   8342  C  CB    . GLU B 1 344 ? 107.359 122.186 147.061 1.00 30.80 ?  344 GLU B CB    1 
ATOM   8343  C  CG    . GLU B 1 344 ? 106.177 121.955 147.989 1.00 33.67 ?  344 GLU B CG    1 
ATOM   8344  C  CD    . GLU B 1 344 ? 105.072 121.154 147.335 1.00 38.15 ?  344 GLU B CD    1 
ATOM   8345  O  OE1   . GLU B 1 344 ? 105.294 120.637 146.221 1.00 39.86 ?  344 GLU B OE1   1 
ATOM   8346  O  OE2   . GLU B 1 344 ? 103.980 121.046 147.932 1.00 37.98 -1 344 GLU B OE2   1 
ATOM   8347  N  N     . LYS B 1 345 ? 109.578 123.968 145.546 1.00 29.24 ?  345 LYS B N     1 
ATOM   8348  C  CA    . LYS B 1 345 ? 110.803 124.103 144.765 1.00 27.16 ?  345 LYS B CA    1 
ATOM   8349  C  C     . LYS B 1 345 ? 111.850 124.908 145.523 1.00 30.72 ?  345 LYS B C     1 
ATOM   8350  O  O     . LYS B 1 345 ? 113.040 124.574 145.496 1.00 32.03 ?  345 LYS B O     1 
ATOM   8351  C  CB    . LYS B 1 345 ? 110.499 124.753 143.416 1.00 26.14 ?  345 LYS B CB    1 
ATOM   8352  C  CG    . LYS B 1 345 ? 111.711 124.895 142.514 1.00 29.85 ?  345 LYS B CG    1 
ATOM   8353  C  CD    . LYS B 1 345 ? 111.336 125.468 141.160 1.00 30.37 ?  345 LYS B CD    1 
ATOM   8354  C  CE    . LYS B 1 345 ? 112.550 125.563 140.253 1.00 30.62 ?  345 LYS B CE    1 
ATOM   8355  N  NZ    . LYS B 1 345 ? 112.216 126.151 138.928 1.00 31.25 1  345 LYS B NZ    1 
ATOM   8356  N  N     . LEU B 1 346 ? 111.426 125.977 146.203 1.00 29.75 ?  346 LEU B N     1 
ATOM   8357  C  CA    . LEU B 1 346 ? 112.349 126.748 147.030 1.00 23.48 ?  346 LEU B CA    1 
ATOM   8358  C  C     . LEU B 1 346 ? 112.951 125.881 148.126 1.00 27.62 ?  346 LEU B C     1 
ATOM   8359  O  O     . LEU B 1 346 ? 114.163 125.916 148.370 1.00 30.54 ?  346 LEU B O     1 
ATOM   8360  C  CB    . LEU B 1 346 ? 111.630 127.950 147.647 1.00 24.10 ?  346 LEU B CB    1 
ATOM   8361  C  CG    . LEU B 1 346 ? 111.088 129.056 146.743 1.00 26.77 ?  346 LEU B CG    1 
ATOM   8362  C  CD1   . LEU B 1 346 ? 110.306 130.065 147.565 1.00 28.15 ?  346 LEU B CD1   1 
ATOM   8363  C  CD2   . LEU B 1 346 ? 112.212 129.740 146.001 1.00 26.32 ?  346 LEU B CD2   1 
ATOM   8364  N  N     . ALA B 1 347 ? 112.112 125.090 148.798 1.00 26.89 ?  347 ALA B N     1 
ATOM   8365  C  CA    . ALA B 1 347 ? 112.601 124.227 149.870 1.00 20.29 ?  347 ALA B CA    1 
ATOM   8366  C  C     . ALA B 1 347 ? 113.560 123.169 149.340 1.00 29.91 ?  347 ALA B C     1 
ATOM   8367  O  O     . ALA B 1 347 ? 114.594 122.896 149.960 1.00 35.16 ?  347 ALA B O     1 
ATOM   8368  C  CB    . ALA B 1 347 ? 111.425 123.573 150.594 1.00 22.69 ?  347 ALA B CB    1 
ATOM   8369  N  N     . MET B 1 348 ? 113.236 122.565 148.194 1.00 31.69 ?  348 MET B N     1 
ATOM   8370  C  CA    . MET B 1 348 ? 114.123 121.570 147.600 1.00 29.01 ?  348 MET B CA    1 
ATOM   8371  C  C     . MET B 1 348 ? 115.456 122.187 147.199 1.00 31.20 ?  348 MET B C     1 
ATOM   8372  O  O     . MET B 1 348 ? 116.517 121.598 147.433 1.00 35.64 ?  348 MET B O     1 
ATOM   8373  C  CB    . MET B 1 348 ? 113.443 120.925 146.392 1.00 31.96 ?  348 MET B CB    1 
ATOM   8374  C  CG    . MET B 1 348 ? 114.384 120.160 145.474 1.00 38.36 ?  348 MET B CG    1 
ATOM   8375  S  SD    . MET B 1 348 ? 114.602 120.970 143.878 1.00 53.07 ?  348 MET B SD    1 
ATOM   8376  C  CE    . MET B 1 348 ? 112.920 120.973 143.267 1.00 37.32 ?  348 MET B CE    1 
ATOM   8377  N  N     . LEU B 1 349 ? 115.422 123.378 146.598 1.00 28.67 ?  349 LEU B N     1 
ATOM   8378  C  CA    . LEU B 1 349 ? 116.656 124.050 146.208 1.00 25.58 ?  349 LEU B CA    1 
ATOM   8379  C  C     . LEU B 1 349 ? 117.505 124.391 147.423 1.00 25.72 ?  349 LEU B C     1 
ATOM   8380  O  O     . LEU B 1 349 ? 118.733 124.250 147.390 1.00 30.40 ?  349 LEU B O     1 
ATOM   8381  C  CB    . LEU B 1 349 ? 116.332 125.315 145.413 1.00 30.48 ?  349 LEU B CB    1 
ATOM   8382  C  CG    . LEU B 1 349 ? 116.681 125.321 143.927 1.00 31.43 ?  349 LEU B CG    1 
ATOM   8383  C  CD1   . LEU B 1 349 ? 115.604 124.621 143.117 1.00 31.89 ?  349 LEU B CD1   1 
ATOM   8384  C  CD2   . LEU B 1 349 ? 116.877 126.748 143.453 1.00 28.13 ?  349 LEU B CD2   1 
ATOM   8385  N  N     . ARG B 1 350 ? 116.873 124.856 148.503 1.00 25.07 ?  350 ARG B N     1 
ATOM   8386  C  CA    . ARG B 1 350 ? 117.625 125.174 149.711 1.00 25.84 ?  350 ARG B CA    1 
ATOM   8387  C  C     . ARG B 1 350 ? 118.193 123.923 150.365 1.00 28.68 ?  350 ARG B C     1 
ATOM   8388  O  O     . ARG B 1 350 ? 119.287 123.968 150.938 1.00 33.54 ?  350 ARG B O     1 
ATOM   8389  C  CB    . ARG B 1 350 ? 116.742 125.945 150.691 1.00 22.89 ?  350 ARG B CB    1 
ATOM   8390  C  CG    . ARG B 1 350 ? 116.359 127.334 150.211 1.00 23.30 ?  350 ARG B CG    1 
ATOM   8391  C  CD    . ARG B 1 350 ? 115.298 127.959 151.098 1.00 23.06 ?  350 ARG B CD    1 
ATOM   8392  N  NE    . ARG B 1 350 ? 115.723 128.017 152.490 1.00 34.99 ?  350 ARG B NE    1 
ATOM   8393  C  CZ    . ARG B 1 350 ? 116.588 128.898 152.975 1.00 31.12 ?  350 ARG B CZ    1 
ATOM   8394  N  NH1   . ARG B 1 350 ? 117.137 129.825 152.207 1.00 26.96 1  350 ARG B NH1   1 
ATOM   8395  N  NH2   . ARG B 1 350 ? 116.911 128.847 154.263 1.00 27.93 ?  350 ARG B NH2   1 
ATOM   8396  N  N     . SER B 1 351 ? 117.470 122.805 150.302 1.00 28.79 ?  351 SER B N     1 
ATOM   8397  C  CA    . SER B 1 351 ? 118.018 121.549 150.802 1.00 29.95 ?  351 SER B CA    1 
ATOM   8398  C  C     . SER B 1 351 ? 119.220 121.104 149.979 1.00 33.63 ?  351 SER B C     1 
ATOM   8399  O  O     . SER B 1 351 ? 120.224 120.643 150.534 1.00 40.76 ?  351 SER B O     1 
ATOM   8400  C  CB    . SER B 1 351 ? 116.938 120.468 150.804 1.00 31.21 ?  351 SER B CB    1 
ATOM   8401  O  OG    . SER B 1 351 ? 115.804 120.880 151.546 1.00 36.59 ?  351 SER B OG    1 
ATOM   8402  N  N     . GLU B 1 352 ? 119.138 121.235 148.654 1.00 31.55 ?  352 GLU B N     1 
ATOM   8403  C  CA    . GLU B 1 352 ? 120.216 120.752 147.796 1.00 30.05 ?  352 GLU B CA    1 
ATOM   8404  C  C     . GLU B 1 352 ? 121.454 121.640 147.880 1.00 35.96 ?  352 GLU B C     1 
ATOM   8405  O  O     . GLU B 1 352 ? 122.576 121.133 147.992 1.00 39.68 ?  352 GLU B O     1 
ATOM   8406  C  CB    . GLU B 1 352 ? 119.733 120.645 146.350 1.00 34.33 ?  352 GLU B CB    1 
ATOM   8407  C  CG    . GLU B 1 352 ? 118.595 119.661 146.143 1.00 36.76 ?  352 GLU B CG    1 
ATOM   8408  C  CD    . GLU B 1 352 ? 118.041 119.700 144.734 1.00 41.55 ?  352 GLU B CD    1 
ATOM   8409  O  OE1   . GLU B 1 352 ? 118.100 120.773 144.099 1.00 38.58 ?  352 GLU B OE1   1 
ATOM   8410  O  OE2   . GLU B 1 352 ? 117.543 118.656 144.261 1.00 41.64 -1 352 GLU B OE2   1 
ATOM   8411  N  N     . SER B 1 353 ? 121.278 122.963 147.830 1.00 34.01 ?  353 SER B N     1 
ATOM   8412  C  CA    . SER B 1 353 ? 122.408 123.873 147.705 1.00 35.75 ?  353 SER B CA    1 
ATOM   8413  C  C     . SER B 1 353 ? 122.393 125.048 148.674 1.00 31.83 ?  353 SER B C     1 
ATOM   8414  O  O     . SER B 1 353 ? 123.344 125.836 148.670 1.00 34.71 ?  353 SER B O     1 
ATOM   8415  C  CB    . SER B 1 353 ? 122.493 124.417 146.271 1.00 35.48 ?  353 SER B CB    1 
ATOM   8416  O  OG    . SER B 1 353 ? 121.374 125.231 145.968 1.00 36.62 ?  353 SER B OG    1 
ATOM   8417  N  N     . GLY B 1 354 ? 121.355 125.196 149.494 1.00 22.19 ?  354 GLY B N     1 
ATOM   8418  C  CA    . GLY B 1 354 ? 121.271 126.322 150.399 1.00 23.41 ?  354 GLY B CA    1 
ATOM   8419  C  C     . GLY B 1 354 ? 120.736 127.599 149.789 1.00 21.72 ?  354 GLY B C     1 
ATOM   8420  O  O     . GLY B 1 354 ? 120.626 128.605 150.500 1.00 28.76 ?  354 GLY B O     1 
ATOM   8421  N  N     . TYR B 1 355 ? 120.402 127.590 148.508 1.00 25.60 ?  355 TYR B N     1 
ATOM   8422  C  CA    . TYR B 1 355 ? 119.850 128.723 147.791 1.00 17.85 ?  355 TYR B CA    1 
ATOM   8423  C  C     . TYR B 1 355 ? 118.393 128.457 147.438 1.00 20.21 ?  355 TYR B C     1 
ATOM   8424  O  O     . TYR B 1 355 ? 117.976 127.301 147.328 1.00 28.32 ?  355 TYR B O     1 
ATOM   8425  C  CB    . TYR B 1 355 ? 120.656 128.987 146.512 1.00 22.73 ?  355 TYR B CB    1 
ATOM   8426  C  CG    . TYR B 1 355 ? 122.051 129.500 146.768 1.00 25.91 ?  355 TYR B CG    1 
ATOM   8427  C  CD1   . TYR B 1 355 ? 122.264 130.620 147.559 1.00 23.53 ?  355 TYR B CD1   1 
ATOM   8428  C  CD2   . TYR B 1 355 ? 123.158 128.863 146.223 1.00 26.75 ?  355 TYR B CD2   1 
ATOM   8429  C  CE1   . TYR B 1 355 ? 123.536 131.092 147.798 1.00 26.24 ?  355 TYR B CE1   1 
ATOM   8430  C  CE2   . TYR B 1 355 ? 124.434 129.329 146.456 1.00 28.07 ?  355 TYR B CE2   1 
ATOM   8431  C  CZ    . TYR B 1 355 ? 124.618 130.444 147.244 1.00 29.17 ?  355 TYR B CZ    1 
ATOM   8432  O  OH    . TYR B 1 355 ? 125.888 130.914 147.482 1.00 30.83 ?  355 TYR B OH    1 
ATOM   8433  N  N     . PRO B 1 356 ? 117.581 129.503 147.241 1.00 21.44 ?  356 PRO B N     1 
ATOM   8434  C  CA    . PRO B 1 356 ? 117.880 130.939 147.298 1.00 17.78 ?  356 PRO B CA    1 
ATOM   8435  C  C     . PRO B 1 356 ? 117.840 131.541 148.693 1.00 17.32 ?  356 PRO B C     1 
ATOM   8436  O  O     . PRO B 1 356 ? 117.337 130.941 149.637 1.00 20.04 ?  356 PRO B O     1 
ATOM   8437  C  CB    . PRO B 1 356 ? 116.773 131.537 146.427 1.00 16.77 ?  356 PRO B CB    1 
ATOM   8438  C  CG    . PRO B 1 356 ? 115.601 130.658 146.722 1.00 19.79 ?  356 PRO B CG    1 
ATOM   8439  C  CD    . PRO B 1 356 ? 116.178 129.267 146.857 1.00 17.79 ?  356 PRO B CD    1 
ATOM   8440  N  N     . TYR B 1 357 ? 118.380 132.747 148.838 1.00 23.57 ?  357 TYR B N     1 
ATOM   8441  C  CA    . TYR B 1 357 ? 118.048 133.569 149.988 1.00 11.38 ?  357 TYR B CA    1 
ATOM   8442  C  C     . TYR B 1 357 ? 116.574 133.940 149.922 1.00 17.94 ?  357 TYR B C     1 
ATOM   8443  O  O     . TYR B 1 357 ? 116.030 134.190 148.843 1.00 26.55 ?  357 TYR B O     1 
ATOM   8444  C  CB    . TYR B 1 357 ? 118.905 134.835 150.018 1.00 16.41 ?  357 TYR B CB    1 
ATOM   8445  C  CG    . TYR B 1 357 ? 120.391 134.602 149.870 1.00 21.16 ?  357 TYR B CG    1 
ATOM   8446  C  CD1   . TYR B 1 357 ? 120.987 133.457 150.370 1.00 15.33 ?  357 TYR B CD1   1 
ATOM   8447  C  CD2   . TYR B 1 357 ? 121.199 135.532 149.229 1.00 20.38 ?  357 TYR B CD2   1 
ATOM   8448  C  CE1   . TYR B 1 357 ? 122.341 133.240 150.243 1.00 20.34 ?  357 TYR B CE1   1 
ATOM   8449  C  CE2   . TYR B 1 357 ? 122.555 135.324 149.093 1.00 15.32 ?  357 TYR B CE2   1 
ATOM   8450  C  CZ    . TYR B 1 357 ? 123.121 134.175 149.603 1.00 21.33 ?  357 TYR B CZ    1 
ATOM   8451  O  OH    . TYR B 1 357 ? 124.473 133.959 149.475 1.00 31.57 ?  357 TYR B OH    1 
ATOM   8452  N  N     . ILE B 1 358 ? 115.920 133.968 151.076 1.00 15.26 ?  358 ILE B N     1 
ATOM   8453  C  CA    . ILE B 1 358 ? 114.502 134.290 151.160 1.00 14.09 ?  358 ILE B CA    1 
ATOM   8454  C  C     . ILE B 1 358 ? 114.372 135.647 151.833 1.00 15.26 ?  358 ILE B C     1 
ATOM   8455  O  O     . ILE B 1 358 ? 114.844 135.836 152.959 1.00 24.51 ?  358 ILE B O     1 
ATOM   8456  C  CB    . ILE B 1 358 ? 113.719 133.215 151.927 1.00 23.12 ?  358 ILE B CB    1 
ATOM   8457  C  CG1   . ILE B 1 358 ? 113.802 131.871 151.201 1.00 15.21 ?  358 ILE B CG1   1 
ATOM   8458  C  CG2   . ILE B 1 358 ? 112.270 133.638 152.094 1.00 16.12 ?  358 ILE B CG2   1 
ATOM   8459  C  CD1   . ILE B 1 358 ? 113.255 131.905 149.793 1.00 19.53 ?  358 ILE B CD1   1 
ATOM   8460  N  N     . MET B 1 359 ? 113.738 136.589 151.141 1.00 17.72 ?  359 MET B N     1 
ATOM   8461  C  CA    . MET B 1 359 ? 113.461 137.917 151.679 1.00 7.28  ?  359 MET B CA    1 
ATOM   8462  C  C     . MET B 1 359 ? 111.952 138.105 151.721 1.00 9.30  ?  359 MET B C     1 
ATOM   8463  O  O     . MET B 1 359 ? 111.303 138.188 150.673 1.00 20.49 ?  359 MET B O     1 
ATOM   8464  C  CB    . MET B 1 359 ? 114.124 139.006 150.839 1.00 8.65  ?  359 MET B CB    1 
ATOM   8465  C  CG    . MET B 1 359 ? 114.022 140.392 151.450 1.00 9.10  ?  359 MET B CG    1 
ATOM   8466  S  SD    . MET B 1 359 ? 113.949 141.702 150.221 1.00 32.53 ?  359 MET B SD    1 
ATOM   8467  C  CE    . MET B 1 359 ? 112.954 142.913 151.079 1.00 9.56  ?  359 MET B CE    1 
ATOM   8468  N  N     . PHE B 1 360 ? 111.396 138.165 152.926 1.00 10.36 ?  360 PHE B N     1 
ATOM   8469  C  CA    . PHE B 1 360 ? 109.968 138.410 153.101 1.00 10.65 ?  360 PHE B CA    1 
ATOM   8470  C  C     . PHE B 1 360 ? 109.746 139.913 153.006 1.00 16.04 ?  360 PHE B C     1 
ATOM   8471  O  O     . PHE B 1 360 ? 109.930 140.644 153.981 1.00 19.76 ?  360 PHE B O     1 
ATOM   8472  C  CB    . PHE B 1 360 ? 109.488 137.840 154.428 1.00 12.02 ?  360 PHE B CB    1 
ATOM   8473  C  CG    . PHE B 1 360 ? 109.592 136.344 154.508 1.00 15.34 ?  360 PHE B CG    1 
ATOM   8474  C  CD1   . PHE B 1 360 ? 108.873 135.539 153.641 1.00 15.19 ?  360 PHE B CD1   1 
ATOM   8475  C  CD2   . PHE B 1 360 ? 110.422 135.744 155.439 1.00 14.96 ?  360 PHE B CD2   1 
ATOM   8476  C  CE1   . PHE B 1 360 ? 108.974 134.163 153.708 1.00 13.79 ?  360 PHE B CE1   1 
ATOM   8477  C  CE2   . PHE B 1 360 ? 110.526 134.370 155.510 1.00 14.37 ?  360 PHE B CE2   1 
ATOM   8478  C  CZ    . PHE B 1 360 ? 109.801 133.579 154.644 1.00 17.05 ?  360 PHE B CZ    1 
ATOM   8479  N  N     . GLN B 1 361 ? 109.339 140.370 151.818 1.00 16.85 ?  361 GLN B N     1 
ATOM   8480  C  CA    . GLN B 1 361 ? 109.308 141.800 151.523 1.00 9.93  ?  361 GLN B CA    1 
ATOM   8481  C  C     . GLN B 1 361 ? 108.380 142.554 152.467 1.00 13.61 ?  361 GLN B C     1 
ATOM   8482  O  O     . GLN B 1 361 ? 108.722 143.640 152.950 1.00 15.15 ?  361 GLN B O     1 
ATOM   8483  C  CB    . GLN B 1 361 ? 108.881 142.016 150.072 1.00 15.59 ?  361 GLN B CB    1 
ATOM   8484  C  CG    . GLN B 1 361 ? 108.911 143.459 149.614 1.00 15.46 ?  361 GLN B CG    1 
ATOM   8485  C  CD    . GLN B 1 361 ? 109.046 143.585 148.113 1.00 17.89 ?  361 GLN B CD    1 
ATOM   8486  O  OE1   . GLN B 1 361 ? 108.471 142.799 147.361 1.00 27.70 ?  361 GLN B OE1   1 
ATOM   8487  N  NE2   . GLN B 1 361 ? 109.811 144.572 147.667 1.00 18.34 ?  361 GLN B NE2   1 
ATOM   8488  N  N     . ASP B 1 362 ? 107.197 141.998 152.736 1.00 20.04 ?  362 ASP B N     1 
ATOM   8489  C  CA    . ASP B 1 362 ? 106.251 142.687 153.605 1.00 15.90 ?  362 ASP B CA    1 
ATOM   8490  C  C     . ASP B 1 362 ? 106.740 142.729 155.046 1.00 16.17 ?  362 ASP B C     1 
ATOM   8491  O  O     . ASP B 1 362 ? 106.503 143.719 155.746 1.00 23.66 ?  362 ASP B O     1 
ATOM   8492  C  CB    . ASP B 1 362 ? 104.880 142.024 153.522 1.00 22.13 ?  362 ASP B CB    1 
ATOM   8493  C  CG    . ASP B 1 362 ? 104.104 142.452 152.294 1.00 29.34 ?  362 ASP B CG    1 
ATOM   8494  O  OD1   . ASP B 1 362 ? 104.425 141.969 151.188 1.00 29.39 ?  362 ASP B OD1   1 
ATOM   8495  O  OD2   . ASP B 1 362 ? 103.174 143.273 152.433 1.00 30.44 -1 362 ASP B OD2   1 
ATOM   8496  N  N     . ASN B 1 363 ? 107.426 141.680 155.504 1.00 21.55 ?  363 ASN B N     1 
ATOM   8497  C  CA    . ASN B 1 363 ? 108.026 141.718 156.833 1.00 10.88 ?  363 ASN B CA    1 
ATOM   8498  C  C     . ASN B 1 363 ? 109.080 142.809 156.934 1.00 14.86 ?  363 ASN B C     1 
ATOM   8499  O  O     . ASN B 1 363 ? 109.232 143.433 157.989 1.00 25.42 ?  363 ASN B O     1 
ATOM   8500  C  CB    . ASN B 1 363 ? 108.639 140.359 157.173 1.00 12.50 ?  363 ASN B CB    1 
ATOM   8501  C  CG    . ASN B 1 363 ? 107.595 139.320 157.520 1.00 16.62 ?  363 ASN B CG    1 
ATOM   8502  O  OD1   . ASN B 1 363 ? 106.472 139.655 157.894 1.00 21.40 ?  363 ASN B OD1   1 
ATOM   8503  N  ND2   . ASN B 1 363 ? 107.960 138.052 157.399 1.00 15.52 ?  363 ASN B ND2   1 
ATOM   8504  N  N     . VAL B 1 364 ? 109.823 143.047 155.852 1.00 14.12 ?  364 VAL B N     1 
ATOM   8505  C  CA    . VAL B 1 364 ? 110.817 144.114 155.847 1.00 9.03  ?  364 VAL B CA    1 
ATOM   8506  C  C     . VAL B 1 364 ? 110.142 145.479 155.845 1.00 16.84 ?  364 VAL B C     1 
ATOM   8507  O  O     . VAL B 1 364 ? 110.559 146.393 156.568 1.00 18.99 ?  364 VAL B O     1 
ATOM   8508  C  CB    . VAL B 1 364 ? 111.763 143.954 154.644 1.00 2.44  ?  364 VAL B CB    1 
ATOM   8509  C  CG1   . VAL B 1 364 ? 112.845 145.015 154.679 1.00 6.38  ?  364 VAL B CG1   1 
ATOM   8510  C  CG2   . VAL B 1 364 ? 112.375 142.569 154.633 1.00 9.06  ?  364 VAL B CG2   1 
ATOM   8511  N  N     . ASN B 1 365 ? 109.094 145.645 155.040 1.00 18.91 ?  365 ASN B N     1 
ATOM   8512  C  CA    . ASN B 1 365 ? 108.531 146.964 154.792 1.00 7.74  ?  365 ASN B CA    1 
ATOM   8513  C  C     . ASN B 1 365 ? 107.428 147.361 155.764 1.00 15.37 ?  365 ASN B C     1 
ATOM   8514  O  O     . ASN B 1 365 ? 107.022 148.528 155.759 1.00 22.95 ?  365 ASN B O     1 
ATOM   8515  C  CB    . ASN B 1 365 ? 107.995 147.045 153.360 1.00 11.88 ?  365 ASN B CB    1 
ATOM   8516  C  CG    . ASN B 1 365 ? 109.102 147.103 152.330 1.00 13.44 ?  365 ASN B CG    1 
ATOM   8517  O  OD1   . ASN B 1 365 ? 110.015 147.921 152.431 1.00 15.79 ?  365 ASN B OD1   1 
ATOM   8518  N  ND2   . ASN B 1 365 ? 109.029 146.234 151.334 1.00 19.25 ?  365 ASN B ND2   1 
ATOM   8519  N  N     . LYS B 1 366 ? 106.931 146.442 156.592 1.00 15.39 ?  366 LYS B N     1 
ATOM   8520  C  CA    . LYS B 1 366 ? 105.947 146.826 157.595 1.00 17.04 ?  366 LYS B CA    1 
ATOM   8521  C  C     . LYS B 1 366 ? 106.577 147.574 158.761 1.00 19.24 ?  366 LYS B C     1 
ATOM   8522  O  O     . LYS B 1 366 ? 105.871 148.297 159.471 1.00 26.94 ?  366 LYS B O     1 
ATOM   8523  C  CB    . LYS B 1 366 ? 105.202 145.593 158.111 1.00 18.92 ?  366 LYS B CB    1 
ATOM   8524  C  CG    . LYS B 1 366 ? 106.086 144.561 158.792 1.00 22.26 ?  366 LYS B CG    1 
ATOM   8525  C  CD    . LYS B 1 366 ? 105.278 143.649 159.708 1.00 24.45 ?  366 LYS B CD    1 
ATOM   8526  C  CE    . LYS B 1 366 ? 103.932 143.282 159.100 1.00 24.01 ?  366 LYS B CE    1 
ATOM   8527  N  NZ    . LYS B 1 366 ? 104.062 142.290 157.998 1.00 24.16 1  366 LYS B NZ    1 
ATOM   8528  N  N     . VAL B 1 367 ? 107.882 147.416 158.968 1.00 24.11 ?  367 VAL B N     1 
ATOM   8529  C  CA    . VAL B 1 367 ? 108.620 148.152 159.984 1.00 14.42 ?  367 VAL B CA    1 
ATOM   8530  C  C     . VAL B 1 367 ? 109.728 149.003 159.389 1.00 16.80 ?  367 VAL B C     1 
ATOM   8531  O  O     . VAL B 1 367 ? 110.489 149.622 160.139 1.00 22.49 ?  367 VAL B O     1 
ATOM   8532  C  CB    . VAL B 1 367 ? 109.193 147.206 161.059 1.00 12.46 ?  367 VAL B CB    1 
ATOM   8533  C  CG1   . VAL B 1 367 ? 108.066 146.507 161.799 1.00 19.88 ?  367 VAL B CG1   1 
ATOM   8534  C  CG2   . VAL B 1 367 ? 110.123 146.192 160.424 1.00 9.76  ?  367 VAL B CG2   1 
ATOM   8535  N  N     . HIS B 1 368 ? 109.843 149.048 158.064 1.00 20.92 ?  368 HIS B N     1 
ATOM   8536  C  CA    . HIS B 1 368 ? 110.849 149.875 157.413 1.00 5.32  ?  368 HIS B CA    1 
ATOM   8537  C  C     . HIS B 1 368 ? 110.570 151.348 157.681 1.00 15.48 ?  368 HIS B C     1 
ATOM   8538  O  O     . HIS B 1 368 ? 109.452 151.829 157.471 1.00 25.96 ?  368 HIS B O     1 
ATOM   8539  C  CB    . HIS B 1 368 ? 110.858 149.595 155.912 1.00 13.01 ?  368 HIS B CB    1 
ATOM   8540  C  CG    . HIS B 1 368 ? 111.924 150.327 155.162 1.00 10.56 ?  368 HIS B CG    1 
ATOM   8541  N  ND1   . HIS B 1 368 ? 111.747 150.777 153.872 1.00 14.86 ?  368 HIS B ND1   1 
ATOM   8542  C  CD2   . HIS B 1 368 ? 113.181 150.684 155.516 1.00 7.35  ?  368 HIS B CD2   1 
ATOM   8543  C  CE1   . HIS B 1 368 ? 112.849 151.381 153.464 1.00 14.41 ?  368 HIS B CE1   1 
ATOM   8544  N  NE2   . HIS B 1 368 ? 113.734 151.338 154.443 1.00 10.81 ?  368 HIS B NE2   1 
ATOM   8545  N  N     . ALA B 1 369 ? 111.592 152.065 158.144 1.00 20.22 ?  369 ALA B N     1 
ATOM   8546  C  CA    . ALA B 1 369 ? 111.428 153.455 158.541 1.00 10.07 ?  369 ALA B CA    1 
ATOM   8547  C  C     . ALA B 1 369 ? 111.536 154.434 157.381 1.00 17.57 ?  369 ALA B C     1 
ATOM   8548  O  O     . ALA B 1 369 ? 111.195 155.608 157.555 1.00 26.04 ?  369 ALA B O     1 
ATOM   8549  C  CB    . ALA B 1 369 ? 112.462 153.816 159.609 1.00 10.84 ?  369 ALA B CB    1 
ATOM   8550  N  N     . ASN B 1 370 ? 111.991 153.991 156.213 1.00 16.15 ?  370 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 370 ? 112.239 154.873 155.080 1.00 14.72 ?  370 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 370 ? 111.470 154.420 153.846 1.00 12.00 ?  370 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 370 ? 111.991 154.431 152.729 1.00 18.38 ?  370 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 370 ? 113.733 154.963 154.784 1.00 11.27 ?  370 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 370 ? 114.527 155.493 155.959 1.00 11.90 ?  370 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 370 ? 114.295 156.606 156.427 1.00 26.54 ?  370 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 370 ? 115.467 154.695 156.446 1.00 16.28 ?  370 ASN B ND2   1 
ATOM   8558  N  N     . ASN B 1 371 ? 110.215 154.010 154.036 1.00 20.31 ?  371 ASN B N     1 
ATOM   8559  C  CA    . ASN B 1 371 ? 109.376 153.628 152.908 1.00 10.79 ?  371 ASN B CA    1 
ATOM   8560  C  C     . ASN B 1 371 ? 109.079 154.801 151.985 1.00 16.41 ?  371 ASN B C     1 
ATOM   8561  O  O     . ASN B 1 371 ? 108.798 154.587 150.802 1.00 19.64 ?  371 ASN B O     1 
ATOM   8562  C  CB    . ASN B 1 371 ? 108.066 153.016 153.406 1.00 6.58  ?  371 ASN B CB    1 
ATOM   8563  C  CG    . ASN B 1 371 ? 108.187 151.537 153.695 1.00 16.28 ?  371 ASN B CG    1 
ATOM   8564  O  OD1   . ASN B 1 371 ? 109.054 150.855 153.148 1.00 20.36 ?  371 ASN B OD1   1 
ATOM   8565  N  ND2   . ASN B 1 371 ? 107.316 151.030 154.556 1.00 19.92 ?  371 ASN B ND2   1 
ATOM   8566  N  N     . HIS B 1 372 ? 109.126 156.030 152.504 1.00 21.65 ?  372 HIS B N     1 
ATOM   8567  C  CA    . HIS B 1 372 ? 108.898 157.203 151.666 1.00 17.77 ?  372 HIS B CA    1 
ATOM   8568  C  C     . HIS B 1 372 ? 109.969 157.329 150.590 1.00 20.25 ?  372 HIS B C     1 
ATOM   8569  O  O     . HIS B 1 372 ? 109.664 157.647 149.435 1.00 26.17 ?  372 HIS B O     1 
ATOM   8570  C  CB    . HIS B 1 372 ? 108.856 158.461 152.534 1.00 19.55 ?  372 HIS B CB    1 
ATOM   8571  C  CG    . HIS B 1 372 ? 110.158 158.774 153.202 1.00 19.08 ?  372 HIS B CG    1 
ATOM   8572  N  ND1   . HIS B 1 372 ? 110.759 157.919 154.100 1.00 22.10 ?  372 HIS B ND1   1 
ATOM   8573  C  CD2   . HIS B 1 372 ? 110.980 159.844 153.094 1.00 20.71 ?  372 HIS B CD2   1 
ATOM   8574  C  CE1   . HIS B 1 372 ? 111.894 158.449 154.518 1.00 17.13 ?  372 HIS B CE1   1 
ATOM   8575  N  NE2   . HIS B 1 372 ? 112.049 159.619 153.925 1.00 24.73 ?  372 HIS B NE2   1 
ATOM   8576  N  N     . ILE B 1 373 ? 111.233 157.095 150.952 1.00 16.01 ?  373 ILE B N     1 
ATOM   8577  C  CA    . ILE B 1 373 ? 112.306 157.114 149.963 1.00 18.41 ?  373 ILE B CA    1 
ATOM   8578  C  C     . ILE B 1 373 ? 112.099 155.999 148.949 1.00 18.51 ?  373 ILE B C     1 
ATOM   8579  O  O     . ILE B 1 373 ? 112.096 156.229 147.733 1.00 28.73 ?  373 ILE B O     1 
ATOM   8580  C  CB    . ILE B 1 373 ? 113.674 156.990 150.656 1.00 20.64 ?  373 ILE B CB    1 
ATOM   8581  C  CG1   . ILE B 1 373 ? 113.897 158.163 151.608 1.00 18.92 ?  373 ILE B CG1   1 
ATOM   8582  C  CG2   . ILE B 1 373 ? 114.792 156.908 149.628 1.00 19.25 ?  373 ILE B CG2   1 
ATOM   8583  C  CD1   . ILE B 1 373 ? 115.057 157.976 152.548 1.00 14.77 ?  373 ILE B CD1   1 
ATOM   8584  N  N     . SER B 1 374 ? 111.898 154.780 149.443 1.00 17.14 ?  374 SER B N     1 
ATOM   8585  C  CA    . SER B 1 374 ? 111.670 153.604 148.617 1.00 6.86  ?  374 SER B CA    1 
ATOM   8586  C  C     . SER B 1 374 ? 111.375 152.413 149.515 1.00 13.56 ?  374 SER B C     1 
ATOM   8587  O  O     . SER B 1 374 ? 111.800 152.387 150.674 1.00 16.95 ?  374 SER B O     1 
ATOM   8588  C  CB    . SER B 1 374 ? 112.882 153.312 147.732 1.00 18.97 ?  374 SER B CB    1 
ATOM   8589  O  OG    . SER B 1 374 ? 112.526 152.496 146.633 1.00 32.64 ?  374 SER B OG    1 
ATOM   8590  N  N     . LYS B 1 375 ? 110.646 151.431 149.003 1.00 24.02 ?  375 LYS B N     1 
ATOM   8591  C  CA    . LYS B 1 375 ? 110.502 150.173 149.713 1.00 14.13 ?  375 LYS B CA    1 
ATOM   8592  C  C     . LYS B 1 375 ? 111.744 149.319 149.501 1.00 15.05 ?  375 LYS B C     1 
ATOM   8593  O  O     . LYS B 1 375 ? 112.435 149.433 148.487 1.00 23.95 ?  375 LYS B O     1 
ATOM   8594  C  CB    . LYS B 1 375 ? 109.260 149.418 149.239 1.00 11.94 ?  375 LYS B CB    1 
ATOM   8595  C  CG    . LYS B 1 375 ? 107.961 150.169 149.445 1.00 17.96 ?  375 LYS B CG    1 
ATOM   8596  C  CD    . LYS B 1 375 ? 107.131 149.539 150.547 1.00 17.81 ?  375 LYS B CD    1 
ATOM   8597  C  CE    . LYS B 1 375 ? 105.805 150.256 150.712 1.00 16.98 ?  375 LYS B CE    1 
ATOM   8598  N  NZ    . LYS B 1 375 ? 105.938 151.722 150.498 1.00 23.96 1  375 LYS B NZ    1 
ATOM   8599  N  N     . VAL B 1 376 ? 112.033 148.464 150.476 1.00 9.75  ?  376 VAL B N     1 
ATOM   8600  C  CA    . VAL B 1 376 ? 113.153 147.540 150.352 1.00 13.73 ?  376 VAL B CA    1 
ATOM   8601  C  C     . VAL B 1 376 ? 112.737 146.413 149.416 1.00 16.12 ?  376 VAL B C     1 
ATOM   8602  O  O     . VAL B 1 376 ? 111.816 145.649 149.720 1.00 23.12 ?  376 VAL B O     1 
ATOM   8603  C  CB    . VAL B 1 376 ? 113.583 146.998 151.720 1.00 11.90 ?  376 VAL B CB    1 
ATOM   8604  C  CG1   . VAL B 1 376 ? 114.787 146.088 151.567 1.00 10.55 ?  376 VAL B CG1   1 
ATOM   8605  C  CG2   . VAL B 1 376 ? 113.893 148.140 152.668 1.00 6.92  ?  376 VAL B CG2   1 
ATOM   8606  N  N     . LYS B 1 377 ? 113.410 146.313 148.271 1.00 14.55 ?  377 LYS B N     1 
ATOM   8607  C  CA    . LYS B 1 377 ? 113.039 145.339 147.255 1.00 9.58  ?  377 LYS B CA    1 
ATOM   8608  C  C     . LYS B 1 377 ? 113.974 144.143 147.188 1.00 9.63  ?  377 LYS B C     1 
ATOM   8609  O  O     . LYS B 1 377 ? 113.626 143.148 146.547 1.00 24.47 ?  377 LYS B O     1 
ATOM   8610  C  CB    . LYS B 1 377 ? 112.989 145.998 145.872 1.00 13.22 ?  377 LYS B CB    1 
ATOM   8611  C  CG    . LYS B 1 377 ? 112.236 147.306 145.833 1.00 9.80  ?  377 LYS B CG    1 
ATOM   8612  C  CD    . LYS B 1 377 ? 112.886 148.252 144.850 1.00 18.20 ?  377 LYS B CD    1 
ATOM   8613  C  CE    . LYS B 1 377 ? 112.711 149.690 145.276 1.00 20.76 ?  377 LYS B CE    1 
ATOM   8614  N  NZ    . LYS B 1 377 ? 113.616 150.594 144.516 1.00 19.82 1  377 LYS B NZ    1 
ATOM   8615  N  N     . PHE B 1 378 ? 115.144 144.215 147.813 1.00 11.14 ?  378 PHE B N     1 
ATOM   8616  C  CA    . PHE B 1 378 ? 116.094 143.111 147.794 1.00 8.11  ?  378 PHE B CA    1 
ATOM   8617  C  C     . PHE B 1 378 ? 117.077 143.301 148.942 1.00 7.41  ?  378 PHE B C     1 
ATOM   8618  O  O     . PHE B 1 378 ? 117.067 144.325 149.632 1.00 16.36 ?  378 PHE B O     1 
ATOM   8619  C  CB    . PHE B 1 378 ? 116.797 143.005 146.437 1.00 4.29  ?  378 PHE B CB    1 
ATOM   8620  C  CG    . PHE B 1 378 ? 117.805 144.088 146.175 1.00 4.17  ?  378 PHE B CG    1 
ATOM   8621  C  CD1   . PHE B 1 378 ? 117.423 145.417 146.129 1.00 10.59 ?  378 PHE B CD1   1 
ATOM   8622  C  CD2   . PHE B 1 378 ? 119.132 143.771 145.953 1.00 3.19  ?  378 PHE B CD2   1 
ATOM   8623  C  CE1   . PHE B 1 378 ? 118.347 146.408 145.882 1.00 7.65  ?  378 PHE B CE1   1 
ATOM   8624  C  CE2   . PHE B 1 378 ? 120.058 144.759 145.703 1.00 10.18 ?  378 PHE B CE2   1 
ATOM   8625  C  CZ    . PHE B 1 378 ? 119.664 146.080 145.666 1.00 11.71 ?  378 PHE B CZ    1 
ATOM   8626  N  N     . SER B 1 379 ? 117.924 142.301 149.146 1.00 2.13  ?  379 SER B N     1 
ATOM   8627  C  CA    . SER B 1 379 ? 118.905 142.295 150.222 1.00 0.54  ?  379 SER B CA    1 
ATOM   8628  C  C     . SER B 1 379 ? 120.306 142.154 149.630 1.00 4.59  ?  379 SER B C     1 
ATOM   8629  O  O     . SER B 1 379 ? 120.496 142.173 148.412 1.00 7.64  ?  379 SER B O     1 
ATOM   8630  C  CB    . SER B 1 379 ? 118.597 141.179 151.221 1.00 10.27 ?  379 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 379 ? 119.030 141.536 152.521 1.00 10.56 ?  379 SER B OG    1 
ATOM   8632  N  N     . ASN B 1 380 ? 121.294 142.023 150.509 1.00 11.08 ?  380 ASN B N     1 
ATOM   8633  C  CA    . ASN B 1 380 ? 122.688 141.952 150.112 1.00 7.33  ?  380 ASN B CA    1 
ATOM   8634  C  C     . ASN B 1 380 ? 123.115 140.494 149.956 1.00 13.50 ?  380 ASN B C     1 
ATOM   8635  O  O     . ASN B 1 380 ? 122.296 139.572 149.990 1.00 16.85 ?  380 ASN B O     1 
ATOM   8636  C  CB    . ASN B 1 380 ? 123.560 142.698 151.123 1.00 8.68  ?  380 ASN B CB    1 
ATOM   8637  C  CG    . ASN B 1 380 ? 123.607 142.017 152.471 1.00 6.85  ?  380 ASN B CG    1 
ATOM   8638  O  OD1   . ASN B 1 380 ? 122.579 141.613 153.011 1.00 19.12 ?  380 ASN B OD1   1 
ATOM   8639  N  ND2   . ASN B 1 380 ? 124.805 141.885 153.023 1.00 13.32 ?  380 ASN B ND2   1 
ATOM   8640  N  N     . LEU B 1 381 ? 124.419 140.282 149.768 1.00 18.23 ?  381 LEU B N     1 
ATOM   8641  C  CA    . LEU B 1 381 ? 124.950 138.938 149.585 1.00 11.49 ?  381 LEU B CA    1 
ATOM   8642  C  C     . LEU B 1 381 ? 124.801 138.082 150.837 1.00 7.62  ?  381 LEU B C     1 
ATOM   8643  O  O     . LEU B 1 381 ? 124.729 136.853 150.728 1.00 18.28 ?  381 LEU B O     1 
ATOM   8644  C  CB    . LEU B 1 381 ? 126.420 139.022 149.164 1.00 17.87 ?  381 LEU B CB    1 
ATOM   8645  C  CG    . LEU B 1 381 ? 127.239 137.739 149.011 1.00 19.37 ?  381 LEU B CG    1 
ATOM   8646  C  CD1   . LEU B 1 381 ? 126.764 136.924 147.822 1.00 15.88 ?  381 LEU B CD1   1 
ATOM   8647  C  CD2   . LEU B 1 381 ? 128.713 138.073 148.880 1.00 17.74 ?  381 LEU B CD2   1 
ATOM   8648  N  N     . CYS B 1 382 ? 124.741 138.696 152.015 1.00 11.63 ?  382 CYS B N     1 
ATOM   8649  C  CA    . CYS B 1 382 ? 124.520 137.974 153.259 1.00 5.10  ?  382 CYS B CA    1 
ATOM   8650  C  C     . CYS B 1 382 ? 123.090 138.097 153.763 1.00 8.11  ?  382 CYS B C     1 
ATOM   8651  O  O     . CYS B 1 382 ? 122.786 137.596 154.850 1.00 17.87 ?  382 CYS B O     1 
ATOM   8652  C  CB    . CYS B 1 382 ? 125.498 138.459 154.332 1.00 16.37 ?  382 CYS B CB    1 
ATOM   8653  S  SG    . CYS B 1 382 ? 127.226 138.499 153.803 1.00 31.70 ?  382 CYS B SG    1 
ATOM   8654  N  N     . SER B 1 383 ? 122.210 138.749 153.000 1.00 10.35 ?  383 SER B N     1 
ATOM   8655  C  CA    . SER B 1 383 ? 120.779 138.838 153.301 1.00 9.66  ?  383 SER B CA    1 
ATOM   8656  C  C     . SER B 1 383 ? 120.519 139.416 154.690 1.00 12.91 ?  383 SER B C     1 
ATOM   8657  O  O     . SER B 1 383 ? 119.682 138.921 155.446 1.00 23.55 ?  383 SER B O     1 
ATOM   8658  C  CB    . SER B 1 383 ? 120.097 137.477 153.146 1.00 13.23 ?  383 SER B CB    1 
ATOM   8659  O  OG    . SER B 1 383 ? 120.635 136.526 154.042 1.00 18.79 ?  383 SER B OG    1 
ATOM   8660  N  N     . GLU B 1 384 ? 121.249 140.475 155.036 1.00 7.46  ?  384 GLU B N     1 
ATOM   8661  C  CA    . GLU B 1 384 ? 120.983 141.209 156.264 1.00 8.37  ?  384 GLU B CA    1 
ATOM   8662  C  C     . GLU B 1 384 ? 120.850 142.709 156.054 1.00 13.49 ?  384 GLU B C     1 
ATOM   8663  O  O     . GLU B 1 384 ? 120.367 143.399 156.960 1.00 23.85 ?  384 GLU B O     1 
ATOM   8664  C  CB    . GLU B 1 384 ? 122.076 140.934 157.312 1.00 6.60  ?  384 GLU B CB    1 
ATOM   8665  C  CG    . GLU B 1 384 ? 123.108 142.034 157.503 1.00 10.32 ?  384 GLU B CG    1 
ATOM   8666  C  CD    . GLU B 1 384 ? 124.196 142.008 156.455 1.00 19.47 ?  384 GLU B CD    1 
ATOM   8667  O  OE1   . GLU B 1 384 ? 124.307 140.991 155.743 1.00 13.01 ?  384 GLU B OE1   1 
ATOM   8668  O  OE2   . GLU B 1 384 ? 124.950 142.996 156.356 1.00 26.60 -1 384 GLU B OE2   1 
ATOM   8669  N  N     . VAL B 1 385 ? 121.236 143.233 154.898 1.00 10.47 ?  385 VAL B N     1 
ATOM   8670  C  CA    . VAL B 1 385 ? 121.080 144.649 154.592 1.00 6.73  ?  385 VAL B CA    1 
ATOM   8671  C  C     . VAL B 1 385 ? 119.733 144.845 153.912 1.00 15.55 ?  385 VAL B C     1 
ATOM   8672  O  O     . VAL B 1 385 ? 119.471 144.261 152.855 1.00 24.31 ?  385 VAL B O     1 
ATOM   8673  C  CB    . VAL B 1 385 ? 122.223 145.154 153.703 1.00 6.60  ?  385 VAL B CB    1 
ATOM   8674  C  CG1   . VAL B 1 385 ? 121.948 146.570 153.262 1.00 6.70  ?  385 VAL B CG1   1 
ATOM   8675  C  CG2   . VAL B 1 385 ? 123.533 145.080 154.449 1.00 11.92 ?  385 VAL B CG2   1 
ATOM   8676  N  N     . LEU B 1 386 ? 118.876 145.664 154.520 1.00 12.50 ?  386 LEU B N     1 
ATOM   8677  C  CA    . LEU B 1 386 ? 117.521 145.912 154.026 1.00 2.08  ?  386 LEU B CA    1 
ATOM   8678  C  C     . LEU B 1 386 ? 117.274 147.415 154.074 1.00 5.19  ?  386 LEU B C     1 
ATOM   8679  O  O     . LEU B 1 386 ? 116.846 147.952 155.098 1.00 11.17 ?  386 LEU B O     1 
ATOM   8680  C  CB    . LEU B 1 386 ? 116.499 145.138 154.844 1.00 5.06  ?  386 LEU B CB    1 
ATOM   8681  C  CG    . LEU B 1 386 ? 116.626 143.621 154.711 1.00 5.85  ?  386 LEU B CG    1 
ATOM   8682  C  CD1   . LEU B 1 386 ? 115.825 142.936 155.784 1.00 10.23 ?  386 LEU B CD1   1 
ATOM   8683  C  CD2   . LEU B 1 386 ? 116.181 143.164 153.332 1.00 8.67  ?  386 LEU B CD2   1 
ATOM   8684  N  N     . GLN B 1 387 ? 117.546 148.088 152.960 1.00 11.72 ?  387 GLN B N     1 
ATOM   8685  C  CA    . GLN B 1 387 ? 117.490 149.539 152.898 1.00 9.78  ?  387 GLN B CA    1 
ATOM   8686  C  C     . GLN B 1 387 ? 116.754 149.976 151.641 1.00 11.25 ?  387 GLN B C     1 
ATOM   8687  O  O     . GLN B 1 387 ? 116.616 149.218 150.678 1.00 19.86 ?  387 GLN B O     1 
ATOM   8688  C  CB    . GLN B 1 387 ? 118.894 150.154 152.924 1.00 4.43  ?  387 GLN B CB    1 
ATOM   8689  C  CG    . GLN B 1 387 ? 119.741 149.705 154.097 1.00 6.44  ?  387 GLN B CG    1 
ATOM   8690  C  CD    . GLN B 1 387 ? 121.089 150.377 154.120 1.00 10.27 ?  387 GLN B CD    1 
ATOM   8691  O  OE1   . GLN B 1 387 ? 121.303 151.379 153.440 1.00 21.83 ?  387 GLN B OE1   1 
ATOM   8692  N  NE2   . GLN B 1 387 ? 122.010 149.834 154.904 1.00 10.90 ?  387 GLN B NE2   1 
ATOM   8693  N  N     . ALA B 1 388 ? 116.268 151.213 151.670 1.00 13.59 ?  388 ALA B N     1 
ATOM   8694  C  CA    . ALA B 1 388 ? 115.623 151.797 150.505 1.00 10.79 ?  388 ALA B CA    1 
ATOM   8695  C  C     . ALA B 1 388 ? 116.638 152.023 149.392 1.00 17.73 ?  388 ALA B C     1 
ATOM   8696  O  O     . ALA B 1 388 ? 117.758 152.478 149.633 1.00 23.67 ?  388 ALA B O     1 
ATOM   8697  C  CB    . ALA B 1 388 ? 114.950 153.117 150.875 1.00 9.43  ?  388 ALA B CB    1 
ATOM   8698  N  N     . SER B 1 389 ? 116.240 151.699 148.165 1.00 21.15 ?  389 SER B N     1 
ATOM   8699  C  CA    . SER B 1 389 ? 117.082 151.910 147.000 1.00 8.55  ?  389 SER B CA    1 
ATOM   8700  C  C     . SER B 1 389 ? 116.241 152.468 145.866 1.00 16.13 ?  389 SER B C     1 
ATOM   8701  O  O     . SER B 1 389 ? 115.104 152.038 145.653 1.00 23.96 ?  389 SER B O     1 
ATOM   8702  C  CB    . SER B 1 389 ? 117.765 150.614 146.553 1.00 14.47 ?  389 SER B CB    1 
ATOM   8703  O  OG    . SER B 1 389 ? 116.823 149.568 146.391 1.00 24.83 ?  389 SER B OG    1 
ATOM   8704  N  N     . GLN B 1 390 ? 116.806 153.429 145.142 1.00 17.90 ?  390 GLN B N     1 
ATOM   8705  C  CA    . GLN B 1 390 ? 116.187 153.994 143.954 1.00 11.04 ?  390 GLN B CA    1 
ATOM   8706  C  C     . GLN B 1 390 ? 117.023 153.610 142.743 1.00 12.59 ?  390 GLN B C     1 
ATOM   8707  O  O     . GLN B 1 390 ? 118.245 153.793 142.745 1.00 26.82 ?  390 GLN B O     1 
ATOM   8708  C  CB    . GLN B 1 390 ? 116.065 155.515 144.068 1.00 16.03 ?  390 GLN B CB    1 
ATOM   8709  C  CG    . GLN B 1 390 ? 115.070 155.970 145.126 1.00 18.30 ?  390 GLN B CG    1 
ATOM   8710  C  CD    . GLN B 1 390 ? 115.116 157.464 145.372 1.00 22.91 ?  390 GLN B CD    1 
ATOM   8711  O  OE1   . GLN B 1 390 ? 115.987 158.164 144.857 1.00 25.83 ?  390 GLN B OE1   1 
ATOM   8712  N  NE2   . GLN B 1 390 ? 114.173 157.961 146.165 1.00 18.30 ?  390 GLN B NE2   1 
ATOM   8713  N  N     . VAL B 1 391 ? 116.367 153.064 141.720 1.00 22.98 ?  391 VAL B N     1 
ATOM   8714  C  CA    . VAL B 1 391 ? 117.087 152.603 140.540 1.00 20.87 ?  391 VAL B CA    1 
ATOM   8715  C  C     . VAL B 1 391 ? 117.656 153.798 139.784 1.00 23.00 ?  391 VAL B C     1 
ATOM   8716  O  O     . VAL B 1 391 ? 117.102 154.905 139.805 1.00 21.34 ?  391 VAL B O     1 
ATOM   8717  C  CB    . VAL B 1 391 ? 116.173 151.746 139.644 1.00 15.39 ?  391 VAL B CB    1 
ATOM   8718  C  CG1   . VAL B 1 391 ? 115.230 152.619 138.830 1.00 20.83 ?  391 VAL B CG1   1 
ATOM   8719  C  CG2   . VAL B 1 391 ? 117.001 150.849 138.737 1.00 17.46 ?  391 VAL B CG2   1 
ATOM   8720  N  N     . SER B 1 392 ? 118.790 153.578 139.127 1.00 28.78 ?  392 SER B N     1 
ATOM   8721  C  CA    . SER B 1 392 ? 119.450 154.607 138.341 1.00 21.82 ?  392 SER B CA    1 
ATOM   8722  C  C     . SER B 1 392 ? 119.104 154.444 136.868 1.00 28.18 ?  392 SER B C     1 
ATOM   8723  O  O     . SER B 1 392 ? 118.914 153.331 136.374 1.00 31.29 ?  392 SER B O     1 
ATOM   8724  C  CB    . SER B 1 392 ? 120.968 154.550 138.526 1.00 20.84 ?  392 SER B CB    1 
ATOM   8725  O  OG    . SER B 1 392 ? 121.325 154.717 139.886 1.00 30.03 ?  392 SER B OG    1 
ATOM   8726  N  N     . SER B 1 393 ? 119.020 155.571 136.171 1.00 25.65 ?  393 SER B N     1 
ATOM   8727  C  CA    . SER B 1 393 ? 118.758 155.597 134.735 1.00 23.85 ?  393 SER B CA    1 
ATOM   8728  C  C     . SER B 1 393 ? 120.077 155.924 134.040 1.00 25.99 ?  393 SER B C     1 
ATOM   8729  O  O     . SER B 1 393 ? 120.399 157.087 133.800 1.00 31.14 ?  393 SER B O     1 
ATOM   8730  C  CB    . SER B 1 393 ? 117.672 156.610 134.388 1.00 28.94 ?  393 SER B CB    1 
ATOM   8731  O  OG    . SER B 1 393 ? 116.537 156.446 135.220 1.00 31.30 ?  393 SER B OG    1 
ATOM   8732  N  N     . TYR B 1 394 ? 120.843 154.882 133.728 1.00 28.75 ?  394 TYR B N     1 
ATOM   8733  C  CA    . TYR B 1 394 ? 122.084 155.042 132.979 1.00 26.75 ?  394 TYR B CA    1 
ATOM   8734  C  C     . TYR B 1 394 ? 121.735 155.150 131.501 1.00 26.39 ?  394 TYR B C     1 
ATOM   8735  O  O     . TYR B 1 394 ? 121.293 154.173 130.886 1.00 29.18 ?  394 TYR B O     1 
ATOM   8736  C  CB    . TYR B 1 394 ? 123.026 153.875 133.247 1.00 24.95 ?  394 TYR B CB    1 
ATOM   8737  C  CG    . TYR B 1 394 ? 123.458 153.763 134.693 1.00 23.85 ?  394 TYR B CG    1 
ATOM   8738  C  CD1   . TYR B 1 394 ? 124.265 154.730 135.273 1.00 23.65 ?  394 TYR B CD1   1 
ATOM   8739  C  CD2   . TYR B 1 394 ? 123.050 152.693 135.477 1.00 25.91 ?  394 TYR B CD2   1 
ATOM   8740  C  CE1   . TYR B 1 394 ? 124.660 154.633 136.594 1.00 28.58 ?  394 TYR B CE1   1 
ATOM   8741  C  CE2   . TYR B 1 394 ? 123.438 152.586 136.797 1.00 26.75 ?  394 TYR B CE2   1 
ATOM   8742  C  CZ    . TYR B 1 394 ? 124.242 153.559 137.350 1.00 30.68 ?  394 TYR B CZ    1 
ATOM   8743  O  OH    . TYR B 1 394 ? 124.632 153.458 138.666 1.00 34.71 ?  394 TYR B OH    1 
ATOM   8744  N  N     . THR B 1 395 ? 121.919 156.333 130.934 1.00 31.26 ?  395 THR B N     1 
ATOM   8745  C  CA    . THR B 1 395 ? 121.497 156.627 129.578 1.00 30.91 ?  395 THR B CA    1 
ATOM   8746  C  C     . THR B 1 395 ? 122.637 156.356 128.600 1.00 32.44 ?  395 THR B C     1 
ATOM   8747  O  O     . THR B 1 395 ? 123.679 155.797 128.958 1.00 32.19 ?  395 THR B O     1 
ATOM   8748  C  CB    . THR B 1 395 ? 121.003 158.071 129.493 1.00 30.55 ?  395 THR B CB    1 
ATOM   8749  O  OG1   . THR B 1 395 ? 122.041 158.958 129.929 1.00 32.79 ?  395 THR B OG1   1 
ATOM   8750  C  CG2   . THR B 1 395 ? 119.781 158.265 130.375 1.00 30.29 ?  395 THR B CG2   1 
ATOM   8751  N  N     . ASP B 1 396 ? 122.440 156.752 127.346 1.00 33.29 ?  396 ASP B N     1 
ATOM   8752  C  CA    . ASP B 1 396 ? 123.457 156.564 126.326 1.00 31.68 ?  396 ASP B CA    1 
ATOM   8753  C  C     . ASP B 1 396 ? 124.666 157.451 126.603 1.00 34.49 ?  396 ASP B C     1 
ATOM   8754  O  O     . ASP B 1 396 ? 124.623 158.373 127.422 1.00 40.59 ?  396 ASP B O     1 
ATOM   8755  C  CB    . ASP B 1 396 ? 122.895 156.876 124.939 1.00 33.18 ?  396 ASP B CB    1 
ATOM   8756  C  CG    . ASP B 1 396 ? 121.793 155.924 124.526 1.00 36.09 ?  396 ASP B CG    1 
ATOM   8757  O  OD1   . ASP B 1 396 ? 121.738 154.800 125.068 1.00 39.61 ?  396 ASP B OD1   1 
ATOM   8758  O  OD2   . ASP B 1 396 ? 120.983 156.298 123.652 1.00 36.46 -1 396 ASP B OD2   1 
ATOM   8759  N  N     . TYR B 1 397 ? 125.762 157.152 125.911 1.00 32.92 ?  397 TYR B N     1 
ATOM   8760  C  CA    . TYR B 1 397 ? 126.939 158.002 125.988 1.00 32.88 ?  397 TYR B CA    1 
ATOM   8761  C  C     . TYR B 1 397 ? 126.612 159.392 125.456 1.00 38.23 ?  397 TYR B C     1 
ATOM   8762  O  O     . TYR B 1 397 ? 125.780 159.557 124.559 1.00 43.77 ?  397 TYR B O     1 
ATOM   8763  C  CB    . TYR B 1 397 ? 128.098 157.389 125.202 1.00 31.40 ?  397 TYR B CB    1 
ATOM   8764  C  CG    . TYR B 1 397 ? 129.460 157.846 125.667 1.00 31.29 ?  397 TYR B CG    1 
ATOM   8765  C  CD1   . TYR B 1 397 ? 130.016 159.026 125.193 1.00 34.49 ?  397 TYR B CD1   1 
ATOM   8766  C  CD2   . TYR B 1 397 ? 130.188 157.100 126.582 1.00 32.36 ?  397 TYR B CD2   1 
ATOM   8767  C  CE1   . TYR B 1 397 ? 131.260 159.448 125.615 1.00 33.49 ?  397 TYR B CE1   1 
ATOM   8768  C  CE2   . TYR B 1 397 ? 131.434 157.513 127.009 1.00 29.46 ?  397 TYR B CE2   1 
ATOM   8769  C  CZ    . TYR B 1 397 ? 131.964 158.688 126.524 1.00 31.74 ?  397 TYR B CZ    1 
ATOM   8770  O  OH    . TYR B 1 397 ? 133.204 159.106 126.946 1.00 35.13 ?  397 TYR B OH    1 
ATOM   8771  N  N     . ASP B 1 398 ? 127.261 160.400 126.041 1.00 35.77 ?  398 ASP B N     1 
ATOM   8772  C  CA    . ASP B 1 398 ? 127.025 161.820 125.788 1.00 40.56 ?  398 ASP B CA    1 
ATOM   8773  C  C     . ASP B 1 398 ? 125.667 162.282 126.295 1.00 41.34 ?  398 ASP B C     1 
ATOM   8774  O  O     . ASP B 1 398 ? 125.235 163.395 125.967 1.00 39.21 ?  398 ASP B O     1 
ATOM   8775  C  CB    . ASP B 1 398 ? 127.166 162.177 124.302 1.00 39.07 ?  398 ASP B CB    1 
ATOM   8776  C  CG    . ASP B 1 398 ? 128.467 162.890 123.996 1.00 44.22 ?  398 ASP B CG    1 
ATOM   8777  O  OD1   . ASP B 1 398 ? 128.565 163.511 122.916 1.00 42.46 ?  398 ASP B OD1   1 
ATOM   8778  O  OD2   . ASP B 1 398 ? 129.392 162.830 124.832 1.00 45.23 -1 398 ASP B OD2   1 
ATOM   8779  N  N     . GLU B 1 399 ? 124.980 161.463 127.086 1.00 44.70 ?  399 GLU B N     1 
ATOM   8780  C  CA    . GLU B 1 399 ? 123.723 161.831 127.719 1.00 41.11 ?  399 GLU B CA    1 
ATOM   8781  C  C     . GLU B 1 399 ? 123.882 161.734 129.228 1.00 44.21 ?  399 GLU B C     1 
ATOM   8782  O  O     . GLU B 1 399 ? 124.547 160.824 129.735 1.00 39.66 ?  399 GLU B O     1 
ATOM   8783  C  CB    . GLU B 1 399 ? 122.575 160.929 127.252 1.00 37.86 ?  399 GLU B CB    1 
ATOM   8784  C  CG    . GLU B 1 399 ? 122.261 161.040 125.770 1.00 43.97 ?  399 GLU B CG    1 
ATOM   8785  C  CD    . GLU B 1 399 ? 121.622 162.366 125.408 1.00 47.43 ?  399 GLU B CD    1 
ATOM   8786  O  OE1   . GLU B 1 399 ? 120.751 162.837 126.169 1.00 47.85 ?  399 GLU B OE1   1 
ATOM   8787  O  OE2   . GLU B 1 399 ? 121.991 162.939 124.360 1.00 46.53 -1 399 GLU B OE2   1 
ATOM   8788  N  N     . GLU B 1 400 ? 123.277 162.677 129.945 1.00 45.70 ?  400 GLU B N     1 
ATOM   8789  C  CA    . GLU B 1 400 ? 123.370 162.684 131.398 1.00 39.54 ?  400 GLU B CA    1 
ATOM   8790  C  C     . GLU B 1 400 ? 122.599 161.509 131.983 1.00 40.22 ?  400 GLU B C     1 
ATOM   8791  O  O     . GLU B 1 400 ? 121.474 161.217 131.564 1.00 39.36 ?  400 GLU B O     1 
ATOM   8792  C  CB    . GLU B 1 400 ? 122.837 164.000 131.959 1.00 40.02 ?  400 GLU B CB    1 
ATOM   8793  C  CG    . GLU B 1 400 ? 123.852 165.130 131.953 1.00 44.35 ?  400 GLU B CG    1 
ATOM   8794  C  CD    . GLU B 1 400 ? 125.166 164.737 132.596 1.00 47.31 ?  400 GLU B CD    1 
ATOM   8795  O  OE1   . GLU B 1 400 ? 125.162 164.390 133.795 1.00 46.59 ?  400 GLU B OE1   1 
ATOM   8796  O  OE2   . GLU B 1 400 ? 126.204 164.774 131.903 1.00 45.60 -1 400 GLU B OE2   1 
ATOM   8797  N  N     . ASP B 1 401 ? 123.207 160.833 132.954 1.00 35.64 ?  401 ASP B N     1 
ATOM   8798  C  CA    . ASP B 1 401 ? 122.572 159.712 133.631 1.00 31.88 ?  401 ASP B CA    1 
ATOM   8799  C  C     . ASP B 1 401 ? 121.821 160.198 134.862 1.00 32.92 ?  401 ASP B C     1 
ATOM   8800  O  O     . ASP B 1 401 ? 122.283 161.094 135.573 1.00 38.51 ?  401 ASP B O     1 
ATOM   8801  C  CB    . ASP B 1 401 ? 123.610 158.665 134.037 1.00 31.73 ?  401 ASP B CB    1 
ATOM   8802  C  CG    . ASP B 1 401 ? 124.425 158.164 132.863 1.00 36.42 ?  401 ASP B CG    1 
ATOM   8803  O  OD1   . ASP B 1 401 ? 123.964 158.304 131.711 1.00 38.79 ?  401 ASP B OD1   1 
ATOM   8804  O  OD2   . ASP B 1 401 ? 125.528 157.628 133.092 1.00 38.06 -1 401 ASP B OD2   1 
ATOM   8805  N  N     . GLU B 1 402 ? 120.658 159.601 135.108 1.00 29.52 ?  402 GLU B N     1 
ATOM   8806  C  CA    . GLU B 1 402 ? 119.888 159.870 136.321 1.00 27.64 ?  402 GLU B CA    1 
ATOM   8807  C  C     . GLU B 1 402 ? 120.378 158.908 137.395 1.00 29.15 ?  402 GLU B C     1 
ATOM   8808  O  O     . GLU B 1 402 ? 120.052 157.720 137.378 1.00 30.97 ?  402 GLU B O     1 
ATOM   8809  C  CB    . GLU B 1 402 ? 118.394 159.718 136.063 1.00 29.73 ?  402 GLU B CB    1 
ATOM   8810  C  CG    . GLU B 1 402 ? 117.797 160.812 135.194 1.00 33.82 ?  402 GLU B CG    1 
ATOM   8811  C  CD    . GLU B 1 402 ? 118.292 162.195 135.572 1.00 39.10 ?  402 GLU B CD    1 
ATOM   8812  O  OE1   . GLU B 1 402 ? 117.905 162.693 136.650 1.00 35.36 ?  402 GLU B OE1   1 
ATOM   8813  O  OE2   . GLU B 1 402 ? 119.070 162.783 134.793 1.00 36.60 -1 402 GLU B OE2   1 
ATOM   8814  N  N     . ILE B 1 403 ? 121.165 159.425 138.331 1.00 29.66 ?  403 ILE B N     1 
ATOM   8815  C  CA    . ILE B 1 403 ? 121.807 158.605 139.352 1.00 24.05 ?  403 ILE B CA    1 
ATOM   8816  C  C     . ILE B 1 403 ? 120.830 158.397 140.501 1.00 25.63 ?  403 ILE B C     1 
ATOM   8817  O  O     . ILE B 1 403 ? 120.332 159.362 141.090 1.00 30.61 ?  403 ILE B O     1 
ATOM   8818  C  CB    . ILE B 1 403 ? 123.109 159.254 139.844 1.00 21.38 ?  403 ILE B CB    1 
ATOM   8819  C  CG1   . ILE B 1 403 ? 124.140 159.298 138.715 1.00 23.71 ?  403 ILE B CG1   1 
ATOM   8820  C  CG2   . ILE B 1 403 ? 123.658 158.503 141.041 1.00 20.95 ?  403 ILE B CG2   1 
ATOM   8821  C  CD1   . ILE B 1 403 ? 124.358 157.967 138.035 1.00 27.98 ?  403 ILE B CD1   1 
ATOM   8822  N  N     . GLY B 1 404 ? 120.558 157.139 140.819 1.00 22.24 ?  404 GLY B N     1 
ATOM   8823  C  CA    . GLY B 1 404 ? 119.680 156.777 141.913 1.00 10.85 ?  404 GLY B CA    1 
ATOM   8824  C  C     . GLY B 1 404 ? 120.438 156.507 143.193 1.00 19.17 ?  404 GLY B C     1 
ATOM   8825  O  O     . GLY B 1 404 ? 121.496 157.086 143.455 1.00 26.62 ?  404 GLY B O     1 
ATOM   8826  N  N     . LEU B 1 405 ? 119.889 155.609 144.004 1.00 23.93 ?  405 LEU B N     1 
ATOM   8827  C  CA    . LEU B 1 405 ? 120.479 155.236 145.283 1.00 10.66 ?  405 LEU B CA    1 
ATOM   8828  C  C     . LEU B 1 405 ? 120.758 153.740 145.281 1.00 13.07 ?  405 LEU B C     1 
ATOM   8829  O  O     . LEU B 1 405 ? 119.828 152.934 145.176 1.00 14.56 ?  405 LEU B O     1 
ATOM   8830  C  CB    . LEU B 1 405 ? 119.554 155.608 146.443 1.00 17.18 ?  405 LEU B CB    1 
ATOM   8831  C  CG    . LEU B 1 405 ? 119.198 157.088 146.588 1.00 17.59 ?  405 LEU B CG    1 
ATOM   8832  C  CD1   . LEU B 1 405 ? 118.012 157.260 147.518 1.00 20.83 ?  405 LEU B CD1   1 
ATOM   8833  C  CD2   . LEU B 1 405 ? 120.388 157.889 147.085 1.00 16.71 ?  405 LEU B CD2   1 
ATOM   8834  N  N     . ASP B 1 406 ? 122.030 153.374 145.398 1.00 24.08 ?  406 ASP B N     1 
ATOM   8835  C  CA    . ASP B 1 406 ? 122.445 151.982 145.508 1.00 17.26 ?  406 ASP B CA    1 
ATOM   8836  C  C     . ASP B 1 406 ? 122.965 151.732 146.915 1.00 18.11 ?  406 ASP B C     1 
ATOM   8837  O  O     . ASP B 1 406 ? 123.877 152.423 147.378 1.00 27.75 ?  406 ASP B O     1 
ATOM   8838  C  CB    . ASP B 1 406 ? 123.517 151.638 144.474 1.00 17.89 ?  406 ASP B CB    1 
ATOM   8839  C  CG    . ASP B 1 406 ? 122.930 151.231 143.138 1.00 29.59 ?  406 ASP B CG    1 
ATOM   8840  O  OD1   . ASP B 1 406 ? 121.711 150.965 143.076 1.00 31.46 ?  406 ASP B OD1   1 
ATOM   8841  O  OD2   . ASP B 1 406 ? 123.688 151.173 142.148 1.00 31.03 -1 406 ASP B OD2   1 
ATOM   8842  N  N     . ILE B 1 407 ? 122.396 150.728 147.582 1.00 18.55 ?  407 ILE B N     1 
ATOM   8843  C  CA    . ILE B 1 407 ? 122.633 150.537 149.006 1.00 14.68 ?  407 ILE B CA    1 
ATOM   8844  C  C     . ILE B 1 407 ? 124.089 150.167 149.267 1.00 15.53 ?  407 ILE B C     1 
ATOM   8845  O  O     . ILE B 1 407 ? 124.723 149.428 148.500 1.00 21.25 ?  407 ILE B O     1 
ATOM   8846  C  CB    . ILE B 1 407 ? 121.680 149.465 149.561 1.00 15.58 ?  407 ILE B CB    1 
ATOM   8847  C  CG1   . ILE B 1 407 ? 120.226 149.829 149.263 1.00 3.84  ?  407 ILE B CG1   1 
ATOM   8848  C  CG2   . ILE B 1 407 ? 121.884 149.287 151.042 1.00 13.32 ?  407 ILE B CG2   1 
ATOM   8849  C  CD1   . ILE B 1 407 ? 119.336 148.628 149.096 1.00 11.74 ?  407 ILE B CD1   1 
ATOM   8850  N  N     . SER B 1 408 ? 124.624 150.695 150.366 1.00 26.34 ?  408 SER B N     1 
ATOM   8851  C  CA    . SER B 1 408 ? 125.960 150.360 150.843 1.00 23.56 ?  408 SER B CA    1 
ATOM   8852  C  C     . SER B 1 408 ? 126.057 150.799 152.294 1.00 27.78 ?  408 SER B C     1 
ATOM   8853  O  O     . SER B 1 408 ? 125.776 151.959 152.608 1.00 38.28 ?  408 SER B O     1 
ATOM   8854  C  CB    . SER B 1 408 ? 127.039 151.046 149.998 1.00 29.16 ?  408 SER B CB    1 
ATOM   8855  O  OG    . SER B 1 408 ? 128.173 151.366 150.782 1.00 27.58 ?  408 SER B OG    1 
ATOM   8856  N  N     . CYS B 1 409 ? 126.438 149.878 153.176 1.00 23.83 ?  409 CYS B N     1 
ATOM   8857  C  CA    . CYS B 1 409 ? 126.587 150.190 154.589 1.00 30.39 ?  409 CYS B CA    1 
ATOM   8858  C  C     . CYS B 1 409 ? 127.869 149.568 155.123 1.00 28.90 ?  409 CYS B C     1 
ATOM   8859  O  O     . CYS B 1 409 ? 128.383 148.585 154.584 1.00 26.96 ?  409 CYS B O     1 
ATOM   8860  C  CB    . CYS B 1 409 ? 125.382 149.708 155.412 1.00 25.10 ?  409 CYS B CB    1 
ATOM   8861  S  SG    . CYS B 1 409 ? 125.337 147.935 155.738 1.00 45.46 ?  409 CYS B SG    1 
ATOM   8862  N  N     . ASN B 1 410 ? 128.378 150.165 156.195 1.00 22.93 ?  410 ASN B N     1 
ATOM   8863  C  CA    . ASN B 1 410 ? 129.600 149.717 156.849 1.00 20.91 ?  410 ASN B CA    1 
ATOM   8864  C  C     . ASN B 1 410 ? 129.238 148.827 158.027 1.00 25.91 ?  410 ASN B C     1 
ATOM   8865  O  O     . ASN B 1 410 ? 128.345 149.162 158.812 1.00 28.35 ?  410 ASN B O     1 
ATOM   8866  C  CB    . ASN B 1 410 ? 130.430 150.909 157.319 1.00 24.20 ?  410 ASN B CB    1 
ATOM   8867  C  CG    . ASN B 1 410 ? 130.204 152.136 156.470 1.00 32.33 ?  410 ASN B CG    1 
ATOM   8868  O  OD1   . ASN B 1 410 ? 129.614 153.114 156.924 1.00 34.43 ?  410 ASN B OD1   1 
ATOM   8869  N  ND2   . ASN B 1 410 ? 130.669 152.093 155.227 1.00 34.92 ?  410 ASN B ND2   1 
ATOM   8870  N  N     . LEU B 1 411 ? 129.928 147.701 158.146 1.00 19.65 ?  411 LEU B N     1 
ATOM   8871  C  CA    . LEU B 1 411 ? 129.613 146.700 159.151 1.00 10.94 ?  411 LEU B CA    1 
ATOM   8872  C  C     . LEU B 1 411 ? 130.506 146.860 160.375 1.00 11.69 ?  411 LEU B C     1 
ATOM   8873  O  O     . LEU B 1 411 ? 131.672 147.249 160.275 1.00 22.88 ?  411 LEU B O     1 
ATOM   8874  C  CB    . LEU B 1 411 ? 129.767 145.289 158.581 1.00 19.20 ?  411 LEU B CB    1 
ATOM   8875  C  CG    . LEU B 1 411 ? 128.602 144.659 157.816 1.00 17.67 ?  411 LEU B CG    1 
ATOM   8876  C  CD1   . LEU B 1 411 ? 128.315 145.395 156.520 1.00 18.06 ?  411 LEU B CD1   1 
ATOM   8877  C  CD2   . LEU B 1 411 ? 128.910 143.200 157.539 1.00 23.52 ?  411 LEU B CD2   1 
ATOM   8878  N  N     . GLY B 1 412 ? 129.934 146.561 161.535 1.00 17.26 ?  412 GLY B N     1 
ATOM   8879  C  CA    . GLY B 1 412 ? 130.661 146.532 162.787 1.00 11.56 ?  412 GLY B CA    1 
ATOM   8880  C  C     . GLY B 1 412 ? 129.858 145.769 163.815 1.00 10.58 ?  412 GLY B C     1 
ATOM   8881  O  O     . GLY B 1 412 ? 128.646 145.967 163.915 1.00 27.55 ?  412 GLY B O     1 
ATOM   8882  N  N     . SER B 1 413 ? 130.499 144.890 164.578 1.00 11.05 ?  413 SER B N     1 
ATOM   8883  C  CA    . SER B 1 413 ? 129.783 143.988 165.467 1.00 11.98 ?  413 SER B CA    1 
ATOM   8884  C  C     . SER B 1 413 ? 130.143 144.250 166.922 1.00 19.09 ?  413 SER B C     1 
ATOM   8885  O  O     . SER B 1 413 ? 131.317 144.406 167.266 1.00 20.96 ?  413 SER B O     1 
ATOM   8886  C  CB    . SER B 1 413 ? 130.086 142.530 165.120 1.00 13.26 ?  413 SER B CB    1 
ATOM   8887  O  OG    . SER B 1 413 ? 129.565 142.199 163.846 1.00 31.25 ?  413 SER B OG    1 
ATOM   8888  N  N     . LEU B 1 414 ? 129.127 144.283 167.774 1.00 20.36 ?  414 LEU B N     1 
ATOM   8889  C  CA    . LEU B 1 414 ? 129.336 144.298 169.210 1.00 13.08 ?  414 LEU B CA    1 
ATOM   8890  C  C     . LEU B 1 414 ? 129.557 142.876 169.702 1.00 21.50 ?  414 LEU B C     1 
ATOM   8891  O  O     . LEU B 1 414 ? 128.838 141.954 169.312 1.00 25.61 ?  414 LEU B O     1 
ATOM   8892  C  CB    . LEU B 1 414 ? 128.136 144.912 169.931 1.00 22.88 ?  414 LEU B CB    1 
ATOM   8893  C  CG    . LEU B 1 414 ? 127.607 146.249 169.419 1.00 21.75 ?  414 LEU B CG    1 
ATOM   8894  C  CD1   . LEU B 1 414 ? 126.341 146.616 170.164 1.00 22.36 ?  414 LEU B CD1   1 
ATOM   8895  C  CD2   . LEU B 1 414 ? 128.657 147.333 169.580 1.00 24.62 ?  414 LEU B CD2   1 
ATOM   8896  N  N     . ASN B 1 415 ? 130.562 142.702 170.552 1.00 29.80 ?  415 ASN B N     1 
ATOM   8897  C  CA    . ASN B 1 415 ? 130.767 141.426 171.227 1.00 27.12 ?  415 ASN B CA    1 
ATOM   8898  C  C     . ASN B 1 415 ? 129.899 141.422 172.477 1.00 25.14 ?  415 ASN B C     1 
ATOM   8899  O  O     . ASN B 1 415 ? 130.209 142.104 173.459 1.00 29.23 ?  415 ASN B O     1 
ATOM   8900  C  CB    . ASN B 1 415 ? 132.241 141.228 171.563 1.00 22.71 ?  415 ASN B CB    1 
ATOM   8901  C  CG    . ASN B 1 415 ? 132.573 139.796 171.927 1.00 28.99 ?  415 ASN B CG    1 
ATOM   8902  O  OD1   . ASN B 1 415 ? 131.842 139.143 172.668 1.00 34.87 ?  415 ASN B OD1   1 
ATOM   8903  N  ND2   . ASN B 1 415 ? 133.687 139.300 171.405 1.00 29.53 ?  415 ASN B ND2   1 
ATOM   8904  N  N     . ILE B 1 416 ? 128.809 140.653 172.438 1.00 20.40 ?  416 ILE B N     1 
ATOM   8905  C  CA    . ILE B 1 416 ? 127.798 140.727 173.491 1.00 23.03 ?  416 ILE B CA    1 
ATOM   8906  C  C     . ILE B 1 416 ? 128.391 140.338 174.838 1.00 30.00 ?  416 ILE B C     1 
ATOM   8907  O  O     . ILE B 1 416 ? 128.123 140.983 175.859 1.00 30.28 ?  416 ILE B O     1 
ATOM   8908  C  CB    . ILE B 1 416 ? 126.587 139.850 173.122 1.00 22.35 ?  416 ILE B CB    1 
ATOM   8909  C  CG1   . ILE B 1 416 ? 125.845 140.462 171.931 1.00 22.82 ?  416 ILE B CG1   1 
ATOM   8910  C  CG2   . ILE B 1 416 ? 125.651 139.701 174.304 1.00 17.29 ?  416 ILE B CG2   1 
ATOM   8911  C  CD1   . ILE B 1 416 ? 124.725 139.605 171.394 1.00 21.61 ?  416 ILE B CD1   1 
ATOM   8912  N  N     . LEU B 1 417 ? 129.216 139.288 174.864 1.00 24.98 ?  417 LEU B N     1 
ATOM   8913  C  CA    . LEU B 1 417 ? 129.821 138.855 176.119 1.00 27.55 ?  417 LEU B CA    1 
ATOM   8914  C  C     . LEU B 1 417 ? 130.715 139.939 176.706 1.00 28.75 ?  417 LEU B C     1 
ATOM   8915  O  O     . LEU B 1 417 ? 130.625 140.256 177.898 1.00 34.00 ?  417 LEU B O     1 
ATOM   8916  C  CB    . LEU B 1 417 ? 130.615 137.567 175.899 1.00 28.61 ?  417 LEU B CB    1 
ATOM   8917  C  CG    . LEU B 1 417 ? 131.240 136.952 177.151 1.00 29.91 ?  417 LEU B CG    1 
ATOM   8918  C  CD1   . LEU B 1 417 ? 130.697 135.558 177.381 1.00 27.31 ?  417 LEU B CD1   1 
ATOM   8919  C  CD2   . LEU B 1 417 ? 132.754 136.927 177.034 1.00 32.64 ?  417 LEU B CD2   1 
ATOM   8920  N  N     . ASN B 1 418 ? 131.577 140.532 175.878 1.00 34.08 ?  418 ASN B N     1 
ATOM   8921  C  CA    . ASN B 1 418 ? 132.486 141.558 176.375 1.00 29.41 ?  418 ASN B CA    1 
ATOM   8922  C  C     . ASN B 1 418 ? 131.756 142.857 176.684 1.00 29.20 ?  418 ASN B C     1 
ATOM   8923  O  O     . ASN B 1 418 ? 132.120 143.560 177.634 1.00 35.03 ?  418 ASN B O     1 
ATOM   8924  C  CB    . ASN B 1 418 ? 133.605 141.798 175.364 1.00 27.06 ?  418 ASN B CB    1 
ATOM   8925  C  CG    . ASN B 1 418 ? 134.539 140.613 175.244 1.00 28.65 ?  418 ASN B CG    1 
ATOM   8926  O  OD1   . ASN B 1 418 ? 134.873 139.971 176.238 1.00 36.71 ?  418 ASN B OD1   1 
ATOM   8927  N  ND2   . ASN B 1 418 ? 134.964 140.313 174.023 1.00 30.28 ?  418 ASN B ND2   1 
ATOM   8928  N  N     . VAL B 1 419 ? 130.733 143.197 175.897 1.00 31.16 ?  419 VAL B N     1 
ATOM   8929  C  CA    . VAL B 1 419 ? 129.968 144.413 176.154 1.00 31.46 ?  419 VAL B CA    1 
ATOM   8930  C  C     . VAL B 1 419 ? 129.223 144.308 177.479 1.00 29.36 ?  419 VAL B C     1 
ATOM   8931  O  O     . VAL B 1 419 ? 129.225 145.245 178.286 1.00 36.08 ?  419 VAL B O     1 
ATOM   8932  C  CB    . VAL B 1 419 ? 129.011 144.700 174.982 1.00 26.47 ?  419 VAL B CB    1 
ATOM   8933  C  CG1   . VAL B 1 419 ? 127.927 145.663 175.405 1.00 28.15 ?  419 VAL B CG1   1 
ATOM   8934  C  CG2   . VAL B 1 419 ? 129.778 145.264 173.804 1.00 25.84 ?  419 VAL B CG2   1 
ATOM   8935  N  N     . MET B 1 420 ? 128.580 143.165 177.731 1.00 31.99 ?  420 MET B N     1 
ATOM   8936  C  CA    . MET B 1 420 ? 127.822 143.012 178.967 1.00 34.66 ?  420 MET B CA    1 
ATOM   8937  C  C     . MET B 1 420 ? 128.722 142.771 180.172 1.00 33.26 ?  420 MET B C     1 
ATOM   8938  O  O     . MET B 1 420 ? 128.364 143.160 181.289 1.00 35.93 ?  420 MET B O     1 
ATOM   8939  C  CB    . MET B 1 420 ? 126.804 141.880 178.832 1.00 32.45 ?  420 MET B CB    1 
ATOM   8940  C  CG    . MET B 1 420 ? 125.742 142.140 177.781 1.00 30.51 ?  420 MET B CG    1 
ATOM   8941  S  SD    . MET B 1 420 ? 124.206 142.762 178.487 1.00 43.53 ?  420 MET B SD    1 
ATOM   8942  C  CE    . MET B 1 420 ? 124.036 141.726 179.934 1.00 31.04 ?  420 MET B CE    1 
ATOM   8943  N  N     . GLU B 1 421 ? 129.878 142.134 179.976 1.00 37.77 ?  421 GLU B N     1 
ATOM   8944  C  CA    . GLU B 1 421 ? 130.825 141.973 181.074 1.00 34.78 ?  421 GLU B CA    1 
ATOM   8945  C  C     . GLU B 1 421 ? 131.346 143.323 181.546 1.00 38.51 ?  421 GLU B C     1 
ATOM   8946  O  O     . GLU B 1 421 ? 131.503 143.553 182.751 1.00 41.72 ?  421 GLU B O     1 
ATOM   8947  C  CB    . GLU B 1 421 ? 131.977 141.066 180.642 1.00 34.46 ?  421 GLU B CB    1 
ATOM   8948  C  CG    . GLU B 1 421 ? 133.222 141.180 181.504 1.00 42.35 ?  421 GLU B CG    1 
ATOM   8949  C  CD    . GLU B 1 421 ? 134.495 141.220 180.682 1.00 44.83 ?  421 GLU B CD    1 
ATOM   8950  O  OE1   . GLU B 1 421 ? 134.403 141.135 179.438 1.00 43.17 ?  421 GLU B OE1   1 
ATOM   8951  O  OE2   . GLU B 1 421 ? 135.586 141.338 181.278 1.00 41.27 -1 421 GLU B OE2   1 
ATOM   8952  N  N     . HIS B 1 422 ? 131.608 144.234 180.612 1.00 34.24 ?  422 HIS B N     1 
ATOM   8953  C  CA    . HIS B 1 422 ? 132.056 145.579 180.946 1.00 35.44 ?  422 HIS B CA    1 
ATOM   8954  C  C     . HIS B 1 422 ? 130.908 146.512 181.307 1.00 38.64 ?  422 HIS B C     1 
ATOM   8955  O  O     . HIS B 1 422 ? 131.169 147.658 181.687 1.00 41.12 ?  422 HIS B O     1 
ATOM   8956  C  CB    . HIS B 1 422 ? 132.853 146.169 179.779 1.00 32.69 ?  422 HIS B CB    1 
ATOM   8957  C  CG    . HIS B 1 422 ? 134.168 145.493 179.543 1.00 35.81 ?  422 HIS B CG    1 
ATOM   8958  N  ND1   . HIS B 1 422 ? 134.302 144.394 178.722 1.00 36.57 ?  422 HIS B ND1   1 
ATOM   8959  C  CD2   . HIS B 1 422 ? 135.405 145.759 180.022 1.00 37.01 ?  422 HIS B CD2   1 
ATOM   8960  C  CE1   . HIS B 1 422 ? 135.566 144.012 178.705 1.00 39.80 ?  422 HIS B CE1   1 
ATOM   8961  N  NE2   . HIS B 1 422 ? 136.256 144.823 179.486 1.00 39.81 ?  422 HIS B NE2   1 
ATOM   8962  N  N     . LYS B 1 423 ? 129.660 146.049 181.202 1.00 40.97 ?  423 LYS B N     1 
ATOM   8963  C  CA    . LYS B 1 423 ? 128.482 146.858 181.522 1.00 42.37 ?  423 LYS B CA    1 
ATOM   8964  C  C     . LYS B 1 423 ? 128.494 148.174 180.749 1.00 43.69 ?  423 LYS B C     1 
ATOM   8965  O  O     . LYS B 1 423 ? 128.219 149.244 181.295 1.00 46.33 ?  423 LYS B O     1 
ATOM   8966  C  CB    . LYS B 1 423 ? 128.383 147.110 183.027 1.00 40.41 ?  423 LYS B CB    1 
ATOM   8967  C  CG    . LYS B 1 423 ? 127.883 145.921 183.827 1.00 42.43 ?  423 LYS B CG    1 
ATOM   8968  C  CD    . LYS B 1 423 ? 127.994 146.179 185.320 1.00 43.32 ?  423 LYS B CD    1 
ATOM   8969  C  CE    . LYS B 1 423 ? 129.168 145.423 185.925 1.00 45.85 ?  423 LYS B CE    1 
ATOM   8970  N  NZ    . LYS B 1 423 ? 128.730 144.447 186.961 1.00 43.92 1  423 LYS B NZ    1 
ATOM   8971  N  N     . SER B 1 424 ? 128.813 148.091 179.462 1.00 31.73 ?  424 SER B N     1 
ATOM   8972  C  CA    . SER B 1 424 ? 129.059 149.265 178.634 1.00 33.97 ?  424 SER B CA    1 
ATOM   8973  C  C     . SER B 1 424 ? 128.312 149.165 177.313 1.00 34.09 ?  424 SER B C     1 
ATOM   8974  O  O     . SER B 1 424 ? 128.877 149.375 176.239 1.00 32.55 ?  424 SER B O     1 
ATOM   8975  C  CB    . SER B 1 424 ? 130.552 149.441 178.386 1.00 35.65 ?  424 SER B CB    1 
ATOM   8976  O  OG    . SER B 1 424 ? 131.039 148.429 177.523 1.00 32.02 ?  424 SER B OG    1 
ATOM   8977  N  N     . ILE B 1 425 ? 127.021 148.833 177.371 1.00 33.46 ?  425 ILE B N     1 
ATOM   8978  C  CA    . ILE B 1 425 ? 126.212 148.821 176.154 1.00 26.93 ?  425 ILE B CA    1 
ATOM   8979  C  C     . ILE B 1 425 ? 126.177 150.211 175.533 1.00 32.03 ?  425 ILE B C     1 
ATOM   8980  O  O     . ILE B 1 425 ? 126.410 150.381 174.331 1.00 35.69 ?  425 ILE B O     1 
ATOM   8981  C  CB    . ILE B 1 425 ? 124.793 148.303 176.449 1.00 32.10 ?  425 ILE B CB    1 
ATOM   8982  C  CG1   . ILE B 1 425 ? 124.796 146.786 176.635 1.00 32.37 ?  425 ILE B CG1   1 
ATOM   8983  C  CG2   . ILE B 1 425 ? 123.841 148.684 175.326 1.00 27.48 ?  425 ILE B CG2   1 
ATOM   8984  C  CD1   . ILE B 1 425 ? 123.460 146.230 177.069 1.00 33.35 ?  425 ILE B CD1   1 
ATOM   8985  N  N     . GLU B 1 426 ? 125.910 151.230 176.354 1.00 27.69 ?  426 GLU B N     1 
ATOM   8986  C  CA    . GLU B 1 426 ? 125.767 152.587 175.836 1.00 23.51 ?  426 GLU B CA    1 
ATOM   8987  C  C     . GLU B 1 426 ? 127.064 153.084 175.210 1.00 26.23 ?  426 GLU B C     1 
ATOM   8988  O  O     . GLU B 1 426 ? 127.076 153.541 174.061 1.00 34.59 ?  426 GLU B O     1 
ATOM   8989  C  CB    . GLU B 1 426 ? 125.319 153.525 176.956 1.00 26.59 ?  426 GLU B CB    1 
ATOM   8990  C  CG    . GLU B 1 426 ? 125.513 154.997 176.641 1.00 29.01 ?  426 GLU B CG    1 
ATOM   8991  C  CD    . GLU B 1 426 ? 125.037 155.900 177.758 1.00 33.93 ?  426 GLU B CD    1 
ATOM   8992  O  OE1   . GLU B 1 426 ? 124.692 155.381 178.840 1.00 33.66 ?  426 GLU B OE1   1 
ATOM   8993  O  OE2   . GLU B 1 426 ? 125.008 157.133 177.556 1.00 36.80 -1 426 GLU B OE2   1 
ATOM   8994  N  N     . LYS B 1 427 ? 128.169 153.004 175.956 1.00 33.18 ?  427 LYS B N     1 
ATOM   8995  C  CA    . LYS B 1 427 ? 129.433 153.538 175.461 1.00 27.99 ?  427 LYS B CA    1 
ATOM   8996  C  C     . LYS B 1 427 ? 129.901 152.792 174.220 1.00 28.32 ?  427 LYS B C     1 
ATOM   8997  O  O     . LYS B 1 427 ? 130.342 153.411 173.243 1.00 32.78 ?  427 LYS B O     1 
ATOM   8998  C  CB    . LYS B 1 427 ? 130.493 153.478 176.561 1.00 28.87 ?  427 LYS B CB    1 
ATOM   8999  C  CG    . LYS B 1 427 ? 131.908 153.746 176.078 1.00 32.24 ?  427 LYS B CG    1 
ATOM   9000  C  CD    . LYS B 1 427 ? 132.928 153.490 177.174 1.00 33.02 ?  427 LYS B CD    1 
ATOM   9001  C  CE    . LYS B 1 427 ? 132.942 152.031 177.597 1.00 31.84 ?  427 LYS B CE    1 
ATOM   9002  N  NZ    . LYS B 1 427 ? 132.866 151.108 176.432 1.00 33.99 1  427 LYS B NZ    1 
ATOM   9003  N  N     . THR B 1 428 ? 129.802 151.461 174.234 1.00 30.09 ?  428 THR B N     1 
ATOM   9004  C  CA    . THR B 1 428 ? 130.224 150.679 173.079 1.00 24.75 ?  428 THR B CA    1 
ATOM   9005  C  C     . THR B 1 428 ? 129.367 150.990 171.861 1.00 24.98 ?  428 THR B C     1 
ATOM   9006  O  O     . THR B 1 428 ? 129.891 151.141 170.753 1.00 32.34 ?  428 THR B O     1 
ATOM   9007  C  CB    . THR B 1 428 ? 130.171 149.186 173.396 1.00 24.64 ?  428 THR B CB    1 
ATOM   9008  O  OG1   . THR B 1 428 ? 130.819 148.940 174.650 1.00 26.31 ?  428 THR B OG1   1 
ATOM   9009  C  CG2   . THR B 1 428 ? 130.869 148.393 172.307 1.00 25.22 ?  428 THR B CG2   1 
ATOM   9010  N  N     . VAL B 1 429 ? 128.049 151.095 172.045 1.00 23.05 ?  429 VAL B N     1 
ATOM   9011  C  CA    . VAL B 1 429 ? 127.168 151.381 170.917 1.00 22.40 ?  429 VAL B CA    1 
ATOM   9012  C  C     . VAL B 1 429 ? 127.478 152.752 170.332 1.00 27.00 ?  429 VAL B C     1 
ATOM   9013  O  O     . VAL B 1 429 ? 127.569 152.912 169.109 1.00 28.05 ?  429 VAL B O     1 
ATOM   9014  C  CB    . VAL B 1 429 ? 125.692 151.263 171.340 1.00 25.19 ?  429 VAL B CB    1 
ATOM   9015  C  CG1   . VAL B 1 429 ? 124.799 151.948 170.327 1.00 22.74 ?  429 VAL B CG1   1 
ATOM   9016  C  CG2   . VAL B 1 429 ? 125.296 149.806 171.470 1.00 26.03 ?  429 VAL B CG2   1 
ATOM   9017  N  N     . LYS B 1 430 ? 127.652 153.763 171.188 1.00 25.79 ?  430 LYS B N     1 
ATOM   9018  C  CA    . LYS B 1 430 ? 127.924 155.106 170.681 1.00 20.82 ?  430 LYS B CA    1 
ATOM   9019  C  C     . LYS B 1 430 ? 129.273 155.177 169.974 1.00 23.73 ?  430 LYS B C     1 
ATOM   9020  O  O     . LYS B 1 430 ? 129.386 155.789 168.904 1.00 30.67 ?  430 LYS B O     1 
ATOM   9021  C  CB    . LYS B 1 430 ? 127.854 156.126 171.819 1.00 23.66 ?  430 LYS B CB    1 
ATOM   9022  C  CG    . LYS B 1 430 ? 126.539 156.110 172.578 1.00 25.85 ?  430 LYS B CG    1 
ATOM   9023  C  CD    . LYS B 1 430 ? 125.831 157.448 172.532 1.00 27.12 ?  430 LYS B CD    1 
ATOM   9024  C  CE    . LYS B 1 430 ? 124.695 157.493 173.537 1.00 29.17 ?  430 LYS B CE    1 
ATOM   9025  N  NZ    . LYS B 1 430 ? 124.200 158.878 173.760 1.00 32.65 1  430 LYS B NZ    1 
ATOM   9026  N  N     . LEU B 1 431 ? 130.306 154.552 170.545 1.00 25.57 ?  431 LEU B N     1 
ATOM   9027  C  CA    . LEU B 1 431 ? 131.617 154.575 169.904 1.00 21.63 ?  431 LEU B CA    1 
ATOM   9028  C  C     . LEU B 1 431 ? 131.608 153.806 168.588 1.00 24.56 ?  431 LEU B C     1 
ATOM   9029  O  O     . LEU B 1 431 ? 132.241 154.228 167.612 1.00 28.94 ?  431 LEU B O     1 
ATOM   9030  C  CB    . LEU B 1 431 ? 132.672 154.012 170.853 1.00 26.72 ?  431 LEU B CB    1 
ATOM   9031  C  CG    . LEU B 1 431 ? 133.380 155.023 171.753 1.00 29.74 ?  431 LEU B CG    1 
ATOM   9032  C  CD1   . LEU B 1 431 ? 134.261 154.309 172.761 1.00 27.85 ?  431 LEU B CD1   1 
ATOM   9033  C  CD2   . LEU B 1 431 ? 134.192 156.002 170.922 1.00 28.68 ?  431 LEU B CD2   1 
ATOM   9034  N  N     . ALA B 1 432 ? 130.899 152.676 168.539 1.00 26.78 ?  432 ALA B N     1 
ATOM   9035  C  CA    . ALA B 1 432 ? 130.784 151.924 167.295 1.00 15.82 ?  432 ALA B CA    1 
ATOM   9036  C  C     . ALA B 1 432 ? 130.027 152.718 166.241 1.00 25.44 ?  432 ALA B C     1 
ATOM   9037  O  O     . ALA B 1 432 ? 130.381 152.687 165.058 1.00 27.92 ?  432 ALA B O     1 
ATOM   9038  C  CB    . ALA B 1 432 ? 130.096 150.587 167.557 1.00 17.76 ?  432 ALA B CB    1 
ATOM   9039  N  N     . THR B 1 433 ? 128.975 153.429 166.651 1.00 25.72 ?  433 THR B N     1 
ATOM   9040  C  CA    . THR B 1 433 ? 128.249 154.282 165.718 1.00 19.97 ?  433 THR B CA    1 
ATOM   9041  C  C     . THR B 1 433 ? 129.150 155.383 165.175 1.00 23.21 ?  433 THR B C     1 
ATOM   9042  O  O     . THR B 1 433 ? 129.112 155.691 163.979 1.00 32.64 ?  433 THR B O     1 
ATOM   9043  C  CB    . THR B 1 433 ? 127.020 154.881 166.403 1.00 22.90 ?  433 THR B CB    1 
ATOM   9044  O  OG1   . THR B 1 433 ? 126.194 153.826 166.909 1.00 31.80 ?  433 THR B OG1   1 
ATOM   9045  C  CG2   . THR B 1 433 ? 126.213 155.721 165.424 1.00 22.05 ?  433 THR B CG2   1 
ATOM   9046  N  N     . ASP B 1 434 ? 129.974 155.979 166.038 1.00 23.10 ?  434 ASP B N     1 
ATOM   9047  C  CA    . ASP B 1 434 ? 130.912 157.000 165.579 1.00 23.64 ?  434 ASP B CA    1 
ATOM   9048  C  C     . ASP B 1 434 ? 131.929 156.424 164.600 1.00 20.53 ?  434 ASP B C     1 
ATOM   9049  O  O     . ASP B 1 434 ? 132.249 157.052 163.583 1.00 25.07 ?  434 ASP B O     1 
ATOM   9050  C  CB    . ASP B 1 434 ? 131.618 157.638 166.774 1.00 26.42 ?  434 ASP B CB    1 
ATOM   9051  C  CG    . ASP B 1 434 ? 130.678 158.439 167.644 1.00 32.91 ?  434 ASP B CG    1 
ATOM   9052  O  OD1   . ASP B 1 434 ? 129.744 159.058 167.093 1.00 34.35 ?  434 ASP B OD1   1 
ATOM   9053  O  OD2   . ASP B 1 434 ? 130.871 158.452 168.877 1.00 33.39 -1 434 ASP B OD2   1 
ATOM   9054  N  N     . SER B 1 435 ? 132.452 155.232 164.893 1.00 23.60 ?  435 SER B N     1 
ATOM   9055  C  CA    . SER B 1 435 ? 133.421 154.608 163.996 1.00 18.43 ?  435 SER B CA    1 
ATOM   9056  C  C     . SER B 1 435 ? 132.797 154.277 162.644 1.00 22.69 ?  435 SER B C     1 
ATOM   9057  O  O     . SER B 1 435 ? 133.422 154.484 161.597 1.00 32.06 ?  435 SER B O     1 
ATOM   9058  C  CB    . SER B 1 435 ? 133.999 153.350 164.642 1.00 22.49 ?  435 SER B CB    1 
ATOM   9059  O  OG    . SER B 1 435 ? 133.051 152.298 164.649 1.00 23.75 ?  435 SER B OG    1 
ATOM   9060  N  N     . LEU B 1 436 ? 131.565 153.766 162.645 1.00 21.95 ?  436 LEU B N     1 
ATOM   9061  C  CA    . LEU B 1 436 ? 130.893 153.455 161.388 1.00 13.09 ?  436 LEU B CA    1 
ATOM   9062  C  C     . LEU B 1 436 ? 130.560 154.723 160.612 1.00 18.56 ?  436 LEU B C     1 
ATOM   9063  O  O     . LEU B 1 436 ? 130.630 154.739 159.377 1.00 23.01 ?  436 LEU B O     1 
ATOM   9064  C  CB    . LEU B 1 436 ? 129.632 152.635 161.660 1.00 22.43 ?  436 LEU B CB    1 
ATOM   9065  C  CG    . LEU B 1 436 ? 129.862 151.239 162.242 1.00 21.08 ?  436 LEU B CG    1 
ATOM   9066  C  CD1   . LEU B 1 436 ? 128.577 150.677 162.824 1.00 18.38 ?  436 LEU B CD1   1 
ATOM   9067  C  CD2   . LEU B 1 436 ? 130.430 150.307 161.189 1.00 18.57 ?  436 LEU B CD2   1 
ATOM   9068  N  N     . THR B 1 437 ? 130.202 155.796 161.319 1.00 21.16 ?  437 THR B N     1 
ATOM   9069  C  CA    . THR B 1 437 ? 129.985 157.079 160.662 1.00 20.15 ?  437 THR B CA    1 
ATOM   9070  C  C     . THR B 1 437 ? 131.266 157.581 160.012 1.00 22.83 ?  437 THR B C     1 
ATOM   9071  O  O     . THR B 1 437 ? 131.242 158.099 158.890 1.00 29.74 ?  437 THR B O     1 
ATOM   9072  C  CB    . THR B 1 437 ? 129.462 158.100 161.672 1.00 20.41 ?  437 THR B CB    1 
ATOM   9073  O  OG1   . THR B 1 437 ? 128.312 157.568 162.338 1.00 23.40 ?  437 THR B OG1   1 
ATOM   9074  C  CG2   . THR B 1 437 ? 129.087 159.394 160.978 1.00 20.77 ?  437 THR B CG2   1 
ATOM   9075  N  N     . HIS B 1 438 ? 132.398 157.432 160.702 1.00 21.30 ?  438 HIS B N     1 
ATOM   9076  C  CA    . HIS B 1 438 ? 133.677 157.815 160.115 1.00 21.63 ?  438 HIS B CA    1 
ATOM   9077  C  C     . HIS B 1 438 ? 133.990 156.977 158.881 1.00 23.01 ?  438 HIS B C     1 
ATOM   9078  O  O     . HIS B 1 438 ? 134.454 157.507 157.863 1.00 32.46 ?  438 HIS B O     1 
ATOM   9079  C  CB    . HIS B 1 438 ? 134.791 157.679 161.152 1.00 26.49 ?  438 HIS B CB    1 
ATOM   9080  C  CG    . HIS B 1 438 ? 136.158 157.953 160.606 1.00 27.67 ?  438 HIS B CG    1 
ATOM   9081  N  ND1   . HIS B 1 438 ? 136.646 159.230 160.432 1.00 25.54 ?  438 HIS B ND1   1 
ATOM   9082  C  CD2   . HIS B 1 438 ? 137.134 157.116 160.186 1.00 28.00 ?  438 HIS B CD2   1 
ATOM   9083  C  CE1   . HIS B 1 438 ? 137.869 159.167 159.936 1.00 30.66 ?  438 HIS B CE1   1 
ATOM   9084  N  NE2   . HIS B 1 438 ? 138.188 157.895 159.776 1.00 31.16 ?  438 HIS B NE2   1 
ATOM   9085  N  N     . VAL B 1 439 ? 133.740 155.669 158.952 1.00 21.40 ?  439 VAL B N     1 
ATOM   9086  C  CA    . VAL B 1 439 ? 134.005 154.797 157.809 1.00 19.11 ?  439 VAL B CA    1 
ATOM   9087  C  C     . VAL B 1 439 ? 133.145 155.203 156.620 1.00 28.84 ?  439 VAL B C     1 
ATOM   9088  O  O     . VAL B 1 439 ? 133.611 155.220 155.475 1.00 32.53 ?  439 VAL B O     1 
ATOM   9089  C  CB    . VAL B 1 439 ? 133.782 153.323 158.194 1.00 23.77 ?  439 VAL B CB    1 
ATOM   9090  C  CG1   . VAL B 1 439 ? 133.823 152.435 156.959 1.00 20.70 ?  439 VAL B CG1   1 
ATOM   9091  C  CG2   . VAL B 1 439 ? 134.825 152.878 159.194 1.00 21.77 ?  439 VAL B CG2   1 
ATOM   9092  N  N     . SER B 1 440 ? 131.878 155.538 156.871 1.00 24.41 ?  440 SER B N     1 
ATOM   9093  C  CA    . SER B 1 440 ? 131.013 156.019 155.799 1.00 20.03 ?  440 SER B CA    1 
ATOM   9094  C  C     . SER B 1 440 ? 131.522 157.338 155.228 1.00 25.90 ?  440 SER B C     1 
ATOM   9095  O  O     . SER B 1 440 ? 131.523 157.536 154.008 1.00 31.54 ?  440 SER B O     1 
ATOM   9096  C  CB    . SER B 1 440 ? 129.581 156.174 156.309 1.00 22.41 ?  440 SER B CB    1 
ATOM   9097  O  OG    . SER B 1 440 ? 128.683 156.430 155.243 1.00 31.27 ?  440 SER B OG    1 
ATOM   9098  N  N     . GLU B 1 441 ? 131.955 158.253 156.098 1.00 26.70 ?  441 GLU B N     1 
ATOM   9099  C  CA    . GLU B 1 441 ? 132.378 159.575 155.645 1.00 24.82 ?  441 GLU B CA    1 
ATOM   9100  C  C     . GLU B 1 441 ? 133.640 159.503 154.793 1.00 32.63 ?  441 GLU B C     1 
ATOM   9101  O  O     . GLU B 1 441 ? 133.756 160.217 153.791 1.00 40.05 ?  441 GLU B O     1 
ATOM   9102  C  CB    . GLU B 1 441 ? 132.591 160.496 156.844 1.00 27.11 ?  441 GLU B CB    1 
ATOM   9103  C  CG    . GLU B 1 441 ? 131.311 161.122 157.369 1.00 27.69 ?  441 GLU B CG    1 
ATOM   9104  C  CD    . GLU B 1 441 ? 131.385 161.457 158.846 1.00 35.39 ?  441 GLU B CD    1 
ATOM   9105  O  OE1   . GLU B 1 441 ? 132.417 161.150 159.479 1.00 37.20 ?  441 GLU B OE1   1 
ATOM   9106  O  OE2   . GLU B 1 441 ? 130.407 162.025 159.373 1.00 36.45 -1 441 GLU B OE2   1 
ATOM   9107  N  N     . THR B 1 442 ? 134.595 158.655 155.169 1.00 31.61 ?  442 THR B N     1 
ATOM   9108  C  CA    . THR B 1 442 ? 135.833 158.533 154.410 1.00 30.94 ?  442 THR B CA    1 
ATOM   9109  C  C     . THR B 1 442 ? 135.724 157.572 153.233 1.00 29.64 ?  442 THR B C     1 
ATOM   9110  O  O     . THR B 1 442 ? 136.720 157.357 152.536 1.00 34.42 ?  442 THR B O     1 
ATOM   9111  C  CB    . THR B 1 442 ? 136.989 158.096 155.318 1.00 29.54 ?  442 THR B CB    1 
ATOM   9112  O  OG1   . THR B 1 442 ? 136.928 156.681 155.537 1.00 31.14 ?  442 THR B OG1   1 
ATOM   9113  C  CG2   . THR B 1 442 ? 136.946 158.835 156.641 1.00 31.60 ?  442 THR B CG2   1 
ATOM   9114  N  N     . THR B 1 443 ? 134.552 156.992 152.994 1.00 30.24 ?  443 THR B N     1 
ATOM   9115  C  CA    . THR B 1 443 ? 134.340 156.134 151.838 1.00 34.71 ?  443 THR B CA    1 
ATOM   9116  C  C     . THR B 1 443 ? 133.924 156.979 150.642 1.00 35.60 ?  443 THR B C     1 
ATOM   9117  O  O     . THR B 1 443 ? 132.946 157.729 150.713 1.00 36.53 ?  443 THR B O     1 
ATOM   9118  C  CB    . THR B 1 443 ? 133.276 155.075 152.130 1.00 33.90 ?  443 THR B CB    1 
ATOM   9119  O  OG1   . THR B 1 443 ? 133.780 154.138 153.089 1.00 39.26 ?  443 THR B OG1   1 
ATOM   9120  C  CG2   . THR B 1 443 ? 132.902 154.337 150.855 1.00 27.95 ?  443 THR B CG2   1 
ATOM   9121  N  N     . ASP B 1 444 ? 134.670 156.855 149.546 1.00 39.02 ?  444 ASP B N     1 
ATOM   9122  C  CA    . ASP B 1 444 ? 134.369 157.565 148.306 1.00 38.94 ?  444 ASP B CA    1 
ATOM   9123  C  C     . ASP B 1 444 ? 134.718 156.644 147.146 1.00 39.94 ?  444 ASP B C     1 
ATOM   9124  O  O     . ASP B 1 444 ? 135.900 156.423 146.861 1.00 40.16 ?  444 ASP B O     1 
ATOM   9125  C  CB    . ASP B 1 444 ? 135.142 158.881 148.217 1.00 41.00 ?  444 ASP B CB    1 
ATOM   9126  C  CG    . ASP B 1 444 ? 134.413 159.930 147.401 1.00 46.45 ?  444 ASP B CG    1 
ATOM   9127  O  OD1   . ASP B 1 444 ? 133.277 160.291 147.773 1.00 44.63 ?  444 ASP B OD1   1 
ATOM   9128  O  OD2   . ASP B 1 444 ? 134.977 160.397 146.389 1.00 43.46 -1 444 ASP B OD2   1 
ATOM   9129  N  N     . ILE B 1 445 ? 133.700 156.111 146.481 1.00 37.64 ?  445 ILE B N     1 
ATOM   9130  C  CA    . ILE B 1 445 ? 133.878 155.170 145.382 1.00 36.46 ?  445 ILE B CA    1 
ATOM   9131  C  C     . ILE B 1 445 ? 133.656 155.919 144.076 1.00 37.15 ?  445 ILE B C     1 
ATOM   9132  O  O     . ILE B 1 445 ? 132.571 156.460 143.837 1.00 42.66 ?  445 ILE B O     1 
ATOM   9133  C  CB    . ILE B 1 445 ? 132.922 153.974 145.511 1.00 32.65 ?  445 ILE B CB    1 
ATOM   9134  C  CG1   . ILE B 1 445 ? 133.374 153.069 146.655 1.00 33.55 ?  445 ILE B CG1   1 
ATOM   9135  C  CG2   . ILE B 1 445 ? 132.874 153.191 144.211 1.00 35.35 ?  445 ILE B CG2   1 
ATOM   9136  C  CD1   . ILE B 1 445 ? 132.295 152.161 147.167 1.00 35.02 ?  445 ILE B CD1   1 
ATOM   9137  N  N     . ARG B 1 446 ? 134.683 155.945 143.230 1.00 36.82 ?  446 ARG B N     1 
ATOM   9138  C  CA    . ARG B 1 446 ? 134.690 156.784 142.041 1.00 39.43 ?  446 ARG B CA    1 
ATOM   9139  C  C     . ARG B 1 446 ? 134.154 156.082 140.800 1.00 40.16 ?  446 ARG B C     1 
ATOM   9140  O  O     . ARG B 1 446 ? 134.096 156.705 139.735 1.00 37.10 ?  446 ARG B O     1 
ATOM   9141  C  CB    . ARG B 1 446 ? 136.111 157.290 141.770 1.00 37.35 ?  446 ARG B CB    1 
ATOM   9142  C  CG    . ARG B 1 446 ? 136.974 157.387 143.018 1.00 37.48 ?  446 ARG B CG    1 
ATOM   9143  C  CD    . ARG B 1 446 ? 136.660 158.636 143.826 1.00 39.79 ?  446 ARG B CD    1 
ATOM   9144  N  NE    . ARG B 1 446 ? 136.504 159.816 142.986 1.00 40.67 ?  446 ARG B NE    1 
ATOM   9145  C  CZ    . ARG B 1 446 ? 136.615 161.064 143.422 1.00 40.52 ?  446 ARG B CZ    1 
ATOM   9146  N  NH1   . ARG B 1 446 ? 136.883 161.331 144.689 1.00 37.72 1  446 ARG B NH1   1 
ATOM   9147  N  NH2   . ARG B 1 446 ? 136.452 162.068 142.565 1.00 39.59 ?  446 ARG B NH2   1 
ATOM   9148  N  N     . ASN B 1 447 ? 133.757 154.813 140.903 1.00 33.35 ?  447 ASN B N     1 
ATOM   9149  C  CA    . ASN B 1 447 ? 133.238 154.076 139.762 1.00 25.93 ?  447 ASN B CA    1 
ATOM   9150  C  C     . ASN B 1 447 ? 131.822 153.560 139.973 1.00 30.51 ?  447 ASN B C     1 
ATOM   9151  O  O     . ASN B 1 447 ? 131.258 152.955 139.054 1.00 37.20 ?  447 ASN B O     1 
ATOM   9152  C  CB    . ASN B 1 447 ? 134.164 152.903 139.418 1.00 31.43 ?  447 ASN B CB    1 
ATOM   9153  C  CG    . ASN B 1 447 ? 135.213 153.278 138.394 1.00 30.80 ?  447 ASN B CG    1 
ATOM   9154  O  OD1   . ASN B 1 447 ? 134.892 153.629 137.261 1.00 34.38 ?  447 ASN B OD1   1 
ATOM   9155  N  ND2   . ASN B 1 447 ? 136.478 153.209 138.791 1.00 29.87 ?  447 ASN B ND2   1 
ATOM   9156  N  N     . ALA B 1 448 ? 131.235 153.776 141.148 1.00 31.55 ?  448 ALA B N     1 
ATOM   9157  C  CA    . ALA B 1 448 ? 129.840 153.441 141.426 1.00 26.92 ?  448 ALA B CA    1 
ATOM   9158  C  C     . ALA B 1 448 ? 129.136 154.731 141.825 1.00 27.73 ?  448 ALA B C     1 
ATOM   9159  O  O     . ALA B 1 448 ? 129.200 155.148 142.992 1.00 29.36 ?  448 ALA B O     1 
ATOM   9160  C  CB    . ALA B 1 448 ? 129.728 152.380 142.517 1.00 26.31 ?  448 ALA B CB    1 
ATOM   9161  N  N     . PRO B 1 449 ? 128.464 155.402 140.887 1.00 27.20 ?  449 PRO B N     1 
ATOM   9162  C  CA    . PRO B 1 449 ? 127.880 156.711 141.218 1.00 24.21 ?  449 PRO B CA    1 
ATOM   9163  C  C     . PRO B 1 449 ? 126.692 156.612 142.153 1.00 24.86 ?  449 PRO B C     1 
ATOM   9164  O  O     . PRO B 1 449 ? 126.562 157.432 143.072 1.00 21.81 ?  449 PRO B O     1 
ATOM   9165  C  CB    . PRO B 1 449 ? 127.474 157.277 139.848 1.00 21.18 ?  449 PRO B CB    1 
ATOM   9166  C  CG    . PRO B 1 449 ? 127.992 156.305 138.825 1.00 25.67 ?  449 PRO B CG    1 
ATOM   9167  C  CD    . PRO B 1 449 ? 128.175 155.000 139.503 1.00 25.18 ?  449 PRO B CD    1 
ATOM   9168  N  N     . ALA B 1 450 ? 125.811 155.634 141.940 1.00 28.94 ?  450 ALA B N     1 
ATOM   9169  C  CA    . ALA B 1 450 ? 124.663 155.471 142.823 1.00 19.52 ?  450 ALA B CA    1 
ATOM   9170  C  C     . ALA B 1 450 ? 125.102 155.064 144.223 1.00 23.03 ?  450 ALA B C     1 
ATOM   9171  O  O     . ALA B 1 450 ? 124.528 155.524 145.215 1.00 24.84 ?  450 ALA B O     1 
ATOM   9172  C  CB    . ALA B 1 450 ? 123.691 154.449 142.236 1.00 19.72 ?  450 ALA B CB    1 
ATOM   9173  N  N     . VAL B 1 451 ? 126.124 154.211 144.324 1.00 26.08 ?  451 VAL B N     1 
ATOM   9174  C  CA    . VAL B 1 451 ? 126.655 153.837 145.632 1.00 19.47 ?  451 VAL B CA    1 
ATOM   9175  C  C     . VAL B 1 451 ? 127.228 155.056 146.342 1.00 19.53 ?  451 VAL B C     1 
ATOM   9176  O  O     . VAL B 1 451 ? 126.999 155.257 147.540 1.00 26.05 ?  451 VAL B O     1 
ATOM   9177  C  CB    . VAL B 1 451 ? 127.707 152.720 145.488 1.00 22.52 ?  451 VAL B CB    1 
ATOM   9178  C  CG1   . VAL B 1 451 ? 128.422 152.484 146.807 1.00 25.41 ?  451 VAL B CG1   1 
ATOM   9179  C  CG2   . VAL B 1 451 ? 127.059 151.438 144.999 1.00 19.90 ?  451 VAL B CG2   1 
ATOM   9180  N  N     . ARG B 1 452 ? 127.978 155.889 145.619 1.00 21.20 ?  452 ARG B N     1 
ATOM   9181  C  CA    . ARG B 1 452 ? 128.552 157.089 146.221 1.00 23.42 ?  452 ARG B CA    1 
ATOM   9182  C  C     . ARG B 1 452 ? 127.460 158.043 146.692 1.00 24.60 ?  452 ARG B C     1 
ATOM   9183  O  O     . ARG B 1 452 ? 127.518 158.573 147.810 1.00 30.17 ?  452 ARG B O     1 
ATOM   9184  C  CB    . ARG B 1 452 ? 129.477 157.782 145.220 1.00 20.90 ?  452 ARG B CB    1 
ATOM   9185  C  CG    . ARG B 1 452 ? 129.980 159.136 145.682 1.00 24.84 ?  452 ARG B CG    1 
ATOM   9186  C  CD    . ARG B 1 452 ? 131.391 159.402 145.194 1.00 27.79 ?  452 ARG B CD    1 
ATOM   9187  N  NE    . ARG B 1 452 ? 131.402 160.287 144.036 1.00 33.94 ?  452 ARG B NE    1 
ATOM   9188  C  CZ    . ARG B 1 452 ? 132.404 160.380 143.173 1.00 38.90 ?  452 ARG B CZ    1 
ATOM   9189  N  NH1   . ARG B 1 452 ? 133.499 159.652 143.306 1.00 31.79 1  452 ARG B NH1   1 
ATOM   9190  N  NH2   . ARG B 1 452 ? 132.304 161.225 142.151 1.00 34.38 ?  452 ARG B NH2   1 
ATOM   9191  N  N     . ARG B 1 453 ? 126.450 158.269 145.850 1.00 22.40 ?  453 ARG B N     1 
ATOM   9192  C  CA    . ARG B 1 453 ? 125.370 159.180 146.215 1.00 20.83 ?  453 ARG B CA    1 
ATOM   9193  C  C     . ARG B 1 453 ? 124.585 158.654 147.410 1.00 23.25 ?  453 ARG B C     1 
ATOM   9194  O  O     . ARG B 1 453 ? 124.225 159.420 148.310 1.00 25.88 ?  453 ARG B O     1 
ATOM   9195  C  CB    . ARG B 1 453 ? 124.450 159.407 145.015 1.00 20.64 ?  453 ARG B CB    1 
ATOM   9196  C  CG    . ARG B 1 453 ? 123.095 159.991 145.366 1.00 20.05 ?  453 ARG B CG    1 
ATOM   9197  C  CD    . ARG B 1 453 ? 122.416 160.586 144.146 1.00 20.46 ?  453 ARG B CD    1 
ATOM   9198  N  NE    . ARG B 1 453 ? 121.068 160.064 143.965 1.00 22.82 ?  453 ARG B NE    1 
ATOM   9199  C  CZ    . ARG B 1 453 ? 119.987 160.560 144.550 1.00 26.10 ?  453 ARG B CZ    1 
ATOM   9200  N  NH1   . ARG B 1 453 ? 120.058 161.598 145.366 1.00 28.13 1  453 ARG B NH1   1 
ATOM   9201  N  NH2   . ARG B 1 453 ? 118.805 159.999 144.313 1.00 25.07 ?  453 ARG B NH2   1 
ATOM   9202  N  N     . ALA B 1 454 ? 124.316 157.346 147.441 1.00 23.91 ?  454 ALA B N     1 
ATOM   9203  C  CA    . ALA B 1 454 ? 123.590 156.767 148.564 1.00 17.46 ?  454 ALA B CA    1 
ATOM   9204  C  C     . ALA B 1 454 ? 124.415 156.809 149.843 1.00 21.92 ?  454 ALA B C     1 
ATOM   9205  O  O     . ALA B 1 454 ? 123.869 157.023 150.928 1.00 24.78 ?  454 ALA B O     1 
ATOM   9206  C  CB    . ALA B 1 454 ? 123.176 155.334 148.238 1.00 19.55 ?  454 ALA B CB    1 
ATOM   9207  N  N     . ASN B 1 455 ? 125.728 156.597 149.746 1.00 23.90 ?  455 ASN B N     1 
ATOM   9208  C  CA    . ASN B 1 455 ? 126.577 156.723 150.923 1.00 20.72 ?  455 ASN B CA    1 
ATOM   9209  C  C     . ASN B 1 455 ? 126.567 158.151 151.450 1.00 26.36 ?  455 ASN B C     1 
ATOM   9210  O  O     . ASN B 1 455 ? 126.522 158.376 152.665 1.00 30.59 ?  455 ASN B O     1 
ATOM   9211  C  CB    . ASN B 1 455 ? 128.002 156.281 150.595 1.00 20.52 ?  455 ASN B CB    1 
ATOM   9212  C  CG    . ASN B 1 455 ? 128.888 156.217 151.821 1.00 24.75 ?  455 ASN B CG    1 
ATOM   9213  O  OD1   . ASN B 1 455 ? 128.769 155.307 152.639 1.00 30.97 ?  455 ASN B OD1   1 
ATOM   9214  N  ND2   . ASN B 1 455 ? 129.780 157.190 151.957 1.00 27.07 ?  455 ASN B ND2   1 
ATOM   9215  N  N     . LYS B 1 456 ? 126.608 159.133 150.546 1.00 27.25 ?  456 LYS B N     1 
ATOM   9216  C  CA    . LYS B 1 456 ? 126.617 160.528 150.972 1.00 25.06 ?  456 LYS B CA    1 
ATOM   9217  C  C     . LYS B 1 456 ? 125.273 160.964 151.543 1.00 23.96 ?  456 LYS B C     1 
ATOM   9218  O  O     . LYS B 1 456 ? 125.233 161.797 152.454 1.00 32.65 ?  456 LYS B O     1 
ATOM   9219  C  CB    . LYS B 1 456 ? 127.009 161.429 149.800 1.00 26.81 ?  456 LYS B CB    1 
ATOM   9220  C  CG    . LYS B 1 456 ? 128.137 162.398 150.110 1.00 30.51 ?  456 LYS B CG    1 
ATOM   9221  C  CD    . LYS B 1 456 ? 128.665 163.054 148.844 1.00 33.74 ?  456 LYS B CD    1 
ATOM   9222  C  CE    . LYS B 1 456 ? 129.163 162.018 147.850 1.00 33.23 ?  456 LYS B CE    1 
ATOM   9223  N  NZ    . LYS B 1 456 ? 130.431 161.378 148.296 1.00 28.20 1  456 LYS B NZ    1 
ATOM   9224  N  N     . ALA B 1 457 ? 124.169 160.424 151.027 1.00 24.59 ?  457 ALA B N     1 
ATOM   9225  C  CA    . ALA B 1 457 ? 122.838 160.885 151.410 1.00 18.66 ?  457 ALA B CA    1 
ATOM   9226  C  C     . ALA B 1 457 ? 122.253 160.071 152.562 1.00 26.26 ?  457 ALA B C     1 
ATOM   9227  O  O     . ALA B 1 457 ? 121.884 160.628 153.601 1.00 32.54 ?  457 ALA B O     1 
ATOM   9228  C  CB    . ALA B 1 457 ? 121.907 160.837 150.194 1.00 18.26 ?  457 ALA B CB    1 
ATOM   9229  N  N     . MET B 1 458 ? 122.146 158.755 152.379 1.00 24.94 ?  458 MET B N     1 
ATOM   9230  C  CA    . MET B 1 458 ? 121.567 157.890 153.400 1.00 16.55 ?  458 MET B CA    1 
ATOM   9231  C  C     . MET B 1 458 ? 122.403 157.889 154.674 1.00 21.35 ?  458 MET B C     1 
ATOM   9232  O  O     . MET B 1 458 ? 121.853 157.871 155.782 1.00 30.53 ?  458 MET B O     1 
ATOM   9233  C  CB    . MET B 1 458 ? 121.430 156.467 152.857 1.00 22.58 ?  458 MET B CB    1 
ATOM   9234  C  CG    . MET B 1 458 ? 120.775 156.377 151.490 1.00 21.89 ?  458 MET B CG    1 
ATOM   9235  S  SD    . MET B 1 458 ? 119.220 157.276 151.407 1.00 29.65 ?  458 MET B SD    1 
ATOM   9236  C  CE    . MET B 1 458 ? 118.204 156.250 152.463 1.00 23.61 ?  458 MET B CE    1 
ATOM   9237  N  N     . LYS B 1 459 ? 123.730 157.887 154.536 1.00 19.92 ?  459 LYS B N     1 
ATOM   9238  C  CA    . LYS B 1 459 ? 124.648 157.777 155.673 1.00 17.97 ?  459 LYS B CA    1 
ATOM   9239  C  C     . LYS B 1 459 ? 124.370 156.508 156.476 1.00 20.01 ?  459 LYS B C     1 
ATOM   9240  O  O     . LYS B 1 459 ? 124.511 156.481 157.699 1.00 26.61 ?  459 LYS B O     1 
ATOM   9241  C  CB    . LYS B 1 459 ? 124.578 159.012 156.573 1.00 20.12 ?  459 LYS B CB    1 
ATOM   9242  C  CG    . LYS B 1 459 ? 125.108 160.283 155.939 1.00 24.69 ?  459 LYS B CG    1 
ATOM   9243  C  CD    . LYS B 1 459 ? 124.328 161.495 156.415 1.00 25.09 ?  459 LYS B CD    1 
ATOM   9244  C  CE    . LYS B 1 459 ? 124.478 162.659 155.456 1.00 25.13 ?  459 LYS B CE    1 
ATOM   9245  N  NZ    . LYS B 1 459 ? 125.905 163.044 155.275 1.00 27.84 1  459 LYS B NZ    1 
ATOM   9246  N  N     . SER B 1 460 ? 123.973 155.450 155.778 1.00 24.04 ?  460 SER B N     1 
ATOM   9247  C  CA    . SER B 1 460 ? 123.577 154.213 156.430 1.00 13.89 ?  460 SER B CA    1 
ATOM   9248  C  C     . SER B 1 460 ? 124.791 153.453 156.944 1.00 13.09 ?  460 SER B C     1 
ATOM   9249  O  O     . SER B 1 460 ? 125.817 153.353 156.265 1.00 26.30 ?  460 SER B O     1 
ATOM   9250  C  CB    . SER B 1 460 ? 122.786 153.334 155.465 1.00 15.88 ?  460 SER B CB    1 
ATOM   9251  O  OG    . SER B 1 460 ? 123.000 151.964 155.747 1.00 26.50 ?  460 SER B OG    1 
ATOM   9252  N  N     . ILE B 1 461 ? 124.665 152.913 158.156 1.00 10.69 ?  461 ILE B N     1 
ATOM   9253  C  CA    . ILE B 1 461 ? 125.697 152.091 158.767 1.00 19.56 ?  461 ILE B CA    1 
ATOM   9254  C  C     . ILE B 1 461 ? 125.049 150.806 159.261 1.00 16.81 ?  461 ILE B C     1 
ATOM   9255  O  O     . ILE B 1 461 ? 123.834 150.724 159.443 1.00 20.02 ?  461 ILE B O     1 
ATOM   9256  C  CB    . ILE B 1 461 ? 126.415 152.812 159.928 1.00 14.38 ?  461 ILE B CB    1 
ATOM   9257  C  CG1   . ILE B 1 461 ? 125.428 153.122 161.053 1.00 10.83 ?  461 ILE B CG1   1 
ATOM   9258  C  CG2   . ILE B 1 461 ? 127.090 154.084 159.435 1.00 17.22 ?  461 ILE B CG2   1 
ATOM   9259  C  CD1   . ILE B 1 461 ? 126.076 153.656 162.307 1.00 14.55 ?  461 ILE B CD1   1 
ATOM   9260  N  N     . GLY B 1 462 ? 125.880 149.788 159.456 1.00 15.87 ?  462 GLY B N     1 
ATOM   9261  C  CA    . GLY B 1 462 ? 125.400 148.546 160.025 1.00 6.58  ?  462 GLY B CA    1 
ATOM   9262  C  C     . GLY B 1 462 ? 126.144 148.160 161.284 1.00 11.82 ?  462 GLY B C     1 
ATOM   9263  O  O     . GLY B 1 462 ? 127.322 147.798 161.227 1.00 26.95 ?  462 GLY B O     1 
ATOM   9264  N  N     . LEU B 1 463 ? 125.467 148.223 162.425 1.00 12.36 ?  463 LEU B N     1 
ATOM   9265  C  CA    . LEU B 1 463 ? 126.053 147.847 163.706 1.00 11.25 ?  463 LEU B CA    1 
ATOM   9266  C  C     . LEU B 1 463 ? 125.468 146.500 164.113 1.00 13.98 ?  463 LEU B C     1 
ATOM   9267  O  O     . LEU B 1 463 ? 124.305 146.416 164.518 1.00 25.51 ?  463 LEU B O     1 
ATOM   9268  C  CB    . LEU B 1 463 ? 125.786 148.913 164.765 1.00 19.67 ?  463 LEU B CB    1 
ATOM   9269  C  CG    . LEU B 1 463 ? 126.286 148.610 166.180 1.00 18.45 ?  463 LEU B CG    1 
ATOM   9270  C  CD1   . LEU B 1 463 ? 127.743 148.185 166.152 1.00 6.51  ?  463 LEU B CD1   1 
ATOM   9271  C  CD2   . LEU B 1 463 ? 126.093 149.814 167.086 1.00 14.56 ?  463 LEU B CD2   1 
ATOM   9272  N  N     . GLY B 1 464 ? 126.278 145.447 164.001 1.00 14.85 ?  464 GLY B N     1 
ATOM   9273  C  CA    . GLY B 1 464 ? 125.850 144.105 164.318 1.00 13.86 ?  464 GLY B CA    1 
ATOM   9274  C  C     . GLY B 1 464 ? 126.211 143.696 165.734 1.00 13.07 ?  464 GLY B C     1 
ATOM   9275  O  O     . GLY B 1 464 ? 126.602 144.506 166.576 1.00 15.05 ?  464 GLY B O     1 
ATOM   9276  N  N     . ALA B 1 465 ? 126.071 142.398 165.989 1.00 15.16 ?  465 ALA B N     1 
ATOM   9277  C  CA    . ALA B 1 465 ? 126.394 141.831 167.287 1.00 12.37 ?  465 ALA B CA    1 
ATOM   9278  C  C     . ALA B 1 465 ? 126.894 140.409 167.092 1.00 14.17 ?  465 ALA B C     1 
ATOM   9279  O  O     . ALA B 1 465 ? 126.429 139.698 166.197 1.00 28.53 ?  465 ALA B O     1 
ATOM   9280  C  CB    . ALA B 1 465 ? 125.184 141.846 168.228 1.00 19.00 ?  465 ALA B CB    1 
ATOM   9281  N  N     . MET B 1 466 ? 127.847 140.008 167.927 1.00 20.66 ?  466 MET B N     1 
ATOM   9282  C  CA    . MET B 1 466 ? 128.392 138.661 167.923 1.00 20.75 ?  466 MET B CA    1 
ATOM   9283  C  C     . MET B 1 466 ? 128.391 138.122 169.346 1.00 20.58 ?  466 MET B C     1 
ATOM   9284  O  O     . MET B 1 466 ? 128.175 138.859 170.313 1.00 26.81 ?  466 MET B O     1 
ATOM   9285  C  CB    . MET B 1 466 ? 129.813 138.625 167.340 1.00 27.19 ?  466 MET B CB    1 
ATOM   9286  C  CG    . MET B 1 466 ? 130.760 139.646 167.952 1.00 22.89 ?  466 MET B CG    1 
ATOM   9287  S  SD    . MET B 1 466 ? 132.427 139.584 167.270 1.00 38.02 ?  466 MET B SD    1 
ATOM   9288  C  CE    . MET B 1 466 ? 132.089 139.546 165.514 1.00 29.36 ?  466 MET B CE    1 
ATOM   9289  N  N     . ASN B 1 467 ? 128.621 136.813 169.462 1.00 19.96 ?  467 ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 467 ? 128.767 136.135 170.752 1.00 19.55 ?  467 ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 467 ? 127.475 136.170 171.567 1.00 20.51 ?  467 ASN B C     1 
ATOM   9292  O  O     . ASN B 1 467 ? 127.507 136.285 172.792 1.00 27.46 ?  467 ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 467 ? 129.925 136.717 171.565 1.00 21.54 ?  467 ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 467 ? 130.732 135.652 172.272 1.00 24.57 ?  467 ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 467 ? 130.548 134.458 172.037 1.00 28.94 ?  467 ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 467 ? 131.636 136.077 173.143 1.00 28.00 ?  467 ASN B ND2   1 
ATOM   9297  N  N     . LEU B 1 468 ? 126.330 136.079 170.889 1.00 19.53 ?  468 LEU B N     1 
ATOM   9298  C  CA    . LEU B 1 468 ? 125.076 135.903 171.614 1.00 18.12 ?  468 LEU B CA    1 
ATOM   9299  C  C     . LEU B 1 468 ? 125.015 134.523 172.254 1.00 22.01 ?  468 LEU B C     1 
ATOM   9300  O  O     . LEU B 1 468 ? 124.753 134.392 173.457 1.00 25.58 ?  468 LEU B O     1 
ATOM   9301  C  CB    . LEU B 1 468 ? 123.888 136.110 170.677 1.00 24.55 ?  468 LEU B CB    1 
ATOM   9302  C  CG    . LEU B 1 468 ? 122.529 135.739 171.275 1.00 20.38 ?  468 LEU B CG    1 
ATOM   9303  C  CD1   . LEU B 1 468 ? 122.185 136.659 172.433 1.00 17.94 ?  468 LEU B CD1   1 
ATOM   9304  C  CD2   . LEU B 1 468 ? 121.436 135.764 170.221 1.00 15.41 ?  468 LEU B CD2   1 
ATOM   9305  N  N     . HIS B 1 469 ? 125.284 133.481 171.467 1.00 25.31 ?  469 HIS B N     1 
ATOM   9306  C  CA    . HIS B 1 469 ? 125.258 132.125 172.002 1.00 16.96 ?  469 HIS B CA    1 
ATOM   9307  C  C     . HIS B 1 469 ? 126.391 131.906 172.993 1.00 26.08 ?  469 HIS B C     1 
ATOM   9308  O  O     . HIS B 1 469 ? 126.222 131.190 173.983 1.00 38.87 ?  469 HIS B O     1 
ATOM   9309  C  CB    . HIS B 1 469 ? 125.333 131.103 170.871 1.00 20.40 ?  469 HIS B CB    1 
ATOM   9310  C  CG    . HIS B 1 469 ? 124.921 129.724 171.282 1.00 24.73 ?  469 HIS B CG    1 
ATOM   9311  N  ND1   . HIS B 1 469 ? 125.068 128.627 170.463 1.00 28.72 ?  469 HIS B ND1   1 
ATOM   9312  C  CD2   . HIS B 1 469 ? 124.367 129.264 172.429 1.00 25.30 ?  469 HIS B CD2   1 
ATOM   9313  C  CE1   . HIS B 1 469 ? 124.622 127.551 171.086 1.00 22.84 ?  469 HIS B CE1   1 
ATOM   9314  N  NE2   . HIS B 1 469 ? 124.192 127.910 172.281 1.00 25.44 ?  469 HIS B NE2   1 
ATOM   9315  N  N     . GLY B 1 470 ? 127.555 132.506 172.741 1.00 21.78 ?  470 GLY B N     1 
ATOM   9316  C  CA    . GLY B 1 470 ? 128.644 132.403 173.698 1.00 18.71 ?  470 GLY B CA    1 
ATOM   9317  C  C     . GLY B 1 470 ? 128.286 133.003 175.042 1.00 19.99 ?  470 GLY B C     1 
ATOM   9318  O  O     . GLY B 1 470 ? 128.530 132.402 176.091 1.00 34.01 ?  470 GLY B O     1 
ATOM   9319  N  N     . TYR B 1 471 ? 127.687 134.196 175.027 1.00 22.88 ?  471 TYR B N     1 
ATOM   9320  C  CA    . TYR B 1 471 ? 127.271 134.826 176.275 1.00 25.52 ?  471 TYR B CA    1 
ATOM   9321  C  C     . TYR B 1 471 ? 126.198 134.005 176.975 1.00 27.96 ?  471 TYR B C     1 
ATOM   9322  O  O     . TYR B 1 471 ? 126.237 133.834 178.200 1.00 32.88 ?  471 TYR B O     1 
ATOM   9323  C  CB    . TYR B 1 471 ? 126.765 136.244 176.013 1.00 24.23 ?  471 TYR B CB    1 
ATOM   9324  C  CG    . TYR B 1 471 ? 126.383 136.984 177.274 1.00 26.56 ?  471 TYR B CG    1 
ATOM   9325  C  CD1   . TYR B 1 471 ? 127.356 137.432 178.158 1.00 28.31 ?  471 TYR B CD1   1 
ATOM   9326  C  CD2   . TYR B 1 471 ? 125.053 137.213 177.594 1.00 18.57 ?  471 TYR B CD2   1 
ATOM   9327  C  CE1   . TYR B 1 471 ? 127.015 138.104 179.313 1.00 28.21 ?  471 TYR B CE1   1 
ATOM   9328  C  CE2   . TYR B 1 471 ? 124.704 137.881 178.751 1.00 21.27 ?  471 TYR B CE2   1 
ATOM   9329  C  CZ    . TYR B 1 471 ? 125.689 138.324 179.605 1.00 27.48 ?  471 TYR B CZ    1 
ATOM   9330  O  OH    . TYR B 1 471 ? 125.348 138.987 180.760 1.00 32.99 ?  471 TYR B OH    1 
ATOM   9331  N  N     . LEU B 1 472 ? 125.226 133.490 176.217 1.00 26.27 ?  472 LEU B N     1 
ATOM   9332  C  CA    . LEU B 1 472 ? 124.145 132.725 176.831 1.00 23.87 ?  472 LEU B CA    1 
ATOM   9333  C  C     . LEU B 1 472 ? 124.651 131.416 177.428 1.00 25.52 ?  472 LEU B C     1 
ATOM   9334  O  O     . LEU B 1 472 ? 124.240 131.032 178.528 1.00 31.23 ?  472 LEU B O     1 
ATOM   9335  C  CB    . LEU B 1 472 ? 123.042 132.458 175.807 1.00 28.13 ?  472 LEU B CB    1 
ATOM   9336  C  CG    . LEU B 1 472 ? 122.291 133.677 175.272 1.00 27.42 ?  472 LEU B CG    1 
ATOM   9337  C  CD1   . LEU B 1 472 ? 121.434 133.294 174.076 1.00 24.49 ?  472 LEU B CD1   1 
ATOM   9338  C  CD2   . LEU B 1 472 ? 121.446 134.314 176.363 1.00 19.86 ?  472 LEU B CD2   1 
ATOM   9339  N  N     . ALA B 1 473 ? 125.540 130.716 176.718 1.00 25.93 ?  473 ALA B N     1 
ATOM   9340  C  CA    . ALA B 1 473 ? 126.044 129.440 177.208 1.00 26.31 ?  473 ALA B CA    1 
ATOM   9341  C  C     . ALA B 1 473 ? 127.002 129.630 178.374 1.00 33.22 ?  473 ALA B C     1 
ATOM   9342  O  O     . ALA B 1 473 ? 127.014 128.825 179.312 1.00 38.99 ?  473 ALA B O     1 
ATOM   9343  C  CB    . ALA B 1 473 ? 126.722 128.677 176.072 1.00 26.76 ?  473 ALA B CB    1 
ATOM   9344  N  N     . GLN B 1 474 ? 127.816 130.686 178.338 1.00 27.75 ?  474 GLN B N     1 
ATOM   9345  C  CA    . GLN B 1 474 ? 128.731 130.963 179.436 1.00 28.56 ?  474 GLN B CA    1 
ATOM   9346  C  C     . GLN B 1 474 ? 128.025 131.517 180.665 1.00 29.18 ?  474 GLN B C     1 
ATOM   9347  O  O     . GLN B 1 474 ? 128.650 131.613 181.727 1.00 36.85 ?  474 GLN B O     1 
ATOM   9348  C  CB    . GLN B 1 474 ? 129.820 131.936 178.978 1.00 28.71 ?  474 GLN B CB    1 
ATOM   9349  C  CG    . GLN B 1 474 ? 130.867 131.296 178.084 1.00 28.77 ?  474 GLN B CG    1 
ATOM   9350  C  CD    . GLN B 1 474 ? 131.841 132.303 177.514 1.00 33.70 ?  474 GLN B CD    1 
ATOM   9351  O  OE1   . GLN B 1 474 ? 132.649 132.882 178.239 1.00 36.08 ?  474 GLN B OE1   1 
ATOM   9352  N  NE2   . GLN B 1 474 ? 131.772 132.518 176.205 1.00 33.97 ?  474 GLN B NE2   1 
ATOM   9353  N  N     . ASN B 1 475 ? 126.750 131.883 180.548 1.00 31.43 ?  475 ASN B N     1 
ATOM   9354  C  CA    . ASN B 1 475 ? 125.954 132.347 181.674 1.00 31.52 ?  475 ASN B CA    1 
ATOM   9355  C  C     . ASN B 1 475 ? 124.872 131.351 182.067 1.00 31.77 ?  475 ASN B C     1 
ATOM   9356  O  O     . ASN B 1 475 ? 123.970 131.701 182.834 1.00 34.96 ?  475 ASN B O     1 
ATOM   9357  C  CB    . ASN B 1 475 ? 125.331 133.707 181.354 1.00 30.74 ?  475 ASN B CB    1 
ATOM   9358  C  CG    . ASN B 1 475 ? 126.346 134.828 181.380 1.00 30.26 ?  475 ASN B CG    1 
ATOM   9359  O  OD1   . ASN B 1 475 ? 126.540 135.483 182.404 1.00 38.24 ?  475 ASN B OD1   1 
ATOM   9360  N  ND2   . ASN B 1 475 ? 127.011 135.047 180.254 1.00 28.97 ?  475 ASN B ND2   1 
ATOM   9361  N  N     . GLY B 1 476 ? 124.939 130.125 181.560 1.00 31.06 ?  476 GLY B N     1 
ATOM   9362  C  CA    . GLY B 1 476 ? 123.967 129.103 181.904 1.00 30.18 ?  476 GLY B CA    1 
ATOM   9363  C  C     . GLY B 1 476 ? 122.561 129.371 181.412 1.00 35.17 ?  476 GLY B C     1 
ATOM   9364  O  O     . GLY B 1 476 ? 121.596 129.128 182.147 1.00 37.39 ?  476 GLY B O     1 
ATOM   9365  N  N     . ILE B 1 477 ? 122.419 129.871 180.188 1.00 32.15 ?  477 ILE B N     1 
ATOM   9366  C  CA    . ILE B 1 477 ? 121.118 130.125 179.581 1.00 27.50 ?  477 ILE B CA    1 
ATOM   9367  C  C     . ILE B 1 477 ? 121.054 129.360 178.268 1.00 31.33 ?  477 ILE B C     1 
ATOM   9368  O  O     . ILE B 1 477 ? 121.916 129.538 177.398 1.00 36.33 ?  477 ILE B O     1 
ATOM   9369  C  CB    . ILE B 1 477 ? 120.871 131.623 179.354 1.00 26.02 ?  477 ILE B CB    1 
ATOM   9370  C  CG1   . ILE B 1 477 ? 121.003 132.395 180.667 1.00 29.49 ?  477 ILE B CG1   1 
ATOM   9371  C  CG2   . ILE B 1 477 ? 119.498 131.847 178.748 1.00 30.20 ?  477 ILE B CG2   1 
ATOM   9372  C  CD1   . ILE B 1 477 ? 121.265 133.866 180.477 1.00 32.35 ?  477 ILE B CD1   1 
ATOM   9373  N  N     . ALA B 1 478 ? 120.039 128.511 178.127 1.00 33.41 ?  478 ALA B N     1 
ATOM   9374  C  CA    . ALA B 1 478 ? 119.842 127.784 176.881 1.00 27.28 ?  478 ALA B CA    1 
ATOM   9375  C  C     . ALA B 1 478 ? 119.411 128.746 175.782 1.00 32.74 ?  478 ALA B C     1 
ATOM   9376  O  O     . ALA B 1 478 ? 118.551 129.604 175.999 1.00 34.41 ?  478 ALA B O     1 
ATOM   9377  C  CB    . ALA B 1 478 ? 118.799 126.684 177.068 1.00 27.73 ?  478 ALA B CB    1 
ATOM   9378  N  N     . TYR B 1 479 ? 120.011 128.598 174.598 1.00 30.56 ?  479 TYR B N     1 
ATOM   9379  C  CA    . TYR B 1 479 ? 119.721 129.507 173.493 1.00 23.51 ?  479 TYR B CA    1 
ATOM   9380  C  C     . TYR B 1 479 ? 118.249 129.466 173.100 1.00 26.65 ?  479 TYR B C     1 
ATOM   9381  O  O     . TYR B 1 479 ? 117.691 130.485 172.681 1.00 32.90 ?  479 TYR B O     1 
ATOM   9382  C  CB    . TYR B 1 479 ? 120.611 129.164 172.298 1.00 18.58 ?  479 TYR B CB    1 
ATOM   9383  C  CG    . TYR B 1 479 ? 120.475 130.080 171.099 1.00 26.64 ?  479 TYR B CG    1 
ATOM   9384  C  CD1   . TYR B 1 479 ? 119.516 129.844 170.121 1.00 24.92 ?  479 TYR B CD1   1 
ATOM   9385  C  CD2   . TYR B 1 479 ? 121.320 131.169 170.936 1.00 25.29 ?  479 TYR B CD2   1 
ATOM   9386  C  CE1   . TYR B 1 479 ? 119.395 130.675 169.024 1.00 22.84 ?  479 TYR B CE1   1 
ATOM   9387  C  CE2   . TYR B 1 479 ? 121.207 132.005 169.842 1.00 22.12 ?  479 TYR B CE2   1 
ATOM   9388  C  CZ    . TYR B 1 479 ? 120.244 131.753 168.890 1.00 28.95 ?  479 TYR B CZ    1 
ATOM   9389  O  OH    . TYR B 1 479 ? 120.131 132.585 167.799 1.00 29.93 ?  479 TYR B OH    1 
ATOM   9390  N  N     . GLU B 1 480 ? 117.606 128.307 173.225 1.00 28.98 ?  480 GLU B N     1 
ATOM   9391  C  CA    . GLU B 1 480 ? 116.195 128.177 172.893 1.00 28.27 ?  480 GLU B CA    1 
ATOM   9392  C  C     . GLU B 1 480 ? 115.272 128.564 174.040 1.00 27.46 ?  480 GLU B C     1 
ATOM   9393  O  O     . GLU B 1 480 ? 114.053 128.621 173.840 1.00 33.76 ?  480 GLU B O     1 
ATOM   9394  C  CB    . GLU B 1 480 ? 115.878 126.741 172.467 1.00 30.32 ?  480 GLU B CB    1 
ATOM   9395  C  CG    . GLU B 1 480 ? 116.602 126.273 171.220 1.00 28.24 ?  480 GLU B CG    1 
ATOM   9396  C  CD    . GLU B 1 480 ? 116.440 124.784 170.995 1.00 36.35 ?  480 GLU B CD    1 
ATOM   9397  O  OE1   . GLU B 1 480 ? 115.324 124.354 170.637 1.00 36.92 ?  480 GLU B OE1   1 
ATOM   9398  O  OE2   . GLU B 1 480 ? 117.424 124.041 171.185 1.00 36.74 -1 480 GLU B OE2   1 
ATOM   9399  N  N     . SER B 1 481 ? 115.813 128.829 175.224 1.00 26.14 ?  481 SER B N     1 
ATOM   9400  C  CA    . SER B 1 481 ? 114.979 129.112 176.378 1.00 26.98 ?  481 SER B CA    1 
ATOM   9401  C  C     . SER B 1 481 ? 114.311 130.479 176.241 1.00 28.79 ?  481 SER B C     1 
ATOM   9402  O  O     . SER B 1 481 ? 114.824 131.366 175.554 1.00 29.80 ?  481 SER B O     1 
ATOM   9403  C  CB    . SER B 1 481 ? 115.810 129.069 177.656 1.00 28.32 ?  481 SER B CB    1 
ATOM   9404  O  OG    . SER B 1 481 ? 116.384 130.333 177.932 1.00 32.20 ?  481 SER B OG    1 
ATOM   9405  N  N     . PRO B 1 482 ? 113.150 130.668 176.875 1.00 36.02 ?  482 PRO B N     1 
ATOM   9406  C  CA    . PRO B 1 482 ? 112.548 132.009 176.905 1.00 32.05 ?  482 PRO B CA    1 
ATOM   9407  C  C     . PRO B 1 482 ? 113.421 133.041 177.594 1.00 31.69 ?  482 PRO B C     1 
ATOM   9408  O  O     . PRO B 1 482 ? 113.318 134.233 177.279 1.00 31.35 ?  482 PRO B O     1 
ATOM   9409  C  CB    . PRO B 1 482 ? 111.231 131.785 177.661 1.00 30.81 ?  482 PRO B CB    1 
ATOM   9410  C  CG    . PRO B 1 482 ? 110.944 130.332 177.506 1.00 31.49 ?  482 PRO B CG    1 
ATOM   9411  C  CD    . PRO B 1 482 ? 112.277 129.654 177.490 1.00 33.90 ?  482 PRO B CD    1 
ATOM   9412  N  N     . GLU B 1 483 ? 114.270 132.623 178.536 1.00 34.74 ?  483 GLU B N     1 
ATOM   9413  C  CA    . GLU B 1 483 ? 115.180 133.560 179.185 1.00 33.51 ?  483 GLU B CA    1 
ATOM   9414  C  C     . GLU B 1 483 ? 116.177 134.139 178.189 1.00 33.18 ?  483 GLU B C     1 
ATOM   9415  O  O     . GLU B 1 483 ? 116.516 135.326 178.258 1.00 38.65 ?  483 GLU B O     1 
ATOM   9416  C  CB    . GLU B 1 483 ? 115.912 132.871 180.335 1.00 36.12 ?  483 GLU B CB    1 
ATOM   9417  C  CG    . GLU B 1 483 ? 115.059 132.652 181.570 1.00 37.22 ?  483 GLU B CG    1 
ATOM   9418  C  CD    . GLU B 1 483 ? 114.438 131.272 181.609 1.00 41.25 ?  483 GLU B CD    1 
ATOM   9419  O  OE1   . GLU B 1 483 ? 114.038 130.767 180.539 1.00 39.62 ?  483 GLU B OE1   1 
ATOM   9420  O  OE2   . GLU B 1 483 ? 114.348 130.691 182.712 1.00 40.92 -1 483 GLU B OE2   1 
ATOM   9421  N  N     . ALA B 1 484 ? 116.665 133.311 177.264 1.00 26.92 ?  484 ALA B N     1 
ATOM   9422  C  CA    . ALA B 1 484 ? 117.572 133.803 176.233 1.00 25.36 ?  484 ALA B CA    1 
ATOM   9423  C  C     . ALA B 1 484 ? 116.886 134.823 175.333 1.00 27.63 ?  484 ALA B C     1 
ATOM   9424  O  O     . ALA B 1 484 ? 117.484 135.844 174.972 1.00 27.44 ?  484 ALA B O     1 
ATOM   9425  C  CB    . ALA B 1 484 ? 118.108 132.633 175.413 1.00 24.44 ?  484 ALA B CB    1 
ATOM   9426  N  N     . ARG B 1 485 ? 115.633 134.562 174.955 1.00 29.59 ?  485 ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 485 ? 114.898 135.524 174.141 1.00 22.93 ?  485 ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 485 ? 114.621 136.809 174.910 1.00 23.94 ?  485 ARG B C     1 
ATOM   9429  O  O     . ARG B 1 485 ? 114.650 137.895 174.326 1.00 33.77 ?  485 ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 485 ? 113.595 134.907 173.640 1.00 28.90 ?  485 ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 485 ? 113.796 133.789 172.633 1.00 27.03 ?  485 ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 485 ? 112.482 133.378 171.998 1.00 27.04 ?  485 ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 485 ? 111.499 132.957 172.989 1.00 27.22 ?  485 ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 485 ? 111.376 131.718 173.442 1.00 27.87 ?  485 ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 485 ? 112.170 130.746 173.022 1.00 25.07 1  485 ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 485 ? 110.432 131.446 174.337 1.00 30.16 ?  485 ARG B NH2   1 
ATOM   9437  N  N     . ASP B 1 486 ? 114.356 136.705 176.213 1.00 30.99 ?  486 ASP B N     1 
ATOM   9438  C  CA    . ASP B 1 486 ? 114.197 137.897 177.040 1.00 27.43 ?  486 ASP B CA    1 
ATOM   9439  C  C     . ASP B 1 486 ? 115.483 138.714 177.082 1.00 26.61 ?  486 ASP B C     1 
ATOM   9440  O  O     . ASP B 1 486 ? 115.453 139.949 176.967 1.00 33.37 ?  486 ASP B O     1 
ATOM   9441  C  CB    . ASP B 1 486 ? 113.770 137.487 178.449 1.00 32.56 ?  486 ASP B CB    1 
ATOM   9442  C  CG    . ASP B 1 486 ? 113.438 138.670 179.328 1.00 40.37 ?  486 ASP B CG    1 
ATOM   9443  O  OD1   . ASP B 1 486 ? 112.634 139.525 178.904 1.00 37.86 ?  486 ASP B OD1   1 
ATOM   9444  O  OD2   . ASP B 1 486 ? 113.981 138.735 180.450 1.00 37.16 -1 486 ASP B OD2   1 
ATOM   9445  N  N     . PHE B 1 487 ? 116.623 138.040 177.240 1.00 25.12 ?  487 PHE B N     1 
ATOM   9446  C  CA    . PHE B 1 487 ? 117.900 138.742 177.221 1.00 24.05 ?  487 PHE B CA    1 
ATOM   9447  C  C     . PHE B 1 487 ? 118.131 139.420 175.880 1.00 23.70 ?  487 PHE B C     1 
ATOM   9448  O  O     . PHE B 1 487 ? 118.598 140.560 175.825 1.00 29.55 ?  487 PHE B O     1 
ATOM   9449  C  CB    . PHE B 1 487 ? 119.055 137.791 177.520 1.00 25.33 ?  487 PHE B CB    1 
ATOM   9450  C  CG    . PHE B 1 487 ? 120.386 138.343 177.106 1.00 27.57 ?  487 PHE B CG    1 
ATOM   9451  C  CD1   . PHE B 1 487 ? 121.007 139.315 177.869 1.00 22.50 ?  487 PHE B CD1   1 
ATOM   9452  C  CD2   . PHE B 1 487 ? 120.995 137.929 175.933 1.00 29.01 ?  487 PHE B CD2   1 
ATOM   9453  C  CE1   . PHE B 1 487 ? 122.216 139.846 177.486 1.00 24.30 ?  487 PHE B CE1   1 
ATOM   9454  C  CE2   . PHE B 1 487 ? 122.205 138.460 175.545 1.00 25.24 ?  487 PHE B CE2   1 
ATOM   9455  C  CZ    . PHE B 1 487 ? 122.817 139.420 176.324 1.00 27.43 ?  487 PHE B CZ    1 
ATOM   9456  N  N     . ALA B 1 488 ? 117.846 138.714 174.785 1.00 24.45 ?  488 ALA B N     1 
ATOM   9457  C  CA    . ALA B 1 488 ? 118.034 139.304 173.465 1.00 19.89 ?  488 ALA B CA    1 
ATOM   9458  C  C     . ALA B 1 488 ? 117.137 140.519 173.282 1.00 26.39 ?  488 ALA B C     1 
ATOM   9459  O  O     . ALA B 1 488 ? 117.579 141.557 172.779 1.00 31.88 ?  488 ALA B O     1 
ATOM   9460  C  CB    . ALA B 1 488 ? 117.763 138.265 172.378 1.00 20.17 ?  488 ALA B CB    1 
ATOM   9461  N  N     . ASN B 1 489 ? 115.880 140.413 173.714 1.00 25.22 ?  489 ASN B N     1 
ATOM   9462  C  CA    . ASN B 1 489 ? 114.956 141.538 173.637 1.00 24.36 ?  489 ASN B CA    1 
ATOM   9463  C  C     . ASN B 1 489 ? 115.512 142.751 174.366 1.00 23.95 ?  489 ASN B C     1 
ATOM   9464  O  O     . ASN B 1 489 ? 115.613 143.842 173.793 1.00 24.39 ?  489 ASN B O     1 
ATOM   9465  C  CB    . ASN B 1 489 ? 113.603 141.132 174.221 1.00 21.91 ?  489 ASN B CB    1 
ATOM   9466  C  CG    . ASN B 1 489 ? 112.524 142.156 173.962 1.00 27.14 ?  489 ASN B CG    1 
ATOM   9467  O  OD1   . ASN B 1 489 ? 112.388 142.664 172.851 1.00 33.77 ?  489 ASN B OD1   1 
ATOM   9468  N  ND2   . ASN B 1 489 ? 111.743 142.462 174.989 1.00 30.58 ?  489 ASN B ND2   1 
ATOM   9469  N  N     . THR B 1 490 ? 115.912 142.570 175.626 1.00 27.27 ?  490 THR B N     1 
ATOM   9470  C  CA    . THR B 1 490 ? 116.398 143.703 176.408 1.00 22.97 ?  490 THR B CA    1 
ATOM   9471  C  C     . THR B 1 490 ? 117.693 144.265 175.832 1.00 24.75 ?  490 THR B C     1 
ATOM   9472  O  O     . THR B 1 490 ? 117.833 145.484 175.664 1.00 25.78 ?  490 THR B O     1 
ATOM   9473  C  CB    . THR B 1 490 ? 116.595 143.293 177.866 1.00 28.98 ?  490 THR B CB    1 
ATOM   9474  O  OG1   . THR B 1 490 ? 115.377 142.736 178.376 1.00 32.64 ?  490 THR B OG1   1 
ATOM   9475  C  CG2   . THR B 1 490 ? 116.990 144.499 178.702 1.00 26.06 ?  490 THR B CG2   1 
ATOM   9476  N  N     . PHE B 1 491 ? 118.650 143.389 175.513 1.00 24.63 ?  491 PHE B N     1 
ATOM   9477  C  CA    . PHE B 1 491 ? 119.953 143.839 175.039 1.00 19.07 ?  491 PHE B CA    1 
ATOM   9478  C  C     . PHE B 1 491 ? 119.833 144.591 173.723 1.00 19.39 ?  491 PHE B C     1 
ATOM   9479  O  O     . PHE B 1 491 ? 120.450 145.648 173.546 1.00 28.67 ?  491 PHE B O     1 
ATOM   9480  C  CB    . PHE B 1 491 ? 120.893 142.642 174.890 1.00 25.23 ?  491 PHE B CB    1 
ATOM   9481  C  CG    . PHE B 1 491 ? 122.209 142.979 174.246 1.00 23.98 ?  491 PHE B CG    1 
ATOM   9482  C  CD1   . PHE B 1 491 ? 123.265 143.445 175.009 1.00 19.94 ?  491 PHE B CD1   1 
ATOM   9483  C  CD2   . PHE B 1 491 ? 122.394 142.825 172.881 1.00 19.44 ?  491 PHE B CD2   1 
ATOM   9484  C  CE1   . PHE B 1 491 ? 124.476 143.756 174.426 1.00 16.87 ?  491 PHE B CE1   1 
ATOM   9485  C  CE2   . PHE B 1 491 ? 123.600 143.138 172.293 1.00 17.20 ?  491 PHE B CE2   1 
ATOM   9486  C  CZ    . PHE B 1 491 ? 124.643 143.604 173.067 1.00 23.78 ?  491 PHE B CZ    1 
ATOM   9487  N  N     . PHE B 1 492 ? 119.046 144.070 172.784 1.00 17.42 ?  492 PHE B N     1 
ATOM   9488  C  CA    . PHE B 1 492 ? 118.935 144.729 171.495 1.00 12.24 ?  492 PHE B CA    1 
ATOM   9489  C  C     . PHE B 1 492 ? 118.013 145.938 171.534 1.00 13.03 ?  492 PHE B C     1 
ATOM   9490  O  O     . PHE B 1 492 ? 118.194 146.853 170.728 1.00 24.31 ?  492 PHE B O     1 
ATOM   9491  C  CB    . PHE B 1 492 ? 118.493 143.719 170.439 1.00 17.91 ?  492 PHE B CB    1 
ATOM   9492  C  CG    . PHE B 1 492 ? 119.586 142.771 170.039 1.00 20.42 ?  492 PHE B CG    1 
ATOM   9493  C  CD1   . PHE B 1 492 ? 120.611 143.188 169.209 1.00 14.94 ?  492 PHE B CD1   1 
ATOM   9494  C  CD2   . PHE B 1 492 ? 119.613 141.476 170.525 1.00 19.18 ?  492 PHE B CD2   1 
ATOM   9495  C  CE1   . PHE B 1 492 ? 121.627 142.325 168.853 1.00 10.03 ?  492 PHE B CE1   1 
ATOM   9496  C  CE2   . PHE B 1 492 ? 120.625 140.609 170.174 1.00 15.06 ?  492 PHE B CE2   1 
ATOM   9497  C  CZ    . PHE B 1 492 ? 121.633 141.034 169.336 1.00 15.00 ?  492 PHE B CZ    1 
ATOM   9498  N  N     . MET B 1 493 ? 117.068 145.999 172.477 1.00 16.96 ?  493 MET B N     1 
ATOM   9499  C  CA    . MET B 1 493 ? 116.365 147.257 172.701 1.00 17.53 ?  493 MET B CA    1 
ATOM   9500  C  C     . MET B 1 493 ? 117.323 148.322 173.219 1.00 17.63 ?  493 MET B C     1 
ATOM   9501  O  O     . MET B 1 493 ? 117.254 149.480 172.798 1.00 26.01 ?  493 MET B O     1 
ATOM   9502  C  CB    . MET B 1 493 ? 115.192 147.043 173.662 1.00 17.60 ?  493 MET B CB    1 
ATOM   9503  C  CG    . MET B 1 493 ? 114.556 148.313 174.232 1.00 20.72 ?  493 MET B CG    1 
ATOM   9504  S  SD    . MET B 1 493 ? 115.401 149.040 175.653 1.00 30.63 ?  493 MET B SD    1 
ATOM   9505  C  CE    . MET B 1 493 ? 115.398 147.653 176.781 1.00 24.03 ?  493 MET B CE    1 
ATOM   9506  N  N     . MET B 1 494 ? 118.226 147.947 174.131 1.00 21.86 ?  494 MET B N     1 
ATOM   9507  C  CA    . MET B 1 494 ? 119.250 148.883 174.592 1.00 16.39 ?  494 MET B CA    1 
ATOM   9508  C  C     . MET B 1 494 ? 120.151 149.328 173.447 1.00 19.03 ?  494 MET B C     1 
ATOM   9509  O  O     . MET B 1 494 ? 120.484 150.516 173.328 1.00 22.87 ?  494 MET B O     1 
ATOM   9510  C  CB    . MET B 1 494 ? 120.088 148.244 175.700 1.00 20.19 ?  494 MET B CB    1 
ATOM   9511  C  CG    . MET B 1 494 ? 119.330 147.911 176.970 1.00 20.19 ?  494 MET B CG    1 
ATOM   9512  S  SD    . MET B 1 494 ? 120.441 147.746 178.380 1.00 37.53 ?  494 MET B SD    1 
ATOM   9513  C  CE    . MET B 1 494 ? 120.849 149.457 178.701 1.00 30.33 ?  494 MET B CE    1 
ATOM   9514  N  N     . VAL B 1 495 ? 120.565 148.383 172.602 1.00 19.01 ?  495 VAL B N     1 
ATOM   9515  C  CA    . VAL B 1 495 ? 121.421 148.712 171.467 1.00 17.66 ?  495 VAL B CA    1 
ATOM   9516  C  C     . VAL B 1 495 ? 120.708 149.670 170.522 1.00 17.55 ?  495 VAL B C     1 
ATOM   9517  O  O     . VAL B 1 495 ? 121.292 150.657 170.065 1.00 28.72 ?  495 VAL B O     1 
ATOM   9518  C  CB    . VAL B 1 495 ? 121.869 147.429 170.743 1.00 15.28 ?  495 VAL B CB    1 
ATOM   9519  C  CG1   . VAL B 1 495 ? 122.523 147.767 169.413 1.00 10.14 ?  495 VAL B CG1   1 
ATOM   9520  C  CG2   . VAL B 1 495 ? 122.823 146.637 171.615 1.00 19.24 ?  495 VAL B CG2   1 
ATOM   9521  N  N     . ASN B 1 496 ? 119.436 149.399 170.219 1.00 19.18 ?  496 ASN B N     1 
ATOM   9522  C  CA    . ASN B 1 496 ? 118.670 150.288 169.352 1.00 12.13 ?  496 ASN B CA    1 
ATOM   9523  C  C     . ASN B 1 496 ? 118.501 151.664 169.980 1.00 19.26 ?  496 ASN B C     1 
ATOM   9524  O  O     . ASN B 1 496 ? 118.627 152.685 169.296 1.00 30.91 ?  496 ASN B O     1 
ATOM   9525  C  CB    . ASN B 1 496 ? 117.307 149.671 169.043 1.00 16.23 ?  496 ASN B CB    1 
ATOM   9526  C  CG    . ASN B 1 496 ? 116.640 150.307 167.843 1.00 16.08 ?  496 ASN B CG    1 
ATOM   9527  O  OD1   . ASN B 1 496 ? 117.309 150.788 166.930 1.00 24.74 ?  496 ASN B OD1   1 
ATOM   9528  N  ND2   . ASN B 1 496 ? 115.314 150.316 167.839 1.00 15.35 ?  496 ASN B ND2   1 
ATOM   9529  N  N     . PHE B 1 497 ? 118.217 151.711 171.282 1.00 20.27 ?  497 PHE B N     1 
ATOM   9530  C  CA    . PHE B 1 497 ? 118.041 152.985 171.968 1.00 15.60 ?  497 PHE B CA    1 
ATOM   9531  C  C     . PHE B 1 497 ? 119.303 153.827 171.878 1.00 19.24 ?  497 PHE B C     1 
ATOM   9532  O  O     . PHE B 1 497 ? 119.255 155.007 171.513 1.00 26.32 ?  497 PHE B O     1 
ATOM   9533  C  CB    . PHE B 1 497 ? 117.661 152.737 173.429 1.00 17.84 ?  497 PHE B CB    1 
ATOM   9534  C  CG    . PHE B 1 497 ? 117.507 153.989 174.245 1.00 20.97 ?  497 PHE B CG    1 
ATOM   9535  C  CD1   . PHE B 1 497 ? 118.591 154.537 174.914 1.00 21.66 ?  497 PHE B CD1   1 
ATOM   9536  C  CD2   . PHE B 1 497 ? 116.277 154.612 174.353 1.00 21.23 ?  497 PHE B CD2   1 
ATOM   9537  C  CE1   . PHE B 1 497 ? 118.449 155.686 175.664 1.00 22.63 ?  497 PHE B CE1   1 
ATOM   9538  C  CE2   . PHE B 1 497 ? 116.130 155.761 175.103 1.00 20.87 ?  497 PHE B CE2   1 
ATOM   9539  C  CZ    . PHE B 1 497 ? 117.218 156.297 175.760 1.00 23.33 ?  497 PHE B CZ    1 
ATOM   9540  N  N     . TYR B 1 498 ? 120.452 153.230 172.191 1.00 26.89 ?  498 TYR B N     1 
ATOM   9541  C  CA    . TYR B 1 498 ? 121.684 154.006 172.198 1.00 18.43 ?  498 TYR B CA    1 
ATOM   9542  C  C     . TYR B 1 498 ? 122.178 154.305 170.789 1.00 18.27 ?  498 TYR B C     1 
ATOM   9543  O  O     . TYR B 1 498 ? 122.808 155.344 170.574 1.00 26.71 ?  498 TYR B O     1 
ATOM   9544  C  CB    . TYR B 1 498 ? 122.746 153.285 173.025 1.00 18.97 ?  498 TYR B CB    1 
ATOM   9545  C  CG    . TYR B 1 498 ? 122.433 153.332 174.503 1.00 22.61 ?  498 TYR B CG    1 
ATOM   9546  C  CD1   . TYR B 1 498 ? 122.270 154.548 175.153 1.00 23.34 ?  498 TYR B CD1   1 
ATOM   9547  C  CD2   . TYR B 1 498 ? 122.273 152.168 175.241 1.00 26.29 ?  498 TYR B CD2   1 
ATOM   9548  C  CE1   . TYR B 1 498 ? 121.971 154.604 176.498 1.00 24.09 ?  498 TYR B CE1   1 
ATOM   9549  C  CE2   . TYR B 1 498 ? 121.974 152.214 176.588 1.00 25.24 ?  498 TYR B CE2   1 
ATOM   9550  C  CZ    . TYR B 1 498 ? 121.824 153.435 177.211 1.00 29.24 ?  498 TYR B CZ    1 
ATOM   9551  O  OH    . TYR B 1 498 ? 121.528 153.489 178.553 1.00 35.73 ?  498 TYR B OH    1 
ATOM   9552  N  N     . SER B 1 499 ? 121.867 153.449 169.813 1.00 19.26 ?  499 SER B N     1 
ATOM   9553  C  CA    . SER B 1 499 ? 122.196 153.764 168.428 1.00 13.36 ?  499 SER B CA    1 
ATOM   9554  C  C     . SER B 1 499 ? 121.371 154.941 167.922 1.00 18.33 ?  499 SER B C     1 
ATOM   9555  O  O     . SER B 1 499 ? 121.902 155.832 167.252 1.00 20.27 ?  499 SER B O     1 
ATOM   9556  C  CB    . SER B 1 499 ? 121.982 152.535 167.546 1.00 14.93 ?  499 SER B CB    1 
ATOM   9557  O  OG    . SER B 1 499 ? 122.653 152.674 166.308 1.00 19.27 ?  499 SER B OG    1 
ATOM   9558  N  N     . ILE B 1 500 ? 120.074 154.965 168.240 1.00 18.14 ?  500 ILE B N     1 
ATOM   9559  C  CA    . ILE B 1 500 ? 119.235 156.100 167.866 1.00 20.90 ?  500 ILE B CA    1 
ATOM   9560  C  C     . ILE B 1 500 ? 119.707 157.361 168.572 1.00 19.50 ?  500 ILE B C     1 
ATOM   9561  O  O     . ILE B 1 500 ? 119.742 158.446 167.979 1.00 26.97 ?  500 ILE B O     1 
ATOM   9562  C  CB    . ILE B 1 500 ? 117.757 155.798 168.175 1.00 23.62 ?  500 ILE B CB    1 
ATOM   9563  C  CG1   . ILE B 1 500 ? 117.234 154.686 167.270 1.00 18.38 ?  500 ILE B CG1   1 
ATOM   9564  C  CG2   . ILE B 1 500 ? 116.905 157.042 168.010 1.00 18.21 ?  500 ILE B CG2   1 
ATOM   9565  C  CD1   . ILE B 1 500 ? 115.932 154.104 167.737 1.00 22.35 ?  500 ILE B CD1   1 
ATOM   9566  N  N     . GLN B 1 501 ? 120.074 157.242 169.849 1.00 20.82 ?  501 GLN B N     1 
ATOM   9567  C  CA    . GLN B 1 501 ? 120.568 158.398 170.587 1.00 22.83 ?  501 GLN B CA    1 
ATOM   9568  C  C     . GLN B 1 501 ? 121.848 158.942 169.969 1.00 24.83 ?  501 GLN B C     1 
ATOM   9569  O  O     . GLN B 1 501 ? 121.993 160.157 169.801 1.00 30.68 ?  501 GLN B O     1 
ATOM   9570  C  CB    . GLN B 1 501 ? 120.790 158.028 172.052 1.00 27.35 ?  501 GLN B CB    1 
ATOM   9571  C  CG    . GLN B 1 501 ? 120.709 159.206 173.004 1.00 24.19 ?  501 GLN B CG    1 
ATOM   9572  C  CD    . GLN B 1 501 ? 120.657 158.777 174.454 1.00 28.90 ?  501 GLN B CD    1 
ATOM   9573  O  OE1   . GLN B 1 501 ? 121.469 157.972 174.905 1.00 34.53 ?  501 GLN B OE1   1 
ATOM   9574  N  NE2   . GLN B 1 501 ? 119.695 159.314 175.195 1.00 31.97 ?  501 GLN B NE2   1 
ATOM   9575  N  N     . ARG B 1 502 ? 122.786 158.060 169.615 1.00 23.90 ?  502 ARG B N     1 
ATOM   9576  C  CA    . ARG B 1 502 ? 124.022 158.512 168.987 1.00 20.10 ?  502 ARG B CA    1 
ATOM   9577  C  C     . ARG B 1 502 ? 123.762 159.117 167.613 1.00 22.90 ?  502 ARG B C     1 
ATOM   9578  O  O     . ARG B 1 502 ? 124.392 160.110 167.243 1.00 30.30 ?  502 ARG B O     1 
ATOM   9579  C  CB    . ARG B 1 502 ? 125.018 157.359 168.882 1.00 23.30 ?  502 ARG B CB    1 
ATOM   9580  C  CG    . ARG B 1 502 ? 126.428 157.816 168.552 1.00 26.41 ?  502 ARG B CG    1 
ATOM   9581  C  CD    . ARG B 1 502 ? 126.856 158.958 169.456 1.00 26.01 ?  502 ARG B CD    1 
ATOM   9582  N  NE    . ARG B 1 502 ? 128.075 159.602 168.983 1.00 24.91 ?  502 ARG B NE    1 
ATOM   9583  C  CZ    . ARG B 1 502 ? 128.323 160.900 169.083 1.00 23.93 ?  502 ARG B CZ    1 
ATOM   9584  N  NH1   . ARG B 1 502 ? 127.459 161.727 169.647 1.00 30.63 1  502 ARG B NH1   1 
ATOM   9585  N  NH2   . ARG B 1 502 ? 129.468 161.380 168.607 1.00 28.82 ?  502 ARG B NH2   1 
ATOM   9586  N  N     . SER B 1 503 ? 122.849 158.527 166.838 1.00 23.38 ?  503 SER B N     1 
ATOM   9587  C  CA    . SER B 1 503 ? 122.524 159.085 165.530 1.00 22.11 ?  503 SER B CA    1 
ATOM   9588  C  C     . SER B 1 503 ? 121.935 160.483 165.665 1.00 23.05 ?  503 SER B C     1 
ATOM   9589  O  O     . SER B 1 503 ? 122.308 161.400 164.923 1.00 28.92 ?  503 SER B O     1 
ATOM   9590  C  CB    . SER B 1 503 ? 121.558 158.158 164.794 1.00 18.74 ?  503 SER B CB    1 
ATOM   9591  O  OG    . SER B 1 503 ? 121.650 158.326 163.392 1.00 24.69 ?  503 SER B OG    1 
ATOM   9592  N  N     . ALA B 1 504 ? 121.029 160.670 166.626 1.00 23.24 ?  504 ALA B N     1 
ATOM   9593  C  CA    . ALA B 1 504 ? 120.447 161.988 166.853 1.00 25.89 ?  504 ALA B CA    1 
ATOM   9594  C  C     . ALA B 1 504 ? 121.488 162.975 167.365 1.00 27.48 ?  504 ALA B C     1 
ATOM   9595  O  O     . ALA B 1 504 ? 121.466 164.154 166.994 1.00 34.08 ?  504 ALA B O     1 
ATOM   9596  C  CB    . ALA B 1 504 ? 119.276 161.879 167.828 1.00 26.38 ?  504 ALA B CB    1 
ATOM   9597  N  N     . GLU B 1 505 ? 122.412 162.516 168.213 1.00 25.13 ?  505 GLU B N     1 
ATOM   9598  C  CA    . GLU B 1 505 ? 123.466 163.396 168.709 1.00 25.65 ?  505 GLU B CA    1 
ATOM   9599  C  C     . GLU B 1 505 ? 124.408 163.820 167.589 1.00 26.97 ?  505 GLU B C     1 
ATOM   9600  O  O     . GLU B 1 505 ? 124.846 164.975 167.546 1.00 31.65 ?  505 GLU B O     1 
ATOM   9601  C  CB    . GLU B 1 505 ? 124.241 162.704 169.829 1.00 26.13 ?  505 GLU B CB    1 
ATOM   9602  C  CG    . GLU B 1 505 ? 123.494 162.637 171.148 1.00 27.47 ?  505 GLU B CG    1 
ATOM   9603  C  CD    . GLU B 1 505 ? 124.030 161.560 172.065 1.00 32.39 ?  505 GLU B CD    1 
ATOM   9604  O  OE1   . GLU B 1 505 ? 125.034 160.914 171.698 1.00 31.08 ?  505 GLU B OE1   1 
ATOM   9605  O  OE2   . GLU B 1 505 ? 123.452 161.358 173.153 1.00 34.66 -1 505 GLU B OE2   1 
ATOM   9606  N  N     . ILE B 1 506 ? 124.738 162.901 166.681 1.00 26.20 ?  506 ILE B N     1 
ATOM   9607  C  CA    . ILE B 1 506 ? 125.560 163.252 165.528 1.00 26.19 ?  506 ILE B CA    1 
ATOM   9608  C  C     . ILE B 1 506 ? 124.823 164.233 164.627 1.00 26.67 ?  506 ILE B C     1 
ATOM   9609  O  O     . ILE B 1 506 ? 125.414 165.191 164.114 1.00 33.16 ?  506 ILE B O     1 
ATOM   9610  C  CB    . ILE B 1 506 ? 125.984 161.984 164.765 1.00 25.49 ?  506 ILE B CB    1 
ATOM   9611  C  CG1   . ILE B 1 506 ? 126.878 161.106 165.640 1.00 28.34 ?  506 ILE B CG1   1 
ATOM   9612  C  CG2   . ILE B 1 506 ? 126.709 162.345 163.482 1.00 24.77 ?  506 ILE B CG2   1 
ATOM   9613  C  CD1   . ILE B 1 506 ? 127.100 159.718 165.086 1.00 21.69 ?  506 ILE B CD1   1 
ATOM   9614  N  N     . ALA B 1 507 ? 123.522 164.016 164.421 1.00 26.64 ?  507 ALA B N     1 
ATOM   9615  C  CA    . ALA B 1 507 ? 122.734 164.954 163.626 1.00 28.48 ?  507 ALA B CA    1 
ATOM   9616  C  C     . ALA B 1 507 ? 122.714 166.337 164.266 1.00 32.25 ?  507 ALA B C     1 
ATOM   9617  O  O     . ALA B 1 507 ? 122.778 167.355 163.568 1.00 36.65 ?  507 ALA B O     1 
ATOM   9618  C  CB    . ALA B 1 507 ? 121.313 164.423 163.447 1.00 24.25 ?  507 ALA B CB    1 
ATOM   9619  N  N     . LYS B 1 508 ? 122.616 166.390 165.595 1.00 32.69 ?  508 LYS B N     1 
ATOM   9620  C  CA    . LYS B 1 508 ? 122.634 167.667 166.300 1.00 30.69 ?  508 LYS B CA    1 
ATOM   9621  C  C     . LYS B 1 508 ? 123.994 168.348 166.191 1.00 36.95 ?  508 LYS B C     1 
ATOM   9622  O  O     . LYS B 1 508 ? 124.071 169.558 165.951 1.00 43.58 ?  508 LYS B O     1 
ATOM   9623  C  CB    . LYS B 1 508 ? 122.259 167.450 167.766 1.00 34.62 ?  508 LYS B CB    1 
ATOM   9624  C  CG    . LYS B 1 508 ? 122.367 168.687 168.637 1.00 35.60 ?  508 LYS B CG    1 
ATOM   9625  C  CD    . LYS B 1 508 ? 122.252 168.321 170.108 1.00 34.74 ?  508 LYS B CD    1 
ATOM   9626  C  CE    . LYS B 1 508 ? 122.055 169.552 170.975 1.00 36.44 ?  508 LYS B CE    1 
ATOM   9627  N  NZ    . LYS B 1 508 ? 121.268 169.244 172.200 1.00 38.05 1  508 LYS B NZ    1 
ATOM   9628  N  N     . GLU B 1 509 ? 125.076 167.585 166.363 1.00 34.40 ?  509 GLU B N     1 
ATOM   9629  C  CA    . GLU B 1 509 ? 126.411 168.174 166.359 1.00 35.15 ?  509 GLU B CA    1 
ATOM   9630  C  C     . GLU B 1 509 ? 126.844 168.592 164.960 1.00 36.28 ?  509 GLU B C     1 
ATOM   9631  O  O     . GLU B 1 509 ? 127.664 169.505 164.815 1.00 39.64 ?  509 GLU B O     1 
ATOM   9632  C  CB    . GLU B 1 509 ? 127.414 167.192 166.969 1.00 35.08 ?  509 GLU B CB    1 
ATOM   9633  C  CG    . GLU B 1 509 ? 128.215 166.387 165.959 1.00 32.91 ?  509 GLU B CG    1 
ATOM   9634  C  CD    . GLU B 1 509 ? 128.818 165.132 166.560 1.00 41.57 ?  509 GLU B CD    1 
ATOM   9635  O  OE1   . GLU B 1 509 ? 128.762 164.977 167.799 1.00 40.77 ?  509 GLU B OE1   1 
ATOM   9636  O  OE2   . GLU B 1 509 ? 129.344 164.298 165.794 1.00 40.46 -1 509 GLU B OE2   1 
ATOM   9637  N  N     . LYS B 1 510 ? 126.311 167.945 163.924 1.00 32.33 ?  510 LYS B N     1 
ATOM   9638  C  CA    . LYS B 1 510 ? 126.629 168.301 162.549 1.00 31.26 ?  510 LYS B CA    1 
ATOM   9639  C  C     . LYS B 1 510 ? 125.557 169.158 161.892 1.00 35.37 ?  510 LYS B C     1 
ATOM   9640  O  O     . LYS B 1 510 ? 125.787 169.669 160.790 1.00 39.87 ?  510 LYS B O     1 
ATOM   9641  C  CB    . LYS B 1 510 ? 126.853 167.035 161.713 1.00 30.84 ?  510 LYS B CB    1 
ATOM   9642  C  CG    . LYS B 1 510 ? 127.918 166.112 162.272 1.00 32.21 ?  510 LYS B CG    1 
ATOM   9643  C  CD    . LYS B 1 510 ? 128.373 165.097 161.241 1.00 31.73 ?  510 LYS B CD    1 
ATOM   9644  C  CE    . LYS B 1 510 ? 129.524 164.258 161.769 1.00 33.69 ?  510 LYS B CE    1 
ATOM   9645  N  NZ    . LYS B 1 510 ? 130.497 163.915 160.698 1.00 32.53 1  510 LYS B NZ    1 
ATOM   9646  N  N     . GLY B 1 511 ? 124.404 169.328 162.534 1.00 32.71 ?  511 GLY B N     1 
ATOM   9647  C  CA    . GLY B 1 511 ? 123.336 170.124 161.965 1.00 32.43 ?  511 GLY B CA    1 
ATOM   9648  C  C     . GLY B 1 511 ? 122.697 169.546 160.725 1.00 36.03 ?  511 GLY B C     1 
ATOM   9649  O  O     . GLY B 1 511 ? 121.958 170.258 160.040 1.00 39.42 ?  511 GLY B O     1 
ATOM   9650  N  N     . GLU B 1 512 ? 122.955 168.279 160.413 1.00 33.04 ?  512 GLU B N     1 
ATOM   9651  C  CA    . GLU B 1 512 ? 122.426 167.646 159.215 1.00 29.38 ?  512 GLU B CA    1 
ATOM   9652  C  C     . GLU B 1 512 ? 121.905 166.257 159.545 1.00 31.47 ?  512 GLU B C     1 
ATOM   9653  O  O     . GLU B 1 512 ? 122.478 165.546 160.376 1.00 32.91 ?  512 GLU B O     1 
ATOM   9654  C  CB    . GLU B 1 512 ? 123.493 167.553 158.115 1.00 31.29 ?  512 GLU B CB    1 
ATOM   9655  C  CG    . GLU B 1 512 ? 124.790 166.900 158.557 1.00 31.45 ?  512 GLU B CG    1 
ATOM   9656  C  CD    . GLU B 1 512 ? 125.559 166.293 157.400 1.00 36.04 ?  512 GLU B CD    1 
ATOM   9657  O  OE1   . GLU B 1 512 ? 124.916 165.820 156.440 1.00 32.30 ?  512 GLU B OE1   1 
ATOM   9658  O  OE2   . GLU B 1 512 ? 126.808 166.286 157.451 1.00 36.73 -1 512 GLU B OE2   1 
ATOM   9659  N  N     . THR B 1 513 ? 120.811 165.882 158.893 1.00 31.96 ?  513 THR B N     1 
ATOM   9660  C  CA    . THR B 1 513 ? 120.242 164.547 158.965 1.00 26.26 ?  513 THR B CA    1 
ATOM   9661  C  C     . THR B 1 513 ? 120.501 163.824 157.647 1.00 27.02 ?  513 THR B C     1 
ATOM   9662  O  O     . THR B 1 513 ? 121.103 164.373 156.721 1.00 34.08 ?  513 THR B O     1 
ATOM   9663  C  CB    . THR B 1 513 ? 118.744 164.616 159.273 1.00 27.27 ?  513 THR B CB    1 
ATOM   9664  O  OG1   . THR B 1 513 ? 118.065 165.276 158.199 1.00 29.20 ?  513 THR B OG1   1 
ATOM   9665  C  CG2   . THR B 1 513 ? 118.504 165.386 160.559 1.00 24.46 ?  513 THR B CG2   1 
ATOM   9666  N  N     . PHE B 1 514 ? 120.045 162.578 157.563 1.00 21.67 ?  514 PHE B N     1 
ATOM   9667  C  CA    . PHE B 1 514 ? 120.149 161.884 156.292 1.00 22.78 ?  514 PHE B CA    1 
ATOM   9668  C  C     . PHE B 1 514 ? 119.086 162.401 155.329 1.00 22.05 ?  514 PHE B C     1 
ATOM   9669  O  O     . PHE B 1 514 ? 118.070 162.972 155.734 1.00 26.25 ?  514 PHE B O     1 
ATOM   9670  C  CB    . PHE B 1 514 ? 120.033 160.367 156.475 1.00 19.13 ?  514 PHE B CB    1 
ATOM   9671  C  CG    . PHE B 1 514 ? 118.696 159.900 156.982 1.00 19.25 ?  514 PHE B CG    1 
ATOM   9672  C  CD1   . PHE B 1 514 ? 118.447 159.813 158.340 1.00 17.52 ?  514 PHE B CD1   1 
ATOM   9673  C  CD2   . PHE B 1 514 ? 117.700 159.516 156.098 1.00 19.76 ?  514 PHE B CD2   1 
ATOM   9674  C  CE1   . PHE B 1 514 ? 117.227 159.368 158.806 1.00 20.16 ?  514 PHE B CE1   1 
ATOM   9675  C  CE2   . PHE B 1 514 ? 116.479 159.073 156.559 1.00 14.93 ?  514 PHE B CE2   1 
ATOM   9676  C  CZ    . PHE B 1 514 ? 116.242 158.999 157.915 1.00 21.93 ?  514 PHE B CZ    1 
ATOM   9677  N  N     . ASP B 1 515 ? 119.341 162.209 154.039 1.00 25.10 ?  515 ASP B N     1 
ATOM   9678  C  CA    . ASP B 1 515 ? 118.459 162.756 153.019 1.00 26.53 ?  515 ASP B CA    1 
ATOM   9679  C  C     . ASP B 1 515 ? 117.064 162.158 153.132 1.00 31.04 ?  515 ASP B C     1 
ATOM   9680  O  O     . ASP B 1 515 ? 116.900 160.953 153.345 1.00 40.44 ?  515 ASP B O     1 
ATOM   9681  C  CB    . ASP B 1 515 ? 119.033 162.497 151.627 1.00 29.27 ?  515 ASP B CB    1 
ATOM   9682  C  CG    . ASP B 1 515 ? 119.972 163.595 151.173 1.00 33.63 ?  515 ASP B CG    1 
ATOM   9683  O  OD1   . ASP B 1 515 ? 120.431 164.378 152.031 1.00 32.53 ?  515 ASP B OD1   1 
ATOM   9684  O  OD2   . ASP B 1 515 ? 120.253 163.676 149.960 1.00 38.46 -1 515 ASP B OD2   1 
ATOM   9685  N  N     . GLN B 1 516 ? 116.054 163.021 152.995 1.00 28.92 ?  516 GLN B N     1 
ATOM   9686  C  CA    . GLN B 1 516 ? 114.647 162.635 153.088 1.00 26.49 ?  516 GLN B CA    1 
ATOM   9687  C  C     . GLN B 1 516 ? 114.306 162.054 154.458 1.00 27.05 ?  516 GLN B C     1 
ATOM   9688  O  O     . GLN B 1 516 ? 113.450 161.176 154.572 1.00 32.99 ?  516 GLN B O     1 
ATOM   9689  C  CB    . GLN B 1 516 ? 114.262 161.650 151.982 1.00 26.22 ?  516 GLN B CB    1 
ATOM   9690  C  CG    . GLN B 1 516 ? 114.494 162.158 150.574 1.00 29.62 ?  516 GLN B CG    1 
ATOM   9691  C  CD    . GLN B 1 516 ? 114.333 161.068 149.535 1.00 32.34 ?  516 GLN B CD    1 
ATOM   9692  O  OE1   . GLN B 1 516 ? 113.219 160.643 149.232 1.00 29.80 ?  516 GLN B OE1   1 
ATOM   9693  N  NE2   . GLN B 1 516 ? 115.449 160.605 148.984 1.00 32.48 ?  516 GLN B NE2   1 
ATOM   9694  N  N     . TYR B 1 517 ? 114.971 162.533 155.510 1.00 24.80 ?  517 TYR B N     1 
ATOM   9695  C  CA    . TYR B 1 517 ? 114.634 162.074 156.853 1.00 22.80 ?  517 TYR B CA    1 
ATOM   9696  C  C     . TYR B 1 517 ? 113.248 162.546 157.275 1.00 29.59 ?  517 TYR B C     1 
ATOM   9697  O  O     . TYR B 1 517 ? 112.580 161.872 158.069 1.00 35.82 ?  517 TYR B O     1 
ATOM   9698  C  CB    . TYR B 1 517 ? 115.684 162.550 157.859 1.00 18.52 ?  517 TYR B CB    1 
ATOM   9699  C  CG    . TYR B 1 517 ? 115.135 162.766 159.252 1.00 28.00 ?  517 TYR B CG    1 
ATOM   9700  C  CD1   . TYR B 1 517 ? 114.976 161.701 160.130 1.00 23.79 ?  517 TYR B CD1   1 
ATOM   9701  C  CD2   . TYR B 1 517 ? 114.766 164.034 159.686 1.00 29.52 ?  517 TYR B CD2   1 
ATOM   9702  C  CE1   . TYR B 1 517 ? 114.467 161.894 161.398 1.00 27.50 ?  517 TYR B CE1   1 
ATOM   9703  C  CE2   . TYR B 1 517 ? 114.256 164.233 160.950 1.00 24.93 ?  517 TYR B CE2   1 
ATOM   9704  C  CZ    . TYR B 1 517 ? 114.108 163.160 161.802 1.00 27.75 ?  517 TYR B CZ    1 
ATOM   9705  O  OH    . TYR B 1 517 ? 113.603 163.358 163.065 1.00 36.93 ?  517 TYR B OH    1 
ATOM   9706  N  N     . GLU B 1 518 ? 112.797 163.688 156.751 1.00 28.16 ?  518 GLU B N     1 
ATOM   9707  C  CA    . GLU B 1 518 ? 111.553 164.292 157.219 1.00 30.08 ?  518 GLU B CA    1 
ATOM   9708  C  C     . GLU B 1 518 ? 110.348 163.401 156.948 1.00 34.42 ?  518 GLU B C     1 
ATOM   9709  O  O     . GLU B 1 518 ? 109.378 163.425 157.715 1.00 35.10 ?  518 GLU B O     1 
ATOM   9710  C  CB    . GLU B 1 518 ? 111.356 165.661 156.568 1.00 29.58 ?  518 GLU B CB    1 
ATOM   9711  C  CG    . GLU B 1 518 ? 112.433 166.685 156.908 1.00 34.09 ?  518 GLU B CG    1 
ATOM   9712  C  CD    . GLU B 1 518 ? 113.711 166.484 156.114 1.00 41.01 ?  518 GLU B CD    1 
ATOM   9713  O  OE1   . GLU B 1 518 ? 113.627 166.018 154.957 1.00 38.63 ?  518 GLU B OE1   1 
ATOM   9714  O  OE2   . GLU B 1 518 ? 114.799 166.790 156.646 1.00 38.53 -1 518 GLU B OE2   1 
ATOM   9715  N  N     . GLY B 1 519 ? 110.381 162.619 155.875 1.00 23.98 ?  519 GLY B N     1 
ATOM   9716  C  CA    . GLY B 1 519 ? 109.314 161.689 155.579 1.00 20.26 ?  519 GLY B CA    1 
ATOM   9717  C  C     . GLY B 1 519 ? 109.417 160.352 156.270 1.00 19.74 ?  519 GLY B C     1 
ATOM   9718  O  O     . GLY B 1 519 ? 108.507 159.527 156.141 1.00 28.28 ?  519 GLY B O     1 
ATOM   9719  N  N     . SER B 1 520 ? 110.497 160.108 157.005 1.00 21.17 ?  520 SER B N     1 
ATOM   9720  C  CA    . SER B 1 520 ? 110.709 158.827 157.657 1.00 22.77 ?  520 SER B CA    1 
ATOM   9721  C  C     . SER B 1 520 ? 109.853 158.708 158.913 1.00 22.36 ?  520 SER B C     1 
ATOM   9722  O  O     . SER B 1 520 ? 109.326 159.691 159.440 1.00 24.18 ?  520 SER B O     1 
ATOM   9723  C  CB    . SER B 1 520 ? 112.184 158.642 158.010 1.00 18.69 ?  520 SER B CB    1 
ATOM   9724  O  OG    . SER B 1 520 ? 112.613 159.620 158.939 1.00 23.96 ?  520 SER B OG    1 
ATOM   9725  N  N     . THR B 1 521 ? 109.714 157.468 159.389 1.00 21.97 ?  521 THR B N     1 
ATOM   9726  C  CA    . THR B 1 521 ? 108.980 157.225 160.624 1.00 18.95 ?  521 THR B CA    1 
ATOM   9727  C  C     . THR B 1 521 ? 109.733 157.730 161.847 1.00 25.21 ?  521 THR B C     1 
ATOM   9728  O  O     . THR B 1 521 ? 109.128 157.883 162.912 1.00 26.86 ?  521 THR B O     1 
ATOM   9729  C  CB    . THR B 1 521 ? 108.677 155.734 160.775 1.00 24.09 ?  521 THR B CB    1 
ATOM   9730  O  OG1   . THR B 1 521 ? 109.878 155.029 161.107 1.00 29.44 ?  521 THR B OG1   1 
ATOM   9731  C  CG2   . THR B 1 521 ? 108.113 155.176 159.482 1.00 15.63 ?  521 THR B CG2   1 
ATOM   9732  N  N     . TYR B 1 522 ? 111.039 157.981 161.722 1.00 25.01 ?  522 TYR B N     1 
ATOM   9733  C  CA    . TYR B 1 522 ? 111.771 158.629 162.804 1.00 20.83 ?  522 TYR B CA    1 
ATOM   9734  C  C     . TYR B 1 522 ? 111.288 160.058 163.011 1.00 25.33 ?  522 TYR B C     1 
ATOM   9735  O  O     . TYR B 1 522 ? 111.131 160.510 164.151 1.00 24.25 ?  522 TYR B O     1 
ATOM   9736  C  CB    . TYR B 1 522 ? 113.271 158.617 162.510 1.00 18.01 ?  522 TYR B CB    1 
ATOM   9737  C  CG    . TYR B 1 522 ? 113.894 157.242 162.465 1.00 24.21 ?  522 TYR B CG    1 
ATOM   9738  C  CD1   . TYR B 1 522 ? 113.955 156.445 163.601 1.00 24.70 ?  522 TYR B CD1   1 
ATOM   9739  C  CD2   . TYR B 1 522 ? 114.437 156.747 161.288 1.00 22.12 ?  522 TYR B CD2   1 
ATOM   9740  C  CE1   . TYR B 1 522 ? 114.530 155.192 163.561 1.00 24.61 ?  522 TYR B CE1   1 
ATOM   9741  C  CE2   . TYR B 1 522 ? 115.015 155.495 161.241 1.00 20.99 ?  522 TYR B CE2   1 
ATOM   9742  C  CZ    . TYR B 1 522 ? 115.058 154.722 162.379 1.00 22.49 ?  522 TYR B CZ    1 
ATOM   9743  O  OH    . TYR B 1 522 ? 115.631 153.474 162.334 1.00 28.05 ?  522 TYR B OH    1 
ATOM   9744  N  N     . ALA B 1 523 ? 111.048 160.785 161.916 1.00 27.79 ?  523 ALA B N     1 
ATOM   9745  C  CA    . ALA B 1 523 ? 110.618 162.175 162.022 1.00 30.41 ?  523 ALA B CA    1 
ATOM   9746  C  C     . ALA B 1 523 ? 109.184 162.278 162.522 1.00 29.48 ?  523 ALA B C     1 
ATOM   9747  O  O     . ALA B 1 523 ? 108.861 163.167 163.318 1.00 28.29 ?  523 ALA B O     1 
ATOM   9748  C  CB    . ALA B 1 523 ? 110.768 162.872 160.671 1.00 27.66 ?  523 ALA B CB    1 
ATOM   9749  N  N     . THR B 1 524 ? 108.310 161.382 162.065 1.00 26.48 ?  524 THR B N     1 
ATOM   9750  C  CA    . THR B 1 524 ? 106.909 161.414 162.461 1.00 27.99 ?  524 THR B CA    1 
ATOM   9751  C  C     . THR B 1 524 ? 106.664 160.811 163.838 1.00 33.26 ?  524 THR B C     1 
ATOM   9752  O  O     . THR B 1 524 ? 105.561 160.968 164.374 1.00 38.05 ?  524 THR B O     1 
ATOM   9753  C  CB    . THR B 1 524 ? 106.051 160.681 161.426 1.00 28.49 ?  524 THR B CB    1 
ATOM   9754  O  OG1   . THR B 1 524 ? 106.336 159.278 161.473 1.00 32.57 ?  524 THR B OG1   1 
ATOM   9755  C  CG2   . THR B 1 524 ? 106.339 161.205 160.029 1.00 27.48 ?  524 THR B CG2   1 
ATOM   9756  N  N     . GLY B 1 525 ? 107.651 160.135 164.419 1.00 25.50 ?  525 GLY B N     1 
ATOM   9757  C  CA    . GLY B 1 525 ? 107.496 159.515 165.716 1.00 23.63 ?  525 GLY B CA    1 
ATOM   9758  C  C     . GLY B 1 525 ? 106.836 158.156 165.704 1.00 26.91 ?  525 GLY B C     1 
ATOM   9759  O  O     . GLY B 1 525 ? 106.683 157.551 166.772 1.00 31.03 ?  525 GLY B O     1 
ATOM   9760  N  N     . GLU B 1 526 ? 106.438 157.655 164.532 1.00 31.40 ?  526 GLU B N     1 
ATOM   9761  C  CA    . GLU B 1 526 ? 105.800 156.344 164.461 1.00 30.90 ?  526 GLU B CA    1 
ATOM   9762  C  C     . GLU B 1 526 ? 106.766 155.237 164.865 1.00 31.91 ?  526 GLU B C     1 
ATOM   9763  O  O     . GLU B 1 526 ? 106.370 154.266 165.521 1.00 36.63 ?  526 GLU B O     1 
ATOM   9764  C  CB    . GLU B 1 526 ? 105.259 156.109 163.051 1.00 29.22 ?  526 GLU B CB    1 
ATOM   9765  C  CG    . GLU B 1 526 ? 104.868 154.672 162.753 1.00 33.58 ?  526 GLU B CG    1 
ATOM   9766  C  CD    . GLU B 1 526 ? 104.725 154.406 161.268 1.00 39.33 ?  526 GLU B CD    1 
ATOM   9767  O  OE1   . GLU B 1 526 ? 104.182 155.276 160.556 1.00 39.85 ?  526 GLU B OE1   1 
ATOM   9768  O  OE2   . GLU B 1 526 ? 105.158 153.327 160.811 1.00 35.42 -1 526 GLU B OE2   1 
ATOM   9769  N  N     . TYR B 1 527 ? 108.043 155.377 164.495 1.00 33.11 ?  527 TYR B N     1 
ATOM   9770  C  CA    . TYR B 1 527 ? 109.034 154.344 164.780 1.00 22.71 ?  527 TYR B CA    1 
ATOM   9771  C  C     . TYR B 1 527 ? 109.104 154.026 166.268 1.00 25.58 ?  527 TYR B C     1 
ATOM   9772  O  O     . TYR B 1 527 ? 109.335 152.877 166.657 1.00 30.15 ?  527 TYR B O     1 
ATOM   9773  C  CB    . TYR B 1 527 ? 110.407 154.785 164.271 1.00 18.10 ?  527 TYR B CB    1 
ATOM   9774  C  CG    . TYR B 1 527 ? 111.504 153.776 164.522 1.00 26.66 ?  527 TYR B CG    1 
ATOM   9775  C  CD1   . TYR B 1 527 ? 111.773 152.777 163.597 1.00 26.45 ?  527 TYR B CD1   1 
ATOM   9776  C  CD2   . TYR B 1 527 ? 112.266 153.817 165.681 1.00 24.18 ?  527 TYR B CD2   1 
ATOM   9777  C  CE1   . TYR B 1 527 ? 112.769 151.852 163.817 1.00 23.64 ?  527 TYR B CE1   1 
ATOM   9778  C  CE2   . TYR B 1 527 ? 113.262 152.893 165.911 1.00 19.65 ?  527 TYR B CE2   1 
ATOM   9779  C  CZ    . TYR B 1 527 ? 113.510 151.914 164.975 1.00 20.98 ?  527 TYR B CZ    1 
ATOM   9780  O  OH    . TYR B 1 527 ? 114.505 150.991 165.198 1.00 30.81 ?  527 TYR B OH    1 
ATOM   9781  N  N     . PHE B 1 528 ? 108.908 155.033 167.113 1.00 29.04 ?  528 PHE B N     1 
ATOM   9782  C  CA    . PHE B 1 528 ? 109.027 154.874 168.554 1.00 26.61 ?  528 PHE B CA    1 
ATOM   9783  C  C     . PHE B 1 528 ? 107.749 154.366 169.207 1.00 33.94 ?  528 PHE B C     1 
ATOM   9784  O  O     . PHE B 1 528 ? 107.720 154.224 170.434 1.00 38.82 ?  528 PHE B O     1 
ATOM   9785  C  CB    . PHE B 1 528 ? 109.434 156.204 169.196 1.00 27.80 ?  528 PHE B CB    1 
ATOM   9786  C  CG    . PHE B 1 528 ? 110.688 156.795 168.622 1.00 29.99 ?  528 PHE B CG    1 
ATOM   9787  C  CD1   . PHE B 1 528 ? 111.925 156.469 169.147 1.00 26.60 ?  528 PHE B CD1   1 
ATOM   9788  C  CD2   . PHE B 1 528 ? 110.629 157.680 167.559 1.00 25.41 ?  528 PHE B CD2   1 
ATOM   9789  C  CE1   . PHE B 1 528 ? 113.081 157.012 168.622 1.00 28.91 ?  528 PHE B CE1   1 
ATOM   9790  C  CE2   . PHE B 1 528 ? 111.780 158.226 167.030 1.00 27.68 ?  528 PHE B CE2   1 
ATOM   9791  C  CZ    . PHE B 1 528 ? 113.007 157.890 167.562 1.00 27.60 ?  528 PHE B CZ    1 
ATOM   9792  N  N     . ASP B 1 529 ? 106.703 154.089 168.423 1.00 31.57 ?  529 ASP B N     1 
ATOM   9793  C  CA    . ASP B 1 529 ? 105.412 153.700 168.987 1.00 31.29 ?  529 ASP B CA    1 
ATOM   9794  C  C     . ASP B 1 529 ? 105.554 152.529 169.954 1.00 32.79 ?  529 ASP B C     1 
ATOM   9795  O  O     . ASP B 1 529 ? 105.279 152.657 171.153 1.00 37.04 ?  529 ASP B O     1 
ATOM   9796  C  CB    . ASP B 1 529 ? 104.441 153.352 167.859 1.00 31.85 ?  529 ASP B CB    1 
ATOM   9797  C  CG    . ASP B 1 529 ? 103.822 154.581 167.224 1.00 33.93 ?  529 ASP B CG    1 
ATOM   9798  O  OD1   . ASP B 1 529 ? 104.044 155.694 167.746 1.00 36.54 ?  529 ASP B OD1   1 
ATOM   9799  O  OD2   . ASP B 1 529 ? 103.119 154.433 166.203 1.00 36.46 -1 529 ASP B OD2   1 
ATOM   9800  N  N     . LYS B 1 530 ? 106.020 151.383 169.451 1.00 34.54 ?  530 LYS B N     1 
ATOM   9801  C  CA    . LYS B 1 530 ? 106.178 150.210 170.302 1.00 34.43 ?  530 LYS B CA    1 
ATOM   9802  C  C     . LYS B 1 530 ? 107.168 150.450 171.432 1.00 36.06 ?  530 LYS B C     1 
ATOM   9803  O  O     . LYS B 1 530 ? 107.150 149.716 172.424 1.00 36.80 ?  530 LYS B O     1 
ATOM   9804  C  CB    . LYS B 1 530 ? 106.626 149.008 169.469 1.00 33.22 ?  530 LYS B CB    1 
ATOM   9805  C  CG    . LYS B 1 530 ? 108.131 148.806 169.433 1.00 31.06 ?  530 LYS B CG    1 
ATOM   9806  C  CD    . LYS B 1 530 ? 108.540 147.873 168.314 1.00 32.94 ?  530 LYS B CD    1 
ATOM   9807  C  CE    . LYS B 1 530 ? 110.028 147.599 168.358 1.00 31.12 ?  530 LYS B CE    1 
ATOM   9808  N  NZ    . LYS B 1 530 ? 110.662 147.799 167.026 1.00 37.43 1  530 LYS B NZ    1 
ATOM   9809  N  N     . TYR B 1 531 ? 108.027 151.459 171.307 1.00 35.29 ?  531 TYR B N     1 
ATOM   9810  C  CA    . TYR B 1 531 ? 108.983 151.768 172.357 1.00 28.42 ?  531 TYR B CA    1 
ATOM   9811  C  C     . TYR B 1 531 ? 108.431 152.725 173.401 1.00 29.68 ?  531 TYR B C     1 
ATOM   9812  O  O     . TYR B 1 531 ? 108.991 152.807 174.501 1.00 33.16 ?  531 TYR B O     1 
ATOM   9813  C  CB    . TYR B 1 531 ? 110.258 152.354 171.748 1.00 27.04 ?  531 TYR B CB    1 
ATOM   9814  C  CG    . TYR B 1 531 ? 111.126 151.329 171.059 1.00 28.11 ?  531 TYR B CG    1 
ATOM   9815  C  CD1   . TYR B 1 531 ? 111.589 150.214 171.742 1.00 25.95 ?  531 TYR B CD1   1 
ATOM   9816  C  CD2   . TYR B 1 531 ? 111.480 151.475 169.725 1.00 27.49 ?  531 TYR B CD2   1 
ATOM   9817  C  CE1   . TYR B 1 531 ? 112.384 149.275 171.119 1.00 28.69 ?  531 TYR B CE1   1 
ATOM   9818  C  CE2   . TYR B 1 531 ? 112.275 150.540 169.093 1.00 23.66 ?  531 TYR B CE2   1 
ATOM   9819  C  CZ    . TYR B 1 531 ? 112.723 149.443 169.795 1.00 28.29 ?  531 TYR B CZ    1 
ATOM   9820  O  OH    . TYR B 1 531 ? 113.514 148.509 169.170 1.00 32.32 ?  531 TYR B OH    1 
ATOM   9821  N  N     . VAL B 1 532 ? 107.349 153.445 173.094 1.00 33.72 ?  532 VAL B N     1 
ATOM   9822  C  CA    . VAL B 1 532 ? 106.746 154.357 174.060 1.00 31.71 ?  532 VAL B CA    1 
ATOM   9823  C  C     . VAL B 1 532 ? 105.489 153.782 174.691 1.00 34.87 ?  532 VAL B C     1 
ATOM   9824  O  O     . VAL B 1 532 ? 104.810 154.486 175.451 1.00 40.13 ?  532 VAL B O     1 
ATOM   9825  C  CB    . VAL B 1 532 ? 106.444 155.729 173.421 1.00 34.38 ?  532 VAL B CB    1 
ATOM   9826  C  CG1   . VAL B 1 532 ? 107.721 156.364 172.895 1.00 32.64 ?  532 VAL B CG1   1 
ATOM   9827  C  CG2   . VAL B 1 532 ? 105.410 155.595 172.316 1.00 34.61 ?  532 VAL B CG2   1 
ATOM   9828  N  N     . SER B 1 533 ? 105.159 152.524 174.403 1.00 40.20 ?  533 SER B N     1 
ATOM   9829  C  CA    . SER B 1 533 ? 103.960 151.903 174.949 1.00 39.75 ?  533 SER B CA    1 
ATOM   9830  C  C     . SER B 1 533 ? 104.281 150.552 175.573 1.00 40.09 ?  533 SER B C     1 
ATOM   9831  O  O     . SER B 1 533 ? 103.571 150.094 176.475 1.00 44.55 ?  533 SER B O     1 
ATOM   9832  C  CB    . SER B 1 533 ? 102.901 151.746 173.857 1.00 41.09 ?  533 SER B CB    1 
ATOM   9833  O  OG    . SER B 1 533 ? 103.270 150.738 172.934 1.00 42.45 ?  533 SER B OG    1 
ATOM   9834  N  N     . THR B 1 534 ? 105.345 149.909 175.104 1.00 39.24 ?  534 THR B N     1 
ATOM   9835  C  CA    . THR B 1 534 ? 105.751 148.597 175.585 1.00 38.89 ?  534 THR B CA    1 
ATOM   9836  C  C     . THR B 1 534 ? 107.081 148.701 176.318 1.00 37.46 ?  534 THR B C     1 
ATOM   9837  O  O     . THR B 1 534 ? 108.004 149.380 175.856 1.00 43.15 ?  534 THR B O     1 
ATOM   9838  C  CB    . THR B 1 534 ? 105.869 147.596 174.433 1.00 39.21 ?  534 THR B CB    1 
ATOM   9839  O  OG1   . THR B 1 534 ? 104.687 147.653 173.624 1.00 40.92 ?  534 THR B OG1   1 
ATOM   9840  C  CG2   . THR B 1 534 ? 106.047 146.181 174.964 1.00 40.55 ?  534 THR B CG2   1 
ATOM   9841  N  N     . ASP B 1 535 ? 107.171 148.026 177.459 1.00 42.63 ?  535 ASP B N     1 
ATOM   9842  C  CA    . ASP B 1 535 ? 108.393 147.992 178.249 1.00 41.49 ?  535 ASP B CA    1 
ATOM   9843  C  C     . ASP B 1 535 ? 109.201 146.754 177.884 1.00 41.07 ?  535 ASP B C     1 
ATOM   9844  O  O     . ASP B 1 535 ? 108.672 145.637 177.883 1.00 42.97 ?  535 ASP B O     1 
ATOM   9845  C  CB    . ASP B 1 535 ? 108.065 147.997 179.743 1.00 38.42 ?  535 ASP B CB    1 
ATOM   9846  C  CG    . ASP B 1 535 ? 109.289 147.793 180.608 1.00 44.29 ?  535 ASP B CG    1 
ATOM   9847  O  OD1   . ASP B 1 535 ? 109.987 148.786 180.899 1.00 47.58 ?  535 ASP B OD1   1 
ATOM   9848  O  OD2   . ASP B 1 535 ? 109.547 146.637 181.000 1.00 46.27 -1 535 ASP B OD2   1 
ATOM   9849  N  N     . PHE B 1 536 ? 110.481 146.955 177.575 1.00 32.24 ?  536 PHE B N     1 
ATOM   9850  C  CA    . PHE B 1 536 ? 111.360 145.874 177.152 1.00 32.66 ?  536 PHE B CA    1 
ATOM   9851  C  C     . PHE B 1 536 ? 112.384 145.510 178.223 1.00 33.90 ?  536 PHE B C     1 
ATOM   9852  O  O     . PHE B 1 536 ? 113.428 144.932 177.908 1.00 35.05 ?  536 PHE B O     1 
ATOM   9853  C  CB    . PHE B 1 536 ? 112.058 146.241 175.842 1.00 29.99 ?  536 PHE B CB    1 
ATOM   9854  C  CG    . PHE B 1 536 ? 111.117 146.391 174.682 1.00 27.01 ?  536 PHE B CG    1 
ATOM   9855  C  CD1   . PHE B 1 536 ? 110.795 145.303 173.889 1.00 28.60 ?  536 PHE B CD1   1 
ATOM   9856  C  CD2   . PHE B 1 536 ? 110.546 147.618 174.389 1.00 30.83 ?  536 PHE B CD2   1 
ATOM   9857  C  CE1   . PHE B 1 536 ? 109.927 145.437 172.824 1.00 30.63 ?  536 PHE B CE1   1 
ATOM   9858  C  CE2   . PHE B 1 536 ? 109.677 147.757 173.326 1.00 35.58 ?  536 PHE B CE2   1 
ATOM   9859  C  CZ    . PHE B 1 536 ? 109.368 146.665 172.541 1.00 32.38 ?  536 PHE B CZ    1 
ATOM   9860  N  N     . SER B 1 537 ? 112.103 145.840 179.479 1.00 35.74 ?  537 SER B N     1 
ATOM   9861  C  CA    . SER B 1 537 ? 112.948 145.393 180.572 1.00 33.49 ?  537 SER B CA    1 
ATOM   9862  C  C     . SER B 1 537 ? 112.816 143.880 180.739 1.00 37.92 ?  537 SER B C     1 
ATOM   9863  O  O     . SER B 1 537 ? 111.787 143.298 180.385 1.00 39.77 ?  537 SER B O     1 
ATOM   9864  C  CB    . SER B 1 537 ? 112.564 146.100 181.868 1.00 35.62 ?  537 SER B CB    1 
ATOM   9865  O  OG    . SER B 1 537 ? 112.613 147.508 181.713 1.00 41.80 ?  537 SER B OG    1 
ATOM   9866  N  N     . PRO B 1 538 ? 113.849 143.217 181.258 1.00 35.53 ?  538 PRO B N     1 
ATOM   9867  C  CA    . PRO B 1 538 ? 113.796 141.755 181.378 1.00 34.54 ?  538 PRO B CA    1 
ATOM   9868  C  C     . PRO B 1 538 ? 112.645 141.298 182.263 1.00 38.77 ?  538 PRO B C     1 
ATOM   9869  O  O     . PRO B 1 538 ? 112.375 141.877 183.317 1.00 41.83 ?  538 PRO B O     1 
ATOM   9870  C  CB    . PRO B 1 538 ? 115.155 141.401 181.994 1.00 36.06 ?  538 PRO B CB    1 
ATOM   9871  C  CG    . PRO B 1 538 ? 116.030 142.565 181.689 1.00 37.65 ?  538 PRO B CG    1 
ATOM   9872  C  CD    . PRO B 1 538 ? 115.134 143.759 181.727 1.00 35.67 ?  538 PRO B CD    1 
ATOM   9873  N  N     . LYS B 1 539 ? 111.969 140.240 181.819 1.00 41.02 ?  539 LYS B N     1 
ATOM   9874  C  CA    . LYS B 1 539 ? 110.877 139.641 182.573 1.00 41.05 ?  539 LYS B CA    1 
ATOM   9875  C  C     . LYS B 1 539 ? 111.344 138.553 183.530 1.00 44.29 ?  539 LYS B C     1 
ATOM   9876  O  O     . LYS B 1 539 ? 110.547 138.093 184.355 1.00 47.25 ?  539 LYS B O     1 
ATOM   9877  C  CB    . LYS B 1 539 ? 109.831 139.059 181.617 1.00 42.03 ?  539 LYS B CB    1 
ATOM   9878  C  CG    . LYS B 1 539 ? 109.614 139.886 180.363 1.00 42.44 ?  539 LYS B CG    1 
ATOM   9879  C  CD    . LYS B 1 539 ? 108.400 140.789 180.503 1.00 42.09 ?  539 LYS B CD    1 
ATOM   9880  C  CE    . LYS B 1 539 ? 108.168 141.600 179.238 1.00 44.54 ?  539 LYS B CE    1 
ATOM   9881  N  NZ    . LYS B 1 539 ? 109.425 142.231 178.747 1.00 45.96 1  539 LYS B NZ    1 
ATOM   9882  N  N     . TYR B 1 540 ? 112.602 138.136 183.441 1.00 42.27 ?  540 TYR B N     1 
ATOM   9883  C  CA    . TYR B 1 540 ? 113.159 137.104 184.301 1.00 39.72 ?  540 TYR B CA    1 
ATOM   9884  C  C     . TYR B 1 540 ? 114.195 137.717 185.232 1.00 46.19 ?  540 TYR B C     1 
ATOM   9885  O  O     . TYR B 1 540 ? 114.932 138.628 184.842 1.00 47.07 ?  540 TYR B O     1 
ATOM   9886  C  CB    . TYR B 1 540 ? 113.787 135.980 183.473 1.00 41.89 ?  540 TYR B CB    1 
ATOM   9887  C  CG    . TYR B 1 540 ? 112.785 135.195 182.659 1.00 45.05 ?  540 TYR B CG    1 
ATOM   9888  C  CD1   . TYR B 1 540 ? 112.430 135.602 181.379 1.00 42.64 ?  540 TYR B CD1   1 
ATOM   9889  C  CD2   . TYR B 1 540 ? 112.187 134.053 183.172 1.00 45.24 ?  540 TYR B CD2   1 
ATOM   9890  C  CE1   . TYR B 1 540 ? 111.511 134.889 180.632 1.00 42.42 ?  540 TYR B CE1   1 
ATOM   9891  C  CE2   . TYR B 1 540 ? 111.268 133.334 182.433 1.00 42.26 ?  540 TYR B CE2   1 
ATOM   9892  C  CZ    . TYR B 1 540 ? 110.934 133.756 181.165 1.00 43.92 ?  540 TYR B CZ    1 
ATOM   9893  O  OH    . TYR B 1 540 ? 110.018 133.042 180.428 1.00 46.28 ?  540 TYR B OH    1 
ATOM   9894  N  N     . GLU B 1 541 ? 114.240 137.215 186.468 1.00 49.66 ?  541 GLU B N     1 
ATOM   9895  C  CA    . GLU B 1 541 ? 115.160 137.764 187.458 1.00 45.98 ?  541 GLU B CA    1 
ATOM   9896  C  C     . GLU B 1 541 ? 116.611 137.533 187.057 1.00 46.37 ?  541 GLU B C     1 
ATOM   9897  O  O     . GLU B 1 541 ? 117.472 138.386 187.302 1.00 45.04 ?  541 GLU B O     1 
ATOM   9898  C  CB    . GLU B 1 541 ? 114.880 137.155 188.832 1.00 46.69 ?  541 GLU B CB    1 
ATOM   9899  C  CG    . GLU B 1 541 ? 115.555 137.889 189.978 1.00 48.66 ?  541 GLU B CG    1 
ATOM   9900  C  CD    . GLU B 1 541 ? 115.367 139.391 189.899 1.00 50.84 ?  541 GLU B CD    1 
ATOM   9901  O  OE1   . GLU B 1 541 ? 114.204 139.844 189.854 1.00 50.80 ?  541 GLU B OE1   1 
ATOM   9902  O  OE2   . GLU B 1 541 ? 116.381 140.119 189.877 1.00 52.89 -1 541 GLU B OE2   1 
ATOM   9903  N  N     . LYS B 1 542 ? 116.906 136.380 186.452 1.00 42.48 ?  542 LYS B N     1 
ATOM   9904  C  CA    . LYS B 1 542 ? 118.276 136.091 186.036 1.00 39.80 ?  542 LYS B CA    1 
ATOM   9905  C  C     . LYS B 1 542 ? 118.759 137.089 184.991 1.00 42.82 ?  542 LYS B C     1 
ATOM   9906  O  O     . LYS B 1 542 ? 119.892 137.579 185.063 1.00 44.21 ?  542 LYS B O     1 
ATOM   9907  C  CB    . LYS B 1 542 ? 118.367 134.662 185.501 1.00 38.45 ?  542 LYS B CB    1 
ATOM   9908  C  CG    . LYS B 1 542 ? 119.770 134.229 185.113 1.00 43.63 ?  542 LYS B CG    1 
ATOM   9909  C  CD    . LYS B 1 542 ? 119.796 132.770 184.692 1.00 42.93 ?  542 LYS B CD    1 
ATOM   9910  C  CE    . LYS B 1 542 ? 121.218 132.292 184.453 1.00 43.45 ?  542 LYS B CE    1 
ATOM   9911  N  NZ    . LYS B 1 542 ? 121.284 130.819 184.248 1.00 41.95 1  542 LYS B NZ    1 
ATOM   9912  N  N     . ILE B 1 543 ? 117.908 137.414 184.017 1.00 39.40 ?  543 ILE B N     1 
ATOM   9913  C  CA    . ILE B 1 543 ? 118.289 138.379 182.990 1.00 37.20 ?  543 ILE B CA    1 
ATOM   9914  C  C     . ILE B 1 543 ? 118.447 139.770 183.592 1.00 36.34 ?  543 ILE B C     1 
ATOM   9915  O  O     . ILE B 1 543 ? 119.364 140.518 183.231 1.00 39.33 ?  543 ILE B O     1 
ATOM   9916  C  CB    . ILE B 1 543 ? 117.262 138.365 181.845 1.00 36.93 ?  543 ILE B CB    1 
ATOM   9917  C  CG1   . ILE B 1 543 ? 117.030 136.934 181.353 1.00 36.34 ?  543 ILE B CG1   1 
ATOM   9918  C  CG2   . ILE B 1 543 ? 117.729 139.248 180.710 1.00 35.21 ?  543 ILE B CG2   1 
ATOM   9919  C  CD1   . ILE B 1 543 ? 118.298 136.208 180.955 1.00 34.56 ?  543 ILE B CD1   1 
ATOM   9920  N  N     . ALA B 1 544 ? 117.555 140.143 184.514 1.00 37.78 ?  544 ALA B N     1 
ATOM   9921  C  CA    . ALA B 1 544 ? 117.675 141.437 185.177 1.00 40.15 ?  544 ALA B CA    1 
ATOM   9922  C  C     . ALA B 1 544 ? 118.982 141.536 185.953 1.00 39.96 ?  544 ALA B C     1 
ATOM   9923  O  O     . ALA B 1 544 ? 119.640 142.584 185.946 1.00 42.67 ?  544 ALA B O     1 
ATOM   9924  C  CB    . ALA B 1 544 ? 116.480 141.667 186.102 1.00 41.98 ?  544 ALA B CB    1 
ATOM   9925  N  N     . ASN B 1 545 ? 119.373 140.456 186.633 1.00 43.77 ?  545 ASN B N     1 
ATOM   9926  C  CA    . ASN B 1 545 ? 120.667 140.430 187.305 1.00 47.64 ?  545 ASN B CA    1 
ATOM   9927  C  C     . ASN B 1 545 ? 121.808 140.535 186.302 1.00 45.05 ?  545 ASN B C     1 
ATOM   9928  O  O     . ASN B 1 545 ? 122.821 141.191 186.568 1.00 46.84 ?  545 ASN B O     1 
ATOM   9929  C  CB    . ASN B 1 545 ? 120.800 139.155 188.140 1.00 44.49 ?  545 ASN B CB    1 
ATOM   9930  C  CG    . ASN B 1 545 ? 119.823 139.113 189.295 1.00 47.52 ?  545 ASN B CG    1 
ATOM   9931  O  OD1   . ASN B 1 545 ? 119.340 140.150 189.752 1.00 49.39 ?  545 ASN B OD1   1 
ATOM   9932  N  ND2   . ASN B 1 545 ? 119.525 137.912 189.775 1.00 44.45 ?  545 ASN B ND2   1 
ATOM   9933  N  N     . LEU B 1 546 ? 121.665 139.880 185.148 1.00 38.60 ?  546 LEU B N     1 
ATOM   9934  C  CA    . LEU B 1 546 ? 122.656 140.018 184.086 1.00 39.55 ?  546 LEU B CA    1 
ATOM   9935  C  C     . LEU B 1 546 ? 122.800 141.466 183.641 1.00 39.47 ?  546 LEU B C     1 
ATOM   9936  O  O     . LEU B 1 546 ? 123.902 141.904 183.294 1.00 39.00 ?  546 LEU B O     1 
ATOM   9937  C  CB    . LEU B 1 546 ? 122.277 139.135 182.898 1.00 36.75 ?  546 LEU B CB    1 
ATOM   9938  C  CG    . LEU B 1 546 ? 122.692 137.666 182.967 1.00 39.09 ?  546 LEU B CG    1 
ATOM   9939  C  CD1   . LEU B 1 546 ? 122.654 137.048 181.583 1.00 37.33 ?  546 LEU B CD1   1 
ATOM   9940  C  CD2   . LEU B 1 546 ? 124.075 137.524 183.582 1.00 38.77 ?  546 LEU B CD2   1 
ATOM   9941  N  N     . PHE B 1 547 ? 121.705 142.223 183.649 1.00 40.07 ?  547 PHE B N     1 
ATOM   9942  C  CA    . PHE B 1 547 ? 121.718 143.622 183.246 1.00 37.64 ?  547 PHE B CA    1 
ATOM   9943  C  C     . PHE B 1 547 ? 121.952 144.579 184.408 1.00 39.81 ?  547 PHE B C     1 
ATOM   9944  O  O     . PHE B 1 547 ? 121.756 145.787 184.245 1.00 43.53 ?  547 PHE B O     1 
ATOM   9945  C  CB    . PHE B 1 547 ? 120.407 143.980 182.544 1.00 35.49 ?  547 PHE B CB    1 
ATOM   9946  C  CG    . PHE B 1 547 ? 120.343 143.536 181.115 1.00 36.65 ?  547 PHE B CG    1 
ATOM   9947  C  CD1   . PHE B 1 547 ? 120.986 144.256 180.124 1.00 35.91 ?  547 PHE B CD1   1 
ATOM   9948  C  CD2   . PHE B 1 547 ? 119.640 142.398 180.759 1.00 35.72 ?  547 PHE B CD2   1 
ATOM   9949  C  CE1   . PHE B 1 547 ? 120.929 143.851 178.807 1.00 34.64 ?  547 PHE B CE1   1 
ATOM   9950  C  CE2   . PHE B 1 547 ? 119.581 141.990 179.444 1.00 36.03 ?  547 PHE B CE2   1 
ATOM   9951  C  CZ    . PHE B 1 547 ? 120.227 142.716 178.468 1.00 35.01 ?  547 PHE B CZ    1 
ATOM   9952  N  N     . GLU B 1 548 ? 122.361 144.075 185.570 1.00 47.04 ?  548 GLU B N     1 
ATOM   9953  C  CA    . GLU B 1 548 ? 122.615 144.944 186.710 1.00 47.44 ?  548 GLU B CA    1 
ATOM   9954  C  C     . GLU B 1 548 ? 123.826 145.835 186.456 1.00 47.26 ?  548 GLU B C     1 
ATOM   9955  O  O     . GLU B 1 548 ? 124.762 145.463 185.743 1.00 50.56 ?  548 GLU B O     1 
ATOM   9956  C  CB    . GLU B 1 548 ? 122.830 144.123 187.981 1.00 46.82 ?  548 GLU B CB    1 
ATOM   9957  C  CG    . GLU B 1 548 ? 121.545 143.652 188.644 1.00 48.12 ?  548 GLU B CG    1 
ATOM   9958  C  CD    . GLU B 1 548 ? 120.639 144.798 189.062 1.00 50.79 ?  548 GLU B CD    1 
ATOM   9959  O  OE1   . GLU B 1 548 ? 121.148 145.911 189.310 1.00 48.80 ?  548 GLU B OE1   1 
ATOM   9960  O  OE2   . GLU B 1 548 ? 119.412 144.582 189.143 1.00 50.91 -1 548 GLU B OE2   1 
ATOM   9961  N  N     . GLY B 1 549 ? 123.796 147.024 187.051 1.00 45.31 ?  549 GLY B N     1 
ATOM   9962  C  CA    . GLY B 1 549 ? 124.821 148.017 186.822 1.00 44.97 ?  549 GLY B CA    1 
ATOM   9963  C  C     . GLY B 1 549 ? 124.656 148.810 185.548 1.00 46.10 ?  549 GLY B C     1 
ATOM   9964  O  O     . GLY B 1 549 ? 125.532 149.625 185.227 1.00 47.53 ?  549 GLY B O     1 
ATOM   9965  N  N     . MET B 1 550 ? 123.568 148.600 184.812 1.00 45.44 ?  550 MET B N     1 
ATOM   9966  C  CA    . MET B 1 550 ? 123.315 149.281 183.552 1.00 44.20 ?  550 MET B CA    1 
ATOM   9967  C  C     . MET B 1 550 ? 121.882 149.788 183.548 1.00 44.33 ?  550 MET B C     1 
ATOM   9968  O  O     . MET B 1 550 ? 120.964 149.061 183.941 1.00 46.15 ?  550 MET B O     1 
ATOM   9969  C  CB    . MET B 1 550 ? 123.555 148.342 182.367 1.00 43.15 ?  550 MET B CB    1 
ATOM   9970  C  CG    . MET B 1 550 ? 124.796 148.669 181.565 1.00 48.10 ?  550 MET B CG    1 
ATOM   9971  S  SD    . MET B 1 550 ? 124.852 147.780 180.003 1.00 54.89 ?  550 MET B SD    1 
ATOM   9972  C  CE    . MET B 1 550 ? 124.842 146.082 180.573 1.00 44.40 ?  550 MET B CE    1 
ATOM   9973  N  N     . HIS B 1 551 ? 121.691 151.027 183.105 1.00 40.63 ?  551 HIS B N     1 
ATOM   9974  C  CA    . HIS B 1 551 ? 120.368 151.644 183.098 1.00 40.60 ?  551 HIS B CA    1 
ATOM   9975  C  C     . HIS B 1 551 ? 119.593 151.169 181.875 1.00 40.33 ?  551 HIS B C     1 
ATOM   9976  O  O     . HIS B 1 551 ? 119.834 151.636 180.758 1.00 41.37 ?  551 HIS B O     1 
ATOM   9977  C  CB    . HIS B 1 551 ? 120.483 153.165 183.106 1.00 39.84 ?  551 HIS B CB    1 
ATOM   9978  C  CG    . HIS B 1 551 ? 119.195 153.863 182.802 1.00 41.55 ?  551 HIS B CG    1 
ATOM   9979  N  ND1   . HIS B 1 551 ? 118.125 153.862 183.669 1.00 44.88 ?  551 HIS B ND1   1 
ATOM   9980  C  CD2   . HIS B 1 551 ? 118.802 154.575 181.720 1.00 41.27 ?  551 HIS B CD2   1 
ATOM   9981  C  CE1   . HIS B 1 551 ? 117.129 154.546 183.137 1.00 43.33 ?  551 HIS B CE1   1 
ATOM   9982  N  NE2   . HIS B 1 551 ? 117.513 154.991 181.955 1.00 40.71 ?  551 HIS B NE2   1 
ATOM   9983  N  N     . ILE B 1 552 ? 118.652 150.255 182.087 1.00 35.98 ?  552 ILE B N     1 
ATOM   9984  C  CA    . ILE B 1 552 ? 117.801 149.750 181.014 1.00 32.38 ?  552 ILE B CA    1 
ATOM   9985  C  C     . ILE B 1 552 ? 116.783 150.826 180.658 1.00 33.83 ?  552 ILE B C     1 
ATOM   9986  O  O     . ILE B 1 552 ? 116.022 151.268 181.531 1.00 38.54 ?  552 ILE B O     1 
ATOM   9987  C  CB    . ILE B 1 552 ? 117.109 148.440 181.423 1.00 35.25 ?  552 ILE B CB    1 
ATOM   9988  C  CG1   . ILE B 1 552 ? 118.150 147.395 181.825 1.00 34.38 ?  552 ILE B CG1   1 
ATOM   9989  C  CG2   . ILE B 1 552 ? 116.238 147.923 180.294 1.00 35.00 ?  552 ILE B CG2   1 
ATOM   9990  C  CD1   . ILE B 1 552 ? 117.584 146.262 182.641 1.00 33.66 ?  552 ILE B CD1   1 
ATOM   9991  N  N     . PRO B 1 553 ? 116.739 151.284 179.407 1.00 37.53 ?  553 PRO B N     1 
ATOM   9992  C  CA    . PRO B 1 553 ? 115.788 152.341 179.043 1.00 34.70 ?  553 PRO B CA    1 
ATOM   9993  C  C     . PRO B 1 553 ? 114.347 151.886 179.228 1.00 35.12 ?  553 PRO B C     1 
ATOM   9994  O  O     . PRO B 1 553 ? 113.980 150.761 178.885 1.00 37.86 ?  553 PRO B O     1 
ATOM   9995  C  CB    . PRO B 1 553 ? 116.106 152.614 177.569 1.00 32.01 ?  553 PRO B CB    1 
ATOM   9996  C  CG    . PRO B 1 553 ? 117.494 152.099 177.372 1.00 30.36 ?  553 PRO B CG    1 
ATOM   9997  C  CD    . PRO B 1 553 ? 117.620 150.923 178.286 1.00 32.54 ?  553 PRO B CD    1 
ATOM   9998  N  N     . THR B 1 554 ? 113.533 152.780 179.773 1.00 39.81 ?  554 THR B N     1 
ATOM   9999  C  CA    . THR B 1 554 ? 112.118 152.535 179.977 1.00 38.48 ?  554 THR B CA    1 
ATOM   10000 C  C     . THR B 1 554 ? 111.315 153.293 178.923 1.00 36.43 ?  554 THR B C     1 
ATOM   10001 O  O     . THR B 1 554 ? 111.871 153.876 177.987 1.00 36.73 ?  554 THR B O     1 
ATOM   10002 C  CB    . THR B 1 554 ? 111.713 152.932 181.398 1.00 38.13 ?  554 THR B CB    1 
ATOM   10003 O  OG1   . THR B 1 554 ? 111.931 154.335 181.584 1.00 37.11 ?  554 THR B OG1   1 
ATOM   10004 C  CG2   . THR B 1 554 ? 112.535 152.159 182.420 1.00 36.24 ?  554 THR B CG2   1 
ATOM   10005 N  N     . THR B 1 555 ? 109.989 153.285 179.067 1.00 39.09 ?  555 THR B N     1 
ATOM   10006 C  CA    . THR B 1 555 ? 109.151 154.031 178.135 1.00 36.65 ?  555 THR B CA    1 
ATOM   10007 C  C     . THR B 1 555 ? 109.382 155.532 178.249 1.00 39.53 ?  555 THR B C     1 
ATOM   10008 O  O     . THR B 1 555 ? 109.232 156.255 177.259 1.00 40.35 ?  555 THR B O     1 
ATOM   10009 C  CB    . THR B 1 555 ? 107.675 153.705 178.368 1.00 38.95 ?  555 THR B CB    1 
ATOM   10010 O  OG1   . THR B 1 555 ? 107.337 153.961 179.736 1.00 44.10 ?  555 THR B OG1   1 
ATOM   10011 C  CG2   . THR B 1 555 ? 107.396 152.245 178.043 1.00 39.39 ?  555 THR B CG2   1 
ATOM   10012 N  N     . GLU B 1 556 ? 109.749 156.018 179.437 1.00 37.71 ?  556 GLU B N     1 
ATOM   10013 C  CA    . GLU B 1 556 ? 110.033 157.441 179.598 1.00 37.73 ?  556 GLU B CA    1 
ATOM   10014 C  C     . GLU B 1 556 ? 111.323 157.833 178.884 1.00 40.49 ?  556 GLU B C     1 
ATOM   10015 O  O     . GLU B 1 556 ? 111.384 158.882 178.230 1.00 41.86 ?  556 GLU B O     1 
ATOM   10016 C  CB    . GLU B 1 556 ? 110.112 157.796 181.081 1.00 39.97 ?  556 GLU B CB    1 
ATOM   10017 C  CG    . GLU B 1 556 ? 108.769 157.792 181.792 1.00 41.23 ?  556 GLU B CG    1 
ATOM   10018 C  CD    . GLU B 1 556 ? 107.663 158.403 180.954 1.00 44.19 ?  556 GLU B CD    1 
ATOM   10019 O  OE1   . GLU B 1 556 ? 107.697 159.631 180.726 1.00 42.40 ?  556 GLU B OE1   1 
ATOM   10020 O  OE2   . GLU B 1 556 ? 106.759 157.656 180.523 1.00 44.24 -1 556 GLU B OE2   1 
ATOM   10021 N  N     . ASP B 1 557 ? 112.365 157.008 179.004 1.00 40.06 ?  557 ASP B N     1 
ATOM   10022 C  CA    . ASP B 1 557 ? 113.600 157.269 178.272 1.00 34.63 ?  557 ASP B CA    1 
ATOM   10023 C  C     . ASP B 1 557 ? 113.363 157.222 176.770 1.00 36.07 ?  557 ASP B C     1 
ATOM   10024 O  O     . ASP B 1 557 ? 113.927 158.025 176.018 1.00 38.98 ?  557 ASP B O     1 
ATOM   10025 C  CB    . ASP B 1 557 ? 114.679 156.263 178.677 1.00 32.74 ?  557 ASP B CB    1 
ATOM   10026 C  CG    . ASP B 1 557 ? 114.682 155.980 180.164 1.00 41.14 ?  557 ASP B CG    1 
ATOM   10027 O  OD1   . ASP B 1 557 ? 113.638 155.538 180.688 1.00 44.16 ?  557 ASP B OD1   1 
ATOM   10028 O  OD2   . ASP B 1 557 ? 115.728 156.197 180.810 1.00 42.26 -1 557 ASP B OD2   1 
ATOM   10029 N  N     . TRP B 1 558 ? 112.524 156.290 176.315 1.00 32.21 ?  558 TRP B N     1 
ATOM   10030 C  CA    . TRP B 1 558 ? 112.204 156.216 174.895 1.00 26.34 ?  558 TRP B CA    1 
ATOM   10031 C  C     . TRP B 1 558 ? 111.394 157.424 174.440 1.00 31.81 ?  558 TRP B C     1 
ATOM   10032 O  O     . TRP B 1 558 ? 111.571 157.902 173.317 1.00 38.07 ?  558 TRP B O     1 
ATOM   10033 C  CB    . TRP B 1 558 ? 111.459 154.918 174.597 1.00 27.19 ?  558 TRP B CB    1 
ATOM   10034 C  CG    . TRP B 1 558 ? 112.366 153.790 174.227 1.00 27.01 ?  558 TRP B CG    1 
ATOM   10035 C  CD1   . TRP B 1 558 ? 112.671 152.701 174.987 1.00 26.33 ?  558 TRP B CD1   1 
ATOM   10036 C  CD2   . TRP B 1 558 ? 113.081 153.635 172.996 1.00 27.89 ?  558 TRP B CD2   1 
ATOM   10037 N  NE1   . TRP B 1 558 ? 113.534 151.877 174.306 1.00 30.65 ?  558 TRP B NE1   1 
ATOM   10038 C  CE2   . TRP B 1 558 ? 113.800 152.427 173.081 1.00 28.06 ?  558 TRP B CE2   1 
ATOM   10039 C  CE3   . TRP B 1 558 ? 113.180 154.398 171.829 1.00 31.92 ?  558 TRP B CE3   1 
ATOM   10040 C  CZ2   . TRP B 1 558 ? 114.607 151.967 172.044 1.00 25.09 ?  558 TRP B CZ2   1 
ATOM   10041 C  CZ3   . TRP B 1 558 ? 113.983 153.940 170.803 1.00 26.96 ?  558 TRP B CZ3   1 
ATOM   10042 C  CH2   . TRP B 1 558 ? 114.686 152.736 170.917 1.00 21.83 ?  558 TRP B CH2   1 
ATOM   10043 N  N     . LYS B 1 559 ? 110.500 157.932 175.292 1.00 36.75 ?  559 LYS B N     1 
ATOM   10044 C  CA    . LYS B 1 559 ? 109.772 159.153 174.956 1.00 31.12 ?  559 LYS B CA    1 
ATOM   10045 C  C     . LYS B 1 559 ? 110.714 160.346 174.856 1.00 34.26 ?  559 LYS B C     1 
ATOM   10046 O  O     . LYS B 1 559 ? 110.585 161.178 173.947 1.00 34.78 ?  559 LYS B O     1 
ATOM   10047 C  CB    . LYS B 1 559 ? 108.683 159.417 175.996 1.00 35.39 ?  559 LYS B CB    1 
ATOM   10048 C  CG    . LYS B 1 559 ? 107.428 158.582 175.812 1.00 37.52 ?  559 LYS B CG    1 
ATOM   10049 C  CD    . LYS B 1 559 ? 106.552 158.627 177.052 1.00 36.46 ?  559 LYS B CD    1 
ATOM   10050 C  CE    . LYS B 1 559 ? 105.601 157.443 177.101 1.00 37.55 ?  559 LYS B CE    1 
ATOM   10051 N  NZ    . LYS B 1 559 ? 105.142 157.159 178.489 1.00 36.41 1  559 LYS B NZ    1 
ATOM   10052 N  N     . LYS B 1 560 ? 111.668 160.446 175.783 1.00 31.68 ?  560 LYS B N     1 
ATOM   10053 C  CA    . LYS B 1 560 ? 112.659 161.514 175.715 1.00 30.42 ?  560 LYS B CA    1 
ATOM   10054 C  C     . LYS B 1 560 ? 113.504 161.397 174.454 1.00 34.62 ?  560 LYS B C     1 
ATOM   10055 O  O     . LYS B 1 560 ? 113.812 162.404 173.807 1.00 36.67 ?  560 LYS B O     1 
ATOM   10056 C  CB    . LYS B 1 560 ? 113.543 161.493 176.961 1.00 30.64 ?  560 LYS B CB    1 
ATOM   10057 C  CG    . LYS B 1 560 ? 112.866 162.027 178.211 1.00 35.01 ?  560 LYS B CG    1 
ATOM   10058 C  CD    . LYS B 1 560 ? 113.829 162.055 179.386 1.00 37.36 ?  560 LYS B CD    1 
ATOM   10059 C  CE    . LYS B 1 560 ? 113.086 162.102 180.710 1.00 35.42 ?  560 LYS B CE    1 
ATOM   10060 N  NZ    . LYS B 1 560 ? 112.453 160.794 181.040 1.00 37.29 1  560 LYS B NZ    1 
ATOM   10061 N  N     . LEU B 1 561 ? 113.888 160.172 174.087 1.00 31.74 ?  561 LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 561 ? 114.651 159.967 172.862 1.00 27.68 ?  561 LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 561 ? 113.827 160.316 171.629 1.00 31.16 ?  561 LEU B C     1 
ATOM   10064 O  O     . LEU B 1 561 ? 114.356 160.865 170.658 1.00 33.36 ?  561 LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 561 ? 115.144 158.522 172.785 1.00 29.77 ?  561 LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 561 ? 115.951 158.167 171.536 1.00 28.99 ?  561 LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 561 ? 117.117 159.126 171.371 1.00 25.20 ?  561 LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 561 ? 116.438 156.734 171.598 1.00 26.50 ?  561 LEU B CD2   1 
ATOM   10069 N  N     . LYS B 1 562 ? 112.532 159.995 171.645 1.00 31.63 ?  562 LYS B N     1 
ATOM   10070 C  CA    . LYS B 1 562 ? 111.657 160.360 170.537 1.00 29.39 ?  562 LYS B CA    1 
ATOM   10071 C  C     . LYS B 1 562 ? 111.562 161.872 170.389 1.00 31.00 ?  562 LYS B C     1 
ATOM   10072 O  O     . LYS B 1 562 ? 111.615 162.401 169.274 1.00 35.93 ?  562 LYS B O     1 
ATOM   10073 C  CB    . LYS B 1 562 ? 110.274 159.745 170.748 1.00 27.01 ?  562 LYS B CB    1 
ATOM   10074 C  CG    . LYS B 1 562 ? 109.202 160.252 169.801 1.00 29.64 ?  562 LYS B CG    1 
ATOM   10075 C  CD    . LYS B 1 562 ? 107.844 159.675 170.165 1.00 30.78 ?  562 LYS B CD    1 
ATOM   10076 C  CE    . LYS B 1 562 ? 106.750 160.204 169.253 1.00 32.17 ?  562 LYS B CE    1 
ATOM   10077 N  NZ    . LYS B 1 562 ? 105.522 159.364 169.320 1.00 32.25 1  562 LYS B NZ    1 
ATOM   10078 N  N     . ALA B 1 563 ? 111.426 162.586 171.509 1.00 31.70 ?  563 ALA B N     1 
ATOM   10079 C  CA    . ALA B 1 563 ? 111.409 164.046 171.456 1.00 32.22 ?  563 ALA B CA    1 
ATOM   10080 C  C     . ALA B 1 563 ? 112.740 164.595 170.955 1.00 32.55 ?  563 ALA B C     1 
ATOM   10081 O  O     . ALA B 1 563 ? 112.773 165.548 170.166 1.00 36.45 ?  563 ALA B O     1 
ATOM   10082 C  CB    . ALA B 1 563 ? 111.075 164.617 172.834 1.00 32.53 ?  563 ALA B CB    1 
ATOM   10083 N  N     . PHE B 1 564 ? 113.849 164.001 171.401 1.00 32.33 ?  564 PHE B N     1 
ATOM   10084 C  CA    . PHE B 1 564 ? 115.168 164.438 170.957 1.00 27.46 ?  564 PHE B CA    1 
ATOM   10085 C  C     . PHE B 1 564 ? 115.340 164.234 169.456 1.00 30.75 ?  564 PHE B C     1 
ATOM   10086 O  O     . PHE B 1 564 ? 115.899 165.092 168.765 1.00 33.53 ?  564 PHE B O     1 
ATOM   10087 C  CB    . PHE B 1 564 ? 116.244 163.680 171.735 1.00 28.79 ?  564 PHE B CB    1 
ATOM   10088 C  CG    . PHE B 1 564 ? 117.622 164.254 171.589 1.00 32.18 ?  564 PHE B CG    1 
ATOM   10089 C  CD1   . PHE B 1 564 ? 118.027 165.323 172.368 1.00 31.86 ?  564 PHE B CD1   1 
ATOM   10090 C  CD2   . PHE B 1 564 ? 118.518 163.715 170.682 1.00 33.00 ?  564 PHE B CD2   1 
ATOM   10091 C  CE1   . PHE B 1 564 ? 119.298 165.848 172.240 1.00 34.64 ?  564 PHE B CE1   1 
ATOM   10092 C  CE2   . PHE B 1 564 ? 119.789 164.236 170.549 1.00 32.71 ?  564 PHE B CE2   1 
ATOM   10093 C  CZ    . PHE B 1 564 ? 120.180 165.304 171.328 1.00 34.29 ?  564 PHE B CZ    1 
ATOM   10094 N  N     . VAL B 1 565 ? 114.867 163.100 168.937 1.00 31.07 ?  565 VAL B N     1 
ATOM   10095 C  CA    . VAL B 1 565 ? 114.938 162.839 167.503 1.00 27.20 ?  565 VAL B CA    1 
ATOM   10096 C  C     . VAL B 1 565 ? 114.053 163.814 166.737 1.00 32.84 ?  565 VAL B C     1 
ATOM   10097 O  O     . VAL B 1 565 ? 114.446 164.335 165.688 1.00 34.16 ?  565 VAL B O     1 
ATOM   10098 C  CB    . VAL B 1 565 ? 114.561 161.376 167.209 1.00 27.17 ?  565 VAL B CB    1 
ATOM   10099 C  CG1   . VAL B 1 565 ? 114.373 161.163 165.717 1.00 27.37 ?  565 VAL B CG1   1 
ATOM   10100 C  CG2   . VAL B 1 565 ? 115.628 160.441 167.743 1.00 29.85 ?  565 VAL B CG2   1 
ATOM   10101 N  N     . ALA B 1 566 ? 112.849 164.078 167.246 1.00 34.96 ?  566 ALA B N     1 
ATOM   10102 C  CA    . ALA B 1 566 ? 111.968 165.036 166.588 1.00 34.18 ?  566 ALA B CA    1 
ATOM   10103 C  C     . ALA B 1 566 ? 112.603 166.419 166.535 1.00 36.19 ?  566 ALA B C     1 
ATOM   10104 O  O     . ALA B 1 566 ? 112.443 167.148 165.549 1.00 38.31 ?  566 ALA B O     1 
ATOM   10105 C  CB    . ALA B 1 566 ? 110.619 165.089 167.304 1.00 33.11 ?  566 ALA B CB    1 
ATOM   10106 N  N     . GLU B 1 567 ? 113.327 166.799 167.589 1.00 36.81 ?  567 GLU B N     1 
ATOM   10107 C  CA    . GLU B 1 567 ? 113.958 168.114 167.614 1.00 35.87 ?  567 GLU B CA    1 
ATOM   10108 C  C     . GLU B 1 567 ? 115.181 168.171 166.701 1.00 38.64 ?  567 GLU B C     1 
ATOM   10109 O  O     . GLU B 1 567 ? 115.372 169.154 165.974 1.00 44.38 ?  567 GLU B O     1 
ATOM   10110 C  CB    . GLU B 1 567 ? 114.337 168.483 169.048 1.00 34.73 ?  567 GLU B CB    1 
ATOM   10111 C  CG    . GLU B 1 567 ? 115.562 169.372 169.164 1.00 37.84 ?  567 GLU B CG    1 
ATOM   10112 C  CD    . GLU B 1 567 ? 115.473 170.336 170.329 1.00 42.89 ?  567 GLU B CD    1 
ATOM   10113 O  OE1   . GLU B 1 567 ? 116.410 171.141 170.508 1.00 42.59 ?  567 GLU B OE1   1 
ATOM   10114 O  OE2   . GLU B 1 567 ? 114.465 170.289 171.065 1.00 42.45 -1 567 GLU B OE2   1 
ATOM   10115 N  N     . HIS B 1 568 ? 116.015 167.128 166.712 1.00 34.94 ?  568 HIS B N     1 
ATOM   10116 C  CA    . HIS B 1 568 ? 117.306 167.173 166.037 1.00 31.70 ?  568 HIS B CA    1 
ATOM   10117 C  C     . HIS B 1 568 ? 117.411 166.284 164.808 1.00 32.49 ?  568 HIS B C     1 
ATOM   10118 O  O     . HIS B 1 568 ? 118.283 166.528 163.968 1.00 37.18 ?  568 HIS B O     1 
ATOM   10119 C  CB    . HIS B 1 568 ? 118.427 166.787 167.012 1.00 31.46 ?  568 HIS B CB    1 
ATOM   10120 C  CG    . HIS B 1 568 ? 118.618 167.763 168.129 1.00 35.80 ?  568 HIS B CG    1 
ATOM   10121 N  ND1   . HIS B 1 568 ? 118.504 167.409 169.455 1.00 36.83 ?  568 HIS B ND1   1 
ATOM   10122 C  CD2   . HIS B 1 568 ? 118.914 169.084 168.115 1.00 34.09 ?  568 HIS B CD2   1 
ATOM   10123 C  CE1   . HIS B 1 568 ? 118.724 168.470 170.211 1.00 32.59 ?  568 HIS B CE1   1 
ATOM   10124 N  NE2   . HIS B 1 568 ? 118.974 169.499 169.424 1.00 39.37 ?  568 HIS B NE2   1 
ATOM   10125 N  N     . GLY B 1 569 ? 116.563 165.273 164.674 1.00 28.65 ?  569 GLY B N     1 
ATOM   10126 C  CA    . GLY B 1 569 ? 116.670 164.363 163.554 1.00 27.61 ?  569 GLY B CA    1 
ATOM   10127 C  C     . GLY B 1 569 ? 117.658 163.243 163.811 1.00 29.72 ?  569 GLY B C     1 
ATOM   10128 O  O     . GLY B 1 569 ? 118.219 163.095 164.899 1.00 33.19 ?  569 GLY B O     1 
ATOM   10129 N  N     . MET B 1 570 ? 117.865 162.432 162.776 1.00 26.84 ?  570 MET B N     1 
ATOM   10130 C  CA    . MET B 1 570 ? 118.799 161.317 162.830 1.00 24.33 ?  570 MET B CA    1 
ATOM   10131 C  C     . MET B 1 570 ? 119.812 161.444 161.705 1.00 26.64 ?  570 MET B C     1 
ATOM   10132 O  O     . MET B 1 570 ? 119.452 161.750 160.565 1.00 30.44 ?  570 MET B O     1 
ATOM   10133 C  CB    . MET B 1 570 ? 118.080 159.970 162.726 1.00 25.96 ?  570 MET B CB    1 
ATOM   10134 C  CG    . MET B 1 570 ? 117.138 159.673 163.874 1.00 23.78 ?  570 MET B CG    1 
ATOM   10135 S  SD    . MET B 1 570 ? 117.509 158.096 164.652 1.00 38.72 ?  570 MET B SD    1 
ATOM   10136 C  CE    . MET B 1 570 ? 117.550 157.019 163.226 1.00 28.81 ?  570 MET B CE    1 
ATOM   10137 N  N     . TYR B 1 571 ? 121.081 161.204 162.032 1.00 19.73 ?  571 TYR B N     1 
ATOM   10138 C  CA    . TYR B 1 571 ? 122.135 161.290 161.028 1.00 11.33 ?  571 TYR B CA    1 
ATOM   10139 C  C     . TYR B 1 571 ? 122.142 160.091 160.091 1.00 18.37 ?  571 TYR B C     1 
ATOM   10140 O  O     . TYR B 1 571 ? 122.524 160.227 158.924 1.00 22.60 ?  571 TYR B O     1 
ATOM   10141 C  CB    . TYR B 1 571 ? 123.498 161.423 161.704 1.00 19.31 ?  571 TYR B CB    1 
ATOM   10142 C  CG    . TYR B 1 571 ? 124.601 161.831 160.758 1.00 20.16 ?  571 TYR B CG    1 
ATOM   10143 C  CD1   . TYR B 1 571 ? 124.671 163.125 160.263 1.00 23.18 ?  571 TYR B CD1   1 
ATOM   10144 C  CD2   . TYR B 1 571 ? 125.568 160.921 160.354 1.00 18.13 ?  571 TYR B CD2   1 
ATOM   10145 C  CE1   . TYR B 1 571 ? 125.675 163.504 159.397 1.00 23.37 ?  571 TYR B CE1   1 
ATOM   10146 C  CE2   . TYR B 1 571 ? 126.576 161.292 159.486 1.00 22.50 ?  571 TYR B CE2   1 
ATOM   10147 C  CZ    . TYR B 1 571 ? 126.625 162.584 159.011 1.00 27.73 ?  571 TYR B CZ    1 
ATOM   10148 O  OH    . TYR B 1 571 ? 127.628 162.957 158.148 1.00 26.73 ?  571 TYR B OH    1 
ATOM   10149 N  N     . HIS B 1 572 ? 121.733 158.921 160.571 1.00 20.02 ?  572 HIS B N     1 
ATOM   10150 C  CA    . HIS B 1 572 ? 121.820 157.684 159.809 1.00 13.85 ?  572 HIS B CA    1 
ATOM   10151 C  C     . HIS B 1 572 ? 120.425 157.194 159.453 1.00 22.03 ?  572 HIS B C     1 
ATOM   10152 O  O     . HIS B 1 572 ? 119.561 157.080 160.329 1.00 26.66 ?  572 HIS B O     1 
ATOM   10153 C  CB    . HIS B 1 572 ? 122.566 156.605 160.598 1.00 13.30 ?  572 HIS B CB    1 
ATOM   10154 C  CG    . HIS B 1 572 ? 123.851 157.077 161.199 1.00 14.70 ?  572 HIS B CG    1 
ATOM   10155 N  ND1   . HIS B 1 572 ? 123.936 157.563 162.486 1.00 18.30 ?  572 HIS B ND1   1 
ATOM   10156 C  CD2   . HIS B 1 572 ? 125.105 157.137 160.692 1.00 16.96 ?  572 HIS B CD2   1 
ATOM   10157 C  CE1   . HIS B 1 572 ? 125.186 157.903 162.745 1.00 19.14 ?  572 HIS B CE1   1 
ATOM   10158 N  NE2   . HIS B 1 572 ? 125.915 157.654 161.673 1.00 26.58 ?  572 HIS B NE2   1 
ATOM   10159 N  N     . SER B 1 573 ? 120.211 156.909 158.168 1.00 13.21 ?  573 SER B N     1 
ATOM   10160 C  CA    . SER B 1 573 ? 118.959 156.293 157.747 1.00 7.91  ?  573 SER B CA    1 
ATOM   10161 C  C     . SER B 1 573 ? 118.824 154.887 158.314 1.00 14.44 ?  573 SER B C     1 
ATOM   10162 O  O     . SER B 1 573 ? 117.727 154.468 158.702 1.00 21.39 ?  573 SER B O     1 
ATOM   10163 C  CB    . SER B 1 573 ? 118.874 156.268 156.223 1.00 14.15 ?  573 SER B CB    1 
ATOM   10164 O  OG    . SER B 1 573 ? 120.076 155.776 155.660 1.00 22.11 ?  573 SER B OG    1 
ATOM   10165 N  N     . TYR B 1 574 ? 119.926 154.144 158.363 1.00 14.03 ?  574 TYR B N     1 
ATOM   10166 C  CA    . TYR B 1 574 ? 119.948 152.793 158.897 1.00 7.35  ?  574 TYR B CA    1 
ATOM   10167 C  C     . TYR B 1 574 ? 121.165 152.653 159.796 1.00 8.48  ?  574 TYR B C     1 
ATOM   10168 O  O     . TYR B 1 574 ? 122.241 153.162 159.476 1.00 18.38 ?  574 TYR B O     1 
ATOM   10169 C  CB    . TYR B 1 574 ? 119.980 151.749 157.775 1.00 10.15 ?  574 TYR B CB    1 
ATOM   10170 C  CG    . TYR B 1 574 ? 118.862 151.914 156.774 1.00 7.41  ?  574 TYR B CG    1 
ATOM   10171 C  CD1   . TYR B 1 574 ? 119.000 152.766 155.686 1.00 9.48  ?  574 TYR B CD1   1 
ATOM   10172 C  CD2   . TYR B 1 574 ? 117.666 151.225 156.918 1.00 7.15  ?  574 TYR B CD2   1 
ATOM   10173 C  CE1   . TYR B 1 574 ? 117.981 152.929 154.774 1.00 9.78  ?  574 TYR B CE1   1 
ATOM   10174 C  CE2   . TYR B 1 574 ? 116.642 151.381 156.008 1.00 9.31  ?  574 TYR B CE2   1 
ATOM   10175 C  CZ    . TYR B 1 574 ? 116.806 152.234 154.939 1.00 4.50  ?  574 TYR B CZ    1 
ATOM   10176 O  OH    . TYR B 1 574 ? 115.790 152.391 154.026 1.00 17.16 ?  574 TYR B OH    1 
ATOM   10177 N  N     . ARG B 1 575 ? 120.988 151.970 160.920 1.00 10.32 ?  575 ARG B N     1 
ATOM   10178 C  CA    . ARG B 1 575 ? 122.027 151.894 161.939 1.00 4.99  ?  575 ARG B CA    1 
ATOM   10179 C  C     . ARG B 1 575 ? 122.444 150.476 162.289 1.00 12.76 ?  575 ARG B C     1 
ATOM   10180 O  O     . ARG B 1 575 ? 123.638 150.217 162.452 1.00 18.56 ?  575 ARG B O     1 
ATOM   10181 C  CB    . ARG B 1 575 ? 121.559 152.606 163.213 1.00 13.95 ?  575 ARG B CB    1 
ATOM   10182 C  CG    . ARG B 1 575 ? 121.236 154.074 163.024 1.00 6.32  ?  575 ARG B CG    1 
ATOM   10183 C  CD    . ARG B 1 575 ? 120.241 154.547 164.065 1.00 13.67 ?  575 ARG B CD    1 
ATOM   10184 N  NE    . ARG B 1 575 ? 118.926 153.946 163.875 1.00 18.22 ?  575 ARG B NE    1 
ATOM   10185 C  CZ    . ARG B 1 575 ? 118.450 152.938 164.593 1.00 13.40 ?  575 ARG B CZ    1 
ATOM   10186 N  NH1   . ARG B 1 575 ? 119.162 152.382 165.559 1.00 12.95 1  575 ARG B NH1   1 
ATOM   10187 N  NH2   . ARG B 1 575 ? 117.230 152.476 164.335 1.00 11.24 ?  575 ARG B NH2   1 
ATOM   10188 N  N     . LEU B 1 576 ? 121.500 149.549 162.406 1.00 20.40 ?  576 LEU B N     1 
ATOM   10189 C  CA    . LEU B 1 576 ? 121.774 148.213 162.916 1.00 10.53 ?  576 LEU B CA    1 
ATOM   10190 C  C     . LEU B 1 576 ? 121.507 147.176 161.837 1.00 5.36  ?  576 LEU B C     1 
ATOM   10191 O  O     . LEU B 1 576 ? 120.410 147.127 161.275 1.00 15.05 ?  576 LEU B O     1 
ATOM   10192 C  CB    . LEU B 1 576 ? 120.919 147.914 164.150 1.00 6.04  ?  576 LEU B CB    1 
ATOM   10193 C  CG    . LEU B 1 576 ? 120.956 148.940 165.283 1.00 7.13  ?  576 LEU B CG    1 
ATOM   10194 C  CD1   . LEU B 1 576 ? 119.951 148.574 166.360 1.00 13.51 ?  576 LEU B CD1   1 
ATOM   10195 C  CD2   . LEU B 1 576 ? 122.350 149.044 165.865 1.00 10.43 ?  576 LEU B CD2   1 
ATOM   10196 N  N     . CYS B 1 577 ? 122.513 146.354 161.552 1.00 14.04 ?  577 CYS B N     1 
ATOM   10197 C  CA    . CYS B 1 577 ? 122.353 145.180 160.707 1.00 8.07  ?  577 CYS B CA    1 
ATOM   10198 C  C     . CYS B 1 577 ? 123.309 144.115 161.219 1.00 14.92 ?  577 CYS B C     1 
ATOM   10199 O  O     . CYS B 1 577 ? 124.481 144.404 161.476 1.00 21.80 ?  577 CYS B O     1 
ATOM   10200 C  CB    . CYS B 1 577 ? 122.610 145.504 159.226 1.00 5.93  ?  577 CYS B CB    1 
ATOM   10201 S  SG    . CYS B 1 577 ? 124.316 145.367 158.638 1.00 35.18 ?  577 CYS B SG    1 
ATOM   10202 N  N     . ILE B 1 578 ? 122.804 142.900 161.393 1.00 16.01 ?  578 ILE B N     1 
ATOM   10203 C  CA    . ILE B 1 578 ? 123.559 141.818 162.013 1.00 12.46 ?  578 ILE B CA    1 
ATOM   10204 C  C     . ILE B 1 578 ? 124.108 140.938 160.895 1.00 9.65  ?  578 ILE B C     1 
ATOM   10205 O  O     . ILE B 1 578 ? 123.403 140.086 160.347 1.00 18.17 ?  578 ILE B O     1 
ATOM   10206 C  CB    . ILE B 1 578 ? 122.703 141.026 163.004 1.00 9.77  ?  578 ILE B CB    1 
ATOM   10207 C  CG1   . ILE B 1 578 ? 122.170 141.958 164.093 1.00 8.00  ?  578 ILE B CG1   1 
ATOM   10208 C  CG2   . ILE B 1 578 ? 123.509 139.909 163.631 1.00 9.50  ?  578 ILE B CG2   1 
ATOM   10209 C  CD1   . ILE B 1 578 ? 121.475 141.243 165.217 1.00 8.95  ?  578 ILE B CD1   1 
ATOM   10210 N  N     . ALA B 1 579 ? 125.375 141.154 160.557 1.00 17.09 ?  579 ALA B N     1 
ATOM   10211 C  CA    . ALA B 1 579 ? 126.074 140.392 159.540 1.00 7.33  ?  579 ALA B CA    1 
ATOM   10212 C  C     . ALA B 1 579 ? 126.475 139.019 160.073 1.00 21.03 ?  579 ALA B C     1 
ATOM   10213 O  O     . ALA B 1 579 ? 126.472 138.789 161.284 1.00 28.62 ?  579 ALA B O     1 
ATOM   10214 C  CB    . ALA B 1 579 ? 127.305 141.162 159.075 1.00 11.73 ?  579 ALA B CB    1 
ATOM   10215 N  N     . PRO B 1 580 ? 126.799 138.073 159.184 1.00 25.04 ?  580 PRO B N     1 
ATOM   10216 C  CA    . PRO B 1 580 ? 127.246 136.752 159.657 1.00 22.61 ?  580 PRO B CA    1 
ATOM   10217 C  C     . PRO B 1 580 ? 128.512 136.787 160.500 1.00 25.92 ?  580 PRO B C     1 
ATOM   10218 O  O     . PRO B 1 580 ? 128.656 135.949 161.400 1.00 32.85 ?  580 PRO B O     1 
ATOM   10219 C  CB    . PRO B 1 580 ? 127.455 135.961 158.356 1.00 22.52 ?  580 PRO B CB    1 
ATOM   10220 C  CG    . PRO B 1 580 ? 127.457 136.975 157.260 1.00 21.75 ?  580 PRO B CG    1 
ATOM   10221 C  CD    . PRO B 1 580 ? 126.595 138.092 157.726 1.00 19.76 ?  580 PRO B CD    1 
ATOM   10222 N  N     . THR B 1 581 ? 129.428 137.723 160.241 1.00 21.55 ?  581 THR B N     1 
ATOM   10223 C  CA    . THR B 1 581 ? 130.696 137.842 160.971 1.00 29.18 ?  581 THR B CA    1 
ATOM   10224 C  C     . THR B 1 581 ? 131.447 136.506 160.991 1.00 28.51 ?  581 THR B C     1 
ATOM   10225 O  O     . THR B 1 581 ? 131.660 135.885 162.031 1.00 27.81 ?  581 THR B O     1 
ATOM   10226 C  CB    . THR B 1 581 ? 130.484 138.361 162.399 1.00 28.11 ?  581 THR B CB    1 
ATOM   10227 O  OG1   . THR B 1 581 ? 130.242 137.259 163.284 1.00 27.66 ?  581 THR B OG1   1 
ATOM   10228 C  CG2   . THR B 1 581 ? 129.326 139.343 162.466 1.00 30.44 ?  581 THR B CG2   1 
ATOM   10229 N  N     . GLY B 1 582 ? 131.849 136.085 159.794 1.00 31.48 ?  582 GLY B N     1 
ATOM   10230 C  CA    . GLY B 1 582 ? 132.422 134.767 159.610 1.00 33.44 ?  582 GLY B CA    1 
ATOM   10231 C  C     . GLY B 1 582 ? 133.764 134.531 160.274 1.00 37.00 ?  582 GLY B C     1 
ATOM   10232 O  O     . GLY B 1 582 ? 133.858 133.741 161.219 1.00 38.24 ?  582 GLY B O     1 
ATOM   10233 N  N     . SER B 1 583 ? 134.812 135.206 159.800 1.00 31.25 ?  583 SER B N     1 
ATOM   10234 C  CA    . SER B 1 583 ? 136.166 134.911 160.251 1.00 33.74 ?  583 SER B CA    1 
ATOM   10235 C  C     . SER B 1 583 ? 136.672 135.852 161.334 1.00 35.09 ?  583 SER B C     1 
ATOM   10236 O  O     . SER B 1 583 ? 137.570 135.468 162.091 1.00 37.38 ?  583 SER B O     1 
ATOM   10237 C  CB    . SER B 1 583 ? 137.139 134.948 159.066 1.00 37.87 ?  583 SER B CB    1 
ATOM   10238 O  OG    . SER B 1 583 ? 137.159 133.702 158.391 1.00 41.00 ?  583 SER B OG    1 
ATOM   10239 N  N     . ILE B 1 584 ? 136.124 137.065 161.431 1.00 33.94 ?  584 ILE B N     1 
ATOM   10240 C  CA    . ILE B 1 584 ? 136.555 137.982 162.477 1.00 27.57 ?  584 ILE B CA    1 
ATOM   10241 C  C     . ILE B 1 584 ? 136.016 137.571 163.841 1.00 26.21 ?  584 ILE B C     1 
ATOM   10242 O  O     . ILE B 1 584 ? 136.484 138.079 164.867 1.00 29.85 ?  584 ILE B O     1 
ATOM   10243 C  CB    . ILE B 1 584 ? 136.142 139.423 162.125 1.00 31.69 ?  584 ILE B CB    1 
ATOM   10244 C  CG1   . ILE B 1 584 ? 137.086 140.424 162.791 1.00 28.37 ?  584 ILE B CG1   1 
ATOM   10245 C  CG2   . ILE B 1 584 ? 134.700 139.686 162.533 1.00 29.13 ?  584 ILE B CG2   1 
ATOM   10246 C  CD1   . ILE B 1 584 ? 138.539 140.218 162.474 1.00 31.61 ?  584 ILE B CD1   1 
ATOM   10247 N  N     . SER B 1 585 ? 135.043 136.658 163.883 1.00 31.58 ?  585 SER B N     1 
ATOM   10248 C  CA    . SER B 1 585 ? 134.570 136.148 165.164 1.00 30.22 ?  585 SER B CA    1 
ATOM   10249 C  C     . SER B 1 585 ? 135.617 135.267 165.831 1.00 28.05 ?  585 SER B C     1 
ATOM   10250 O  O     . SER B 1 585 ? 135.609 135.117 167.057 1.00 26.72 ?  585 SER B O     1 
ATOM   10251 C  CB    . SER B 1 585 ? 133.265 135.375 164.975 1.00 25.61 ?  585 SER B CB    1 
ATOM   10252 O  OG    . SER B 1 585 ? 133.452 134.259 164.123 1.00 30.23 ?  585 SER B OG    1 
ATOM   10253 N  N     . TYR B 1 586 ? 136.515 134.673 165.042 1.00 31.10 ?  586 TYR B N     1 
ATOM   10254 C  CA    . TYR B 1 586 ? 137.605 133.887 165.606 1.00 32.10 ?  586 TYR B CA    1 
ATOM   10255 C  C     . TYR B 1 586 ? 138.532 134.760 166.441 1.00 31.26 ?  586 TYR B C     1 
ATOM   10256 O  O     . TYR B 1 586 ? 138.902 134.398 167.564 1.00 34.53 ?  586 TYR B O     1 
ATOM   10257 C  CB    . TYR B 1 586 ? 138.387 133.207 164.484 1.00 28.08 ?  586 TYR B CB    1 
ATOM   10258 C  CG    . TYR B 1 586 ? 137.704 131.999 163.892 1.00 31.07 ?  586 TYR B CG    1 
ATOM   10259 C  CD1   . TYR B 1 586 ? 137.420 130.886 164.670 1.00 31.09 ?  586 TYR B CD1   1 
ATOM   10260 C  CD2   . TYR B 1 586 ? 137.339 131.976 162.554 1.00 31.81 ?  586 TYR B CD2   1 
ATOM   10261 C  CE1   . TYR B 1 586 ? 136.794 129.783 164.129 1.00 33.96 ?  586 TYR B CE1   1 
ATOM   10262 C  CE2   . TYR B 1 586 ? 136.712 130.877 162.005 1.00 30.57 ?  586 TYR B CE2   1 
ATOM   10263 C  CZ    . TYR B 1 586 ? 136.443 129.784 162.797 1.00 34.73 ?  586 TYR B CZ    1 
ATOM   10264 O  OH    . TYR B 1 586 ? 135.818 128.687 162.251 1.00 37.76 ?  586 TYR B OH    1 
ATOM   10265 N  N     . VAL B 1 587 ? 138.908 135.924 165.906 1.00 28.11 ?  587 VAL B N     1 
ATOM   10266 C  CA    . VAL B 1 587 ? 139.859 136.799 166.586 1.00 24.65 ?  587 VAL B CA    1 
ATOM   10267 C  C     . VAL B 1 587 ? 139.278 137.310 167.897 1.00 29.14 ?  587 VAL B C     1 
ATOM   10268 O  O     . VAL B 1 587 ? 139.991 137.453 168.897 1.00 35.72 ?  587 VAL B O     1 
ATOM   10269 C  CB    . VAL B 1 587 ? 140.268 137.960 165.660 1.00 30.15 ?  587 VAL B CB    1 
ATOM   10270 C  CG1   . VAL B 1 587 ? 141.400 138.761 166.278 1.00 30.11 ?  587 VAL B CG1   1 
ATOM   10271 C  CG2   . VAL B 1 587 ? 140.663 137.432 164.291 1.00 28.67 ?  587 VAL B CG2   1 
ATOM   10272 N  N     . GLN B 1 588 ? 137.978 137.587 167.916 1.00 31.14 ?  588 GLN B N     1 
ATOM   10273 C  CA    . GLN B 1 588 ? 137.320 138.114 169.102 1.00 24.26 ?  588 GLN B CA    1 
ATOM   10274 C  C     . GLN B 1 588 ? 136.966 137.035 170.115 1.00 25.55 ?  588 GLN B C     1 
ATOM   10275 O  O     . GLN B 1 588 ? 136.433 137.366 171.179 1.00 32.76 ?  588 GLN B O     1 
ATOM   10276 C  CB    . GLN B 1 588 ? 136.054 138.876 168.706 1.00 25.03 ?  588 GLN B CB    1 
ATOM   10277 C  CG    . GLN B 1 588 ? 136.320 140.228 168.072 1.00 28.82 ?  588 GLN B CG    1 
ATOM   10278 C  CD    . GLN B 1 588 ? 136.217 141.363 169.070 1.00 24.32 ?  588 GLN B CD    1 
ATOM   10279 O  OE1   . GLN B 1 588 ? 135.264 141.439 169.842 1.00 29.94 ?  588 GLN B OE1   1 
ATOM   10280 N  NE2   . GLN B 1 588 ? 137.200 142.253 169.058 1.00 26.90 ?  588 GLN B NE2   1 
ATOM   10281 N  N     . SER B 1 589 ? 137.257 135.769 169.814 1.00 30.06 ?  589 SER B N     1 
ATOM   10282 C  CA    . SER B 1 589 ? 136.874 134.639 170.656 1.00 27.12 ?  589 SER B CA    1 
ATOM   10283 C  C     . SER B 1 589 ? 135.375 134.679 170.940 1.00 26.93 ?  589 SER B C     1 
ATOM   10284 O  O     . SER B 1 589 ? 134.921 134.716 172.085 1.00 28.72 ?  589 SER B O     1 
ATOM   10285 C  CB    . SER B 1 589 ? 137.689 134.614 171.952 1.00 32.57 ?  589 SER B CB    1 
ATOM   10286 O  OG    . SER B 1 589 ? 139.063 134.412 171.681 1.00 36.64 ?  589 SER B OG    1 
ATOM   10287 N  N     . SER B 1 590 ? 134.607 134.684 169.854 1.00 25.89 ?  590 SER B N     1 
ATOM   10288 C  CA    . SER B 1 590 ? 133.169 134.871 169.921 1.00 22.92 ?  590 SER B CA    1 
ATOM   10289 C  C     . SER B 1 590 ? 132.485 133.917 168.956 1.00 25.94 ?  590 SER B C     1 
ATOM   10290 O  O     . SER B 1 590 ? 133.055 133.527 167.934 1.00 29.51 ?  590 SER B O     1 
ATOM   10291 C  CB    . SER B 1 590 ? 132.783 136.317 169.588 1.00 21.98 ?  590 SER B CB    1 
ATOM   10292 O  OG    . SER B 1 590 ? 132.522 136.470 168.205 1.00 31.28 ?  590 SER B OG    1 
ATOM   10293 N  N     . THR B 1 591 ? 131.256 133.538 169.295 1.00 25.52 ?  591 THR B N     1 
ATOM   10294 C  CA    . THR B 1 591 ? 130.436 132.771 168.372 1.00 21.76 ?  591 THR B CA    1 
ATOM   10295 C  C     . THR B 1 591 ? 129.955 133.664 167.235 1.00 24.15 ?  591 THR B C     1 
ATOM   10296 O  O     . THR B 1 591 ? 129.731 134.864 167.409 1.00 22.75 ?  591 THR B O     1 
ATOM   10297 C  CB    . THR B 1 591 ? 129.246 132.148 169.097 1.00 22.02 ?  591 THR B CB    1 
ATOM   10298 O  OG1   . THR B 1 591 ? 128.289 133.166 169.416 1.00 29.69 ?  591 THR B OG1   1 
ATOM   10299 C  CG2   . THR B 1 591 ? 129.704 131.471 170.375 1.00 20.22 ?  591 THR B CG2   1 
ATOM   10300 N  N     . ALA B 1 592 ? 129.800 133.063 166.059 1.00 22.71 ?  592 ALA B N     1 
ATOM   10301 C  CA    . ALA B 1 592 ? 129.499 133.824 164.854 1.00 20.11 ?  592 ALA B CA    1 
ATOM   10302 C  C     . ALA B 1 592 ? 128.112 134.450 164.947 1.00 19.32 ?  592 ALA B C     1 
ATOM   10303 O  O     . ALA B 1 592 ? 127.104 133.738 164.991 1.00 27.49 ?  592 ALA B O     1 
ATOM   10304 C  CB    . ALA B 1 592 ? 129.596 132.923 163.626 1.00 24.99 ?  592 ALA B CB    1 
ATOM   10305 N  N     . SER B 1 593 ? 128.071 135.778 164.985 1.00 25.09 ?  593 SER B N     1 
ATOM   10306 C  CA    . SER B 1 593 ? 126.832 136.560 164.886 1.00 14.55 ?  593 SER B CA    1 
ATOM   10307 C  C     . SER B 1 593 ? 125.910 136.187 166.049 1.00 16.18 ?  593 SER B C     1 
ATOM   10308 O  O     . SER B 1 593 ? 126.372 135.751 167.111 1.00 27.98 ?  593 SER B O     1 
ATOM   10309 C  CB    . SER B 1 593 ? 126.226 136.359 163.508 1.00 27.06 ?  593 SER B CB    1 
ATOM   10310 O  OG    . SER B 1 593 ? 125.167 137.266 163.273 1.00 23.36 ?  593 SER B OG    1 
ATOM   10311 N  N     . VAL B 1 594 ? 124.602 136.360 165.859 1.00 19.65 ?  594 VAL B N     1 
ATOM   10312 C  CA    . VAL B 1 594 ? 123.608 135.927 166.830 1.00 19.52 ?  594 VAL B CA    1 
ATOM   10313 C  C     . VAL B 1 594 ? 123.123 134.510 166.543 1.00 18.59 ?  594 VAL B C     1 
ATOM   10314 O  O     . VAL B 1 594 ? 122.199 134.026 167.202 1.00 18.18 ?  594 VAL B O     1 
ATOM   10315 C  CB    . VAL B 1 594 ? 122.426 136.908 166.889 1.00 17.07 ?  594 VAL B CB    1 
ATOM   10316 C  CG1   . VAL B 1 594 ? 122.898 138.277 167.349 1.00 12.24 ?  594 VAL B CG1   1 
ATOM   10317 C  CG2   . VAL B 1 594 ? 121.746 137.003 165.534 1.00 19.04 ?  594 VAL B CG2   1 
ATOM   10318 N  N     . MET B 1 595 ? 123.727 133.836 165.568 1.00 23.61 ?  595 MET B N     1 
ATOM   10319 C  CA    . MET B 1 595 ? 123.363 132.465 165.263 1.00 19.01 ?  595 MET B CA    1 
ATOM   10320 C  C     . MET B 1 595 ? 123.879 131.524 166.348 1.00 26.69 ?  595 MET B C     1 
ATOM   10321 O  O     . MET B 1 595 ? 124.902 131.796 166.984 1.00 29.65 ?  595 MET B O     1 
ATOM   10322 C  CB    . MET B 1 595 ? 123.937 132.046 163.912 1.00 18.08 ?  595 MET B CB    1 
ATOM   10323 C  CG    . MET B 1 595 ? 123.111 132.449 162.698 1.00 24.07 ?  595 MET B CG    1 
ATOM   10324 S  SD    . MET B 1 595 ? 121.345 132.587 163.019 1.00 29.78 ?  595 MET B SD    1 
ATOM   10325 C  CE    . MET B 1 595 ? 121.164 134.365 163.052 1.00 22.55 ?  595 MET B CE    1 
ATOM   10326 N  N     . PRO B 1 596 ? 123.190 130.412 166.584 1.00 29.56 ?  596 PRO B N     1 
ATOM   10327 C  CA    . PRO B 1 596 ? 123.738 129.382 167.469 1.00 19.09 ?  596 PRO B CA    1 
ATOM   10328 C  C     . PRO B 1 596 ? 124.908 128.663 166.815 1.00 25.93 ?  596 PRO B C     1 
ATOM   10329 O  O     . PRO B 1 596 ? 125.042 128.614 165.590 1.00 30.62 ?  596 PRO B O     1 
ATOM   10330 C  CB    . PRO B 1 596 ? 122.555 128.438 167.696 1.00 20.74 ?  596 PRO B CB    1 
ATOM   10331 C  CG    . PRO B 1 596 ? 121.694 128.622 166.498 1.00 23.25 ?  596 PRO B CG    1 
ATOM   10332 C  CD    . PRO B 1 596 ? 121.861 130.050 166.061 1.00 25.77 ?  596 PRO B CD    1 
ATOM   10333 N  N     . ILE B 1 597 ? 125.772 128.103 167.664 1.00 28.44 ?  597 ILE B N     1 
ATOM   10334 C  CA    . ILE B 1 597 ? 126.999 127.480 167.187 1.00 31.03 ?  597 ILE B CA    1 
ATOM   10335 C  C     . ILE B 1 597 ? 126.671 126.252 166.347 1.00 34.42 ?  597 ILE B C     1 
ATOM   10336 O  O     . ILE B 1 597 ? 125.752 125.483 166.661 1.00 37.08 ?  597 ILE B O     1 
ATOM   10337 C  CB    . ILE B 1 597 ? 127.915 127.118 168.367 1.00 32.17 ?  597 ILE B CB    1 
ATOM   10338 C  CG1   . ILE B 1 597 ? 127.236 126.098 169.284 1.00 30.45 ?  597 ILE B CG1   1 
ATOM   10339 C  CG2   . ILE B 1 597 ? 128.292 128.363 169.144 1.00 29.22 ?  597 ILE B CG2   1 
ATOM   10340 C  CD1   . ILE B 1 597 ? 128.195 125.162 169.973 1.00 29.18 ?  597 ILE B CD1   1 
ATOM   10341 N  N     . MET B 1 598 ? 127.418 126.074 165.257 1.00 40.22 ?  598 MET B N     1 
ATOM   10342 C  CA    . MET B 1 598 ? 127.243 124.886 164.429 1.00 38.65 ?  598 MET B CA    1 
ATOM   10343 C  C     . MET B 1 598 ? 127.759 123.642 165.138 1.00 36.48 ?  598 MET B C     1 
ATOM   10344 O  O     . MET B 1 598 ? 127.116 122.587 165.103 1.00 42.09 ?  598 MET B O     1 
ATOM   10345 C  CB    . MET B 1 598 ? 127.952 125.073 163.089 1.00 38.14 ?  598 MET B CB    1 
ATOM   10346 C  CG    . MET B 1 598 ? 127.145 125.846 162.065 1.00 35.63 ?  598 MET B CG    1 
ATOM   10347 S  SD    . MET B 1 598 ? 128.171 126.624 160.804 1.00 53.34 ?  598 MET B SD    1 
ATOM   10348 C  CE    . MET B 1 598 ? 129.317 127.549 161.822 1.00 40.76 ?  598 MET B CE    1 
ATOM   10349 N  N     . GLU B 1 599 ? 128.916 123.746 165.788 1.00 37.86 ?  599 GLU B N     1 
ATOM   10350 C  CA    . GLU B 1 599 ? 129.511 122.624 166.496 1.00 37.80 ?  599 GLU B CA    1 
ATOM   10351 C  C     . GLU B 1 599 ? 130.251 123.149 167.715 1.00 34.97 ?  599 GLU B C     1 
ATOM   10352 O  O     . GLU B 1 599 ? 130.712 124.293 167.732 1.00 40.23 ?  599 GLU B O     1 
ATOM   10353 C  CB    . GLU B 1 599 ? 130.464 121.833 165.594 1.00 39.85 ?  599 GLU B CB    1 
ATOM   10354 C  CG    . GLU B 1 599 ? 131.454 122.703 164.842 1.00 37.81 ?  599 GLU B CG    1 
ATOM   10355 C  CD    . GLU B 1 599 ? 131.720 122.205 163.436 1.00 43.29 ?  599 GLU B CD    1 
ATOM   10356 O  OE1   . GLU B 1 599 ? 131.593 120.985 163.203 1.00 44.64 ?  599 GLU B OE1   1 
ATOM   10357 O  OE2   . GLU B 1 599 ? 132.058 123.034 162.565 1.00 43.83 -1 599 GLU B OE2   1 
ATOM   10358 N  N     . ARG B 1 600 ? 130.357 122.301 168.739 1.00 36.52 ?  600 ARG B N     1 
ATOM   10359 C  CA    . ARG B 1 600 ? 131.066 122.695 169.951 1.00 32.88 ?  600 ARG B CA    1 
ATOM   10360 C  C     . ARG B 1 600 ? 132.559 122.833 169.693 1.00 33.71 ?  600 ARG B C     1 
ATOM   10361 O  O     . ARG B 1 600 ? 133.178 123.833 170.074 1.00 39.87 ?  600 ARG B O     1 
ATOM   10362 C  CB    . ARG B 1 600 ? 130.799 121.682 171.062 1.00 35.62 ?  600 ARG B CB    1 
ATOM   10363 C  CG    . ARG B 1 600 ? 129.421 121.803 171.674 1.00 33.67 ?  600 ARG B CG    1 
ATOM   10364 C  CD    . ARG B 1 600 ? 129.301 120.962 172.922 1.00 31.09 ?  600 ARG B CD    1 
ATOM   10365 N  NE    . ARG B 1 600 ? 127.945 120.962 173.454 1.00 32.40 ?  600 ARG B NE    1 
ATOM   10366 C  CZ    . ARG B 1 600 ? 126.959 120.208 172.989 1.00 34.59 ?  600 ARG B CZ    1 
ATOM   10367 N  NH1   . ARG B 1 600 ? 127.139 119.386 171.969 1.00 33.92 1  600 ARG B NH1   1 
ATOM   10368 N  NH2   . ARG B 1 600 ? 125.762 120.281 173.563 1.00 35.08 ?  600 ARG B NH2   1 
ATOM   10369 N  N     . ILE B 1 601 ? 133.158 121.836 169.048 1.00 38.78 ?  601 ILE B N     1 
ATOM   10370 C  CA    . ILE B 1 601 ? 134.554 121.876 168.633 1.00 37.26 ?  601 ILE B CA    1 
ATOM   10371 C  C     . ILE B 1 601 ? 134.587 121.649 167.130 1.00 37.70 ?  601 ILE B C     1 
ATOM   10372 O  O     . ILE B 1 601 ? 134.085 120.628 166.642 1.00 42.98 ?  601 ILE B O     1 
ATOM   10373 C  CB    . ILE B 1 601 ? 135.405 120.828 169.366 1.00 39.69 ?  601 ILE B CB    1 
ATOM   10374 C  CG1   . ILE B 1 601 ? 135.118 120.858 170.867 1.00 40.45 ?  601 ILE B CG1   1 
ATOM   10375 C  CG2   . ILE B 1 601 ? 136.882 121.065 169.101 1.00 37.99 ?  601 ILE B CG2   1 
ATOM   10376 C  CD1   . ILE B 1 601 ? 135.752 119.719 171.633 1.00 39.25 ?  601 ILE B CD1   1 
ATOM   10377 N  N     . GLU B 1 602 ? 135.173 122.590 166.399 1.00 45.48 ?  602 GLU B N     1 
ATOM   10378 C  CA    . GLU B 1 602 ? 135.241 122.508 164.948 1.00 46.01 ?  602 GLU B CA    1 
ATOM   10379 C  C     . GLU B 1 602 ? 136.639 122.097 164.509 1.00 47.78 ?  602 GLU B C     1 
ATOM   10380 O  O     . GLU B 1 602 ? 137.636 122.673 164.952 1.00 47.96 ?  602 GLU B O     1 
ATOM   10381 C  CB    . GLU B 1 602 ? 134.864 123.842 164.303 1.00 44.80 ?  602 GLU B CB    1 
ATOM   10382 C  CG    . GLU B 1 602 ? 135.418 125.058 165.015 1.00 47.22 ?  602 GLU B CG    1 
ATOM   10383 C  CD    . GLU B 1 602 ? 135.422 126.289 164.136 1.00 50.05 ?  602 GLU B CD    1 
ATOM   10384 O  OE1   . GLU B 1 602 ? 134.332 126.835 163.867 1.00 48.81 ?  602 GLU B OE1   1 
ATOM   10385 O  OE2   . GLU B 1 602 ? 136.518 126.707 163.708 1.00 49.61 -1 602 GLU B OE2   1 
ATOM   10386 N  N     . GLU B 1 603 ? 136.705 121.098 163.633 1.00 53.84 ?  603 GLU B N     1 
ATOM   10387 C  CA    . GLU B 1 603 ? 137.965 120.597 163.099 1.00 54.70 ?  603 GLU B CA    1 
ATOM   10388 C  C     . GLU B 1 603 ? 138.180 121.216 161.722 1.00 53.81 ?  603 GLU B C     1 
ATOM   10389 O  O     . GLU B 1 603 ? 137.427 120.937 160.783 1.00 54.77 ?  603 GLU B O     1 
ATOM   10390 C  CB    . GLU B 1 603 ? 137.960 119.072 163.027 1.00 54.03 ?  603 GLU B CB    1 
ATOM   10391 C  CG    . GLU B 1 603 ? 139.230 118.471 162.451 1.00 56.11 ?  603 GLU B CG    1 
ATOM   10392 C  CD    . GLU B 1 603 ? 139.051 117.026 162.028 1.00 58.17 ?  603 GLU B CD    1 
ATOM   10393 O  OE1   . GLU B 1 603 ? 139.007 116.147 162.914 1.00 57.94 ?  603 GLU B OE1   1 
ATOM   10394 O  OE2   . GLU B 1 603 ? 138.952 116.769 160.810 1.00 56.54 -1 603 GLU B OE2   1 
ATOM   10395 N  N     . ARG B 1 604 ? 139.207 122.054 161.606 1.00 55.14 ?  604 ARG B N     1 
ATOM   10396 C  CA    . ARG B 1 604 ? 139.526 122.749 160.369 1.00 55.62 ?  604 ARG B CA    1 
ATOM   10397 C  C     . ARG B 1 604 ? 140.920 122.352 159.909 1.00 56.99 ?  604 ARG B C     1 
ATOM   10398 O  O     . ARG B 1 604 ? 141.855 122.288 160.712 1.00 58.94 ?  604 ARG B O     1 
ATOM   10399 C  CB    . ARG B 1 604 ? 139.449 124.268 160.555 1.00 57.20 ?  604 ARG B CB    1 
ATOM   10400 C  CG    . ARG B 1 604 ? 138.036 124.831 160.581 1.00 57.77 ?  604 ARG B CG    1 
ATOM   10401 C  CD    . ARG B 1 604 ? 137.148 124.173 159.539 1.00 56.81 ?  604 ARG B CD    1 
ATOM   10402 N  NE    . ARG B 1 604 ? 136.125 123.330 160.148 1.00 59.20 ?  604 ARG B NE    1 
ATOM   10403 C  CZ    . ARG B 1 604 ? 134.971 123.778 160.623 1.00 59.01 ?  604 ARG B CZ    1 
ATOM   10404 N  NH1   . ARG B 1 604 ? 134.658 125.062 160.583 1.00 56.40 1  604 ARG B NH1   1 
ATOM   10405 N  NH2   . ARG B 1 604 ? 134.108 122.913 161.149 1.00 56.67 ?  604 ARG B NH2   1 
ATOM   10406 N  N     . THR B 1 605 ? 141.062 122.096 158.613 1.00 63.74 ?  605 THR B N     1 
ATOM   10407 C  CA    . THR B 1 605 ? 142.332 121.677 158.037 1.00 64.57 ?  605 THR B CA    1 
ATOM   10408 C  C     . THR B 1 605 ? 143.038 122.889 157.441 1.00 64.75 ?  605 THR B C     1 
ATOM   10409 O  O     . THR B 1 605 ? 142.502 123.544 156.540 1.00 64.19 ?  605 THR B O     1 
ATOM   10410 C  CB    . THR B 1 605 ? 142.123 120.602 156.971 1.00 64.44 ?  605 THR B CB    1 
ATOM   10411 O  OG1   . THR B 1 605 ? 141.500 119.455 157.564 1.00 64.01 ?  605 THR B OG1   1 
ATOM   10412 C  CG2   . THR B 1 605 ? 143.455 120.192 156.365 1.00 64.39 ?  605 THR B CG2   1 
ATOM   10413 N  N     . TYR B 1 606 ? 144.232 123.183 157.947 1.00 64.82 ?  606 TYR B N     1 
ATOM   10414 C  CA    . TYR B 1 606 ? 145.072 124.254 157.428 1.00 66.48 ?  606 TYR B CA    1 
ATOM   10415 C  C     . TYR B 1 606 ? 146.398 123.657 156.983 1.00 67.41 ?  606 TYR B C     1 
ATOM   10416 O  O     . TYR B 1 606 ? 147.059 122.956 157.758 1.00 65.23 ?  606 TYR B O     1 
ATOM   10417 C  CB    . TYR B 1 606 ? 145.296 125.344 158.480 1.00 64.43 ?  606 TYR B CB    1 
ATOM   10418 C  CG    . TYR B 1 606 ? 144.017 125.995 158.958 1.00 65.10 ?  606 TYR B CG    1 
ATOM   10419 C  CD1   . TYR B 1 606 ? 143.312 126.868 158.139 1.00 64.08 ?  606 TYR B CD1   1 
ATOM   10420 C  CD2   . TYR B 1 606 ? 143.514 125.737 160.227 1.00 63.67 ?  606 TYR B CD2   1 
ATOM   10421 C  CE1   . TYR B 1 606 ? 142.144 127.464 158.569 1.00 64.22 ?  606 TYR B CE1   1 
ATOM   10422 C  CE2   . TYR B 1 606 ? 142.346 126.329 160.665 1.00 62.41 ?  606 TYR B CE2   1 
ATOM   10423 C  CZ    . TYR B 1 606 ? 141.665 127.192 159.833 1.00 65.40 ?  606 TYR B CZ    1 
ATOM   10424 O  OH    . TYR B 1 606 ? 140.500 127.784 160.265 1.00 66.17 ?  606 TYR B OH    1 
ATOM   10425 N  N     . GLY B 1 607 ? 146.781 123.936 155.740 1.00 74.58 ?  607 GLY B N     1 
ATOM   10426 C  CA    . GLY B 1 607 ? 147.959 123.298 155.180 1.00 74.32 ?  607 GLY B CA    1 
ATOM   10427 C  C     . GLY B 1 607 ? 147.787 121.792 155.178 1.00 75.00 ?  607 GLY B C     1 
ATOM   10428 O  O     . GLY B 1 607 ? 146.759 121.261 154.746 1.00 73.95 ?  607 GLY B O     1 
ATOM   10429 N  N     . ASN B 1 608 ? 148.803 121.088 155.670 1.00 78.45 ?  608 ASN B N     1 
ATOM   10430 C  CA    . ASN B 1 608 ? 148.734 119.648 155.862 1.00 78.79 ?  608 ASN B CA    1 
ATOM   10431 C  C     . ASN B 1 608 ? 148.372 119.271 157.291 1.00 78.89 ?  608 ASN B C     1 
ATOM   10432 O  O     . ASN B 1 608 ? 148.345 118.081 157.621 1.00 79.13 ?  608 ASN B O     1 
ATOM   10433 C  CB    . ASN B 1 608 ? 150.060 118.997 155.465 1.00 78.58 ?  608 ASN B CB    1 
ATOM   10434 C  CG    . ASN B 1 608 ? 150.258 118.948 153.963 1.00 79.08 ?  608 ASN B CG    1 
ATOM   10435 O  OD1   . ASN B 1 608 ? 149.311 119.122 153.195 1.00 78.71 ?  608 ASN B OD1   1 
ATOM   10436 N  ND2   . ASN B 1 608 ? 151.492 118.708 153.535 1.00 78.97 ?  608 ASN B ND2   1 
ATOM   10437 N  N     . SER B 1 609 ? 148.093 120.252 158.143 1.00 72.52 ?  609 SER B N     1 
ATOM   10438 C  CA    . SER B 1 609 ? 147.771 120.016 159.541 1.00 71.89 ?  609 SER B CA    1 
ATOM   10439 C  C     . SER B 1 609 ? 146.281 120.220 159.783 1.00 70.62 ?  609 SER B C     1 
ATOM   10440 O  O     . SER B 1 609 ? 145.575 120.841 158.986 1.00 71.68 ?  609 SER B O     1 
ATOM   10441 C  CB    . SER B 1 609 ? 148.580 120.941 160.454 1.00 69.93 ?  609 SER B CB    1 
ATOM   10442 O  OG    . SER B 1 609 ? 148.189 122.293 160.281 1.00 69.72 ?  609 SER B OG    1 
ATOM   10443 N  N     . LYS B 1 610 ? 145.809 119.678 160.901 1.00 61.32 ?  610 LYS B N     1 
ATOM   10444 C  CA    . LYS B 1 610 ? 144.429 119.838 161.331 1.00 61.43 ?  610 LYS B CA    1 
ATOM   10445 C  C     . LYS B 1 610 ? 144.405 120.462 162.719 1.00 61.84 ?  610 LYS B C     1 
ATOM   10446 O  O     . LYS B 1 610 ? 145.241 120.141 163.570 1.00 59.72 ?  610 LYS B O     1 
ATOM   10447 C  CB    . LYS B 1 610 ? 143.685 118.496 161.323 1.00 62.88 ?  610 LYS B CB    1 
ATOM   10448 C  CG    . LYS B 1 610 ? 144.178 117.484 162.345 1.00 61.41 ?  610 LYS B CG    1 
ATOM   10449 C  CD    . LYS B 1 610 ? 143.228 116.301 162.469 1.00 61.32 ?  610 LYS B CD    1 
ATOM   10450 C  CE    . LYS B 1 610 ? 142.472 116.039 161.174 1.00 61.36 ?  610 LYS B CE    1 
ATOM   10451 N  NZ    . LYS B 1 610 ? 141.493 114.927 161.314 1.00 60.10 1  610 LYS B NZ    1 
ATOM   10452 N  N     . THR B 1 611 ? 143.462 121.375 162.932 1.00 60.71 ?  611 THR B N     1 
ATOM   10453 C  CA    . THR B 1 611 ? 143.331 122.095 164.187 1.00 57.67 ?  611 THR B CA    1 
ATOM   10454 C  C     . THR B 1 611 ? 141.902 121.975 164.689 1.00 54.85 ?  611 THR B C     1 
ATOM   10455 O  O     . THR B 1 611 ? 140.961 121.838 163.903 1.00 57.03 ?  611 THR B O     1 
ATOM   10456 C  CB    . THR B 1 611 ? 143.695 123.578 164.032 1.00 58.17 ?  611 THR B CB    1 
ATOM   10457 O  OG1   . THR B 1 611 ? 142.840 124.176 163.052 1.00 58.82 ?  611 THR B OG1   1 
ATOM   10458 C  CG2   . THR B 1 611 ? 145.139 123.733 163.595 1.00 55.74 ?  611 THR B CG2   1 
ATOM   10459 N  N     . TYR B 1 612 ? 141.746 122.015 166.008 1.00 49.86 ?  612 TYR B N     1 
ATOM   10460 C  CA    . TYR B 1 612 ? 140.435 121.961 166.639 1.00 50.17 ?  612 TYR B CA    1 
ATOM   10461 C  C     . TYR B 1 612 ? 140.203 123.251 167.408 1.00 50.25 ?  612 TYR B C     1 
ATOM   10462 O  O     . TYR B 1 612 ? 140.993 123.605 168.291 1.00 51.80 ?  612 TYR B O     1 
ATOM   10463 C  CB    . TYR B 1 612 ? 140.297 120.748 167.563 1.00 52.03 ?  612 TYR B CB    1 
ATOM   10464 C  CG    . TYR B 1 612 ? 140.646 119.424 166.917 1.00 54.51 ?  612 TYR B CG    1 
ATOM   10465 C  CD1   . TYR B 1 612 ? 141.966 119.060 166.685 1.00 53.62 ?  612 TYR B CD1   1 
ATOM   10466 C  CD2   . TYR B 1 612 ? 139.646 118.553 166.508 1.00 54.03 ?  612 TYR B CD2   1 
ATOM   10467 C  CE1   . TYR B 1 612 ? 142.279 117.854 166.090 1.00 55.62 ?  612 TYR B CE1   1 
ATOM   10468 C  CE2   . TYR B 1 612 ? 139.949 117.346 165.913 1.00 54.22 ?  612 TYR B CE2   1 
ATOM   10469 C  CZ    . TYR B 1 612 ? 141.266 117.002 165.705 1.00 55.61 ?  612 TYR B CZ    1 
ATOM   10470 O  OH    . TYR B 1 612 ? 141.568 115.800 165.111 1.00 55.81 ?  612 TYR B OH    1 
ATOM   10471 N  N     . TYR B 1 613 ? 139.125 123.948 167.070 1.00 42.10 ?  613 TYR B N     1 
ATOM   10472 C  CA    . TYR B 1 613 ? 138.724 125.165 167.761 1.00 38.05 ?  613 TYR B CA    1 
ATOM   10473 C  C     . TYR B 1 613 ? 137.505 124.877 168.620 1.00 38.01 ?  613 TYR B C     1 
ATOM   10474 O  O     . TYR B 1 613 ? 136.416 124.629 168.074 1.00 36.70 ?  613 TYR B O     1 
ATOM   10475 C  CB    . TYR B 1 613 ? 138.420 126.283 166.762 1.00 38.76 ?  613 TYR B CB    1 
ATOM   10476 C  CG    . TYR B 1 613 ? 137.912 127.554 167.401 1.00 35.14 ?  613 TYR B CG    1 
ATOM   10477 C  CD1   . TYR B 1 613 ? 138.679 128.242 168.331 1.00 36.58 ?  613 TYR B CD1   1 
ATOM   10478 C  CD2   . TYR B 1 613 ? 136.666 128.070 167.073 1.00 36.96 ?  613 TYR B CD2   1 
ATOM   10479 C  CE1   . TYR B 1 613 ? 138.222 129.405 168.914 1.00 38.78 ?  613 TYR B CE1   1 
ATOM   10480 C  CE2   . TYR B 1 613 ? 136.199 129.233 167.652 1.00 39.76 ?  613 TYR B CE2   1 
ATOM   10481 C  CZ    . TYR B 1 613 ? 136.982 129.896 168.572 1.00 41.14 ?  613 TYR B CZ    1 
ATOM   10482 O  OH    . TYR B 1 613 ? 136.525 131.056 169.152 1.00 40.64 ?  613 TYR B OH    1 
ATOM   10483 N  N     . PRO B 1 614 ? 137.639 124.835 169.942 1.00 35.86 ?  614 PRO B N     1 
ATOM   10484 C  CA    . PRO B 1 614 ? 136.452 124.776 170.797 1.00 34.87 ?  614 PRO B CA    1 
ATOM   10485 C  C     . PRO B 1 614 ? 135.732 126.113 170.809 1.00 38.36 ?  614 PRO B C     1 
ATOM   10486 O  O     . PRO B 1 614 ? 136.332 127.170 170.598 1.00 39.87 ?  614 PRO B O     1 
ATOM   10487 C  CB    . PRO B 1 614 ? 137.021 124.437 172.182 1.00 33.93 ?  614 PRO B CB    1 
ATOM   10488 C  CG    . PRO B 1 614 ? 138.446 124.019 171.944 1.00 36.88 ?  614 PRO B CG    1 
ATOM   10489 C  CD    . PRO B 1 614 ? 138.884 124.744 170.718 1.00 35.12 ?  614 PRO B CD    1 
ATOM   10490 N  N     . MET B 1 615 ? 134.429 126.056 171.055 1.00 32.85 ?  615 MET B N     1 
ATOM   10491 C  CA    . MET B 1 615 ? 133.657 127.281 171.168 1.00 29.77 ?  615 MET B CA    1 
ATOM   10492 C  C     . MET B 1 615 ? 134.144 128.089 172.367 1.00 36.44 ?  615 MET B C     1 
ATOM   10493 O  O     . MET B 1 615 ? 134.575 127.511 173.372 1.00 40.66 ?  615 MET B O     1 
ATOM   10494 C  CB    . MET B 1 615 ? 132.167 126.966 171.301 1.00 30.91 ?  615 MET B CB    1 
ATOM   10495 C  CG    . MET B 1 615 ? 131.467 126.643 169.984 1.00 35.52 ?  615 MET B CG    1 
ATOM   10496 S  SD    . MET B 1 615 ? 132.102 127.531 168.542 1.00 41.17 ?  615 MET B SD    1 
ATOM   10497 C  CE    . MET B 1 615 ? 133.234 126.338 167.830 1.00 34.86 ?  615 MET B CE    1 
ATOM   10498 N  N     . PRO B 1 616 ? 134.111 129.420 172.292 1.00 37.15 ?  616 PRO B N     1 
ATOM   10499 C  CA    . PRO B 1 616 ? 134.681 130.245 173.370 1.00 33.00 ?  616 PRO B CA    1 
ATOM   10500 C  C     . PRO B 1 616 ? 133.991 129.992 174.699 1.00 35.01 ?  616 PRO B C     1 
ATOM   10501 O  O     . PRO B 1 616 ? 132.776 130.150 174.831 1.00 37.07 ?  616 PRO B O     1 
ATOM   10502 C  CB    . PRO B 1 616 ? 134.449 131.676 172.874 1.00 34.26 ?  616 PRO B CB    1 
ATOM   10503 C  CG    . PRO B 1 616 ? 134.267 131.546 171.398 1.00 33.99 ?  616 PRO B CG    1 
ATOM   10504 C  CD    . PRO B 1 616 ? 133.592 130.238 171.184 1.00 33.29 ?  616 PRO B CD    1 
ATOM   10505 N  N     . GLY B 1 617 ? 134.782 129.605 175.696 1.00 35.39 ?  617 GLY B N     1 
ATOM   10506 C  CA    . GLY B 1 617 ? 134.251 129.305 177.007 1.00 33.60 ?  617 GLY B CA    1 
ATOM   10507 C  C     . GLY B 1 617 ? 133.686 127.915 177.169 1.00 38.16 ?  617 GLY B C     1 
ATOM   10508 O  O     . GLY B 1 617 ? 133.091 127.627 178.214 1.00 41.04 ?  617 GLY B O     1 
ATOM   10509 N  N     . LEU B 1 618 ? 133.843 127.047 176.172 1.00 38.93 ?  618 LEU B N     1 
ATOM   10510 C  CA    . LEU B 1 618 ? 133.350 125.682 176.288 1.00 33.74 ?  618 LEU B CA    1 
ATOM   10511 C  C     . LEU B 1 618 ? 134.103 124.938 177.383 1.00 36.51 ?  618 LEU B C     1 
ATOM   10512 O  O     . LEU B 1 618 ? 135.330 125.023 177.486 1.00 38.95 ?  618 LEU B O     1 
ATOM   10513 C  CB    . LEU B 1 618 ? 133.494 124.950 174.952 1.00 30.87 ?  618 LEU B CB    1 
ATOM   10514 C  CG    . LEU B 1 618 ? 133.000 123.503 174.896 1.00 35.47 ?  618 LEU B CG    1 
ATOM   10515 C  CD1   . LEU B 1 618 ? 131.503 123.431 175.153 1.00 36.01 ?  618 LEU B CD1   1 
ATOM   10516 C  CD2   . LEU B 1 618 ? 133.348 122.873 173.559 1.00 35.81 ?  618 LEU B CD2   1 
ATOM   10517 N  N     . ALA B 1 619 ? 133.360 124.205 178.202 1.00 42.84 ?  619 ALA B N     1 
ATOM   10518 C  CA    . ALA B 1 619 ? 133.928 123.464 179.320 1.00 42.21 ?  619 ALA B CA    1 
ATOM   10519 C  C     . ALA B 1 619 ? 132.946 122.363 179.704 1.00 43.92 ?  619 ALA B C     1 
ATOM   10520 O  O     . ALA B 1 619 ? 131.944 122.136 179.019 1.00 49.67 ?  619 ALA B O     1 
ATOM   10521 C  CB    . ALA B 1 619 ? 134.240 124.399 180.493 1.00 41.95 ?  619 ALA B CB    1 
ATOM   10522 N  N     . SER B 1 620 ? 133.240 121.671 180.806 1.00 47.85 ?  620 SER B N     1 
ATOM   10523 C  CA    . SER B 1 620 ? 132.367 120.592 181.255 1.00 49.40 ?  620 SER B CA    1 
ATOM   10524 C  C     . SER B 1 620 ? 131.046 121.129 181.793 1.00 49.40 ?  620 SER B C     1 
ATOM   10525 O  O     . SER B 1 620 ? 129.985 120.548 181.542 1.00 51.23 ?  620 SER B O     1 
ATOM   10526 C  CB    . SER B 1 620 ? 133.076 119.753 182.317 1.00 50.49 ?  620 SER B CB    1 
ATOM   10527 O  OG    . SER B 1 620 ? 134.464 119.658 182.049 1.00 53.13 ?  620 SER B OG    1 
ATOM   10528 N  N     . ASN B 1 621 ? 131.089 122.237 182.535 1.00 47.53 ?  621 ASN B N     1 
ATOM   10529 C  CA    . ASN B 1 621 ? 129.882 122.754 183.169 1.00 49.06 ?  621 ASN B CA    1 
ATOM   10530 C  C     . ASN B 1 621 ? 128.930 123.409 182.178 1.00 50.49 ?  621 ASN B C     1 
ATOM   10531 O  O     . ASN B 1 621 ? 127.726 123.473 182.449 1.00 51.11 ?  621 ASN B O     1 
ATOM   10532 C  CB    . ASN B 1 621 ? 130.250 123.752 184.269 1.00 48.58 ?  621 ASN B CB    1 
ATOM   10533 C  CG    . ASN B 1 621 ? 131.162 124.854 183.774 1.00 51.79 ?  621 ASN B CG    1 
ATOM   10534 O  OD1   . ASN B 1 621 ? 131.955 124.653 182.855 1.00 54.59 ?  621 ASN B OD1   1 
ATOM   10535 N  ND2   . ASN B 1 621 ? 131.055 126.028 184.383 1.00 50.11 ?  621 ASN B ND2   1 
ATOM   10536 N  N     . ASN B 1 622 ? 129.431 123.892 181.042 1.00 42.43 ?  622 ASN B N     1 
ATOM   10537 C  CA    . ASN B 1 622 ? 128.596 124.537 180.036 1.00 42.64 ?  622 ASN B CA    1 
ATOM   10538 C  C     . ASN B 1 622 ? 128.631 123.784 178.709 1.00 45.50 ?  622 ASN B C     1 
ATOM   10539 O  O     . ASN B 1 622 ? 128.425 124.376 177.647 1.00 48.48 ?  622 ASN B O     1 
ATOM   10540 C  CB    . ASN B 1 622 ? 129.008 125.998 179.841 1.00 42.25 ?  622 ASN B CB    1 
ATOM   10541 C  CG    . ASN B 1 622 ? 130.461 126.154 179.421 1.00 43.85 ?  622 ASN B CG    1 
ATOM   10542 O  OD1   . ASN B 1 622 ? 131.142 125.179 179.106 1.00 45.91 ?  622 ASN B OD1   1 
ATOM   10543 N  ND2   . ASN B 1 622 ? 130.940 127.391 179.415 1.00 41.49 ?  622 ASN B ND2   1 
ATOM   10544 N  N     . TRP B 1 623 ? 128.903 122.478 178.757 1.00 40.13 ?  623 TRP B N     1 
ATOM   10545 C  CA    . TRP B 1 623 ? 128.929 121.687 177.530 1.00 38.16 ?  623 TRP B CA    1 
ATOM   10546 C  C     . TRP B 1 623 ? 127.548 121.611 176.891 1.00 39.87 ?  623 TRP B C     1 
ATOM   10547 O  O     . TRP B 1 623 ? 127.409 121.784 175.675 1.00 42.48 ?  623 TRP B O     1 
ATOM   10548 C  CB    . TRP B 1 623 ? 129.467 120.286 177.819 1.00 42.24 ?  623 TRP B CB    1 
ATOM   10549 C  CG    . TRP B 1 623 ? 129.394 119.354 176.645 1.00 40.48 ?  623 TRP B CG    1 
ATOM   10550 C  CD1   . TRP B 1 623 ? 128.339 118.566 176.288 1.00 39.05 ?  623 TRP B CD1   1 
ATOM   10551 C  CD2   . TRP B 1 623 ? 130.419 119.116 175.673 1.00 39.60 ?  623 TRP B CD2   1 
ATOM   10552 N  NE1   . TRP B 1 623 ? 128.643 117.852 175.156 1.00 40.20 ?  623 TRP B NE1   1 
ATOM   10553 C  CE2   . TRP B 1 623 ? 129.914 118.170 174.759 1.00 39.80 ?  623 TRP B CE2   1 
ATOM   10554 C  CE3   . TRP B 1 623 ? 131.713 119.609 175.487 1.00 40.04 ?  623 TRP B CE3   1 
ATOM   10555 C  CZ2   . TRP B 1 623 ? 130.657 117.711 173.674 1.00 39.15 ?  623 TRP B CZ2   1 
ATOM   10556 C  CZ3   . TRP B 1 623 ? 132.450 119.150 174.411 1.00 39.84 ?  623 TRP B CZ3   1 
ATOM   10557 C  CH2   . TRP B 1 623 ? 131.920 118.211 173.518 1.00 39.02 ?  623 TRP B CH2   1 
ATOM   10558 N  N     . PHE B 1 624 ? 126.514 121.354 177.692 1.00 44.42 ?  624 PHE B N     1 
ATOM   10559 C  CA    . PHE B 1 624 ? 125.167 121.215 177.158 1.00 44.06 ?  624 PHE B CA    1 
ATOM   10560 C  C     . PHE B 1 624 ? 124.467 122.547 176.941 1.00 41.51 ?  624 PHE B C     1 
ATOM   10561 O  O     . PHE B 1 624 ? 123.454 122.586 176.235 1.00 46.26 ?  624 PHE B O     1 
ATOM   10562 C  CB    . PHE B 1 624 ? 124.328 120.326 178.077 1.00 42.66 ?  624 PHE B CB    1 
ATOM   10563 C  CG    . PHE B 1 624 ? 124.749 118.885 178.066 1.00 44.84 ?  624 PHE B CG    1 
ATOM   10564 C  CD1   . PHE B 1 624 ? 124.339 118.041 177.048 1.00 42.91 ?  624 PHE B CD1   1 
ATOM   10565 C  CD2   . PHE B 1 624 ? 125.563 118.378 179.064 1.00 45.60 ?  624 PHE B CD2   1 
ATOM   10566 C  CE1   . PHE B 1 624 ? 124.728 116.716 177.029 1.00 42.49 ?  624 PHE B CE1   1 
ATOM   10567 C  CE2   . PHE B 1 624 ? 125.956 117.054 179.050 1.00 45.60 ?  624 PHE B CE2   1 
ATOM   10568 C  CZ    . PHE B 1 624 ? 125.537 116.222 178.032 1.00 45.64 ?  624 PHE B CZ    1 
ATOM   10569 N  N     . PHE B 1 625 ? 124.972 123.636 177.524 1.00 37.19 ?  625 PHE B N     1 
ATOM   10570 C  CA    . PHE B 1 625 ? 124.474 124.956 177.163 1.00 32.73 ?  625 PHE B CA    1 
ATOM   10571 C  C     . PHE B 1 625 ? 124.987 125.396 175.802 1.00 30.95 ?  625 PHE B C     1 
ATOM   10572 O  O     . PHE B 1 625 ? 124.353 126.232 175.150 1.00 33.43 ?  625 PHE B O     1 
ATOM   10573 C  CB    . PHE B 1 625 ? 124.856 125.979 178.231 1.00 29.88 ?  625 PHE B CB    1 
ATOM   10574 C  CG    . PHE B 1 625 ? 124.012 125.902 179.469 1.00 32.89 ?  625 PHE B CG    1 
ATOM   10575 C  CD1   . PHE B 1 625 ? 122.660 126.196 179.420 1.00 33.41 ?  625 PHE B CD1   1 
ATOM   10576 C  CD2   . PHE B 1 625 ? 124.568 125.532 180.683 1.00 33.39 ?  625 PHE B CD2   1 
ATOM   10577 C  CE1   . PHE B 1 625 ? 121.880 126.125 180.556 1.00 33.55 ?  625 PHE B CE1   1 
ATOM   10578 C  CE2   . PHE B 1 625 ? 123.792 125.459 181.821 1.00 35.07 ?  625 PHE B CE2   1 
ATOM   10579 C  CZ    . PHE B 1 625 ? 122.445 125.757 181.758 1.00 35.94 ?  625 PHE B CZ    1 
ATOM   10580 N  N     . TYR B 1 626 ? 126.115 124.848 175.358 1.00 29.75 ?  626 TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 626 ? 126.618 125.070 174.004 1.00 29.27 ?  626 TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 626 ? 125.994 124.084 173.024 1.00 32.33 ?  626 TYR B C     1 
ATOM   10583 O  O     . TYR B 1 626 ? 126.682 123.387 172.281 1.00 35.80 ?  626 TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 626 ? 128.138 124.972 173.990 1.00 31.54 ?  626 TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 626 ? 128.829 126.310 174.061 1.00 29.75 ?  626 TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 626 ? 128.756 127.205 173.004 1.00 33.90 ?  626 TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 626 ? 129.555 126.679 175.185 1.00 28.57 ?  626 TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 626 ? 129.384 128.430 173.062 1.00 30.73 ?  626 TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 626 ? 130.187 127.903 175.253 1.00 31.89 ?  626 TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 626 ? 130.099 128.773 174.187 1.00 33.56 ?  626 TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 626 ? 130.725 129.994 174.246 1.00 36.80 ?  626 TYR B OH    1 
ATOM   10592 N  N     . LYS B 1 627 ? 124.665 124.024 173.032 1.00 33.36 ?  627 LYS B N     1 
ATOM   10593 C  CA    . LYS B 1 627 ? 123.946 123.106 172.161 1.00 31.32 ?  627 LYS B CA    1 
ATOM   10594 C  C     . LYS B 1 627 ? 124.198 123.451 170.699 1.00 31.42 ?  627 LYS B C     1 
ATOM   10595 O  O     . LYS B 1 627 ? 124.170 124.620 170.306 1.00 34.42 ?  627 LYS B O     1 
ATOM   10596 C  CB    . LYS B 1 627 ? 122.451 123.162 172.472 1.00 32.93 ?  627 LYS B CB    1 
ATOM   10597 C  CG    . LYS B 1 627 ? 121.608 122.141 171.735 1.00 33.39 ?  627 LYS B CG    1 
ATOM   10598 C  CD    . LYS B 1 627 ? 120.173 122.182 172.226 1.00 30.93 ?  627 LYS B CD    1 
ATOM   10599 C  CE    . LYS B 1 627 ? 119.291 121.217 171.458 1.00 36.51 ?  627 LYS B CE    1 
ATOM   10600 N  NZ    . LYS B 1 627 ? 117.866 121.334 171.870 1.00 36.73 1  627 LYS B NZ    1 
ATOM   10601 N  N     . GLU B 1 628 ? 124.455 122.424 169.896 1.00 33.49 ?  628 GLU B N     1 
ATOM   10602 C  CA    . GLU B 1 628 ? 124.709 122.641 168.480 1.00 33.47 ?  628 GLU B CA    1 
ATOM   10603 C  C     . GLU B 1 628 ? 123.435 123.079 167.770 1.00 35.41 ?  628 GLU B C     1 
ATOM   10604 O  O     . GLU B 1 628 ? 122.324 122.678 168.129 1.00 39.24 ?  628 GLU B O     1 
ATOM   10605 C  CB    . GLU B 1 628 ? 125.272 121.374 167.838 1.00 35.21 ?  628 GLU B CB    1 
ATOM   10606 C  CG    . GLU B 1 628 ? 126.696 121.063 168.260 1.00 33.53 ?  628 GLU B CG    1 
ATOM   10607 C  CD    . GLU B 1 628 ? 127.274 119.865 167.537 1.00 41.02 ?  628 GLU B CD    1 
ATOM   10608 O  OE1   . GLU B 1 628 ? 126.660 119.413 166.547 1.00 41.66 ?  628 GLU B OE1   1 
ATOM   10609 O  OE2   . GLU B 1 628 ? 128.344 119.377 167.956 1.00 38.10 -1 628 GLU B OE2   1 
ATOM   10610 N  N     . ALA B 1 629 ? 123.610 123.922 166.750 1.00 33.48 ?  629 ALA B N     1 
ATOM   10611 C  CA    . ALA B 1 629 ? 122.467 124.514 166.063 1.00 28.50 ?  629 ALA B CA    1 
ATOM   10612 C  C     . ALA B 1 629 ? 121.612 123.456 165.377 1.00 33.82 ?  629 ALA B C     1 
ATOM   10613 O  O     . ALA B 1 629 ? 120.380 123.555 165.368 1.00 41.85 ?  629 ALA B O     1 
ATOM   10614 C  CB    . ALA B 1 629 ? 122.949 125.550 165.051 1.00 29.76 ?  629 ALA B CB    1 
ATOM   10615 N  N     . TYR B 1 630 ? 122.247 122.441 164.787 1.00 39.39 ?  630 TYR B N     1 
ATOM   10616 C  CA    . TYR B 1 630 ? 121.494 121.407 164.085 1.00 37.06 ?  630 TYR B CA    1 
ATOM   10617 C  C     . TYR B 1 630 ? 120.607 120.612 165.032 1.00 39.49 ?  630 TYR B C     1 
ATOM   10618 O  O     . TYR B 1 630 ? 119.537 120.145 164.629 1.00 42.63 ?  630 TYR B O     1 
ATOM   10619 C  CB    . TYR B 1 630 ? 122.451 120.477 163.341 1.00 34.90 ?  630 TYR B CB    1 
ATOM   10620 C  CG    . TYR B 1 630 ? 123.335 121.192 162.347 1.00 37.14 ?  630 TYR B CG    1 
ATOM   10621 C  CD1   . TYR B 1 630 ? 122.849 121.565 161.101 1.00 33.86 ?  630 TYR B CD1   1 
ATOM   10622 C  CD2   . TYR B 1 630 ? 124.653 121.494 162.654 1.00 37.66 ?  630 TYR B CD2   1 
ATOM   10623 C  CE1   . TYR B 1 630 ? 123.652 122.220 160.190 1.00 37.39 ?  630 TYR B CE1   1 
ATOM   10624 C  CE2   . TYR B 1 630 ? 125.465 122.147 161.748 1.00 36.27 ?  630 TYR B CE2   1 
ATOM   10625 C  CZ    . TYR B 1 630 ? 124.959 122.508 160.518 1.00 39.87 ?  630 TYR B CZ    1 
ATOM   10626 O  OH    . TYR B 1 630 ? 125.761 123.159 159.611 1.00 43.03 ?  630 TYR B OH    1 
ATOM   10627 N  N     . ASP B 1 631 ? 121.025 120.452 166.287 1.00 36.75 ?  631 ASP B N     1 
ATOM   10628 C  CA    . ASP B 1 631 ? 120.218 119.750 167.276 1.00 32.70 ?  631 ASP B CA    1 
ATOM   10629 C  C     . ASP B 1 631 ? 119.091 120.607 167.837 1.00 37.19 ?  631 ASP B C     1 
ATOM   10630 O  O     . ASP B 1 631 ? 118.249 120.087 168.575 1.00 39.80 ?  631 ASP B O     1 
ATOM   10631 C  CB    . ASP B 1 631 ? 121.104 119.261 168.424 1.00 34.41 ?  631 ASP B CB    1 
ATOM   10632 C  CG    . ASP B 1 631 ? 122.210 118.338 167.953 1.00 41.11 ?  631 ASP B CG    1 
ATOM   10633 O  OD1   . ASP B 1 631 ? 121.941 117.471 167.096 1.00 43.19 ?  631 ASP B OD1   1 
ATOM   10634 O  OD2   . ASP B 1 631 ? 123.352 118.480 168.440 1.00 42.19 -1 631 ASP B OD2   1 
ATOM   10635 N  N     . MET B 1 632 ? 119.053 121.892 167.503 1.00 36.47 ?  632 MET B N     1 
ATOM   10636 C  CA    . MET B 1 632 ? 118.079 122.814 168.064 1.00 32.57 ?  632 MET B CA    1 
ATOM   10637 C  C     . MET B 1 632 ? 116.798 122.824 167.243 1.00 34.91 ?  632 MET B C     1 
ATOM   10638 O  O     . MET B 1 632 ? 116.795 122.510 166.050 1.00 34.50 ?  632 MET B O     1 
ATOM   10639 C  CB    . MET B 1 632 ? 118.651 124.230 168.123 1.00 31.54 ?  632 MET B CB    1 
ATOM   10640 C  CG    . MET B 1 632 ? 119.794 124.397 169.097 1.00 36.57 ?  632 MET B CG    1 
ATOM   10641 S  SD    . MET B 1 632 ? 120.410 126.085 169.135 1.00 39.71 ?  632 MET B SD    1 
ATOM   10642 C  CE    . MET B 1 632 ? 121.249 126.089 170.712 1.00 30.53 ?  632 MET B CE    1 
ATOM   10643 N  N     . ASP B 1 633 ? 115.703 123.194 167.900 1.00 33.36 ?  633 ASP B N     1 
ATOM   10644 C  CA    . ASP B 1 633 ? 114.445 123.422 167.205 1.00 26.12 ?  633 ASP B CA    1 
ATOM   10645 C  C     . ASP B 1 633 ? 114.538 124.716 166.409 1.00 31.27 ?  633 ASP B C     1 
ATOM   10646 O  O     . ASP B 1 633 ? 114.762 125.788 166.982 1.00 37.33 ?  633 ASP B O     1 
ATOM   10647 C  CB    . ASP B 1 633 ? 113.293 123.486 168.205 1.00 28.86 ?  633 ASP B CB    1 
ATOM   10648 C  CG    . ASP B 1 633 ? 111.935 123.481 167.534 1.00 36.59 ?  633 ASP B CG    1 
ATOM   10649 O  OD1   . ASP B 1 633 ? 111.874 123.276 166.304 1.00 39.85 ?  633 ASP B OD1   1 
ATOM   10650 O  OD2   . ASP B 1 633 ? 110.924 123.683 168.238 1.00 35.97 -1 633 ASP B OD2   1 
ATOM   10651 N  N     . MET B 1 634 ? 114.375 124.620 165.089 1.00 28.97 ?  634 MET B N     1 
ATOM   10652 C  CA    . MET B 1 634 ? 114.464 125.807 164.249 1.00 19.79 ?  634 MET B CA    1 
ATOM   10653 C  C     . MET B 1 634 ? 113.353 126.806 164.537 1.00 23.83 ?  634 MET B C     1 
ATOM   10654 O  O     . MET B 1 634 ? 113.518 127.993 164.244 1.00 30.66 ?  634 MET B O     1 
ATOM   10655 C  CB    . MET B 1 634 ? 114.439 125.414 162.771 1.00 24.77 ?  634 MET B CB    1 
ATOM   10656 C  CG    . MET B 1 634 ? 115.814 125.299 162.122 1.00 26.45 ?  634 MET B CG    1 
ATOM   10657 S  SD    . MET B 1 634 ? 116.982 126.563 162.662 1.00 40.68 ?  634 MET B SD    1 
ATOM   10658 C  CE    . MET B 1 634 ? 118.049 125.611 163.741 1.00 27.98 ?  634 MET B CE    1 
ATOM   10659 N  N     . PHE B 1 635 ? 112.232 126.357 165.105 1.00 22.81 ?  635 PHE B N     1 
ATOM   10660 C  CA    . PHE B 1 635 ? 111.159 127.286 165.449 1.00 23.82 ?  635 PHE B CA    1 
ATOM   10661 C  C     . PHE B 1 635 ? 111.577 128.215 166.582 1.00 20.23 ?  635 PHE B C     1 
ATOM   10662 O  O     . PHE B 1 635 ? 111.276 129.414 166.555 1.00 23.00 ?  635 PHE B O     1 
ATOM   10663 C  CB    . PHE B 1 635 ? 109.897 126.510 165.823 1.00 22.81 ?  635 PHE B CB    1 
ATOM   10664 C  CG    . PHE B 1 635 ? 109.004 126.209 164.654 1.00 23.55 ?  635 PHE B CG    1 
ATOM   10665 C  CD1   . PHE B 1 635 ? 109.540 125.784 163.449 1.00 25.61 ?  635 PHE B CD1   1 
ATOM   10666 C  CD2   . PHE B 1 635 ? 107.632 126.350 164.758 1.00 24.32 ?  635 PHE B CD2   1 
ATOM   10667 C  CE1   . PHE B 1 635 ? 108.725 125.507 162.370 1.00 22.74 ?  635 PHE B CE1   1 
ATOM   10668 C  CE2   . PHE B 1 635 ? 106.811 126.074 163.682 1.00 25.49 ?  635 PHE B CE2   1 
ATOM   10669 C  CZ    . PHE B 1 635 ? 107.358 125.651 162.487 1.00 23.57 ?  635 PHE B CZ    1 
ATOM   10670 N  N     . LYS B 1 636 ? 112.288 127.689 167.580 1.00 26.75 ?  636 LYS B N     1 
ATOM   10671 C  CA    . LYS B 1 636 ? 112.762 128.530 168.671 1.00 29.79 ?  636 LYS B CA    1 
ATOM   10672 C  C     . LYS B 1 636 ? 113.906 129.438 168.230 1.00 26.40 ?  636 LYS B C     1 
ATOM   10673 O  O     . LYS B 1 636 ? 114.028 130.564 168.729 1.00 29.33 ?  636 LYS B O     1 
ATOM   10674 C  CB    . LYS B 1 636 ? 113.184 127.659 169.852 1.00 27.22 ?  636 LYS B CB    1 
ATOM   10675 C  CG    . LYS B 1 636 ? 112.040 126.838 170.427 1.00 27.67 ?  636 LYS B CG    1 
ATOM   10676 C  CD    . LYS B 1 636 ? 112.433 126.148 171.719 1.00 33.78 ?  636 LYS B CD    1 
ATOM   10677 C  CE    . LYS B 1 636 ? 111.325 125.237 172.216 1.00 33.82 ?  636 LYS B CE    1 
ATOM   10678 N  NZ    . LYS B 1 636 ? 111.758 124.425 173.386 1.00 35.15 1  636 LYS B NZ    1 
ATOM   10679 N  N     . VAL B 1 637 ? 114.733 128.982 167.289 1.00 22.60 ?  637 VAL B N     1 
ATOM   10680 C  CA    . VAL B 1 637 ? 115.730 129.869 166.700 1.00 19.51 ?  637 VAL B CA    1 
ATOM   10681 C  C     . VAL B 1 637 ? 115.048 130.989 165.923 1.00 25.77 ?  637 VAL B C     1 
ATOM   10682 O  O     . VAL B 1 637 ? 115.492 132.142 165.954 1.00 26.46 ?  637 VAL B O     1 
ATOM   10683 C  CB    . VAL B 1 637 ? 116.703 129.069 165.816 1.00 19.65 ?  637 VAL B CB    1 
ATOM   10684 C  CG1   . VAL B 1 637 ? 117.845 129.953 165.348 1.00 20.23 ?  637 VAL B CG1   1 
ATOM   10685 C  CG2   . VAL B 1 637 ? 117.239 127.867 166.575 1.00 24.93 ?  637 VAL B CG2   1 
ATOM   10686 N  N     . VAL B 1 638 ? 113.958 130.670 165.222 1.00 20.68 ?  638 VAL B N     1 
ATOM   10687 C  CA    . VAL B 1 638 ? 113.175 131.699 164.541 1.00 20.02 ?  638 VAL B CA    1 
ATOM   10688 C  C     . VAL B 1 638 ? 112.602 132.684 165.551 1.00 20.80 ?  638 VAL B C     1 
ATOM   10689 O  O     . VAL B 1 638 ? 112.571 133.896 165.311 1.00 28.07 ?  638 VAL B O     1 
ATOM   10690 C  CB    . VAL B 1 638 ? 112.061 131.052 163.692 1.00 22.27 ?  638 VAL B CB    1 
ATOM   10691 C  CG1   . VAL B 1 638 ? 111.000 132.076 163.330 1.00 16.86 ?  638 VAL B CG1   1 
ATOM   10692 C  CG2   . VAL B 1 638 ? 112.637 130.425 162.437 1.00 18.92 ?  638 VAL B CG2   1 
ATOM   10693 N  N     . ASP B 1 639 ? 112.127 132.176 166.690 1.00 21.40 ?  639 ASP B N     1 
ATOM   10694 C  CA    . ASP B 1 639 ? 111.618 133.052 167.740 1.00 16.39 ?  639 ASP B CA    1 
ATOM   10695 C  C     . ASP B 1 639 ? 112.702 133.997 168.245 1.00 22.64 ?  639 ASP B C     1 
ATOM   10696 O  O     . ASP B 1 639 ? 112.459 135.197 168.420 1.00 31.87 ?  639 ASP B O     1 
ATOM   10697 C  CB    . ASP B 1 639 ? 111.060 132.219 168.892 1.00 20.16 ?  639 ASP B CB    1 
ATOM   10698 C  CG    . ASP B 1 639 ? 109.692 131.653 168.593 1.00 30.99 ?  639 ASP B CG    1 
ATOM   10699 O  OD1   . ASP B 1 639 ? 108.894 132.346 167.927 1.00 30.17 ?  639 ASP B OD1   1 
ATOM   10700 O  OD2   . ASP B 1 639 ? 109.410 130.516 169.025 1.00 33.70 -1 639 ASP B OD2   1 
ATOM   10701 N  N     . MET B 1 640 ? 113.907 133.472 168.478 1.00 20.10 ?  640 MET B N     1 
ATOM   10702 C  CA    . MET B 1 640 ? 115.024 134.319 168.890 1.00 16.85 ?  640 MET B CA    1 
ATOM   10703 C  C     . MET B 1 640 ? 115.337 135.377 167.841 1.00 18.80 ?  640 MET B C     1 
ATOM   10704 O  O     . MET B 1 640 ? 115.549 136.553 168.167 1.00 24.56 ?  640 MET B O     1 
ATOM   10705 C  CB    . MET B 1 640 ? 116.262 133.468 169.159 1.00 18.97 ?  640 MET B CB    1 
ATOM   10706 C  CG    . MET B 1 640 ? 117.470 134.295 169.567 1.00 23.29 ?  640 MET B CG    1 
ATOM   10707 S  SD    . MET B 1 640 ? 117.444 134.839 171.279 1.00 26.94 ?  640 MET B SD    1 
ATOM   10708 C  CE    . MET B 1 640 ? 118.358 133.509 172.037 1.00 20.08 ?  640 MET B CE    1 
ATOM   10709 N  N     . ILE B 1 641 ? 115.389 134.973 166.572 1.00 22.96 ?  641 ILE B N     1 
ATOM   10710 C  CA    . ILE B 1 641 ? 115.771 135.909 165.524 1.00 18.61 ?  641 ILE B CA    1 
ATOM   10711 C  C     . ILE B 1 641 ? 114.705 136.982 165.352 1.00 17.77 ?  641 ILE B C     1 
ATOM   10712 O  O     . ILE B 1 641 ? 115.022 138.144 165.102 1.00 25.68 ?  641 ILE B O     1 
ATOM   10713 C  CB    . ILE B 1 641 ? 116.062 135.164 164.207 1.00 23.86 ?  641 ILE B CB    1 
ATOM   10714 C  CG1   . ILE B 1 641 ? 117.222 134.187 164.401 1.00 22.05 ?  641 ILE B CG1   1 
ATOM   10715 C  CG2   . ILE B 1 641 ? 116.425 136.144 163.108 1.00 13.33 ?  641 ILE B CG2   1 
ATOM   10716 C  CD1   . ILE B 1 641 ? 118.364 134.746 165.219 1.00 20.77 ?  641 ILE B CD1   1 
ATOM   10717 N  N     . ALA B 1 642 ? 113.430 136.619 165.507 1.00 9.77  ?  642 ALA B N     1 
ATOM   10718 C  CA    . ALA B 1 642 ? 112.362 137.614 165.448 1.00 17.35 ?  642 ALA B CA    1 
ATOM   10719 C  C     . ALA B 1 642 ? 112.426 138.567 166.635 1.00 19.47 ?  642 ALA B C     1 
ATOM   10720 O  O     . ALA B 1 642 ? 112.197 139.778 166.486 1.00 29.13 ?  642 ALA B O     1 
ATOM   10721 C  CB    . ALA B 1 642 ? 111.002 136.921 165.389 1.00 23.44 ?  642 ALA B CB    1 
ATOM   10722 N  N     . THR B 1 643 ? 112.735 138.039 167.822 1.00 13.83 ?  643 THR B N     1 
ATOM   10723 C  CA    . THR B 1 643 ? 112.886 138.888 168.998 1.00 15.50 ?  643 THR B CA    1 
ATOM   10724 C  C     . THR B 1 643 ? 114.006 139.901 168.802 1.00 18.38 ?  643 THR B C     1 
ATOM   10725 O  O     . THR B 1 643 ? 113.864 141.074 169.165 1.00 22.78 ?  643 THR B O     1 
ATOM   10726 C  CB    . THR B 1 643 ? 113.152 138.026 170.232 1.00 18.85 ?  643 THR B CB    1 
ATOM   10727 O  OG1   . THR B 1 643 ? 112.072 137.104 170.416 1.00 23.42 ?  643 THR B OG1   1 
ATOM   10728 C  CG2   . THR B 1 643 ? 113.286 138.890 171.470 1.00 17.01 ?  643 THR B CG2   1 
ATOM   10729 N  N     . ILE B 1 644 ? 115.129 139.466 168.233 1.00 16.84 ?  644 ILE B N     1 
ATOM   10730 C  CA    . ILE B 1 644 ? 116.209 140.401 167.935 1.00 12.86 ?  644 ILE B CA    1 
ATOM   10731 C  C     . ILE B 1 644 ? 115.799 141.358 166.820 1.00 16.93 ?  644 ILE B C     1 
ATOM   10732 O  O     . ILE B 1 644 ? 116.103 142.556 166.867 1.00 23.05 ?  644 ILE B O     1 
ATOM   10733 C  CB    . ILE B 1 644 ? 117.496 139.635 167.579 1.00 14.99 ?  644 ILE B CB    1 
ATOM   10734 C  CG1   . ILE B 1 644 ? 117.898 138.705 168.722 1.00 15.83 ?  644 ILE B CG1   1 
ATOM   10735 C  CG2   . ILE B 1 644 ? 118.615 140.604 167.263 1.00 10.19 ?  644 ILE B CG2   1 
ATOM   10736 C  CD1   . ILE B 1 644 ? 118.952 137.697 168.336 1.00 18.65 ?  644 ILE B CD1   1 
ATOM   10737 N  N     . GLN B 1 645 ? 115.090 140.847 165.811 1.00 7.72  ?  645 GLN B N     1 
ATOM   10738 C  CA    . GLN B 1 645 ? 114.758 141.618 164.622 1.00 14.27 ?  645 GLN B CA    1 
ATOM   10739 C  C     . GLN B 1 645 ? 113.808 142.761 164.937 1.00 20.95 ?  645 GLN B C     1 
ATOM   10740 O  O     . GLN B 1 645 ? 113.837 143.794 164.258 1.00 28.01 ?  645 GLN B O     1 
ATOM   10741 C  CB    . GLN B 1 645 ? 114.143 140.693 163.572 1.00 12.79 ?  645 GLN B CB    1 
ATOM   10742 C  CG    . GLN B 1 645 ? 113.804 141.361 162.258 1.00 10.57 ?  645 GLN B CG    1 
ATOM   10743 C  CD    . GLN B 1 645 ? 115.011 141.493 161.361 1.00 15.11 ?  645 GLN B CD    1 
ATOM   10744 O  OE1   . GLN B 1 645 ? 115.703 142.506 161.386 1.00 8.69  ?  645 GLN B OE1   1 
ATOM   10745 N  NE2   . GLN B 1 645 ? 115.271 140.468 160.560 1.00 17.69 ?  645 GLN B NE2   1 
ATOM   10746 N  N     . GLN B 1 646 ? 112.962 142.596 165.953 1.00 18.85 ?  646 GLN B N     1 
ATOM   10747 C  CA    . GLN B 1 646 ? 112.054 143.676 166.318 1.00 16.53 ?  646 GLN B CA    1 
ATOM   10748 C  C     . GLN B 1 646 ? 112.799 144.937 166.749 1.00 13.75 ?  646 GLN B C     1 
ATOM   10749 O  O     . GLN B 1 646 ? 112.215 146.024 166.721 1.00 21.39 ?  646 GLN B O     1 
ATOM   10750 C  CB    . GLN B 1 646 ? 111.102 143.210 167.419 1.00 19.98 ?  646 GLN B CB    1 
ATOM   10751 C  CG    . GLN B 1 646 ? 111.664 143.300 168.818 1.00 21.39 ?  646 GLN B CG    1 
ATOM   10752 C  CD    . GLN B 1 646 ? 110.718 142.738 169.857 1.00 27.82 ?  646 GLN B CD    1 
ATOM   10753 O  OE1   . GLN B 1 646 ? 111.020 141.742 170.513 1.00 25.23 ?  646 GLN B OE1   1 
ATOM   10754 N  NE2   . GLN B 1 646 ? 109.563 143.374 170.010 1.00 27.04 ?  646 GLN B NE2   1 
ATOM   10755 N  N     . HIS B 1 647 ? 114.074 144.823 167.121 1.00 22.19 ?  647 HIS B N     1 
ATOM   10756 C  CA    . HIS B 1 647 ? 114.883 145.970 167.510 1.00 19.27 ?  647 HIS B CA    1 
ATOM   10757 C  C     . HIS B 1 647 ? 115.949 146.332 166.485 1.00 16.97 ?  647 HIS B C     1 
ATOM   10758 O  O     . HIS B 1 647 ? 116.712 147.275 166.714 1.00 22.98 ?  647 HIS B O     1 
ATOM   10759 C  CB    . HIS B 1 647 ? 115.550 145.711 168.865 1.00 13.76 ?  647 HIS B CB    1 
ATOM   10760 C  CG    . HIS B 1 647 ? 114.591 145.322 169.944 1.00 17.51 ?  647 HIS B CG    1 
ATOM   10761 N  ND1   . HIS B 1 647 ? 113.623 146.178 170.422 1.00 13.19 ?  647 HIS B ND1   1 
ATOM   10762 C  CD2   . HIS B 1 647 ? 114.452 144.169 170.639 1.00 16.95 ?  647 HIS B CD2   1 
ATOM   10763 C  CE1   . HIS B 1 647 ? 112.928 145.568 171.364 1.00 19.01 ?  647 HIS B CE1   1 
ATOM   10764 N  NE2   . HIS B 1 647 ? 113.410 144.349 171.516 1.00 21.98 ?  647 HIS B NE2   1 
ATOM   10765 N  N     . ILE B 1 648 ? 116.024 145.617 165.366 1.00 12.68 ?  648 ILE B N     1 
ATOM   10766 C  CA    . ILE B 1 648 ? 117.009 145.870 164.321 1.00 11.44 ?  648 ILE B CA    1 
ATOM   10767 C  C     . ILE B 1 648 ? 116.283 146.458 163.120 1.00 16.81 ?  648 ILE B C     1 
ATOM   10768 O  O     . ILE B 1 648 ? 115.323 145.861 162.616 1.00 27.46 ?  648 ILE B O     1 
ATOM   10769 C  CB    . ILE B 1 648 ? 117.766 144.586 163.939 1.00 13.28 ?  648 ILE B CB    1 
ATOM   10770 C  CG1   . ILE B 1 648 ? 118.424 143.964 165.172 1.00 16.65 ?  648 ILE B CG1   1 
ATOM   10771 C  CG2   . ILE B 1 648 ? 118.809 144.872 162.876 1.00 5.40  ?  648 ILE B CG2   1 
ATOM   10772 C  CD1   . ILE B 1 648 ? 119.471 144.839 165.815 1.00 8.73  ?  648 ILE B CD1   1 
ATOM   10773 N  N     . ASP B 1 649 ? 116.734 147.630 162.666 1.00 12.87 ?  649 ASP B N     1 
ATOM   10774 C  CA    . ASP B 1 649 ? 116.056 148.306 161.563 1.00 7.33  ?  649 ASP B CA    1 
ATOM   10775 C  C     . ASP B 1 649 ? 116.321 147.617 160.230 1.00 10.36 ?  649 ASP B C     1 
ATOM   10776 O  O     . ASP B 1 649 ? 115.428 147.542 159.381 1.00 29.65 ?  649 ASP B O     1 
ATOM   10777 C  CB    . ASP B 1 649 ? 116.475 149.775 161.506 1.00 16.59 ?  649 ASP B CB    1 
ATOM   10778 C  CG    . ASP B 1 649 ? 117.960 149.966 161.714 1.00 16.75 ?  649 ASP B CG    1 
ATOM   10779 O  OD1   . ASP B 1 649 ? 118.499 149.382 162.674 1.00 20.57 ?  649 ASP B OD1   1 
ATOM   10780 O  OD2   . ASP B 1 649 ? 118.584 150.703 160.928 1.00 15.48 -1 649 ASP B OD2   1 
ATOM   10781 N  N     . GLN B 1 650 ? 117.534 147.122 160.024 1.00 12.34 ?  650 GLN B N     1 
ATOM   10782 C  CA    . GLN B 1 650 ? 117.842 146.301 158.862 1.00 3.46  ?  650 GLN B CA    1 
ATOM   10783 C  C     . GLN B 1 650 ? 117.610 144.836 159.233 1.00 7.97  ?  650 GLN B C     1 
ATOM   10784 O  O     . GLN B 1 650 ? 116.987 144.538 160.255 1.00 18.13 ?  650 GLN B O     1 
ATOM   10785 C  CB    . GLN B 1 650 ? 119.265 146.582 158.378 1.00 7.16  ?  650 GLN B CB    1 
ATOM   10786 C  CG    . GLN B 1 650 ? 119.514 148.025 158.001 1.00 8.51  ?  650 GLN B CG    1 
ATOM   10787 C  CD    . GLN B 1 650 ? 120.920 148.252 157.495 1.00 13.48 ?  650 GLN B CD    1 
ATOM   10788 O  OE1   . GLN B 1 650 ? 121.260 147.863 156.380 1.00 18.42 ?  650 GLN B OE1   1 
ATOM   10789 N  NE2   . GLN B 1 650 ? 121.746 148.889 158.315 1.00 6.77  ?  650 GLN B NE2   1 
ATOM   10790 N  N     . GLY B 1 651 ? 118.085 143.907 158.408 1.00 7.27  ?  651 GLY B N     1 
ATOM   10791 C  CA    . GLY B 1 651 ? 117.850 142.500 158.640 1.00 8.37  ?  651 GLY B CA    1 
ATOM   10792 C  C     . GLY B 1 651 ? 118.958 141.826 159.426 1.00 7.98  ?  651 GLY B C     1 
ATOM   10793 O  O     . GLY B 1 651 ? 119.931 142.440 159.863 1.00 12.97 ?  651 GLY B O     1 
ATOM   10794 N  N     . ILE B 1 652 ? 118.783 140.521 159.610 1.00 12.55 ?  652 ILE B N     1 
ATOM   10795 C  CA    . ILE B 1 652 ? 119.737 139.664 160.299 1.00 11.63 ?  652 ILE B CA    1 
ATOM   10796 C  C     . ILE B 1 652 ? 120.032 138.482 159.390 1.00 14.25 ?  652 ILE B C     1 
ATOM   10797 O  O     . ILE B 1 652 ? 119.107 137.869 158.847 1.00 25.45 ?  652 ILE B O     1 
ATOM   10798 C  CB    . ILE B 1 652 ? 119.195 139.174 161.654 1.00 6.36  ?  652 ILE B CB    1 
ATOM   10799 C  CG1   . ILE B 1 652 ? 118.756 140.354 162.521 1.00 6.35  ?  652 ILE B CG1   1 
ATOM   10800 C  CG2   . ILE B 1 652 ? 120.229 138.328 162.373 1.00 10.09 ?  652 ILE B CG2   1 
ATOM   10801 C  CD1   . ILE B 1 652 ? 117.953 139.943 163.729 1.00 9.76  ?  652 ILE B CD1   1 
ATOM   10802 N  N     . SER B 1 653 ? 121.311 138.161 159.224 1.00 5.70  ?  653 SER B N     1 
ATOM   10803 C  CA    . SER B 1 653 ? 121.694 137.012 158.409 1.00 12.44 ?  653 SER B CA    1 
ATOM   10804 C  C     . SER B 1 653 ? 121.306 135.748 159.163 1.00 19.34 ?  653 SER B C     1 
ATOM   10805 O  O     . SER B 1 653 ? 122.048 135.261 160.017 1.00 23.48 ?  653 SER B O     1 
ATOM   10806 C  CB    . SER B 1 653 ? 123.185 137.042 158.102 1.00 12.43 ?  653 SER B CB    1 
ATOM   10807 O  OG    . SER B 1 653 ? 123.448 137.849 156.969 1.00 21.12 ?  653 SER B OG    1 
ATOM   10808 N  N     . PHE B 1 654 ? 120.132 135.215 158.844 1.00 19.33 ?  654 PHE B N     1 
ATOM   10809 C  CA    . PHE B 1 654 ? 119.544 134.092 159.565 1.00 12.91 ?  654 PHE B CA    1 
ATOM   10810 C  C     . PHE B 1 654 ? 119.790 132.822 158.757 1.00 16.26 ?  654 PHE B C     1 
ATOM   10811 O  O     . PHE B 1 654 ? 119.125 132.572 157.750 1.00 25.36 ?  654 PHE B O     1 
ATOM   10812 C  CB    . PHE B 1 654 ? 118.058 134.336 159.799 1.00 13.27 ?  654 PHE B CB    1 
ATOM   10813 C  CG    . PHE B 1 654 ? 117.381 133.269 160.607 1.00 16.91 ?  654 PHE B CG    1 
ATOM   10814 C  CD1   . PHE B 1 654 ? 118.109 132.419 161.421 1.00 18.96 ?  654 PHE B CD1   1 
ATOM   10815 C  CD2   . PHE B 1 654 ? 116.008 133.120 160.552 1.00 17.86 ?  654 PHE B CD2   1 
ATOM   10816 C  CE1   . PHE B 1 654 ? 117.482 131.440 162.158 1.00 19.71 ?  654 PHE B CE1   1 
ATOM   10817 C  CE2   . PHE B 1 654 ? 115.377 132.145 161.288 1.00 17.55 ?  654 PHE B CE2   1 
ATOM   10818 C  CZ    . PHE B 1 654 ? 116.113 131.304 162.094 1.00 16.60 ?  654 PHE B CZ    1 
ATOM   10819 N  N     . THR B 1 655 ? 120.744 132.018 159.212 1.00 21.60 ?  655 THR B N     1 
ATOM   10820 C  CA    . THR B 1 655 ? 121.029 130.730 158.602 1.00 22.15 ?  655 THR B CA    1 
ATOM   10821 C  C     . THR B 1 655 ? 120.183 129.654 159.270 1.00 22.47 ?  655 THR B C     1 
ATOM   10822 O  O     . THR B 1 655 ? 120.142 129.565 160.501 1.00 27.99 ?  655 THR B O     1 
ATOM   10823 C  CB    . THR B 1 655 ? 122.515 130.390 158.728 1.00 24.56 ?  655 THR B CB    1 
ATOM   10824 O  OG1   . THR B 1 655 ? 123.286 131.317 157.954 1.00 31.42 ?  655 THR B OG1   1 
ATOM   10825 C  CG2   . THR B 1 655 ? 122.789 128.977 158.236 1.00 24.12 ?  655 THR B CG2   1 
ATOM   10826 N  N     . LEU B 1 656 ? 119.500 128.854 158.460 1.00 28.74 ?  656 LEU B N     1 
ATOM   10827 C  CA    . LEU B 1 656 ? 118.746 127.714 158.961 1.00 31.33 ?  656 LEU B CA    1 
ATOM   10828 C  C     . LEU B 1 656 ? 119.674 126.513 159.066 1.00 24.98 ?  656 LEU B C     1 
ATOM   10829 O  O     . LEU B 1 656 ? 120.464 126.252 158.155 1.00 30.77 ?  656 LEU B O     1 
ATOM   10830 C  CB    . LEU B 1 656 ? 117.562 127.397 158.049 1.00 28.54 ?  656 LEU B CB    1 
ATOM   10831 C  CG    . LEU B 1 656 ? 116.467 128.463 158.000 1.00 29.96 ?  656 LEU B CG    1 
ATOM   10832 C  CD1   . LEU B 1 656 ? 115.301 127.996 157.149 1.00 27.74 ?  656 LEU B CD1   1 
ATOM   10833 C  CD2   . LEU B 1 656 ? 116.003 128.828 159.402 1.00 26.15 ?  656 LEU B CD2   1 
ATOM   10834 N  N     . PHE B 1 657 ? 119.594 125.805 160.186 1.00 25.49 ?  657 PHE B N     1 
ATOM   10835 C  CA    . PHE B 1 657 ? 120.443 124.649 160.455 1.00 29.93 ?  657 PHE B CA    1 
ATOM   10836 C  C     . PHE B 1 657 ? 119.549 123.418 160.495 1.00 34.81 ?  657 PHE B C     1 
ATOM   10837 O  O     . PHE B 1 657 ? 118.772 123.238 161.438 1.00 38.68 ?  657 PHE B O     1 
ATOM   10838 C  CB    . PHE B 1 657 ? 121.209 124.836 161.761 1.00 28.95 ?  657 PHE B CB    1 
ATOM   10839 C  CG    . PHE B 1 657 ? 122.034 126.088 161.796 1.00 33.74 ?  657 PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 1 657 ? 123.303 126.113 161.245 1.00 32.30 ?  657 PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 1 657 ? 121.536 127.247 162.369 1.00 33.75 ?  657 PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 1 657 ? 124.061 127.268 161.271 1.00 32.19 ?  657 PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 1 657 ? 122.291 128.401 162.402 1.00 31.68 ?  657 PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 1 657 ? 123.555 128.412 161.851 1.00 31.73 ?  657 PHE B CZ    1 
ATOM   10845 N  N     . LEU B 1 658 ? 119.660 122.576 159.474 1.00 35.52 ?  658 LEU B N     1 
ATOM   10846 C  CA    . LEU B 1 658 ? 118.720 121.494 159.247 1.00 38.84 ?  658 LEU B CA    1 
ATOM   10847 C  C     . LEU B 1 658 ? 119.417 120.148 159.393 1.00 42.86 ?  658 LEU B C     1 
ATOM   10848 O  O     . LEU B 1 658 ? 120.626 120.030 159.180 1.00 42.45 ?  658 LEU B O     1 
ATOM   10849 C  CB    . LEU B 1 658 ? 118.104 121.602 157.851 1.00 38.92 ?  658 LEU B CB    1 
ATOM   10850 C  CG    . LEU B 1 658 ? 117.544 122.975 157.469 1.00 36.73 ?  658 LEU B CG    1 
ATOM   10851 C  CD1   . LEU B 1 658 ? 117.615 123.155 155.964 1.00 36.74 ?  658 LEU B CD1   1 
ATOM   10852 C  CD2   . LEU B 1 658 ? 116.133 123.197 157.978 1.00 34.53 ?  658 LEU B CD2   1 
ATOM   10853 N  N     . LYS B 1 659 ? 118.643 119.140 159.778 1.00 46.82 ?  659 LYS B N     1 
ATOM   10854 C  CA    . LYS B 1 659 ? 119.119 117.767 159.793 1.00 45.01 ?  659 LYS B CA    1 
ATOM   10855 C  C     . LYS B 1 659 ? 118.791 117.087 158.470 1.00 47.48 ?  659 LYS B C     1 
ATOM   10856 O  O     . LYS B 1 659 ? 117.856 117.474 157.765 1.00 49.57 ?  659 LYS B O     1 
ATOM   10857 C  CB    . LYS B 1 659 ? 118.500 116.985 160.951 1.00 45.65 ?  659 LYS B CB    1 
ATOM   10858 C  CG    . LYS B 1 659 ? 118.891 117.492 162.327 1.00 46.86 ?  659 LYS B CG    1 
ATOM   10859 C  CD    . LYS B 1 659 ? 118.388 116.560 163.417 1.00 49.12 ?  659 LYS B CD    1 
ATOM   10860 C  CE    . LYS B 1 659 ? 118.825 117.031 164.794 1.00 46.79 ?  659 LYS B CE    1 
ATOM   10861 N  NZ    . LYS B 1 659 ? 118.632 115.981 165.832 1.00 49.98 1  659 LYS B NZ    1 
ATOM   10862 N  N     . ASP B 1 660 ? 119.583 116.066 158.135 1.00 53.65 ?  660 ASP B N     1 
ATOM   10863 C  CA    . ASP B 1 660 ? 119.355 115.322 156.901 1.00 52.62 ?  660 ASP B CA    1 
ATOM   10864 C  C     . ASP B 1 660 ? 118.044 114.548 156.924 1.00 51.96 ?  660 ASP B C     1 
ATOM   10865 O  O     . ASP B 1 660 ? 117.473 114.288 155.859 1.00 51.23 ?  660 ASP B O     1 
ATOM   10866 C  CB    . ASP B 1 660 ? 120.520 114.363 156.648 1.00 53.34 ?  660 ASP B CB    1 
ATOM   10867 C  CG    . ASP B 1 660 ? 121.469 114.867 155.579 1.00 55.56 ?  660 ASP B CG    1 
ATOM   10868 O  OD1   . ASP B 1 660 ? 121.022 115.629 154.697 1.00 54.48 ?  660 ASP B OD1   1 
ATOM   10869 O  OD2   . ASP B 1 660 ? 122.663 114.502 155.621 1.00 53.90 -1 660 ASP B OD2   1 
ATOM   10870 N  N     . THR B 1 661 ? 117.555 114.179 158.110 1.00 52.85 ?  661 THR B N     1 
ATOM   10871 C  CA    . THR B 1 661 ? 116.346 113.365 158.196 1.00 52.27 ?  661 THR B CA    1 
ATOM   10872 C  C     . THR B 1 661 ? 115.108 114.150 157.778 1.00 52.80 ?  661 THR B C     1 
ATOM   10873 O  O     . THR B 1 661 ? 114.188 113.591 157.171 1.00 55.96 ?  661 THR B O     1 
ATOM   10874 C  CB    . THR B 1 661 ? 116.177 112.825 159.615 1.00 53.12 ?  661 THR B CB    1 
ATOM   10875 O  OG1   . THR B 1 661 ? 116.218 113.911 160.550 1.00 54.39 ?  661 THR B OG1   1 
ATOM   10876 C  CG2   . THR B 1 661 ? 117.286 111.838 159.945 1.00 52.13 ?  661 THR B CG2   1 
ATOM   10877 N  N     . MET B 1 662 ? 115.064 115.441 158.095 1.00 51.33 ?  662 MET B N     1 
ATOM   10878 C  CA    . MET B 1 662 ? 113.873 116.234 157.830 1.00 52.61 ?  662 MET B CA    1 
ATOM   10879 C  C     . MET B 1 662 ? 113.697 116.476 156.334 1.00 51.05 ?  662 MET B C     1 
ATOM   10880 O  O     . MET B 1 662 ? 114.655 116.461 155.558 1.00 52.14 ?  662 MET B O     1 
ATOM   10881 C  CB    . MET B 1 662 ? 113.940 117.560 158.587 1.00 51.42 ?  662 MET B CB    1 
ATOM   10882 C  CG    . MET B 1 662 ? 114.732 118.649 157.898 1.00 49.54 ?  662 MET B CG    1 
ATOM   10883 S  SD    . MET B 1 662 ? 114.750 120.157 158.881 1.00 59.95 ?  662 MET B SD    1 
ATOM   10884 C  CE    . MET B 1 662 ? 114.748 119.487 160.542 1.00 49.08 ?  662 MET B CE    1 
ATOM   10885 N  N     . THR B 1 663 ? 112.447 116.697 155.936 1.00 43.99 ?  663 THR B N     1 
ATOM   10886 C  CA    . THR B 1 663 ? 112.061 116.786 154.539 1.00 44.61 ?  663 THR B CA    1 
ATOM   10887 C  C     . THR B 1 663 ? 111.962 118.247 154.103 1.00 44.35 ?  663 THR B C     1 
ATOM   10888 O  O     . THR B 1 663 ? 112.157 119.175 154.890 1.00 47.40 ?  663 THR B O     1 
ATOM   10889 C  CB    . THR B 1 663 ? 110.732 116.062 154.312 1.00 44.65 ?  663 THR B CB    1 
ATOM   10890 O  OG1   . THR B 1 663 ? 109.706 116.695 155.085 1.00 46.81 ?  663 THR B OG1   1 
ATOM   10891 C  CG2   . THR B 1 663 ? 110.844 114.608 154.736 1.00 45.09 ?  663 THR B CG2   1 
ATOM   10892 N  N     . THR B 1 664 ? 111.656 118.446 152.817 1.00 36.56 ?  664 THR B N     1 
ATOM   10893 C  CA    . THR B 1 664 ? 111.433 119.798 152.316 1.00 37.93 ?  664 THR B CA    1 
ATOM   10894 C  C     . THR B 1 664 ? 110.187 120.420 152.930 1.00 36.91 ?  664 THR B C     1 
ATOM   10895 O  O     . THR B 1 664 ? 110.070 121.648 152.990 1.00 39.76 ?  664 THR B O     1 
ATOM   10896 C  CB    . THR B 1 664 ? 111.316 119.792 150.790 1.00 37.84 ?  664 THR B CB    1 
ATOM   10897 O  OG1   . THR B 1 664 ? 110.124 119.097 150.403 1.00 38.33 ?  664 THR B OG1   1 
ATOM   10898 C  CG2   . THR B 1 664 ? 112.524 119.112 150.165 1.00 37.08 ?  664 THR B CG2   1 
ATOM   10899 N  N     . ARG B 1 665 ? 109.244 119.591 153.383 1.00 39.50 ?  665 ARG B N     1 
ATOM   10900 C  CA    . ARG B 1 665 ? 108.068 120.108 154.073 1.00 37.27 ?  665 ARG B CA    1 
ATOM   10901 C  C     . ARG B 1 665 ? 108.449 120.760 155.395 1.00 40.60 ?  665 ARG B C     1 
ATOM   10902 O  O     . ARG B 1 665 ? 107.879 121.788 155.772 1.00 42.67 ?  665 ARG B O     1 
ATOM   10903 C  CB    . ARG B 1 665 ? 107.059 118.982 154.288 1.00 39.03 ?  665 ARG B CB    1 
ATOM   10904 C  CG    . ARG B 1 665 ? 105.732 119.401 154.899 1.00 36.25 ?  665 ARG B CG    1 
ATOM   10905 C  CD    . ARG B 1 665 ? 105.555 118.779 156.274 1.00 39.06 ?  665 ARG B CD    1 
ATOM   10906 N  NE    . ARG B 1 665 ? 104.155 118.498 156.569 1.00 42.59 ?  665 ARG B NE    1 
ATOM   10907 C  CZ    . ARG B 1 665 ? 103.539 118.843 157.690 1.00 42.49 ?  665 ARG B CZ    1 
ATOM   10908 N  NH1   . ARG B 1 665 ? 104.173 119.481 158.659 1.00 43.20 1  665 ARG B NH1   1 
ATOM   10909 N  NH2   . ARG B 1 665 ? 102.254 118.538 157.845 1.00 41.16 ?  665 ARG B NH2   1 
ATOM   10910 N  N     . ASP B 1 666 ? 109.415 120.182 156.112 1.00 40.52 ?  666 ASP B N     1 
ATOM   10911 C  CA    . ASP B 1 666 ? 109.901 120.807 157.337 1.00 36.31 ?  666 ASP B CA    1 
ATOM   10912 C  C     . ASP B 1 666 ? 110.577 122.141 157.046 1.00 40.69 ?  666 ASP B C     1 
ATOM   10913 O  O     . ASP B 1 666 ? 110.396 123.112 157.791 1.00 43.81 ?  666 ASP B O     1 
ATOM   10914 C  CB    . ASP B 1 666 ? 110.860 119.863 158.061 1.00 39.39 ?  666 ASP B CB    1 
ATOM   10915 C  CG    . ASP B 1 666 ? 110.174 118.607 158.560 1.00 46.56 ?  666 ASP B CG    1 
ATOM   10916 O  OD1   . ASP B 1 666 ? 109.117 118.726 159.214 1.00 46.49 ?  666 ASP B OD1   1 
ATOM   10917 O  OD2   . ASP B 1 666 ? 110.688 117.501 158.296 1.00 46.36 -1 666 ASP B OD2   1 
ATOM   10918 N  N     . LEU B 1 667 ? 111.361 122.208 155.968 1.00 34.44 ?  667 LEU B N     1 
ATOM   10919 C  CA    . LEU B 1 667 ? 111.988 123.467 155.581 1.00 29.98 ?  667 LEU B CA    1 
ATOM   10920 C  C     . LEU B 1 667 ? 110.941 124.515 155.221 1.00 28.63 ?  667 LEU B C     1 
ATOM   10921 O  O     . LEU B 1 667 ? 111.067 125.686 155.600 1.00 35.33 ?  667 LEU B O     1 
ATOM   10922 C  CB    . LEU B 1 667 ? 112.942 123.231 154.409 1.00 33.52 ?  667 LEU B CB    1 
ATOM   10923 C  CG    . LEU B 1 667 ? 113.867 124.377 154.006 1.00 32.74 ?  667 LEU B CG    1 
ATOM   10924 C  CD1   . LEU B 1 667 ? 114.456 125.044 155.234 1.00 34.04 ?  667 LEU B CD1   1 
ATOM   10925 C  CD2   . LEU B 1 667 ? 114.966 123.867 153.094 1.00 31.27 ?  667 LEU B CD2   1 
ATOM   10926 N  N     . ASN B 1 668 ? 109.898 124.110 154.494 1.00 29.56 ?  668 ASN B N     1 
ATOM   10927 C  CA    . ASN B 1 668 ? 108.822 125.037 154.160 1.00 24.89 ?  668 ASN B CA    1 
ATOM   10928 C  C     . ASN B 1 668 ? 108.087 125.502 155.410 1.00 26.58 ?  668 ASN B C     1 
ATOM   10929 O  O     . ASN B 1 668 ? 107.711 126.673 155.512 1.00 28.91 ?  668 ASN B O     1 
ATOM   10930 C  CB    . ASN B 1 668 ? 107.852 124.386 153.176 1.00 28.31 ?  668 ASN B CB    1 
ATOM   10931 C  CG    . ASN B 1 668 ? 108.242 124.622 151.733 1.00 32.47 ?  668 ASN B CG    1 
ATOM   10932 O  OD1   . ASN B 1 668 ? 108.866 125.629 151.403 1.00 33.33 ?  668 ASN B OD1   1 
ATOM   10933 N  ND2   . ASN B 1 668 ? 107.874 123.690 150.862 1.00 33.17 ?  668 ASN B ND2   1 
ATOM   10934 N  N     . ARG B 1 669 ? 107.867 124.598 156.367 1.00 30.84 ?  669 ARG B N     1 
ATOM   10935 C  CA    . ARG B 1 669 ? 107.227 124.985 157.619 1.00 33.19 ?  669 ARG B CA    1 
ATOM   10936 C  C     . ARG B 1 669 ? 108.079 125.984 158.387 1.00 27.48 ?  669 ARG B C     1 
ATOM   10937 O  O     . ARG B 1 669 ? 107.554 126.943 158.962 1.00 28.14 ?  669 ARG B O     1 
ATOM   10938 C  CB    . ARG B 1 669 ? 106.955 123.752 158.478 1.00 31.40 ?  669 ARG B CB    1 
ATOM   10939 C  CG    . ARG B 1 669 ? 105.490 123.386 158.592 1.00 30.10 ?  669 ARG B CG    1 
ATOM   10940 C  CD    . ARG B 1 669 ? 105.270 122.349 159.683 1.00 32.17 ?  669 ARG B CD    1 
ATOM   10941 N  NE    . ARG B 1 669 ? 105.206 122.943 161.014 1.00 31.03 ?  669 ARG B NE    1 
ATOM   10942 C  CZ    . ARG B 1 669 ? 104.191 123.666 161.471 1.00 34.14 ?  669 ARG B CZ    1 
ATOM   10943 N  NH1   . ARG B 1 669 ? 103.124 123.907 160.727 1.00 33.10 1  669 ARG B NH1   1 
ATOM   10944 N  NH2   . ARG B 1 669 ? 104.247 124.154 162.706 1.00 34.56 ?  669 ARG B NH2   1 
ATOM   10945 N  N     . ILE B 1 670 ? 109.395 125.771 158.415 1.00 24.89 ?  670 ILE B N     1 
ATOM   10946 C  CA    . ILE B 1 670 ? 110.284 126.719 159.083 1.00 28.67 ?  670 ILE B CA    1 
ATOM   10947 C  C     . ILE B 1 670 ? 110.231 128.075 158.391 1.00 27.42 ?  670 ILE B C     1 
ATOM   10948 O  O     . ILE B 1 670 ? 110.175 129.121 159.048 1.00 27.35 ?  670 ILE B O     1 
ATOM   10949 C  CB    . ILE B 1 670 ? 111.720 126.165 159.141 1.00 28.82 ?  670 ILE B CB    1 
ATOM   10950 C  CG1   . ILE B 1 670 ? 111.779 124.929 160.042 1.00 28.87 ?  670 ILE B CG1   1 
ATOM   10951 C  CG2   . ILE B 1 670 ? 112.681 127.223 159.647 1.00 26.47 ?  670 ILE B CG2   1 
ATOM   10952 C  CD1   . ILE B 1 670 ? 112.956 124.025 159.758 1.00 28.03 ?  670 ILE B CD1   1 
ATOM   10953 N  N     . ASP B 1 671 ? 110.240 128.079 157.056 1.00 27.88 ?  671 ASP B N     1 
ATOM   10954 C  CA    . ASP B 1 671 ? 110.163 129.334 156.314 1.00 21.61 ?  671 ASP B CA    1 
ATOM   10955 C  C     . ASP B 1 671 ? 108.853 130.064 156.590 1.00 22.57 ?  671 ASP B C     1 
ATOM   10956 O  O     . ASP B 1 671 ? 108.838 131.287 156.780 1.00 26.72 ?  671 ASP B O     1 
ATOM   10957 C  CB    . ASP B 1 671 ? 110.315 129.066 154.815 1.00 22.56 ?  671 ASP B CB    1 
ATOM   10958 C  CG    . ASP B 1 671 ? 111.718 128.638 154.437 1.00 32.56 ?  671 ASP B CG    1 
ATOM   10959 O  OD1   . ASP B 1 671 ? 112.665 128.968 155.180 1.00 35.53 ?  671 ASP B OD1   1 
ATOM   10960 O  OD2   . ASP B 1 671 ? 111.874 127.968 153.395 1.00 33.40 -1 671 ASP B OD2   1 
ATOM   10961 N  N     . LEU B 1 672 ? 107.740 129.330 156.617 1.00 22.25 ?  672 LEU B N     1 
ATOM   10962 C  CA    . LEU B 1 672 ? 106.444 129.953 156.856 1.00 20.71 ?  672 LEU B CA    1 
ATOM   10963 C  C     . LEU B 1 672 ? 106.308 130.443 158.290 1.00 21.52 ?  672 LEU B C     1 
ATOM   10964 O  O     . LEU B 1 672 ? 105.655 131.462 158.533 1.00 26.69 ?  672 LEU B O     1 
ATOM   10965 C  CB    . LEU B 1 672 ? 105.321 128.976 156.515 1.00 24.45 ?  672 LEU B CB    1 
ATOM   10966 C  CG    . LEU B 1 672 ? 105.232 128.582 155.040 1.00 23.66 ?  672 LEU B CG    1 
ATOM   10967 C  CD1   . LEU B 1 672 ? 104.421 127.308 154.872 1.00 22.52 ?  672 LEU B CD1   1 
ATOM   10968 C  CD2   . LEU B 1 672 ? 104.654 129.718 154.212 1.00 20.82 ?  672 LEU B CD2   1 
ATOM   10969 N  N     . TYR B 1 673 ? 106.905 129.735 159.250 1.00 21.13 ?  673 TYR B N     1 
ATOM   10970 C  CA    . TYR B 1 673 ? 106.909 130.221 160.625 1.00 18.26 ?  673 TYR B CA    1 
ATOM   10971 C  C     . TYR B 1 673 ? 107.771 131.469 160.760 1.00 19.58 ?  673 TYR B C     1 
ATOM   10972 O  O     . TYR B 1 673 ? 107.431 132.385 161.517 1.00 27.13 ?  673 TYR B O     1 
ATOM   10973 C  CB    . TYR B 1 673 ? 107.400 129.125 161.570 1.00 18.99 ?  673 TYR B CB    1 
ATOM   10974 C  CG    . TYR B 1 673 ? 107.338 129.513 163.028 1.00 23.24 ?  673 TYR B CG    1 
ATOM   10975 C  CD1   . TYR B 1 673 ? 106.123 129.788 163.640 1.00 22.65 ?  673 TYR B CD1   1 
ATOM   10976 C  CD2   . TYR B 1 673 ? 108.492 129.607 163.792 1.00 16.57 ?  673 TYR B CD2   1 
ATOM   10977 C  CE1   . TYR B 1 673 ? 106.060 130.142 164.970 1.00 18.82 ?  673 TYR B CE1   1 
ATOM   10978 C  CE2   . TYR B 1 673 ? 108.439 129.962 165.123 1.00 19.29 ?  673 TYR B CE2   1 
ATOM   10979 C  CZ    . TYR B 1 673 ? 107.220 130.227 165.707 1.00 20.46 ?  673 TYR B CZ    1 
ATOM   10980 O  OH    . TYR B 1 673 ? 107.161 130.582 167.035 1.00 28.40 ?  673 TYR B OH    1 
ATOM   10981 N  N     . ALA B 1 674 ? 108.894 131.515 160.042 1.00 18.23 ?  674 ALA B N     1 
ATOM   10982 C  CA    . ALA B 1 674 ? 109.717 132.717 160.024 1.00 14.78 ?  674 ALA B CA    1 
ATOM   10983 C  C     . ALA B 1 674 ? 108.942 133.896 159.454 1.00 19.33 ?  674 ALA B C     1 
ATOM   10984 O  O     . ALA B 1 674 ? 108.974 135.002 160.005 1.00 23.74 ?  674 ALA B O     1 
ATOM   10985 C  CB    . ALA B 1 674 ? 110.990 132.462 159.215 1.00 13.81 ?  674 ALA B CB    1 
ATOM   10986 N  N     . HIS B 1 675 ? 108.224 133.670 158.353 1.00 18.20 ?  675 HIS B N     1 
ATOM   10987 C  CA    . HIS B 1 675 ? 107.393 134.726 157.785 1.00 19.37 ?  675 HIS B CA    1 
ATOM   10988 C  C     . HIS B 1 675 ? 106.302 135.153 158.762 1.00 18.72 ?  675 HIS B C     1 
ATOM   10989 O  O     . HIS B 1 675 ? 106.001 136.345 158.888 1.00 26.02 ?  675 HIS B O     1 
ATOM   10990 C  CB    . HIS B 1 675 ? 106.780 134.256 156.468 1.00 19.31 ?  675 HIS B CB    1 
ATOM   10991 C  CG    . HIS B 1 675 ? 105.725 135.173 155.935 1.00 17.26 ?  675 HIS B CG    1 
ATOM   10992 N  ND1   . HIS B 1 675 ? 104.379 134.960 156.141 1.00 24.61 ?  675 HIS B ND1   1 
ATOM   10993 C  CD2   . HIS B 1 675 ? 105.819 136.311 155.207 1.00 13.15 ?  675 HIS B CD2   1 
ATOM   10994 C  CE1   . HIS B 1 675 ? 103.689 135.925 155.562 1.00 22.93 ?  675 HIS B CE1   1 
ATOM   10995 N  NE2   . HIS B 1 675 ? 104.539 136.758 154.988 1.00 27.16 ?  675 HIS B NE2   1 
ATOM   10996 N  N     . HIS B 1 676 ? 105.697 134.188 159.457 1.00 18.21 ?  676 HIS B N     1 
ATOM   10997 C  CA    . HIS B 1 676 ? 104.653 134.497 160.427 1.00 18.52 ?  676 HIS B CA    1 
ATOM   10998 C  C     . HIS B 1 676 ? 105.202 135.294 161.603 1.00 23.94 ?  676 HIS B C     1 
ATOM   10999 O  O     . HIS B 1 676 ? 104.537 136.205 162.111 1.00 25.31 ?  676 HIS B O     1 
ATOM   11000 C  CB    . HIS B 1 676 ? 103.999 133.203 160.911 1.00 19.23 ?  676 HIS B CB    1 
ATOM   11001 C  CG    . HIS B 1 676 ? 103.165 133.369 162.142 1.00 20.47 ?  676 HIS B CG    1 
ATOM   11002 N  ND1   . HIS B 1 676 ? 101.956 134.032 162.140 1.00 25.04 ?  676 HIS B ND1   1 
ATOM   11003 C  CD2   . HIS B 1 676 ? 103.365 132.958 163.416 1.00 21.47 ?  676 HIS B CD2   1 
ATOM   11004 C  CE1   . HIS B 1 676 ? 101.448 134.021 163.359 1.00 26.61 ?  676 HIS B CE1   1 
ATOM   11005 N  NE2   . HIS B 1 676 ? 102.284 133.375 164.153 1.00 26.42 ?  676 HIS B NE2   1 
ATOM   11006 N  N     . ARG B 1 677 ? 106.413 134.970 162.048 1.00 22.89 ?  677 ARG B N     1 
ATOM   11007 C  CA    . ARG B 1 677 ? 107.003 135.612 163.216 1.00 19.61 ?  677 ARG B CA    1 
ATOM   11008 C  C     . ARG B 1 677 ? 107.649 136.953 162.901 1.00 21.29 ?  677 ARG B C     1 
ATOM   11009 O  O     . ARG B 1 677 ? 108.164 137.602 163.818 1.00 29.33 ?  677 ARG B O     1 
ATOM   11010 C  CB    . ARG B 1 677 ? 108.036 134.683 163.858 1.00 19.71 ?  677 ARG B CB    1 
ATOM   11011 C  CG    . ARG B 1 677 ? 107.429 133.505 164.590 1.00 23.45 ?  677 ARG B CG    1 
ATOM   11012 C  CD    . ARG B 1 677 ? 106.837 133.929 165.922 1.00 21.42 ?  677 ARG B CD    1 
ATOM   11013 N  NE    . ARG B 1 677 ? 107.863 134.364 166.863 1.00 28.85 ?  677 ARG B NE    1 
ATOM   11014 C  CZ    . ARG B 1 677 ? 108.022 135.615 167.274 1.00 35.20 ?  677 ARG B CZ    1 
ATOM   11015 N  NH1   . ARG B 1 677 ? 107.233 136.588 166.849 1.00 30.86 1  677 ARG B NH1   1 
ATOM   11016 N  NH2   . ARG B 1 677 ? 108.999 135.896 168.132 1.00 26.43 ?  677 ARG B NH2   1 
ATOM   11017 N  N     . GLY B 1 678 ? 107.637 137.384 161.645 1.00 20.57 ?  678 GLY B N     1 
ATOM   11018 C  CA    . GLY B 1 678 ? 108.212 138.657 161.278 1.00 13.88 ?  678 GLY B CA    1 
ATOM   11019 C  C     . GLY B 1 678 ? 109.651 138.612 160.825 1.00 12.96 ?  678 GLY B C     1 
ATOM   11020 O  O     . GLY B 1 678 ? 110.288 139.669 160.748 1.00 18.02 ?  678 GLY B O     1 
ATOM   11021 N  N     . ILE B 1 679 ? 110.189 137.427 160.530 1.00 15.56 ?  679 ILE B N     1 
ATOM   11022 C  CA    . ILE B 1 679 ? 111.559 137.335 160.046 1.00 15.82 ?  679 ILE B CA    1 
ATOM   11023 C  C     . ILE B 1 679 ? 111.657 138.032 158.700 1.00 13.14 ?  679 ILE B C     1 
ATOM   11024 O  O     . ILE B 1 679 ? 110.848 137.792 157.795 1.00 26.35 ?  679 ILE B O     1 
ATOM   11025 C  CB    . ILE B 1 679 ? 112.001 135.867 159.951 1.00 16.76 ?  679 ILE B CB    1 
ATOM   11026 C  CG1   . ILE B 1 679 ? 112.037 135.231 161.340 1.00 11.88 ?  679 ILE B CG1   1 
ATOM   11027 C  CG2   . ILE B 1 679 ? 113.354 135.758 159.269 1.00 14.34 ?  679 ILE B CG2   1 
ATOM   11028 C  CD1   . ILE B 1 679 ? 112.975 135.907 162.285 1.00 13.38 ?  679 ILE B CD1   1 
ATOM   11029 N  N     . LYS B 1 680 ? 112.648 138.910 158.564 1.00 9.64  ?  680 LYS B N     1 
ATOM   11030 C  CA    . LYS B 1 680 ? 112.781 139.683 157.338 1.00 9.10  ?  680 LYS B CA    1 
ATOM   11031 C  C     . LYS B 1 680 ? 113.463 138.875 156.241 1.00 6.32  ?  680 LYS B C     1 
ATOM   11032 O  O     . LYS B 1 680 ? 112.976 138.820 155.107 1.00 19.51 ?  680 LYS B O     1 
ATOM   11033 C  CB    . LYS B 1 680 ? 113.552 140.971 157.619 1.00 6.44  ?  680 LYS B CB    1 
ATOM   11034 C  CG    . LYS B 1 680 ? 112.783 141.983 158.443 1.00 0.00  ?  680 LYS B CG    1 
ATOM   11035 C  CD    . LYS B 1 680 ? 113.588 143.251 158.646 1.00 8.90  ?  680 LYS B CD    1 
ATOM   11036 C  CE    . LYS B 1 680 ? 112.984 144.117 159.729 1.00 9.68  ?  680 LYS B CE    1 
ATOM   11037 N  NZ    . LYS B 1 680 ? 113.761 145.365 159.942 1.00 17.63 1  680 LYS B NZ    1 
ATOM   11038 N  N     . THR B 1 681 ? 114.587 138.240 156.558 1.00 14.09 ?  681 THR B N     1 
ATOM   11039 C  CA    . THR B 1 681 ? 115.355 137.493 155.574 1.00 7.46  ?  681 THR B CA    1 
ATOM   11040 C  C     . THR B 1 681 ? 115.830 136.181 156.175 1.00 12.18 ?  681 THR B C     1 
ATOM   11041 O  O     . THR B 1 681 ? 116.023 136.067 157.388 1.00 19.65 ?  681 THR B O     1 
ATOM   11042 C  CB    . THR B 1 681 ? 116.569 138.289 155.069 1.00 12.38 ?  681 THR B CB    1 
ATOM   11043 O  OG1   . THR B 1 681 ? 117.304 138.806 156.186 1.00 23.17 ?  681 THR B OG1   1 
ATOM   11044 C  CG2   . THR B 1 681 ? 116.131 139.441 154.183 1.00 8.64  ?  681 THR B CG2   1 
ATOM   11045 N  N     . ILE B 1 682 ? 116.020 135.191 155.309 1.00 12.38 ?  682 ILE B N     1 
ATOM   11046 C  CA    . ILE B 1 682 ? 116.607 133.908 155.671 1.00 9.09  ?  682 ILE B CA    1 
ATOM   11047 C  C     . ILE B 1 682 ? 117.855 133.714 154.822 1.00 15.98 ?  682 ILE B C     1 
ATOM   11048 O  O     . ILE B 1 682 ? 117.794 133.813 153.592 1.00 19.54 ?  682 ILE B O     1 
ATOM   11049 C  CB    . ILE B 1 682 ? 115.617 132.748 155.469 1.00 11.04 ?  682 ILE B CB    1 
ATOM   11050 C  CG1   . ILE B 1 682 ? 114.274 133.079 156.119 1.00 17.16 ?  682 ILE B CG1   1 
ATOM   11051 C  CG2   . ILE B 1 682 ? 116.180 131.475 156.050 1.00 19.66 ?  682 ILE B CG2   1 
ATOM   11052 C  CD1   . ILE B 1 682 ? 113.226 132.013 155.936 1.00 18.91 ?  682 ILE B CD1   1 
ATOM   11053 N  N     . TYR B 1 683 ? 118.986 133.452 155.478 1.00 13.01 ?  683 TYR B N     1 
ATOM   11054 C  CA    . TYR B 1 683 ? 120.265 133.440 154.768 1.00 12.37 ?  683 TYR B CA    1 
ATOM   11055 C  C     . TYR B 1 683 ? 120.529 132.099 154.086 1.00 20.43 ?  683 TYR B C     1 
ATOM   11056 O  O     . TYR B 1 683 ? 120.563 132.011 152.857 1.00 33.65 ?  683 TYR B O     1 
ATOM   11057 C  CB    . TYR B 1 683 ? 121.397 133.785 155.740 1.00 19.94 ?  683 TYR B CB    1 
ATOM   11058 C  CG    . TYR B 1 683 ? 122.748 133.979 155.089 1.00 16.76 ?  683 TYR B CG    1 
ATOM   11059 C  CD1   . TYR B 1 683 ? 122.855 134.299 153.742 1.00 10.05 ?  683 TYR B CD1   1 
ATOM   11060 C  CD2   . TYR B 1 683 ? 123.916 133.852 155.826 1.00 14.57 ?  683 TYR B CD2   1 
ATOM   11061 C  CE1   . TYR B 1 683 ? 124.084 134.478 153.148 1.00 17.35 ?  683 TYR B CE1   1 
ATOM   11062 C  CE2   . TYR B 1 683 ? 125.152 134.032 155.239 1.00 20.79 ?  683 TYR B CE2   1 
ATOM   11063 C  CZ    . TYR B 1 683 ? 125.230 134.345 153.900 1.00 21.07 ?  683 TYR B CZ    1 
ATOM   11064 O  OH    . TYR B 1 683 ? 126.459 134.525 153.312 1.00 18.47 ?  683 TYR B OH    1 
ATOM   11065 N  N     . TYR B 1 684 ? 120.695 131.041 154.868 1.00 28.72 ?  684 TYR B N     1 
ATOM   11066 C  CA    . TYR B 1 684 ? 121.165 129.779 154.322 1.00 22.47 ?  684 TYR B CA    1 
ATOM   11067 C  C     . TYR B 1 684 ? 120.385 128.627 154.929 1.00 33.54 ?  684 TYR B C     1 
ATOM   11068 O  O     . TYR B 1 684 ? 119.870 128.720 156.046 1.00 33.94 ?  684 TYR B O     1 
ATOM   11069 C  CB    . TYR B 1 684 ? 122.663 129.572 154.581 1.00 23.90 ?  684 TYR B CB    1 
ATOM   11070 C  CG    . TYR B 1 684 ? 123.550 129.950 153.419 1.00 25.15 ?  684 TYR B CG    1 
ATOM   11071 C  CD1   . TYR B 1 684 ? 123.345 129.410 152.157 1.00 28.20 ?  684 TYR B CD1   1 
ATOM   11072 C  CD2   . TYR B 1 684 ? 124.599 130.845 153.586 1.00 27.14 ?  684 TYR B CD2   1 
ATOM   11073 C  CE1   . TYR B 1 684 ? 124.157 129.753 151.093 1.00 30.33 ?  684 TYR B CE1   1 
ATOM   11074 C  CE2   . TYR B 1 684 ? 125.414 131.194 152.530 1.00 27.12 ?  684 TYR B CE2   1 
ATOM   11075 C  CZ    . TYR B 1 684 ? 125.190 130.647 151.286 1.00 30.90 ?  684 TYR B CZ    1 
ATOM   11076 O  OH    . TYR B 1 684 ? 126.003 130.994 150.232 1.00 33.34 ?  684 TYR B OH    1 
ATOM   11077 N  N     . ALA B 1 685 ? 120.308 127.540 154.175 1.00 32.23 ?  685 ALA B N     1 
ATOM   11078 C  CA    . ALA B 1 685 ? 119.776 126.271 154.652 1.00 31.89 ?  685 ALA B CA    1 
ATOM   11079 C  C     . ALA B 1 685 ? 120.942 125.286 154.651 1.00 34.11 ?  685 ALA B C     1 
ATOM   11080 O  O     . ALA B 1 685 ? 121.156 124.554 153.685 1.00 41.93 ?  685 ALA B O     1 
ATOM   11081 C  CB    . ALA B 1 685 ? 118.623 125.795 153.780 1.00 30.04 ?  685 ALA B CB    1 
ATOM   11082 N  N     . ARG B 1 686 ? 121.703 125.283 155.742 1.00 31.14 ?  686 ARG B N     1 
ATOM   11083 C  CA    . ARG B 1 686 ? 122.839 124.383 155.885 1.00 35.59 ?  686 ARG B CA    1 
ATOM   11084 C  C     . ARG B 1 686 ? 122.362 123.074 156.498 1.00 40.36 ?  686 ARG B C     1 
ATOM   11085 O  O     . ARG B 1 686 ? 121.814 123.066 157.605 1.00 39.37 ?  686 ARG B O     1 
ATOM   11086 C  CB    . ARG B 1 686 ? 123.917 125.022 156.756 1.00 35.54 ?  686 ARG B CB    1 
ATOM   11087 C  CG    . ARG B 1 686 ? 124.582 126.236 156.138 1.00 39.12 ?  686 ARG B CG    1 
ATOM   11088 C  CD    . ARG B 1 686 ? 125.725 126.734 157.006 1.00 40.12 ?  686 ARG B CD    1 
ATOM   11089 N  NE    . ARG B 1 686 ? 126.352 125.654 157.757 1.00 42.56 ?  686 ARG B NE    1 
ATOM   11090 C  CZ    . ARG B 1 686 ? 127.569 125.184 157.518 1.00 41.73 ?  686 ARG B CZ    1 
ATOM   11091 N  NH1   . ARG B 1 686 ? 128.322 125.678 156.549 1.00 40.57 1  686 ARG B NH1   1 
ATOM   11092 N  NH2   . ARG B 1 686 ? 128.042 124.194 158.269 1.00 38.17 ?  686 ARG B NH2   1 
ATOM   11093 N  N     . THR B 1 687 ? 122.576 121.972 155.788 1.00 42.20 ?  687 THR B N     1 
ATOM   11094 C  CA    . THR B 1 687 ? 122.144 120.658 156.234 1.00 45.25 ?  687 THR B CA    1 
ATOM   11095 C  C     . THR B 1 687 ? 123.335 119.887 156.786 1.00 45.70 ?  687 THR B C     1 
ATOM   11096 O  O     . THR B 1 687 ? 124.408 119.861 156.177 1.00 45.26 ?  687 THR B O     1 
ATOM   11097 C  CB    . THR B 1 687 ? 121.495 119.873 155.092 1.00 43.73 ?  687 THR B CB    1 
ATOM   11098 O  OG1   . THR B 1 687 ? 120.598 120.728 154.373 1.00 43.79 ?  687 THR B OG1   1 
ATOM   11099 C  CG2   . THR B 1 687 ? 120.716 118.690 155.642 1.00 42.22 ?  687 THR B CG2   1 
ATOM   11100 N  N     . LYS B 1 688 ? 123.136 119.263 157.942 1.00 40.87 ?  688 LYS B N     1 
ATOM   11101 C  CA    . LYS B 1 688 ? 124.203 118.525 158.606 1.00 43.33 ?  688 LYS B CA    1 
ATOM   11102 C  C     . LYS B 1 688 ? 124.508 117.222 157.873 1.00 48.17 ?  688 LYS B C     1 
ATOM   11103 O  O     . LYS B 1 688 ? 123.713 116.283 157.898 1.00 48.97 ?  688 LYS B O     1 
ATOM   11104 C  CB    . LYS B 1 688 ? 123.830 118.239 160.061 1.00 42.70 ?  688 LYS B CB    1 
ATOM   11105 C  CG    . LYS B 1 688 ? 124.918 117.544 160.858 1.00 41.41 ?  688 LYS B CG    1 
ATOM   11106 C  CD    . LYS B 1 688 ? 124.541 117.439 162.325 1.00 44.48 ?  688 LYS B CD    1 
ATOM   11107 C  CE    . LYS B 1 688 ? 125.701 116.914 163.155 1.00 46.73 ?  688 LYS B CE    1 
ATOM   11108 N  NZ    . LYS B 1 688 ? 125.356 116.841 164.601 1.00 44.27 ?  688 LYS B NZ    1 
ATOM   11109 N  N     . ASP C 2 37  ? 143.471 81.480  109.533 1.00 45.99 ?  16  ASP C N     1 
ATOM   11110 C  CA    . ASP C 2 37  ? 142.997 81.957  108.230 1.00 45.47 ?  16  ASP C CA    1 
ATOM   11111 C  C     . ASP C 2 37  ? 141.706 82.774  108.284 1.00 44.13 ?  16  ASP C C     1 
ATOM   11112 O  O     . ASP C 2 37  ? 141.268 83.306  107.262 1.00 44.46 ?  16  ASP C O     1 
ATOM   11113 C  CB    . ASP C 2 37  ? 142.801 80.769  107.285 1.00 45.90 ?  16  ASP C CB    1 
ATOM   11114 C  CG    . ASP C 2 37  ? 144.001 79.853  107.253 1.00 47.25 ?  16  ASP C CG    1 
ATOM   11115 O  OD1   . ASP C 2 37  ? 145.142 80.361  107.284 1.00 47.99 ?  16  ASP C OD1   1 
ATOM   11116 O  OD2   . ASP C 2 37  ? 143.798 78.623  107.201 1.00 49.50 -1 16  ASP C OD2   1 
ATOM   11117 N  N     . PHE C 2 38  ? 141.100 82.878  109.464 1.00 42.17 ?  17  PHE C N     1 
ATOM   11118 C  CA    . PHE C 2 38  ? 139.748 83.440  109.562 1.00 40.67 ?  17  PHE C CA    1 
ATOM   11119 C  C     . PHE C 2 38  ? 139.495 84.484  110.657 1.00 39.46 ?  17  PHE C C     1 
ATOM   11120 O  O     . PHE C 2 38  ? 138.570 85.290  110.530 1.00 39.17 ?  17  PHE C O     1 
ATOM   11121 C  CB    . PHE C 2 38  ? 138.710 82.308  109.664 1.00 40.24 ?  17  PHE C CB    1 
ATOM   11122 C  CG    . PHE C 2 38  ? 138.967 81.334  110.790 1.00 39.58 ?  17  PHE C CG    1 
ATOM   11123 C  CD1   . PHE C 2 38  ? 138.481 81.586  112.074 1.00 38.78 ?  17  PHE C CD1   1 
ATOM   11124 C  CD2   . PHE C 2 38  ? 139.682 80.157  110.564 1.00 39.43 ?  17  PHE C CD2   1 
ATOM   11125 C  CE1   . PHE C 2 38  ? 138.705 80.686  113.116 1.00 38.07 ?  17  PHE C CE1   1 
ATOM   11126 C  CE2   . PHE C 2 38  ? 139.913 79.249  111.602 1.00 39.10 ?  17  PHE C CE2   1 
ATOM   11127 C  CZ    . PHE C 2 38  ? 139.424 79.516  112.881 1.00 38.63 ?  17  PHE C CZ    1 
ATOM   11128 N  N     . THR C 2 39  ? 140.297 84.470  111.724 1.00 38.22 ?  18  THR C N     1 
ATOM   11129 C  CA    . THR C 2 39  ? 140.033 85.338  112.884 1.00 37.09 ?  18  THR C CA    1 
ATOM   11130 C  C     . THR C 2 39  ? 139.958 86.830  112.515 1.00 36.84 ?  18  THR C C     1 
ATOM   11131 O  O     . THR C 2 39  ? 139.032 87.534  112.951 1.00 36.13 ?  18  THR C O     1 
ATOM   11132 C  CB    . THR C 2 39  ? 140.998 85.069  114.075 1.00 36.59 ?  18  THR C CB    1 
ATOM   11133 O  OG1   . THR C 2 39  ? 140.631 83.838  114.704 1.00 36.50 ?  18  THR C OG1   1 
ATOM   11134 C  CG2   . THR C 2 39  ? 140.900 86.164  115.119 1.00 36.06 ?  18  THR C CG2   1 
ATOM   11135 N  N     . GLN C 2 40  ? 140.911 87.296  111.702 1.00 37.01 ?  19  GLN C N     1 
ATOM   11136 C  CA    . GLN C 2 40  ? 140.950 88.709  111.295 1.00 37.33 ?  19  GLN C CA    1 
ATOM   11137 C  C     . GLN C 2 40  ? 139.683 89.163  110.590 1.00 36.63 ?  19  GLN C C     1 
ATOM   11138 O  O     . GLN C 2 40  ? 139.175 90.249  110.866 1.00 36.10 ?  19  GLN C O     1 
ATOM   11139 C  CB    . GLN C 2 40  ? 142.170 89.024  110.431 1.00 38.24 ?  19  GLN C CB    1 
ATOM   11140 C  CG    . GLN C 2 40  ? 143.416 89.283  111.248 1.00 41.33 ?  19  GLN C CG    1 
ATOM   11141 C  CD    . GLN C 2 40  ? 144.315 90.346  110.647 1.00 45.15 ?  19  GLN C CD    1 
ATOM   11142 O  OE1   . GLN C 2 40  ? 144.415 90.481  109.421 1.00 47.33 ?  19  GLN C OE1   1 
ATOM   11143 N  NE2   . GLN C 2 40  ? 144.981 91.110  111.510 1.00 46.51 ?  19  GLN C NE2   1 
ATOM   11144 N  N     . MET C 2 41  ? 139.167 88.326  109.695 1.00 36.23 ?  20  MET C N     1 
ATOM   11145 C  CA    . MET C 2 41  ? 137.933 88.656  108.996 1.00 36.40 ?  20  MET C CA    1 
ATOM   11146 C  C     . MET C 2 41  ? 136.710 88.605  109.931 1.00 34.93 ?  20  MET C C     1 
ATOM   11147 O  O     . MET C 2 41  ? 135.793 89.411  109.787 1.00 34.20 ?  20  MET C O     1 
ATOM   11148 C  CB    . MET C 2 41  ? 137.771 87.844  107.692 1.00 37.35 ?  20  MET C CB    1 
ATOM   11149 C  CG    . MET C 2 41  ? 137.114 86.480  107.787 1.00 40.49 ?  20  MET C CG    1 
ATOM   11150 S  SD    . MET C 2 41  ? 136.819 85.796  106.126 1.00 48.68 ?  20  MET C SD    1 
ATOM   11151 C  CE    . MET C 2 41  ? 138.389 84.987  105.787 1.00 47.17 ?  20  MET C CE    1 
ATOM   11152 N  N     . PHE C 2 42  ? 136.724 87.701  110.914 1.00 33.75 ?  21  PHE C N     1 
ATOM   11153 C  CA    . PHE C 2 42  ? 135.678 87.698  111.948 1.00 32.62 ?  21  PHE C CA    1 
ATOM   11154 C  C     . PHE C 2 42  ? 135.782 88.904  112.874 1.00 32.59 ?  21  PHE C C     1 
ATOM   11155 O  O     . PHE C 2 42  ? 134.764 89.487  113.258 1.00 32.23 ?  21  PHE C O     1 
ATOM   11156 C  CB    . PHE C 2 42  ? 135.669 86.391  112.740 1.00 32.12 ?  21  PHE C CB    1 
ATOM   11157 C  CG    . PHE C 2 42  ? 134.937 85.278  112.050 1.00 31.04 ?  21  PHE C CG    1 
ATOM   11158 C  CD1   . PHE C 2 42  ? 133.593 85.034  112.327 1.00 30.75 ?  21  PHE C CD1   1 
ATOM   11159 C  CD2   . PHE C 2 42  ? 135.585 84.478  111.115 1.00 30.99 ?  21  PHE C CD2   1 
ATOM   11160 C  CE1   . PHE C 2 42  ? 132.904 84.000  111.682 1.00 30.30 ?  21  PHE C CE1   1 
ATOM   11161 C  CE2   . PHE C 2 42  ? 134.906 83.438  110.459 1.00 30.74 ?  21  PHE C CE2   1 
ATOM   11162 C  CZ    . PHE C 2 42  ? 133.565 83.201  110.744 1.00 30.48 ?  21  PHE C CZ    1 
ATOM   11163 N  N     . TYR C 2 43  ? 137.013 89.282  113.219 1.00 32.33 ?  22  TYR C N     1 
ATOM   11164 C  CA    . TYR C 2 43  ? 137.244 90.493  114.001 1.00 32.50 ?  22  TYR C CA    1 
ATOM   11165 C  C     . TYR C 2 43  ? 136.626 91.703  113.303 1.00 33.01 ?  22  TYR C C     1 
ATOM   11166 O  O     . TYR C 2 43  ? 135.865 92.457  113.915 1.00 32.50 ?  22  TYR C O     1 
ATOM   11167 C  CB    . TYR C 2 43  ? 138.742 90.724  114.279 1.00 32.53 ?  22  TYR C CB    1 
ATOM   11168 C  CG    . TYR C 2 43  ? 139.012 92.096  114.872 1.00 33.27 ?  22  TYR C CG    1 
ATOM   11169 C  CD1   . TYR C 2 43  ? 138.826 92.339  116.235 1.00 32.34 ?  22  TYR C CD1   1 
ATOM   11170 C  CD2   . TYR C 2 43  ? 139.413 93.158  114.060 1.00 33.71 ?  22  TYR C CD2   1 
ATOM   11171 C  CE1   . TYR C 2 43  ? 139.052 93.603  116.779 1.00 33.58 ?  22  TYR C CE1   1 
ATOM   11172 C  CE2   . TYR C 2 43  ? 139.636 94.431  114.589 1.00 35.12 ?  22  TYR C CE2   1 
ATOM   11173 C  CZ    . TYR C 2 43  ? 139.458 94.644  115.950 1.00 35.30 ?  22  TYR C CZ    1 
ATOM   11174 O  OH    . TYR C 2 43  ? 139.681 95.900  116.472 1.00 36.54 ?  22  TYR C OH    1 
ATOM   11175 N  N     . ASN C 2 44  ? 136.948 91.869  112.017 1.00 33.80 ?  23  ASN C N     1 
ATOM   11176 C  CA    . ASN C 2 44  ? 136.448 92.991  111.234 1.00 34.80 ?  23  ASN C CA    1 
ATOM   11177 C  C     . ASN C 2 44  ? 134.927 92.966  111.099 1.00 34.40 ?  23  ASN C C     1 
ATOM   11178 O  O     . ASN C 2 44  ? 134.278 93.998  111.230 1.00 33.99 ?  23  ASN C O     1 
ATOM   11179 C  CB    . ASN C 2 44  ? 137.119 93.044  109.851 1.00 35.46 ?  23  ASN C CB    1 
ATOM   11180 C  CG    . ASN C 2 44  ? 138.636 93.279  109.928 1.00 38.28 ?  23  ASN C CG    1 
ATOM   11181 O  OD1   . ASN C 2 44  ? 139.161 93.821  110.911 1.00 41.01 ?  23  ASN C OD1   1 
ATOM   11182 N  ND2   . ASN C 2 44  ? 139.342 92.873  108.874 1.00 39.13 ?  23  ASN C ND2   1 
ATOM   11183 N  N     . GLN C 2 45  ? 134.366 91.780  110.856 1.00 34.49 ?  24  GLN C N     1 
ATOM   11184 C  CA    . GLN C 2 45  ? 132.920 91.627  110.734 1.00 34.81 ?  24  GLN C CA    1 
ATOM   11185 C  C     . GLN C 2 45  ? 132.204 91.939  112.054 1.00 34.68 ?  24  GLN C C     1 
ATOM   11186 O  O     . GLN C 2 45  ? 131.200 92.655  112.065 1.00 34.59 ?  24  GLN C O     1 
ATOM   11187 C  CB    . GLN C 2 45  ? 132.562 90.228  110.224 1.00 34.83 ?  24  GLN C CB    1 
ATOM   11188 C  CG    . GLN C 2 45  ? 131.129 90.086  109.704 1.00 36.14 ?  24  GLN C CG    1 
ATOM   11189 C  CD    . GLN C 2 45  ? 130.817 90.995  108.512 1.00 38.04 ?  24  GLN C CD    1 
ATOM   11190 O  OE1   . GLN C 2 45  ? 131.698 91.339  107.719 1.00 38.57 ?  24  GLN C OE1   1 
ATOM   11191 N  NE2   . GLN C 2 45  ? 129.549 91.389  108.388 1.00 38.67 ?  24  GLN C NE2   1 
ATOM   11192 N  N     . ASN C 2 46  ? 132.727 91.422  113.163 1.00 34.71 ?  25  ASN C N     1 
ATOM   11193 C  CA    . ASN C 2 46  ? 132.122 91.681  114.469 1.00 34.99 ?  25  ASN C CA    1 
ATOM   11194 C  C     . ASN C 2 46  ? 132.113 93.165  114.834 1.00 35.69 ?  25  ASN C C     1 
ATOM   11195 O  O     . ASN C 2 46  ? 131.076 93.707  115.233 1.00 35.41 ?  25  ASN C O     1 
ATOM   11196 C  CB    . ASN C 2 46  ? 132.782 90.841  115.570 1.00 34.64 ?  25  ASN C CB    1 
ATOM   11197 C  CG    . ASN C 2 46  ? 132.239 89.428  115.620 1.00 34.71 ?  25  ASN C CG    1 
ATOM   11198 O  OD1   . ASN C 2 46  ? 131.303 89.150  116.363 1.00 35.68 ?  25  ASN C OD1   1 
ATOM   11199 N  ND2   . ASN C 2 46  ? 132.799 88.534  114.798 1.00 34.71 ?  25  ASN C ND2   1 
ATOM   11200 N  N     . VAL C 2 47  ? 133.252 93.831  114.672 1.00 36.69 ?  26  VAL C N     1 
ATOM   11201 C  CA    . VAL C 2 47  ? 133.335 95.246  115.039 1.00 38.00 ?  26  VAL C CA    1 
ATOM   11202 C  C     . VAL C 2 47  ? 132.528 96.154  114.100 1.00 38.90 ?  26  VAL C C     1 
ATOM   11203 O  O     . VAL C 2 47  ? 132.017 97.183  114.533 1.00 39.46 ?  26  VAL C O     1 
ATOM   11204 C  CB    . VAL C 2 47  ? 134.792 95.753  115.212 1.00 38.16 ?  26  VAL C CB    1 
ATOM   11205 C  CG1   . VAL C 2 47  ? 135.506 94.935  116.271 1.00 37.75 ?  26  VAL C CG1   1 
ATOM   11206 C  CG2   . VAL C 2 47  ? 135.555 95.735  113.890 1.00 38.81 ?  26  VAL C CG2   1 
ATOM   11207 N  N     . LYS C 2 48  ? 132.386 95.758  112.835 1.00 39.67 ?  27  LYS C N     1 
ATOM   11208 C  CA    . LYS C 2 48  ? 131.589 96.539  111.886 1.00 40.50 ?  27  LYS C CA    1 
ATOM   11209 C  C     . LYS C 2 48  ? 130.084 96.323  112.091 1.00 40.02 ?  27  LYS C C     1 
ATOM   11210 O  O     . LYS C 2 48  ? 129.261 97.089  111.583 1.00 40.55 ?  27  LYS C O     1 
ATOM   11211 C  CB    . LYS C 2 48  ? 132.002 96.250  110.430 1.00 41.23 ?  27  LYS C CB    1 
ATOM   11212 C  CG    . LYS C 2 48  ? 131.350 95.016  109.807 1.00 42.50 ?  27  LYS C CG    1 
ATOM   11213 C  CD    . LYS C 2 48  ? 131.747 94.818  108.337 1.00 44.92 ?  27  LYS C CD    1 
ATOM   11214 C  CE    . LYS C 2 48  ? 130.948 95.717  107.395 1.00 46.66 ?  27  LYS C CE    1 
ATOM   11215 N  NZ    . LYS C 2 48  ? 129.482 95.449  107.470 1.00 47.26 1  27  LYS C NZ    1 
ATOM   11216 N  N     . GLN C 2 49  ? 129.727 95.275  112.825 1.00 39.10 ?  28  GLN C N     1 
ATOM   11217 C  CA    . GLN C 2 49  ? 128.336 95.009  113.123 1.00 38.22 ?  28  GLN C CA    1 
ATOM   11218 C  C     . GLN C 2 49  ? 127.901 95.663  114.433 1.00 37.23 ?  28  GLN C C     1 
ATOM   11219 O  O     . GLN C 2 49  ? 126.738 95.540  114.813 1.00 37.40 ?  28  GLN C O     1 
ATOM   11220 C  CB    . GLN C 2 49  ? 128.049 93.497  113.134 1.00 38.69 ?  28  GLN C CB    1 
ATOM   11221 C  CG    . GLN C 2 49  ? 128.019 92.857  111.737 1.00 39.57 ?  28  GLN C CG    1 
ATOM   11222 C  CD    . GLN C 2 49  ? 127.545 91.406  111.734 1.00 41.20 ?  28  GLN C CD    1 
ATOM   11223 O  OE1   . GLN C 2 49  ? 127.548 90.753  110.689 1.00 42.94 ?  28  GLN C OE1   1 
ATOM   11224 N  NE2   . GLN C 2 49  ? 127.135 90.896  112.899 1.00 41.23 ?  28  GLN C NE2   1 
ATOM   11225 N  N     . PHE C 2 50  ? 128.815 96.371  115.106 1.00 35.83 ?  29  PHE C N     1 
ATOM   11226 C  CA    . PHE C 2 50  ? 128.508 96.965  116.414 1.00 34.51 ?  29  PHE C CA    1 
ATOM   11227 C  C     . PHE C 2 50  ? 127.266 97.861  116.393 1.00 33.81 ?  29  PHE C C     1 
ATOM   11228 O  O     . PHE C 2 50  ? 127.108 98.688  115.495 1.00 33.66 ?  29  PHE C O     1 
ATOM   11229 C  CB    . PHE C 2 50  ? 129.698 97.730  117.002 1.00 34.59 ?  29  PHE C CB    1 
ATOM   11230 C  CG    . PHE C 2 50  ? 129.419 98.325  118.371 1.00 34.59 ?  29  PHE C CG    1 
ATOM   11231 C  CD1   . PHE C 2 50  ? 129.323 97.507  119.502 1.00 34.34 ?  29  PHE C CD1   1 
ATOM   11232 C  CD2   . PHE C 2 50  ? 129.230 99.699  118.524 1.00 35.49 ?  29  PHE C CD2   1 
ATOM   11233 C  CE1   . PHE C 2 50  ? 129.057 98.050  120.768 1.00 33.88 ?  29  PHE C CE1   1 
ATOM   11234 C  CE2   . PHE C 2 50  ? 128.960 100.257 119.787 1.00 34.12 ?  29  PHE C CE2   1 
ATOM   11235 C  CZ    . PHE C 2 50  ? 128.874 99.433  120.908 1.00 33.87 ?  29  PHE C CZ    1 
ATOM   11236 N  N     . TRP C 2 51  ? 126.401 97.683  117.394 1.00 32.24 ?  30  TRP C N     1 
ATOM   11237 C  CA    . TRP C 2 51  ? 125.157 98.440  117.509 1.00 31.28 ?  30  TRP C CA    1 
ATOM   11238 C  C     . TRP C 2 51  ? 124.698 98.560  118.963 1.00 31.12 ?  30  TRP C C     1 
ATOM   11239 O  O     . TRP C 2 51  ? 125.186 97.831  119.834 1.00 30.71 ?  30  TRP C O     1 
ATOM   11240 C  CB    . TRP C 2 51  ? 124.058 97.801  116.648 1.00 30.85 ?  30  TRP C CB    1 
ATOM   11241 C  CG    . TRP C 2 51  ? 123.691 96.396  117.058 1.00 29.31 ?  30  TRP C CG    1 
ATOM   11242 C  CD1   . TRP C 2 51  ? 124.341 95.241  116.717 1.00 29.07 ?  30  TRP C CD1   1 
ATOM   11243 C  CD2   . TRP C 2 51  ? 122.602 96.006  117.901 1.00 28.33 ?  30  TRP C CD2   1 
ATOM   11244 N  NE1   . TRP C 2 51  ? 123.720 94.158  117.287 1.00 28.01 ?  30  TRP C NE1   1 
ATOM   11245 C  CE2   . TRP C 2 51  ? 122.648 94.597  118.019 1.00 27.67 ?  30  TRP C CE2   1 
ATOM   11246 C  CE3   . TRP C 2 51  ? 121.593 96.709  118.573 1.00 27.27 ?  30  TRP C CE3   1 
ATOM   11247 C  CZ2   . TRP C 2 51  ? 121.726 93.880  118.780 1.00 26.54 ?  30  TRP C CZ2   1 
ATOM   11248 C  CZ3   . TRP C 2 51  ? 120.668 95.994  119.322 1.00 27.07 ?  30  TRP C CZ3   1 
ATOM   11249 C  CH2   . TRP C 2 51  ? 120.746 94.593  119.425 1.00 26.52 ?  30  TRP C CH2   1 
ATOM   11250 N  N     . LEU C 2 52  ? 123.765 99.484  119.213 1.00 30.65 ?  31  LEU C N     1 
ATOM   11251 C  CA    . LEU C 2 52  ? 123.111 99.644  120.514 1.00 30.38 ?  31  LEU C CA    1 
ATOM   11252 C  C     . LEU C 2 52  ? 121.600 99.731  120.319 1.00 30.51 ?  31  LEU C C     1 
ATOM   11253 O  O     . LEU C 2 52  ? 121.148 100.344 119.350 1.00 30.77 ?  31  LEU C O     1 
ATOM   11254 C  CB    . LEU C 2 52  ? 123.617 100.907 121.230 1.00 30.45 ?  31  LEU C CB    1 
ATOM   11255 C  CG    . LEU C 2 52  ? 125.097 100.902 121.625 1.00 30.29 ?  31  LEU C CG    1 
ATOM   11256 C  CD1   . LEU C 2 52  ? 125.633 102.316 121.889 1.00 30.69 ?  31  LEU C CD1   1 
ATOM   11257 C  CD2   . LEU C 2 52  ? 125.346 99.970  122.821 1.00 29.91 ?  31  LEU C CD2   1 
ATOM   11258 N  N     . PRO C 2 53  ? 120.809 99.130  121.237 1.00 30.73 ?  32  PRO C N     1 
ATOM   11259 C  CA    . PRO C 2 53  ? 119.344 99.142  121.089 1.00 31.17 ?  32  PRO C CA    1 
ATOM   11260 C  C     . PRO C 2 53  ? 118.750 100.546 120.997 1.00 32.18 ?  32  PRO C C     1 
ATOM   11261 O  O     . PRO C 2 53  ? 117.725 100.735 120.322 1.00 32.66 ?  32  PRO C O     1 
ATOM   11262 C  CB    . PRO C 2 53  ? 118.847 98.440  122.358 1.00 30.99 ?  32  PRO C CB    1 
ATOM   11263 C  CG    . PRO C 2 53  ? 120.022 98.446  123.308 1.00 30.50 ?  32  PRO C CG    1 
ATOM   11264 C  CD    . PRO C 2 53  ? 121.227 98.374  122.435 1.00 30.46 ?  32  PRO C CD    1 
ATOM   11265 N  N     . GLU C 2 54  ? 119.395 101.515 121.651 1.00 32.62 ?  33  GLU C N     1 
ATOM   11266 C  CA    . GLU C 2 54  ? 118.942 102.915 121.640 1.00 33.44 ?  33  GLU C CA    1 
ATOM   11267 C  C     . GLU C 2 54  ? 118.940 103.551 120.244 1.00 33.59 ?  33  GLU C C     1 
ATOM   11268 O  O     . GLU C 2 54  ? 118.318 104.591 120.044 1.00 34.05 ?  33  GLU C O     1 
ATOM   11269 C  CB    . GLU C 2 54  ? 119.769 103.783 122.606 1.00 33.72 ?  33  GLU C CB    1 
ATOM   11270 C  CG    . GLU C 2 54  ? 119.496 103.533 124.102 1.00 34.53 ?  33  GLU C CG    1 
ATOM   11271 C  CD    . GLU C 2 54  ? 120.114 102.233 124.617 1.00 35.09 ?  33  GLU C CD    1 
ATOM   11272 O  OE1   . GLU C 2 54  ? 121.086 101.732 123.996 1.00 34.38 ?  33  GLU C OE1   1 
ATOM   11273 O  OE2   . GLU C 2 54  ? 119.623 101.711 125.644 1.00 35.53 -1 33  GLU C OE2   1 
ATOM   11274 N  N     . GLU C 2 55  ? 119.634 102.927 119.289 1.00 33.82 ?  34  GLU C N     1 
ATOM   11275 C  CA    . GLU C 2 55  ? 119.626 103.378 117.895 1.00 34.19 ?  34  GLU C CA    1 
ATOM   11276 C  C     . GLU C 2 55  ? 118.246 103.188 117.247 1.00 33.83 ?  34  GLU C C     1 
ATOM   11277 O  O     . GLU C 2 55  ? 117.932 103.835 116.249 1.00 33.93 ?  34  GLU C O     1 
ATOM   11278 C  CB    . GLU C 2 55  ? 120.680 102.631 117.058 1.00 34.52 ?  34  GLU C CB    1 
ATOM   11279 C  CG    . GLU C 2 55  ? 122.134 102.835 117.475 1.00 36.50 ?  34  GLU C CG    1 
ATOM   11280 C  CD    . GLU C 2 55  ? 123.116 102.293 116.440 1.00 40.03 ?  34  GLU C CD    1 
ATOM   11281 O  OE1   . GLU C 2 55  ? 123.437 103.018 115.472 1.00 42.43 ?  34  GLU C OE1   1 
ATOM   11282 O  OE2   . GLU C 2 55  ? 123.577 101.146 116.594 1.00 39.35 -1 34  GLU C OE2   1 
ATOM   11283 N  N     . ILE C 2 56  ? 117.453 102.276 117.809 1.00 33.31 ?  35  ILE C N     1 
ATOM   11284 C  CA    . ILE C 2 56  ? 116.126 101.921 117.303 1.00 33.14 ?  35  ILE C CA    1 
ATOM   11285 C  C     . ILE C 2 56  ? 115.062 102.485 118.250 1.00 32.58 ?  35  ILE C C     1 
ATOM   11286 O  O     . ILE C 2 56  ? 115.010 102.104 119.414 1.00 32.12 ?  35  ILE C O     1 
ATOM   11287 C  CB    . ILE C 2 56  ? 115.953 100.366 117.214 1.00 33.03 ?  35  ILE C CB    1 
ATOM   11288 C  CG1   . ILE C 2 56  ? 117.113 99.696  116.447 1.00 34.76 ?  35  ILE C CG1   1 
ATOM   11289 C  CG2   . ILE C 2 56  ? 114.586 99.981  116.634 1.00 33.61 ?  35  ILE C CG2   1 
ATOM   11290 C  CD1   . ILE C 2 56  ? 117.190 100.009 114.950 1.00 36.75 ?  35  ILE C CD1   1 
ATOM   11291 N  N     . ALA C 2 57  ? 114.227 103.398 117.757 1.00 32.36 ?  36  ALA C N     1 
ATOM   11292 C  CA    . ALA C 2 57  ? 113.118 103.929 118.555 1.00 32.17 ?  36  ALA C CA    1 
ATOM   11293 C  C     . ALA C 2 57  ? 111.968 102.917 118.592 1.00 31.76 ?  36  ALA C C     1 
ATOM   11294 O  O     . ALA C 2 57  ? 111.566 102.389 117.553 1.00 31.95 ?  36  ALA C O     1 
ATOM   11295 C  CB    . ALA C 2 57  ? 112.646 105.259 117.989 1.00 33.01 ?  36  ALA C CB    1 
ATOM   11296 N  N     . LEU C 2 58  ? 111.441 102.649 119.782 1.00 30.68 ?  37  LEU C N     1 
ATOM   11297 C  CA    . LEU C 2 58  ? 110.518 101.529 119.960 1.00 30.14 ?  37  LEU C CA    1 
ATOM   11298 C  C     . LEU C 2 58  ? 109.051 101.916 120.108 1.00 30.21 ?  37  LEU C C     1 
ATOM   11299 O  O     . LEU C 2 58  ? 108.169 101.050 120.039 1.00 29.91 ?  37  LEU C O     1 
ATOM   11300 C  CB    . LEU C 2 58  ? 110.964 100.655 121.138 1.00 29.46 ?  37  LEU C CB    1 
ATOM   11301 C  CG    . LEU C 2 58  ? 112.280 99.891  120.937 1.00 29.08 ?  37  LEU C CG    1 
ATOM   11302 C  CD1   . LEU C 2 58  ? 112.711 99.209  122.223 1.00 29.23 ?  37  LEU C CD1   1 
ATOM   11303 C  CD2   . LEU C 2 58  ? 112.166 98.869  119.806 1.00 28.84 ?  37  LEU C CD2   1 
ATOM   11304 N  N     . ASN C 2 59  ? 108.792 103.208 120.285 1.00 30.50 ?  38  ASN C N     1 
ATOM   11305 C  CA    . ASN C 2 59  ? 107.426 103.698 120.491 1.00 31.23 ?  38  ASN C CA    1 
ATOM   11306 C  C     . ASN C 2 59  ? 106.477 103.424 119.312 1.00 31.03 ?  38  ASN C C     1 
ATOM   11307 O  O     . ASN C 2 59  ? 105.262 103.413 119.483 1.00 30.82 ?  38  ASN C O     1 
ATOM   11308 C  CB    . ASN C 2 59  ? 107.419 105.182 120.907 1.00 31.98 ?  38  ASN C CB    1 
ATOM   11309 C  CG    . ASN C 2 59  ? 108.092 106.089 119.890 1.00 33.59 ?  38  ASN C CG    1 
ATOM   11310 O  OD1   . ASN C 2 59  ? 109.254 105.882 119.520 1.00 36.48 ?  38  ASN C OD1   1 
ATOM   11311 N  ND2   . ASN C 2 59  ? 107.369 107.112 119.441 1.00 34.77 ?  38  ASN C ND2   1 
ATOM   11312 N  N     . GLY C 2 60  ? 107.047 103.170 118.135 1.00 30.88 ?  39  GLY C N     1 
ATOM   11313 C  CA    . GLY C 2 60  ? 106.277 102.761 116.954 1.00 31.37 ?  39  GLY C CA    1 
ATOM   11314 C  C     . GLY C 2 60  ? 105.581 101.409 117.057 1.00 31.05 ?  39  GLY C C     1 
ATOM   11315 O  O     . GLY C 2 60  ? 104.572 101.197 116.399 1.00 31.21 ?  39  GLY C O     1 
ATOM   11316 N  N     . ASP C 2 61  ? 106.107 100.502 117.883 1.00 30.63 ?  40  ASP C N     1 
ATOM   11317 C  CA    . ASP C 2 61  ? 105.449 99.209  118.155 1.00 30.65 ?  40  ASP C CA    1 
ATOM   11318 C  C     . ASP C 2 61  ? 104.271 99.277  119.133 1.00 31.00 ?  40  ASP C C     1 
ATOM   11319 O  O     . ASP C 2 61  ? 103.568 98.280  119.306 1.00 30.91 ?  40  ASP C O     1 
ATOM   11320 C  CB    . ASP C 2 61  ? 106.448 98.186  118.710 1.00 30.00 ?  40  ASP C CB    1 
ATOM   11321 C  CG    . ASP C 2 61  ? 107.496 97.775  117.704 1.00 30.88 ?  40  ASP C CG    1 
ATOM   11322 O  OD1   . ASP C 2 61  ? 107.490 98.284  116.558 1.00 30.42 ?  40  ASP C OD1   1 
ATOM   11323 O  OD2   . ASP C 2 61  ? 108.342 96.933  118.076 1.00 31.17 -1 40  ASP C OD2   1 
ATOM   11324 N  N     . LEU C 2 62  ? 104.068 100.425 119.778 1.00 31.54 ?  41  LEU C N     1 
ATOM   11325 C  CA    . LEU C 2 62  ? 103.075 100.544 120.859 1.00 32.47 ?  41  LEU C CA    1 
ATOM   11326 C  C     . LEU C 2 62  ? 101.671 100.096 120.471 1.00 33.21 ?  41  LEU C C     1 
ATOM   11327 O  O     . LEU C 2 62  ? 100.991 99.421  121.252 1.00 32.84 ?  41  LEU C O     1 
ATOM   11328 C  CB    . LEU C 2 62  ? 103.027 101.968 121.417 1.00 33.14 ?  41  LEU C CB    1 
ATOM   11329 C  CG    . LEU C 2 62  ? 104.044 102.339 122.496 1.00 34.44 ?  41  LEU C CG    1 
ATOM   11330 C  CD1   . LEU C 2 62  ? 104.053 103.847 122.704 1.00 35.04 ?  41  LEU C CD1   1 
ATOM   11331 C  CD2   . LEU C 2 62  ? 103.738 101.604 123.807 1.00 35.52 ?  41  LEU C CD2   1 
ATOM   11332 N  N     . LEU C 2 63  ? 101.245 100.466 119.265 1.00 33.75 ?  42  LEU C N     1 
ATOM   11333 C  CA    . LEU C 2 63  ? 99.909  100.118 118.802 1.00 34.79 ?  42  LEU C CA    1 
ATOM   11334 C  C     . LEU C 2 63  ? 99.735  98.666  118.361 1.00 34.66 ?  42  LEU C C     1 
ATOM   11335 O  O     . LEU C 2 63  ? 98.757  98.035  118.758 1.00 34.67 ?  42  LEU C O     1 
ATOM   11336 C  CB    . LEU C 2 63  ? 99.414  101.088 117.726 1.00 35.27 ?  42  LEU C CB    1 
ATOM   11337 C  CG    . LEU C 2 63  ? 98.827  102.387 118.293 1.00 36.82 ?  42  LEU C CG    1 
ATOM   11338 C  CD1   . LEU C 2 63  ? 98.404  103.301 117.149 1.00 37.93 ?  42  LEU C CD1   1 
ATOM   11339 C  CD2   . LEU C 2 63  ? 97.641  102.125 119.221 1.00 37.85 ?  42  LEU C CD2   1 
ATOM   11340 N  N     . THR C 2 64  ? 100.656 98.131  117.555 1.00 34.70 ?  43  THR C N     1 
ATOM   11341 C  CA    . THR C 2 64  ? 100.553 96.714  117.168 1.00 35.10 ?  43  THR C CA    1 
ATOM   11342 C  C     . THR C 2 64  ? 100.671 95.778  118.382 1.00 34.78 ?  43  THR C C     1 
ATOM   11343 O  O     . THR C 2 64  ? 100.134 94.676  118.363 1.00 35.04 ?  43  THR C O     1 
ATOM   11344 C  CB    . THR C 2 64  ? 101.516 96.285  116.017 1.00 35.30 ?  43  THR C CB    1 
ATOM   11345 O  OG1   . THR C 2 64  ? 102.878 96.588  116.355 1.00 36.01 ?  43  THR C OG1   1 
ATOM   11346 C  CG2   . THR C 2 64  ? 101.141 96.973  114.705 1.00 35.96 ?  43  THR C CG2   1 
ATOM   11347 N  N     . TRP C 2 65  ? 101.343 96.235  119.441 1.00 34.63 ?  44  TRP C N     1 
ATOM   11348 C  CA    . TRP C 2 65  ? 101.433 95.477  120.696 1.00 34.37 ?  44  TRP C CA    1 
ATOM   11349 C  C     . TRP C 2 65  ? 100.102 95.488  121.447 1.00 35.13 ?  44  TRP C C     1 
ATOM   11350 O  O     . TRP C 2 65  ? 99.596  94.439  121.866 1.00 34.98 ?  44  TRP C O     1 
ATOM   11351 C  CB    . TRP C 2 65  ? 102.537 96.044  121.587 1.00 33.95 ?  44  TRP C CB    1 
ATOM   11352 C  CG    . TRP C 2 65  ? 102.557 95.471  122.968 1.00 33.26 ?  44  TRP C CG    1 
ATOM   11353 C  CD1   . TRP C 2 65  ? 102.106 96.066  124.113 1.00 32.51 ?  44  TRP C CD1   1 
ATOM   11354 C  CD2   . TRP C 2 65  ? 103.061 94.184  123.354 1.00 30.93 ?  44  TRP C CD2   1 
ATOM   11355 N  NE1   . TRP C 2 65  ? 102.303 95.230  125.192 1.00 31.66 ?  44  TRP C NE1   1 
ATOM   11356 C  CE2   . TRP C 2 65  ? 102.887 94.069  124.753 1.00 30.39 ?  44  TRP C CE2   1 
ATOM   11357 C  CE3   . TRP C 2 65  ? 103.647 93.121  122.654 1.00 30.36 ?  44  TRP C CE3   1 
ATOM   11358 C  CZ2   . TRP C 2 65  ? 103.268 92.929  125.464 1.00 29.16 ?  44  TRP C CZ2   1 
ATOM   11359 C  CZ3   . TRP C 2 65  ? 104.033 91.982  123.364 1.00 28.84 ?  44  TRP C CZ3   1 
ATOM   11360 C  CH2   . TRP C 2 65  ? 103.846 91.901  124.755 1.00 29.34 ?  44  TRP C CH2   1 
ATOM   11361 N  N     . LYS C 2 66  ? 99.557  96.690  121.624 1.00 35.69 ?  45  LYS C N     1 
ATOM   11362 C  CA    . LYS C 2 66  ? 98.255  96.889  122.243 1.00 36.38 ?  45  LYS C CA    1 
ATOM   11363 C  C     . LYS C 2 66  ? 97.175  95.995  121.622 1.00 36.24 ?  45  LYS C C     1 
ATOM   11364 O  O     . LYS C 2 66  ? 96.281  95.540  122.326 1.00 36.78 ?  45  LYS C O     1 
ATOM   11365 C  CB    . LYS C 2 66  ? 97.860  98.361  122.108 1.00 37.14 ?  45  LYS C CB    1 
ATOM   11366 C  CG    . LYS C 2 66  ? 96.538  98.746  122.750 1.00 38.91 ?  45  LYS C CG    1 
ATOM   11367 C  CD    . LYS C 2 66  ? 96.137  100.162 122.333 1.00 41.12 ?  45  LYS C CD    1 
ATOM   11368 C  CE    . LYS C 2 66  ? 95.022  100.699 123.215 1.00 43.00 ?  45  LYS C CE    1 
ATOM   11369 N  NZ    . LYS C 2 66  ? 95.334  100.516 124.665 1.00 44.38 1  45  LYS C NZ    1 
ATOM   11370 N  N     . TYR C 2 67  ? 97.302  95.726  120.319 1.00 36.03 ?  46  TYR C N     1 
ATOM   11371 C  CA    . TYR C 2 67  ? 96.296  95.008  119.518 1.00 36.03 ?  46  TYR C CA    1 
ATOM   11372 C  C     . TYR C 2 67  ? 96.378  93.477  119.581 1.00 35.25 ?  46  TYR C C     1 
ATOM   11373 O  O     . TYR C 2 67  ? 95.469  92.781  119.117 1.00 35.32 ?  46  TYR C O     1 
ATOM   11374 C  CB    . TYR C 2 67  ? 96.382  95.433  118.041 1.00 36.60 ?  46  TYR C CB    1 
ATOM   11375 C  CG    . TYR C 2 67  ? 96.099  96.903  117.761 1.00 37.85 ?  46  TYR C CG    1 
ATOM   11376 C  CD1   . TYR C 2 67  ? 95.496  97.718  118.718 1.00 38.97 ?  46  TYR C CD1   1 
ATOM   11377 C  CD2   . TYR C 2 67  ? 96.423  97.471  116.520 1.00 40.06 ?  46  TYR C CD2   1 
ATOM   11378 C  CE1   . TYR C 2 67  ? 95.242  99.065  118.470 1.00 40.36 ?  46  TYR C CE1   1 
ATOM   11379 C  CE2   . TYR C 2 67  ? 96.167  98.826  116.256 1.00 40.53 ?  46  TYR C CE2   1 
ATOM   11380 C  CZ    . TYR C 2 67  ? 95.572  99.614  117.241 1.00 41.43 ?  46  TYR C CZ    1 
ATOM   11381 O  OH    . TYR C 2 67  ? 95.296  100.950 117.012 1.00 41.48 ?  46  TYR C OH    1 
ATOM   11382 N  N     . LEU C 2 68  ? 97.472  92.954  120.129 1.00 33.80 ?  47  LEU C N     1 
ATOM   11383 C  CA    . LEU C 2 68  ? 97.636  91.511  120.260 1.00 32.77 ?  47  LEU C CA    1 
ATOM   11384 C  C     . LEU C 2 68  ? 96.758  90.980  121.386 1.00 31.84 ?  47  LEU C C     1 
ATOM   11385 O  O     . LEU C 2 68  ? 96.501  91.682  122.361 1.00 31.90 ?  47  LEU C O     1 
ATOM   11386 C  CB    . LEU C 2 68  ? 99.096  91.153  120.546 1.00 32.39 ?  47  LEU C CB    1 
ATOM   11387 C  CG    . LEU C 2 68  ? 100.201 91.432  119.524 1.00 32.68 ?  47  LEU C CG    1 
ATOM   11388 C  CD1   . LEU C 2 68  ? 101.541 90.980  120.096 1.00 33.03 ?  47  LEU C CD1   1 
ATOM   11389 C  CD2   . LEU C 2 68  ? 99.937  90.756  118.174 1.00 32.78 ?  47  LEU C CD2   1 
ATOM   11390 N  N     . GLY C 2 69  ? 96.316  89.735  121.256 1.00 30.99 ?  48  GLY C N     1 
ATOM   11391 C  CA    . GLY C 2 69  ? 95.593  89.067  122.337 1.00 30.58 ?  48  GLY C CA    1 
ATOM   11392 C  C     . GLY C 2 69  ? 96.459  88.856  123.572 1.00 29.87 ?  48  GLY C C     1 
ATOM   11393 O  O     . GLY C 2 69  ? 97.686  88.909  123.496 1.00 28.79 ?  48  GLY C O     1 
ATOM   11394 N  N     . LYS C 2 70  ? 95.820  88.627  124.715 1.00 29.89 ?  49  LYS C N     1 
ATOM   11395 C  CA    . LYS C 2 70  ? 96.548  88.384  125.960 1.00 29.49 ?  49  LYS C CA    1 
ATOM   11396 C  C     . LYS C 2 70  ? 97.481  87.163  125.856 1.00 28.74 ?  49  LYS C C     1 
ATOM   11397 O  O     . LYS C 2 70  ? 98.609  87.199  126.365 1.00 27.27 ?  49  LYS C O     1 
ATOM   11398 C  CB    . LYS C 2 70  ? 95.584  88.271  127.145 1.00 30.67 ?  49  LYS C CB    1 
ATOM   11399 C  CG    . LYS C 2 70  ? 95.092  89.648  127.657 1.00 33.73 ?  49  LYS C CG    1 
ATOM   11400 C  CD    . LYS C 2 70  ? 93.839  89.550  128.544 1.00 38.93 ?  49  LYS C CD    1 
ATOM   11401 C  CE    . LYS C 2 70  ? 94.143  89.104  129.980 1.00 41.04 ?  49  LYS C CE    1 
ATOM   11402 N  NZ    . LYS C 2 70  ? 94.822  90.153  130.798 1.00 42.21 1  49  LYS C NZ    1 
ATOM   11403 N  N     . ASN C 2 71  ? 97.008  86.109  125.184 1.00 27.54 ?  50  ASN C N     1 
ATOM   11404 C  CA    . ASN C 2 71  ? 97.817  84.917  124.918 1.00 27.00 ?  50  ASN C CA    1 
ATOM   11405 C  C     . ASN C 2 71  ? 99.081  85.231  124.118 1.00 26.19 ?  50  ASN C C     1 
ATOM   11406 O  O     . ASN C 2 71  ? 100.175 84.711  124.422 1.00 25.38 ?  50  ASN C O     1 
ATOM   11407 C  CB    . ASN C 2 71  ? 96.988  83.830  124.198 1.00 27.08 ?  50  ASN C CB    1 
ATOM   11408 C  CG    . ASN C 2 71  ? 96.422  84.288  122.833 1.00 28.69 ?  50  ASN C CG    1 
ATOM   11409 O  OD1   . ASN C 2 71  ? 95.898  85.408  122.682 1.00 30.45 ?  50  ASN C OD1   1 
ATOM   11410 N  ND2   . ASN C 2 71  ? 96.505  83.394  121.835 1.00 29.42 ?  50  ASN C ND2   1 
ATOM   11411 N  N     . GLU C 2 72  ? 98.923  86.078  123.102 1.00 24.91 ?  51  GLU C N     1 
ATOM   11412 C  CA    . GLU C 2 72  ? 100.030 86.449  122.229 1.00 24.97 ?  51  GLU C CA    1 
ATOM   11413 C  C     . GLU C 2 72  ? 101.081 87.277  122.976 1.00 24.45 ?  51  GLU C C     1 
ATOM   11414 O  O     . GLU C 2 72  ? 102.289 87.027  122.848 1.00 23.90 ?  51  GLU C O     1 
ATOM   11415 C  CB    . GLU C 2 72  ? 99.511  87.208  121.006 1.00 25.27 ?  51  GLU C CB    1 
ATOM   11416 C  CG    . GLU C 2 72  ? 98.640  86.367  120.075 1.00 26.16 ?  51  GLU C CG    1 
ATOM   11417 C  CD    . GLU C 2 72  ? 98.107  87.182  118.904 1.00 28.70 ?  51  GLU C CD    1 
ATOM   11418 O  OE1   . GLU C 2 72  ? 97.158  87.965  119.108 1.00 28.70 ?  51  GLU C OE1   1 
ATOM   11419 O  OE2   . GLU C 2 72  ? 98.637  87.039  117.780 1.00 28.92 -1 51  GLU C OE2   1 
ATOM   11420 N  N     . GLN C 2 73  ? 100.612 88.239  123.770 1.00 23.75 ?  52  GLN C N     1 
ATOM   11421 C  CA    . GLN C 2 73  ? 101.503 89.079  124.566 1.00 23.94 ?  52  GLN C CA    1 
ATOM   11422 C  C     . GLN C 2 73  ? 102.259 88.250  125.606 1.00 23.36 ?  52  GLN C C     1 
ATOM   11423 O  O     . GLN C 2 73  ? 103.437 88.488  125.848 1.00 22.95 ?  52  GLN C O     1 
ATOM   11424 C  CB    . GLN C 2 73  ? 100.722 90.197  125.273 1.00 24.28 ?  52  GLN C CB    1 
ATOM   11425 C  CG    . GLN C 2 73  ? 100.225 91.335  124.359 1.00 25.22 ?  52  GLN C CG    1 
ATOM   11426 C  CD    . GLN C 2 73  ? 99.538  92.469  125.129 1.00 29.02 ?  52  GLN C CD    1 
ATOM   11427 O  OE1   . GLN C 2 73  ? 99.411  92.418  126.351 1.00 32.08 ?  52  GLN C OE1   1 
ATOM   11428 N  NE2   . GLN C 2 73  ? 99.096  93.493  124.409 1.00 29.13 ?  52  GLN C NE2   1 
ATOM   11429 N  N     . ASP C 2 74  ? 101.560 87.302  126.232 1.00 23.02 ?  53  ASP C N     1 
ATOM   11430 C  CA    . ASP C 2 74  ? 102.153 86.428  127.236 1.00 23.44 ?  53  ASP C CA    1 
ATOM   11431 C  C     . ASP C 2 74  ? 103.291 85.599  126.626 1.00 23.00 ?  53  ASP C C     1 
ATOM   11432 O  O     . ASP C 2 74  ? 104.385 85.549  127.180 1.00 22.96 ?  53  ASP C O     1 
ATOM   11433 C  CB    . ASP C 2 74  ? 101.091 85.499  127.840 1.00 23.31 ?  53  ASP C CB    1 
ATOM   11434 C  CG    . ASP C 2 74  ? 101.619 84.692  129.009 1.00 25.80 ?  53  ASP C CG    1 
ATOM   11435 O  OD1   . ASP C 2 74  ? 102.045 85.297  130.026 1.00 27.95 ?  53  ASP C OD1   1 
ATOM   11436 O  OD2   . ASP C 2 74  ? 101.599 83.449  128.914 1.00 26.30 -1 53  ASP C OD2   1 
ATOM   11437 N  N     . THR C 2 75  ? 103.013 84.946  125.500 1.00 22.20 ?  54  THR C N     1 
ATOM   11438 C  CA    . THR C 2 75  ? 104.010 84.139  124.809 1.00 21.84 ?  54  THR C CA    1 
ATOM   11439 C  C     . THR C 2 75  ? 105.193 85.003  124.385 1.00 22.09 ?  54  THR C C     1 
ATOM   11440 O  O     . THR C 2 75  ? 106.341 84.617  124.578 1.00 21.88 ?  54  THR C O     1 
ATOM   11441 C  CB    . THR C 2 75  ? 103.405 83.379  123.596 1.00 21.74 ?  54  THR C CB    1 
ATOM   11442 O  OG1   . THR C 2 75  ? 102.460 82.424  124.080 1.00 22.09 ?  54  THR C OG1   1 
ATOM   11443 C  CG2   . THR C 2 75  ? 104.490 82.620  122.820 1.00 19.76 ?  54  THR C CG2   1 
ATOM   11444 N  N     . TYR C 2 76  ? 104.907 86.174  123.825 1.00 22.38 ?  55  TYR C N     1 
ATOM   11445 C  CA    . TYR C 2 76  ? 105.961 87.092  123.401 1.00 22.85 ?  55  TYR C CA    1 
ATOM   11446 C  C     . TYR C 2 76  ? 106.899 87.501  124.550 1.00 22.56 ?  55  TYR C C     1 
ATOM   11447 O  O     . TYR C 2 76  ? 108.115 87.455  124.387 1.00 21.97 ?  55  TYR C O     1 
ATOM   11448 C  CB    . TYR C 2 76  ? 105.355 88.325  122.744 1.00 23.57 ?  55  TYR C CB    1 
ATOM   11449 C  CG    . TYR C 2 76  ? 106.322 89.152  121.922 1.00 25.59 ?  55  TYR C CG    1 
ATOM   11450 C  CD1   . TYR C 2 76  ? 106.486 88.915  120.553 1.00 27.49 ?  55  TYR C CD1   1 
ATOM   11451 C  CD2   . TYR C 2 76  ? 107.046 90.193  122.503 1.00 27.70 ?  55  TYR C CD2   1 
ATOM   11452 C  CE1   . TYR C 2 76  ? 107.359 89.694  119.785 1.00 30.28 ?  55  TYR C CE1   1 
ATOM   11453 C  CE2   . TYR C 2 76  ? 107.928 90.976  121.746 1.00 30.38 ?  55  TYR C CE2   1 
ATOM   11454 C  CZ    . TYR C 2 76  ? 108.079 90.718  120.389 1.00 31.39 ?  55  TYR C CZ    1 
ATOM   11455 O  OH    . TYR C 2 76  ? 108.939 91.498  119.639 1.00 32.67 ?  55  TYR C OH    1 
ATOM   11456 N  N     . MET C 2 77  ? 106.334 87.903  125.691 1.00 23.14 ?  56  MET C N     1 
ATOM   11457 C  CA    . MET C 2 77  ? 107.130 88.307  126.866 1.00 23.90 ?  56  MET C CA    1 
ATOM   11458 C  C     . MET C 2 77  ? 108.020 87.164  127.336 1.00 23.24 ?  56  MET C C     1 
ATOM   11459 O  O     . MET C 2 77  ? 109.195 87.359  127.674 1.00 22.47 ?  56  MET C O     1 
ATOM   11460 C  CB    . MET C 2 77  ? 106.227 88.713  128.036 1.00 24.38 ?  56  MET C CB    1 
ATOM   11461 C  CG    . MET C 2 77  ? 105.369 89.951  127.822 1.00 28.52 ?  56  MET C CG    1 
ATOM   11462 S  SD    . MET C 2 77  ? 106.304 91.471  127.928 1.00 34.32 ?  56  MET C SD    1 
ATOM   11463 C  CE    . MET C 2 77  ? 106.804 91.476  129.653 1.00 33.84 ?  56  MET C CE    1 
ATOM   11464 N  N     . LYS C 2 78  ? 107.440 85.967  127.364 1.00 23.25 ?  57  LYS C N     1 
ATOM   11465 C  CA    . LYS C 2 78  ? 108.114 84.808  127.934 1.00 22.98 ?  57  LYS C CA    1 
ATOM   11466 C  C     . LYS C 2 78  ? 109.248 84.365  127.021 1.00 22.77 ?  57  LYS C C     1 
ATOM   11467 O  O     . LYS C 2 78  ? 110.344 84.066  127.487 1.00 22.56 ?  57  LYS C O     1 
ATOM   11468 C  CB    . LYS C 2 78  ? 107.106 83.686  128.213 1.00 22.99 ?  57  LYS C CB    1 
ATOM   11469 C  CG    . LYS C 2 78  ? 106.261 83.954  129.461 1.00 24.86 ?  57  LYS C CG    1 
ATOM   11470 C  CD    . LYS C 2 78  ? 105.130 82.940  129.632 1.00 27.37 ?  57  LYS C CD    1 
ATOM   11471 C  CE    . LYS C 2 78  ? 104.464 83.086  131.006 1.00 28.99 ?  57  LYS C CE    1 
ATOM   11472 N  NZ    . LYS C 2 78  ? 103.244 82.229  131.072 1.00 29.82 1  57  LYS C NZ    1 
ATOM   11473 N  N     . VAL C 2 79  ? 108.967 84.356  125.720 1.00 22.70 ?  58  VAL C N     1 
ATOM   11474 C  CA    . VAL C 2 79  ? 109.942 84.066  124.671 1.00 23.48 ?  58  VAL C CA    1 
ATOM   11475 C  C     . VAL C 2 79  ? 111.194 84.968  124.797 1.00 23.04 ?  58  VAL C C     1 
ATOM   11476 O  O     . VAL C 2 79  ? 112.336 84.468  124.840 1.00 22.83 ?  58  VAL C O     1 
ATOM   11477 C  CB    . VAL C 2 79  ? 109.224 84.166  123.288 1.00 24.24 ?  58  VAL C CB    1 
ATOM   11478 C  CG1   . VAL C 2 79  ? 110.106 84.743  122.195 1.00 25.71 ?  58  VAL C CG1   1 
ATOM   11479 C  CG2   . VAL C 2 79  ? 108.608 82.801  122.908 1.00 25.04 ?  58  VAL C CG2   1 
ATOM   11480 N  N     . LEU C 2 80  ? 110.979 86.275  124.909 1.00 22.84 ?  59  LEU C N     1 
ATOM   11481 C  CA    . LEU C 2 80  ? 112.092 87.219  125.036 1.00 23.35 ?  59  LEU C CA    1 
ATOM   11482 C  C     . LEU C 2 80  ? 112.818 87.060  126.377 1.00 22.75 ?  59  LEU C C     1 
ATOM   11483 O  O     . LEU C 2 80  ? 114.031 87.241  126.443 1.00 22.75 ?  59  LEU C O     1 
ATOM   11484 C  CB    . LEU C 2 80  ? 111.635 88.672  124.845 1.00 23.91 ?  59  LEU C CB    1 
ATOM   11485 C  CG    . LEU C 2 80  ? 111.122 89.211  123.495 1.00 26.63 ?  59  LEU C CG    1 
ATOM   11486 C  CD1   . LEU C 2 80  ? 111.173 90.731  123.488 1.00 26.99 ?  59  LEU C CD1   1 
ATOM   11487 C  CD2   . LEU C 2 80  ? 111.892 88.670  122.302 1.00 27.23 ?  59  LEU C CD2   1 
ATOM   11488 N  N     . ALA C 2 81  ? 112.078 86.698  127.428 1.00 22.28 ?  60  ALA C N     1 
ATOM   11489 C  CA    . ALA C 2 81  ? 112.670 86.445  128.745 1.00 22.21 ?  60  ALA C CA    1 
ATOM   11490 C  C     . ALA C 2 81  ? 113.604 85.230  128.714 1.00 22.07 ?  60  ALA C C     1 
ATOM   11491 O  O     . ALA C 2 81  ? 114.683 85.277  129.297 1.00 21.97 ?  60  ALA C O     1 
ATOM   11492 C  CB    . ALA C 2 81  ? 111.576 86.293  129.822 1.00 22.38 ?  60  ALA C CB    1 
ATOM   11493 N  N     . GLY C 2 82  ? 113.197 84.175  127.997 1.00 21.67 ?  61  GLY C N     1 
ATOM   11494 C  CA    . GLY C 2 82  ? 114.020 82.989  127.776 1.00 21.74 ?  61  GLY C CA    1 
ATOM   11495 C  C     . GLY C 2 82  ? 115.293 83.316  127.015 1.00 21.79 ?  61  GLY C C     1 
ATOM   11496 O  O     . GLY C 2 82  ? 116.373 82.785  127.317 1.00 21.93 ?  61  GLY C O     1 
ATOM   11497 N  N     . LEU C 2 83  ? 115.166 84.212  126.038 1.00 21.54 ?  62  LEU C N     1 
ATOM   11498 C  CA    . LEU C 2 83  ? 116.315 84.715  125.286 1.00 21.12 ?  62  LEU C CA    1 
ATOM   11499 C  C     . LEU C 2 83  ? 117.243 85.522  126.183 1.00 20.89 ?  62  LEU C C     1 
ATOM   11500 O  O     . LEU C 2 83  ? 118.463 85.370  126.099 1.00 20.84 ?  62  LEU C O     1 
ATOM   11501 C  CB    . LEU C 2 83  ? 115.874 85.575  124.097 1.00 21.23 ?  62  LEU C CB    1 
ATOM   11502 C  CG    . LEU C 2 83  ? 115.100 84.921  122.944 1.00 21.98 ?  62  LEU C CG    1 
ATOM   11503 C  CD1   . LEU C 2 83  ? 114.611 85.969  121.941 1.00 24.12 ?  62  LEU C CD1   1 
ATOM   11504 C  CD2   . LEU C 2 83  ? 115.926 83.868  122.229 1.00 22.03 ?  62  LEU C CD2   1 
ATOM   11505 N  N     . THR C 2 84  ? 116.661 86.376  127.027 1.00 19.93 ?  63  THR C N     1 
ATOM   11506 C  CA    . THR C 2 84  ? 117.437 87.201  127.950 1.00 19.71 ?  63  THR C CA    1 
ATOM   11507 C  C     . THR C 2 84  ? 118.294 86.334  128.859 1.00 19.63 ?  63  THR C C     1 
ATOM   11508 O  O     . THR C 2 84  ? 119.459 86.657  129.107 1.00 19.62 ?  63  THR C O     1 
ATOM   11509 C  CB    . THR C 2 84  ? 116.527 88.109  128.813 1.00 20.22 ?  63  THR C CB    1 
ATOM   11510 O  OG1   . THR C 2 84  ? 115.619 88.834  127.964 1.00 19.37 ?  63  THR C OG1   1 
ATOM   11511 C  CG2   . THR C 2 84  ? 117.357 89.070  129.629 1.00 19.45 ?  63  THR C CG2   1 
ATOM   11512 N  N     . LEU C 2 85  ? 117.715 85.245  129.357 1.00 19.66 ?  64  LEU C N     1 
ATOM   11513 C  CA    . LEU C 2 85  ? 118.431 84.328  130.241 1.00 20.51 ?  64  LEU C CA    1 
ATOM   11514 C  C     . LEU C 2 85  ? 119.639 83.711  129.529 1.00 20.84 ?  64  LEU C C     1 
ATOM   11515 O  O     . LEU C 2 85  ? 120.753 83.737  130.054 1.00 21.30 ?  64  LEU C O     1 
ATOM   11516 C  CB    . LEU C 2 85  ? 117.499 83.241  130.805 1.00 20.03 ?  64  LEU C CB    1 
ATOM   11517 C  CG    . LEU C 2 85  ? 118.205 82.216  131.722 1.00 21.43 ?  64  LEU C CG    1 
ATOM   11518 C  CD1   . LEU C 2 85  ? 118.731 82.862  133.025 1.00 21.61 ?  64  LEU C CD1   1 
ATOM   11519 C  CD2   . LEU C 2 85  ? 117.319 81.017  132.050 1.00 20.99 ?  64  LEU C CD2   1 
ATOM   11520 N  N     . LEU C 2 86  ? 119.410 83.178  128.334 1.00 21.37 ?  65  LEU C N     1 
ATOM   11521 C  CA    . LEU C 2 86  ? 120.478 82.604  127.513 1.00 21.92 ?  65  LEU C CA    1 
ATOM   11522 C  C     . LEU C 2 86  ? 121.633 83.588  127.261 1.00 21.76 ?  65  LEU C C     1 
ATOM   11523 O  O     . LEU C 2 86  ? 122.797 83.230  127.442 1.00 21.72 ?  65  LEU C O     1 
ATOM   11524 C  CB    . LEU C 2 86  ? 119.922 82.086  126.178 1.00 22.42 ?  65  LEU C CB    1 
ATOM   11525 C  CG    . LEU C 2 86  ? 118.989 80.858  126.129 1.00 24.26 ?  65  LEU C CG    1 
ATOM   11526 C  CD1   . LEU C 2 86  ? 118.483 80.651  124.702 1.00 24.67 ?  65  LEU C CD1   1 
ATOM   11527 C  CD2   . LEU C 2 86  ? 119.687 79.603  126.624 1.00 25.60 ?  65  LEU C CD2   1 
ATOM   11528 N  N     . ASP C 2 87  ? 121.310 84.814  126.845 1.00 21.75 ?  66  ASP C N     1 
ATOM   11529 C  CA    . ASP C 2 87  ? 122.331 85.857  126.623 1.00 21.99 ?  66  ASP C CA    1 
ATOM   11530 C  C     . ASP C 2 87  ? 123.046 86.313  127.900 1.00 21.76 ?  66  ASP C C     1 
ATOM   11531 O  O     . ASP C 2 87  ? 124.236 86.658  127.866 1.00 21.65 ?  66  ASP C O     1 
ATOM   11532 C  CB    . ASP C 2 87  ? 121.720 87.086  125.944 1.00 22.23 ?  66  ASP C CB    1 
ATOM   11533 C  CG    . ASP C 2 87  ? 121.859 87.051  124.448 1.00 24.59 ?  66  ASP C CG    1 
ATOM   11534 O  OD1   . ASP C 2 87  ? 122.947 86.681  123.948 1.00 27.46 ?  66  ASP C OD1   1 
ATOM   11535 O  OD2   . ASP C 2 87  ? 120.876 87.409  123.769 1.00 27.98 -1 66  ASP C OD2   1 
ATOM   11536 N  N     . THR C 2 88  ? 122.310 86.348  129.008 1.00 21.50 ?  67  THR C N     1 
ATOM   11537 C  CA    . THR C 2 88  ? 122.899 86.642  130.309 1.00 21.80 ?  67  THR C CA    1 
ATOM   11538 C  C     . THR C 2 88  ? 124.044 85.659  130.619 1.00 22.04 ?  67  THR C C     1 
ATOM   11539 O  O     . THR C 2 88  ? 125.148 86.077  130.997 1.00 22.21 ?  67  THR C O     1 
ATOM   11540 C  CB    . THR C 2 88  ? 121.832 86.624  131.417 1.00 22.15 ?  67  THR C CB    1 
ATOM   11541 O  OG1   . THR C 2 88  ? 120.839 87.610  131.124 1.00 22.23 ?  67  THR C OG1   1 
ATOM   11542 C  CG2   . THR C 2 88  ? 122.437 86.928  132.791 1.00 21.19 ?  67  THR C CG2   1 
ATOM   11543 N  N     . GLU C 2 89  ? 123.787 84.369  130.425 1.00 21.55 ?  68  GLU C N     1 
ATOM   11544 C  CA    . GLU C 2 89  ? 124.780 83.350  130.741 1.00 21.81 ?  68  GLU C CA    1 
ATOM   11545 C  C     . GLU C 2 89  ? 125.875 83.251  129.667 1.00 21.35 ?  68  GLU C C     1 
ATOM   11546 O  O     . GLU C 2 89  ? 127.036 83.005  129.984 1.00 21.34 ?  68  GLU C O     1 
ATOM   11547 C  CB    . GLU C 2 89  ? 124.106 82.005  131.032 1.00 22.25 ?  68  GLU C CB    1 
ATOM   11548 C  CG    . GLU C 2 89  ? 123.509 81.928  132.467 1.00 24.02 ?  68  GLU C CG    1 
ATOM   11549 C  CD    . GLU C 2 89  ? 124.526 82.289  133.552 1.00 25.78 ?  68  GLU C CD    1 
ATOM   11550 O  OE1   . GLU C 2 89  ? 125.674 81.799  133.498 1.00 26.69 ?  68  GLU C OE1   1 
ATOM   11551 O  OE2   . GLU C 2 89  ? 124.179 83.068  134.471 1.00 28.98 -1 68  GLU C OE2   1 
ATOM   11552 N  N     . GLN C 2 90  ? 125.511 83.496  128.410 1.00 20.82 ?  69  GLN C N     1 
ATOM   11553 C  CA    . GLN C 2 90  ? 126.486 83.519  127.327 1.00 21.28 ?  69  GLN C CA    1 
ATOM   11554 C  C     . GLN C 2 90  ? 127.480 84.671  127.509 1.00 21.24 ?  69  GLN C C     1 
ATOM   11555 O  O     . GLN C 2 90  ? 128.672 84.515  127.230 1.00 20.99 ?  69  GLN C O     1 
ATOM   11556 C  CB    . GLN C 2 90  ? 125.791 83.592  125.955 1.00 21.86 ?  69  GLN C CB    1 
ATOM   11557 C  CG    . GLN C 2 90  ? 126.717 83.264  124.762 1.00 24.29 ?  69  GLN C CG    1 
ATOM   11558 C  CD    . GLN C 2 90  ? 127.127 81.789  124.708 1.00 27.14 ?  69  GLN C CD    1 
ATOM   11559 O  OE1   . GLN C 2 90  ? 127.071 81.079  125.715 1.00 27.13 ?  69  GLN C OE1   1 
ATOM   11560 N  NE2   . GLN C 2 90  ? 127.557 81.332  123.529 1.00 27.69 ?  69  GLN C NE2   1 
ATOM   11561 N  N     . GLY C 2 91  ? 126.986 85.806  128.010 1.00 20.62 ?  70  GLY C N     1 
ATOM   11562 C  CA    . GLY C 2 91  ? 127.821 86.986  128.254 1.00 22.00 ?  70  GLY C CA    1 
ATOM   11563 C  C     . GLY C 2 91  ? 128.607 86.917  129.548 1.00 22.45 ?  70  GLY C C     1 
ATOM   11564 O  O     . GLY C 2 91  ? 129.790 87.250  129.559 1.00 23.53 ?  70  GLY C O     1 
ATOM   11565 N  N     . ASN C 2 92  ? 127.955 86.487  130.630 1.00 22.79 ?  71  ASN C N     1 
ATOM   11566 C  CA    . ASN C 2 92  ? 128.590 86.401  131.955 1.00 23.85 ?  71  ASN C CA    1 
ATOM   11567 C  C     . ASN C 2 92  ? 129.611 85.273  132.045 1.00 24.33 ?  71  ASN C C     1 
ATOM   11568 O  O     . ASN C 2 92  ? 130.630 85.406  132.732 1.00 24.17 ?  71  ASN C O     1 
ATOM   11569 C  CB    . ASN C 2 92  ? 127.549 86.162  133.056 1.00 23.74 ?  71  ASN C CB    1 
ATOM   11570 C  CG    . ASN C 2 92  ? 126.643 87.357  133.303 1.00 24.38 ?  71  ASN C CG    1 
ATOM   11571 O  OD1   . ASN C 2 92  ? 126.735 88.397  132.639 1.00 25.16 ?  71  ASN C OD1   1 
ATOM   11572 N  ND2   . ASN C 2 92  ? 125.748 87.204  134.265 1.00 24.07 ?  71  ASN C ND2   1 
ATOM   11573 N  N     . THR C 2 93  ? 129.334 84.168  131.350 1.00 23.97 ?  72  THR C N     1 
ATOM   11574 C  CA    . THR C 2 93  ? 130.029 82.902  131.627 1.00 24.97 ?  72  THR C CA    1 
ATOM   11575 C  C     . THR C 2 93  ? 130.630 82.275  130.379 1.00 24.52 ?  72  THR C C     1 
ATOM   11576 O  O     . THR C 2 93  ? 131.836 82.070  130.316 1.00 25.39 ?  72  THR C O     1 
ATOM   11577 C  CB    . THR C 2 93  ? 129.086 81.877  132.313 1.00 24.54 ?  72  THR C CB    1 
ATOM   11578 O  OG1   . THR C 2 93  ? 128.499 82.465  133.481 1.00 26.43 ?  72  THR C OG1   1 
ATOM   11579 C  CG2   . THR C 2 93  ? 129.842 80.623  132.721 1.00 26.83 ?  72  THR C CG2   1 
ATOM   11580 N  N     . GLY C 2 94  ? 129.785 81.987  129.400 1.00 24.37 ?  73  GLY C N     1 
ATOM   11581 C  CA    . GLY C 2 94  ? 130.164 81.199  128.216 1.00 24.24 ?  73  GLY C CA    1 
ATOM   11582 C  C     . GLY C 2 94  ? 131.283 81.802  127.394 1.00 24.94 ?  73  GLY C C     1 
ATOM   11583 O  O     . GLY C 2 94  ? 132.346 81.191  127.233 1.00 25.86 ?  73  GLY C O     1 
ATOM   11584 N  N     . MET C 2 95  ? 131.053 83.000  126.870 1.00 24.07 ?  74  MET C N     1 
ATOM   11585 C  CA    . MET C 2 95  ? 132.068 83.651  126.052 1.00 24.35 ?  74  MET C CA    1 
ATOM   11586 C  C     . MET C 2 95  ? 133.368 84.010  126.797 1.00 23.52 ?  74  MET C C     1 
ATOM   11587 O  O     . MET C 2 95  ? 134.437 83.753  126.253 1.00 23.40 ?  74  MET C O     1 
ATOM   11588 C  CB    . MET C 2 95  ? 131.492 84.840  125.283 1.00 24.38 ?  74  MET C CB    1 
ATOM   11589 C  CG    . MET C 2 95  ? 130.538 84.445  124.156 1.00 27.47 ?  74  MET C CG    1 
ATOM   11590 S  SD    . MET C 2 95  ? 131.396 83.465  122.893 1.00 32.54 ?  74  MET C SD    1 
ATOM   11591 C  CE    . MET C 2 95  ? 132.398 84.700  122.146 1.00 34.32 ?  74  MET C CE    1 
ATOM   11592 N  N     . PRO C 2 96  ? 133.286 84.591  128.028 1.00 23.36 ?  75  PRO C N     1 
ATOM   11593 C  CA    . PRO C 2 96  ? 134.519 84.863  128.799 1.00 23.27 ?  75  PRO C CA    1 
ATOM   11594 C  C     . PRO C 2 96  ? 135.343 83.621  129.124 1.00 23.77 ?  75  PRO C C     1 
ATOM   11595 O  O     . PRO C 2 96  ? 136.570 83.669  129.035 1.00 23.46 ?  75  PRO C O     1 
ATOM   11596 C  CB    . PRO C 2 96  ? 133.997 85.472  130.111 1.00 23.55 ?  75  PRO C CB    1 
ATOM   11597 C  CG    . PRO C 2 96  ? 132.690 86.086  129.746 1.00 23.85 ?  75  PRO C CG    1 
ATOM   11598 C  CD    . PRO C 2 96  ? 132.099 85.142  128.711 1.00 22.76 ?  75  PRO C CD    1 
ATOM   11599 N  N     . ILE C 2 97  ? 134.686 82.528  129.517 1.00 23.81 ?  76  ILE C N     1 
ATOM   11600 C  CA    . ILE C 2 97  ? 135.402 81.292  129.842 1.00 24.52 ?  76  ILE C CA    1 
ATOM   11601 C  C     . ILE C 2 97  ? 136.086 80.647  128.617 1.00 23.92 ?  76  ILE C C     1 
ATOM   11602 O  O     . ILE C 2 97  ? 137.236 80.195  128.700 1.00 23.99 ?  76  ILE C O     1 
ATOM   11603 C  CB    . ILE C 2 97  ? 134.508 80.286  130.622 1.00 24.49 ?  76  ILE C CB    1 
ATOM   11604 C  CG1   . ILE C 2 97  ? 135.369 79.307  131.417 1.00 27.08 ?  76  ILE C CG1   1 
ATOM   11605 C  CG2   . ILE C 2 97  ? 133.541 79.522  129.692 1.00 26.06 ?  76  ILE C CG2   1 
ATOM   11606 C  CD1   . ILE C 2 97  ? 134.643 78.722  132.619 1.00 31.37 ?  76  ILE C CD1   1 
ATOM   11607 N  N     . VAL C 2 98  ? 135.396 80.634  127.480 1.00 23.97 ?  77  VAL C N     1 
ATOM   11608 C  CA    . VAL C 2 98  ? 136.010 80.170  126.228 1.00 24.01 ?  77  VAL C CA    1 
ATOM   11609 C  C     . VAL C 2 98  ? 137.187 81.093  125.845 1.00 25.23 ?  77  VAL C C     1 
ATOM   11610 O  O     . VAL C 2 98  ? 138.265 80.614  125.478 1.00 25.77 ?  77  VAL C O     1 
ATOM   11611 C  CB    . VAL C 2 98  ? 134.967 80.053  125.087 1.00 23.98 ?  77  VAL C CB    1 
ATOM   11612 C  CG1   . VAL C 2 98  ? 135.646 79.845  123.736 1.00 23.17 ?  77  VAL C CG1   1 
ATOM   11613 C  CG2   . VAL C 2 98  ? 133.998 78.901  125.384 1.00 22.55 ?  77  VAL C CG2   1 
ATOM   11614 N  N     . ALA C 2 99  ? 136.998 82.407  125.987 1.00 25.42 ?  78  ALA C N     1 
ATOM   11615 C  CA    . ALA C 2 99  ? 138.089 83.363  125.730 1.00 26.72 ?  78  ALA C CA    1 
ATOM   11616 C  C     . ALA C 2 99  ? 139.325 83.041  126.575 1.00 27.46 ?  78  ALA C C     1 
ATOM   11617 O  O     . ALA C 2 99  ? 140.449 83.079  126.075 1.00 28.07 ?  78  ALA C O     1 
ATOM   11618 C  CB    . ALA C 2 99  ? 137.635 84.789  125.979 1.00 26.52 ?  78  ALA C CB    1 
ATOM   11619 N  N     . GLU C 2 100 ? 139.105 82.684  127.840 1.00 28.33 ?  79  GLU C N     1 
ATOM   11620 C  CA    . GLU C 2 100 ? 140.199 82.378  128.764 1.00 29.60 ?  79  GLU C CA    1 
ATOM   11621 C  C     . GLU C 2 100 ? 141.054 81.200  128.289 1.00 29.64 ?  79  GLU C C     1 
ATOM   11622 O  O     . GLU C 2 100 ? 142.280 81.203  128.450 1.00 29.72 ?  79  GLU C O     1 
ATOM   11623 C  CB    . GLU C 2 100 ? 139.657 82.115  130.170 1.00 29.70 ?  79  GLU C CB    1 
ATOM   11624 C  CG    . GLU C 2 100 ? 140.740 81.863  131.218 1.00 33.58 ?  79  GLU C CG    1 
ATOM   11625 C  CD    . GLU C 2 100 ? 140.193 81.478  132.579 1.00 37.83 ?  79  GLU C CD    1 
ATOM   11626 O  OE1   . GLU C 2 100 ? 138.959 81.550  132.800 1.00 40.64 ?  79  GLU C OE1   1 
ATOM   11627 O  OE2   . GLU C 2 100 ? 141.011 81.089  133.440 1.00 41.40 -1 79  GLU C OE2   1 
ATOM   11628 N  N     . HIS C 2 101 ? 140.409 80.204  127.685 1.00 29.43 ?  80  HIS C N     1 
ATOM   11629 C  CA    . HIS C 2 101 ? 141.088 78.960  127.348 1.00 29.74 ?  80  HIS C CA    1 
ATOM   11630 C  C     . HIS C 2 101 ? 141.619 78.878  125.916 1.00 30.18 ?  80  HIS C C     1 
ATOM   11631 O  O     . HIS C 2 101 ? 142.453 78.032  125.615 1.00 30.30 ?  80  HIS C O     1 
ATOM   11632 C  CB    . HIS C 2 101 ? 140.207 77.756  127.719 1.00 29.21 ?  80  HIS C CB    1 
ATOM   11633 C  CG    . HIS C 2 101 ? 140.064 77.567  129.197 1.00 29.60 ?  80  HIS C CG    1 
ATOM   11634 N  ND1   . HIS C 2 101 ? 139.042 78.136  129.928 1.00 30.06 ?  80  HIS C ND1   1 
ATOM   11635 C  CD2   . HIS C 2 101 ? 140.842 76.909  130.089 1.00 29.49 ?  80  HIS C CD2   1 
ATOM   11636 C  CE1   . HIS C 2 101 ? 139.188 77.825  131.205 1.00 29.56 ?  80  HIS C CE1   1 
ATOM   11637 N  NE2   . HIS C 2 101 ? 140.271 77.080  131.329 1.00 30.20 ?  80  HIS C NE2   1 
ATOM   11638 N  N     . VAL C 2 102 ? 141.148 79.767  125.045 1.00 30.70 ?  81  VAL C N     1 
ATOM   11639 C  CA    . VAL C 2 102 ? 141.597 79.814  123.656 1.00 31.47 ?  81  VAL C CA    1 
ATOM   11640 C  C     . VAL C 2 102 ? 142.869 80.655  123.558 1.00 32.45 ?  81  VAL C C     1 
ATOM   11641 O  O     . VAL C 2 102 ? 142.918 81.769  124.093 1.00 32.50 ?  81  VAL C O     1 
ATOM   11642 C  CB    . VAL C 2 102 ? 140.505 80.386  122.713 1.00 31.18 ?  81  VAL C CB    1 
ATOM   11643 C  CG1   . VAL C 2 102 ? 141.058 80.625  121.306 1.00 31.20 ?  81  VAL C CG1   1 
ATOM   11644 C  CG2   . VAL C 2 102 ? 139.316 79.440  122.644 1.00 31.28 ?  81  VAL C CG2   1 
ATOM   11645 N  N     . ASP C 2 103 ? 143.878 80.118  122.869 1.00 33.38 ?  82  ASP C N     1 
ATOM   11646 C  CA    . ASP C 2 103 ? 145.173 80.787  122.715 1.00 34.82 ?  82  ASP C CA    1 
ATOM   11647 C  C     . ASP C 2 103 ? 145.212 81.760  121.542 1.00 34.74 ?  82  ASP C C     1 
ATOM   11648 O  O     . ASP C 2 103 ? 144.646 81.488  120.476 1.00 35.00 ?  82  ASP C O     1 
ATOM   11649 C  CB    . ASP C 2 103 ? 146.303 79.757  122.570 1.00 35.82 ?  82  ASP C CB    1 
ATOM   11650 C  CG    . ASP C 2 103 ? 146.631 79.050  123.882 1.00 38.29 ?  82  ASP C CG    1 
ATOM   11651 O  OD1   . ASP C 2 103 ? 146.500 79.671  124.965 1.00 41.49 ?  82  ASP C OD1   1 
ATOM   11652 O  OD2   . ASP C 2 103 ? 147.025 77.869  123.831 1.00 41.10 -1 82  ASP C OD2   1 
ATOM   11653 N  N     . GLY C 2 104 ? 145.891 82.888  121.750 1.00 34.89 ?  83  GLY C N     1 
ATOM   11654 C  CA    . GLY C 2 104 ? 146.098 83.892  120.701 1.00 35.11 ?  83  GLY C CA    1 
ATOM   11655 C  C     . GLY C 2 104 ? 145.332 85.176  120.956 1.00 34.96 ?  83  GLY C C     1 
ATOM   11656 O  O     . GLY C 2 104 ? 144.106 85.153  121.091 1.00 34.57 ?  83  GLY C O     1 
ATOM   11657 N  N     . HIS C 2 105 ? 146.056 86.297  121.004 1.00 35.02 ?  84  HIS C N     1 
ATOM   11658 C  CA    . HIS C 2 105 ? 145.471 87.600  121.352 1.00 34.83 ?  84  HIS C CA    1 
ATOM   11659 C  C     . HIS C 2 105 ? 144.340 88.045  120.435 1.00 33.77 ?  84  HIS C C     1 
ATOM   11660 O  O     . HIS C 2 105 ? 143.379 88.667  120.891 1.00 33.25 ?  84  HIS C O     1 
ATOM   11661 C  CB    . HIS C 2 105 ? 146.545 88.691  121.446 1.00 36.09 ?  84  HIS C CB    1 
ATOM   11662 C  CG    . HIS C 2 105 ? 147.375 88.608  122.691 1.00 39.17 ?  84  HIS C CG    1 
ATOM   11663 N  ND1   . HIS C 2 105 ? 148.709 88.962  122.723 1.00 43.00 ?  84  HIS C ND1   1 
ATOM   11664 C  CD2   . HIS C 2 105 ? 147.066 88.190  123.943 1.00 41.84 ?  84  HIS C CD2   1 
ATOM   11665 C  CE1   . HIS C 2 105 ? 149.181 88.774  123.945 1.00 43.47 ?  84  HIS C CE1   1 
ATOM   11666 N  NE2   . HIS C 2 105 ? 148.205 88.307  124.704 1.00 43.10 ?  84  HIS C NE2   1 
ATOM   11667 N  N     . GLN C 2 106 ? 144.441 87.714  119.153 1.00 32.84 ?  85  GLN C N     1 
ATOM   11668 C  CA    . GLN C 2 106 ? 143.385 88.073  118.210 1.00 32.29 ?  85  GLN C CA    1 
ATOM   11669 C  C     . GLN C 2 106 ? 142.127 87.216  118.394 1.00 30.88 ?  85  GLN C C     1 
ATOM   11670 O  O     . GLN C 2 106 ? 141.007 87.734  118.326 1.00 30.44 ?  85  GLN C O     1 
ATOM   11671 C  CB    . GLN C 2 106 ? 143.884 87.997  116.776 1.00 32.85 ?  85  GLN C CB    1 
ATOM   11672 C  CG    . GLN C 2 106 ? 144.965 89.020  116.452 1.00 35.55 ?  85  GLN C CG    1 
ATOM   11673 C  CD    . GLN C 2 106 ? 145.512 88.845  115.059 1.00 38.12 ?  85  GLN C CD    1 
ATOM   11674 O  OE1   . GLN C 2 106 ? 144.773 88.526  114.129 1.00 39.96 ?  85  GLN C OE1   1 
ATOM   11675 N  NE2   . GLN C 2 106 ? 146.817 89.056  114.904 1.00 40.39 ?  85  GLN C NE2   1 
ATOM   11676 N  N     . ARG C 2 107 ? 142.314 85.915  118.617 1.00 29.75 ?  86  ARG C N     1 
ATOM   11677 C  CA    . ARG C 2 107 ? 141.184 85.025  118.907 1.00 28.87 ?  86  ARG C CA    1 
ATOM   11678 C  C     . ARG C 2 107 ? 140.494 85.478  120.187 1.00 28.16 ?  86  ARG C C     1 
ATOM   11679 O  O     . ARG C 2 107 ? 139.266 85.514  120.250 1.00 27.55 ?  86  ARG C O     1 
ATOM   11680 C  CB    . ARG C 2 107 ? 141.635 83.571  119.038 1.00 28.48 ?  86  ARG C CB    1 
ATOM   11681 C  CG    . ARG C 2 107 ? 142.025 82.942  117.712 1.00 29.86 ?  86  ARG C CG    1 
ATOM   11682 C  CD    . ARG C 2 107 ? 142.506 81.509  117.875 1.00 30.23 ?  86  ARG C CD    1 
ATOM   11683 N  NE    . ARG C 2 107 ? 142.425 80.834  116.585 1.00 33.04 ?  86  ARG C NE    1 
ATOM   11684 C  CZ    . ARG C 2 107 ? 142.416 79.523  116.415 1.00 31.54 ?  86  ARG C CZ    1 
ATOM   11685 N  NH1   . ARG C 2 107 ? 142.505 78.708  117.456 1.00 31.85 1  86  ARG C NH1   1 
ATOM   11686 N  NH2   . ARG C 2 107 ? 142.325 79.034  115.189 1.00 34.74 ?  86  ARG C NH2   1 
ATOM   11687 N  N     . LYS C 2 108 ? 141.288 85.836  121.195 1.00 27.65 ?  87  LYS C N     1 
ATOM   11688 C  CA    . LYS C 2 108 ? 140.737 86.344  122.455 1.00 27.96 ?  87  LYS C CA    1 
ATOM   11689 C  C     . LYS C 2 108 ? 139.988 87.658  122.285 1.00 27.75 ?  87  LYS C C     1 
ATOM   11690 O  O     . LYS C 2 108 ? 138.969 87.872  122.940 1.00 28.29 ?  87  LYS C O     1 
ATOM   11691 C  CB    . LYS C 2 108 ? 141.820 86.502  123.523 1.00 27.80 ?  87  LYS C CB    1 
ATOM   11692 C  CG    . LYS C 2 108 ? 142.376 85.186  124.027 1.00 29.04 ?  87  LYS C CG    1 
ATOM   11693 C  CD    . LYS C 2 108 ? 143.420 85.442  125.104 1.00 31.15 ?  87  LYS C CD    1 
ATOM   11694 C  CE    . LYS C 2 108 ? 144.154 84.169  125.479 1.00 32.05 ?  87  LYS C CE    1 
ATOM   11695 N  NZ    . LYS C 2 108 ? 143.321 83.319  126.366 1.00 30.88 1  87  LYS C NZ    1 
ATOM   11696 N  N     . ALA C 2 109 ? 140.486 88.532  121.410 1.00 27.69 ?  88  ALA C N     1 
ATOM   11697 C  CA    . ALA C 2 109 ? 139.814 89.810  121.136 1.00 27.46 ?  88  ALA C CA    1 
ATOM   11698 C  C     . ALA C 2 109 ? 138.433 89.625  120.503 1.00 26.87 ?  88  ALA C C     1 
ATOM   11699 O  O     . ALA C 2 109 ? 137.495 90.349  120.833 1.00 26.47 ?  88  ALA C O     1 
ATOM   11700 C  CB    . ALA C 2 109 ? 140.680 90.692  120.260 1.00 27.98 ?  88  ALA C CB    1 
ATOM   11701 N  N     . VAL C 2 110 ? 138.321 88.669  119.582 1.00 25.98 ?  89  VAL C N     1 
ATOM   11702 C  CA    . VAL C 2 110 ? 137.040 88.341  118.952 1.00 25.46 ?  89  VAL C CA    1 
ATOM   11703 C  C     . VAL C 2 110 ? 136.070 87.787  120.001 1.00 24.57 ?  89  VAL C C     1 
ATOM   11704 O  O     . VAL C 2 110 ? 134.935 88.256  120.119 1.00 23.62 ?  89  VAL C O     1 
ATOM   11705 C  CB    . VAL C 2 110 ? 137.221 87.341  117.783 1.00 25.80 ?  89  VAL C CB    1 
ATOM   11706 C  CG1   . VAL C 2 110 ? 135.870 86.810  117.283 1.00 25.44 ?  89  VAL C CG1   1 
ATOM   11707 C  CG2   . VAL C 2 110 ? 137.999 87.995  116.641 1.00 26.23 ?  89  VAL C CG2   1 
ATOM   11708 N  N     . LEU C 2 111 ? 136.537 86.815  120.782 1.00 24.33 ?  90  LEU C N     1 
ATOM   11709 C  CA    . LEU C 2 111 ? 135.694 86.205  121.810 1.00 23.93 ?  90  LEU C CA    1 
ATOM   11710 C  C     . LEU C 2 111 ? 135.268 87.192  122.898 1.00 23.77 ?  90  LEU C C     1 
ATOM   11711 O  O     . LEU C 2 111 ? 134.130 87.137  123.365 1.00 23.04 ?  90  LEU C O     1 
ATOM   11712 C  CB    . LEU C 2 111 ? 136.355 84.964  122.415 1.00 23.73 ?  90  LEU C CB    1 
ATOM   11713 C  CG    . LEU C 2 111 ? 136.577 83.812  121.431 1.00 24.50 ?  90  LEU C CG    1 
ATOM   11714 C  CD1   . LEU C 2 111 ? 137.627 82.844  121.953 1.00 24.02 ?  90  LEU C CD1   1 
ATOM   11715 C  CD2   . LEU C 2 111 ? 135.270 83.083  121.112 1.00 25.38 ?  90  LEU C CD2   1 
ATOM   11716 N  N     . ASN C 2 112 ? 136.181 88.081  123.304 1.00 24.24 ?  91  ASN C N     1 
ATOM   11717 C  CA    . ASN C 2 112 ? 135.840 89.165  124.238 1.00 24.95 ?  91  ASN C CA    1 
ATOM   11718 C  C     . ASN C 2 112 ? 134.789 90.126  123.688 1.00 24.25 ?  91  ASN C C     1 
ATOM   11719 O  O     . ASN C 2 112 ? 133.903 90.562  124.421 1.00 23.99 ?  91  ASN C O     1 
ATOM   11720 C  CB    . ASN C 2 112 ? 137.081 89.968  124.641 1.00 25.81 ?  91  ASN C CB    1 
ATOM   11721 C  CG    . ASN C 2 112 ? 137.808 89.353  125.806 1.00 29.96 ?  91  ASN C CG    1 
ATOM   11722 O  OD1   . ASN C 2 112 ? 137.535 89.689  126.960 1.00 35.44 ?  91  ASN C OD1   1 
ATOM   11723 N  ND2   . ASN C 2 112 ? 138.740 88.444  125.521 1.00 32.37 ?  91  ASN C ND2   1 
ATOM   11724 N  N     . PHE C 2 113 ? 134.917 90.479  122.409 1.00 23.60 ?  92  PHE C N     1 
ATOM   11725 C  CA    . PHE C 2 113 ? 133.930 91.328  121.752 1.00 23.32 ?  92  PHE C CA    1 
ATOM   11726 C  C     . PHE C 2 113 ? 132.551 90.655  121.715 1.00 22.63 ?  92  PHE C C     1 
ATOM   11727 O  O     . PHE C 2 113 ? 131.541 91.294  122.014 1.00 21.94 ?  92  PHE C O     1 
ATOM   11728 C  CB    . PHE C 2 113 ? 134.354 91.675  120.317 1.00 23.27 ?  92  PHE C CB    1 
ATOM   11729 C  CG    . PHE C 2 113 ? 133.502 92.742  119.686 1.00 24.66 ?  92  PHE C CG    1 
ATOM   11730 C  CD1   . PHE C 2 113 ? 133.836 94.096  119.834 1.00 25.72 ?  92  PHE C CD1   1 
ATOM   11731 C  CD2   . PHE C 2 113 ? 132.356 92.406  118.970 1.00 25.36 ?  92  PHE C CD2   1 
ATOM   11732 C  CE1   . PHE C 2 113 ? 133.041 95.092  119.267 1.00 25.92 ?  92  PHE C CE1   1 
ATOM   11733 C  CE2   . PHE C 2 113 ? 131.549 93.397  118.399 1.00 25.82 ?  92  PHE C CE2   1 
ATOM   11734 C  CZ    . PHE C 2 113 ? 131.890 94.743  118.552 1.00 25.80 ?  92  PHE C CZ    1 
ATOM   11735 N  N     . MET C 2 114 ? 132.523 89.379  121.323 1.00 22.03 ?  93  MET C N     1 
ATOM   11736 C  CA    . MET C 2 114 ? 131.281 88.593  121.314 1.00 22.14 ?  93  MET C CA    1 
ATOM   11737 C  C     . MET C 2 114 ? 130.631 88.521  122.707 1.00 21.64 ?  93  MET C C     1 
ATOM   11738 O  O     . MET C 2 114 ? 129.412 88.681  122.830 1.00 21.59 ?  93  MET C O     1 
ATOM   11739 C  CB    . MET C 2 114 ? 131.535 87.193  120.767 1.00 22.46 ?  93  MET C CB    1 
ATOM   11740 C  CG    . MET C 2 114 ? 131.877 87.167  119.285 1.00 23.80 ?  93  MET C CG    1 
ATOM   11741 S  SD    . MET C 2 114 ? 132.356 85.520  118.722 1.00 28.07 ?  93  MET C SD    1 
ATOM   11742 C  CE    . MET C 2 114 ? 132.333 85.798  116.931 1.00 26.42 ?  93  MET C CE    1 
ATOM   11743 N  N     . ALA C 2 115 ? 131.448 88.316  123.746 1.00 20.98 ?  94  ALA C N     1 
ATOM   11744 C  CA    . ALA C 2 115 ? 130.975 88.337  125.143 1.00 20.58 ?  94  ALA C CA    1 
ATOM   11745 C  C     . ALA C 2 115 ? 130.306 89.655  125.527 1.00 21.01 ?  94  ALA C C     1 
ATOM   11746 O  O     . ALA C 2 115 ? 129.254 89.672  126.194 1.00 21.06 ?  94  ALA C O     1 
ATOM   11747 C  CB    . ALA C 2 115 ? 132.145 88.029  126.108 1.00 20.83 ?  94  ALA C CB    1 
ATOM   11748 N  N     . MET C 2 116 ? 130.934 90.764  125.139 1.00 20.36 ?  95  MET C N     1 
ATOM   11749 C  CA    . MET C 2 116 ? 130.381 92.081  125.399 1.00 20.83 ?  95  MET C CA    1 
ATOM   11750 C  C     . MET C 2 116 ? 129.009 92.231  124.720 1.00 20.55 ?  95  MET C C     1 
ATOM   11751 O  O     . MET C 2 116 ? 128.054 92.702  125.335 1.00 20.70 ?  95  MET C O     1 
ATOM   11752 C  CB    . MET C 2 116 ? 131.366 93.162  124.933 1.00 20.64 ?  95  MET C CB    1 
ATOM   11753 C  CG    . MET C 2 116 ? 130.854 94.599  125.034 1.00 21.42 ?  95  MET C CG    1 
ATOM   11754 S  SD    . MET C 2 116 ? 129.774 95.040  123.658 1.00 22.51 ?  95  MET C SD    1 
ATOM   11755 C  CE    . MET C 2 116 ? 130.870 94.826  122.254 1.00 20.66 ?  95  MET C CE    1 
ATOM   11756 N  N     . MET C 2 117 ? 128.918 91.806  123.465 1.00 20.50 ?  96  MET C N     1 
ATOM   11757 C  CA    . MET C 2 117 ? 127.661 91.877  122.732 1.00 21.22 ?  96  MET C CA    1 
ATOM   11758 C  C     . MET C 2 117 ? 126.549 91.124  123.459 1.00 21.11 ?  96  MET C C     1 
ATOM   11759 O  O     . MET C 2 117 ? 125.434 91.638  123.577 1.00 20.71 ?  96  MET C O     1 
ATOM   11760 C  CB    . MET C 2 117 ? 127.824 91.370  121.293 1.00 21.35 ?  96  MET C CB    1 
ATOM   11761 C  CG    . MET C 2 117 ? 128.620 92.320  120.342 1.00 22.54 ?  96  MET C CG    1 
ATOM   11762 S  SD    . MET C 2 117 ? 128.009 94.017  120.229 1.00 24.89 ?  96  MET C SD    1 
ATOM   11763 C  CE    . MET C 2 117 ? 126.551 93.797  119.210 1.00 24.95 ?  96  MET C CE    1 
ATOM   11764 N  N     . GLU C 2 118 ? 126.864 89.928  123.959 1.00 21.18 ?  97  GLU C N     1 
ATOM   11765 C  CA    . GLU C 2 118 ? 125.889 89.091  124.667 1.00 21.99 ?  97  GLU C CA    1 
ATOM   11766 C  C     . GLU C 2 118 ? 125.216 89.821  125.830 1.00 22.10 ?  97  GLU C C     1 
ATOM   11767 O  O     . GLU C 2 118 ? 123.987 89.907  125.883 1.00 22.22 ?  97  GLU C O     1 
ATOM   11768 C  CB    . GLU C 2 118 ? 126.514 87.781  125.175 1.00 22.01 ?  97  GLU C CB    1 
ATOM   11769 C  CG    . GLU C 2 118 ? 127.256 86.913  124.151 1.00 24.38 ?  97  GLU C CG    1 
ATOM   11770 C  CD    . GLU C 2 118 ? 126.405 86.419  122.975 1.00 26.32 ?  97  GLU C CD    1 
ATOM   11771 O  OE1   . GLU C 2 118 ? 125.470 87.109  122.545 1.00 29.86 ?  97  GLU C OE1   1 
ATOM   11772 O  OE2   . GLU C 2 118 ? 126.712 85.341  122.437 1.00 29.19 -1 97  GLU C OE2   1 
ATOM   11773 N  N     . ASN C 2 119 ? 126.009 90.347  126.761 1.00 22.26 ?  98  ASN C N     1 
ATOM   11774 C  CA    . ASN C 2 119 ? 125.418 90.933  127.964 1.00 21.91 ?  98  ASN C CA    1 
ATOM   11775 C  C     . ASN C 2 119 ? 125.257 92.460  127.987 1.00 22.41 ?  98  ASN C C     1 
ATOM   11776 O  O     . ASN C 2 119 ? 124.350 92.973  128.640 1.00 23.07 ?  98  ASN C O     1 
ATOM   11777 C  CB    . ASN C 2 119 ? 126.020 90.354  129.263 1.00 21.93 ?  98  ASN C CB    1 
ATOM   11778 C  CG    . ASN C 2 119 ? 127.495 90.651  129.430 1.00 21.31 ?  98  ASN C CG    1 
ATOM   11779 O  OD1   . ASN C 2 119 ? 128.129 91.267  128.571 1.00 21.88 ?  98  ASN C OD1   1 
ATOM   11780 N  ND2   . ASN C 2 119 ? 128.051 90.218  130.559 1.00 21.73 ?  98  ASN C ND2   1 
ATOM   11781 N  N     . ALA C 2 120 ? 126.136 93.177  127.291 1.00 22.75 ?  99  ALA C N     1 
ATOM   11782 C  CA    . ALA C 2 120 ? 126.056 94.636  127.228 1.00 23.12 ?  99  ALA C CA    1 
ATOM   11783 C  C     . ALA C 2 120 ? 125.134 95.131  126.131 1.00 23.60 ?  99  ALA C C     1 
ATOM   11784 O  O     . ALA C 2 120 ? 124.625 96.252  126.223 1.00 24.14 ?  99  ALA C O     1 
ATOM   11785 C  CB    . ALA C 2 120 ? 127.455 95.273  127.092 1.00 23.28 ?  99  ALA C CB    1 
ATOM   11786 N  N     . VAL C 2 121 ? 124.910 94.309  125.100 1.00 23.23 ?  100 VAL C N     1 
ATOM   11787 C  CA    . VAL C 2 121 ? 124.029 94.723  123.991 1.00 23.74 ?  100 VAL C CA    1 
ATOM   11788 C  C     . VAL C 2 121 ? 122.758 93.882  123.868 1.00 23.62 ?  100 VAL C C     1 
ATOM   11789 O  O     . VAL C 2 121 ? 121.660 94.427  123.943 1.00 24.51 ?  100 VAL C O     1 
ATOM   11790 C  CB    . VAL C 2 121 ? 124.771 94.782  122.638 1.00 23.19 ?  100 VAL C CB    1 
ATOM   11791 C  CG1   . VAL C 2 121 ? 123.807 95.168  121.502 1.00 24.10 ?  100 VAL C CG1   1 
ATOM   11792 C  CG2   . VAL C 2 121 ? 125.938 95.780  122.717 1.00 23.48 ?  100 VAL C CG2   1 
ATOM   11793 N  N     . HIS C 2 122 ? 122.911 92.572  123.691 1.00 23.45 ?  101 HIS C N     1 
ATOM   11794 C  CA    . HIS C 2 122 ? 121.767 91.689  123.451 1.00 23.81 ?  101 HIS C CA    1 
ATOM   11795 C  C     . HIS C 2 122 ? 120.836 91.574  124.641 1.00 24.33 ?  101 HIS C C     1 
ATOM   11796 O  O     . HIS C 2 122 ? 119.641 91.854  124.511 1.00 24.80 ?  101 HIS C O     1 
ATOM   11797 C  CB    . HIS C 2 122 ? 122.206 90.288  123.034 1.00 23.30 ?  101 HIS C CB    1 
ATOM   11798 C  CG    . HIS C 2 122 ? 122.969 90.248  121.748 1.00 22.96 ?  101 HIS C CG    1 
ATOM   11799 N  ND1   . HIS C 2 122 ? 123.559 89.095  121.274 1.00 22.78 ?  101 HIS C ND1   1 
ATOM   11800 C  CD2   . HIS C 2 122 ? 123.268 91.223  120.858 1.00 23.25 ?  101 HIS C CD2   1 
ATOM   11801 C  CE1   . HIS C 2 122 ? 124.174 89.360  120.136 1.00 22.57 ?  101 HIS C CE1   1 
ATOM   11802 N  NE2   . HIS C 2 122 ? 124.013 90.642  119.861 1.00 21.75 ?  101 HIS C NE2   1 
ATOM   11803 N  N     . ALA C 2 123 ? 121.372 91.133  125.782 1.00 24.40 ?  102 ALA C N     1 
ATOM   11804 C  CA    . ALA C 2 123 ? 120.552 90.942  126.981 1.00 24.00 ?  102 ALA C CA    1 
ATOM   11805 C  C     . ALA C 2 123 ? 119.851 92.246  127.364 1.00 24.05 ?  102 ALA C C     1 
ATOM   11806 O  O     . ALA C 2 123 ? 118.682 92.231  127.745 1.00 23.89 ?  102 ALA C O     1 
ATOM   11807 C  CB    . ALA C 2 123 ? 121.389 90.402  128.139 1.00 23.73 ?  102 ALA C CB    1 
ATOM   11808 N  N     . LYS C 2 124 ? 120.559 93.367  127.241 1.00 24.36 ?  103 LYS C N     1 
ATOM   11809 C  CA    . LYS C 2 124 ? 120.000 94.683  127.574 1.00 24.31 ?  103 LYS C CA    1 
ATOM   11810 C  C     . LYS C 2 124 ? 118.879 95.145  126.635 1.00 23.84 ?  103 LYS C C     1 
ATOM   11811 O  O     . LYS C 2 124 ? 117.894 95.738  127.094 1.00 24.21 ?  103 LYS C O     1 
ATOM   11812 C  CB    . LYS C 2 124 ? 121.092 95.751  127.691 1.00 24.93 ?  103 LYS C CB    1 
ATOM   11813 C  CG    . LYS C 2 124 ? 120.572 97.082  128.254 1.00 26.37 ?  103 LYS C CG    1 
ATOM   11814 C  CD    . LYS C 2 124 ? 121.695 98.066  128.534 1.00 29.42 ?  103 LYS C CD    1 
ATOM   11815 C  CE    . LYS C 2 124 ? 121.133 99.435  128.928 1.00 31.51 ?  103 LYS C CE    1 
ATOM   11816 N  NZ    . LYS C 2 124 ? 120.380 100.080 127.811 1.00 32.37 1  103 LYS C NZ    1 
ATOM   11817 N  N     . SER C 2 125 ? 119.019 94.864  125.338 1.00 23.52 ?  104 SER C N     1 
ATOM   11818 C  CA    . SER C 2 125 ? 117.998 95.208  124.342 0.50 23.23 ?  104 SER C CA    1 
ATOM   11819 C  C     . SER C 2 125 ? 116.621 94.659  124.715 1.00 22.91 ?  104 SER C C     1 
ATOM   11820 O  O     . SER C 2 125 ? 115.604 95.291  124.458 1.00 22.33 ?  104 SER C O     1 
ATOM   11821 C  CB    . SER C 2 125 ? 118.391 94.685  122.955 0.50 23.25 ?  104 SER C CB    1 
ATOM   11822 O  OG    . SER C 2 125 ? 119.621 95.234  122.522 0.50 24.57 ?  104 SER C OG    1 
ATOM   11823 N  N     . TYR C 2 126 ? 116.586 93.467  125.306 1.00 22.72 ?  105 TYR C N     1 
ATOM   11824 C  CA    . TYR C 2 126 ? 115.302 92.882  125.693 1.00 23.34 ?  105 TYR C CA    1 
ATOM   11825 C  C     . TYR C 2 126 ? 114.610 93.710  126.750 1.00 23.32 ?  105 TYR C C     1 
ATOM   11826 O  O     . TYR C 2 126 ? 113.393 93.818  126.728 1.00 23.17 ?  105 TYR C O     1 
ATOM   11827 C  CB    . TYR C 2 126 ? 115.429 91.436  126.176 1.00 23.45 ?  105 TYR C CB    1 
ATOM   11828 C  CG    . TYR C 2 126 ? 116.075 90.504  125.177 1.00 25.16 ?  105 TYR C CG    1 
ATOM   11829 C  CD1   . TYR C 2 126 ? 115.499 90.271  123.931 1.00 26.75 ?  105 TYR C CD1   1 
ATOM   11830 C  CD2   . TYR C 2 126 ? 117.269 89.855  125.487 1.00 26.36 ?  105 TYR C CD2   1 
ATOM   11831 C  CE1   . TYR C 2 126 ? 116.113 89.417  123.006 1.00 28.22 ?  105 TYR C CE1   1 
ATOM   11832 C  CE2   . TYR C 2 126 ? 117.886 89.010  124.579 1.00 27.17 ?  105 TYR C CE2   1 
ATOM   11833 C  CZ    . TYR C 2 126 ? 117.297 88.783  123.348 1.00 29.26 ?  105 TYR C CZ    1 
ATOM   11834 O  OH    . TYR C 2 126 ? 117.906 87.929  122.450 1.00 30.76 ?  105 TYR C OH    1 
ATOM   11835 N  N     . SER C 2 127 ? 115.391 94.288  127.667 1.00 23.61 ?  106 SER C N     1 
ATOM   11836 C  CA    . SER C 2 127 ? 114.846 95.183  128.680 1.00 24.40 ?  106 SER C CA    1 
ATOM   11837 C  C     . SER C 2 127 ? 114.320 96.470  128.058 1.00 24.55 ?  106 SER C C     1 
ATOM   11838 O  O     . SER C 2 127 ? 113.348 97.023  128.549 1.00 24.74 ?  106 SER C O     1 
ATOM   11839 C  CB    . SER C 2 127 ? 115.865 95.497  129.775 1.00 24.54 ?  106 SER C CB    1 
ATOM   11840 O  OG    . SER C 2 127 ? 115.986 94.409  130.683 1.00 24.69 ?  106 SER C OG    1 
ATOM   11841 N  N     . ASN C 2 128 ? 114.966 96.943  126.993 1.00 25.28 ?  107 ASN C N     1 
ATOM   11842 C  CA    . ASN C 2 128 ? 114.468 98.112  126.260 1.00 25.88 ?  107 ASN C CA    1 
ATOM   11843 C  C     . ASN C 2 128 ? 113.097 97.804  125.672 1.00 25.48 ?  107 ASN C C     1 
ATOM   11844 O  O     . ASN C 2 128 ? 112.176 98.614  125.762 1.00 25.23 ?  107 ASN C O     1 
ATOM   11845 C  CB    . ASN C 2 128 ? 115.433 98.540  125.147 1.00 26.40 ?  107 ASN C CB    1 
ATOM   11846 C  CG    . ASN C 2 128 ? 116.651 99.293  125.668 1.00 27.90 ?  107 ASN C CG    1 
ATOM   11847 O  OD1   . ASN C 2 128 ? 117.123 99.055  126.781 1.00 30.62 ?  107 ASN C OD1   1 
ATOM   11848 N  ND2   . ASN C 2 128 ? 117.174 100.199 124.848 1.00 27.91 ?  107 ASN C ND2   1 
ATOM   11849 N  N     . ILE C 2 129 ? 112.969 96.622  125.080 1.00 25.44 ?  108 ILE C N     1 
ATOM   11850 C  CA    . ILE C 2 129 ? 111.679 96.183  124.549 1.00 25.48 ?  108 ILE C CA    1 
ATOM   11851 C  C     . ILE C 2 129 ? 110.641 96.066  125.676 1.00 25.93 ?  108 ILE C C     1 
ATOM   11852 O  O     . ILE C 2 129 ? 109.554 96.645  125.570 1.00 25.54 ?  108 ILE C O     1 
ATOM   11853 C  CB    . ILE C 2 129 ? 111.795 94.890  123.700 1.00 25.21 ?  108 ILE C CB    1 
ATOM   11854 C  CG1   . ILE C 2 129 ? 112.702 95.146  122.484 1.00 25.96 ?  108 ILE C CG1   1 
ATOM   11855 C  CG2   . ILE C 2 129 ? 110.399 94.398  123.260 1.00 24.43 ?  108 ILE C CG2   1 
ATOM   11856 C  CD1   . ILE C 2 129 ? 113.131 93.897  121.715 1.00 26.11 ?  108 ILE C CD1   1 
ATOM   11857 N  N     . PHE C 2 130 ? 110.978 95.348  126.752 1.00 26.04 ?  109 PHE C N     1 
ATOM   11858 C  CA    . PHE C 2 130 ? 110.066 95.192  127.900 1.00 26.66 ?  109 PHE C CA    1 
ATOM   11859 C  C     . PHE C 2 130 ? 109.609 96.536  128.473 1.00 27.38 ?  109 PHE C C     1 
ATOM   11860 O  O     . PHE C 2 130 ? 108.416 96.731  128.756 1.00 27.22 ?  109 PHE C O     1 
ATOM   11861 C  CB    . PHE C 2 130 ? 110.721 94.377  129.038 1.00 26.98 ?  109 PHE C CB    1 
ATOM   11862 C  CG    . PHE C 2 130 ? 110.899 92.908  128.742 1.00 27.46 ?  109 PHE C CG    1 
ATOM   11863 C  CD1   . PHE C 2 130 ? 110.040 92.233  127.883 1.00 28.57 ?  109 PHE C CD1   1 
ATOM   11864 C  CD2   . PHE C 2 130 ? 111.933 92.194  129.350 1.00 28.51 ?  109 PHE C CD2   1 
ATOM   11865 C  CE1   . PHE C 2 130 ? 110.215 90.875  127.620 1.00 29.17 ?  109 PHE C CE1   1 
ATOM   11866 C  CE2   . PHE C 2 130 ? 112.114 90.828  129.098 1.00 29.27 ?  109 PHE C CE2   1 
ATOM   11867 C  CZ    . PHE C 2 130 ? 111.254 90.164  128.236 1.00 28.83 ?  109 PHE C CZ    1 
ATOM   11868 N  N     . MET C 2 131 ? 110.551 97.465  128.642 1.00 27.52 ?  110 MET C N     1 
ATOM   11869 C  CA    . MET C 2 131 ? 110.248 98.752  129.278 1.00 29.07 ?  110 MET C CA    1 
ATOM   11870 C  C     . MET C 2 131 ? 109.338 99.635  128.441 1.00 29.58 ?  110 MET C C     1 
ATOM   11871 O  O     . MET C 2 131 ? 108.615 100.472 128.981 1.00 30.07 ?  110 MET C O     1 
ATOM   11872 C  CB    . MET C 2 131 ? 111.520 99.510  129.648 1.00 28.96 ?  110 MET C CB    1 
ATOM   11873 C  CG    . MET C 2 131 ? 112.156 99.014  130.930 1.00 31.09 ?  110 MET C CG    1 
ATOM   11874 S  SD    . MET C 2 131 ? 113.692 99.864  131.362 1.00 35.43 ?  110 MET C SD    1 
ATOM   11875 C  CE    . MET C 2 131 ? 114.790 99.359  130.041 1.00 33.13 ?  110 MET C CE    1 
ATOM   11876 N  N     . THR C 2 132 ? 109.378 99.435  127.130 1.00 30.25 ?  111 THR C N     1 
ATOM   11877 C  CA    . THR C 2 132 ? 108.498 100.137 126.200 1.00 30.97 ?  111 THR C CA    1 
ATOM   11878 C  C     . THR C 2 132 ? 107.077 99.565  126.224 1.00 31.36 ?  111 THR C C     1 
ATOM   11879 O  O     . THR C 2 132 ? 106.098 100.303 126.402 1.00 31.60 ?  111 THR C O     1 
ATOM   11880 C  CB    . THR C 2 132 ? 109.082 100.081 124.759 1.00 30.88 ?  111 THR C CB    1 
ATOM   11881 O  OG1   . THR C 2 132 ? 110.348 100.749 124.742 1.00 29.86 ?  111 THR C OG1   1 
ATOM   11882 C  CG2   . THR C 2 132 ? 108.151 100.753 123.738 1.00 31.44 ?  111 THR C CG2   1 
ATOM   11883 N  N     . LEU C 2 133 ? 106.973 98.250  126.059 1.00 31.34 ?  112 LEU C N     1 
ATOM   11884 C  CA    . LEU C 2 133 ? 105.682 97.593  125.848 1.00 31.68 ?  112 LEU C CA    1 
ATOM   11885 C  C     . LEU C 2 133 ? 104.889 97.237  127.109 1.00 31.96 ?  112 LEU C C     1 
ATOM   11886 O  O     . LEU C 2 133 ? 103.659 97.228  127.086 1.00 31.69 ?  112 LEU C O     1 
ATOM   11887 C  CB    . LEU C 2 133 ? 105.870 96.337  125.003 1.00 31.35 ?  112 LEU C CB    1 
ATOM   11888 C  CG    . LEU C 2 133 ? 106.615 96.489  123.672 1.00 32.14 ?  112 LEU C CG    1 
ATOM   11889 C  CD1   . LEU C 2 133 ? 106.759 95.131  123.026 1.00 32.15 ?  112 LEU C CD1   1 
ATOM   11890 C  CD2   . LEU C 2 133 ? 105.901 97.468  122.743 1.00 32.39 ?  112 LEU C CD2   1 
ATOM   11891 N  N     . ALA C 2 134 ? 105.589 96.942  128.199 1.00 32.12 ?  113 ALA C N     1 
ATOM   11892 C  CA    . ALA C 2 134 ? 104.950 96.342  129.363 1.00 32.53 ?  113 ALA C CA    1 
ATOM   11893 C  C     . ALA C 2 134 ? 105.063 97.186  130.626 1.00 33.15 ?  113 ALA C C     1 
ATOM   11894 O  O     . ALA C 2 134 ? 106.062 97.874  130.823 1.00 32.47 ?  113 ALA C O     1 
ATOM   11895 C  CB    . ALA C 2 134 ? 105.514 94.937  129.608 1.00 32.20 ?  113 ALA C CB    1 
ATOM   11896 N  N     . PRO C 2 135 ? 104.036 97.117  131.497 1.00 34.27 ?  114 PRO C N     1 
ATOM   11897 C  CA    . PRO C 2 135 ? 104.119 97.756  132.803 1.00 35.35 ?  114 PRO C CA    1 
ATOM   11898 C  C     . PRO C 2 135 ? 105.058 96.979  133.719 1.00 36.17 ?  114 PRO C C     1 
ATOM   11899 O  O     . PRO C 2 135 ? 105.271 95.781  133.515 1.00 35.92 ?  114 PRO C O     1 
ATOM   11900 C  CB    . PRO C 2 135 ? 102.675 97.714  133.319 1.00 35.48 ?  114 PRO C CB    1 
ATOM   11901 C  CG    . PRO C 2 135 ? 102.027 96.601  132.592 1.00 34.94 ?  114 PRO C CG    1 
ATOM   11902 C  CD    . PRO C 2 135 ? 102.750 96.421  131.290 1.00 34.50 ?  114 PRO C CD    1 
ATOM   11903 N  N     . THR C 2 136 ? 105.619 97.666  134.708 1.00 37.30 ?  115 THR C N     1 
ATOM   11904 C  CA    . THR C 2 136 ? 106.627 97.096  135.609 1.00 38.49 ?  115 THR C CA    1 
ATOM   11905 C  C     . THR C 2 136 ? 106.249 95.747  136.236 1.00 38.48 ?  115 THR C C     1 
ATOM   11906 O  O     . THR C 2 136 ? 107.110 94.872  136.378 1.00 38.74 ?  115 THR C O     1 
ATOM   11907 C  CB    . THR C 2 136 ? 106.992 98.099  136.722 1.00 38.95 ?  115 THR C CB    1 
ATOM   11908 O  OG1   . THR C 2 136 ? 107.340 99.351  136.123 1.00 40.08 ?  115 THR C OG1   1 
ATOM   11909 C  CG2   . THR C 2 136 ? 108.171 97.600  137.560 1.00 39.82 ?  115 THR C CG2   1 
ATOM   11910 N  N     . GLU C 2 137 ? 104.975 95.584  136.601 1.00 38.89 ?  116 GLU C N     1 
ATOM   11911 C  CA    . GLU C 2 137 ? 104.502 94.363  137.268 1.00 38.65 ?  116 GLU C CA    1 
ATOM   11912 C  C     . GLU C 2 137 ? 104.575 93.149  136.348 1.00 37.38 ?  116 GLU C C     1 
ATOM   11913 O  O     . GLU C 2 137 ? 104.915 92.052  136.787 1.00 37.22 ?  116 GLU C O     1 
ATOM   11914 C  CB    . GLU C 2 137 ? 103.083 94.527  137.855 1.00 39.52 ?  116 GLU C CB    1 
ATOM   11915 C  CG    . GLU C 2 137 ? 101.923 94.624  136.836 1.00 41.90 ?  116 GLU C CG    1 
ATOM   11916 C  CD    . GLU C 2 137 ? 101.123 95.935  136.922 1.00 46.43 ?  116 GLU C CD    1 
ATOM   11917 O  OE1   . GLU C 2 137 ? 101.568 96.891  137.601 1.00 47.84 ?  116 GLU C OE1   1 
ATOM   11918 O  OE2   . GLU C 2 137 ? 100.034 96.006  136.300 1.00 47.52 -1 116 GLU C OE2   1 
ATOM   11919 N  N     . THR C 2 138 ? 104.265 93.363  135.073 1.00 36.05 ?  117 THR C N     1 
ATOM   11920 C  CA    . THR C 2 138 ? 104.344 92.314  134.068 1.00 34.88 ?  117 THR C CA    1 
ATOM   11921 C  C     . THR C 2 138 ? 105.804 91.958  133.807 1.00 33.58 ?  117 THR C C     1 
ATOM   11922 O  O     . THR C 2 138 ? 106.132 90.784  133.615 1.00 33.61 ?  117 THR C O     1 
ATOM   11923 C  CB    . THR C 2 138 ? 103.651 92.737  132.765 1.00 34.85 ?  117 THR C CB    1 
ATOM   11924 O  OG1   . THR C 2 138 ? 102.329 93.194  133.068 1.00 35.98 ?  117 THR C OG1   1 
ATOM   11925 C  CG2   . THR C 2 138 ? 103.565 91.570  131.791 1.00 34.92 ?  117 THR C CG2   1 
ATOM   11926 N  N     . ILE C 2 139 ? 106.669 92.972  133.808 1.00 32.29 ?  118 ILE C N     1 
ATOM   11927 C  CA    . ILE C 2 139 ? 108.110 92.758  133.682 1.00 31.19 ?  118 ILE C CA    1 
ATOM   11928 C  C     . ILE C 2 139 ? 108.645 91.952  134.880 1.00 30.85 ?  118 ILE C C     1 
ATOM   11929 O  O     . ILE C 2 139 ? 109.346 90.958  134.690 1.00 29.77 ?  118 ILE C O     1 
ATOM   11930 C  CB    . ILE C 2 139 ? 108.902 94.086  133.493 1.00 31.25 ?  118 ILE C CB    1 
ATOM   11931 C  CG1   . ILE C 2 139 ? 108.418 94.851  132.248 1.00 30.12 ?  118 ILE C CG1   1 
ATOM   11932 C  CG2   . ILE C 2 139 ? 110.412 93.817  133.390 1.00 30.21 ?  118 ILE C CG2   1 
ATOM   11933 C  CD1   . ILE C 2 139 ? 109.054 96.244  132.084 1.00 29.41 ?  118 ILE C CD1   1 
ATOM   11934 N  N     . ASN C 2 140 ? 108.295 92.373  136.101 1.00 31.17 ?  119 ASN C N     1 
ATOM   11935 C  CA    . ASN C 2 140 ? 108.690 91.652  137.322 1.00 31.76 ?  119 ASN C CA    1 
ATOM   11936 C  C     . ASN C 2 140 ? 108.238 90.187  137.298 1.00 31.25 ?  119 ASN C C     1 
ATOM   11937 O  O     . ASN C 2 140 ? 109.019 89.289  137.615 1.00 31.47 ?  119 ASN C O     1 
ATOM   11938 C  CB    . ASN C 2 140 ? 108.136 92.327  138.586 1.00 32.65 ?  119 ASN C CB    1 
ATOM   11939 C  CG    . ASN C 2 140 ? 108.821 93.650  138.914 1.00 35.14 ?  119 ASN C CG    1 
ATOM   11940 O  OD1   . ASN C 2 140 ? 109.981 93.885  138.563 1.00 36.75 ?  119 ASN C OD1   1 
ATOM   11941 N  ND2   . ASN C 2 140 ? 108.095 94.518  139.626 1.00 38.05 ?  119 ASN C ND2   1 
ATOM   11942 N  N     . GLU C 2 141 ? 106.984 89.968  136.909 1.00 30.96 ?  120 GLU C N     1 
ATOM   11943 C  CA    . GLU C 2 141 ? 106.395 88.632  136.825 1.00 30.36 ?  120 GLU C CA    1 
ATOM   11944 C  C     . GLU C 2 141 ? 107.122 87.729  135.826 1.00 28.60 ?  120 GLU C C     1 
ATOM   11945 O  O     . GLU C 2 141 ? 107.357 86.558  136.116 1.00 27.94 ?  120 GLU C O     1 
ATOM   11946 C  CB    . GLU C 2 141 ? 104.910 88.716  136.460 1.00 30.86 ?  120 GLU C CB    1 
ATOM   11947 C  CG    . GLU C 2 141 ? 103.995 89.123  137.609 1.00 34.89 ?  120 GLU C CG    1 
ATOM   11948 C  CD    . GLU C 2 141 ? 102.565 89.386  137.154 1.00 39.82 ?  120 GLU C CD    1 
ATOM   11949 O  OE1   . GLU C 2 141 ? 102.207 88.998  136.014 1.00 41.95 ?  120 GLU C OE1   1 
ATOM   11950 O  OE2   . GLU C 2 141 ? 101.794 89.978  137.937 1.00 41.94 -1 120 GLU C OE2   1 
ATOM   11951 N  N     . VAL C 2 142 ? 107.475 88.258  134.657 1.00 27.29 ?  121 VAL C N     1 
ATOM   11952 C  CA    . VAL C 2 142 ? 108.156 87.411  133.654 1.00 25.89 ?  121 VAL C CA    1 
ATOM   11953 C  C     . VAL C 2 142 ? 109.572 87.011  134.086 1.00 25.11 ?  121 VAL C C     1 
ATOM   11954 O  O     . VAL C 2 142 ? 110.027 85.907  133.788 1.00 24.23 ?  121 VAL C O     1 
ATOM   11955 C  CB    . VAL C 2 142 ? 108.103 87.993  132.199 1.00 25.99 ?  121 VAL C CB    1 
ATOM   11956 C  CG1   . VAL C 2 142 ? 109.232 88.990  131.924 1.00 25.21 ?  121 VAL C CG1   1 
ATOM   11957 C  CG2   . VAL C 2 142 ? 108.158 86.865  131.179 1.00 25.78 ?  121 VAL C CG2   1 
ATOM   11958 N  N     . PHE C 2 143 ? 110.266 87.891  134.801 1.00 24.69 ?  122 PHE C N     1 
ATOM   11959 C  CA    . PHE C 2 143 ? 111.592 87.531  135.327 1.00 24.77 ?  122 PHE C CA    1 
ATOM   11960 C  C     . PHE C 2 143 ? 111.489 86.515  136.477 1.00 24.99 ?  122 PHE C C     1 
ATOM   11961 O  O     . PHE C 2 143 ? 112.346 85.642  136.627 1.00 24.73 ?  122 PHE C O     1 
ATOM   11962 C  CB    . PHE C 2 143 ? 112.412 88.773  135.699 1.00 24.83 ?  122 PHE C CB    1 
ATOM   11963 C  CG    . PHE C 2 143 ? 113.023 89.463  134.498 1.00 25.12 ?  122 PHE C CG    1 
ATOM   11964 C  CD1   . PHE C 2 143 ? 114.105 88.897  133.828 1.00 26.58 ?  122 PHE C CD1   1 
ATOM   11965 C  CD2   . PHE C 2 143 ? 112.505 90.660  134.027 1.00 24.49 ?  122 PHE C CD2   1 
ATOM   11966 C  CE1   . PHE C 2 143 ? 114.663 89.525  132.706 1.00 26.96 ?  122 PHE C CE1   1 
ATOM   11967 C  CE2   . PHE C 2 143 ? 113.051 91.292  132.920 1.00 25.79 ?  122 PHE C CE2   1 
ATOM   11968 C  CZ    . PHE C 2 143 ? 114.132 90.725  132.252 1.00 26.45 ?  122 PHE C CZ    1 
ATOM   11969 N  N     . GLU C 2 144 ? 110.425 86.615  137.271 1.00 25.22 ?  123 GLU C N     1 
ATOM   11970 C  CA    . GLU C 2 144 ? 110.126 85.580  138.265 1.00 25.72 ?  123 GLU C CA    1 
ATOM   11971 C  C     . GLU C 2 144 ? 109.804 84.252  137.583 1.00 25.08 ?  123 GLU C C     1 
ATOM   11972 O  O     . GLU C 2 144 ? 110.238 83.192  138.035 1.00 24.67 ?  123 GLU C O     1 
ATOM   11973 C  CB    . GLU C 2 144 ? 108.991 86.017  139.188 1.00 26.23 ?  123 GLU C CB    1 
ATOM   11974 C  CG    . GLU C 2 144 ? 109.413 87.109  140.157 1.00 29.96 ?  123 GLU C CG    1 
ATOM   11975 C  CD    . GLU C 2 144 ? 110.655 86.729  140.946 1.00 33.82 ?  123 GLU C CD    1 
ATOM   11976 O  OE1   . GLU C 2 144 ? 110.576 85.773  141.746 1.00 36.54 ?  123 GLU C OE1   1 
ATOM   11977 O  OE2   . GLU C 2 144 ? 111.710 87.370  140.754 1.00 35.84 -1 123 GLU C OE2   1 
ATOM   11978 N  N     . TRP C 2 145 ? 109.068 84.326  136.477 1.00 24.21 ?  124 TRP C N     1 
ATOM   11979 C  CA    . TRP C 2 145 ? 108.727 83.145  135.685 1.00 23.99 ?  124 TRP C CA    1 
ATOM   11980 C  C     . TRP C 2 145 ? 109.951 82.416  135.111 1.00 23.95 ?  124 TRP C C     1 
ATOM   11981 O  O     . TRP C 2 145 ? 109.967 81.171  135.075 1.00 23.31 ?  124 TRP C O     1 
ATOM   11982 C  CB    . TRP C 2 145 ? 107.736 83.506  134.568 1.00 24.13 ?  124 TRP C CB    1 
ATOM   11983 C  CG    . TRP C 2 145 ? 107.566 82.415  133.535 1.00 24.37 ?  124 TRP C CG    1 
ATOM   11984 C  CD1   . TRP C 2 145 ? 106.671 81.371  133.568 1.00 24.76 ?  124 TRP C CD1   1 
ATOM   11985 C  CD2   . TRP C 2 145 ? 108.311 82.269  132.319 1.00 23.31 ?  124 TRP C CD2   1 
ATOM   11986 N  NE1   . TRP C 2 145 ? 106.827 80.583  132.442 1.00 24.97 ?  124 TRP C NE1   1 
ATOM   11987 C  CE2   . TRP C 2 145 ? 107.822 81.113  131.661 1.00 24.20 ?  124 TRP C CE2   1 
ATOM   11988 C  CE3   . TRP C 2 145 ? 109.351 82.996  131.725 1.00 23.76 ?  124 TRP C CE3   1 
ATOM   11989 C  CZ2   . TRP C 2 145 ? 108.339 80.673  130.435 1.00 23.41 ?  124 TRP C CZ2   1 
ATOM   11990 C  CZ3   . TRP C 2 145 ? 109.869 82.556  130.508 1.00 23.29 ?  124 TRP C CZ3   1 
ATOM   11991 C  CH2   . TRP C 2 145 ? 109.353 81.406  129.875 1.00 22.93 ?  124 TRP C CH2   1 
ATOM   11992 N  N     . VAL C 2 146 ? 110.971 83.152  134.655 1.00 23.35 ?  125 VAL C N     1 
ATOM   11993 C  CA    . VAL C 2 146 ? 112.194 82.447  134.192 1.00 23.53 ?  125 VAL C CA    1 
ATOM   11994 C  C     . VAL C 2 146 ? 112.852 81.627  135.309 1.00 23.73 ?  125 VAL C C     1 
ATOM   11995 O  O     . VAL C 2 146 ? 113.273 80.505  135.067 1.00 23.03 ?  125 VAL C O     1 
ATOM   11996 C  CB    . VAL C 2 146 ? 113.226 83.300  133.315 1.00 23.63 ?  125 VAL C CB    1 
ATOM   11997 C  CG1   . VAL C 2 146 ? 112.746 84.687  132.984 1.00 24.40 ?  125 VAL C CG1   1 
ATOM   11998 C  CG2   . VAL C 2 146 ? 114.668 83.288  133.857 1.00 22.97 ?  125 VAL C CG2   1 
ATOM   11999 N  N     . LYS C 2 147 ? 112.880 82.170  136.529 1.00 24.06 ?  126 LYS C N     1 
ATOM   12000 C  CA    . LYS C 2 147 ? 113.513 81.483  137.668 1.00 25.41 ?  126 LYS C CA    1 
ATOM   12001 C  C     . LYS C 2 147 ? 112.865 80.140  138.009 1.00 25.82 ?  126 LYS C C     1 
ATOM   12002 O  O     . LYS C 2 147 ? 113.552 79.220  138.459 1.00 26.08 ?  126 LYS C O     1 
ATOM   12003 C  CB    . LYS C 2 147 ? 113.497 82.368  138.917 1.00 25.49 ?  126 LYS C CB    1 
ATOM   12004 C  CG    . LYS C 2 147 ? 114.378 83.598  138.849 1.00 27.52 ?  126 LYS C CG    1 
ATOM   12005 C  CD    . LYS C 2 147 ? 114.191 84.420  140.119 1.00 30.43 ?  126 LYS C CD    1 
ATOM   12006 C  CE    . LYS C 2 147 ? 114.763 85.815  139.974 1.00 33.10 ?  126 LYS C CE    1 
ATOM   12007 N  NZ    . LYS C 2 147 ? 114.455 86.623  141.187 1.00 34.86 1  126 LYS C NZ    1 
ATOM   12008 N  N     . GLN C 2 148 ? 111.553 80.034  137.796 1.00 26.45 ?  127 GLN C N     1 
ATOM   12009 C  CA    . GLN C 2 148 ? 110.794 78.847  138.200 1.00 26.85 ?  127 GLN C CA    1 
ATOM   12010 C  C     . GLN C 2 148 ? 110.414 77.912  137.050 1.00 26.01 ?  127 GLN C C     1 
ATOM   12011 O  O     . GLN C 2 148 ? 109.870 76.833  137.292 1.00 26.12 ?  127 GLN C O     1 
ATOM   12012 C  CB    . GLN C 2 148 ? 109.544 79.240  139.011 1.00 28.08 ?  127 GLN C CB    1 
ATOM   12013 C  CG    . GLN C 2 148 ? 108.511 80.083  138.257 1.00 30.69 ?  127 GLN C CG    1 
ATOM   12014 C  CD    . GLN C 2 148 ? 107.687 79.277  137.256 1.00 34.64 ?  127 GLN C CD    1 
ATOM   12015 O  OE1   . GLN C 2 148 ? 107.775 79.495  136.035 1.00 33.80 ?  127 GLN C OE1   1 
ATOM   12016 N  NE2   . GLN C 2 148 ? 106.887 78.332  137.766 1.00 36.24 ?  127 GLN C NE2   1 
ATOM   12017 N  N     . ASN C 2 149 ? 110.687 78.323  135.809 1.00 24.97 ?  128 ASN C N     1 
ATOM   12018 C  CA    . ASN C 2 149 ? 110.369 77.502  134.645 1.00 24.03 ?  128 ASN C CA    1 
ATOM   12019 C  C     . ASN C 2 149 ? 111.362 76.358  134.507 1.00 24.13 ?  128 ASN C C     1 
ATOM   12020 O  O     . ASN C 2 149 ? 112.560 76.608  134.350 1.00 22.93 ?  128 ASN C O     1 
ATOM   12021 C  CB    . ASN C 2 149 ? 110.405 78.338  133.375 1.00 23.97 ?  128 ASN C CB    1 
ATOM   12022 C  CG    . ASN C 2 149 ? 109.948 77.561  132.165 1.00 23.94 ?  128 ASN C CG    1 
ATOM   12023 O  OD1   . ASN C 2 149 ? 110.747 76.914  131.490 1.00 24.85 ?  128 ASN C OD1   1 
ATOM   12024 N  ND2   . ASN C 2 149 ? 108.646 77.577  131.909 1.00 24.76 ?  128 ASN C ND2   1 
ATOM   12025 N  N     . LYS C 2 150 ? 110.867 75.118  134.535 1.00 24.32 ?  129 LYS C N     1 
ATOM   12026 C  CA    . LYS C 2 150 ? 111.757 73.942  134.615 1.00 24.77 ?  129 LYS C CA    1 
ATOM   12027 C  C     . LYS C 2 150 ? 112.592 73.662  133.363 1.00 24.54 ?  129 LYS C C     1 
ATOM   12028 O  O     . LYS C 2 150 ? 113.712 73.163  133.468 1.00 24.17 ?  129 LYS C O     1 
ATOM   12029 C  CB    . LYS C 2 150 ? 111.000 72.687  135.070 1.00 25.27 ?  129 LYS C CB    1 
ATOM   12030 C  CG    . LYS C 2 150 ? 109.893 72.215  134.151 1.00 28.72 ?  129 LYS C CG    1 
ATOM   12031 C  CD    . LYS C 2 150 ? 109.472 70.795  134.535 1.00 33.40 ?  129 LYS C CD    1 
ATOM   12032 C  CE    . LYS C 2 150 ? 108.076 70.479  134.035 1.00 36.77 ?  129 LYS C CE    1 
ATOM   12033 N  NZ    . LYS C 2 150 ? 107.605 69.178  134.603 1.00 39.66 1  129 LYS C NZ    1 
ATOM   12034 N  N     . TYR C 2 151 ? 112.043 73.980  132.185 1.00 23.92 ?  130 TYR C N     1 
ATOM   12035 C  CA    . TYR C 2 151 ? 112.761 73.777  130.920 1.00 24.12 ?  130 TYR C CA    1 
ATOM   12036 C  C     . TYR C 2 151 ? 113.885 74.781  130.726 1.00 23.54 ?  130 TYR C C     1 
ATOM   12037 O  O     . TYR C 2 151 ? 114.969 74.436  130.233 1.00 23.32 ?  130 TYR C O     1 
ATOM   12038 C  CB    . TYR C 2 151 ? 111.778 73.809  129.734 1.00 24.53 ?  130 TYR C CB    1 
ATOM   12039 C  CG    . TYR C 2 151 ? 110.522 73.011  130.008 1.00 25.83 ?  130 TYR C CG    1 
ATOM   12040 C  CD1   . TYR C 2 151 ? 110.582 71.630  130.197 1.00 26.57 ?  130 TYR C CD1   1 
ATOM   12041 C  CD2   . TYR C 2 151 ? 109.279 73.645  130.125 1.00 27.87 ?  130 TYR C CD2   1 
ATOM   12042 C  CE1   . TYR C 2 151 ? 109.438 70.889  130.472 1.00 29.65 ?  130 TYR C CE1   1 
ATOM   12043 C  CE2   . TYR C 2 151 ? 108.121 72.909  130.405 1.00 29.91 ?  130 TYR C CE2   1 
ATOM   12044 C  CZ    . TYR C 2 151 ? 108.213 71.534  130.577 1.00 31.19 ?  130 TYR C CZ    1 
ATOM   12045 O  OH    . TYR C 2 151 ? 107.082 70.792  130.853 1.00 34.44 ?  130 TYR C OH    1 
ATOM   12046 N  N     . LEU C 2 152 ? 113.624 76.024  131.117 1.00 23.38 ?  131 LEU C N     1 
ATOM   12047 C  CA    . LEU C 2 152 ? 114.612 77.083  131.033 1.00 23.43 ?  131 LEU C CA    1 
ATOM   12048 C  C     . LEU C 2 152 ? 115.728 76.838  132.054 1.00 23.37 ?  131 LEU C C     1 
ATOM   12049 O  O     . LEU C 2 152 ? 116.910 77.004  131.735 1.00 23.05 ?  131 LEU C O     1 
ATOM   12050 C  CB    . LEU C 2 152 ? 113.926 78.428  131.267 1.00 23.73 ?  131 LEU C CB    1 
ATOM   12051 C  CG    . LEU C 2 152 ? 114.154 79.680  130.429 1.00 24.71 ?  131 LEU C CG    1 
ATOM   12052 C  CD1   . LEU C 2 152 ? 114.772 79.441  129.041 1.00 21.63 ?  131 LEU C CD1   1 
ATOM   12053 C  CD2   . LEU C 2 152 ? 112.843 80.422  130.306 1.00 26.87 ?  131 LEU C CD2   1 
ATOM   12054 N  N     . GLN C 2 153 ? 115.363 76.445  133.278 1.00 22.80 ?  132 GLN C N     1 
ATOM   12055 C  CA    . GLN C 2 153 ? 116.382 76.049  134.263 1.00 22.70 ?  132 GLN C CA    1 
ATOM   12056 C  C     . GLN C 2 153 ? 117.210 74.838  133.822 1.00 22.54 ?  132 GLN C C     1 
ATOM   12057 O  O     . GLN C 2 153 ? 118.441 74.844  133.968 1.00 21.73 ?  132 GLN C O     1 
ATOM   12058 C  CB    . GLN C 2 153 ? 115.788 75.845  135.659 1.00 23.07 ?  132 GLN C CB    1 
ATOM   12059 C  CG    . GLN C 2 153 ? 115.212 77.132  136.251 1.00 21.83 ?  132 GLN C CG    1 
ATOM   12060 C  CD    . GLN C 2 153 ? 116.237 78.263  136.361 1.00 22.34 ?  132 GLN C CD    1 
ATOM   12061 O  OE1   . GLN C 2 153 ? 117.352 78.067  136.849 1.00 24.07 ?  132 GLN C OE1   1 
ATOM   12062 N  NE2   . GLN C 2 153 ? 115.852 79.453  135.920 1.00 22.26 ?  132 GLN C NE2   1 
ATOM   12063 N  N     . LYS C 2 154 ? 116.548 73.813  133.278 1.00 22.53 ?  133 LYS C N     1 
ATOM   12064 C  CA    . LYS C 2 154 ? 117.276 72.647  132.777 1.00 22.84 ?  133 LYS C CA    1 
ATOM   12065 C  C     . LYS C 2 154 ? 118.279 73.018  131.683 1.00 22.42 ?  133 LYS C C     1 
ATOM   12066 O  O     . LYS C 2 154 ? 119.417 72.566  131.728 1.00 21.90 ?  133 LYS C O     1 
ATOM   12067 C  CB    . LYS C 2 154 ? 116.339 71.507  132.314 1.00 22.96 ?  133 LYS C CB    1 
ATOM   12068 C  CG    . LYS C 2 154 ? 117.083 70.230  131.816 1.00 23.45 ?  133 LYS C CG    1 
ATOM   12069 C  CD    . LYS C 2 154 ? 117.896 69.521  132.921 1.00 26.74 ?  133 LYS C CD    1 
ATOM   12070 C  CE    . LYS C 2 154 ? 118.574 68.248  132.394 1.00 27.93 ?  133 LYS C CE    1 
ATOM   12071 N  NZ    . LYS C 2 154 ? 119.530 67.643  133.360 1.00 27.86 1  133 LYS C NZ    1 
ATOM   12072 N  N     . LYS C 2 155 ? 117.877 73.851  130.718 1.00 22.77 ?  134 LYS C N     1 
ATOM   12073 C  CA    . LYS C 2 155 ? 118.784 74.158  129.607 1.00 22.87 ?  134 LYS C CA    1 
ATOM   12074 C  C     . LYS C 2 155 ? 119.974 74.996  130.063 1.00 22.30 ?  134 LYS C C     1 
ATOM   12075 O  O     . LYS C 2 155 ? 121.113 74.730  129.646 1.00 21.89 ?  134 LYS C O     1 
ATOM   12076 C  CB    . LYS C 2 155 ? 118.061 74.737  128.368 1.00 23.33 ?  134 LYS C CB    1 
ATOM   12077 C  CG    . LYS C 2 155 ? 117.626 76.179  128.432 1.00 24.25 ?  134 LYS C CG    1 
ATOM   12078 C  CD    . LYS C 2 155 ? 116.938 76.611  127.125 1.00 26.87 ?  134 LYS C CD    1 
ATOM   12079 C  CE    . LYS C 2 155 ? 115.456 76.253  127.135 1.00 28.26 ?  134 LYS C CE    1 
ATOM   12080 N  NZ    . LYS C 2 155 ? 114.745 76.950  126.020 1.00 28.97 1  134 LYS C NZ    1 
ATOM   12081 N  N     . ALA C 2 156 ? 119.716 75.961  130.946 1.00 21.96 ?  135 ALA C N     1 
ATOM   12082 C  CA    . ALA C 2 156 ? 120.791 76.720  131.615 1.00 22.43 ?  135 ALA C CA    1 
ATOM   12083 C  C     . ALA C 2 156 ? 121.724 75.828  132.436 1.00 22.02 ?  135 ALA C C     1 
ATOM   12084 O  O     . ALA C 2 156 ? 122.939 75.994  132.381 1.00 22.60 ?  135 ALA C O     1 
ATOM   12085 C  CB    . ALA C 2 156 ? 120.215 77.837  132.511 1.00 22.05 ?  135 ALA C CB    1 
ATOM   12086 N  N     . GLN C 2 157 ? 121.157 74.901  133.209 1.00 21.97 ?  136 GLN C N     1 
ATOM   12087 C  CA    . GLN C 2 157 ? 121.963 73.969  134.009 1.00 22.10 ?  136 GLN C CA    1 
ATOM   12088 C  C     . GLN C 2 157 ? 122.923 73.189  133.134 1.00 21.87 ?  136 GLN C C     1 
ATOM   12089 O  O     . GLN C 2 157 ? 124.092 73.032  133.484 1.00 21.75 ?  136 GLN C O     1 
ATOM   12090 C  CB    . GLN C 2 157 ? 121.087 72.960  134.750 1.00 22.50 ?  136 GLN C CB    1 
ATOM   12091 C  CG    . GLN C 2 157 ? 120.446 73.479  136.029 1.00 23.55 ?  136 GLN C CG    1 
ATOM   12092 C  CD    . GLN C 2 157 ? 119.280 72.599  136.444 1.00 26.93 ?  136 GLN C CD    1 
ATOM   12093 O  OE1   . GLN C 2 157 ? 119.223 71.428  136.073 1.00 26.36 ?  136 GLN C OE1   1 
ATOM   12094 N  NE2   . GLN C 2 157 ? 118.335 73.163  137.188 1.00 28.09 ?  136 GLN C NE2   1 
ATOM   12095 N  N     . MET C 2 158 ? 122.411 72.693  132.009 1.00 21.38 ?  137 MET C N     1 
ATOM   12096 C  CA    . MET C 2 158 ? 123.184 71.848  131.112 1.00 22.08 ?  137 MET C CA    1 
ATOM   12097 C  C     . MET C 2 158 ? 124.287 72.618  130.396 1.00 21.70 ?  137 MET C C     1 
ATOM   12098 O  O     . MET C 2 158 ? 125.417 72.143  130.271 1.00 21.83 ?  137 MET C O     1 
ATOM   12099 C  CB    . MET C 2 158 ? 122.273 71.213  130.066 1.00 22.05 ?  137 MET C CB    1 
ATOM   12100 C  CG    . MET C 2 158 ? 121.403 70.065  130.595 1.00 23.93 ?  137 MET C CG    1 
ATOM   12101 S  SD    . MET C 2 158 ? 120.221 69.555  129.331 1.00 27.75 ?  137 MET C SD    1 
ATOM   12102 C  CE    . MET C 2 158 ? 121.348 68.800  128.148 1.00 26.00 ?  137 MET C CE    1 
ATOM   12103 N  N     . ILE C 2 159 ? 123.942 73.794  129.891 1.00 20.90 ?  138 ILE C N     1 
ATOM   12104 C  CA    . ILE C 2 159 ? 124.893 74.572  129.115 1.00 20.60 ?  138 ILE C CA    1 
ATOM   12105 C  C     . ILE C 2 159 ? 125.982 75.144  130.029 1.00 20.36 ?  138 ILE C C     1 
ATOM   12106 O  O     . ILE C 2 159 ? 127.171 74.984  129.745 1.00 19.65 ?  138 ILE C O     1 
ATOM   12107 C  CB    . ILE C 2 159 ? 124.186 75.678  128.278 1.00 20.17 ?  138 ILE C CB    1 
ATOM   12108 C  CG1   . ILE C 2 159 ? 123.297 75.052  127.188 1.00 20.66 ?  138 ILE C CG1   1 
ATOM   12109 C  CG2   . ILE C 2 159 ? 125.204 76.694  127.731 1.00 20.62 ?  138 ILE C CG2   1 
ATOM   12110 C  CD1   . ILE C 2 159 ? 124.003 74.247  126.093 1.00 22.17 ?  138 ILE C CD1   1 
ATOM   12111 N  N     . VAL C 2 160 ? 125.574 75.779  131.127 1.00 19.58 ?  139 VAL C N     1 
ATOM   12112 C  CA    . VAL C 2 160 ? 126.515 76.407  132.060 1.00 19.88 ?  139 VAL C CA    1 
ATOM   12113 C  C     . VAL C 2 160 ? 127.372 75.347  132.757 1.00 19.44 ?  139 VAL C C     1 
ATOM   12114 O  O     . VAL C 2 160 ? 128.526 75.593  133.088 1.00 19.88 ?  139 VAL C O     1 
ATOM   12115 C  CB    . VAL C 2 160 ? 125.799 77.312  133.126 1.00 19.52 ?  139 VAL C CB    1 
ATOM   12116 C  CG1   . VAL C 2 160 ? 126.810 77.878  134.139 1.00 20.75 ?  139 VAL C CG1   1 
ATOM   12117 C  CG2   . VAL C 2 160 ? 125.072 78.470  132.451 1.00 20.03 ?  139 VAL C CG2   1 
ATOM   12118 N  N     . GLY C 2 161 ? 126.806 74.163  132.973 1.00 19.13 ?  140 GLY C N     1 
ATOM   12119 C  CA    . GLY C 2 161 ? 127.561 73.084  133.590 1.00 18.05 ?  140 GLY C CA    1 
ATOM   12120 C  C     . GLY C 2 161 ? 128.756 72.726  132.744 1.00 17.86 ?  140 GLY C C     1 
ATOM   12121 O  O     . GLY C 2 161 ? 129.869 72.551  133.253 1.00 17.47 ?  140 GLY C O     1 
ATOM   12122 N  N     . LEU C 2 162 ? 128.525 72.602  131.442 1.00 17.92 ?  141 LEU C N     1 
ATOM   12123 C  CA    . LEU C 2 162 ? 129.606 72.316  130.506 1.00 18.32 ?  141 LEU C CA    1 
ATOM   12124 C  C     . LEU C 2 162 ? 130.660 73.444  130.445 1.00 18.55 ?  141 LEU C C     1 
ATOM   12125 O  O     . LEU C 2 162 ? 131.858 73.165  130.414 1.00 18.49 ?  141 LEU C O     1 
ATOM   12126 C  CB    . LEU C 2 162 ? 129.030 72.011  129.117 1.00 18.50 ?  141 LEU C CB    1 
ATOM   12127 C  CG    . LEU C 2 162 ? 128.292 70.673  129.032 1.00 19.32 ?  141 LEU C CG    1 
ATOM   12128 C  CD1   . LEU C 2 162 ? 127.432 70.615  127.775 1.00 20.38 ?  141 LEU C CD1   1 
ATOM   12129 C  CD2   . LEU C 2 162 ? 129.272 69.498  129.088 1.00 19.94 ?  141 LEU C CD2   1 
ATOM   12130 N  N     . TYR C 2 163 ? 130.226 74.702  130.463 1.00 19.16 ?  142 TYR C N     1 
ATOM   12131 C  CA    . TYR C 2 163 ? 131.171 75.834  130.543 1.00 20.16 ?  142 TYR C CA    1 
ATOM   12132 C  C     . TYR C 2 163 ? 132.061 75.751  131.770 1.00 20.78 ?  142 TYR C C     1 
ATOM   12133 O  O     . TYR C 2 163 ? 133.269 75.992  131.699 1.00 20.36 ?  142 TYR C O     1 
ATOM   12134 C  CB    . TYR C 2 163 ? 130.440 77.188  130.576 1.00 20.34 ?  142 TYR C CB    1 
ATOM   12135 C  CG    . TYR C 2 163 ? 129.667 77.537  129.312 1.00 22.46 ?  142 TYR C CG    1 
ATOM   12136 C  CD1   . TYR C 2 163 ? 129.999 76.979  128.082 1.00 23.88 ?  142 TYR C CD1   1 
ATOM   12137 C  CD2   . TYR C 2 163 ? 128.609 78.438  129.355 1.00 22.41 ?  142 TYR C CD2   1 
ATOM   12138 C  CE1   . TYR C 2 163 ? 129.278 77.306  126.919 1.00 25.93 ?  142 TYR C CE1   1 
ATOM   12139 C  CE2   . TYR C 2 163 ? 127.893 78.771  128.208 1.00 22.07 ?  142 TYR C CE2   1 
ATOM   12140 C  CZ    . TYR C 2 163 ? 128.235 78.212  127.000 1.00 25.19 ?  142 TYR C CZ    1 
ATOM   12141 O  OH    . TYR C 2 163 ? 127.507 78.559  125.880 1.00 27.43 ?  142 TYR C OH    1 
ATOM   12142 N  N     . LYS C 2 164 ? 131.460 75.404  132.902 1.00 21.39 ?  143 LYS C N     1 
ATOM   12143 C  CA    . LYS C 2 164 ? 132.204 75.410  134.151 1.00 22.49 ?  143 LYS C CA    1 
ATOM   12144 C  C     . LYS C 2 164 ? 133.032 74.142  134.350 1.00 22.49 ?  143 LYS C C     1 
ATOM   12145 O  O     . LYS C 2 164 ? 133.884 74.096  135.231 1.00 22.45 ?  143 LYS C O     1 
ATOM   12146 C  CB    . LYS C 2 164 ? 131.291 75.726  135.332 1.00 23.16 ?  143 LYS C CB    1 
ATOM   12147 C  CG    . LYS C 2 164 ? 130.784 77.166  135.275 1.00 26.08 ?  143 LYS C CG    1 
ATOM   12148 C  CD    . LYS C 2 164 ? 130.353 77.674  136.620 1.00 30.38 ?  143 LYS C CD    1 
ATOM   12149 C  CE    . LYS C 2 164 ? 130.042 79.150  136.560 1.00 32.69 ?  143 LYS C CE    1 
ATOM   12150 N  NZ    . LYS C 2 164 ? 129.568 79.631  137.888 1.00 35.60 1  143 LYS C NZ    1 
ATOM   12151 N  N     . ALA C 2 165 ? 132.830 73.152  133.480 1.00 22.02 ?  144 ALA C N     1 
ATOM   12152 C  CA    . ALA C 2 165 ? 133.622 71.938  133.523 1.00 22.69 ?  144 ALA C CA    1 
ATOM   12153 C  C     . ALA C 2 165 ? 134.936 72.044  132.731 1.00 23.20 ?  144 ALA C C     1 
ATOM   12154 O  O     . ALA C 2 165 ? 135.767 71.147  132.797 1.00 23.80 ?  144 ALA C O     1 
ATOM   12155 C  CB    . ALA C 2 165 ? 132.783 70.724  133.052 1.00 21.79 ?  144 ALA C CB    1 
ATOM   12156 N  N     . ILE C 2 166 ? 135.132 73.133  131.982 1.00 23.97 ?  145 ILE C N     1 
ATOM   12157 C  CA    . ILE C 2 166 ? 136.376 73.302  131.221 1.00 24.29 ?  145 ILE C CA    1 
ATOM   12158 C  C     . ILE C 2 166 ? 137.585 73.258  132.159 1.00 25.49 ?  145 ILE C C     1 
ATOM   12159 O  O     . ILE C 2 166 ? 137.595 73.906  133.200 1.00 25.82 ?  145 ILE C O     1 
ATOM   12160 C  CB    . ILE C 2 166 ? 136.407 74.620  130.394 1.00 24.22 ?  145 ILE C CB    1 
ATOM   12161 C  CG1   . ILE C 2 166 ? 135.268 74.660  129.380 1.00 23.45 ?  145 ILE C CG1   1 
ATOM   12162 C  CG2   . ILE C 2 166 ? 137.746 74.768  129.669 1.00 23.42 ?  145 ILE C CG2   1 
ATOM   12163 C  CD1   . ILE C 2 166 ? 135.045 76.059  128.750 1.00 21.99 ?  145 ILE C CD1   1 
ATOM   12164 N  N     . GLN C 2 167 ? 138.572 72.448  131.801 1.00 26.83 ?  146 GLN C N     1 
ATOM   12165 C  CA    . GLN C 2 167 ? 139.799 72.343  132.577 1.00 28.85 ?  146 GLN C CA    1 
ATOM   12166 C  C     . GLN C 2 167 ? 140.923 72.961  131.767 1.00 29.77 ?  146 GLN C C     1 
ATOM   12167 O  O     . GLN C 2 167 ? 141.015 72.740  130.555 1.00 29.74 ?  146 GLN C O     1 
ATOM   12168 C  CB    . GLN C 2 167 ? 140.128 70.880  132.912 1.00 28.99 ?  146 GLN C CB    1 
ATOM   12169 C  CG    . GLN C 2 167 ? 139.210 70.242  133.955 1.00 30.30 ?  146 GLN C CG    1 
ATOM   12170 C  CD    . GLN C 2 167 ? 139.425 70.796  135.358 1.00 33.32 ?  146 GLN C CD    1 
ATOM   12171 O  OE1   . GLN C 2 167 ? 140.387 71.525  135.609 1.00 34.63 ?  146 GLN C OE1   1 
ATOM   12172 N  NE2   . GLN C 2 167 ? 138.541 70.432  136.283 1.00 32.32 ?  146 GLN C NE2   1 
ATOM   12173 N  N     . LYS C 2 168 ? 141.768 73.735  132.437 1.00 31.29 ?  147 LYS C N     1 
ATOM   12174 C  CA    . LYS C 2 168 ? 142.906 74.380  131.782 1.00 33.14 ?  147 LYS C CA    1 
ATOM   12175 C  C     . LYS C 2 168 ? 143.735 73.330  131.055 1.00 33.79 ?  147 LYS C C     1 
ATOM   12176 O  O     . LYS C 2 168 ? 143.907 72.209  131.546 1.00 34.06 ?  147 LYS C O     1 
ATOM   12177 C  CB    . LYS C 2 168 ? 143.750 75.137  132.805 1.00 33.44 ?  147 LYS C CB    1 
ATOM   12178 C  CG    . LYS C 2 168 ? 144.642 76.238  132.234 1.00 35.61 ?  147 LYS C CG    1 
ATOM   12179 C  CD    . LYS C 2 168 ? 145.385 76.936  133.367 1.00 38.40 ?  147 LYS C CD    1 
ATOM   12180 C  CE    . LYS C 2 168 ? 146.069 78.217  132.919 1.00 40.48 ?  147 LYS C CE    1 
ATOM   12181 N  NZ    . LYS C 2 168 ? 147.505 77.972  132.619 1.00 41.56 1  147 LYS C NZ    1 
ATOM   12182 N  N     . ASP C 2 169 ? 144.199 73.687  129.861 1.00 35.10 ?  148 ASP C N     1 
ATOM   12183 C  CA    . ASP C 2 169 ? 145.021 72.799  129.022 1.00 36.27 ?  148 ASP C CA    1 
ATOM   12184 C  C     . ASP C 2 169 ? 144.373 71.462  128.659 1.00 36.29 ?  148 ASP C C     1 
ATOM   12185 O  O     . ASP C 2 169 ? 145.056 70.534  128.222 1.00 36.95 ?  148 ASP C O     1 
ATOM   12186 C  CB    . ASP C 2 169 ? 146.382 72.548  129.681 1.00 37.15 ?  148 ASP C CB    1 
ATOM   12187 C  CG    . ASP C 2 169 ? 147.261 73.770  129.681 1.00 38.94 ?  148 ASP C CG    1 
ATOM   12188 O  OD1   . ASP C 2 169 ? 147.036 74.676  128.845 1.00 41.71 ?  148 ASP C OD1   1 
ATOM   12189 O  OD2   . ASP C 2 169 ? 148.181 73.822  130.522 1.00 41.64 -1 148 ASP C OD2   1 
ATOM   12190 N  N     . ASP C 2 170 ? 143.062 71.355  128.843 1.00 35.87 ?  149 ASP C N     1 
ATOM   12191 C  CA    . ASP C 2 170 ? 142.352 70.135  128.481 1.00 35.24 ?  149 ASP C CA    1 
ATOM   12192 C  C     . ASP C 2 170 ? 141.404 70.474  127.339 1.00 34.12 ?  149 ASP C C     1 
ATOM   12193 O  O     . ASP C 2 170 ? 140.318 71.052  127.543 1.00 33.52 ?  149 ASP C O     1 
ATOM   12194 C  CB    . ASP C 2 170 ? 141.634 69.537  129.695 1.00 36.09 ?  149 ASP C CB    1 
ATOM   12195 C  CG    . ASP C 2 170 ? 140.719 68.366  129.337 1.00 38.39 ?  149 ASP C CG    1 
ATOM   12196 O  OD1   . ASP C 2 170 ? 140.815 67.803  128.221 1.00 42.06 ?  149 ASP C OD1   1 
ATOM   12197 O  OD2   . ASP C 2 170 ? 139.895 67.996  130.195 1.00 42.21 -1 149 ASP C OD2   1 
ATOM   12198 N  N     . GLU C 2 171 ? 141.846 70.120  126.136 1.00 32.48 ?  150 GLU C N     1 
ATOM   12199 C  CA    . GLU C 2 171 ? 141.167 70.497  124.909 1.00 30.93 ?  150 GLU C CA    1 
ATOM   12200 C  C     . GLU C 2 171 ? 139.814 69.800  124.742 1.00 29.37 ?  150 GLU C C     1 
ATOM   12201 O  O     . GLU C 2 171 ? 138.916 70.342  124.099 1.00 28.99 ?  150 GLU C O     1 
ATOM   12202 C  CB    . GLU C 2 171 ? 142.080 70.273  123.687 1.00 31.30 ?  150 GLU C CB    1 
ATOM   12203 C  CG    . GLU C 2 171 ? 142.346 68.803  123.284 1.00 33.64 ?  150 GLU C CG    1 
ATOM   12204 C  CD    . GLU C 2 171 ? 143.495 68.630  122.261 1.00 36.40 ?  150 GLU C CD    1 
ATOM   12205 O  OE1   . GLU C 2 171 ? 144.082 69.640  121.814 1.00 38.62 ?  150 GLU C OE1   1 
ATOM   12206 O  OE2   . GLU C 2 171 ? 143.815 67.474  121.902 1.00 37.42 -1 150 GLU C OE2   1 
ATOM   12207 N  N     . ILE C 2 172 ? 139.672 68.605  125.317 1.00 27.68 ?  151 ILE C N     1 
ATOM   12208 C  CA    . ILE C 2 172 ? 138.416 67.858  125.211 1.00 26.26 ?  151 ILE C CA    1 
ATOM   12209 C  C     . ILE C 2 172 ? 137.297 68.541  126.001 1.00 24.85 ?  151 ILE C C     1 
ATOM   12210 O  O     . ILE C 2 172 ? 136.186 68.672  125.491 1.00 23.53 ?  151 ILE C O     1 
ATOM   12211 C  CB    . ILE C 2 172 ? 138.573 66.367  125.614 1.00 26.53 ?  151 ILE C CB    1 
ATOM   12212 C  CG1   . ILE C 2 172 ? 139.576 65.657  124.691 1.00 27.59 ?  151 ILE C CG1   1 
ATOM   12213 C  CG2   . ILE C 2 172 ? 137.213 65.644  125.645 1.00 26.51 ?  151 ILE C CG2   1 
ATOM   12214 C  CD1   . ILE C 2 172 ? 139.136 65.505  123.228 1.00 26.91 ?  151 ILE C CD1   1 
ATOM   12215 N  N     . SER C 2 173 ? 137.583 68.987  127.227 1.00 23.58 ?  152 SER C N     1 
ATOM   12216 C  CA    . SER C 2 173 ? 136.565 69.698  127.997 1.00 22.36 ?  152 SER C CA    1 
ATOM   12217 C  C     . SER C 2 173 ? 136.193 71.011  127.305 1.00 21.79 ?  152 SER C C     1 
ATOM   12218 O  O     . SER C 2 173 ? 135.034 71.442  127.353 1.00 20.91 ?  152 SER C O     1 
ATOM   12219 C  CB    . SER C 2 173 ? 136.989 69.921  129.454 1.00 22.43 ?  152 SER C CB    1 
ATOM   12220 O  OG    . SER C 2 173 ? 138.167 70.704  129.544 1.00 24.02 ?  152 SER C OG    1 
ATOM   12221 N  N     . LEU C 2 174 ? 137.181 71.639  126.667 1.00 21.65 ?  153 LEU C N     1 
ATOM   12222 C  CA    . LEU C 2 174 ? 136.957 72.874  125.920 1.00 21.86 ?  153 LEU C CA    1 
ATOM   12223 C  C     . LEU C 2 174 ? 136.058 72.627  124.707 1.00 21.98 ?  153 LEU C C     1 
ATOM   12224 O  O     . LEU C 2 174 ? 135.111 73.385  124.487 1.00 21.64 ?  153 LEU C O     1 
ATOM   12225 C  CB    . LEU C 2 174 ? 138.285 73.549  125.515 1.00 21.71 ?  153 LEU C CB    1 
ATOM   12226 C  CG    . LEU C 2 174 ? 138.233 74.861  124.708 1.00 22.04 ?  153 LEU C CG    1 
ATOM   12227 C  CD1   . LEU C 2 174 ? 137.343 75.920  125.357 1.00 21.99 ?  153 LEU C CD1   1 
ATOM   12228 C  CD2   . LEU C 2 174 ? 139.652 75.404  124.504 1.00 23.37 ?  153 LEU C CD2   1 
ATOM   12229 N  N     . PHE C 2 175 ? 136.350 71.572  123.940 1.00 22.17 ?  154 PHE C N     1 
ATOM   12230 C  CA    . PHE C 2 175 ? 135.506 71.162  122.795 1.00 22.02 ?  154 PHE C CA    1 
ATOM   12231 C  C     . PHE C 2 175 ? 134.049 70.973  123.198 1.00 21.86 ?  154 PHE C C     1 
ATOM   12232 O  O     . PHE C 2 175 ? 133.132 71.406  122.489 1.00 21.62 ?  154 PHE C O     1 
ATOM   12233 C  CB    . PHE C 2 175 ? 136.016 69.848  122.180 1.00 22.08 ?  154 PHE C CB    1 
ATOM   12234 C  CG    . PHE C 2 175 ? 135.106 69.276  121.111 1.00 21.99 ?  154 PHE C CG    1 
ATOM   12235 C  CD1   . PHE C 2 175 ? 135.175 69.739  119.794 1.00 20.87 ?  154 PHE C CD1   1 
ATOM   12236 C  CD2   . PHE C 2 175 ? 134.168 68.282  121.428 1.00 20.82 ?  154 PHE C CD2   1 
ATOM   12237 C  CE1   . PHE C 2 175 ? 134.322 69.238  118.809 1.00 20.27 ?  154 PHE C CE1   1 
ATOM   12238 C  CE2   . PHE C 2 175 ? 133.313 67.761  120.453 1.00 20.19 ?  154 PHE C CE2   1 
ATOM   12239 C  CZ    . PHE C 2 175 ? 133.393 68.236  119.132 1.00 20.93 ?  154 PHE C CZ    1 
ATOM   12240 N  N     . LYS C 2 176 ? 133.843 70.284  124.322 1.00 21.98 ?  155 LYS C N     1 
ATOM   12241 C  CA    . LYS C 2 176 ? 132.492 70.005  124.815 1.00 21.79 ?  155 LYS C CA    1 
ATOM   12242 C  C     . LYS C 2 176 ? 131.730 71.300  125.119 1.00 21.70 ?  155 LYS C C     1 
ATOM   12243 O  O     . LYS C 2 176 ? 130.551 71.434  124.762 1.00 21.10 ?  155 LYS C O     1 
ATOM   12244 C  CB    . LYS C 2 176 ? 132.545 69.080  126.037 1.00 22.00 ?  155 LYS C CB    1 
ATOM   12245 C  CG    . LYS C 2 176 ? 133.049 67.676  125.729 1.00 21.93 ?  155 LYS C CG    1 
ATOM   12246 C  CD    . LYS C 2 176 ? 133.148 66.824  126.982 1.00 23.06 ?  155 LYS C CD    1 
ATOM   12247 C  CE    . LYS C 2 176 ? 133.587 65.411  126.660 1.00 24.91 ?  155 LYS C CE    1 
ATOM   12248 N  NZ    . LYS C 2 176 ? 134.001 64.671  127.899 1.00 25.16 1  155 LYS C NZ    1 
ATOM   12249 N  N     . ALA C 2 177 ? 132.408 72.249  125.773 1.00 21.49 ?  156 ALA C N     1 
ATOM   12250 C  CA    . ALA C 2 177 ? 131.821 73.562  126.023 1.00 20.60 ?  156 ALA C CA    1 
ATOM   12251 C  C     . ALA C 2 177 ? 131.550 74.364  124.730 1.00 20.37 ?  156 ALA C C     1 
ATOM   12252 O  O     . ALA C 2 177 ? 130.553 75.067  124.644 1.00 19.61 ?  156 ALA C O     1 
ATOM   12253 C  CB    . ALA C 2 177 ? 132.679 74.372  126.989 1.00 20.88 ?  156 ALA C CB    1 
ATOM   12254 N  N     . MET C 2 178 ? 132.428 74.242  123.734 1.00 20.70 ?  157 MET C N     1 
ATOM   12255 C  CA    . MET C 2 178 ? 132.219 74.912  122.439 1.00 21.06 ?  157 MET C CA    1 
ATOM   12256 C  C     . MET C 2 178 ? 131.041 74.327  121.685 1.00 20.83 ?  157 MET C C     1 
ATOM   12257 O  O     . MET C 2 178 ? 130.353 75.048  120.954 1.00 21.28 ?  157 MET C O     1 
ATOM   12258 C  CB    . MET C 2 178 ? 133.471 74.836  121.545 1.00 20.68 ?  157 MET C CB    1 
ATOM   12259 C  CG    . MET C 2 178 ? 134.676 75.649  122.015 1.00 21.61 ?  157 MET C CG    1 
ATOM   12260 S  SD    . MET C 2 178 ? 136.131 75.265  121.014 1.00 24.32 ?  157 MET C SD    1 
ATOM   12261 C  CE    . MET C 2 178 ? 137.245 76.592  121.520 1.00 23.64 ?  157 MET C CE    1 
ATOM   12262 N  N     . VAL C 2 179 ? 130.824 73.019  121.821 1.00 20.76 ?  158 VAL C N     1 
ATOM   12263 C  CA    . VAL C 2 179 ? 129.644 72.380  121.224 1.00 20.14 ?  158 VAL C CA    1 
ATOM   12264 C  C     . VAL C 2 179 ? 128.386 72.947  121.891 1.00 20.35 ?  158 VAL C C     1 
ATOM   12265 O  O     . VAL C 2 179 ? 127.414 73.302  121.218 1.00 19.82 ?  158 VAL C O     1 
ATOM   12266 C  CB    . VAL C 2 179 ? 129.666 70.837  121.390 1.00 20.07 ?  158 VAL C CB    1 
ATOM   12267 C  CG1   . VAL C 2 179 ? 128.317 70.233  120.991 1.00 20.07 ?  158 VAL C CG1   1 
ATOM   12268 C  CG2   . VAL C 2 179 ? 130.786 70.225  120.555 1.00 20.57 ?  158 VAL C CG2   1 
ATOM   12269 N  N     . ALA C 2 180 ? 128.426 73.028  123.217 1.00 19.89 ?  159 ALA C N     1 
ATOM   12270 C  CA    . ALA C 2 180 ? 127.330 73.598  124.000 1.00 20.50 ?  159 ALA C CA    1 
ATOM   12271 C  C     . ALA C 2 180 ? 127.040 75.041  123.556 1.00 20.67 ?  159 ALA C C     1 
ATOM   12272 O  O     . ALA C 2 180 ? 125.881 75.410  123.354 1.00 21.27 ?  159 ALA C O     1 
ATOM   12273 C  CB    . ALA C 2 180 ? 127.678 73.560  125.472 1.00 20.03 ?  159 ALA C CB    1 
ATOM   12274 N  N     . SER C 2 181 ? 128.095 75.838  123.394 1.00 20.78 ?  160 SER C N     1 
ATOM   12275 C  CA    . SER C 2 181 ? 127.974 77.222  122.921 1.00 21.26 ?  160 SER C CA    1 
ATOM   12276 C  C     . SER C 2 181 ? 127.385 77.310  121.506 1.00 21.19 ?  160 SER C C     1 
ATOM   12277 O  O     . SER C 2 181 ? 126.487 78.107  121.262 1.00 20.89 ?  160 SER C O     1 
ATOM   12278 C  CB    . SER C 2 181 ? 129.327 77.947  122.995 1.00 21.42 ?  160 SER C CB    1 
ATOM   12279 O  OG    . SER C 2 181 ? 129.199 79.312  122.624 1.00 23.69 ?  160 SER C OG    1 
ATOM   12280 N  N     . VAL C 2 182 ? 127.886 76.495  120.571 1.00 20.99 ?  161 VAL C N     1 
ATOM   12281 C  CA    . VAL C 2 182 ? 127.267 76.456  119.241 1.00 21.18 ?  161 VAL C CA    1 
ATOM   12282 C  C     . VAL C 2 182 ? 125.777 76.085  119.336 1.00 21.15 ?  161 VAL C C     1 
ATOM   12283 O  O     . VAL C 2 182 ? 124.933 76.710  118.673 1.00 21.18 ?  161 VAL C O     1 
ATOM   12284 C  CB    . VAL C 2 182 ? 128.021 75.512  118.251 1.00 21.11 ?  161 VAL C CB    1 
ATOM   12285 C  CG1   . VAL C 2 182 ? 127.229 75.345  116.956 1.00 21.75 ?  161 VAL C CG1   1 
ATOM   12286 C  CG2   . VAL C 2 182 ? 129.417 76.057  117.951 1.00 20.98 ?  161 VAL C CG2   1 
ATOM   12287 N  N     . TYR C 2 183 ? 125.439 75.087  120.165 1.00 21.10 ?  162 TYR C N     1 
ATOM   12288 C  CA    . TYR C 2 183 ? 124.029 74.709  120.340 1.00 21.21 ?  162 TYR C CA    1 
ATOM   12289 C  C     . TYR C 2 183 ? 123.178 75.835  120.927 1.00 21.38 ?  162 TYR C C     1 
ATOM   12290 O  O     . TYR C 2 183 ? 122.007 75.965  120.589 1.00 20.97 ?  162 TYR C O     1 
ATOM   12291 C  CB    . TYR C 2 183 ? 123.855 73.428  121.181 1.00 21.50 ?  162 TYR C CB    1 
ATOM   12292 C  CG    . TYR C 2 183 ? 124.281 72.167  120.478 1.00 22.20 ?  162 TYR C CG    1 
ATOM   12293 C  CD1   . TYR C 2 183 ? 124.372 72.118  119.088 1.00 23.80 ?  162 TYR C CD1   1 
ATOM   12294 C  CD2   . TYR C 2 183 ? 124.577 71.007  121.202 1.00 23.71 ?  162 TYR C CD2   1 
ATOM   12295 C  CE1   . TYR C 2 183 ? 124.769 70.947  118.431 1.00 25.52 ?  162 TYR C CE1   1 
ATOM   12296 C  CE2   . TYR C 2 183 ? 124.966 69.842  120.561 1.00 24.01 ?  162 TYR C CE2   1 
ATOM   12297 C  CZ    . TYR C 2 183 ? 125.070 69.818  119.181 1.00 25.47 ?  162 TYR C CZ    1 
ATOM   12298 O  OH    . TYR C 2 183 ? 125.473 68.665  118.538 1.00 25.37 ?  162 TYR C OH    1 
ATOM   12299 N  N     . LEU C 2 184 ? 123.766 76.626  121.812 1.00 22.12 ?  163 LEU C N     1 
ATOM   12300 C  CA    . LEU C 2 184 ? 123.082 77.824  122.339 1.00 23.80 ?  163 LEU C CA    1 
ATOM   12301 C  C     . LEU C 2 184 ? 122.913 78.874  121.232 1.00 24.21 ?  163 LEU C C     1 
ATOM   12302 O  O     . LEU C 2 184 ? 121.833 79.402  121.066 1.00 24.72 ?  163 LEU C O     1 
ATOM   12303 C  CB    . LEU C 2 184 ? 123.839 78.407  123.536 1.00 23.52 ?  163 LEU C CB    1 
ATOM   12304 C  CG    . LEU C 2 184 ? 123.260 79.606  124.314 1.00 24.91 ?  163 LEU C CG    1 
ATOM   12305 C  CD1   . LEU C 2 184 ? 123.634 79.496  125.770 1.00 24.81 ?  163 LEU C CD1   1 
ATOM   12306 C  CD2   . LEU C 2 184 ? 123.701 80.965  123.753 1.00 26.39 ?  163 LEU C CD2   1 
ATOM   12307 N  N     . GLU C 2 185 ? 123.980 79.151  120.471 1.00 25.17 ?  164 GLU C N     1 
ATOM   12308 C  CA    . GLU C 2 185 ? 123.964 80.211  119.451 1.00 25.30 ?  164 GLU C CA    1 
ATOM   12309 C  C     . GLU C 2 185 ? 123.029 79.910  118.268 1.00 25.07 ?  164 GLU C C     1 
ATOM   12310 O  O     . GLU C 2 185 ? 122.290 80.788  117.791 1.00 24.49 ?  164 GLU C O     1 
ATOM   12311 C  CB    . GLU C 2 185 ? 125.384 80.461  118.891 1.00 26.17 ?  164 GLU C CB    1 
ATOM   12312 C  CG    . GLU C 2 185 ? 126.398 81.036  119.906 1.00 27.05 ?  164 GLU C CG    1 
ATOM   12313 C  CD    . GLU C 2 185 ? 126.213 82.536  120.163 1.00 29.23 ?  164 GLU C CD    1 
ATOM   12314 O  OE1   . GLU C 2 185 ? 125.292 83.171  119.574 1.00 28.79 ?  164 GLU C OE1   1 
ATOM   12315 O  OE2   . GLU C 2 185 ? 127.017 83.110  120.934 1.00 28.65 -1 164 GLU C OE2   1 
ATOM   12316 N  N     . SER C 2 186 ? 123.096 78.671  117.797 1.00 24.23 ?  165 SER C N     1 
ATOM   12317 C  CA    . SER C 2 186 ? 122.580 78.295  116.486 1.00 24.71 ?  165 SER C CA    1 
ATOM   12318 C  C     . SER C 2 186 ? 121.347 77.400  116.546 1.00 24.51 ?  165 SER C C     1 
ATOM   12319 O  O     . SER C 2 186 ? 120.728 77.140  115.517 1.00 24.87 ?  165 SER C O     1 
ATOM   12320 C  CB    . SER C 2 186 ? 123.679 77.585  115.684 1.00 25.06 ?  165 SER C CB    1 
ATOM   12321 O  OG    . SER C 2 186 ? 124.822 78.405  115.532 1.00 26.29 ?  165 SER C OG    1 
ATOM   12322 N  N     . PHE C 2 187 ? 121.007 76.922  117.741 1.00 24.71 ?  166 PHE C N     1 
ATOM   12323 C  CA    . PHE C 2 187 ? 119.851 76.049  117.937 1.00 25.69 ?  166 PHE C CA    1 
ATOM   12324 C  C     . PHE C 2 187 ? 118.886 76.587  119.006 1.00 25.87 ?  166 PHE C C     1 
ATOM   12325 O  O     . PHE C 2 187 ? 117.730 76.870  118.689 1.00 26.03 ?  166 PHE C O     1 
ATOM   12326 C  CB    . PHE C 2 187 ? 120.290 74.609  118.265 1.00 25.54 ?  166 PHE C CB    1 
ATOM   12327 C  CG    . PHE C 2 187 ? 119.168 73.710  118.743 1.00 26.64 ?  166 PHE C CG    1 
ATOM   12328 C  CD1   . PHE C 2 187 ? 118.070 73.430  117.919 1.00 25.90 ?  166 PHE C CD1   1 
ATOM   12329 C  CD2   . PHE C 2 187 ? 119.215 73.132  120.015 1.00 27.45 ?  166 PHE C CD2   1 
ATOM   12330 C  CE1   . PHE C 2 187 ? 117.024 72.598  118.363 1.00 25.64 ?  166 PHE C CE1   1 
ATOM   12331 C  CE2   . PHE C 2 187 ? 118.173 72.291  120.472 1.00 26.52 ?  166 PHE C CE2   1 
ATOM   12332 C  CZ    . PHE C 2 187 ? 117.081 72.027  119.641 1.00 27.18 ?  166 PHE C CZ    1 
ATOM   12333 N  N     . LEU C 2 188 ? 119.369 76.734  120.242 1.00 26.13 ?  167 LEU C N     1 
ATOM   12334 C  CA    . LEU C 2 188 ? 118.516 77.075  121.410 1.00 27.13 ?  167 LEU C CA    1 
ATOM   12335 C  C     . LEU C 2 188 ? 117.812 78.444  121.359 1.00 27.22 ?  167 LEU C C     1 
ATOM   12336 O  O     . LEU C 2 188 ? 116.718 78.602  121.918 1.00 28.03 ?  167 LEU C O     1 
ATOM   12337 C  CB    . LEU C 2 188 ? 119.312 76.986  122.722 1.00 26.89 ?  167 LEU C CB    1 
ATOM   12338 C  CG    . LEU C 2 188 ? 119.866 75.658  123.260 1.00 28.64 ?  167 LEU C CG    1 
ATOM   12339 C  CD1   . LEU C 2 188 ? 120.645 75.897  124.552 1.00 28.34 ?  167 LEU C CD1   1 
ATOM   12340 C  CD2   . LEU C 2 188 ? 118.777 74.625  123.493 1.00 27.90 ?  167 LEU C CD2   1 
ATOM   12341 N  N     . PHE C 2 189 ? 118.448 79.431  120.739 1.00 26.79 ?  168 PHE C N     1 
ATOM   12342 C  CA    . PHE C 2 189 ? 117.842 80.756  120.617 1.00 26.90 ?  168 PHE C CA    1 
ATOM   12343 C  C     . PHE C 2 189 ? 116.587 80.717  119.737 1.00 26.52 ?  168 PHE C C     1 
ATOM   12344 O  O     . PHE C 2 189 ? 115.735 81.611  119.816 1.00 26.02 ?  168 PHE C O     1 
ATOM   12345 C  CB    . PHE C 2 189 ? 118.829 81.770  120.005 1.00 27.03 ?  168 PHE C CB    1 
ATOM   12346 C  CG    . PHE C 2 189 ? 119.755 82.452  121.010 1.00 28.09 ?  168 PHE C CG    1 
ATOM   12347 C  CD1   . PHE C 2 189 ? 119.249 83.149  122.109 1.00 28.69 ?  168 PHE C CD1   1 
ATOM   12348 C  CD2   . PHE C 2 189 ? 121.129 82.458  120.806 1.00 29.15 ?  168 PHE C CD2   1 
ATOM   12349 C  CE1   . PHE C 2 189 ? 120.099 83.794  123.020 1.00 28.50 ?  168 PHE C CE1   1 
ATOM   12350 C  CE2   . PHE C 2 189 ? 121.997 83.101  121.708 1.00 30.19 ?  168 PHE C CE2   1 
ATOM   12351 C  CZ    . PHE C 2 189 ? 121.471 83.773  122.827 1.00 29.81 ?  168 PHE C CZ    1 
ATOM   12352 N  N     . TYR C 2 190 ? 116.480 79.697  118.884 1.00 26.18 ?  169 TYR C N     1 
ATOM   12353 C  CA    . TYR C 2 190 ? 115.524 79.775  117.786 1.00 26.24 ?  169 TYR C CA    1 
ATOM   12354 C  C     . TYR C 2 190 ? 114.051 79.520  118.140 1.00 25.94 ?  169 TYR C C     1 
ATOM   12355 O  O     . TYR C 2 190 ? 113.151 80.003  117.451 1.00 25.71 ?  169 TYR C O     1 
ATOM   12356 C  CB    . TYR C 2 190 ? 116.037 79.000  116.570 1.00 27.13 ?  169 TYR C CB    1 
ATOM   12357 C  CG    . TYR C 2 190 ? 117.118 79.803  115.880 1.00 28.07 ?  169 TYR C CG    1 
ATOM   12358 C  CD1   . TYR C 2 190 ? 118.448 79.746  116.316 1.00 29.54 ?  169 TYR C CD1   1 
ATOM   12359 C  CD2   . TYR C 2 190 ? 116.804 80.677  114.839 1.00 29.31 ?  169 TYR C CD2   1 
ATOM   12360 C  CE1   . TYR C 2 190 ? 119.443 80.512  115.701 1.00 30.44 ?  169 TYR C CE1   1 
ATOM   12361 C  CE2   . TYR C 2 190 ? 117.796 81.449  114.214 1.00 30.64 ?  169 TYR C CE2   1 
ATOM   12362 C  CZ    . TYR C 2 190 ? 119.110 81.363  114.655 1.00 30.40 ?  169 TYR C CZ    1 
ATOM   12363 O  OH    . TYR C 2 190 ? 120.085 82.124  114.052 1.00 28.85 ?  169 TYR C OH    1 
ATOM   12364 N  N     . SER C 2 191 ? 113.813 78.816  119.244 1.00 25.17 ?  170 SER C N     1 
ATOM   12365 C  CA    . SER C 2 191 ? 112.457 78.653  119.763 1.00 25.10 ?  170 SER C CA    1 
ATOM   12366 C  C     . SER C 2 191 ? 111.929 80.025  120.201 1.00 25.16 ?  170 SER C C     1 
ATOM   12367 O  O     . SER C 2 191 ? 110.722 80.279  120.144 1.00 25.30 ?  170 SER C O     1 
ATOM   12368 C  CB    . SER C 2 191 ? 112.429 77.653  120.919 1.00 24.56 ?  170 SER C CB    1 
ATOM   12369 O  OG    . SER C 2 191 ? 113.168 78.129  122.028 1.00 24.98 ?  170 SER C OG    1 
ATOM   12370 N  N     . GLY C 2 192 ? 112.860 80.889  120.623 1.00 24.32 ?  171 GLY C N     1 
ATOM   12371 C  CA    . GLY C 2 192 ? 112.585 82.273  120.985 1.00 23.97 ?  171 GLY C CA    1 
ATOM   12372 C  C     . GLY C 2 192 ? 112.487 83.208  119.791 1.00 23.85 ?  171 GLY C C     1 
ATOM   12373 O  O     . GLY C 2 192 ? 111.507 83.946  119.680 1.00 23.99 ?  171 GLY C O     1 
ATOM   12374 N  N     . PHE C 2 193 ? 113.477 83.166  118.897 1.00 23.28 ?  172 PHE C N     1 
ATOM   12375 C  CA    . PHE C 2 193 ? 113.496 84.025  117.698 1.00 23.85 ?  172 PHE C CA    1 
ATOM   12376 C  C     . PHE C 2 193 ? 112.272 83.870  116.793 1.00 23.72 ?  172 PHE C C     1 
ATOM   12377 O  O     . PHE C 2 193 ? 111.909 84.810  116.090 1.00 23.92 ?  172 PHE C O     1 
ATOM   12378 C  CB    . PHE C 2 193 ? 114.739 83.777  116.833 1.00 23.47 ?  172 PHE C CB    1 
ATOM   12379 C  CG    . PHE C 2 193 ? 116.023 84.333  117.407 1.00 24.32 ?  172 PHE C CG    1 
ATOM   12380 C  CD1   . PHE C 2 193 ? 116.011 85.394  118.315 1.00 22.28 ?  172 PHE C CD1   1 
ATOM   12381 C  CD2   . PHE C 2 193 ? 117.252 83.804  117.009 1.00 23.82 ?  172 PHE C CD2   1 
ATOM   12382 C  CE1   . PHE C 2 193 ? 117.201 85.909  118.844 1.00 23.41 ?  172 PHE C CE1   1 
ATOM   12383 C  CE2   . PHE C 2 193 ? 118.458 84.308  117.528 1.00 24.70 ?  172 PHE C CE2   1 
ATOM   12384 C  CZ    . PHE C 2 193 ? 118.431 85.369  118.447 1.00 24.87 ?  172 PHE C CZ    1 
ATOM   12385 N  N     . TYR C 2 194 ? 111.665 82.681  116.789 1.00 23.31 ?  173 TYR C N     1 
ATOM   12386 C  CA    . TYR C 2 194 ? 110.542 82.391  115.894 1.00 23.26 ?  173 TYR C CA    1 
ATOM   12387 C  C     . TYR C 2 194 ? 109.467 83.480  115.956 1.00 23.04 ?  173 TYR C C     1 
ATOM   12388 O  O     . TYR C 2 194 ? 108.991 83.955  114.921 1.00 23.47 ?  173 TYR C O     1 
ATOM   12389 C  CB    . TYR C 2 194 ? 109.902 81.025  116.201 1.00 23.13 ?  173 TYR C CB    1 
ATOM   12390 C  CG    . TYR C 2 194 ? 108.799 80.644  115.222 1.00 24.10 ?  173 TYR C CG    1 
ATOM   12391 C  CD1   . TYR C 2 194 ? 109.080 79.854  114.106 1.00 25.72 ?  173 TYR C CD1   1 
ATOM   12392 C  CD2   . TYR C 2 194 ? 107.489 81.092  115.397 1.00 27.04 ?  173 TYR C CD2   1 
ATOM   12393 C  CE1   . TYR C 2 194 ? 108.074 79.501  113.197 1.00 28.94 ?  173 TYR C CE1   1 
ATOM   12394 C  CE2   . TYR C 2 194 ? 106.473 80.752  114.484 1.00 27.84 ?  173 TYR C CE2   1 
ATOM   12395 C  CZ    . TYR C 2 194 ? 106.780 79.958  113.391 1.00 29.97 ?  173 TYR C CZ    1 
ATOM   12396 O  OH    . TYR C 2 194 ? 105.799 79.619  112.476 1.00 34.34 ?  173 TYR C OH    1 
ATOM   12397 N  N     . TYR C 2 195 ? 109.090 83.861  117.167 1.00 22.51 ?  174 TYR C N     1 
ATOM   12398 C  CA    . TYR C 2 195 ? 107.896 84.676  117.363 1.00 22.60 ?  174 TYR C CA    1 
ATOM   12399 C  C     . TYR C 2 195 ? 108.075 86.142  116.928 1.00 22.64 ?  174 TYR C C     1 
ATOM   12400 O  O     . TYR C 2 195 ? 107.215 86.658  116.206 1.00 22.39 ?  174 TYR C O     1 
ATOM   12401 C  CB    . TYR C 2 195 ? 107.385 84.537  118.797 1.00 22.32 ?  174 TYR C CB    1 
ATOM   12402 C  CG    . TYR C 2 195 ? 105.884 84.684  118.955 1.00 23.39 ?  174 TYR C CG    1 
ATOM   12403 C  CD1   . TYR C 2 195 ? 104.998 84.272  117.947 1.00 22.84 ?  174 TYR C CD1   1 
ATOM   12404 C  CD2   . TYR C 2 195 ? 105.350 85.200  120.134 1.00 22.23 ?  174 TYR C CD2   1 
ATOM   12405 C  CE1   . TYR C 2 195 ? 103.613 84.402  118.109 1.00 24.05 ?  174 TYR C CE1   1 
ATOM   12406 C  CE2   . TYR C 2 195 ? 103.970 85.321  120.311 1.00 24.11 ?  174 TYR C CE2   1 
ATOM   12407 C  CZ    . TYR C 2 195 ? 103.113 84.920  119.301 1.00 23.92 ?  174 TYR C CZ    1 
ATOM   12408 O  OH    . TYR C 2 195 ? 101.764 85.067  119.481 1.00 25.00 ?  174 TYR C OH    1 
ATOM   12409 N  N     . PRO C 2 196 ? 109.192 86.808  117.344 1.00 22.25 ?  175 PRO C N     1 
ATOM   12410 C  CA    . PRO C 2 196 ? 109.458 88.144  116.785 1.00 22.45 ?  175 PRO C CA    1 
ATOM   12411 C  C     . PRO C 2 196 ? 109.560 88.141  115.259 1.00 22.59 ?  175 PRO C C     1 
ATOM   12412 O  O     . PRO C 2 196 ? 109.085 89.086  114.619 1.00 22.19 ?  175 PRO C O     1 
ATOM   12413 C  CB    . PRO C 2 196 ? 110.804 88.548  117.404 1.00 22.25 ?  175 PRO C CB    1 
ATOM   12414 C  CG    . PRO C 2 196 ? 110.954 87.705  118.628 1.00 22.22 ?  175 PRO C CG    1 
ATOM   12415 C  CD    . PRO C 2 196 ? 110.200 86.426  118.360 1.00 22.32 ?  175 PRO C CD    1 
ATOM   12416 N  N     . LEU C 2 197 ? 110.161 87.093  114.687 1.00 21.92 ?  176 LEU C N     1 
ATOM   12417 C  CA    . LEU C 2 197 ? 110.270 86.974  113.231 1.00 22.35 ?  176 LEU C CA    1 
ATOM   12418 C  C     . LEU C 2 197 ? 108.897 86.764  112.584 1.00 22.60 ?  176 LEU C C     1 
ATOM   12419 O  O     . LEU C 2 197 ? 108.609 87.308  111.514 1.00 22.41 ?  176 LEU C O     1 
ATOM   12420 C  CB    . LEU C 2 197 ? 111.199 85.829  112.832 1.00 22.69 ?  176 LEU C CB    1 
ATOM   12421 C  CG    . LEU C 2 197 ? 112.691 85.878  113.187 1.00 23.68 ?  176 LEU C CG    1 
ATOM   12422 C  CD1   . LEU C 2 197 ? 113.377 84.593  112.697 1.00 23.70 ?  176 LEU C CD1   1 
ATOM   12423 C  CD2   . LEU C 2 197 ? 113.360 87.110  112.585 1.00 23.09 ?  176 LEU C CD2   1 
ATOM   12424 N  N     . TYR C 2 198 ? 108.059 85.970  113.247 1.00 22.64 ?  177 TYR C N     1 
ATOM   12425 C  CA    . TYR C 2 198 ? 106.716 85.667  112.774 1.00 22.92 ?  177 TYR C CA    1 
ATOM   12426 C  C     . TYR C 2 198 ? 105.891 86.965  112.690 1.00 23.68 ?  177 TYR C C     1 
ATOM   12427 O  O     . TYR C 2 198 ? 105.186 87.203  111.706 1.00 23.81 ?  177 TYR C O     1 
ATOM   12428 C  CB    . TYR C 2 198 ? 106.091 84.646  113.718 1.00 22.73 ?  177 TYR C CB    1 
ATOM   12429 C  CG    . TYR C 2 198 ? 104.674 84.224  113.438 1.00 22.91 ?  177 TYR C CG    1 
ATOM   12430 C  CD1   . TYR C 2 198 ? 104.382 83.354  112.386 1.00 23.49 ?  177 TYR C CD1   1 
ATOM   12431 C  CD2   . TYR C 2 198 ? 103.632 84.641  114.266 1.00 21.97 ?  177 TYR C CD2   1 
ATOM   12432 C  CE1   . TYR C 2 198 ? 103.075 82.934  112.140 1.00 23.57 ?  177 TYR C CE1   1 
ATOM   12433 C  CE2   . TYR C 2 198 ? 102.311 84.222  114.032 1.00 22.54 ?  177 TYR C CE2   1 
ATOM   12434 C  CZ    . TYR C 2 198 ? 102.045 83.374  112.966 1.00 22.88 ?  177 TYR C CZ    1 
ATOM   12435 O  OH    . TYR C 2 198 ? 100.755 82.941  112.722 1.00 23.17 ?  177 TYR C OH    1 
ATOM   12436 N  N     . PHE C 2 199 ? 106.017 87.821  113.697 1.00 23.50 ?  178 PHE C N     1 
ATOM   12437 C  CA    . PHE C 2 199 ? 105.349 89.123  113.661 1.00 24.60 ?  178 PHE C CA    1 
ATOM   12438 C  C     . PHE C 2 199 ? 105.944 90.109  112.647 1.00 24.72 ?  178 PHE C C     1 
ATOM   12439 O  O     . PHE C 2 199 ? 105.212 90.749  111.893 1.00 24.19 ?  178 PHE C O     1 
ATOM   12440 C  CB    . PHE C 2 199 ? 105.295 89.743  115.060 1.00 24.35 ?  178 PHE C CB    1 
ATOM   12441 C  CG    . PHE C 2 199 ? 104.264 89.117  115.950 1.00 26.36 ?  178 PHE C CG    1 
ATOM   12442 C  CD1   . PHE C 2 199 ? 102.976 88.862  115.479 1.00 28.53 ?  178 PHE C CD1   1 
ATOM   12443 C  CD2   . PHE C 2 199 ? 104.566 88.795  117.266 1.00 28.23 ?  178 PHE C CD2   1 
ATOM   12444 C  CE1   . PHE C 2 199 ? 102.013 88.274  116.305 1.00 29.37 ?  178 PHE C CE1   1 
ATOM   12445 C  CE2   . PHE C 2 199 ? 103.597 88.215  118.104 1.00 28.69 ?  178 PHE C CE2   1 
ATOM   12446 C  CZ    . PHE C 2 199 ? 102.332 87.956  117.623 1.00 28.43 ?  178 PHE C CZ    1 
ATOM   12447 N  N     . TYR C 2 200 ? 107.270 90.218  112.633 1.00 25.36 ?  179 TYR C N     1 
ATOM   12448 C  CA    . TYR C 2 200 ? 107.989 91.075  111.682 1.00 26.02 ?  179 TYR C CA    1 
ATOM   12449 C  C     . TYR C 2 200 ? 107.526 90.782  110.255 1.00 26.57 ?  179 TYR C C     1 
ATOM   12450 O  O     . TYR C 2 200 ? 107.252 91.698  109.473 1.00 26.30 ?  179 TYR C O     1 
ATOM   12451 C  CB    . TYR C 2 200 ? 109.500 90.836  111.796 1.00 26.19 ?  179 TYR C CB    1 
ATOM   12452 C  CG    . TYR C 2 200 ? 110.356 91.814  111.022 1.00 27.82 ?  179 TYR C CG    1 
ATOM   12453 C  CD1   . TYR C 2 200 ? 110.910 91.460  109.788 1.00 30.77 ?  179 TYR C CD1   1 
ATOM   12454 C  CD2   . TYR C 2 200 ? 110.621 93.090  111.524 1.00 29.20 ?  179 TYR C CD2   1 
ATOM   12455 C  CE1   . TYR C 2 200 ? 111.699 92.353  109.072 1.00 31.82 ?  179 TYR C CE1   1 
ATOM   12456 C  CE2   . TYR C 2 200 ? 111.406 93.992  110.820 1.00 30.44 ?  179 TYR C CE2   1 
ATOM   12457 C  CZ    . TYR C 2 200 ? 111.943 93.615  109.592 1.00 32.74 ?  179 TYR C CZ    1 
ATOM   12458 O  OH    . TYR C 2 200 ? 112.715 94.495  108.876 1.00 34.58 ?  179 TYR C OH    1 
ATOM   12459 N  N     . GLY C 2 201 ? 107.418 89.493  109.940 1.00 26.71 ?  180 GLY C N     1 
ATOM   12460 C  CA    . GLY C 2 201 ? 106.999 89.042  108.620 1.00 27.38 ?  180 GLY C CA    1 
ATOM   12461 C  C     . GLY C 2 201 ? 105.572 89.407  108.242 1.00 27.62 ?  180 GLY C C     1 
ATOM   12462 O  O     . GLY C 2 201 ? 105.234 89.379  107.071 1.00 28.25 ?  180 GLY C O     1 
ATOM   12463 N  N     . GLN C 2 202 ? 104.746 89.747  109.232 1.00 27.60 ?  181 GLN C N     1 
ATOM   12464 C  CA    . GLN C 2 202 ? 103.359 90.186  109.001 1.00 28.24 ?  181 GLN C CA    1 
ATOM   12465 C  C     . GLN C 2 202 ? 103.224 91.698  109.103 1.00 28.30 ?  181 GLN C C     1 
ATOM   12466 O  O     . GLN C 2 202 ? 102.108 92.219  109.064 1.00 27.98 ?  181 GLN C O     1 
ATOM   12467 C  CB    . GLN C 2 202 ? 102.411 89.591  110.046 1.00 27.90 ?  181 GLN C CB    1 
ATOM   12468 C  CG    . GLN C 2 202 ? 102.314 88.100  110.071 1.00 29.54 ?  181 GLN C CG    1 
ATOM   12469 C  CD    . GLN C 2 202 ? 101.452 87.620  111.217 1.00 31.54 ?  181 GLN C CD    1 
ATOM   12470 O  OE1   . GLN C 2 202 ? 100.232 87.807  111.214 1.00 32.11 ?  181 GLN C OE1   1 
ATOM   12471 N  NE2   . GLN C 2 202 ? 102.080 87.005  112.210 1.00 31.29 ?  181 GLN C NE2   1 
ATOM   12472 N  N     . GLY C 2 203 ? 104.352 92.385  109.283 1.00 28.14 ?  182 GLY C N     1 
ATOM   12473 C  CA    . GLY C 2 203 ? 104.369 93.831  109.443 1.00 28.38 ?  182 GLY C CA    1 
ATOM   12474 C  C     . GLY C 2 203 ? 103.927 94.280  110.820 1.00 28.71 ?  182 GLY C C     1 
ATOM   12475 O  O     . GLY C 2 203 ? 103.362 95.359  110.966 1.00 28.80 ?  182 GLY C O     1 
ATOM   12476 N  N     . LYS C 2 204 ? 104.173 93.441  111.826 1.00 28.24 ?  183 LYS C N     1 
ATOM   12477 C  CA    . LYS C 2 204 ? 103.787 93.739  113.196 1.00 28.48 ?  183 LYS C CA    1 
ATOM   12478 C  C     . LYS C 2 204 ? 105.013 93.739  114.104 1.00 27.82 ?  183 LYS C C     1 
ATOM   12479 O  O     . LYS C 2 204 ? 105.936 92.933  113.920 1.00 26.73 ?  183 LYS C O     1 
ATOM   12480 C  CB    . LYS C 2 204 ? 102.756 92.730  113.704 1.00 29.13 ?  183 LYS C CB    1 
ATOM   12481 C  CG    . LYS C 2 204 ? 101.413 92.786  112.975 1.00 30.41 ?  183 LYS C CG    1 
ATOM   12482 C  CD    . LYS C 2 204 ? 100.668 91.467  113.108 1.00 33.74 ?  183 LYS C CD    1 
ATOM   12483 C  CE    . LYS C 2 204 ? 99.284  91.546  112.444 1.00 36.26 ?  183 LYS C CE    1 
ATOM   12484 N  NZ    . LYS C 2 204 ? 98.550  90.258  112.610 1.00 39.17 1  183 LYS C NZ    1 
ATOM   12485 N  N     . LEU C 2 205 ? 105.009 94.645  115.080 1.00 27.77 ?  184 LEU C N     1 
ATOM   12486 C  CA    . LEU C 2 205 ? 106.119 94.803  116.027 1.00 27.79 ?  184 LEU C CA    1 
ATOM   12487 C  C     . LEU C 2 205 ? 107.463 94.920  115.301 1.00 27.85 ?  184 LEU C C     1 
ATOM   12488 O  O     . LEU C 2 205 ? 108.438 94.220  115.609 1.00 27.07 ?  184 LEU C O     1 
ATOM   12489 C  CB    . LEU C 2 205 ? 106.129 93.654  117.056 1.00 27.76 ?  184 LEU C CB    1 
ATOM   12490 C  CG    . LEU C 2 205 ? 104.834 93.465  117.856 1.00 28.62 ?  184 LEU C CG    1 
ATOM   12491 C  CD1   . LEU C 2 205 ? 104.914 92.233  118.736 1.00 29.18 ?  184 LEU C CD1   1 
ATOM   12492 C  CD2   . LEU C 2 205 ? 104.521 94.693  118.698 1.00 28.43 ?  184 LEU C CD2   1 
ATOM   12493 N  N     . MET C 2 206 ? 107.517 95.828  114.339 1.00 28.15 ?  185 MET C N     1 
ATOM   12494 C  CA    . MET C 2 206 ? 108.653 95.865  113.447 1.00 28.80 ?  185 MET C CA    1 
ATOM   12495 C  C     . MET C 2 206 ? 109.904 96.514  114.024 1.00 28.77 ?  185 MET C C     1 
ATOM   12496 O  O     . MET C 2 206 ? 111.008 96.210  113.577 1.00 28.79 ?  185 MET C O     1 
ATOM   12497 C  CB    . MET C 2 206 ? 108.247 96.469  112.116 1.00 29.96 ?  185 MET C CB    1 
ATOM   12498 C  CG    . MET C 2 206 ? 107.272 95.555  111.367 1.00 31.23 ?  185 MET C CG    1 
ATOM   12499 S  SD    . MET C 2 206 ? 107.215 95.989  109.649 1.00 40.10 ?  185 MET C SD    1 
ATOM   12500 C  CE    . MET C 2 206 ? 108.791 95.397  109.066 1.00 35.10 ?  185 MET C CE    1 
ATOM   12501 N  N     . GLN C 2 207 ? 109.743 97.375  115.024 1.00 28.62 ?  186 GLN C N     1 
ATOM   12502 C  CA    . GLN C 2 207 ? 110.901 97.998  115.675 1.00 29.10 ?  186 GLN C CA    1 
ATOM   12503 C  C     . GLN C 2 207 ? 111.606 97.001  116.598 1.00 28.52 ?  186 GLN C C     1 
ATOM   12504 O  O     . GLN C 2 207 ? 112.824 96.852  116.521 1.00 28.28 ?  186 GLN C O     1 
ATOM   12505 C  CB    . GLN C 2 207 ? 110.513 99.275  116.428 1.00 29.21 ?  186 GLN C CB    1 
ATOM   12506 C  CG    . GLN C 2 207 ? 109.978 100.392 115.531 1.00 31.41 ?  186 GLN C CG    1 
ATOM   12507 C  CD    . GLN C 2 207 ? 111.021 100.909 114.560 1.00 34.70 ?  186 GLN C CD    1 
ATOM   12508 O  OE1   . GLN C 2 207 ? 111.127 100.426 113.436 1.00 37.69 ?  186 GLN C OE1   1 
ATOM   12509 N  NE2   . GLN C 2 207 ? 111.819 101.874 115.001 1.00 34.75 ?  186 GLN C NE2   1 
ATOM   12510 N  N     . SER C 2 208 ? 110.831 96.326  117.454 1.00 28.38 ?  187 SER C N     1 
ATOM   12511 C  CA    . SER C 2 208 ? 111.320 95.196  118.255 1.00 28.25 ?  187 SER C CA    1 
ATOM   12512 C  C     . SER C 2 208 ? 111.935 94.146  117.338 1.00 28.00 ?  187 SER C C     1 
ATOM   12513 O  O     . SER C 2 208 ? 112.986 93.584  117.649 1.00 27.90 ?  187 SER C O     1 
ATOM   12514 C  CB    . SER C 2 208 ? 110.176 94.539  119.030 1.00 27.88 ?  187 SER C CB    1 
ATOM   12515 O  OG    . SER C 2 208 ? 109.579 95.436  119.942 1.00 30.27 ?  187 SER C OG    1 
ATOM   12516 N  N     . GLY C 2 209 ? 111.257 93.884  116.215 1.00 27.31 ?  188 GLY C N     1 
ATOM   12517 C  CA    . GLY C 2 209 ? 111.719 92.924  115.216 1.00 27.86 ?  188 GLY C CA    1 
ATOM   12518 C  C     . GLY C 2 209 ? 113.053 93.293  114.594 1.00 27.96 ?  188 GLY C C     1 
ATOM   12519 O  O     . GLY C 2 209 ? 113.867 92.414  114.289 1.00 27.84 ?  188 GLY C O     1 
ATOM   12520 N  N     . GLU C 2 210 ? 113.275 94.594  114.401 1.00 28.21 ?  189 GLU C N     1 
ATOM   12521 C  CA    . GLU C 2 210 ? 114.547 95.094  113.889 1.00 29.15 ?  189 GLU C CA    1 
ATOM   12522 C  C     . GLU C 2 210 ? 115.693 94.788  114.875 1.00 28.02 ?  189 GLU C C     1 
ATOM   12523 O  O     . GLU C 2 210 ? 116.779 94.361  114.477 1.00 27.15 ?  189 GLU C O     1 
ATOM   12524 C  CB    . GLU C 2 210 ? 114.449 96.597  113.615 1.00 30.17 ?  189 GLU C CB    1 
ATOM   12525 C  CG    . GLU C 2 210 ? 114.933 97.015  112.235 1.00 35.68 ?  189 GLU C CG    1 
ATOM   12526 C  CD    . GLU C 2 210 ? 113.908 96.735  111.133 1.00 40.25 ?  189 GLU C CD    1 
ATOM   12527 O  OE1   . GLU C 2 210 ? 112.791 97.305  111.161 1.00 42.98 ?  189 GLU C OE1   1 
ATOM   12528 O  OE2   . GLU C 2 210 ? 114.224 95.947  110.221 1.00 43.59 -1 189 GLU C OE2   1 
ATOM   12529 N  N     . ILE C 2 211 ? 115.440 95.009  116.163 1.00 27.57 ?  190 ILE C N     1 
ATOM   12530 C  CA    . ILE C 2 211 ? 116.398 94.646  117.213 1.00 27.47 ?  190 ILE C CA    1 
ATOM   12531 C  C     . ILE C 2 211 ? 116.734 93.151  117.169 1.00 26.69 ?  190 ILE C C     1 
ATOM   12532 O  O     . ILE C 2 211 ? 117.907 92.756  117.144 1.00 26.56 ?  190 ILE C O     1 
ATOM   12533 C  CB    . ILE C 2 211 ? 115.881 95.070  118.619 1.00 27.84 ?  190 ILE C CB    1 
ATOM   12534 C  CG1   . ILE C 2 211 ? 115.929 96.601  118.750 1.00 28.56 ?  190 ILE C CG1   1 
ATOM   12535 C  CG2   . ILE C 2 211 ? 116.693 94.370  119.735 1.00 27.27 ?  190 ILE C CG2   1 
ATOM   12536 C  CD1   . ILE C 2 211 ? 115.494 97.134  120.110 1.00 30.09 ?  190 ILE C CD1   1 
ATOM   12537 N  N     . ILE C 2 212 ? 115.694 92.327  117.117 1.00 26.33 ?  191 ILE C N     1 
ATOM   12538 C  CA    . ILE C 2 212 ? 115.848 90.876  117.084 1.00 25.96 ?  191 ILE C CA    1 
ATOM   12539 C  C     . ILE C 2 212 ? 116.657 90.405  115.868 1.00 25.46 ?  191 ILE C C     1 
ATOM   12540 O  O     . ILE C 2 212 ? 117.493 89.514  115.999 1.00 24.84 ?  191 ILE C O     1 
ATOM   12541 C  CB    . ILE C 2 212 ? 114.466 90.157  117.173 1.00 26.00 ?  191 ILE C CB    1 
ATOM   12542 C  CG1   . ILE C 2 212 ? 113.804 90.427  118.534 1.00 27.16 ?  191 ILE C CG1   1 
ATOM   12543 C  CG2   . ILE C 2 212 ? 114.588 88.659  116.927 1.00 26.87 ?  191 ILE C CG2   1 
ATOM   12544 C  CD1   . ILE C 2 212 ? 114.556 89.880  119.733 1.00 29.84 ?  191 ILE C CD1   1 
ATOM   12545 N  N     . ASN C 2 213 ? 116.411 91.001  114.698 1.00 25.35 ?  192 ASN C N     1 
ATOM   12546 C  CA    . ASN C 2 213 ? 117.179 90.679  113.491 1.00 25.60 ?  192 ASN C CA    1 
ATOM   12547 C  C     . ASN C 2 213 ? 118.660 91.015  113.629 1.00 25.14 ?  192 ASN C C     1 
ATOM   12548 O  O     . ASN C 2 213 ? 119.530 90.287  113.126 1.00 25.61 ?  192 ASN C O     1 
ATOM   12549 C  CB    . ASN C 2 213 ? 116.603 91.378  112.252 1.00 26.55 ?  192 ASN C CB    1 
ATOM   12550 C  CG    . ASN C 2 213 ? 115.500 90.579  111.595 1.00 28.10 ?  192 ASN C CG    1 
ATOM   12551 O  OD1   . ASN C 2 213 ? 115.721 89.464  111.110 1.00 31.67 ?  192 ASN C OD1   1 
ATOM   12552 N  ND2   . ASN C 2 213 ? 114.307 91.145  111.563 1.00 30.36 ?  192 ASN C ND2   1 
ATOM   12553 N  N     . LEU C 2 214 ? 118.950 92.116  114.313 1.00 24.54 ?  193 LEU C N     1 
ATOM   12554 C  CA    . LEU C 2 214 ? 120.341 92.480  114.594 1.00 24.40 ?  193 LEU C CA    1 
ATOM   12555 C  C     . LEU C 2 214 ? 120.995 91.470  115.539 1.00 23.55 ?  193 LEU C C     1 
ATOM   12556 O  O     . LEU C 2 214 ? 122.127 91.040  115.301 1.00 23.09 ?  193 LEU C O     1 
ATOM   12557 C  CB    . LEU C 2 214 ? 120.439 93.910  115.122 1.00 24.00 ?  193 LEU C CB    1 
ATOM   12558 C  CG    . LEU C 2 214 ? 120.179 95.023  114.084 1.00 25.69 ?  193 LEU C CG    1 
ATOM   12559 C  CD1   . LEU C 2 214 ? 120.008 96.388  114.752 1.00 26.28 ?  193 LEU C CD1   1 
ATOM   12560 C  CD2   . LEU C 2 214 ? 121.295 95.099  113.039 1.00 26.05 ?  193 LEU C CD2   1 
ATOM   12561 N  N     . ILE C 2 215 ? 120.275 91.086  116.596 1.00 23.19 ?  194 ILE C N     1 
ATOM   12562 C  CA    . ILE C 2 215 ? 120.727 90.030  117.509 1.00 22.88 ?  194 ILE C CA    1 
ATOM   12563 C  C     . ILE C 2 215 ? 120.975 88.735  116.719 1.00 23.81 ?  194 ILE C C     1 
ATOM   12564 O  O     . ILE C 2 215 ? 122.026 88.110  116.861 1.00 23.83 ?  194 ILE C O     1 
ATOM   12565 C  CB    . ILE C 2 215 ? 119.718 89.786  118.667 1.00 22.92 ?  194 ILE C CB    1 
ATOM   12566 C  CG1   . ILE C 2 215 ? 119.546 91.051  119.509 1.00 21.11 ?  194 ILE C CG1   1 
ATOM   12567 C  CG2   . ILE C 2 215 ? 120.142 88.600  119.548 1.00 21.89 ?  194 ILE C CG2   1 
ATOM   12568 C  CD1   . ILE C 2 215 ? 118.557 90.911  120.649 1.00 22.26 ?  194 ILE C CD1   1 
ATOM   12569 N  N     . LEU C 2 216 ? 120.030 88.357  115.857 1.00 24.23 ?  195 LEU C N     1 
ATOM   12570 C  CA    . LEU C 2 216 ? 120.148 87.109  115.094 1.00 25.41 ?  195 LEU C CA    1 
ATOM   12571 C  C     . LEU C 2 216 ? 121.343 87.132  114.140 1.00 25.63 ?  195 LEU C C     1 
ATOM   12572 O  O     . LEU C 2 216 ? 122.077 86.139  114.025 1.00 25.46 ?  195 LEU C O     1 
ATOM   12573 C  CB    . LEU C 2 216 ? 118.842 86.807  114.334 1.00 26.03 ?  195 LEU C CB    1 
ATOM   12574 C  CG    . LEU C 2 216 ? 118.700 85.524  113.502 1.00 28.00 ?  195 LEU C CG    1 
ATOM   12575 C  CD1   . LEU C 2 216 ? 117.223 85.219  113.317 1.00 31.45 ?  195 LEU C CD1   1 
ATOM   12576 C  CD2   . LEU C 2 216 ? 119.404 85.625  112.144 1.00 29.83 ?  195 LEU C CD2   1 
ATOM   12577 N  N     . ARG C 2 217 ? 121.537 88.264  113.469 1.00 25.98 ?  196 ARG C N     1 
ATOM   12578 C  CA    . ARG C 2 217 ? 122.691 88.470  112.601 1.00 26.73 ?  196 ARG C CA    1 
ATOM   12579 C  C     . ARG C 2 217 ? 124.013 88.237  113.375 1.00 25.95 ?  196 ARG C C     1 
ATOM   12580 O  O     . ARG C 2 217 ? 124.914 87.569  112.857 1.00 25.75 ?  196 ARG C O     1 
ATOM   12581 C  CB    . ARG C 2 217 ? 122.647 89.875  111.996 1.00 27.29 ?  196 ARG C CB    1 
ATOM   12582 C  CG    . ARG C 2 217 ? 123.641 90.138  110.856 1.00 30.12 ?  196 ARG C CG    1 
ATOM   12583 C  CD    . ARG C 2 217 ? 124.044 91.601  110.861 1.00 35.40 ?  196 ARG C CD    1 
ATOM   12584 N  NE    . ARG C 2 217 ? 124.330 92.000  112.240 1.00 39.87 ?  196 ARG C NE    1 
ATOM   12585 C  CZ    . ARG C 2 217 ? 124.491 93.243  112.675 1.00 40.55 ?  196 ARG C CZ    1 
ATOM   12586 N  NH1   . ARG C 2 217 ? 124.411 94.281  111.842 1.00 40.77 1  196 ARG C NH1   1 
ATOM   12587 N  NH2   . ARG C 2 217 ? 124.732 93.438  113.966 1.00 41.10 ?  196 ARG C NH2   1 
ATOM   12588 N  N     . ASP C 2 218 ? 124.108 88.772  114.598 1.00 24.70 ?  197 ASP C N     1 
ATOM   12589 C  CA    . ASP C 2 218 ? 125.264 88.530  115.484 1.00 24.55 ?  197 ASP C CA    1 
ATOM   12590 C  C     . ASP C 2 218 ? 125.414 87.037  115.843 1.00 24.23 ?  197 ASP C C     1 
ATOM   12591 O  O     . ASP C 2 218 ? 126.501 86.472  115.689 1.00 23.69 ?  197 ASP C O     1 
ATOM   12592 C  CB    . ASP C 2 218 ? 125.196 89.352  116.787 1.00 24.50 ?  197 ASP C CB    1 
ATOM   12593 C  CG    . ASP C 2 218 ? 125.328 90.871  116.571 1.00 25.84 ?  197 ASP C CG    1 
ATOM   12594 O  OD1   . ASP C 2 218 ? 125.907 91.324  115.559 1.00 26.91 ?  197 ASP C OD1   1 
ATOM   12595 O  OD2   . ASP C 2 218 ? 124.859 91.622  117.448 1.00 25.72 -1 197 ASP C OD2   1 
ATOM   12596 N  N     . GLU C 2 219 ? 124.330 86.397  116.292 1.00 23.92 ?  198 GLU C N     1 
ATOM   12597 C  CA    . GLU C 2 219 ? 124.441 85.002  116.753 1.00 24.20 ?  198 GLU C CA    1 
ATOM   12598 C  C     . GLU C 2 219 ? 124.869 84.073  115.632 1.00 24.02 ?  198 GLU C C     1 
ATOM   12599 O  O     . GLU C 2 219 ? 125.602 83.124  115.881 1.00 24.24 ?  198 GLU C O     1 
ATOM   12600 C  CB    . GLU C 2 219 ? 123.159 84.465  117.395 1.00 24.05 ?  198 GLU C CB    1 
ATOM   12601 C  CG    . GLU C 2 219 ? 122.382 85.419  118.284 1.00 25.03 ?  198 GLU C CG    1 
ATOM   12602 C  CD    . GLU C 2 219 ? 123.024 85.762  119.643 1.00 26.31 ?  198 GLU C CD    1 
ATOM   12603 O  OE1   . GLU C 2 219 ? 124.273 85.676  119.834 1.00 27.65 ?  198 GLU C OE1   1 
ATOM   12604 O  OE2   . GLU C 2 219 ? 122.230 86.164  120.538 1.00 26.87 -1 198 GLU C OE2   1 
ATOM   12605 N  N     . ALA C 2 220 ? 124.413 84.343  114.407 1.00 24.00 ?  199 ALA C N     1 
ATOM   12606 C  CA    . ALA C 2 220 ? 124.804 83.537  113.257 1.00 24.72 ?  199 ALA C CA    1 
ATOM   12607 C  C     . ALA C 2 220 ? 126.330 83.509  113.066 1.00 24.80 ?  199 ALA C C     1 
ATOM   12608 O  O     . ALA C 2 220 ? 126.909 82.439  112.856 1.00 25.04 ?  199 ALA C O     1 
ATOM   12609 C  CB    . ALA C 2 220 ? 124.092 84.012  111.965 1.00 24.66 ?  199 ALA C CB    1 
ATOM   12610 N  N     . ILE C 2 221 ? 126.973 84.672  113.150 1.00 24.85 ?  200 ILE C N     1 
ATOM   12611 C  CA    . ILE C 2 221 ? 128.441 84.736  113.031 1.00 25.07 ?  200 ILE C CA    1 
ATOM   12612 C  C     . ILE C 2 221 ? 129.154 84.194  114.279 1.00 23.86 ?  200 ILE C C     1 
ATOM   12613 O  O     . ILE C 2 221 ? 130.230 83.601  114.162 1.00 23.72 ?  200 ILE C O     1 
ATOM   12614 C  CB    . ILE C 2 221 ? 128.988 86.151  112.621 1.00 25.71 ?  200 ILE C CB    1 
ATOM   12615 C  CG1   . ILE C 2 221 ? 128.897 87.153  113.776 1.00 27.10 ?  200 ILE C CG1   1 
ATOM   12616 C  CG2   . ILE C 2 221 ? 128.294 86.656  111.341 1.00 27.18 ?  200 ILE C CG2   1 
ATOM   12617 C  CD1   . ILE C 2 221 ? 129.585 88.500  113.522 1.00 29.63 ?  200 ILE C CD1   1 
ATOM   12618 N  N     . HIS C 2 222 ? 128.551 84.379  115.454 1.00 22.79 ?  201 HIS C N     1 
ATOM   12619 C  CA    . HIS C 2 222 ? 129.091 83.793  116.702 1.00 22.48 ?  201 HIS C CA    1 
ATOM   12620 C  C     . HIS C 2 222 ? 129.110 82.268  116.637 1.00 22.04 ?  201 HIS C C     1 
ATOM   12621 O  O     . HIS C 2 222 ? 130.082 81.647  117.048 1.00 22.06 ?  201 HIS C O     1 
ATOM   12622 C  CB    . HIS C 2 222 ? 128.262 84.180  117.928 1.00 21.77 ?  201 HIS C CB    1 
ATOM   12623 C  CG    . HIS C 2 222 ? 128.292 85.632  118.268 1.00 21.76 ?  201 HIS C CG    1 
ATOM   12624 N  ND1   . HIS C 2 222 ? 127.687 86.133  119.399 1.00 20.70 ?  201 HIS C ND1   1 
ATOM   12625 C  CD2   . HIS C 2 222 ? 128.853 86.692  117.641 1.00 22.07 ?  201 HIS C CD2   1 
ATOM   12626 C  CE1   . HIS C 2 222 ? 127.863 87.440  119.450 1.00 22.26 ?  201 HIS C CE1   1 
ATOM   12627 N  NE2   . HIS C 2 222 ? 128.560 87.805  118.392 1.00 22.52 ?  201 HIS C NE2   1 
ATOM   12628 N  N     . GLY C 2 223 ? 128.015 81.676  116.156 1.00 22.35 ?  202 GLY C N     1 
ATOM   12629 C  CA    . GLY C 2 223 ? 127.904 80.217  115.991 1.00 22.01 ?  202 GLY C CA    1 
ATOM   12630 C  C     . GLY C 2 223 ? 128.896 79.644  114.983 1.00 22.73 ?  202 GLY C C     1 
ATOM   12631 O  O     . GLY C 2 223 ? 129.476 78.568  115.206 1.00 21.99 ?  202 GLY C O     1 
ATOM   12632 N  N     . VAL C 2 224 ? 129.103 80.358  113.874 1.00 22.45 ?  203 VAL C N     1 
ATOM   12633 C  CA    . VAL C 2 224 ? 130.095 79.939  112.882 1.00 22.54 ?  203 VAL C CA    1 
ATOM   12634 C  C     . VAL C 2 224 ? 131.505 79.979  113.475 1.00 22.28 ?  203 VAL C C     1 
ATOM   12635 O  O     . VAL C 2 224 ? 132.245 79.001  113.386 1.00 22.44 ?  203 VAL C O     1 
ATOM   12636 C  CB    . VAL C 2 224 ? 130.035 80.790  111.568 1.00 23.00 ?  203 VAL C CB    1 
ATOM   12637 C  CG1   . VAL C 2 224 ? 131.228 80.460  110.653 1.00 23.10 ?  203 VAL C CG1   1 
ATOM   12638 C  CG2   . VAL C 2 224 ? 128.703 80.550  110.808 1.00 23.14 ?  203 VAL C CG2   1 
ATOM   12639 N  N     . TYR C 2 225 ? 131.854 81.096  114.109 1.00 22.41 ?  204 TYR C N     1 
ATOM   12640 C  CA    . TYR C 2 225 ? 133.188 81.272  114.682 1.00 22.03 ?  204 TYR C CA    1 
ATOM   12641 C  C     . TYR C 2 225 ? 133.526 80.213  115.731 1.00 21.66 ?  204 TYR C C     1 
ATOM   12642 O  O     . TYR C 2 225 ? 134.560 79.538  115.626 1.00 21.72 ?  204 TYR C O     1 
ATOM   12643 C  CB    . TYR C 2 225 ? 133.375 82.683  115.261 1.00 22.22 ?  204 TYR C CB    1 
ATOM   12644 C  CG    . TYR C 2 225 ? 134.810 82.965  115.657 1.00 21.92 ?  204 TYR C CG    1 
ATOM   12645 C  CD1   . TYR C 2 225 ? 135.808 83.088  114.690 1.00 22.36 ?  204 TYR C CD1   1 
ATOM   12646 C  CD2   . TYR C 2 225 ? 135.169 83.097  117.000 1.00 21.43 ?  204 TYR C CD2   1 
ATOM   12647 C  CE1   . TYR C 2 225 ? 137.133 83.330  115.049 1.00 23.82 ?  204 TYR C CE1   1 
ATOM   12648 C  CE2   . TYR C 2 225 ? 136.492 83.349  117.376 1.00 21.49 ?  204 TYR C CE2   1 
ATOM   12649 C  CZ    . TYR C 2 225 ? 137.461 83.463  116.398 1.00 23.58 ?  204 TYR C CZ    1 
ATOM   12650 O  OH    . TYR C 2 225 ? 138.758 83.709  116.764 1.00 25.42 ?  204 TYR C OH    1 
ATOM   12651 N  N     . VAL C 2 226 ? 132.659 80.059  116.734 1.00 20.95 ?  205 VAL C N     1 
ATOM   12652 C  CA    . VAL C 2 226 ? 132.868 79.033  117.764 1.00 20.49 ?  205 VAL C CA    1 
ATOM   12653 C  C     . VAL C 2 226 ? 132.892 77.626  117.140 1.00 20.84 ?  205 VAL C C     1 
ATOM   12654 O  O     . VAL C 2 226 ? 133.713 76.781  117.520 1.00 21.10 ?  205 VAL C O     1 
ATOM   12655 C  CB    . VAL C 2 226 ? 131.853 79.152  118.934 1.00 20.57 ?  205 VAL C CB    1 
ATOM   12656 C  CG1   . VAL C 2 226 ? 132.079 78.039  119.958 1.00 20.35 ?  205 VAL C CG1   1 
ATOM   12657 C  CG2   . VAL C 2 226 ? 131.998 80.523  119.610 1.00 19.60 ?  205 VAL C CG2   1 
ATOM   12658 N  N     . GLY C 2 227 ? 132.033 77.398  116.151 1.00 21.08 ?  206 GLY C N     1 
ATOM   12659 C  CA    . GLY C 2 227 ? 132.068 76.146  115.377 1.00 21.43 ?  206 GLY C CA    1 
ATOM   12660 C  C     . GLY C 2 227 ? 133.425 75.842  114.757 1.00 21.95 ?  206 GLY C C     1 
ATOM   12661 O  O     . GLY C 2 227 ? 133.905 74.696  114.810 1.00 21.84 ?  206 GLY C O     1 
ATOM   12662 N  N     . LEU C 2 228 ? 134.055 76.860  114.171 1.00 22.09 ?  207 LEU C N     1 
ATOM   12663 C  CA    . LEU C 2 228 ? 135.386 76.681  113.580 1.00 22.96 ?  207 LEU C CA    1 
ATOM   12664 C  C     . LEU C 2 228 ? 136.450 76.337  114.633 1.00 22.60 ?  207 LEU C C     1 
ATOM   12665 O  O     . LEU C 2 228 ? 137.318 75.493  114.391 1.00 22.04 ?  207 LEU C O     1 
ATOM   12666 C  CB    . LEU C 2 228 ? 135.797 77.897  112.740 1.00 23.39 ?  207 LEU C CB    1 
ATOM   12667 C  CG    . LEU C 2 228 ? 134.992 78.185  111.459 1.00 24.35 ?  207 LEU C CG    1 
ATOM   12668 C  CD1   . LEU C 2 228 ? 135.242 79.627  110.996 1.00 25.01 ?  207 LEU C CD1   1 
ATOM   12669 C  CD2   . LEU C 2 228 ? 135.316 77.205  110.336 1.00 25.11 ?  207 LEU C CD2   1 
ATOM   12670 N  N     . LEU C 2 229 ? 136.367 76.962  115.805 1.00 22.37 ?  208 LEU C N     1 
ATOM   12671 C  CA    . LEU C 2 229 ? 137.283 76.627  116.913 1.00 22.62 ?  208 LEU C CA    1 
ATOM   12672 C  C     . LEU C 2 229 ? 137.089 75.193  117.418 1.00 22.77 ?  208 LEU C C     1 
ATOM   12673 O  O     . LEU C 2 229 ? 138.069 74.481  117.695 1.00 22.57 ?  208 LEU C O     1 
ATOM   12674 C  CB    . LEU C 2 229 ? 137.164 77.636  118.059 1.00 22.44 ?  208 LEU C CB    1 
ATOM   12675 C  CG    . LEU C 2 229 ? 137.423 79.105  117.691 1.00 23.54 ?  208 LEU C CG    1 
ATOM   12676 C  CD1   . LEU C 2 229 ? 137.175 80.012  118.893 1.00 23.37 ?  208 LEU C CD1   1 
ATOM   12677 C  CD2   . LEU C 2 229 ? 138.845 79.309  117.135 1.00 23.91 ?  208 LEU C CD2   1 
ATOM   12678 N  N     . ALA C 2 230 ? 135.829 74.771  117.525 1.00 22.42 ?  209 ALA C N     1 
ATOM   12679 C  CA    . ALA C 2 230 ? 135.504 73.398  117.910 1.00 22.02 ?  209 ALA C CA    1 
ATOM   12680 C  C     . ALA C 2 230 ? 136.071 72.388  116.907 1.00 22.58 ?  209 ALA C C     1 
ATOM   12681 O  O     . ALA C 2 230 ? 136.667 71.394  117.301 1.00 22.14 ?  209 ALA C O     1 
ATOM   12682 C  CB    . ALA C 2 230 ? 134.008 73.225  118.042 1.00 22.04 ?  209 ALA C CB    1 
ATOM   12683 N  N     . GLN C 2 231 ? 135.897 72.665  115.617 1.00 22.96 ?  210 GLN C N     1 
ATOM   12684 C  CA    . GLN C 2 231 ? 136.450 71.799  114.559 1.00 24.30 ?  210 GLN C CA    1 
ATOM   12685 C  C     . GLN C 2 231 ? 137.961 71.671  114.621 1.00 25.11 ?  210 GLN C C     1 
ATOM   12686 O  O     . GLN C 2 231 ? 138.506 70.603  114.324 1.00 24.97 ?  210 GLN C O     1 
ATOM   12687 C  CB    . GLN C 2 231 ? 136.028 72.292  113.179 1.00 24.38 ?  210 GLN C CB    1 
ATOM   12688 C  CG    . GLN C 2 231 ? 134.523 72.125  112.916 1.00 25.12 ?  210 GLN C CG    1 
ATOM   12689 C  CD    . GLN C 2 231 ? 134.121 72.617  111.542 1.00 28.08 ?  210 GLN C CD    1 
ATOM   12690 O  OE1   . GLN C 2 231 ? 134.677 72.183  110.532 1.00 27.83 ?  210 GLN C OE1   1 
ATOM   12691 N  NE2   . GLN C 2 231 ? 133.161 73.543  111.494 1.00 26.38 ?  210 GLN C NE2   1 
ATOM   12692 N  N     . GLU C 2 232 ? 138.640 72.757  115.001 1.00 25.80 ?  211 GLU C N     1 
ATOM   12693 C  CA    . GLU C 2 232 ? 140.093 72.717  115.192 1.00 27.16 ?  211 GLU C CA    1 
ATOM   12694 C  C     . GLU C 2 232 ? 140.486 71.640  116.199 1.00 26.47 ?  211 GLU C C     1 
ATOM   12695 O  O     . GLU C 2 232 ? 141.429 70.874  115.969 1.00 26.10 ?  211 GLU C O     1 
ATOM   12696 C  CB    . GLU C 2 232 ? 140.614 74.052  115.706 1.00 27.59 ?  211 GLU C CB    1 
ATOM   12697 C  CG    . GLU C 2 232 ? 141.024 75.021  114.640 1.00 32.55 ?  211 GLU C CG    1 
ATOM   12698 C  CD    . GLU C 2 232 ? 142.178 75.910  115.085 1.00 36.72 ?  211 GLU C CD    1 
ATOM   12699 O  OE1   . GLU C 2 232 ? 142.595 75.830  116.266 1.00 38.32 ?  211 GLU C OE1   1 
ATOM   12700 O  OE2   . GLU C 2 232 ? 142.673 76.687  114.243 1.00 40.62 -1 211 GLU C OE2   1 
ATOM   12701 N  N     . ILE C 2 233 ? 139.770 71.601  117.322 1.00 25.55 ?  212 ILE C N     1 
ATOM   12702 C  CA    . ILE C 2 233 ? 140.067 70.641  118.385 1.00 25.32 ?  212 ILE C CA    1 
ATOM   12703 C  C     . ILE C 2 233 ? 139.708 69.221  117.966 1.00 25.48 ?  212 ILE C C     1 
ATOM   12704 O  O     . ILE C 2 233 ? 140.514 68.300  118.120 1.00 25.82 ?  212 ILE C O     1 
ATOM   12705 C  CB    . ILE C 2 233 ? 139.369 71.013  119.712 1.00 25.39 ?  212 ILE C CB    1 
ATOM   12706 C  CG1   . ILE C 2 233 ? 139.969 72.310  120.262 1.00 24.37 ?  212 ILE C CG1   1 
ATOM   12707 C  CG2   . ILE C 2 233 ? 139.493 69.868  120.724 1.00 24.86 ?  212 ILE C CG2   1 
ATOM   12708 C  CD1   . ILE C 2 233 ? 139.107 72.982  121.318 1.00 25.10 ?  212 ILE C CD1   1 
ATOM   12709 N  N     . TYR C 2 234 ? 138.510 69.056  117.413 1.00 25.27 ?  213 TYR C N     1 
ATOM   12710 C  CA    . TYR C 2 234 ? 138.057 67.774  116.867 1.00 25.77 ?  213 TYR C CA    1 
ATOM   12711 C  C     . TYR C 2 234 ? 139.057 67.186  115.856 1.00 26.44 ?  213 TYR C C     1 
ATOM   12712 O  O     . TYR C 2 234 ? 139.338 65.985  115.873 1.00 26.29 ?  213 TYR C O     1 
ATOM   12713 C  CB    . TYR C 2 234 ? 136.677 67.964  116.217 1.00 25.67 ?  213 TYR C CB    1 
ATOM   12714 C  CG    . TYR C 2 234 ? 136.068 66.754  115.539 1.00 25.65 ?  213 TYR C CG    1 
ATOM   12715 C  CD1   . TYR C 2 234 ? 135.210 65.900  116.237 1.00 25.02 ?  213 TYR C CD1   1 
ATOM   12716 C  CD2   . TYR C 2 234 ? 136.302 66.495  114.179 1.00 26.59 ?  213 TYR C CD2   1 
ATOM   12717 C  CE1   . TYR C 2 234 ? 134.625 64.803  115.613 1.00 26.52 ?  213 TYR C CE1   1 
ATOM   12718 C  CE2   . TYR C 2 234 ? 135.726 65.394  113.544 1.00 27.00 ?  213 TYR C CE2   1 
ATOM   12719 C  CZ    . TYR C 2 234 ? 134.892 64.554  114.271 1.00 27.79 ?  213 TYR C CZ    1 
ATOM   12720 O  OH    . TYR C 2 234 ? 134.310 63.483  113.655 1.00 29.00 ?  213 TYR C OH    1 
ATOM   12721 N  N     . ASN C 2 235 ? 139.591 68.030  114.976 1.00 26.96 ?  214 ASN C N     1 
ATOM   12722 C  CA    . ASN C 2 235 ? 140.495 67.551  113.932 1.00 28.05 ?  214 ASN C CA    1 
ATOM   12723 C  C     . ASN C 2 235 ? 141.850 67.061  114.434 1.00 28.24 ?  214 ASN C C     1 
ATOM   12724 O  O     . ASN C 2 235 ? 142.565 66.383  113.702 1.00 28.63 ?  214 ASN C O     1 
ATOM   12725 C  CB    . ASN C 2 235 ? 140.650 68.584  112.806 1.00 28.38 ?  214 ASN C CB    1 
ATOM   12726 C  CG    . ASN C 2 235 ? 139.363 68.776  112.011 1.00 31.14 ?  214 ASN C CG    1 
ATOM   12727 O  OD1   . ASN C 2 235 ? 138.573 67.842  111.844 1.00 34.16 ?  214 ASN C OD1   1 
ATOM   12728 N  ND2   . ASN C 2 235 ? 139.148 69.991  111.520 1.00 32.42 ?  214 ASN C ND2   1 
ATOM   12729 N  N     . LYS C 2 236 ? 142.187 67.384  115.682 1.00 27.91 ?  215 LYS C N     1 
ATOM   12730 C  CA    . LYS C 2 236 ? 143.418 66.905  116.314 1.00 28.49 ?  215 LYS C CA    1 
ATOM   12731 C  C     . LYS C 2 236 ? 143.312 65.474  116.851 1.00 28.50 ?  215 LYS C C     1 
ATOM   12732 O  O     . LYS C 2 236 ? 144.323 64.853  117.188 1.00 28.98 ?  215 LYS C O     1 
ATOM   12733 C  CB    . LYS C 2 236 ? 143.838 67.839  117.454 1.00 28.10 ?  215 LYS C CB    1 
ATOM   12734 C  CG    . LYS C 2 236 ? 144.209 69.247  117.009 1.00 29.25 ?  215 LYS C CG    1 
ATOM   12735 C  CD    . LYS C 2 236 ? 144.635 70.109  118.186 1.00 30.19 ?  215 LYS C CD    1 
ATOM   12736 C  CE    . LYS C 2 236 ? 144.693 71.560  117.769 1.00 32.63 ?  215 LYS C CE    1 
ATOM   12737 N  NZ    . LYS C 2 236 ? 145.097 72.433  118.895 1.00 35.39 1  215 LYS C NZ    1 
ATOM   12738 N  N     . GLN C 2 237 ? 142.097 64.939  116.913 1.00 28.25 ?  216 GLN C N     1 
ATOM   12739 C  CA    . GLN C 2 237 ? 141.874 63.667  117.601 1.00 28.34 ?  216 GLN C CA    1 
ATOM   12740 C  C     . GLN C 2 237 ? 142.100 62.428  116.718 1.00 28.92 ?  216 GLN C C     1 
ATOM   12741 O  O     . GLN C 2 237 ? 142.074 62.516  115.490 1.00 28.53 ?  216 GLN C O     1 
ATOM   12742 C  CB    . GLN C 2 237 ? 140.472 63.653  118.229 1.00 27.68 ?  216 GLN C CB    1 
ATOM   12743 C  CG    . GLN C 2 237 ? 140.146 64.897  119.089 1.00 26.67 ?  216 GLN C CG    1 
ATOM   12744 C  CD    . GLN C 2 237 ? 141.210 65.222  120.133 1.00 25.32 ?  216 GLN C CD    1 
ATOM   12745 O  OE1   . GLN C 2 237 ? 141.714 64.336  120.828 1.00 25.49 ?  216 GLN C OE1   1 
ATOM   12746 N  NE2   . GLN C 2 237 ? 141.555 66.502  120.251 1.00 23.63 ?  216 GLN C NE2   1 
ATOM   12747 N  N     . THR C 2 238 ? 142.319 61.279  117.357 1.00 29.53 ?  217 THR C N     1 
ATOM   12748 C  CA    . THR C 2 238 ? 142.297 59.989  116.660 1.00 30.73 ?  217 THR C CA    1 
ATOM   12749 C  C     . THR C 2 238 ? 140.881 59.729  116.130 1.00 31.13 ?  217 THR C C     1 
ATOM   12750 O  O     . THR C 2 238 ? 139.913 60.374  116.570 1.00 30.17 ?  217 THR C O     1 
ATOM   12751 C  CB    . THR C 2 238 ? 142.655 58.819  117.593 1.00 30.79 ?  217 THR C CB    1 
ATOM   12752 O  OG1   . THR C 2 238 ? 141.607 58.644  118.555 1.00 31.16 ?  217 THR C OG1   1 
ATOM   12753 C  CG2   . THR C 2 238 ? 143.986 59.061  118.315 1.00 31.22 ?  217 THR C CG2   1 
ATOM   12754 N  N     . GLU C 2 239 ? 140.757 58.768  115.211 1.00 31.67 ?  218 GLU C N     1 
ATOM   12755 C  CA    . GLU C 2 239 ? 139.442 58.397  114.686 1.00 32.25 ?  218 GLU C CA    1 
ATOM   12756 C  C     . GLU C 2 239 ? 138.513 57.871  115.786 1.00 31.86 ?  218 GLU C C     1 
ATOM   12757 O  O     . GLU C 2 239 ? 137.316 58.175  115.797 1.00 31.09 ?  218 GLU C O     1 
ATOM   12758 C  CB    . GLU C 2 239 ? 139.572 57.398  113.523 1.00 33.29 ?  218 GLU C CB    1 
ATOM   12759 C  CG    . GLU C 2 239 ? 140.198 58.012  112.257 1.00 35.65 ?  218 GLU C CG    1 
ATOM   12760 C  CD    . GLU C 2 239 ? 139.403 59.206  111.714 1.00 39.17 ?  218 GLU C CD    1 
ATOM   12761 O  OE1   . GLU C 2 239 ? 138.154 59.108  111.612 1.00 41.08 ?  218 GLU C OE1   1 
ATOM   12762 O  OE2   . GLU C 2 239 ? 140.025 60.250  111.396 1.00 39.64 -1 218 GLU C OE2   1 
ATOM   12763 N  N     . GLU C 2 240 ? 139.084 57.118  116.726 1.00 31.72 ?  219 GLU C N     1 
ATOM   12764 C  CA    . GLU C 2 240 ? 138.347 56.581  117.862 1.00 31.76 ?  219 GLU C CA    1 
ATOM   12765 C  C     . GLU C 2 240 ? 137.800 57.704  118.755 1.00 30.21 ?  219 GLU C C     1 
ATOM   12766 O  O     . GLU C 2 240 ? 136.629 57.677  119.160 1.00 29.63 ?  219 GLU C O     1 
ATOM   12767 C  CB    . GLU C 2 240 ? 139.247 55.630  118.654 1.00 32.58 ?  219 GLU C CB    1 
ATOM   12768 C  CG    . GLU C 2 240 ? 138.535 54.821  119.727 1.00 36.93 ?  219 GLU C CG    1 
ATOM   12769 C  CD    . GLU C 2 240 ? 139.367 53.638  120.211 1.00 42.06 ?  219 GLU C CD    1 
ATOM   12770 O  OE1   . GLU C 2 240 ? 139.787 53.641  121.390 1.00 44.09 ?  219 GLU C OE1   1 
ATOM   12771 O  OE2   . GLU C 2 240 ? 139.608 52.706  119.408 1.00 44.45 -1 219 GLU C OE2   1 
ATOM   12772 N  N     . LYS C 2 241 ? 138.649 58.690  119.041 1.00 28.91 ?  220 LYS C N     1 
ATOM   12773 C  CA    . LYS C 2 241 ? 138.263 59.842  119.843 1.00 28.14 ?  220 LYS C CA    1 
ATOM   12774 C  C     . LYS C 2 241 ? 137.193 60.692  119.154 1.00 27.03 ?  220 LYS C C     1 
ATOM   12775 O  O     . LYS C 2 241 ? 136.246 61.147  119.804 1.00 26.72 ?  220 LYS C O     1 
ATOM   12776 C  CB    . LYS C 2 241 ? 139.481 60.701  120.197 1.00 27.83 ?  220 LYS C CB    1 
ATOM   12777 C  CG    . LYS C 2 241 ? 139.159 61.868  121.140 1.00 29.68 ?  220 LYS C CG    1 
ATOM   12778 C  CD    . LYS C 2 241 ? 139.479 61.543  122.592 1.00 33.58 ?  220 LYS C CD    1 
ATOM   12779 C  CE    . LYS C 2 241 ? 138.371 60.776  123.259 1.00 33.71 ?  220 LYS C CE    1 
ATOM   12780 N  NZ    . LYS C 2 241 ? 138.747 60.312  124.635 1.00 34.69 1  220 LYS C NZ    1 
ATOM   12781 N  N     . LYS C 2 242 ? 137.360 60.903  117.847 1.00 26.38 ?  221 LYS C N     1 
ATOM   12782 C  CA    . LYS C 2 242 ? 136.378 61.604  117.015 1.00 25.87 ?  221 LYS C CA    1 
ATOM   12783 C  C     . LYS C 2 242 ? 135.007 60.957  117.086 1.00 25.72 ?  221 LYS C C     1 
ATOM   12784 O  O     . LYS C 2 242 ? 133.993 61.658  117.219 1.00 24.52 ?  221 LYS C O     1 
ATOM   12785 C  CB    . LYS C 2 242 ? 136.827 61.663  115.554 1.00 25.83 ?  221 LYS C CB    1 
ATOM   12786 C  CG    . LYS C 2 242 ? 137.914 62.671  115.259 1.00 26.76 ?  221 LYS C CG    1 
ATOM   12787 C  CD    . LYS C 2 242 ? 138.174 62.728  113.758 1.00 28.40 ?  221 LYS C CD    1 
ATOM   12788 C  CE    . LYS C 2 242 ? 139.395 63.540  113.434 1.00 29.84 ?  221 LYS C CE    1 
ATOM   12789 N  NZ    . LYS C 2 242 ? 139.753 63.398  112.002 1.00 30.96 1  221 LYS C NZ    1 
ATOM   12790 N  N     . ALA C 2 243 ? 134.985 59.625  116.986 1.00 25.97 ?  222 ALA C N     1 
ATOM   12791 C  CA    . ALA C 2 243 ? 133.742 58.858  117.105 1.00 25.79 ?  222 ALA C CA    1 
ATOM   12792 C  C     . ALA C 2 243 ? 133.043 59.118  118.441 1.00 25.24 ?  222 ALA C C     1 
ATOM   12793 O  O     . ALA C 2 243 ? 131.814 59.272  118.482 1.00 25.37 ?  222 ALA C O     1 
ATOM   12794 C  CB    . ALA C 2 243 ? 134.002 57.366  116.895 1.00 26.17 ?  222 ALA C CB    1 
ATOM   12795 N  N     . GLU C 2 244 ? 133.815 59.198  119.523 1.00 25.02 ?  223 GLU C N     1 
ATOM   12796 C  CA    . GLU C 2 244 ? 133.257 59.535  120.842 1.00 25.08 ?  223 GLU C CA    1 
ATOM   12797 C  C     . GLU C 2 244 ? 132.733 60.981  120.908 1.00 24.70 ?  223 GLU C C     1 
ATOM   12798 O  O     . GLU C 2 244 ? 131.687 61.249  121.518 1.00 24.20 ?  223 GLU C O     1 
ATOM   12799 C  CB    . GLU C 2 244 ? 134.277 59.286  121.957 1.00 25.35 ?  223 GLU C CB    1 
ATOM   12800 C  CG    . GLU C 2 244 ? 133.719 59.568  123.363 1.00 26.67 ?  223 GLU C CG    1 
ATOM   12801 C  CD    . GLU C 2 244 ? 134.791 59.603  124.437 1.00 28.29 ?  223 GLU C CD    1 
ATOM   12802 O  OE1   . GLU C 2 244 ? 135.864 58.999  124.247 1.00 29.51 ?  223 GLU C OE1   1 
ATOM   12803 O  OE2   . GLU C 2 244 ? 134.556 60.242  125.479 1.00 29.09 -1 223 GLU C OE2   1 
ATOM   12804 N  N     . LEU C 2 245 ? 133.463 61.905  120.292 1.00 24.27 ?  224 LEU C N     1 
ATOM   12805 C  CA    . LEU C 2 245 ? 133.050 63.310  120.277 1.00 24.54 ?  224 LEU C CA    1 
ATOM   12806 C  C     . LEU C 2 245 ? 131.748 63.539  119.496 1.00 24.42 ?  224 LEU C C     1 
ATOM   12807 O  O     . LEU C 2 245 ? 130.913 64.349  119.905 1.00 24.10 ?  224 LEU C O     1 
ATOM   12808 C  CB    . LEU C 2 245 ? 134.191 64.214  119.773 1.00 23.86 ?  224 LEU C CB    1 
ATOM   12809 C  CG    . LEU C 2 245 ? 135.419 64.306  120.689 1.00 24.78 ?  224 LEU C CG    1 
ATOM   12810 C  CD1   . LEU C 2 245 ? 136.459 65.274  120.117 1.00 25.54 ?  224 LEU C CD1   1 
ATOM   12811 C  CD2   . LEU C 2 245 ? 135.048 64.710  122.124 1.00 25.29 ?  224 LEU C CD2   1 
ATOM   12812 N  N     . ARG C 2 246 ? 131.577 62.814  118.392 1.00 25.26 ?  225 ARG C N     1 
ATOM   12813 C  CA    . ARG C 2 246 ? 130.320 62.836  117.630 1.00 25.97 ?  225 ARG C CA    1 
ATOM   12814 C  C     . ARG C 2 246 ? 129.179 62.295  118.482 1.00 25.85 ?  225 ARG C C     1 
ATOM   12815 O  O     . ARG C 2 246 ? 128.085 62.862  118.482 1.00 25.01 ?  225 ARG C O     1 
ATOM   12816 C  CB    . ARG C 2 246 ? 130.432 62.046  116.309 1.00 26.65 ?  225 ARG C CB    1 
ATOM   12817 C  CG    . ARG C 2 246 ? 131.390 62.670  115.296 1.00 28.90 ?  225 ARG C CG    1 
ATOM   12818 C  CD    . ARG C 2 246 ? 131.212 62.117  113.861 1.00 31.26 ?  225 ARG C CD    1 
ATOM   12819 N  NE    . ARG C 2 246 ? 131.422 60.670  113.774 1.00 34.01 ?  225 ARG C NE    1 
ATOM   12820 C  CZ    . ARG C 2 246 ? 132.611 60.068  113.784 1.00 35.64 ?  225 ARG C CZ    1 
ATOM   12821 N  NH1   . ARG C 2 246 ? 133.730 60.774  113.882 1.00 36.11 1  225 ARG C NH1   1 
ATOM   12822 N  NH2   . ARG C 2 246 ? 132.680 58.744  113.698 1.00 37.05 ?  225 ARG C NH2   1 
ATOM   12823 N  N     . GLU C 2 247 ? 129.441 61.209  119.213 1.00 26.01 ?  226 GLU C N     1 
ATOM   12824 C  CA    . GLU C 2 247 ? 128.460 60.657  120.155 1.00 26.48 ?  226 GLU C CA    1 
ATOM   12825 C  C     . GLU C 2 247 ? 128.063 61.696  121.202 1.00 25.72 ?  226 GLU C C     1 
ATOM   12826 O  O     . GLU C 2 247 ? 126.868 61.893  121.468 1.00 25.16 ?  226 GLU C O     1 
ATOM   12827 C  CB    . GLU C 2 247 ? 128.992 59.406  120.860 1.00 27.18 ?  226 GLU C CB    1 
ATOM   12828 C  CG    . GLU C 2 247 ? 127.890 58.575  121.505 1.00 30.38 ?  226 GLU C CG    1 
ATOM   12829 C  CD    . GLU C 2 247 ? 128.281 57.931  122.823 1.00 35.77 ?  226 GLU C CD    1 
ATOM   12830 O  OE1   . GLU C 2 247 ? 129.473 57.628  123.043 1.00 38.02 ?  226 GLU C OE1   1 
ATOM   12831 O  OE2   . GLU C 2 247 ? 127.372 57.720  123.655 1.00 40.39 -1 226 GLU C OE2   1 
ATOM   12832 N  N     . PHE C 2 248 ? 129.063 62.358  121.787 1.00 24.71 ?  227 PHE C N     1 
ATOM   12833 C  CA    . PHE C 2 248 ? 128.805 63.419  122.759 1.00 23.71 ?  227 PHE C CA    1 
ATOM   12834 C  C     . PHE C 2 248 ? 127.906 64.496  122.147 1.00 23.14 ?  227 PHE C C     1 
ATOM   12835 O  O     . PHE C 2 248 ? 126.909 64.890  122.755 1.00 22.40 ?  227 PHE C O     1 
ATOM   12836 C  CB    . PHE C 2 248 ? 130.102 64.058  123.286 1.00 23.85 ?  227 PHE C CB    1 
ATOM   12837 C  CG    . PHE C 2 248 ? 129.869 65.362  124.007 1.00 23.64 ?  227 PHE C CG    1 
ATOM   12838 C  CD1   . PHE C 2 248 ? 129.478 65.366  125.348 1.00 23.07 ?  227 PHE C CD1   1 
ATOM   12839 C  CD2   . PHE C 2 248 ? 129.971 66.585  123.322 1.00 23.04 ?  227 PHE C CD2   1 
ATOM   12840 C  CE1   . PHE C 2 248 ? 129.233 66.564  126.018 1.00 22.73 ?  227 PHE C CE1   1 
ATOM   12841 C  CE2   . PHE C 2 248 ? 129.721 67.793  123.976 1.00 23.31 ?  227 PHE C CE2   1 
ATOM   12842 C  CZ    . PHE C 2 248 ? 129.353 67.786  125.332 1.00 21.51 ?  227 PHE C CZ    1 
ATOM   12843 N  N     . ALA C 2 249 ? 128.265 64.955  120.947 1.00 22.95 ?  228 ALA C N     1 
ATOM   12844 C  CA    . ALA C 2 249 ? 127.564 66.070  120.294 1.00 22.96 ?  228 ALA C CA    1 
ATOM   12845 C  C     . ALA C 2 249 ? 126.116 65.713  119.968 1.00 23.31 ?  228 ALA C C     1 
ATOM   12846 O  O     . ALA C 2 249 ? 125.205 66.514  120.187 1.00 22.63 ?  228 ALA C O     1 
ATOM   12847 C  CB    . ALA C 2 249 ? 128.305 66.507  119.033 1.00 22.40 ?  228 ALA C CB    1 
ATOM   12848 N  N     . ILE C 2 250 ? 125.919 64.507  119.448 1.00 23.66 ?  229 ILE C N     1 
ATOM   12849 C  CA    . ILE C 2 250 ? 124.586 64.029  119.077 1.00 25.00 ?  229 ILE C CA    1 
ATOM   12850 C  C     . ILE C 2 250 ? 123.723 63.718  120.308 1.00 24.64 ?  229 ILE C C     1 
ATOM   12851 O  O     . ILE C 2 250 ? 122.547 64.102  120.352 1.00 24.26 ?  229 ILE C O     1 
ATOM   12852 C  CB    . ILE C 2 250 ? 124.664 62.845  118.063 1.00 25.43 ?  229 ILE C CB    1 
ATOM   12853 C  CG1   . ILE C 2 250 ? 125.129 63.379  116.700 1.00 27.27 ?  229 ILE C CG1   1 
ATOM   12854 C  CG2   . ILE C 2 250 ? 123.273 62.177  117.881 1.00 27.62 ?  229 ILE C CG2   1 
ATOM   12855 C  CD1   . ILE C 2 250 ? 126.040 62.431  115.907 1.00 31.32 ?  229 ILE C CD1   1 
ATOM   12856 N  N     . ASP C 2 251 ? 124.303 63.064  121.314 1.00 24.78 ?  230 ASP C N     1 
ATOM   12857 C  CA    . ASP C 2 251 ? 123.591 62.840  122.586 1.00 25.20 ?  230 ASP C CA    1 
ATOM   12858 C  C     . ASP C 2 251 ? 123.168 64.153  123.245 1.00 24.08 ?  230 ASP C C     1 
ATOM   12859 O  O     . ASP C 2 251 ? 122.049 64.272  123.766 1.00 23.34 ?  230 ASP C O     1 
ATOM   12860 C  CB    . ASP C 2 251 ? 124.456 62.065  123.591 1.00 25.73 ?  230 ASP C CB    1 
ATOM   12861 C  CG    . ASP C 2 251 ? 124.560 60.592  123.270 1.00 28.78 ?  230 ASP C CG    1 
ATOM   12862 O  OD1   . ASP C 2 251 ? 123.886 60.114  122.328 1.00 29.99 ?  230 ASP C OD1   1 
ATOM   12863 O  OD2   . ASP C 2 251 ? 125.335 59.910  123.973 1.00 33.31 -1 230 ASP C OD2   1 
ATOM   12864 N  N     . LEU C 2 252 ? 124.071 65.130  123.235 1.00 22.98 ?  231 LEU C N     1 
ATOM   12865 C  CA    . LEU C 2 252 ? 123.769 66.431  123.834 1.00 21.63 ?  231 LEU C CA    1 
ATOM   12866 C  C     . LEU C 2 252 ? 122.667 67.134  123.049 1.00 21.66 ?  231 LEU C C     1 
ATOM   12867 O  O     . LEU C 2 252 ? 121.752 67.722  123.626 1.00 19.41 ?  231 LEU C O     1 
ATOM   12868 C  CB    . LEU C 2 252 ? 125.013 67.319  123.887 1.00 21.89 ?  231 LEU C CB    1 
ATOM   12869 C  CG    . LEU C 2 252 ? 124.832 68.755  124.411 1.00 21.33 ?  231 LEU C CG    1 
ATOM   12870 C  CD1   . LEU C 2 252 ? 124.254 68.776  125.842 1.00 20.89 ?  231 LEU C CD1   1 
ATOM   12871 C  CD2   . LEU C 2 252 ? 126.173 69.490  124.336 1.00 20.31 ?  231 LEU C CD2   1 
ATOM   12872 N  N     . LEU C 2 253 ? 122.769 67.075  121.724 1.00 22.28 ?  232 LEU C N     1 
ATOM   12873 C  CA    . LEU C 2 253 ? 121.768 67.716  120.879 1.00 23.05 ?  232 LEU C CA    1 
ATOM   12874 C  C     . LEU C 2 253 ? 120.385 67.125  121.134 1.00 23.36 ?  232 LEU C C     1 
ATOM   12875 O  O     . LEU C 2 253 ? 119.419 67.877  121.353 1.00 22.96 ?  232 LEU C O     1 
ATOM   12876 C  CB    . LEU C 2 253 ? 122.144 67.619  119.399 1.00 23.53 ?  232 LEU C CB    1 
ATOM   12877 C  CG    . LEU C 2 253 ? 121.135 68.285  118.456 1.00 25.63 ?  232 LEU C CG    1 
ATOM   12878 C  CD1   . LEU C 2 253 ? 121.059 69.795  118.682 1.00 25.88 ?  232 LEU C CD1   1 
ATOM   12879 C  CD2   . LEU C 2 253 ? 121.501 67.971  117.013 1.00 27.67 ?  232 LEU C CD2   1 
ATOM   12880 N  N     . ASN C 2 254 ? 120.296 65.792  121.124 1.00 23.55 ?  233 ASN C N     1 
ATOM   12881 C  CA    . ASN C 2 254 ? 119.029 65.098  121.416 1.00 24.61 ?  233 ASN C CA    1 
ATOM   12882 C  C     . ASN C 2 254 ? 118.450 65.432  122.794 1.00 23.57 ?  233 ASN C C     1 
ATOM   12883 O  O     . ASN C 2 254 ? 117.247 65.641  122.936 1.00 23.52 ?  233 ASN C O     1 
ATOM   12884 C  CB    . ASN C 2 254 ? 119.176 63.583  121.252 1.00 24.99 ?  233 ASN C CB    1 
ATOM   12885 C  CG    . ASN C 2 254 ? 118.989 63.129  119.810 1.00 28.92 ?  233 ASN C CG    1 
ATOM   12886 O  OD1   . ASN C 2 254 ? 117.953 63.376  119.191 1.00 33.75 ?  233 ASN C OD1   1 
ATOM   12887 N  ND2   . ASN C 2 254 ? 119.992 62.459  119.275 1.00 30.99 ?  233 ASN C ND2   1 
ATOM   12888 N  N     . GLN C 2 255 ? 119.310 65.487  123.806 1.00 23.22 ?  234 GLN C N     1 
ATOM   12889 C  CA    . GLN C 2 255 ? 118.862 65.840  125.146 1.00 22.54 ?  234 GLN C CA    1 
ATOM   12890 C  C     . GLN C 2 255 ? 118.311 67.281  125.200 1.00 22.00 ?  234 GLN C C     1 
ATOM   12891 O  O     . GLN C 2 255 ? 117.249 67.536  125.793 1.00 21.73 ?  234 GLN C O     1 
ATOM   12892 C  CB    . GLN C 2 255 ? 119.992 65.649  126.156 1.00 22.85 ?  234 GLN C CB    1 
ATOM   12893 C  CG    . GLN C 2 255 ? 119.526 65.699  127.596 1.00 23.87 ?  234 GLN C CG    1 
ATOM   12894 C  CD    . GLN C 2 255 ? 120.663 65.540  128.599 1.00 24.95 ?  234 GLN C CD    1 
ATOM   12895 O  OE1   . GLN C 2 255 ? 121.798 65.219  128.232 1.00 24.21 ?  234 GLN C OE1   1 
ATOM   12896 N  NE2   . GLN C 2 255 ? 120.361 65.791  129.875 1.00 25.97 ?  234 GLN C NE2   1 
ATOM   12897 N  N     . LEU C 2 256 ? 119.031 68.210  124.584 1.00 21.27 ?  235 LEU C N     1 
ATOM   12898 C  CA    . LEU C 2 256 ? 118.582 69.597  124.505 1.00 21.37 ?  235 LEU C CA    1 
ATOM   12899 C  C     . LEU C 2 256 ? 117.302 69.710  123.671 1.00 21.21 ?  235 LEU C C     1 
ATOM   12900 O  O     . LEU C 2 256 ? 116.391 70.463  124.010 1.00 20.75 ?  235 LEU C O     1 
ATOM   12901 C  CB    . LEU C 2 256 ? 119.683 70.473  123.893 1.00 20.93 ?  235 LEU C CB    1 
ATOM   12902 C  CG    . LEU C 2 256 ? 120.931 70.779  124.724 1.00 21.74 ?  235 LEU C CG    1 
ATOM   12903 C  CD1   . LEU C 2 256 ? 121.947 71.557  123.874 1.00 20.15 ?  235 LEU C CD1   1 
ATOM   12904 C  CD2   . LEU C 2 256 ? 120.599 71.547  126.003 1.00 20.90 ?  235 LEU C CD2   1 
ATOM   12905 N  N     . TYR C 2 257 ? 117.262 68.963  122.573 1.00 21.68 ?  236 TYR C N     1 
ATOM   12906 C  CA    . TYR C 2 257 ? 116.116 68.952  121.664 1.00 22.40 ?  236 TYR C CA    1 
ATOM   12907 C  C     . TYR C 2 257 ? 114.829 68.517  122.385 1.00 23.31 ?  236 TYR C C     1 
ATOM   12908 O  O     . TYR C 2 257 ? 113.801 69.218  122.310 1.00 22.99 ?  236 TYR C O     1 
ATOM   12909 C  CB    . TYR C 2 257 ? 116.411 68.060  120.455 1.00 22.81 ?  236 TYR C CB    1 
ATOM   12910 C  CG    . TYR C 2 257 ? 115.244 67.855  119.508 1.00 23.76 ?  236 TYR C CG    1 
ATOM   12911 C  CD1   . TYR C 2 257 ? 114.739 68.915  118.750 1.00 24.05 ?  236 TYR C CD1   1 
ATOM   12912 C  CD2   . TYR C 2 257 ? 114.640 66.606  119.382 1.00 24.04 ?  236 TYR C CD2   1 
ATOM   12913 C  CE1   . TYR C 2 257 ? 113.661 68.735  117.890 1.00 24.40 ?  236 TYR C CE1   1 
ATOM   12914 C  CE2   . TYR C 2 257 ? 113.562 66.417  118.519 1.00 26.30 ?  236 TYR C CE2   1 
ATOM   12915 C  CZ    . TYR C 2 257 ? 113.090 67.484  117.777 1.00 25.80 ?  236 TYR C CZ    1 
ATOM   12916 O  OH    . TYR C 2 257 ? 112.039 67.292  116.926 1.00 28.42 ?  236 TYR C OH    1 
ATOM   12917 N  N     . GLU C 2 258 ? 114.900 67.397  123.112 1.00 22.99 ?  237 GLU C N     1 
ATOM   12918 C  CA    . GLU C 2 258 ? 113.736 66.869  123.833 1.00 24.46 ?  237 GLU C CA    1 
ATOM   12919 C  C     . GLU C 2 258 ? 113.208 67.861  124.857 1.00 23.86 ?  237 GLU C C     1 
ATOM   12920 O  O     . GLU C 2 258 ? 111.998 68.038  124.987 1.00 24.01 ?  237 GLU C O     1 
ATOM   12921 C  CB    . GLU C 2 258 ? 114.038 65.507  124.481 1.00 25.21 ?  237 GLU C CB    1 
ATOM   12922 C  CG    . GLU C 2 258 ? 114.230 64.363  123.459 1.00 30.12 ?  237 GLU C CG    1 
ATOM   12923 C  CD    . GLU C 2 258 ? 112.953 64.033  122.680 1.00 35.29 ?  237 GLU C CD    1 
ATOM   12924 O  OE1   . GLU C 2 258 ? 111.839 64.226  123.218 1.00 37.71 ?  237 GLU C OE1   1 
ATOM   12925 O  OE2   . GLU C 2 258 ? 113.064 63.571  121.520 1.00 39.07 -1 237 GLU C OE2   1 
ATOM   12926 N  N     . ASN C 2 259 ? 114.120 68.529  125.562 1.00 23.25 ?  238 ASN C N     1 
ATOM   12927 C  CA    . ASN C 2 259 ? 113.741 69.591  126.491 1.00 23.10 ?  238 ASN C CA    1 
ATOM   12928 C  C     . ASN C 2 259 ? 113.120 70.795  125.757 1.00 22.68 ?  238 ASN C C     1 
ATOM   12929 O  O     . ASN C 2 259 ? 112.128 71.371  126.213 1.00 22.73 ?  238 ASN C O     1 
ATOM   12930 C  CB    . ASN C 2 259 ? 114.954 70.012  127.324 1.00 23.22 ?  238 ASN C CB    1 
ATOM   12931 C  CG    . ASN C 2 259 ? 114.620 71.086  128.339 1.00 24.46 ?  238 ASN C CG    1 
ATOM   12932 O  OD1   . ASN C 2 259 ? 113.921 70.835  129.325 1.00 26.28 ?  238 ASN C OD1   1 
ATOM   12933 N  ND2   . ASN C 2 259 ? 115.119 72.294  128.103 1.00 24.93 ?  238 ASN C ND2   1 
ATOM   12934 N  N     . GLU C 2 260 ? 113.687 71.154  124.608 1.00 22.64 ?  239 GLU C N     1 
ATOM   12935 C  CA    . GLU C 2 260 ? 113.196 72.300  123.841 1.00 23.18 ?  239 GLU C CA    1 
ATOM   12936 C  C     . GLU C 2 260 ? 111.779 72.059  123.293 1.00 23.40 ?  239 GLU C C     1 
ATOM   12937 O  O     . GLU C 2 260 ? 110.968 72.995  123.210 1.00 23.57 ?  239 GLU C O     1 
ATOM   12938 C  CB    . GLU C 2 260 ? 114.170 72.665  122.711 1.00 23.19 ?  239 GLU C CB    1 
ATOM   12939 C  CG    . GLU C 2 260 ? 114.128 74.156  122.299 1.00 24.33 ?  239 GLU C CG    1 
ATOM   12940 C  CD    . GLU C 2 260 ? 114.587 75.114  123.413 1.00 27.99 ?  239 GLU C CD    1 
ATOM   12941 O  OE1   . GLU C 2 260 ? 115.081 74.660  124.468 1.00 27.36 ?  239 GLU C OE1   1 
ATOM   12942 O  OE2   . GLU C 2 260 ? 114.442 76.343  123.235 1.00 28.98 -1 239 GLU C OE2   1 
ATOM   12943 N  N     . LEU C 2 261 ? 111.485 70.809  122.934 1.00 23.35 ?  240 LEU C N     1 
ATOM   12944 C  CA    . LEU C 2 261 ? 110.126 70.426  122.519 1.00 23.74 ?  240 LEU C CA    1 
ATOM   12945 C  C     . LEU C 2 261 ? 109.082 70.744  123.592 1.00 23.80 ?  240 LEU C C     1 
ATOM   12946 O  O     . LEU C 2 261 ? 108.034 71.345  123.303 1.00 23.33 ?  240 LEU C O     1 
ATOM   12947 C  CB    . LEU C 2 261 ? 110.058 68.940  122.157 1.00 24.09 ?  240 LEU C CB    1 
ATOM   12948 C  CG    . LEU C 2 261 ? 110.779 68.497  120.883 1.00 24.07 ?  240 LEU C CG    1 
ATOM   12949 C  CD1   . LEU C 2 261 ? 110.618 66.994  120.696 1.00 24.77 ?  240 LEU C CD1   1 
ATOM   12950 C  CD2   . LEU C 2 261 ? 110.256 69.266  119.652 1.00 24.38 ?  240 LEU C CD2   1 
ATOM   12951 N  N     . GLU C 2 262 ? 109.368 70.332  124.821 1.00 23.41 ?  241 GLU C N     1 
ATOM   12952 C  CA    . GLU C 2 262 ? 108.480 70.599  125.950 1.00 24.02 ?  241 GLU C CA    1 
ATOM   12953 C  C     . GLU C 2 262 ? 108.343 72.103  126.234 1.00 22.91 ?  241 GLU C C     1 
ATOM   12954 O  O     . GLU C 2 262 ? 107.248 72.582  126.501 1.00 22.94 ?  241 GLU C O     1 
ATOM   12955 C  CB    . GLU C 2 262 ? 108.984 69.864  127.194 1.00 24.92 ?  241 GLU C CB    1 
ATOM   12956 C  CG    . GLU C 2 262 ? 108.927 68.348  127.091 1.00 27.82 ?  241 GLU C CG    1 
ATOM   12957 C  CD    . GLU C 2 262 ? 109.409 67.666  128.360 1.00 33.08 ?  241 GLU C CD    1 
ATOM   12958 O  OE1   . GLU C 2 262 ? 110.638 67.527  128.551 1.00 36.94 ?  241 GLU C OE1   1 
ATOM   12959 O  OE2   . GLU C 2 262 ? 108.553 67.260  129.167 1.00 37.48 -1 241 GLU C OE2   1 
ATOM   12960 N  N     . TYR C 2 263 ? 109.462 72.828  126.182 1.00 21.84 ?  242 TYR C N     1 
ATOM   12961 C  CA    . TYR C 2 263 ? 109.485 74.283  126.314 1.00 21.66 ?  242 TYR C CA    1 
ATOM   12962 C  C     . TYR C 2 263 ? 108.638 74.942  125.232 1.00 21.28 ?  242 TYR C C     1 
ATOM   12963 O  O     . TYR C 2 263 ? 107.854 75.859  125.515 1.00 21.14 ?  242 TYR C O     1 
ATOM   12964 C  CB    . TYR C 2 263 ? 110.930 74.792  126.191 1.00 21.44 ?  242 TYR C CB    1 
ATOM   12965 C  CG    . TYR C 2 263 ? 111.127 76.295  126.332 1.00 21.89 ?  242 TYR C CG    1 
ATOM   12966 C  CD1   . TYR C 2 263 ? 110.959 76.931  127.563 1.00 22.52 ?  242 TYR C CD1   1 
ATOM   12967 C  CD2   . TYR C 2 263 ? 111.520 77.073  125.239 1.00 22.58 ?  242 TYR C CD2   1 
ATOM   12968 C  CE1   . TYR C 2 263 ? 111.162 78.304  127.699 1.00 22.67 ?  242 TYR C CE1   1 
ATOM   12969 C  CE2   . TYR C 2 263 ? 111.732 78.451  125.366 1.00 24.03 ?  242 TYR C CE2   1 
ATOM   12970 C  CZ    . TYR C 2 263 ? 111.558 79.054  126.607 1.00 23.75 ?  242 TYR C CZ    1 
ATOM   12971 O  OH    . TYR C 2 263 ? 111.755 80.413  126.753 1.00 26.82 ?  242 TYR C OH    1 
ATOM   12972 N  N     . THR C 2 264 ? 108.803 74.474  123.998 1.00 20.66 ?  243 THR C N     1 
ATOM   12973 C  CA    . THR C 2 264 ? 108.072 75.029  122.850 1.00 20.99 ?  243 THR C CA    1 
ATOM   12974 C  C     . THR C 2 264 ? 106.561 74.830  123.015 1.00 21.22 ?  243 THR C C     1 
ATOM   12975 O  O     . THR C 2 264 ? 105.779 75.774  122.824 1.00 20.95 ?  243 THR C O     1 
ATOM   12976 C  CB    . THR C 2 264 ? 108.568 74.412  121.513 1.00 20.58 ?  243 THR C CB    1 
ATOM   12977 O  OG1   . THR C 2 264 ? 109.926 74.805  121.294 1.00 20.84 ?  243 THR C OG1   1 
ATOM   12978 C  CG2   . THR C 2 264 ? 107.722 74.884  120.329 1.00 20.90 ?  243 THR C CG2   1 
ATOM   12979 N  N     . GLU C 2 265 ? 106.155 73.618  123.397 1.00 21.62 ?  244 GLU C N     1 
ATOM   12980 C  CA    . GLU C 2 265 ? 104.736 73.334  123.617 1.00 23.46 ?  244 GLU C CA    1 
ATOM   12981 C  C     . GLU C 2 265 ? 104.168 74.189  124.732 1.00 23.33 ?  244 GLU C C     1 
ATOM   12982 O  O     . GLU C 2 265 ? 103.071 74.738  124.617 1.00 22.86 ?  244 GLU C O     1 
ATOM   12983 C  CB    . GLU C 2 265 ? 104.497 71.855  123.919 1.00 24.31 ?  244 GLU C CB    1 
ATOM   12984 C  CG    . GLU C 2 265 ? 104.678 70.949  122.705 1.00 27.63 ?  244 GLU C CG    1 
ATOM   12985 C  CD    . GLU C 2 265 ? 104.424 69.479  123.028 1.00 33.27 ?  244 GLU C CD    1 
ATOM   12986 O  OE1   . GLU C 2 265 ? 103.609 69.191  123.933 1.00 35.56 ?  244 GLU C OE1   1 
ATOM   12987 O  OE2   . GLU C 2 265 ? 105.036 68.610  122.366 1.00 35.96 -1 244 GLU C OE2   1 
ATOM   12988 N  N     . ASP C 2 266 ? 104.929 74.307  125.809 1.00 23.36 ?  245 ASP C N     1 
ATOM   12989 C  CA    . ASP C 2 266 ? 104.519 75.112  126.948 1.00 24.18 ?  245 ASP C CA    1 
ATOM   12990 C  C     . ASP C 2 266 ? 104.246 76.578  126.559 1.00 23.96 ?  245 ASP C C     1 
ATOM   12991 O  O     . ASP C 2 266 ? 103.280 77.179  127.025 1.00 24.19 ?  245 ASP C O     1 
ATOM   12992 C  CB    . ASP C 2 266 ? 105.595 75.040  128.028 1.00 25.14 ?  245 ASP C CB    1 
ATOM   12993 C  CG    . ASP C 2 266 ? 105.145 75.636  129.325 1.00 27.35 ?  245 ASP C CG    1 
ATOM   12994 O  OD1   . ASP C 2 266 ? 104.101 75.195  129.851 1.00 28.45 ?  245 ASP C OD1   1 
ATOM   12995 O  OD2   . ASP C 2 266 ? 105.839 76.552  129.816 1.00 31.99 -1 245 ASP C OD2   1 
ATOM   12996 N  N     . LEU C 2 267 ? 105.083 77.139  125.695 1.00 23.34 ?  246 LEU C N     1 
ATOM   12997 C  CA    . LEU C 2 267 ? 104.931 78.538  125.284 1.00 23.53 ?  246 LEU C CA    1 
ATOM   12998 C  C     . LEU C 2 267 ? 103.945 78.764  124.148 1.00 22.94 ?  246 LEU C C     1 
ATOM   12999 O  O     . LEU C 2 267 ? 103.178 79.728  124.173 1.00 23.14 ?  246 LEU C O     1 
ATOM   13000 C  CB    . LEU C 2 267 ? 106.284 79.119  124.881 1.00 23.37 ?  246 LEU C CB    1 
ATOM   13001 C  CG    . LEU C 2 267 ? 107.293 79.391  125.999 1.00 26.17 ?  246 LEU C CG    1 
ATOM   13002 C  CD1   . LEU C 2 267 ? 108.542 79.979  125.383 1.00 27.31 ?  246 LEU C CD1   1 
ATOM   13003 C  CD2   . LEU C 2 267 ? 106.713 80.352  127.032 1.00 28.08 ?  246 LEU C CD2   1 
ATOM   13004 N  N     . TYR C 2 268 ? 103.985 77.890  123.146 1.00 22.46 ?  247 TYR C N     1 
ATOM   13005 C  CA    . TYR C 2 268 ? 103.265 78.136  121.900 1.00 22.00 ?  247 TYR C CA    1 
ATOM   13006 C  C     . TYR C 2 268 ? 101.891 77.509  121.739 1.00 22.26 ?  247 TYR C C     1 
ATOM   13007 O  O     . TYR C 2 268 ? 101.152 77.923  120.844 1.00 22.17 ?  247 TYR C O     1 
ATOM   13008 C  CB    . TYR C 2 268 ? 104.139 77.769  120.693 1.00 21.73 ?  247 TYR C CB    1 
ATOM   13009 C  CG    . TYR C 2 268 ? 105.285 78.725  120.467 1.00 21.49 ?  247 TYR C CG    1 
ATOM   13010 C  CD1   . TYR C 2 268 ? 106.579 78.403  120.887 1.00 19.45 ?  247 TYR C CD1   1 
ATOM   13011 C  CD2   . TYR C 2 268 ? 105.072 79.961  119.847 1.00 22.71 ?  247 TYR C CD2   1 
ATOM   13012 C  CE1   . TYR C 2 268 ? 107.640 79.292  120.688 1.00 20.30 ?  247 TYR C CE1   1 
ATOM   13013 C  CE2   . TYR C 2 268 ? 106.129 80.863  119.635 1.00 21.69 ?  247 TYR C CE2   1 
ATOM   13014 C  CZ    . TYR C 2 268 ? 107.405 80.510  120.046 1.00 21.40 ?  247 TYR C CZ    1 
ATOM   13015 O  OH    . TYR C 2 268 ? 108.438 81.386  119.833 1.00 22.11 ?  247 TYR C OH    1 
ATOM   13016 N  N     . ASP C 2 269 ? 101.542 76.510  122.557 1.00 22.40 ?  248 ASP C N     1 
ATOM   13017 C  CA    . ASP C 2 269 ? 100.204 75.901  122.450 1.00 22.75 ?  248 ASP C CA    1 
ATOM   13018 C  C     . ASP C 2 269 ? 99.090  76.942  122.576 1.00 22.55 ?  248 ASP C C     1 
ATOM   13019 O  O     . ASP C 2 269 ? 98.083  76.862  121.862 1.00 22.22 ?  248 ASP C O     1 
ATOM   13020 C  CB    . ASP C 2 269 ? 99.991  74.757  123.459 1.00 23.03 ?  248 ASP C CB    1 
ATOM   13021 C  CG    . ASP C 2 269 ? 100.604 73.443  123.004 1.00 25.02 ?  248 ASP C CG    1 
ATOM   13022 O  OD1   . ASP C 2 269 ? 101.026 73.327  121.833 1.00 26.85 ?  248 ASP C OD1   1 
ATOM   13023 O  OD2   . ASP C 2 269 ? 100.660 72.507  123.827 1.00 28.74 -1 248 ASP C OD2   1 
ATOM   13024 N  N     . GLN C 2 270 ? 99.277  77.920  123.467 1.00 22.21 ?  249 GLN C N     1 
ATOM   13025 C  CA    . GLN C 2 270 ? 98.248  78.965  123.675 1.00 22.39 ?  249 GLN C CA    1 
ATOM   13026 C  C     . GLN C 2 270 ? 98.081  79.938  122.500 1.00 21.65 ?  249 GLN C C     1 
ATOM   13027 O  O     . GLN C 2 270 ? 97.108  80.692  122.460 1.00 21.70 ?  249 GLN C O     1 
ATOM   13028 C  CB    . GLN C 2 270 ? 98.469  79.734  124.988 1.00 22.53 ?  249 GLN C CB    1 
ATOM   13029 C  CG    . GLN C 2 270 ? 99.801  80.519  125.096 1.00 22.73 ?  249 GLN C CG    1 
ATOM   13030 C  CD    . GLN C 2 270 ? 99.920  81.241  126.422 1.00 25.39 ?  249 GLN C CD    1 
ATOM   13031 O  OE1   . GLN C 2 270 ? 99.192  80.938  127.370 1.00 27.88 ?  249 GLN C OE1   1 
ATOM   13032 N  NE2   . GLN C 2 270 ? 100.831 82.207  126.501 1.00 24.88 ?  249 GLN C NE2   1 
ATOM   13033 N  N     . VAL C 2 271 ? 99.025  79.920  121.557 1.00 20.91 ?  250 VAL C N     1 
ATOM   13034 C  CA    . VAL C 2 271 ? 98.936  80.760  120.339 1.00 20.62 ?  250 VAL C CA    1 
ATOM   13035 C  C     . VAL C 2 271 ? 98.839  79.910  119.058 1.00 20.53 ?  250 VAL C C     1 
ATOM   13036 O  O     . VAL C 2 271 ? 98.785  80.446  117.940 1.00 20.05 ?  250 VAL C O     1 
ATOM   13037 C  CB    . VAL C 2 271 ? 100.083 81.835  120.245 1.00 20.32 ?  250 VAL C CB    1 
ATOM   13038 C  CG1   . VAL C 2 271 ? 99.975  82.846  121.381 1.00 20.35 ?  250 VAL C CG1   1 
ATOM   13039 C  CG2   . VAL C 2 271 ? 101.480 81.196  120.243 1.00 19.32 ?  250 VAL C CG2   1 
ATOM   13040 N  N     . GLY C 2 272 ? 98.804  78.588  119.240 1.00 20.29 ?  251 GLY C N     1 
ATOM   13041 C  CA    . GLY C 2 272 ? 98.527  77.647  118.151 1.00 20.51 ?  251 GLY C CA    1 
ATOM   13042 C  C     . GLY C 2 272 ? 99.682  77.352  117.207 1.00 20.99 ?  251 GLY C C     1 
ATOM   13043 O  O     . GLY C 2 272 ? 99.459  76.906  116.070 1.00 20.22 ?  251 GLY C O     1 
ATOM   13044 N  N     . LEU C 2 273 ? 100.914 77.596  117.664 1.00 20.76 ?  252 LEU C N     1 
ATOM   13045 C  CA    . LEU C 2 273 ? 102.063 77.571  116.754 1.00 21.38 ?  252 LEU C CA    1 
ATOM   13046 C  C     . LEU C 2 273 ? 103.128 76.516  117.039 1.00 21.86 ?  252 LEU C C     1 
ATOM   13047 O  O     . LEU C 2 273 ? 104.167 76.497  116.381 1.00 22.45 ?  252 LEU C O     1 
ATOM   13048 C  CB    . LEU C 2 273 ? 102.708 78.965  116.657 1.00 21.44 ?  252 LEU C CB    1 
ATOM   13049 C  CG    . LEU C 2 273 ? 101.850 80.143  116.191 1.00 22.02 ?  252 LEU C CG    1 
ATOM   13050 C  CD1   . LEU C 2 273 ? 102.672 81.426  116.246 1.00 22.86 ?  252 LEU C CD1   1 
ATOM   13051 C  CD2   . LEU C 2 273 ? 101.289 79.901  114.772 1.00 23.88 ?  252 LEU C CD2   1 
ATOM   13052 N  N     . SER C 2 274 ? 102.872 75.624  117.995 1.00 22.19 ?  253 SER C N     1 
ATOM   13053 C  CA    . SER C 2 274 ? 103.916 74.730  118.491 1.00 22.47 ?  253 SER C CA    1 
ATOM   13054 C  C     . SER C 2 274 ? 104.545 73.865  117.398 1.00 22.94 ?  253 SER C C     1 
ATOM   13055 O  O     . SER C 2 274 ? 105.764 73.744  117.326 1.00 22.07 ?  253 SER C O     1 
ATOM   13056 C  CB    . SER C 2 274 ? 103.376 73.850  119.622 1.00 22.91 ?  253 SER C CB    1 
ATOM   13057 O  OG    . SER C 2 274 ? 103.106 74.647  120.757 1.00 24.25 ?  253 SER C OG    1 
ATOM   13058 N  N     . HIS C 2 275 ? 103.710 73.299  116.529 1.00 24.59 ?  254 HIS C N     1 
ATOM   13059 C  CA    . HIS C 2 275 ? 104.193 72.428  115.452 1.00 25.66 ?  254 HIS C CA    1 
ATOM   13060 C  C     . HIS C 2 275 ? 105.094 73.183  114.461 1.00 26.01 ?  254 HIS C C     1 
ATOM   13061 O  O     . HIS C 2 275 ? 106.121 72.656  113.999 1.00 26.23 ?  254 HIS C O     1 
ATOM   13062 C  CB    . HIS C 2 275 ? 103.009 71.781  114.722 1.00 26.89 ?  254 HIS C CB    1 
ATOM   13063 C  CG    . HIS C 2 275 ? 103.414 70.796  113.669 1.00 29.10 ?  254 HIS C CG    1 
ATOM   13064 N  ND1   . HIS C 2 275 ? 104.253 69.731  113.928 1.00 32.70 ?  254 HIS C ND1   1 
ATOM   13065 C  CD2   . HIS C 2 275 ? 103.095 70.712  112.357 1.00 31.68 ?  254 HIS C CD2   1 
ATOM   13066 C  CE1   . HIS C 2 275 ? 104.435 69.037  112.819 1.00 33.55 ?  254 HIS C CE1   1 
ATOM   13067 N  NE2   . HIS C 2 275 ? 103.731 69.601  111.855 1.00 33.71 ?  254 HIS C NE2   1 
ATOM   13068 N  N     . ASP C 2 276 ? 104.701 74.411  114.144 1.00 25.93 ?  255 ASP C N     1 
ATOM   13069 C  CA    . ASP C 2 276 ? 105.473 75.279  113.259 1.00 26.65 ?  255 ASP C CA    1 
ATOM   13070 C  C     . ASP C 2 276 ? 106.846 75.621  113.839 1.00 25.61 ?  255 ASP C C     1 
ATOM   13071 O  O     . ASP C 2 276 ? 107.858 75.541  113.130 1.00 25.34 ?  255 ASP C O     1 
ATOM   13072 C  CB    . ASP C 2 276 ? 104.695 76.560  112.951 1.00 27.44 ?  255 ASP C CB    1 
ATOM   13073 C  CG    . ASP C 2 276 ? 104.277 76.646  111.500 1.00 32.09 ?  255 ASP C CG    1 
ATOM   13074 O  OD1   . ASP C 2 276 ? 105.121 76.346  110.620 1.00 36.67 ?  255 ASP C OD1   1 
ATOM   13075 O  OD2   . ASP C 2 276 ? 103.105 76.999  111.233 1.00 36.30 -1 255 ASP C OD2   1 
ATOM   13076 N  N     . VAL C 2 277 ? 106.868 75.998  115.122 1.00 24.17 ?  256 VAL C N     1 
ATOM   13077 C  CA    . VAL C 2 277 ? 108.120 76.315  115.822 1.00 23.71 ?  256 VAL C CA    1 
ATOM   13078 C  C     . VAL C 2 277 ? 109.043 75.094  115.869 1.00 23.48 ?  256 VAL C C     1 
ATOM   13079 O  O     . VAL C 2 277 ? 110.252 75.219  115.670 1.00 23.08 ?  256 VAL C O     1 
ATOM   13080 C  CB    . VAL C 2 277 ? 107.879 76.838  117.266 1.00 23.27 ?  256 VAL C CB    1 
ATOM   13081 C  CG1   . VAL C 2 277 ? 109.207 77.160  117.960 1.00 24.02 ?  256 VAL C CG1   1 
ATOM   13082 C  CG2   . VAL C 2 277 ? 106.980 78.067  117.260 1.00 23.35 ?  256 VAL C CG2   1 
ATOM   13083 N  N     . LYS C 2 278 ? 108.471 73.922  116.132 1.00 23.36 ?  257 LYS C N     1 
ATOM   13084 C  CA    . LYS C 2 278 ? 109.239 72.676  116.153 1.00 24.12 ?  257 LYS C CA    1 
ATOM   13085 C  C     . LYS C 2 278 ? 109.979 72.417  114.843 1.00 24.30 ?  257 LYS C C     1 
ATOM   13086 O  O     . LYS C 2 278 ? 111.141 71.985  114.851 1.00 24.37 ?  257 LYS C O     1 
ATOM   13087 C  CB    . LYS C 2 278 ? 108.346 71.486  116.500 1.00 24.22 ?  257 LYS C CB    1 
ATOM   13088 C  CG    . LYS C 2 278 ? 107.944 71.421  117.964 1.00 24.96 ?  257 LYS C CG    1 
ATOM   13089 C  CD    . LYS C 2 278 ? 106.944 70.291  118.168 1.00 26.34 ?  257 LYS C CD    1 
ATOM   13090 C  CE    . LYS C 2 278 ? 106.482 70.213  119.597 1.00 27.16 ?  257 LYS C CE    1 
ATOM   13091 N  NZ    . LYS C 2 278 ? 105.514 69.082  119.730 1.00 29.60 1  257 LYS C NZ    1 
ATOM   13092 N  N     . LYS C 2 279 ? 109.315 72.684  113.720 1.00 24.55 ?  258 LYS C N     1 
ATOM   13093 C  CA    . LYS C 2 279 ? 109.962 72.559  112.417 1.00 24.85 ?  258 LYS C CA    1 
ATOM   13094 C  C     . LYS C 2 279 ? 111.137 73.529  112.309 1.00 24.57 ?  258 LYS C C     1 
ATOM   13095 O  O     . LYS C 2 279 ? 112.191 73.170  111.787 1.00 24.07 ?  258 LYS C O     1 
ATOM   13096 C  CB    . LYS C 2 279 ? 108.963 72.817  111.289 1.00 25.30 ?  258 LYS C CB    1 
ATOM   13097 C  CG    . LYS C 2 279 ? 107.806 71.844  111.255 1.00 26.63 ?  258 LYS C CG    1 
ATOM   13098 C  CD    . LYS C 2 279 ? 106.877 72.199  110.101 1.00 29.30 ?  258 LYS C CD    1 
ATOM   13099 C  CE    . LYS C 2 279 ? 105.806 71.162  109.941 1.00 31.79 ?  258 LYS C CE    1 
ATOM   13100 N  NZ    . LYS C 2 279 ? 104.733 71.694  109.064 1.00 33.80 1  258 LYS C NZ    1 
ATOM   13101 N  N     . PHE C 2 280 ? 110.950 74.741  112.833 1.00 24.29 ?  259 PHE C N     1 
ATOM   13102 C  CA    . PHE C 2 280 ? 111.979 75.790  112.796 1.00 24.90 ?  259 PHE C CA    1 
ATOM   13103 C  C     . PHE C 2 280 ? 113.222 75.417  113.624 1.00 24.86 ?  259 PHE C C     1 
ATOM   13104 O  O     . PHE C 2 280 ? 114.358 75.617  113.179 1.00 24.68 ?  259 PHE C O     1 
ATOM   13105 C  CB    . PHE C 2 280 ? 111.366 77.119  113.259 1.00 24.70 ?  259 PHE C CB    1 
ATOM   13106 C  CG    . PHE C 2 280 ? 112.245 78.330  113.047 1.00 25.70 ?  259 PHE C CG    1 
ATOM   13107 C  CD1   . PHE C 2 280 ? 112.693 78.680  111.773 1.00 26.86 ?  259 PHE C CD1   1 
ATOM   13108 C  CD2   . PHE C 2 280 ? 112.586 79.153  114.128 1.00 26.19 ?  259 PHE C CD2   1 
ATOM   13109 C  CE1   . PHE C 2 280 ? 113.488 79.818  111.575 1.00 26.66 ?  259 PHE C CE1   1 
ATOM   13110 C  CE2   . PHE C 2 280 ? 113.371 80.295  113.939 1.00 26.52 ?  259 PHE C CE2   1 
ATOM   13111 C  CZ    . PHE C 2 280 ? 113.828 80.624  112.657 1.00 26.23 ?  259 PHE C CZ    1 
ATOM   13112 N  N     . ILE C 2 281 ? 113.007 74.867  114.820 1.00 25.53 ?  260 ILE C N     1 
ATOM   13113 C  CA    . ILE C 2 281 ? 114.131 74.485  115.678 1.00 26.21 ?  260 ILE C CA    1 
ATOM   13114 C  C     . ILE C 2 281 ? 114.918 73.298  115.104 1.00 26.47 ?  260 ILE C C     1 
ATOM   13115 O  O     . ILE C 2 281 ? 116.135 73.241  115.252 1.00 26.52 ?  260 ILE C O     1 
ATOM   13116 C  CB    . ILE C 2 281 ? 113.736 74.284  117.182 1.00 26.27 ?  260 ILE C CB    1 
ATOM   13117 C  CG1   . ILE C 2 281 ? 113.052 72.936  117.421 1.00 27.37 ?  260 ILE C CG1   1 
ATOM   13118 C  CG2   . ILE C 2 281 ? 112.890 75.476  117.683 1.00 26.92 ?  260 ILE C CG2   1 
ATOM   13119 C  CD1   . ILE C 2 281 ? 112.708 72.656  118.885 1.00 29.51 ?  260 ILE C CD1   1 
ATOM   13120 N  N     . ARG C 2 282 ? 114.230 72.385  114.416 1.00 26.57 ?  261 ARG C N     1 
ATOM   13121 C  CA    . ARG C 2 282 ? 114.904 71.273  113.740 1.00 26.84 ?  261 ARG C CA    1 
ATOM   13122 C  C     . ARG C 2 282 ? 115.778 71.781  112.594 1.00 27.34 ?  261 ARG C C     1 
ATOM   13123 O  O     . ARG C 2 282 ? 116.917 71.348  112.439 1.00 27.54 ?  261 ARG C O     1 
ATOM   13124 C  CB    . ARG C 2 282 ? 113.906 70.224  113.245 1.00 26.98 ?  261 ARG C CB    1 
ATOM   13125 C  CG    . ARG C 2 282 ? 113.400 69.284  114.322 1.00 26.53 ?  261 ARG C CG    1 
ATOM   13126 C  CD    . ARG C 2 282 ? 112.637 68.085  113.721 1.00 27.77 ?  261 ARG C CD    1 
ATOM   13127 N  NE    . ARG C 2 282 ? 111.352 68.465  113.142 1.00 28.67 ?  261 ARG C NE    1 
ATOM   13128 C  CZ    . ARG C 2 282 ? 110.213 68.573  113.830 1.00 29.68 ?  261 ARG C CZ    1 
ATOM   13129 N  NH1   . ARG C 2 282 ? 110.181 68.329  115.139 1.00 28.31 1  261 ARG C NH1   1 
ATOM   13130 N  NH2   . ARG C 2 282 ? 109.098 68.917  113.206 1.00 29.15 ?  261 ARG C NH2   1 
ATOM   13131 N  N     . TYR C 2 283 ? 115.232 72.708  111.810 1.00 27.78 ?  262 TYR C N     1 
ATOM   13132 C  CA    . TYR C 2 283 ? 115.970 73.405  110.757 1.00 28.18 ?  262 TYR C CA    1 
ATOM   13133 C  C     . TYR C 2 283 ? 117.274 74.015  111.302 1.00 27.08 ?  262 TYR C C     1 
ATOM   13134 O  O     . TYR C 2 283 ? 118.364 73.814  110.744 1.00 26.51 ?  262 TYR C O     1 
ATOM   13135 C  CB    . TYR C 2 283 ? 115.079 74.498  110.155 1.00 29.11 ?  262 TYR C CB    1 
ATOM   13136 C  CG    . TYR C 2 283 ? 115.713 75.288  109.036 1.00 32.56 ?  262 TYR C CG    1 
ATOM   13137 C  CD1   . TYR C 2 283 ? 115.847 74.738  107.760 1.00 36.59 ?  262 TYR C CD1   1 
ATOM   13138 C  CD2   . TYR C 2 283 ? 116.165 76.595  109.244 1.00 36.34 ?  262 TYR C CD2   1 
ATOM   13139 C  CE1   . TYR C 2 283 ? 116.427 75.463  106.714 1.00 39.47 ?  262 TYR C CE1   1 
ATOM   13140 C  CE2   . TYR C 2 283 ? 116.746 77.336  108.198 1.00 39.23 ?  262 TYR C CE2   1 
ATOM   13141 C  CZ    . TYR C 2 283 ? 116.873 76.757  106.939 1.00 40.48 ?  262 TYR C CZ    1 
ATOM   13142 O  OH    . TYR C 2 283 ? 117.442 77.461  105.903 1.00 44.00 ?  262 TYR C OH    1 
ATOM   13143 N  N     . ASN C 2 284 ? 117.158 74.736  112.408 1.00 26.08 ?  263 ASN C N     1 
ATOM   13144 C  CA    . ASN C 2 284 ? 118.318 75.371  113.015 1.00 25.73 ?  263 ASN C CA    1 
ATOM   13145 C  C     . ASN C 2 284 ? 119.277 74.415  113.727 1.00 25.24 ?  263 ASN C C     1 
ATOM   13146 O  O     . ASN C 2 284 ? 120.492 74.657  113.734 1.00 25.56 ?  263 ASN C O     1 
ATOM   13147 C  CB    . ASN C 2 284 ? 117.881 76.541  113.897 1.00 25.69 ?  263 ASN C CB    1 
ATOM   13148 C  CG    . ASN C 2 284 ? 117.459 77.739  113.076 1.00 26.39 ?  263 ASN C CG    1 
ATOM   13149 O  OD1   . ASN C 2 284 ? 118.299 78.457  112.527 1.00 26.91 ?  263 ASN C OD1   1 
ATOM   13150 N  ND2   . ASN C 2 284 ? 116.156 77.961  112.978 1.00 27.56 ?  263 ASN C ND2   1 
ATOM   13151 N  N     . ALA C 2 285 ? 118.755 73.323  114.292 1.00 24.51 ?  264 ALA C N     1 
ATOM   13152 C  CA    . ALA C 2 285 ? 119.619 72.238  114.793 1.00 24.19 ?  264 ALA C CA    1 
ATOM   13153 C  C     . ALA C 2 285 ? 120.591 71.725  113.711 1.00 24.63 ?  264 ALA C C     1 
ATOM   13154 O  O     . ALA C 2 285 ? 121.770 71.507  113.982 1.00 24.01 ?  264 ALA C O     1 
ATOM   13155 C  CB    . ALA C 2 285 ? 118.795 71.088  115.341 1.00 23.63 ?  264 ALA C CB    1 
ATOM   13156 N  N     . ASN C 2 286 ? 120.086 71.539  112.492 1.00 24.66 ?  265 ASN C N     1 
ATOM   13157 C  CA    . ASN C 2 286 ? 120.928 71.151  111.360 1.00 25.24 ?  265 ASN C CA    1 
ATOM   13158 C  C     . ASN C 2 286 ? 122.027 72.156  111.032 1.00 25.09 ?  265 ASN C C     1 
ATOM   13159 O  O     . ASN C 2 286 ? 123.138 71.753  110.648 1.00 24.14 ?  265 ASN C O     1 
ATOM   13160 C  CB    . ASN C 2 286 ? 120.082 70.872  110.104 1.00 25.62 ?  265 ASN C CB    1 
ATOM   13161 C  CG    . ASN C 2 286 ? 119.335 69.551  110.188 1.00 26.46 ?  265 ASN C CG    1 
ATOM   13162 O  OD1   . ASN C 2 286 ? 119.600 68.726  111.067 1.00 27.14 ?  265 ASN C OD1   1 
ATOM   13163 N  ND2   . ASN C 2 286 ? 118.379 69.350  109.279 1.00 27.89 ?  265 ASN C ND2   1 
ATOM   13164 N  N     . LYS C 2 287 ? 121.707 73.446  111.166 1.00 24.99 ?  266 LYS C N     1 
ATOM   13165 C  CA    . LYS C 2 287 ? 122.671 74.531  110.974 1.00 25.91 ?  266 LYS C CA    1 
ATOM   13166 C  C     . LYS C 2 287 ? 123.745 74.508  112.057 1.00 25.23 ?  266 LYS C C     1 
ATOM   13167 O  O     . LYS C 2 287 ? 124.920 74.748  111.772 1.00 25.34 ?  266 LYS C O     1 
ATOM   13168 C  CB    . LYS C 2 287 ? 121.988 75.899  110.994 1.00 25.96 ?  266 LYS C CB    1 
ATOM   13169 C  CG    . LYS C 2 287 ? 121.195 76.262  109.748 1.00 29.60 ?  266 LYS C CG    1 
ATOM   13170 C  CD    . LYS C 2 287 ? 120.809 77.745  109.824 1.00 34.20 ?  266 LYS C CD    1 
ATOM   13171 C  CE    . LYS C 2 287 ? 120.101 78.222  108.581 1.00 37.67 ?  266 LYS C CE    1 
ATOM   13172 N  NZ    . LYS C 2 287 ? 119.877 79.704  108.656 1.00 39.48 1  266 LYS C NZ    1 
ATOM   13173 N  N     . ALA C 2 288 ? 123.339 74.238  113.295 1.00 24.87 ?  267 ALA C N     1 
ATOM   13174 C  CA    . ALA C 2 288 ? 124.299 74.072  114.402 1.00 24.23 ?  267 ALA C CA    1 
ATOM   13175 C  C     . ALA C 2 288 ? 125.255 72.901  114.144 1.00 24.24 ?  267 ALA C C     1 
ATOM   13176 O  O     . ALA C 2 288 ? 126.469 73.036  114.304 1.00 23.96 ?  267 ALA C O     1 
ATOM   13177 C  CB    . ALA C 2 288 ? 123.571 73.886  115.720 1.00 24.23 ?  267 ALA C CB    1 
ATOM   13178 N  N     . LEU C 2 289 ? 124.709 71.754  113.739 1.00 24.63 ?  268 LEU C N     1 
ATOM   13179 C  CA    . LEU C 2 289 ? 125.544 70.603  113.385 1.00 25.14 ?  268 LEU C CA    1 
ATOM   13180 C  C     . LEU C 2 289 ? 126.513 70.965  112.272 1.00 25.58 ?  268 LEU C C     1 
ATOM   13181 O  O     . LEU C 2 289 ? 127.692 70.635  112.344 1.00 25.42 ?  268 LEU C O     1 
ATOM   13182 C  CB    . LEU C 2 289 ? 124.698 69.383  112.987 1.00 25.28 ?  268 LEU C CB    1 
ATOM   13183 C  CG    . LEU C 2 289 ? 123.996 68.667  114.145 1.00 25.93 ?  268 LEU C CG    1 
ATOM   13184 C  CD1   . LEU C 2 289 ? 122.864 67.797  113.636 1.00 26.50 ?  268 LEU C CD1   1 
ATOM   13185 C  CD2   . LEU C 2 289 ? 124.975 67.859  115.018 1.00 25.20 ?  268 LEU C CD2   1 
ATOM   13186 N  N     . MET C 2 290 ? 126.020 71.664  111.249 1.00 26.32 ?  269 MET C N     1 
ATOM   13187 C  CA    . MET C 2 290 ? 126.887 72.067  110.146 1.00 27.41 ?  269 MET C CA    1 
ATOM   13188 C  C     . MET C 2 290 ? 128.002 73.014  110.582 1.00 26.66 ?  269 MET C C     1 
ATOM   13189 O  O     . MET C 2 290 ? 129.133 72.893  110.106 1.00 26.69 ?  269 MET C O     1 
ATOM   13190 C  CB    . MET C 2 290 ? 126.077 72.630  108.982 1.00 28.28 ?  269 MET C CB    1 
ATOM   13191 C  CG    . MET C 2 290 ? 125.689 71.535  107.990 1.00 32.91 ?  269 MET C CG    1 
ATOM   13192 S  SD    . MET C 2 290 ? 124.461 72.071  106.794 1.00 42.49 ?  269 MET C SD    1 
ATOM   13193 C  CE    . MET C 2 290 ? 123.002 71.220  107.394 1.00 38.74 ?  269 MET C CE    1 
ATOM   13194 N  N     . ASN C 2 291 ? 127.693 73.924  111.508 1.00 25.48 ?  270 ASN C N     1 
ATOM   13195 C  CA    . ASN C 2 291 ? 128.700 74.822  112.095 1.00 25.39 ?  270 ASN C CA    1 
ATOM   13196 C  C     . ASN C 2 291 ? 129.821 74.049  112.809 1.00 25.18 ?  270 ASN C C     1 
ATOM   13197 O  O     . ASN C 2 291 ? 130.959 74.530  112.913 1.00 24.73 ?  270 ASN C O     1 
ATOM   13198 C  CB    . ASN C 2 291 ? 128.043 75.821  113.056 1.00 24.83 ?  270 ASN C CB    1 
ATOM   13199 C  CG    . ASN C 2 291 ? 127.281 76.934  112.327 1.00 25.58 ?  270 ASN C CG    1 
ATOM   13200 O  OD1   . ASN C 2 291 ? 127.424 77.119  111.122 1.00 25.58 ?  270 ASN C OD1   1 
ATOM   13201 N  ND2   . ASN C 2 291 ? 126.470 77.673  113.067 1.00 24.32 ?  270 ASN C ND2   1 
ATOM   13202 N  N     . LEU C 2 292 ? 129.481 72.840  113.265 1.00 25.09 ?  271 LEU C N     1 
ATOM   13203 C  CA    . LEU C 2 292 ? 130.419 71.911  113.911 1.00 25.46 ?  271 LEU C CA    1 
ATOM   13204 C  C     . LEU C 2 292 ? 131.094 70.921  112.948 1.00 26.18 ?  271 LEU C C     1 
ATOM   13205 O  O     . LEU C 2 292 ? 131.890 70.062  113.370 1.00 26.06 ?  271 LEU C O     1 
ATOM   13206 C  CB    . LEU C 2 292 ? 129.703 71.162  115.042 1.00 25.19 ?  271 LEU C CB    1 
ATOM   13207 C  CG    . LEU C 2 292 ? 129.249 72.030  116.228 1.00 25.03 ?  271 LEU C CG    1 
ATOM   13208 C  CD1   . LEU C 2 292 ? 128.306 71.256  117.122 1.00 24.50 ?  271 LEU C CD1   1 
ATOM   13209 C  CD2   . LEU C 2 292 ? 130.465 72.537  117.020 1.00 25.64 ?  271 LEU C CD2   1 
ATOM   13210 N  N     . GLY C 2 293 ? 130.783 71.042  111.658 1.00 26.71 ?  272 GLY C N     1 
ATOM   13211 C  CA    . GLY C 2 293 ? 131.341 70.152  110.633 1.00 28.06 ?  272 GLY C CA    1 
ATOM   13212 C  C     . GLY C 2 293 ? 130.693 68.779  110.551 1.00 29.34 ?  272 GLY C C     1 
ATOM   13213 O  O     . GLY C 2 293 ? 131.300 67.826  110.040 1.00 29.73 ?  272 GLY C O     1 
ATOM   13214 N  N     . PHE C 2 294 ? 129.463 68.672  111.049 1.00 29.88 ?  273 PHE C N     1 
ATOM   13215 C  CA    . PHE C 2 294 ? 128.721 67.413  111.045 1.00 31.24 ?  273 PHE C CA    1 
ATOM   13216 C  C     . PHE C 2 294 ? 127.567 67.452  110.034 1.00 32.42 ?  273 PHE C C     1 
ATOM   13217 O  O     . PHE C 2 294 ? 127.091 68.531  109.654 1.00 32.30 ?  273 PHE C O     1 
ATOM   13218 C  CB    . PHE C 2 294 ? 128.192 67.085  112.448 1.00 30.82 ?  273 PHE C CB    1 
ATOM   13219 C  CG    . PHE C 2 294 ? 129.274 66.921  113.496 1.00 30.93 ?  273 PHE C CG    1 
ATOM   13220 C  CD1   . PHE C 2 294 ? 130.390 66.118  113.261 1.00 30.85 ?  273 PHE C CD1   1 
ATOM   13221 C  CD2   . PHE C 2 294 ? 129.165 67.561  114.721 1.00 30.30 ?  273 PHE C CD2   1 
ATOM   13222 C  CE1   . PHE C 2 294 ? 131.384 65.976  114.227 1.00 30.75 ?  273 PHE C CE1   1 
ATOM   13223 C  CE2   . PHE C 2 294 ? 130.147 67.414  115.704 1.00 30.41 ?  273 PHE C CE2   1 
ATOM   13224 C  CZ    . PHE C 2 294 ? 131.257 66.615  115.458 1.00 30.88 ?  273 PHE C CZ    1 
ATOM   13225 N  N     . ASP C 2 295 ? 127.138 66.270  109.595 1.00 33.81 ?  274 ASP C N     1 
ATOM   13226 C  CA    . ASP C 2 295 ? 126.001 66.131  108.681 1.00 35.32 ?  274 ASP C CA    1 
ATOM   13227 C  C     . ASP C 2 295 ? 124.673 66.504  109.364 1.00 35.36 ?  274 ASP C C     1 
ATOM   13228 O  O     . ASP C 2 295 ? 124.525 66.299  110.567 1.00 34.78 ?  274 ASP C O     1 
ATOM   13229 C  CB    . ASP C 2 295 ? 125.908 64.686  108.170 1.00 35.95 ?  274 ASP C CB    1 
ATOM   13230 C  CG    . ASP C 2 295 ? 127.116 64.269  107.335 1.00 37.98 ?  274 ASP C CG    1 
ATOM   13231 O  OD1   . ASP C 2 295 ? 127.765 65.134  106.707 1.00 39.83 ?  274 ASP C OD1   1 
ATOM   13232 O  OD2   . ASP C 2 295 ? 127.412 63.055  107.307 1.00 40.03 -1 274 ASP C OD2   1 
ATOM   13233 N  N     . PRO C 2 296 ? 123.705 67.043  108.598 1.00 36.33 ?  275 PRO C N     1 
ATOM   13234 C  CA    . PRO C 2 296 ? 122.360 67.308  109.155 1.00 36.92 ?  275 PRO C CA    1 
ATOM   13235 C  C     . PRO C 2 296 ? 121.707 66.052  109.754 1.00 37.68 ?  275 PRO C C     1 
ATOM   13236 O  O     . PRO C 2 296 ? 121.894 64.950  109.231 1.00 38.07 ?  275 PRO C O     1 
ATOM   13237 C  CB    . PRO C 2 296 ? 121.561 67.805  107.940 1.00 36.82 ?  275 PRO C CB    1 
ATOM   13238 C  CG    . PRO C 2 296 ? 122.412 67.467  106.724 1.00 37.42 ?  275 PRO C CG    1 
ATOM   13239 C  CD    . PRO C 2 296 ? 123.824 67.508  107.204 1.00 36.41 ?  275 PRO C CD    1 
ATOM   13240 N  N     . TYR C 2 297 ? 120.954 66.226  110.840 1.00 38.10 ?  276 TYR C N     1 
ATOM   13241 C  CA    . TYR C 2 297 ? 120.375 65.106  111.597 1.00 38.96 ?  276 TYR C CA    1 
ATOM   13242 C  C     . TYR C 2 297 ? 118.862 64.968  111.394 1.00 39.71 ?  276 TYR C C     1 
ATOM   13243 O  O     . TYR C 2 297 ? 118.312 63.866  111.498 1.00 40.18 ?  276 TYR C O     1 
ATOM   13244 C  CB    . TYR C 2 297 ? 120.688 65.292  113.086 1.00 38.94 ?  276 TYR C CB    1 
ATOM   13245 C  CG    . TYR C 2 297 ? 120.268 64.186  114.030 1.00 39.64 ?  276 TYR C CG    1 
ATOM   13246 C  CD1   . TYR C 2 297 ? 121.055 63.044  114.201 1.00 40.43 ?  276 TYR C CD1   1 
ATOM   13247 C  CD2   . TYR C 2 297 ? 119.117 64.308  114.802 1.00 41.04 ?  276 TYR C CD2   1 
ATOM   13248 C  CE1   . TYR C 2 297 ? 120.678 62.033  115.087 1.00 41.69 ?  276 TYR C CE1   1 
ATOM   13249 C  CE2   . TYR C 2 297 ? 118.728 63.304  115.690 1.00 41.60 ?  276 TYR C CE2   1 
ATOM   13250 C  CZ    . TYR C 2 297 ? 119.515 62.174  115.832 1.00 41.92 ?  276 TYR C CZ    1 
ATOM   13251 O  OH    . TYR C 2 297 ? 119.132 61.190  116.717 1.00 42.52 ?  276 TYR C OH    1 
ATOM   13252 N  N     . PHE C 2 298 ? 118.190 66.081  111.121 1.00 39.85 ?  277 PHE C N     1 
ATOM   13253 C  CA    . PHE C 2 298 ? 116.745 66.066  110.925 1.00 40.77 ?  277 PHE C CA    1 
ATOM   13254 C  C     . PHE C 2 298 ? 116.402 66.222  109.452 1.00 41.95 ?  277 PHE C C     1 
ATOM   13255 O  O     . PHE C 2 298 ? 117.137 66.874  108.710 1.00 41.91 ?  277 PHE C O     1 
ATOM   13256 C  CB    . PHE C 2 298 ? 116.082 67.180  111.743 1.00 39.94 ?  277 PHE C CB    1 
ATOM   13257 C  CG    . PHE C 2 298 ? 116.251 67.029  113.231 1.00 39.09 ?  277 PHE C CG    1 
ATOM   13258 C  CD1   . PHE C 2 298 ? 117.120 67.857  113.931 1.00 37.84 ?  277 PHE C CD1   1 
ATOM   13259 C  CD2   . PHE C 2 298 ? 115.529 66.068  113.935 1.00 38.97 ?  277 PHE C CD2   1 
ATOM   13260 C  CE1   . PHE C 2 298 ? 117.279 67.729  115.308 1.00 37.46 ?  277 PHE C CE1   1 
ATOM   13261 C  CE2   . PHE C 2 298 ? 115.678 65.931  115.309 1.00 38.20 ?  277 PHE C CE2   1 
ATOM   13262 C  CZ    . PHE C 2 298 ? 116.555 66.764  116.000 1.00 37.91 ?  277 PHE C CZ    1 
ATOM   13263 N  N     . GLU C 2 299 ? 115.292 65.624  109.019 1.00 43.74 ?  278 GLU C N     1 
ATOM   13264 C  CA    . GLU C 2 299 ? 114.862 65.765  107.624 1.00 45.61 ?  278 GLU C CA    1 
ATOM   13265 C  C     . GLU C 2 299 ? 114.317 67.170  107.367 1.00 46.04 ?  278 GLU C C     1 
ATOM   13266 O  O     . GLU C 2 299 ? 113.770 67.808  108.267 1.00 45.88 ?  278 GLU C O     1 
ATOM   13267 C  CB    . GLU C 2 299 ? 113.820 64.709  107.239 1.00 46.43 ?  278 GLU C CB    1 
ATOM   13268 C  CG    . GLU C 2 299 ? 113.879 64.308  105.755 1.00 48.82 ?  278 GLU C CG    1 
ATOM   13269 C  CD    . GLU C 2 299 ? 112.594 63.674  105.245 1.00 51.86 ?  278 GLU C CD    1 
ATOM   13270 O  OE1   . GLU C 2 299 ? 112.544 63.330  104.042 1.00 53.35 ?  278 GLU C OE1   1 
ATOM   13271 O  OE2   . GLU C 2 299 ? 111.631 63.522  106.033 1.00 53.10 -1 278 GLU C OE2   1 
ATOM   13272 N  N     . GLU C 2 300 ? 114.487 67.647  106.135 1.00 47.16 ?  279 GLU C N     1 
ATOM   13273 C  CA    . GLU C 2 300 ? 114.004 68.970  105.723 1.00 47.75 ?  279 GLU C CA    1 
ATOM   13274 C  C     . GLU C 2 300 ? 112.471 69.071  105.740 1.00 47.71 ?  279 GLU C C     1 
ATOM   13275 O  O     . GLU C 2 300 ? 111.774 68.118  105.374 1.00 47.77 ?  279 GLU C O     1 
ATOM   13276 C  CB    . GLU C 2 300 ? 114.566 69.336  104.338 1.00 48.42 ?  279 GLU C CB    1 
ATOM   13277 C  CG    . GLU C 2 300 ? 114.373 68.262  103.261 1.00 50.63 ?  279 GLU C CG    1 
ATOM   13278 C  CD    . GLU C 2 300 ? 115.375 68.376  102.111 1.00 53.06 ?  279 GLU C CD    1 
ATOM   13279 O  OE1   . GLU C 2 300 ? 115.480 69.469  101.505 1.00 54.35 ?  279 GLU C OE1   1 
ATOM   13280 O  OE2   . GLU C 2 300 ? 116.047 67.364  101.807 1.00 53.32 -1 279 GLU C OE2   1 
ATOM   13281 N  N     . GLU C 2 301 ? 111.968 70.222  106.186 1.00 47.40 ?  280 GLU C N     1 
ATOM   13282 C  CA    . GLU C 2 301 ? 110.529 70.509  106.239 1.00 47.46 ?  280 GLU C CA    1 
ATOM   13283 C  C     . GLU C 2 301 ? 110.250 71.945  105.778 1.00 47.31 ?  280 GLU C C     1 
ATOM   13284 O  O     . GLU C 2 301 ? 111.135 72.803  105.843 1.00 47.21 ?  280 GLU C O     1 
ATOM   13285 C  CB    . GLU C 2 301 ? 109.986 70.324  107.663 1.00 47.19 ?  280 GLU C CB    1 
ATOM   13286 C  CG    . GLU C 2 301 ? 110.119 68.918  108.251 1.00 47.14 ?  280 GLU C CG    1 
ATOM   13287 C  CD    . GLU C 2 301 ? 110.052 68.915  109.775 1.00 47.21 ?  280 GLU C CD    1 
ATOM   13288 O  OE1   . GLU C 2 301 ? 109.017 68.483  110.322 1.00 46.97 ?  280 GLU C OE1   1 
ATOM   13289 O  OE2   . GLU C 2 301 ? 111.029 69.357  110.426 1.00 46.13 -1 280 GLU C OE2   1 
ATOM   13290 N  N     . ASP C 2 302 ? 109.024 72.204  105.321 1.00 47.15 ?  281 ASP C N     1 
ATOM   13291 C  CA    . ASP C 2 302 ? 108.624 73.554  104.913 1.00 47.04 ?  281 ASP C CA    1 
ATOM   13292 C  C     . ASP C 2 302 ? 108.391 74.445  106.137 1.00 46.05 ?  281 ASP C C     1 
ATOM   13293 O  O     . ASP C 2 302 ? 107.524 74.157  106.969 1.00 46.10 ?  281 ASP C O     1 
ATOM   13294 C  CB    . ASP C 2 302 ? 107.357 73.524  104.037 1.00 47.66 ?  281 ASP C CB    1 
ATOM   13295 C  CG    . ASP C 2 302 ? 107.614 72.997  102.623 1.00 49.53 ?  281 ASP C CG    1 
ATOM   13296 O  OD1   . ASP C 2 302 ? 108.707 73.244  102.064 1.00 50.58 ?  281 ASP C OD1   1 
ATOM   13297 O  OD2   . ASP C 2 302 ? 106.699 72.351  102.056 1.00 51.14 -1 281 ASP C OD2   1 
ATOM   13298 N  N     . ILE C 2 303 ? 109.179 75.513  106.244 1.00 44.96 ?  282 ILE C N     1 
ATOM   13299 C  CA    . ILE C 2 303 ? 109.035 76.503  107.317 1.00 43.99 ?  282 ILE C CA    1 
ATOM   13300 C  C     . ILE C 2 303 ? 107.979 77.540  106.924 1.00 43.53 ?  282 ILE C C     1 
ATOM   13301 O  O     . ILE C 2 303 ? 107.840 77.862  105.743 1.00 43.52 ?  282 ILE C O     1 
ATOM   13302 C  CB    . ILE C 2 303 ? 110.389 77.211  107.621 1.00 43.84 ?  282 ILE C CB    1 
ATOM   13303 C  CG1   . ILE C 2 303 ? 111.498 76.188  107.932 1.00 43.91 ?  282 ILE C CG1   1 
ATOM   13304 C  CG2   . ILE C 2 303 ? 110.243 78.258  108.738 1.00 43.55 ?  282 ILE C CG2   1 
ATOM   13305 C  CD1   . ILE C 2 303 ? 111.223 75.264  109.122 1.00 42.76 ?  282 ILE C CD1   1 
ATOM   13306 N  N     . ASN C 2 304 ? 107.235 78.046  107.908 1.00 42.51 ?  283 ASN C N     1 
ATOM   13307 C  CA    . ASN C 2 304 ? 106.233 79.086  107.669 1.00 41.93 ?  283 ASN C CA    1 
ATOM   13308 C  C     . ASN C 2 304 ? 106.840 80.237  106.850 1.00 41.78 ?  283 ASN C C     1 
ATOM   13309 O  O     . ASN C 2 304 ? 107.829 80.845  107.282 1.00 41.13 ?  283 ASN C O     1 
ATOM   13310 C  CB    . ASN C 2 304 ? 105.675 79.606  109.003 1.00 41.83 ?  283 ASN C CB    1 
ATOM   13311 C  CG    . ASN C 2 304 ? 104.323 80.304  108.856 1.00 41.27 ?  283 ASN C CG    1 
ATOM   13312 O  OD1   . ASN C 2 304 ? 104.115 81.116  107.958 1.00 41.28 ?  283 ASN C OD1   1 
ATOM   13313 N  ND2   . ASN C 2 304 ? 103.403 79.989  109.755 1.00 40.67 ?  283 ASN C ND2   1 
ATOM   13314 N  N     . PRO C 2 305 ? 106.263 80.527  105.658 1.00 41.74 ?  284 PRO C N     1 
ATOM   13315 C  CA    . PRO C 2 305 ? 106.837 81.564  104.786 1.00 41.82 ?  284 PRO C CA    1 
ATOM   13316 C  C     . PRO C 2 305 ? 106.815 82.961  105.417 1.00 41.56 ?  284 PRO C C     1 
ATOM   13317 O  O     . PRO C 2 305 ? 107.607 83.822  105.029 1.00 41.46 ?  284 PRO C O     1 
ATOM   13318 C  CB    . PRO C 2 305 ? 105.955 81.509  103.522 1.00 42.14 ?  284 PRO C CB    1 
ATOM   13319 C  CG    . PRO C 2 305 ? 104.696 80.848  103.948 1.00 42.59 ?  284 PRO C CG    1 
ATOM   13320 C  CD    . PRO C 2 305 ? 105.082 79.886  105.046 1.00 42.05 ?  284 PRO C CD    1 
ATOM   13321 N  N     . ILE C 2 306 ? 105.927 83.167  106.387 1.00 41.19 ?  285 ILE C N     1 
ATOM   13322 C  CA    . ILE C 2 306 ? 105.875 84.410  107.156 1.00 41.47 ?  285 ILE C CA    1 
ATOM   13323 C  C     . ILE C 2 306 ? 107.203 84.636  107.891 1.00 41.71 ?  285 ILE C C     1 
ATOM   13324 O  O     . ILE C 2 306 ? 107.762 85.731  107.855 1.00 41.38 ?  285 ILE C O     1 
ATOM   13325 C  CB    . ILE C 2 306 ? 104.709 84.397  108.180 1.00 41.22 ?  285 ILE C CB    1 
ATOM   13326 C  CG1   . ILE C 2 306 ? 103.357 84.285  107.463 1.00 41.27 ?  285 ILE C CG1   1 
ATOM   13327 C  CG2   . ILE C 2 306 ? 104.758 85.629  109.081 1.00 40.37 ?  285 ILE C CG2   1 
ATOM   13328 C  CD1   . ILE C 2 306 ? 102.207 83.891  108.379 1.00 41.85 ?  285 ILE C CD1   1 
ATOM   13329 N  N     . VAL C 2 307 ? 107.693 83.585  108.549 1.00 42.33 ?  286 VAL C N     1 
ATOM   13330 C  CA    . VAL C 2 307 ? 108.967 83.624  109.273 1.00 43.36 ?  286 VAL C CA    1 
ATOM   13331 C  C     . VAL C 2 307 ? 110.157 83.861  108.334 1.00 44.51 ?  286 VAL C C     1 
ATOM   13332 O  O     . VAL C 2 307 ? 111.112 84.540  108.705 1.00 44.57 ?  286 VAL C O     1 
ATOM   13333 C  CB    . VAL C 2 307 ? 109.154 82.353  110.136 1.00 42.97 ?  286 VAL C CB    1 
ATOM   13334 C  CG1   . VAL C 2 307 ? 110.607 82.200  110.617 1.00 42.86 ?  286 VAL C CG1   1 
ATOM   13335 C  CG2   . VAL C 2 307 ? 108.200 82.400  111.315 1.00 41.93 ?  286 VAL C CG2   1 
ATOM   13336 N  N     . LEU C 2 308 ? 110.070 83.316  107.120 1.00 46.21 ?  287 LEU C N     1 
ATOM   13337 C  CA    . LEU C 2 308 ? 111.083 83.516  106.073 1.00 47.66 ?  287 LEU C CA    1 
ATOM   13338 C  C     . LEU C 2 308 ? 111.103 84.953  105.553 1.00 48.82 ?  287 LEU C C     1 
ATOM   13339 O  O     . LEU C 2 308 ? 112.171 85.484  105.220 1.00 49.02 ?  287 LEU C O     1 
ATOM   13340 C  CB    . LEU C 2 308 ? 110.871 82.525  104.921 1.00 47.95 ?  287 LEU C CB    1 
ATOM   13341 C  CG    . LEU C 2 308 ? 111.591 81.166  104.977 1.00 48.23 ?  287 LEU C CG    1 
ATOM   13342 C  CD1   . LEU C 2 308 ? 111.918 80.694  106.401 1.00 48.10 ?  287 LEU C CD1   1 
ATOM   13343 C  CD2   . LEU C 2 308 ? 110.813 80.098  104.213 1.00 48.81 ?  287 LEU C CD2   1 
ATOM   13344 N  N     . ASN C 2 309 ? 109.923 85.570  105.483 1.00 49.80 ?  288 ASN C N     1 
ATOM   13345 C  CA    . ASN C 2 309 ? 109.810 87.004  105.227 1.00 51.09 ?  288 ASN C CA    1 
ATOM   13346 C  C     . ASN C 2 309 ? 110.282 87.852  106.411 1.00 51.08 ?  288 ASN C C     1 
ATOM   13347 O  O     . ASN C 2 309 ? 110.687 89.001  106.232 1.00 51.41 ?  288 ASN C O     1 
ATOM   13348 C  CB    . ASN C 2 309 ? 108.383 87.381  104.821 1.00 51.37 ?  288 ASN C CB    1 
ATOM   13349 C  CG    . ASN C 2 309 ? 108.101 87.098  103.359 1.00 53.22 ?  288 ASN C CG    1 
ATOM   13350 O  OD1   . ASN C 2 309 ? 108.424 86.022  102.844 1.00 54.39 ?  288 ASN C OD1   1 
ATOM   13351 N  ND2   . ASN C 2 309 ? 107.496 88.066  102.678 1.00 54.70 ?  288 ASN C ND2   1 
ATOM   13352 N  N     . GLY C 2 310 ? 110.229 87.280  107.614 1.00 51.25 ?  289 GLY C N     1 
ATOM   13353 C  CA    . GLY C 2 310 ? 110.777 87.912  108.815 1.00 51.35 ?  289 GLY C CA    1 
ATOM   13354 C  C     . GLY C 2 310 ? 112.293 88.059  108.781 1.00 51.86 ?  289 GLY C C     1 
ATOM   13355 O  O     . GLY C 2 310 ? 112.858 88.892  109.498 1.00 51.49 ?  289 GLY C O     1 
ATOM   13356 N  N     . LEU C 2 311 ? 112.950 87.248  107.951 1.00 52.45 ?  290 LEU C N     1 
ATOM   13357 C  CA    . LEU C 2 311 ? 114.402 87.316  107.767 1.00 52.99 ?  290 LEU C CA    1 
ATOM   13358 C  C     . LEU C 2 311 ? 114.782 88.331  106.686 1.00 53.65 ?  290 LEU C C     1 
ATOM   13359 O  O     . LEU C 2 311 ? 114.545 88.116  105.491 1.00 54.22 ?  290 LEU C O     1 
ATOM   13360 C  CB    . LEU C 2 311 ? 114.971 85.936  107.423 1.00 53.08 ?  290 LEU C CB    1 
ATOM   13361 C  CG    . LEU C 2 311 ? 115.045 84.864  108.515 1.00 53.33 ?  290 LEU C CG    1 
ATOM   13362 C  CD1   . LEU C 2 311 ? 115.272 83.493  107.895 1.00 53.79 ?  290 LEU C CD1   1 
ATOM   13363 C  CD2   . LEU C 2 311 ? 116.136 85.181  109.540 1.00 53.22 ?  290 LEU C CD2   1 
ATOM   13364 N  N     . LYS C 2 330 ? 140.902 116.365 113.716 1.00 58.93 ?  309 LYS C N     1 
ATOM   13365 C  CA    . LYS C 2 330 ? 142.353 116.477 113.628 1.00 61.98 ?  309 LYS C CA    1 
ATOM   13366 C  C     . LYS C 2 330 ? 142.844 116.205 112.210 1.00 61.97 ?  309 LYS C C     1 
ATOM   13367 O  O     . LYS C 2 330 ? 142.289 115.369 111.497 1.00 59.24 ?  309 LYS C O     1 
ATOM   13368 C  CB    . LYS C 2 330 ? 143.026 115.514 114.608 1.00 60.82 ?  309 LYS C CB    1 
ATOM   13369 C  CG    . LYS C 2 330 ? 142.683 115.767 116.067 1.00 60.80 ?  309 LYS C CG    1 
ATOM   13370 C  CD    . LYS C 2 330 ? 143.188 117.125 116.524 1.00 60.28 ?  309 LYS C CD    1 
ATOM   13371 C  CE    . LYS C 2 330 ? 142.913 117.353 118.002 1.00 62.15 ?  309 LYS C CE    1 
ATOM   13372 N  NZ    . LYS C 2 330 ? 143.381 118.689 118.458 1.00 62.59 1  309 LYS C NZ    1 
ATOM   13373 N  N     . ALA C 2 331 ? 143.891 116.920 111.810 1.00 55.97 ?  310 ALA C N     1 
ATOM   13374 C  CA    . ALA C 2 331 ? 144.504 116.762 110.502 1.00 53.20 ?  310 ALA C CA    1 
ATOM   13375 C  C     . ALA C 2 331 ? 145.953 116.321 110.657 1.00 52.13 ?  310 ALA C C     1 
ATOM   13376 O  O     . ALA C 2 331 ? 146.596 116.597 111.674 1.00 53.07 ?  310 ALA C O     1 
ATOM   13377 C  CB    . ALA C 2 331 ? 144.437 118.065 109.698 1.00 51.98 ?  310 ALA C CB    1 
ATOM   13378 N  N     . THR C 2 332 ? 146.455 115.624 109.639 1.00 45.82 ?  311 THR C N     1 
ATOM   13379 C  CA    . THR C 2 332 ? 147.837 115.164 109.651 1.00 46.85 ?  311 THR C CA    1 
ATOM   13380 C  C     . THR C 2 332 ? 148.795 116.345 109.755 1.00 43.12 ?  311 THR C C     1 
ATOM   13381 O  O     . THR C 2 332 ? 148.584 117.394 109.141 1.00 48.26 ?  311 THR C O     1 
ATOM   13382 C  CB    . THR C 2 332 ? 148.130 114.341 108.394 1.00 45.72 ?  311 THR C CB    1 
ATOM   13383 O  OG1   . THR C 2 332 ? 149.416 113.720 108.510 1.00 46.36 ?  311 THR C OG1   1 
ATOM   13384 C  CG2   . THR C 2 332 ? 148.079 115.215 107.154 1.00 44.89 ?  311 THR C CG2   1 
ATOM   13385 N  N     . VAL C 2 333 ? 149.846 116.167 110.549 1.00 42.01 ?  312 VAL C N     1 
ATOM   13386 C  CA    . VAL C 2 333 ? 150.752 117.246 110.927 1.00 38.55 ?  312 VAL C CA    1 
ATOM   13387 C  C     . VAL C 2 333 ? 152.144 116.906 110.414 1.00 41.18 ?  312 VAL C C     1 
ATOM   13388 O  O     . VAL C 2 333 ? 152.688 115.839 110.728 1.00 46.85 ?  312 VAL C O     1 
ATOM   13389 C  CB    . VAL C 2 333 ? 150.766 117.466 112.446 1.00 37.39 ?  312 VAL C CB    1 
ATOM   13390 C  CG1   . VAL C 2 333 ? 151.951 118.329 112.849 1.00 40.81 ?  312 VAL C CG1   1 
ATOM   13391 C  CG2   . VAL C 2 333 ? 149.457 118.082 112.911 1.00 39.47 ?  312 VAL C CG2   1 
ATOM   13392 N  N     . GLU C 2 334 ? 152.728 117.812 109.625 1.00 34.01 ?  313 GLU C N     1 
ATOM   13393 C  CA    . GLU C 2 334 ? 154.137 117.718 109.287 1.00 34.45 ?  313 GLU C CA    1 
ATOM   13394 C  C     . GLU C 2 334 ? 154.891 118.924 109.837 1.00 37.55 ?  313 GLU C C     1 
ATOM   13395 O  O     . GLU C 2 334 ? 154.349 120.033 109.880 1.00 40.51 ?  313 GLU C O     1 
ATOM   13396 C  CB    . GLU C 2 334 ? 154.375 117.646 107.774 1.00 34.27 ?  313 GLU C CB    1 
ATOM   13397 C  CG    . GLU C 2 334 ? 155.816 117.475 107.344 1.00 38.73 ?  313 GLU C CG    1 
ATOM   13398 C  CD    . GLU C 2 334 ? 155.949 117.365 105.836 1.00 42.14 ?  313 GLU C CD    1 
ATOM   13399 O  OE1   . GLU C 2 334 ? 154.916 117.462 105.141 1.00 40.76 ?  313 GLU C OE1   1 
ATOM   13400 O  OE2   . GLU C 2 334 ? 157.078 117.164 105.346 1.00 39.96 -1 313 GLU C OE2   1 
ATOM   13401 N  N     . PRO C 2 335 ? 156.136 118.744 110.268 1.00 33.56 ?  314 PRO C N     1 
ATOM   13402 C  CA    . PRO C 2 335 ? 156.941 119.892 110.696 1.00 34.05 ?  314 PRO C CA    1 
ATOM   13403 C  C     . PRO C 2 335 ? 157.322 120.763 109.508 1.00 35.93 ?  314 PRO C C     1 
ATOM   13404 O  O     . PRO C 2 335 ? 157.348 120.329 108.355 1.00 36.72 ?  314 PRO C O     1 
ATOM   13405 C  CB    . PRO C 2 335 ? 158.176 119.252 111.341 1.00 36.78 ?  314 PRO C CB    1 
ATOM   13406 C  CG    . PRO C 2 335 ? 157.822 117.801 111.533 1.00 33.20 ?  314 PRO C CG    1 
ATOM   13407 C  CD    . PRO C 2 335 ? 156.851 117.473 110.450 1.00 33.09 ?  314 PRO C CD    1 
ATOM   13408 N  N     . LEU C 2 336 ? 157.619 122.023 109.809 1.00 31.29 ?  315 LEU C N     1 
ATOM   13409 C  CA    . LEU C 2 336 ? 158.008 122.988 108.792 1.00 25.88 ?  315 LEU C CA    1 
ATOM   13410 C  C     . LEU C 2 336 ? 159.497 122.874 108.502 1.00 28.32 ?  315 LEU C C     1 
ATOM   13411 O  O     . LEU C 2 336 ? 160.325 122.969 109.414 1.00 26.34 ?  315 LEU C O     1 
ATOM   13412 C  CB    . LEU C 2 336 ? 157.666 124.411 109.235 1.00 25.22 ?  315 LEU C CB    1 
ATOM   13413 C  CG    . LEU C 2 336 ? 156.246 124.878 108.925 1.00 26.15 ?  315 LEU C CG    1 
ATOM   13414 C  CD1   . LEU C 2 336 ? 156.026 126.290 109.437 1.00 26.32 ?  315 LEU C CD1   1 
ATOM   13415 C  CD2   . LEU C 2 336 ? 155.998 124.804 107.429 1.00 21.64 ?  315 LEU C CD2   1 
ATOM   13416 N  N     . LYS C 2 337 ? 159.832 122.669 107.234 1.00 24.69 ?  316 LYS C N     1 
ATOM   13417 C  CA    . LYS C 2 337 ? 161.217 122.648 106.794 1.00 25.14 ?  316 LYS C CA    1 
ATOM   13418 C  C     . LYS C 2 337 ? 161.700 124.067 106.517 1.00 19.78 ?  316 LYS C C     1 
ATOM   13419 O  O     . LYS C 2 337 ? 160.910 124.988 106.302 1.00 30.21 ?  316 LYS C O     1 
ATOM   13420 C  CB    . LYS C 2 337 ? 161.375 121.785 105.541 1.00 29.25 ?  316 LYS C CB    1 
ATOM   13421 C  CG    . LYS C 2 337 ? 161.127 120.303 105.764 1.00 28.02 ?  316 LYS C CG    1 
ATOM   13422 C  CD    . LYS C 2 337 ? 161.277 119.515 104.475 1.00 27.52 ?  316 LYS C CD    1 
ATOM   13423 C  CE    . LYS C 2 337 ? 161.052 118.031 104.706 1.00 32.76 ?  316 LYS C CE    1 
ATOM   13424 N  NZ    . LYS C 2 337 ? 161.173 117.246 103.446 1.00 30.53 1  316 LYS C NZ    1 
ATOM   13425 N  N     . ASP C 2 338 ? 163.023 124.234 106.527 1.00 29.74 ?  317 ASP C N     1 
ATOM   13426 C  CA    . ASP C 2 338 ? 163.605 125.534 106.220 1.00 26.29 ?  317 ASP C CA    1 
ATOM   13427 C  C     . ASP C 2 338 ? 163.360 125.950 104.777 1.00 29.71 ?  317 ASP C C     1 
ATOM   13428 O  O     . ASP C 2 338 ? 163.461 127.141 104.464 1.00 21.95 ?  317 ASP C O     1 
ATOM   13429 C  CB    . ASP C 2 338 ? 165.106 125.521 106.513 1.00 25.78 ?  317 ASP C CB    1 
ATOM   13430 C  CG    . ASP C 2 338 ? 165.436 124.836 107.823 1.00 35.15 ?  317 ASP C CG    1 
ATOM   13431 O  OD1   . ASP C 2 338 ? 165.068 123.653 107.987 1.00 32.75 ?  317 ASP C OD1   1 
ATOM   13432 O  OD2   . ASP C 2 338 ? 166.063 125.480 108.690 1.00 36.30 -1 317 ASP C OD2   1 
ATOM   13433 N  N     . ASP C 2 339 ? 163.038 125.003 103.897 1.00 26.99 ?  318 ASP C N     1 
ATOM   13434 C  CA    . ASP C 2 339 ? 162.757 125.307 102.501 1.00 24.15 ?  318 ASP C CA    1 
ATOM   13435 C  C     . ASP C 2 339 ? 161.323 125.758 102.265 1.00 20.41 ?  318 ASP C C     1 
ATOM   13436 O  O     . ASP C 2 339 ? 161.017 126.251 101.174 1.00 28.59 ?  318 ASP C O     1 
ATOM   13437 C  CB    . ASP C 2 339 ? 163.057 124.085 101.625 1.00 23.02 ?  318 ASP C CB    1 
ATOM   13438 C  CG    . ASP C 2 339 ? 164.246 123.289 102.125 1.00 32.33 ?  318 ASP C CG    1 
ATOM   13439 O  OD1   . ASP C 2 339 ? 164.040 122.180 102.660 1.00 34.56 ?  318 ASP C OD1   1 
ATOM   13440 O  OD2   . ASP C 2 339 ? 165.388 123.775 101.984 1.00 32.78 -1 318 ASP C OD2   1 
ATOM   13441 N  N     . ASP C 2 340 ? 160.441 125.603 103.250 1.00 18.60 ?  319 ASP C N     1 
ATOM   13442 C  CA    . ASP C 2 340 ? 159.066 126.072 103.141 1.00 13.68 ?  319 ASP C CA    1 
ATOM   13443 C  C     . ASP C 2 340 ? 158.932 127.561 103.424 1.00 14.05 ?  319 ASP C C     1 
ATOM   13444 O  O     . ASP C 2 340 ? 157.842 128.115 103.248 1.00 30.27 ?  319 ASP C O     1 
ATOM   13445 C  CB    . ASP C 2 340 ? 158.161 125.285 104.093 1.00 12.38 ?  319 ASP C CB    1 
ATOM   13446 C  CG    . ASP C 2 340 ? 158.396 123.792 104.020 1.00 24.62 ?  319 ASP C CG    1 
ATOM   13447 O  OD1   . ASP C 2 340 ? 158.547 123.266 102.898 1.00 25.90 ?  319 ASP C OD1   1 
ATOM   13448 O  OD2   . ASP C 2 340 ? 158.424 123.141 105.085 1.00 30.97 -1 319 ASP C OD2   1 
ATOM   13449 N  N     . PHE C 2 341 ? 160.005 128.214 103.860 1.00 14.34 ?  320 PHE C N     1 
ATOM   13450 C  CA    . PHE C 2 341 ? 160.005 129.640 104.144 1.00 3.83  ?  320 PHE C CA    1 
ATOM   13451 C  C     . PHE C 2 341 ? 160.572 130.462 102.995 1.00 6.43  ?  320 PHE C C     1 
ATOM   13452 O  O     . PHE C 2 341 ? 160.711 131.681 103.128 1.00 11.38 ?  320 PHE C O     1 
ATOM   13453 C  CB    . PHE C 2 341 ? 160.797 129.917 105.421 1.00 8.01  ?  320 PHE C CB    1 
ATOM   13454 C  CG    . PHE C 2 341 ? 160.090 129.497 106.676 1.00 9.69  ?  320 PHE C CG    1 
ATOM   13455 C  CD1   . PHE C 2 341 ? 159.250 130.373 107.339 1.00 6.44  ?  320 PHE C CD1   1 
ATOM   13456 C  CD2   . PHE C 2 341 ? 160.268 128.225 107.194 1.00 7.94  ?  320 PHE C CD2   1 
ATOM   13457 C  CE1   . PHE C 2 341 ? 158.600 129.990 108.494 1.00 10.55 ?  320 PHE C CE1   1 
ATOM   13458 C  CE2   . PHE C 2 341 ? 159.618 127.836 108.348 1.00 8.92  ?  320 PHE C CE2   1 
ATOM   13459 C  CZ    . PHE C 2 341 ? 158.782 128.721 108.999 1.00 6.02  ?  320 PHE C CZ    1 
ATOM   13460 N  N     . TYR C 2 342 ? 160.900 129.825 101.873 1.00 6.07  ?  321 TYR C N     1 
ATOM   13461 C  CA    . TYR C 2 342 ? 161.494 130.500 100.730 1.00 12.59 ?  321 TYR C CA    1 
ATOM   13462 C  C     . TYR C 2 342 ? 160.751 130.097 99.466  1.00 16.10 ?  321 TYR C C     1 
ATOM   13463 O  O     . TYR C 2 342 ? 160.365 128.936 99.305  1.00 16.79 ?  321 TYR C O     1 
ATOM   13464 C  CB    . TYR C 2 342 ? 162.982 130.162 100.597 1.00 6.93  ?  321 TYR C CB    1 
ATOM   13465 C  CG    . TYR C 2 342 ? 163.809 130.608 101.779 1.00 3.43  ?  321 TYR C CG    1 
ATOM   13466 C  CD1   . TYR C 2 342 ? 163.983 129.781 102.880 1.00 8.24  ?  321 TYR C CD1   1 
ATOM   13467 C  CD2   . TYR C 2 342 ? 164.407 131.859 101.799 1.00 11.16 ?  321 TYR C CD2   1 
ATOM   13468 C  CE1   . TYR C 2 342 ? 164.734 130.185 103.965 1.00 12.34 ?  321 TYR C CE1   1 
ATOM   13469 C  CE2   . TYR C 2 342 ? 165.160 132.273 102.879 1.00 13.11 ?  321 TYR C CE2   1 
ATOM   13470 C  CZ    . TYR C 2 342 ? 165.321 131.432 103.959 1.00 17.37 ?  321 TYR C CZ    1 
ATOM   13471 O  OH    . TYR C 2 342 ? 166.071 131.842 105.036 1.00 21.45 ?  321 TYR C OH    1 
ATOM   13472 N  N     . PHE C 2 343 ? 160.551 131.063 98.575  1.00 12.77 ?  322 PHE C N     1 
ATOM   13473 C  CA    . PHE C 2 343 ? 159.804 130.827 97.347  1.00 15.81 ?  322 PHE C CA    1 
ATOM   13474 C  C     . PHE C 2 343 ? 160.479 131.513 96.166  1.00 24.63 ?  322 PHE C C     1 
ATOM   13475 O  O     . PHE C 2 343 ? 161.303 132.410 96.341  1.00 24.06 ?  322 PHE C O     1 
ATOM   13476 C  CB    . PHE C 2 343 ? 158.350 131.311 97.473  1.00 11.49 ?  322 PHE C CB    1 
ATOM   13477 C  CG    . PHE C 2 343 ? 157.741 131.098 98.836  1.00 8.46  ?  322 PHE C CG    1 
ATOM   13478 C  CD1   . PHE C 2 343 ? 158.029 131.950 99.892  1.00 8.80  ?  322 PHE C CD1   1 
ATOM   13479 C  CD2   . PHE C 2 343 ? 156.896 130.027 99.062  1.00 13.46 ?  322 PHE C CD2   1 
ATOM   13480 C  CE1   . PHE C 2 343 ? 157.475 131.741 101.137 1.00 5.58  ?  322 PHE C CE1   1 
ATOM   13481 C  CE2   . PHE C 2 343 ? 156.341 129.815 100.306 1.00 8.14  ?  322 PHE C CE2   1 
ATOM   13482 C  CZ    . PHE C 2 343 ? 156.631 130.671 101.344 1.00 2.41  ?  322 PHE C CZ    1 
ATOM   13483 N  N     . ASP D 2 37  ? 123.857 102.219 142.693 1.00 32.44 ?  16  ASP D N     1 
ATOM   13484 C  CA    . ASP D 2 37  ? 123.584 103.638 142.448 1.00 32.83 ?  16  ASP D CA    1 
ATOM   13485 C  C     . ASP D 2 37  ? 124.276 104.199 141.206 1.00 31.65 ?  16  ASP D C     1 
ATOM   13486 O  O     . ASP D 2 37  ? 124.030 105.350 140.839 1.00 32.65 ?  16  ASP D O     1 
ATOM   13487 C  CB    . ASP D 2 37  ? 124.024 104.491 143.648 1.00 33.73 ?  16  ASP D CB    1 
ATOM   13488 C  CG    . ASP D 2 37  ? 123.225 104.208 144.911 1.00 36.81 ?  16  ASP D CG    1 
ATOM   13489 O  OD1   . ASP D 2 37  ? 123.724 104.567 146.004 1.00 39.69 ?  16  ASP D OD1   1 
ATOM   13490 O  OD2   . ASP D 2 37  ? 122.116 103.631 144.823 1.00 39.67 -1 16  ASP D OD2   1 
ATOM   13491 N  N     . PHE D 2 38  ? 125.136 103.411 140.564 1.00 29.55 ?  17  PHE D N     1 
ATOM   13492 C  CA    . PHE D 2 38  ? 126.067 103.990 139.596 1.00 27.75 ?  17  PHE D CA    1 
ATOM   13493 C  C     . PHE D 2 38  ? 126.317 103.210 138.295 1.00 26.21 ?  17  PHE D C     1 
ATOM   13494 O  O     . PHE D 2 38  ? 126.793 103.785 137.323 1.00 25.93 ?  17  PHE D O     1 
ATOM   13495 C  CB    . PHE D 2 38  ? 127.407 104.304 140.300 1.00 27.37 ?  17  PHE D CB    1 
ATOM   13496 C  CG    . PHE D 2 38  ? 128.070 103.094 140.905 1.00 27.32 ?  17  PHE D CG    1 
ATOM   13497 C  CD1   . PHE D 2 38  ? 128.876 102.267 140.129 1.00 27.01 ?  17  PHE D CD1   1 
ATOM   13498 C  CD2   . PHE D 2 38  ? 127.889 102.781 142.246 1.00 28.02 ?  17  PHE D CD2   1 
ATOM   13499 C  CE1   . PHE D 2 38  ? 129.486 101.142 140.681 1.00 27.66 ?  17  PHE D CE1   1 
ATOM   13500 C  CE2   . PHE D 2 38  ? 128.490 101.658 142.801 1.00 27.68 ?  17  PHE D CE2   1 
ATOM   13501 C  CZ    . PHE D 2 38  ? 129.291 100.836 142.014 1.00 27.47 ?  17  PHE D CZ    1 
ATOM   13502 N  N     . THR D 2 39  ? 126.005 101.918 138.275 1.00 24.88 ?  18  THR D N     1 
ATOM   13503 C  CA    . THR D 2 39  ? 126.377 101.059 137.138 1.00 23.81 ?  18  THR D CA    1 
ATOM   13504 C  C     . THR D 2 39  ? 125.709 101.443 135.805 1.00 23.56 ?  18  THR D C     1 
ATOM   13505 O  O     . THR D 2 39  ? 126.355 101.452 134.757 1.00 23.02 ?  18  THR D O     1 
ATOM   13506 C  CB    . THR D 2 39  ? 126.209 99.557  137.477 1.00 23.40 ?  18  THR D CB    1 
ATOM   13507 O  OG1   . THR D 2 39  ? 127.317 99.134  138.281 1.00 23.77 ?  18  THR D OG1   1 
ATOM   13508 C  CG2   . THR D 2 39  ? 126.181 98.698  136.223 1.00 22.31 ?  18  THR D CG2   1 
ATOM   13509 N  N     . GLN D 2 40  ? 124.426 101.778 135.837 1.00 23.78 ?  19  GLN D N     1 
ATOM   13510 C  CA    . GLN D 2 40  ? 123.759 102.187 134.598 1.00 23.88 ?  19  GLN D CA    1 
ATOM   13511 C  C     . GLN D 2 40  ? 124.323 103.498 134.043 1.00 24.09 ?  19  GLN D C     1 
ATOM   13512 O  O     . GLN D 2 40  ? 124.533 103.625 132.844 1.00 23.15 ?  19  GLN D O     1 
ATOM   13513 C  CB    . GLN D 2 40  ? 122.240 102.250 134.773 1.00 24.53 ?  19  GLN D CB    1 
ATOM   13514 C  CG    . GLN D 2 40  ? 121.633 100.871 134.981 1.00 24.06 ?  19  GLN D CG    1 
ATOM   13515 C  CD    . GLN D 2 40  ? 120.147 100.823 134.709 1.00 25.83 ?  19  GLN D CD    1 
ATOM   13516 O  OE1   . GLN D 2 40  ? 119.581 101.753 134.140 1.00 25.90 ?  19  GLN D OE1   1 
ATOM   13517 N  NE2   . GLN D 2 40  ? 119.508 99.719  135.098 1.00 23.56 ?  19  GLN D NE2   1 
ATOM   13518 N  N     . MET D 2 41  ? 124.613 104.449 134.921 1.00 24.07 ?  20  MET D N     1 
ATOM   13519 C  CA    . MET D 2 41  ? 125.285 105.681 134.505 1.00 25.53 ?  20  MET D CA    1 
ATOM   13520 C  C     . MET D 2 41  ? 126.653 105.415 133.844 1.00 24.24 ?  20  MET D C     1 
ATOM   13521 O  O     . MET D 2 41  ? 126.974 106.009 132.811 1.00 23.16 ?  20  MET D O     1 
ATOM   13522 C  CB    . MET D 2 41  ? 125.427 106.630 135.699 1.00 26.79 ?  20  MET D CB    1 
ATOM   13523 C  CG    . MET D 2 41  ? 126.137 107.935 135.397 1.00 32.62 ?  20  MET D CG    1 
ATOM   13524 S  SD    . MET D 2 41  ? 126.532 108.797 136.937 1.00 44.01 ?  20  MET D SD    1 
ATOM   13525 C  CE    . MET D 2 41  ? 127.931 109.799 136.425 1.00 41.93 ?  20  MET D CE    1 
ATOM   13526 N  N     . PHE D 2 42  ? 127.449 104.516 134.428 1.00 23.31 ?  21  PHE D N     1 
ATOM   13527 C  CA    . PHE D 2 42  ? 128.749 104.186 133.844 1.00 23.44 ?  21  PHE D CA    1 
ATOM   13528 C  C     . PHE D 2 42  ? 128.613 103.394 132.559 1.00 23.55 ?  21  PHE D C     1 
ATOM   13529 O  O     . PHE D 2 42  ? 129.418 103.555 131.648 1.00 23.74 ?  21  PHE D O     1 
ATOM   13530 C  CB    . PHE D 2 42  ? 129.652 103.461 134.845 1.00 22.97 ?  21  PHE D CB    1 
ATOM   13531 C  CG    . PHE D 2 42  ? 130.415 104.396 135.717 1.00 23.86 ?  21  PHE D CG    1 
ATOM   13532 C  CD1   . PHE D 2 42  ? 131.715 104.769 135.387 1.00 24.55 ?  21  PHE D CD1   1 
ATOM   13533 C  CD2   . PHE D 2 42  ? 129.826 104.941 136.842 1.00 24.06 ?  21  PHE D CD2   1 
ATOM   13534 C  CE1   . PHE D 2 42  ? 132.425 105.662 136.193 1.00 25.78 ?  21  PHE D CE1   1 
ATOM   13535 C  CE2   . PHE D 2 42  ? 130.529 105.836 137.654 1.00 25.25 ?  21  PHE D CE2   1 
ATOM   13536 C  CZ    . PHE D 2 42  ? 131.820 106.198 137.328 1.00 25.79 ?  21  PHE D CZ    1 
ATOM   13537 N  N     . TYR D 2 43  ? 127.581 102.556 132.490 1.00 24.08 ?  22  TYR D N     1 
ATOM   13538 C  CA    . TYR D 2 43  ? 127.257 101.854 131.259 1.00 24.74 ?  22  TYR D CA    1 
ATOM   13539 C  C     . TYR D 2 43  ? 127.098 102.866 130.122 1.00 25.72 ?  22  TYR D C     1 
ATOM   13540 O  O     . TYR D 2 43  ? 127.707 102.721 129.058 1.00 25.56 ?  22  TYR D O     1 
ATOM   13541 C  CB    . TYR D 2 43  ? 125.983 101.005 131.401 1.00 24.90 ?  22  TYR D CB    1 
ATOM   13542 C  CG    . TYR D 2 43  ? 125.549 100.408 130.069 1.00 24.38 ?  22  TYR D CG    1 
ATOM   13543 C  CD1   . TYR D 2 43  ? 126.024 99.170  129.655 1.00 23.96 ?  22  TYR D CD1   1 
ATOM   13544 C  CD2   . TYR D 2 43  ? 124.710 101.117 129.205 1.00 24.73 ?  22  TYR D CD2   1 
ATOM   13545 C  CE1   . TYR D 2 43  ? 125.657 98.636  128.418 1.00 23.42 ?  22  TYR D CE1   1 
ATOM   13546 C  CE2   . TYR D 2 43  ? 124.323 100.589 127.971 1.00 26.65 ?  22  TYR D CE2   1 
ATOM   13547 C  CZ    . TYR D 2 43  ? 124.806 99.350  127.587 1.00 25.68 ?  22  TYR D CZ    1 
ATOM   13548 O  OH    . TYR D 2 43  ? 124.431 98.827  126.371 1.00 26.57 ?  22  TYR D OH    1 
ATOM   13549 N  N     . ASN D 2 44  ? 126.271 103.881 130.364 1.00 26.77 ?  23  ASN D N     1 
ATOM   13550 C  CA    . ASN D 2 44  ? 125.996 104.917 129.375 1.00 28.57 ?  23  ASN D CA    1 
ATOM   13551 C  C     . ASN D 2 44  ? 127.252 105.638 128.924 1.00 28.70 ?  23  ASN D C     1 
ATOM   13552 O  O     . ASN D 2 44  ? 127.516 105.730 127.723 1.00 28.99 ?  23  ASN D O     1 
ATOM   13553 C  CB    . ASN D 2 44  ? 124.946 105.898 129.906 1.00 29.62 ?  23  ASN D CB    1 
ATOM   13554 C  CG    . ASN D 2 44  ? 123.564 105.265 130.007 1.00 32.44 ?  23  ASN D CG    1 
ATOM   13555 O  OD1   . ASN D 2 44  ? 123.272 104.266 129.335 1.00 34.30 ?  23  ASN D OD1   1 
ATOM   13556 N  ND2   . ASN D 2 44  ? 122.706 105.837 130.848 1.00 35.17 ?  23  ASN D ND2   1 
ATOM   13557 N  N     . GLN D 2 45  ? 128.043 106.103 129.888 1.00 28.97 ?  24  GLN D N     1 
ATOM   13558 C  CA    . GLN D 2 45  ? 129.273 106.825 129.584 1.00 29.99 ?  24  GLN D CA    1 
ATOM   13559 C  C     . GLN D 2 45  ? 130.288 105.958 128.825 1.00 29.69 ?  24  GLN D C     1 
ATOM   13560 O  O     . GLN D 2 45  ? 130.943 106.435 127.899 1.00 30.01 ?  24  GLN D O     1 
ATOM   13561 C  CB    . GLN D 2 45  ? 129.893 107.416 130.856 1.00 30.27 ?  24  GLN D CB    1 
ATOM   13562 C  CG    . GLN D 2 45  ? 131.065 108.387 130.586 1.00 32.29 ?  24  GLN D CG    1 
ATOM   13563 C  CD    . GLN D 2 45  ? 130.651 109.626 129.802 1.00 35.95 ?  24  GLN D CD    1 
ATOM   13564 O  OE1   . GLN D 2 45  ? 129.500 110.068 129.870 1.00 36.72 ?  24  GLN D OE1   1 
ATOM   13565 N  NE2   . GLN D 2 45  ? 131.592 110.193 129.054 1.00 37.05 ?  24  GLN D NE2   1 
ATOM   13566 N  N     . ASN D 2 46  ? 130.393 104.683 129.199 1.00 28.93 ?  25  ASN D N     1 
ATOM   13567 C  CA    . ASN D 2 46  ? 131.280 103.759 128.513 1.00 28.70 ?  25  ASN D CA    1 
ATOM   13568 C  C     . ASN D 2 46  ? 130.912 103.528 127.053 1.00 29.05 ?  25  ASN D C     1 
ATOM   13569 O  O     . ASN D 2 46  ? 131.764 103.668 126.171 1.00 28.51 ?  25  ASN D O     1 
ATOM   13570 C  CB    . ASN D 2 46  ? 131.375 102.420 129.257 1.00 28.36 ?  25  ASN D CB    1 
ATOM   13571 C  CG    . ASN D 2 46  ? 132.451 102.426 130.321 1.00 28.45 ?  25  ASN D CG    1 
ATOM   13572 O  OD1   . ASN D 2 46  ? 133.565 101.969 130.076 1.00 28.03 ?  25  ASN D OD1   1 
ATOM   13573 N  ND2   . ASN D 2 46  ? 132.137 102.970 131.495 1.00 26.53 ?  25  ASN D ND2   1 
ATOM   13574 N  N     . VAL D 2 47  ? 129.646 103.200 126.797 1.00 29.66 ?  26  VAL D N     1 
ATOM   13575 C  CA    . VAL D 2 47  ? 129.225 102.847 125.441 1.00 31.15 ?  26  VAL D CA    1 
ATOM   13576 C  C     . VAL D 2 47  ? 129.202 104.065 124.522 1.00 32.39 ?  26  VAL D C     1 
ATOM   13577 O  O     . VAL D 2 47  ? 129.441 103.943 123.322 1.00 32.80 ?  26  VAL D O     1 
ATOM   13578 C  CB    . VAL D 2 47  ? 127.876 102.055 125.383 1.00 31.08 ?  26  VAL D CB    1 
ATOM   13579 C  CG1   . VAL D 2 47  ? 127.949 100.799 126.243 1.00 31.09 ?  26  VAL D CG1   1 
ATOM   13580 C  CG2   . VAL D 2 47  ? 126.678 102.931 125.778 1.00 30.81 ?  26  VAL D CG2   1 
ATOM   13581 N  N     . LYS D 2 48  ? 128.949 105.244 125.078 1.00 33.28 ?  27  LYS D N     1 
ATOM   13582 C  CA    . LYS D 2 48  ? 128.965 106.435 124.244 1.00 34.87 ?  27  LYS D CA    1 
ATOM   13583 C  C     . LYS D 2 48  ? 130.387 106.921 123.897 1.00 34.91 ?  27  LYS D C     1 
ATOM   13584 O  O     . LYS D 2 48  ? 130.558 107.760 123.016 1.00 34.92 ?  27  LYS D O     1 
ATOM   13585 C  CB    . LYS D 2 48  ? 128.071 107.541 124.824 1.00 35.45 ?  27  LYS D CB    1 
ATOM   13586 C  CG    . LYS D 2 48  ? 128.702 108.443 125.859 1.00 37.41 ?  27  LYS D CG    1 
ATOM   13587 C  CD    . LYS D 2 48  ? 127.842 109.705 126.042 1.00 40.91 ?  27  LYS D CD    1 
ATOM   13588 C  CE    . LYS D 2 48  ? 128.625 110.807 126.761 1.00 42.46 ?  27  LYS D CE    1 
ATOM   13589 N  NZ    . LYS D 2 48  ? 127.883 112.101 126.822 1.00 45.13 1  27  LYS D NZ    1 
ATOM   13590 N  N     . GLN D 2 49  ? 131.392 106.369 124.581 1.00 34.66 ?  28  GLN D N     1 
ATOM   13591 C  CA    . GLN D 2 49  ? 132.798 106.658 124.311 1.00 34.64 ?  28  GLN D CA    1 
ATOM   13592 C  C     . GLN D 2 49  ? 133.407 105.647 123.341 1.00 34.20 ?  28  GLN D C     1 
ATOM   13593 O  O     . GLN D 2 49  ? 134.620 105.657 123.128 1.00 34.53 ?  28  GLN D O     1 
ATOM   13594 C  CB    . GLN D 2 49  ? 133.618 106.661 125.616 1.00 34.89 ?  28  GLN D CB    1 
ATOM   13595 C  CG    . GLN D 2 49  ? 133.656 107.999 126.352 1.00 36.47 ?  28  GLN D CG    1 
ATOM   13596 C  CD    . GLN D 2 49  ? 134.309 107.917 127.734 1.00 38.37 ?  28  GLN D CD    1 
ATOM   13597 O  OE1   . GLN D 2 49  ? 133.937 108.659 128.643 1.00 40.68 ?  28  GLN D OE1   1 
ATOM   13598 N  NE2   . GLN D 2 49  ? 135.280 107.018 127.897 1.00 38.57 ?  28  GLN D NE2   1 
ATOM   13599 N  N     . PHE D 2 50  ? 132.583 104.774 122.760 1.00 33.42 ?  29  PHE D N     1 
ATOM   13600 C  CA    . PHE D 2 50  ? 133.099 103.721 121.887 1.00 32.57 ?  29  PHE D CA    1 
ATOM   13601 C  C     . PHE D 2 50  ? 133.794 104.332 120.669 1.00 32.60 ?  29  PHE D C     1 
ATOM   13602 O  O     . PHE D 2 50  ? 133.316 105.314 120.093 1.00 32.39 ?  29  PHE D O     1 
ATOM   13603 C  CB    . PHE D 2 50  ? 131.998 102.737 121.460 1.00 32.77 ?  29  PHE D CB    1 
ATOM   13604 C  CG    . PHE D 2 50  ? 132.492 101.606 120.579 1.00 32.24 ?  29  PHE D CG    1 
ATOM   13605 C  CD1   . PHE D 2 50  ? 133.212 100.544 121.118 1.00 31.50 ?  29  PHE D CD1   1 
ATOM   13606 C  CD2   . PHE D 2 50  ? 132.238 101.610 119.213 1.00 33.60 ?  29  PHE D CD2   1 
ATOM   13607 C  CE1   . PHE D 2 50  ? 133.669 99.510  120.318 1.00 33.02 ?  29  PHE D CE1   1 
ATOM   13608 C  CE2   . PHE D 2 50  ? 132.695 100.576 118.393 1.00 33.78 ?  29  PHE D CE2   1 
ATOM   13609 C  CZ    . PHE D 2 50  ? 133.405 99.522  118.946 1.00 33.13 ?  29  PHE D CZ    1 
ATOM   13610 N  N     . TRP D 2 51  ? 134.927 103.748 120.299 1.00 31.95 ?  30  TRP D N     1 
ATOM   13611 C  CA    . TRP D 2 51  ? 135.719 104.217 119.161 1.00 32.03 ?  30  TRP D CA    1 
ATOM   13612 C  C     . TRP D 2 51  ? 136.525 103.055 118.596 1.00 33.03 ?  30  TRP D C     1 
ATOM   13613 O  O     . TRP D 2 51  ? 136.620 101.994 119.217 1.00 32.54 ?  30  TRP D O     1 
ATOM   13614 C  CB    . TRP D 2 51  ? 136.634 105.384 119.562 1.00 31.19 ?  30  TRP D CB    1 
ATOM   13615 C  CG    . TRP D 2 51  ? 137.646 105.036 120.635 1.00 28.11 ?  30  TRP D CG    1 
ATOM   13616 C  CD1   . TRP D 2 51  ? 137.417 104.946 121.973 1.00 26.51 ?  30  TRP D CD1   1 
ATOM   13617 C  CD2   . TRP D 2 51  ? 139.036 104.727 120.444 1.00 25.93 ?  30  TRP D CD2   1 
ATOM   13618 N  NE1   . TRP D 2 51  ? 138.579 104.606 122.634 1.00 24.52 ?  30  TRP D NE1   1 
ATOM   13619 C  CE2   . TRP D 2 51  ? 139.586 104.463 121.720 1.00 24.42 ?  30  TRP D CE2   1 
ATOM   13620 C  CE3   . TRP D 2 51  ? 139.872 104.655 119.320 1.00 25.37 ?  30  TRP D CE3   1 
ATOM   13621 C  CZ2   . TRP D 2 51  ? 140.936 104.135 121.906 1.00 24.00 ?  30  TRP D CZ2   1 
ATOM   13622 C  CZ3   . TRP D 2 51  ? 141.214 104.320 119.504 1.00 24.99 ?  30  TRP D CZ3   1 
ATOM   13623 C  CH2   . TRP D 2 51  ? 141.730 104.064 120.787 1.00 23.72 ?  30  TRP D CH2   1 
ATOM   13624 N  N     . LEU D 2 52  ? 137.084 103.262 117.408 1.00 34.81 ?  31  LEU D N     1 
ATOM   13625 C  CA    . LEU D 2 52  ? 137.868 102.249 116.717 1.00 36.58 ?  31  LEU D CA    1 
ATOM   13626 C  C     . LEU D 2 52  ? 139.168 102.859 116.199 1.00 37.80 ?  31  LEU D C     1 
ATOM   13627 O  O     . LEU D 2 52  ? 139.192 104.031 115.835 1.00 37.92 ?  31  LEU D O     1 
ATOM   13628 C  CB    . LEU D 2 52  ? 137.059 101.638 115.562 1.00 36.95 ?  31  LEU D CB    1 
ATOM   13629 C  CG    . LEU D 2 52  ? 136.030 100.545 115.871 1.00 38.15 ?  31  LEU D CG    1 
ATOM   13630 C  CD1   . LEU D 2 52  ? 135.606 99.844  114.586 1.00 39.50 ?  31  LEU D CD1   1 
ATOM   13631 C  CD2   . LEU D 2 52  ? 136.568 99.517  116.860 1.00 37.94 ?  31  LEU D CD2   1 
ATOM   13632 N  N     . PRO D 2 53  ? 140.256 102.063 116.158 1.00 39.26 ?  32  PRO D N     1 
ATOM   13633 C  CA    . PRO D 2 53  ? 141.571 102.544 115.696 1.00 40.41 ?  32  PRO D CA    1 
ATOM   13634 C  C     . PRO D 2 53  ? 141.539 103.181 114.300 1.00 41.91 ?  32  PRO D C     1 
ATOM   13635 O  O     . PRO D 2 53  ? 142.128 104.247 114.090 1.00 42.52 ?  32  PRO D O     1 
ATOM   13636 C  CB    . PRO D 2 53  ? 142.417 101.266 115.658 1.00 40.42 ?  32  PRO D CB    1 
ATOM   13637 C  CG    . PRO D 2 53  ? 141.732 100.319 116.558 1.00 40.01 ?  32  PRO D CG    1 
ATOM   13638 C  CD    . PRO D 2 53  ? 140.278 100.626 116.483 1.00 39.30 ?  32  PRO D CD    1 
ATOM   13639 N  N     . GLU D 2 54  ? 140.837 102.539 113.370 1.00 43.27 ?  33  GLU D N     1 
ATOM   13640 C  CA    . GLU D 2 54  ? 140.731 102.981 111.970 1.00 45.17 ?  33  GLU D CA    1 
ATOM   13641 C  C     . GLU D 2 54  ? 140.271 104.435 111.773 1.00 45.57 ?  33  GLU D C     1 
ATOM   13642 O  O     . GLU D 2 54  ? 140.517 105.029 110.718 1.00 46.08 ?  33  GLU D O     1 
ATOM   13643 C  CB    . GLU D 2 54  ? 139.796 102.040 111.195 1.00 45.55 ?  33  GLU D CB    1 
ATOM   13644 C  CG    . GLU D 2 54  ? 140.446 100.742 110.711 1.00 48.19 ?  33  GLU D CG    1 
ATOM   13645 C  CD    . GLU D 2 54  ? 140.921 99.837  111.840 1.00 50.61 ?  33  GLU D CD    1 
ATOM   13646 O  OE1   . GLU D 2 54  ? 140.142 99.601  112.794 1.00 51.10 ?  33  GLU D OE1   1 
ATOM   13647 O  OE2   . GLU D 2 54  ? 142.081 99.365  111.769 1.00 52.64 -1 33  GLU D OE2   1 
ATOM   13648 N  N     . GLU D 2 55  ? 139.609 104.998 112.784 1.00 45.74 ?  34  GLU D N     1 
ATOM   13649 C  CA    . GLU D 2 55  ? 139.061 106.357 112.708 1.00 46.28 ?  34  GLU D CA    1 
ATOM   13650 C  C     . GLU D 2 55  ? 140.141 107.443 112.611 1.00 46.49 ?  34  GLU D C     1 
ATOM   13651 O  O     . GLU D 2 55  ? 139.916 108.499 112.012 1.00 46.73 ?  34  GLU D O     1 
ATOM   13652 C  CB    . GLU D 2 55  ? 138.135 106.640 113.895 1.00 46.17 ?  34  GLU D CB    1 
ATOM   13653 C  CG    . GLU D 2 55  ? 136.883 105.760 113.960 1.00 47.10 ?  34  GLU D CG    1 
ATOM   13654 C  CD    . GLU D 2 55  ? 135.974 106.129 115.130 1.00 48.43 ?  34  GLU D CD    1 
ATOM   13655 O  OE1   . GLU D 2 55  ? 135.451 107.265 115.149 1.00 49.62 ?  34  GLU D OE1   1 
ATOM   13656 O  OE2   . GLU D 2 55  ? 135.778 105.284 116.029 1.00 47.11 -1 34  GLU D OE2   1 
ATOM   13657 N  N     . ILE D 2 56  ? 141.305 107.181 113.206 1.00 46.23 ?  35  ILE D N     1 
ATOM   13658 C  CA    . ILE D 2 56  ? 142.426 108.115 113.159 1.00 46.25 ?  35  ILE D CA    1 
ATOM   13659 C  C     . ILE D 2 56  ? 143.455 107.625 112.141 1.00 46.30 ?  35  ILE D C     1 
ATOM   13660 O  O     . ILE D 2 56  ? 143.990 106.520 112.273 1.00 46.36 ?  35  ILE D O     1 
ATOM   13661 C  CB    . ILE D 2 56  ? 143.112 108.283 114.560 1.00 45.84 ?  35  ILE D CB    1 
ATOM   13662 C  CG1   . ILE D 2 56  ? 142.084 108.382 115.706 1.00 46.15 ?  35  ILE D CG1   1 
ATOM   13663 C  CG2   . ILE D 2 56  ? 144.109 109.460 114.557 1.00 45.72 ?  35  ILE D CG2   1 
ATOM   13664 C  CD1   . ILE D 2 56  ? 141.147 109.583 115.661 1.00 47.27 ?  35  ILE D CD1   1 
ATOM   13665 N  N     . ALA D 2 57  ? 143.720 108.437 111.122 1.00 46.51 ?  36  ALA D N     1 
ATOM   13666 C  CA    . ALA D 2 57  ? 144.777 108.140 110.152 1.00 46.56 ?  36  ALA D CA    1 
ATOM   13667 C  C     . ALA D 2 57  ? 146.139 108.450 110.780 1.00 46.08 ?  36  ALA D C     1 
ATOM   13668 O  O     . ALA D 2 57  ? 146.357 109.561 111.262 1.00 45.70 ?  36  ALA D O     1 
ATOM   13669 C  CB    . ALA D 2 57  ? 144.576 108.945 108.872 1.00 47.10 ?  36  ALA D CB    1 
ATOM   13670 N  N     . LEU D 2 58  ? 147.047 107.476 110.760 1.00 45.66 ?  37  LEU D N     1 
ATOM   13671 C  CA    . LEU D 2 58  ? 148.329 107.609 111.470 1.00 45.27 ?  37  LEU D CA    1 
ATOM   13672 C  C     . LEU D 2 58  ? 149.519 108.095 110.645 1.00 45.25 ?  37  LEU D C     1 
ATOM   13673 O  O     . LEU D 2 58  ? 150.498 108.600 111.206 1.00 44.82 ?  37  LEU D O     1 
ATOM   13674 C  CB    . LEU D 2 58  ? 148.694 106.296 112.161 1.00 45.05 ?  37  LEU D CB    1 
ATOM   13675 C  CG    . LEU D 2 58  ? 147.953 106.037 113.472 1.00 45.41 ?  37  LEU D CG    1 
ATOM   13676 C  CD1   . LEU D 2 58  ? 148.345 104.681 114.026 1.00 45.40 ?  37  LEU D CD1   1 
ATOM   13677 C  CD2   . LEU D 2 58  ? 148.238 107.142 114.487 1.00 44.70 ?  37  LEU D CD2   1 
ATOM   13678 N  N     . ASN D 2 59  ? 149.435 107.960 109.324 1.00 45.33 ?  38  ASN D N     1 
ATOM   13679 C  CA    . ASN D 2 59  ? 150.600 108.174 108.461 1.00 45.22 ?  38  ASN D CA    1 
ATOM   13680 C  C     . ASN D 2 59  ? 151.243 109.566 108.543 1.00 44.39 ?  38  ASN D C     1 
ATOM   13681 O  O     . ASN D 2 59  ? 152.464 109.693 108.401 1.00 44.33 ?  38  ASN D O     1 
ATOM   13682 C  CB    . ASN D 2 59  ? 150.264 107.816 107.015 1.00 46.22 ?  38  ASN D CB    1 
ATOM   13683 C  CG    . ASN D 2 59  ? 151.439 107.191 106.284 1.00 47.90 ?  38  ASN D CG    1 
ATOM   13684 O  OD1   . ASN D 2 59  ? 151.933 107.738 105.299 1.00 49.28 ?  38  ASN D OD1   1 
ATOM   13685 N  ND2   . ASN D 2 59  ? 151.893 106.033 106.766 1.00 49.18 ?  38  ASN D ND2   1 
ATOM   13686 N  N     . GLY D 2 60  ? 150.427 110.591 108.796 1.00 43.45 ?  39  GLY D N     1 
ATOM   13687 C  CA    . GLY D 2 60  ? 150.903 111.973 108.918 1.00 42.42 ?  39  GLY D CA    1 
ATOM   13688 C  C     . GLY D 2 60  ? 151.813 112.265 110.108 1.00 41.55 ?  39  GLY D C     1 
ATOM   13689 O  O     . GLY D 2 60  ? 152.376 113.360 110.214 1.00 41.29 ?  39  GLY D O     1 
ATOM   13690 N  N     . ASP D 2 61  ? 151.956 111.297 111.011 1.00 40.35 ?  40  ASP D N     1 
ATOM   13691 C  CA    . ASP D 2 61  ? 152.896 111.422 112.131 1.00 39.53 ?  40  ASP D CA    1 
ATOM   13692 C  C     . ASP D 2 61  ? 154.354 111.333 111.701 1.00 39.38 ?  40  ASP D C     1 
ATOM   13693 O  O     . ASP D 2 61  ? 155.240 111.834 112.390 1.00 38.90 ?  40  ASP D O     1 
ATOM   13694 C  CB    . ASP D 2 61  ? 152.620 110.356 113.181 1.00 38.93 ?  40  ASP D CB    1 
ATOM   13695 C  CG    . ASP D 2 61  ? 151.556 110.769 114.157 1.00 38.21 ?  40  ASP D CG    1 
ATOM   13696 O  OD1   . ASP D 2 61  ? 151.030 111.899 114.048 1.00 38.79 ?  40  ASP D OD1   1 
ATOM   13697 O  OD2   . ASP D 2 61  ? 151.251 109.959 115.047 1.00 38.02 -1 40  ASP D OD2   1 
ATOM   13698 N  N     . LEU D 2 62  ? 154.592 110.692 110.562 1.00 39.82 ?  41  LEU D N     1 
ATOM   13699 C  CA    . LEU D 2 62  ? 155.940 110.516 110.035 1.00 40.22 ?  41  LEU D CA    1 
ATOM   13700 C  C     . LEU D 2 62  ? 156.593 111.855 109.692 1.00 40.40 ?  41  LEU D C     1 
ATOM   13701 O  O     . LEU D 2 62  ? 157.819 111.947 109.614 1.00 40.91 ?  41  LEU D O     1 
ATOM   13702 C  CB    . LEU D 2 62  ? 155.914 109.583 108.821 1.00 40.52 ?  41  LEU D CB    1 
ATOM   13703 C  CG    . LEU D 2 62  ? 155.501 108.132 109.094 1.00 41.03 ?  41  LEU D CG    1 
ATOM   13704 C  CD1   . LEU D 2 62  ? 155.422 107.343 107.795 1.00 42.53 ?  41  LEU D CD1   1 
ATOM   13705 C  CD2   . LEU D 2 62  ? 156.450 107.455 110.093 1.00 41.89 ?  41  LEU D CD2   1 
ATOM   13706 N  N     . LEU D 2 63  ? 155.744 112.806 109.489 1.00 40.20 ?  42  LEU D N     1 
ATOM   13707 C  CA    . LEU D 2 63  ? 156.306 114.107 109.166 1.00 39.85 ?  42  LEU D CA    1 
ATOM   13708 C  C     . LEU D 2 63  ? 157.075 114.571 110.412 1.00 38.90 ?  42  LEU D C     1 
ATOM   13709 O  O     . LEU D 2 63  ? 158.266 114.909 110.249 1.00 39.48 ?  42  LEU D O     1 
ATOM   13710 C  CB    . LEU D 2 63  ? 155.010 114.807 108.806 1.00 40.50 ?  42  LEU D CB    1 
ATOM   13711 C  CG    . LEU D 2 63  ? 154.229 114.051 107.724 1.00 41.98 ?  42  LEU D CG    1 
ATOM   13712 C  CD1   . LEU D 2 63  ? 152.881 114.682 107.409 1.00 43.07 ?  42  LEU D CD1   1 
ATOM   13713 C  CD2   . LEU D 2 63  ? 155.055 113.891 106.456 1.00 43.17 ?  42  LEU D CD2   1 
ATOM   13714 N  N     . THR D 2 64  ? 156.481 114.505 111.614 1.00 37.28 ?  43  THR D N     1 
ATOM   13715 C  CA    . THR D 2 64  ? 157.104 115.022 112.871 1.00 35.53 ?  43  THR D CA    1 
ATOM   13716 C  C     . THR D 2 64  ? 158.142 114.050 113.401 1.00 34.57 ?  43  THR D C     1 
ATOM   13717 O  O     . THR D 2 64  ? 159.205 114.496 113.872 1.00 34.23 ?  43  THR D O     1 
ATOM   13718 C  CB    . THR D 2 64  ? 156.049 115.166 113.974 1.00 35.18 ?  43  THR D CB    1 
ATOM   13719 O  OG1   . THR D 2 64  ? 155.248 113.986 113.950 1.00 34.59 ?  43  THR D OG1   1 
ATOM   13720 C  CG2   . THR D 2 64  ? 155.146 116.369 113.813 1.00 35.48 ?  43  THR D CG2   1 
ATOM   13721 N  N     . TRP D 2 65  ? 157.820 112.779 113.315 1.00 33.62 ?  44  TRP D N     1 
ATOM   13722 C  CA    . TRP D 2 65  ? 158.653 111.690 113.850 1.00 32.87 ?  44  TRP D CA    1 
ATOM   13723 C  C     . TRP D 2 65  ? 160.096 111.769 113.334 1.00 33.46 ?  44  TRP D C     1 
ATOM   13724 O  O     . TRP D 2 65  ? 161.046 111.608 114.101 1.00 32.58 ?  44  TRP D O     1 
ATOM   13725 C  CB    . TRP D 2 65  ? 158.028 110.333 113.494 1.00 32.09 ?  44  TRP D CB    1 
ATOM   13726 C  CG    . TRP D 2 65  ? 158.823 109.134 113.930 1.00 30.42 ?  44  TRP D CG    1 
ATOM   13727 C  CD1   . TRP D 2 65  ? 159.555 108.303 113.127 1.00 29.35 ?  44  TRP D CD1   1 
ATOM   13728 C  CD2   . TRP D 2 65  ? 158.963 108.626 115.266 1.00 28.04 ?  44  TRP D CD2   1 
ATOM   13729 N  NE1   . TRP D 2 65  ? 160.140 107.311 113.878 1.00 28.44 ?  44  TRP D NE1   1 
ATOM   13730 C  CE2   . TRP D 2 65  ? 159.797 107.488 115.194 1.00 28.14 ?  44  TRP D CE2   1 
ATOM   13731 C  CE3   . TRP D 2 65  ? 158.473 109.027 116.516 1.00 27.11 ?  44  TRP D CE3   1 
ATOM   13732 C  CZ2   . TRP D 2 65  ? 160.147 106.736 116.324 1.00 27.21 ?  44  TRP D CZ2   1 
ATOM   13733 C  CZ3   . TRP D 2 65  ? 158.815 108.273 117.643 1.00 27.45 ?  44  TRP D CZ3   1 
ATOM   13734 C  CH2   . TRP D 2 65  ? 159.641 107.137 117.533 1.00 27.25 ?  44  TRP D CH2   1 
ATOM   13735 N  N     . LYS D 2 66  ? 160.235 112.022 112.033 1.00 34.52 ?  45  LYS D N     1 
ATOM   13736 C  CA    . LYS D 2 66  ? 161.534 112.151 111.380 1.00 36.41 ?  45  LYS D CA    1 
ATOM   13737 C  C     . LYS D 2 66  ? 162.400 113.280 111.936 1.00 36.26 ?  45  LYS D C     1 
ATOM   13738 O  O     . LYS D 2 66  ? 163.619 113.258 111.770 1.00 36.52 ?  45  LYS D O     1 
ATOM   13739 C  CB    . LYS D 2 66  ? 161.361 112.322 109.865 1.00 36.98 ?  45  LYS D CB    1 
ATOM   13740 C  CG    . LYS D 2 66  ? 161.630 111.051 109.062 1.00 40.03 ?  45  LYS D CG    1 
ATOM   13741 C  CD    . LYS D 2 66  ? 160.546 109.986 109.264 1.00 43.70 ?  45  LYS D CD    1 
ATOM   13742 C  CE    . LYS D 2 66  ? 160.813 108.748 108.403 1.00 45.57 ?  45  LYS D CE    1 
ATOM   13743 N  NZ    . LYS D 2 66  ? 160.804 109.045 106.940 1.00 46.59 1  45  LYS D NZ    1 
ATOM   13744 N  N     . TYR D 2 67  ? 161.774 114.246 112.603 1.00 36.26 ?  46  TYR D N     1 
ATOM   13745 C  CA    . TYR D 2 67  ? 162.512 115.387 113.154 1.00 36.90 ?  46  TYR D CA    1 
ATOM   13746 C  C     . TYR D 2 67  ? 162.912 115.249 114.625 1.00 36.28 ?  46  TYR D C     1 
ATOM   13747 O  O     . TYR D 2 67  ? 163.555 116.142 115.169 1.00 36.44 ?  46  TYR D O     1 
ATOM   13748 C  CB    . TYR D 2 67  ? 161.761 116.702 112.920 1.00 37.15 ?  46  TYR D CB    1 
ATOM   13749 C  CG    . TYR D 2 67  ? 161.466 116.979 111.464 1.00 39.40 ?  46  TYR D CG    1 
ATOM   13750 C  CD1   . TYR D 2 67  ? 162.435 116.761 110.481 1.00 41.26 ?  46  TYR D CD1   1 
ATOM   13751 C  CD2   . TYR D 2 67  ? 160.230 117.483 111.071 1.00 41.06 ?  46  TYR D CD2   1 
ATOM   13752 C  CE1   . TYR D 2 67  ? 162.168 117.012 109.136 1.00 43.03 ?  46  TYR D CE1   1 
ATOM   13753 C  CE2   . TYR D 2 67  ? 159.954 117.746 109.727 1.00 43.05 ?  46  TYR D CE2   1 
ATOM   13754 C  CZ    . TYR D 2 67  ? 160.924 117.510 108.766 1.00 43.80 ?  46  TYR D CZ    1 
ATOM   13755 O  OH    . TYR D 2 67  ? 160.647 117.767 107.436 1.00 45.18 ?  46  TYR D OH    1 
ATOM   13756 N  N     . LEU D 2 68  ? 162.531 114.147 115.269 1.00 35.71 ?  47  LEU D N     1 
ATOM   13757 C  CA    . LEU D 2 68  ? 162.942 113.909 116.654 1.00 34.92 ?  47  LEU D CA    1 
ATOM   13758 C  C     . LEU D 2 68  ? 164.354 113.318 116.707 1.00 34.32 ?  47  LEU D C     1 
ATOM   13759 O  O     . LEU D 2 68  ? 164.761 112.576 115.809 1.00 34.50 ?  47  LEU D O     1 
ATOM   13760 C  CB    . LEU D 2 68  ? 161.951 112.991 117.385 1.00 35.00 ?  47  LEU D CB    1 
ATOM   13761 C  CG    . LEU D 2 68  ? 160.450 113.330 117.371 1.00 35.82 ?  47  LEU D CG    1 
ATOM   13762 C  CD1   . LEU D 2 68  ? 159.673 112.286 118.159 1.00 35.95 ?  47  LEU D CD1   1 
ATOM   13763 C  CD2   . LEU D 2 68  ? 160.151 114.731 117.903 1.00 35.97 ?  47  LEU D CD2   1 
ATOM   13764 N  N     . GLY D 2 69  ? 165.092 113.653 117.764 1.00 33.50 ?  48  GLY D N     1 
ATOM   13765 C  CA    . GLY D 2 69  ? 166.389 113.040 118.040 1.00 32.41 ?  48  GLY D CA    1 
ATOM   13766 C  C     . GLY D 2 69  ? 166.275 111.565 118.401 1.00 32.15 ?  48  GLY D C     1 
ATOM   13767 O  O     . GLY D 2 69  ? 165.180 111.060 118.678 1.00 30.98 ?  48  GLY D O     1 
ATOM   13768 N  N     . LYS D 2 70  ? 167.415 110.878 118.406 1.00 32.14 ?  49  LYS D N     1 
ATOM   13769 C  CA    . LYS D 2 70  ? 167.465 109.459 118.744 1.00 32.25 ?  49  LYS D CA    1 
ATOM   13770 C  C     . LYS D 2 70  ? 166.951 109.172 120.153 1.00 31.24 ?  49  LYS D C     1 
ATOM   13771 O  O     . LYS D 2 70  ? 166.213 108.208 120.341 1.00 31.34 ?  49  LYS D O     1 
ATOM   13772 C  CB    . LYS D 2 70  ? 168.881 108.904 118.575 1.00 33.07 ?  49  LYS D CB    1 
ATOM   13773 C  CG    . LYS D 2 70  ? 169.407 108.978 117.150 1.00 35.74 ?  49  LYS D CG    1 
ATOM   13774 C  CD    . LYS D 2 70  ? 170.904 108.683 117.122 1.00 39.67 ?  49  LYS D CD    1 
ATOM   13775 C  CE    . LYS D 2 70  ? 171.520 109.063 115.785 1.00 40.96 ?  49  LYS D CE    1 
ATOM   13776 N  NZ    . LYS D 2 70  ? 173.000 109.051 115.885 1.00 42.55 1  49  LYS D NZ    1 
ATOM   13777 N  N     . ASN D 2 71  ? 167.328 110.007 121.127 1.00 29.92 ?  50  ASN D N     1 
ATOM   13778 C  CA    . ASN D 2 71  ? 166.874 109.833 122.511 1.00 29.37 ?  50  ASN D CA    1 
ATOM   13779 C  C     . ASN D 2 71  ? 165.362 109.995 122.639 1.00 28.35 ?  50  ASN D C     1 
ATOM   13780 O  O     . ASN D 2 71  ? 164.719 109.242 123.380 1.00 27.64 ?  50  ASN D O     1 
ATOM   13781 C  CB    . ASN D 2 71  ? 167.587 110.784 123.491 1.00 29.38 ?  50  ASN D CB    1 
ATOM   13782 C  CG    . ASN D 2 71  ? 169.017 110.351 123.811 1.00 31.22 ?  50  ASN D CG    1 
ATOM   13783 O  OD1   . ASN D 2 71  ? 169.343 109.162 123.814 1.00 33.03 ?  50  ASN D OD1   1 
ATOM   13784 N  ND2   . ASN D 2 71  ? 169.875 111.324 124.096 1.00 31.97 ?  50  ASN D ND2   1 
ATOM   13785 N  N     . GLU D 2 72  ? 164.805 110.965 121.908 1.00 27.72 ?  51  GLU D N     1 
ATOM   13786 C  CA    . GLU D 2 72  ? 163.350 111.185 121.901 1.00 27.70 ?  51  GLU D CA    1 
ATOM   13787 C  C     . GLU D 2 72  ? 162.604 109.994 121.293 1.00 27.62 ?  51  GLU D C     1 
ATOM   13788 O  O     . GLU D 2 72  ? 161.572 109.562 121.815 1.00 27.56 ?  51  GLU D O     1 
ATOM   13789 C  CB    . GLU D 2 72  ? 162.981 112.463 121.141 1.00 27.55 ?  51  GLU D CB    1 
ATOM   13790 C  CG    . GLU D 2 72  ? 163.597 113.752 121.701 1.00 28.77 ?  51  GLU D CG    1 
ATOM   13791 C  CD    . GLU D 2 72  ? 163.084 114.980 120.971 1.00 31.18 ?  51  GLU D CD    1 
ATOM   13792 O  OE1   . GLU D 2 72  ? 163.476 115.188 119.803 1.00 33.17 ?  51  GLU D OE1   1 
ATOM   13793 O  OE2   . GLU D 2 72  ? 162.281 115.730 121.561 1.00 31.66 -1 51  GLU D OE2   1 
ATOM   13794 N  N     . GLN D 2 73  ? 163.135 109.471 120.192 1.00 27.32 ?  52  GLN D N     1 
ATOM   13795 C  CA    . GLN D 2 73  ? 162.531 108.329 119.513 1.00 27.33 ?  52  GLN D CA    1 
ATOM   13796 C  C     . GLN D 2 73  ? 162.636 107.077 120.388 1.00 26.85 ?  52  GLN D C     1 
ATOM   13797 O  O     . GLN D 2 73  ? 161.678 106.306 120.498 1.00 26.24 ?  52  GLN D O     1 
ATOM   13798 C  CB    . GLN D 2 73  ? 163.180 108.102 118.153 1.00 27.65 ?  52  GLN D CB    1 
ATOM   13799 C  CG    . GLN D 2 73  ? 162.798 109.134 117.075 1.00 29.66 ?  52  GLN D CG    1 
ATOM   13800 C  CD    . GLN D 2 73  ? 163.312 108.764 115.684 1.00 32.60 ?  52  GLN D CD    1 
ATOM   13801 O  OE1   . GLN D 2 73  ? 164.244 107.977 115.542 1.00 34.76 ?  52  GLN D OE1   1 
ATOM   13802 N  NE2   . GLN D 2 73  ? 162.713 109.347 114.656 1.00 33.42 ?  52  GLN D NE2   1 
ATOM   13803 N  N     . ASP D 2 74  ? 163.790 106.913 121.032 1.00 26.26 ?  53  ASP D N     1 
ATOM   13804 C  CA    . ASP D 2 74  ? 164.053 105.797 121.948 1.00 26.50 ?  53  ASP D CA    1 
ATOM   13805 C  C     . ASP D 2 74  ? 163.114 105.830 123.145 1.00 25.81 ?  53  ASP D C     1 
ATOM   13806 O  O     . ASP D 2 74  ? 162.514 104.816 123.491 1.00 26.12 ?  53  ASP D O     1 
ATOM   13807 C  CB    . ASP D 2 74  ? 165.510 105.851 122.429 1.00 26.84 ?  53  ASP D CB    1 
ATOM   13808 C  CG    . ASP D 2 74  ? 165.915 104.641 123.270 1.00 29.50 ?  53  ASP D CG    1 
ATOM   13809 O  OD1   . ASP D 2 74  ? 165.922 103.505 122.750 1.00 32.08 ?  53  ASP D OD1   1 
ATOM   13810 O  OD2   . ASP D 2 74  ? 166.276 104.836 124.448 1.00 33.52 -1 53  ASP D OD2   1 
ATOM   13811 N  N     . THR D 2 75  ? 162.982 106.995 123.779 1.00 25.10 ?  54  THR D N     1 
ATOM   13812 C  CA    . THR D 2 75  ? 162.094 107.126 124.938 1.00 24.11 ?  54  THR D CA    1 
ATOM   13813 C  C     . THR D 2 75  ? 160.646 106.826 124.539 1.00 23.82 ?  54  THR D C     1 
ATOM   13814 O  O     . THR D 2 75  ? 159.960 106.056 125.211 1.00 23.81 ?  54  THR D O     1 
ATOM   13815 C  CB    . THR D 2 75  ? 162.216 108.513 125.600 1.00 23.80 ?  54  THR D CB    1 
ATOM   13816 O  OG1   . THR D 2 75  ? 163.550 108.674 126.101 1.00 24.62 ?  54  THR D OG1   1 
ATOM   13817 C  CG2   . THR D 2 75  ? 161.220 108.656 126.764 1.00 23.25 ?  54  THR D CG2   1 
ATOM   13818 N  N     . TYR D 2 76  ? 160.192 107.446 123.458 1.00 24.06 ?  55  TYR D N     1 
ATOM   13819 C  CA    . TYR D 2 76  ? 158.845 107.210 122.945 1.00 24.76 ?  55  TYR D CA    1 
ATOM   13820 C  C     . TYR D 2 76  ? 158.553 105.722 122.704 1.00 24.85 ?  55  TYR D C     1 
ATOM   13821 O  O     . TYR D 2 76  ? 157.521 105.213 123.150 1.00 24.83 ?  55  TYR D O     1 
ATOM   13822 C  CB    . TYR D 2 76  ? 158.603 108.004 121.661 1.00 24.78 ?  55  TYR D CB    1 
ATOM   13823 C  CG    . TYR D 2 76  ? 157.133 108.205 121.357 1.00 26.19 ?  55  TYR D CG    1 
ATOM   13824 C  CD1   . TYR D 2 76  ? 156.461 109.331 121.834 1.00 27.81 ?  55  TYR D CD1   1 
ATOM   13825 C  CD2   . TYR D 2 76  ? 156.409 107.270 120.610 1.00 28.03 ?  55  TYR D CD2   1 
ATOM   13826 C  CE1   . TYR D 2 76  ? 155.113 109.534 121.567 1.00 29.32 ?  55  TYR D CE1   1 
ATOM   13827 C  CE2   . TYR D 2 76  ? 155.047 107.463 120.337 1.00 29.01 ?  55  TYR D CE2   1 
ATOM   13828 C  CZ    . TYR D 2 76  ? 154.413 108.601 120.823 1.00 30.76 ?  55  TYR D CZ    1 
ATOM   13829 O  OH    . TYR D 2 76  ? 153.080 108.830 120.571 1.00 34.50 ?  55  TYR D OH    1 
ATOM   13830 N  N     . MET D 2 77  ? 159.456 105.040 122.001 1.00 25.76 ?  56  MET D N     1 
ATOM   13831 C  CA    . MET D 2 77  ? 159.314 103.603 121.742 1.00 26.81 ?  56  MET D CA    1 
ATOM   13832 C  C     . MET D 2 77  ? 159.194 102.800 123.042 1.00 26.23 ?  56  MET D C     1 
ATOM   13833 O  O     . MET D 2 77  ? 158.322 101.938 123.171 1.00 25.00 ?  56  MET D O     1 
ATOM   13834 C  CB    . MET D 2 77  ? 160.489 103.079 120.919 1.00 28.11 ?  56  MET D CB    1 
ATOM   13835 C  CG    . MET D 2 77  ? 160.536 103.565 119.466 1.00 32.52 ?  56  MET D CG    1 
ATOM   13836 S  SD    . MET D 2 77  ? 159.289 102.819 118.402 1.00 42.68 ?  56  MET D SD    1 
ATOM   13837 C  CE    . MET D 2 77  ? 157.870 103.885 118.658 1.00 38.97 ?  56  MET D CE    1 
ATOM   13838 N  N     . LYS D 2 78  ? 160.082 103.091 123.992 1.00 26.01 ?  57  LYS D N     1 
ATOM   13839 C  CA    . LYS D 2 78  ? 160.119 102.371 125.269 1.00 26.07 ?  57  LYS D CA    1 
ATOM   13840 C  C     . LYS D 2 78  ? 158.865 102.613 126.107 1.00 25.69 ?  57  LYS D C     1 
ATOM   13841 O  O     . LYS D 2 78  ? 158.340 101.687 126.737 1.00 25.58 ?  57  LYS D O     1 
ATOM   13842 C  CB    . LYS D 2 78  ? 161.378 102.731 126.069 1.00 26.08 ?  57  LYS D CB    1 
ATOM   13843 C  CG    . LYS D 2 78  ? 162.677 102.190 125.455 1.00 27.64 ?  57  LYS D CG    1 
ATOM   13844 C  CD    . LYS D 2 78  ? 163.904 102.719 126.186 1.00 29.47 ?  57  LYS D CD    1 
ATOM   13845 C  CE    . LYS D 2 78  ? 165.161 102.011 125.705 1.00 31.69 ?  57  LYS D CE    1 
ATOM   13846 N  NZ    . LYS D 2 78  ? 166.380 102.485 126.412 1.00 33.36 1  57  LYS D NZ    1 
ATOM   13847 N  N     . VAL D 2 79  ? 158.395 103.858 126.112 1.00 25.32 ?  58  VAL D N     1 
ATOM   13848 C  CA    . VAL D 2 79  ? 157.179 104.237 126.840 1.00 25.47 ?  58  VAL D CA    1 
ATOM   13849 C  C     . VAL D 2 79  ? 155.983 103.516 126.225 1.00 25.09 ?  58  VAL D C     1 
ATOM   13850 O  O     . VAL D 2 79  ? 155.167 102.917 126.931 1.00 24.46 ?  58  VAL D O     1 
ATOM   13851 C  CB    . VAL D 2 79  ? 156.980 105.778 126.796 1.00 25.83 ?  58  VAL D CB    1 
ATOM   13852 C  CG1   . VAL D 2 79  ? 155.522 106.157 126.920 1.00 27.35 ?  58  VAL D CG1   1 
ATOM   13853 C  CG2   . VAL D 2 79  ? 157.838 106.448 127.869 1.00 26.42 ?  58  VAL D CG2   1 
ATOM   13854 N  N     . LEU D 2 80  ? 155.925 103.542 124.896 1.00 25.27 ?  59  LEU D N     1 
ATOM   13855 C  CA    . LEU D 2 80  ? 154.832 102.941 124.163 1.00 25.55 ?  59  LEU D CA    1 
ATOM   13856 C  C     . LEU D 2 80  ? 154.757 101.443 124.453 1.00 24.94 ?  59  LEU D C     1 
ATOM   13857 O  O     . LEU D 2 80  ? 153.672 100.913 124.685 1.00 24.82 ?  59  LEU D O     1 
ATOM   13858 C  CB    . LEU D 2 80  ? 155.009 103.185 122.663 1.00 25.80 ?  59  LEU D CB    1 
ATOM   13859 C  CG    . LEU D 2 80  ? 153.939 103.892 121.824 1.00 28.76 ?  59  LEU D CG    1 
ATOM   13860 C  CD1   . LEU D 2 80  ? 153.993 103.325 120.405 1.00 30.25 ?  59  LEU D CD1   1 
ATOM   13861 C  CD2   . LEU D 2 80  ? 152.529 103.789 122.380 1.00 27.79 ?  59  LEU D CD2   1 
ATOM   13862 N  N     . ALA D 2 81  ? 155.912 100.775 124.443 1.00 24.86 ?  60  ALA D N     1 
ATOM   13863 C  CA    . ALA D 2 81  ? 155.981 99.332  124.714 1.00 24.60 ?  60  ALA D CA    1 
ATOM   13864 C  C     . ALA D 2 81  ? 155.565 99.034  126.152 1.00 23.80 ?  60  ALA D C     1 
ATOM   13865 O  O     . ALA D 2 81  ? 154.895 98.043  126.419 1.00 24.07 ?  60  ALA D O     1 
ATOM   13866 C  CB    . ALA D 2 81  ? 157.388 98.800  124.443 1.00 24.48 ?  60  ALA D CB    1 
ATOM   13867 N  N     . GLY D 2 82  ? 155.962 99.905  127.072 1.00 23.54 ?  61  GLY D N     1 
ATOM   13868 C  CA    . GLY D 2 82  ? 155.551 99.798  128.468 1.00 22.53 ?  61  GLY D CA    1 
ATOM   13869 C  C     . GLY D 2 82  ? 154.043 99.825  128.608 1.00 22.23 ?  61  GLY D C     1 
ATOM   13870 O  O     . GLY D 2 82  ? 153.458 98.966  129.267 1.00 21.27 ?  61  GLY D O     1 
ATOM   13871 N  N     . LEU D 2 83  ? 153.408 100.815 127.981 1.00 22.36 ?  62  LEU D N     1 
ATOM   13872 C  CA    . LEU D 2 83  ? 151.945 100.927 128.012 1.00 22.42 ?  62  LEU D CA    1 
ATOM   13873 C  C     . LEU D 2 83  ? 151.284 99.709  127.382 1.00 22.91 ?  62  LEU D C     1 
ATOM   13874 O  O     . LEU D 2 83  ? 150.309 99.173  127.925 1.00 22.99 ?  62  LEU D O     1 
ATOM   13875 C  CB    . LEU D 2 83  ? 151.470 102.198 127.298 1.00 22.19 ?  62  LEU D CB    1 
ATOM   13876 C  CG    . LEU D 2 83  ? 151.867 103.540 127.935 1.00 22.17 ?  62  LEU D CG    1 
ATOM   13877 C  CD1   . LEU D 2 83  ? 151.628 104.681 126.937 1.00 21.55 ?  62  LEU D CD1   1 
ATOM   13878 C  CD2   . LEU D 2 83  ? 151.075 103.758 129.213 1.00 22.42 ?  62  LEU D CD2   1 
ATOM   13879 N  N     . THR D 2 84  ? 151.829 99.264  126.254 1.00 23.39 ?  63  THR D N     1 
ATOM   13880 C  CA    . THR D 2 84  ? 151.270 98.125  125.531 1.00 24.42 ?  63  THR D CA    1 
ATOM   13881 C  C     . THR D 2 84  ? 151.275 96.866  126.401 1.00 24.55 ?  63  THR D C     1 
ATOM   13882 O  O     . THR D 2 84  ? 150.255 96.184  126.532 1.00 23.68 ?  63  THR D O     1 
ATOM   13883 C  CB    . THR D 2 84  ? 152.033 97.849  124.210 1.00 24.70 ?  63  THR D CB    1 
ATOM   13884 O  OG1   . THR D 2 84  ? 151.970 99.010  123.372 1.00 25.57 ?  63  THR D OG1   1 
ATOM   13885 C  CG2   . THR D 2 84  ? 151.403 96.683  123.468 1.00 25.36 ?  63  THR D CG2   1 
ATOM   13886 N  N     . LEU D 2 85  ? 152.433 96.582  126.989 1.00 25.38 ?  64  LEU D N     1 
ATOM   13887 C  CA    . LEU D 2 85  ? 152.608 95.406  127.830 1.00 26.44 ?  64  LEU D CA    1 
ATOM   13888 C  C     . LEU D 2 85  ? 151.687 95.424  129.053 1.00 25.96 ?  64  LEU D C     1 
ATOM   13889 O  O     . LEU D 2 85  ? 151.018 94.418  129.330 1.00 25.83 ?  64  LEU D O     1 
ATOM   13890 C  CB    . LEU D 2 85  ? 154.087 95.205  128.196 1.00 26.65 ?  64  LEU D CB    1 
ATOM   13891 C  CG    . LEU D 2 85  ? 154.911 94.628  127.028 1.00 29.62 ?  64  LEU D CG    1 
ATOM   13892 C  CD1   . LEU D 2 85  ? 156.389 94.944  127.162 1.00 31.57 ?  64  LEU D CD1   1 
ATOM   13893 C  CD2   . LEU D 2 85  ? 154.710 93.108  126.874 1.00 30.96 ?  64  LEU D CD2   1 
ATOM   13894 N  N     . LEU D 2 86  ? 151.605 96.561  129.748 1.00 25.63 ?  65  LEU D N     1 
ATOM   13895 C  CA    . LEU D 2 86  ? 150.694 96.667  130.890 1.00 25.59 ?  65  LEU D CA    1 
ATOM   13896 C  C     . LEU D 2 86  ? 149.221 96.537  130.505 1.00 25.60 ?  65  LEU D C     1 
ATOM   13897 O  O     . LEU D 2 86  ? 148.430 95.936  131.237 1.00 25.47 ?  65  LEU D O     1 
ATOM   13898 C  CB    . LEU D 2 86  ? 150.928 97.955  131.702 1.00 25.76 ?  65  LEU D CB    1 
ATOM   13899 C  CG    . LEU D 2 86  ? 152.244 98.031  132.486 1.00 26.71 ?  65  LEU D CG    1 
ATOM   13900 C  CD1   . LEU D 2 86  ? 152.524 99.447  132.980 1.00 28.01 ?  65  LEU D CD1   1 
ATOM   13901 C  CD2   . LEU D 2 86  ? 152.250 97.068  133.651 1.00 28.01 ?  65  LEU D CD2   1 
ATOM   13902 N  N     . ASP D 2 87  ? 148.846 97.107  129.365 1.00 25.49 ?  66  ASP D N     1 
ATOM   13903 C  CA    . ASP D 2 87  ? 147.453 97.089  128.952 1.00 25.83 ?  66  ASP D CA    1 
ATOM   13904 C  C     . ASP D 2 87  ? 146.989 95.687  128.535 1.00 26.20 ?  66  ASP D C     1 
ATOM   13905 O  O     . ASP D 2 87  ? 145.827 95.336  128.709 1.00 25.99 ?  66  ASP D O     1 
ATOM   13906 C  CB    . ASP D 2 87  ? 147.210 98.100  127.839 1.00 25.50 ?  66  ASP D CB    1 
ATOM   13907 C  CG    . ASP D 2 87  ? 145.825 98.678  127.892 1.00 25.76 ?  66  ASP D CG    1 
ATOM   13908 O  OD1   . ASP D 2 87  ? 145.250 98.736  129.006 1.00 26.91 ?  66  ASP D OD1   1 
ATOM   13909 O  OD2   . ASP D 2 87  ? 145.302 99.078  126.833 1.00 23.11 -1 66  ASP D OD2   1 
ATOM   13910 N  N     . THR D 2 88  ? 147.916 94.890  128.008 1.00 27.12 ?  67  THR D N     1 
ATOM   13911 C  CA    . THR D 2 88  ? 147.653 93.500  127.663 1.00 28.40 ?  67  THR D CA    1 
ATOM   13912 C  C     . THR D 2 88  ? 147.321 92.676  128.896 1.00 28.28 ?  67  THR D C     1 
ATOM   13913 O  O     . THR D 2 88  ? 146.406 91.856  128.864 1.00 28.10 ?  67  THR D O     1 
ATOM   13914 C  CB    . THR D 2 88  ? 148.844 92.869  126.914 1.00 29.04 ?  67  THR D CB    1 
ATOM   13915 O  OG1   . THR D 2 88  ? 149.088 93.615  125.720 1.00 31.00 ?  67  THR D OG1   1 
ATOM   13916 C  CG2   . THR D 2 88  ? 148.535 91.423  126.530 1.00 30.16 ?  67  THR D CG2   1 
ATOM   13917 N  N     . GLU D 2 89  ? 148.056 92.893  129.985 1.00 28.28 ?  68  GLU D N     1 
ATOM   13918 C  CA    . GLU D 2 89  ? 147.738 92.222  131.240 1.00 29.16 ?  68  GLU D CA    1 
ATOM   13919 C  C     . GLU D 2 89  ? 146.322 92.588  131.683 1.00 28.65 ?  68  GLU D C     1 
ATOM   13920 O  O     . GLU D 2 89  ? 145.574 91.731  132.132 1.00 28.44 ?  68  GLU D O     1 
ATOM   13921 C  CB    . GLU D 2 89  ? 148.743 92.574  132.346 1.00 29.32 ?  68  GLU D CB    1 
ATOM   13922 C  CG    . GLU D 2 89  ? 150.196 92.183  132.039 1.00 31.95 ?  68  GLU D CG    1 
ATOM   13923 C  CD    . GLU D 2 89  ? 150.418 90.679  131.907 1.00 35.19 ?  68  GLU D CD    1 
ATOM   13924 O  OE1   . GLU D 2 89  ? 149.559 89.878  132.339 1.00 35.47 ?  68  GLU D OE1   1 
ATOM   13925 O  OE2   . GLU D 2 89  ? 151.471 90.297  131.355 1.00 38.06 -1 68  GLU D OE2   1 
ATOM   13926 N  N     . GLN D 2 90  ? 145.957 93.859  131.534 1.00 28.45 ?  69  GLN D N     1 
ATOM   13927 C  CA    . GLN D 2 90  ? 144.631 94.316  131.948 1.00 28.47 ?  69  GLN D CA    1 
ATOM   13928 C  C     . GLN D 2 90  ? 143.516 93.687  131.101 1.00 28.97 ?  69  GLN D C     1 
ATOM   13929 O  O     . GLN D 2 90  ? 142.464 93.329  131.628 1.00 28.84 ?  69  GLN D O     1 
ATOM   13930 C  CB    . GLN D 2 90  ? 144.555 95.847  131.936 1.00 28.21 ?  69  GLN D CB    1 
ATOM   13931 C  CG    . GLN D 2 90  ? 143.391 96.432  132.734 1.00 27.75 ?  69  GLN D CG    1 
ATOM   13932 C  CD    . GLN D 2 90  ? 143.550 96.309  134.245 1.00 28.91 ?  69  GLN D CD    1 
ATOM   13933 O  OE1   . GLN D 2 90  ? 144.301 95.464  134.751 1.00 27.62 ?  69  GLN D OE1   1 
ATOM   13934 N  NE2   . GLN D 2 90  ? 142.816 97.147  134.979 1.00 28.23 ?  69  GLN D NE2   1 
ATOM   13935 N  N     . GLY D 2 91  ? 143.763 93.532  129.800 1.00 29.62 ?  70  GLY D N     1 
ATOM   13936 C  CA    . GLY D 2 91  ? 142.803 92.893  128.897 1.00 30.43 ?  70  GLY D CA    1 
ATOM   13937 C  C     . GLY D 2 91  ? 142.671 91.384  129.063 1.00 31.11 ?  70  GLY D C     1 
ATOM   13938 O  O     . GLY D 2 91  ? 141.567 90.832  129.004 1.00 30.77 ?  70  GLY D O     1 
ATOM   13939 N  N     . ASN D 2 92  ? 143.793 90.707  129.260 1.00 31.69 ?  71  ASN D N     1 
ATOM   13940 C  CA    . ASN D 2 92  ? 143.765 89.256  129.395 1.00 32.72 ?  71  ASN D CA    1 
ATOM   13941 C  C     . ASN D 2 92  ? 143.411 88.741  130.783 1.00 32.60 ?  71  ASN D C     1 
ATOM   13942 O  O     . ASN D 2 92  ? 142.837 87.656  130.904 1.00 33.12 ?  71  ASN D O     1 
ATOM   13943 C  CB    . ASN D 2 92  ? 145.079 88.649  128.923 1.00 33.68 ?  71  ASN D CB    1 
ATOM   13944 C  CG    . ASN D 2 92  ? 145.237 88.716  127.419 1.00 35.15 ?  71  ASN D CG    1 
ATOM   13945 O  OD1   . ASN D 2 92  ? 146.352 88.743  126.914 1.00 40.21 ?  71  ASN D OD1   1 
ATOM   13946 N  ND2   . ASN D 2 92  ? 144.116 88.754  126.695 1.00 36.91 ?  71  ASN D ND2   1 
ATOM   13947 N  N     . THR D 2 93  ? 143.731 89.524  131.814 1.00 31.76 ?  72  THR D N     1 
ATOM   13948 C  CA    . THR D 2 93  ? 143.562 89.082  133.193 1.00 31.47 ?  72  THR D CA    1 
ATOM   13949 C  C     . THR D 2 93  ? 142.777 90.060  134.064 1.00 30.62 ?  72  THR D C     1 
ATOM   13950 O  O     . THR D 2 93  ? 141.743 89.695  134.617 1.00 30.71 ?  72  THR D O     1 
ATOM   13951 C  CB    . THR D 2 93  ? 144.914 88.793  133.838 1.00 31.60 ?  72  THR D CB    1 
ATOM   13952 O  OG1   . THR D 2 93  ? 145.618 87.837  133.035 1.00 33.14 ?  72  THR D OG1   1 
ATOM   13953 C  CG2   . THR D 2 93  ? 144.733 88.240  135.243 1.00 31.89 ?  72  THR D CG2   1 
ATOM   13954 N  N     . GLY D 2 94  ? 143.269 91.292  134.176 1.00 29.61 ?  73  GLY D N     1 
ATOM   13955 C  CA    . GLY D 2 94  ? 142.707 92.281  135.098 1.00 28.47 ?  73  GLY D CA    1 
ATOM   13956 C  C     . GLY D 2 94  ? 141.210 92.498  135.005 1.00 27.90 ?  73  GLY D C     1 
ATOM   13957 O  O     . GLY D 2 94  ? 140.486 92.377  136.003 1.00 28.27 ?  73  GLY D O     1 
ATOM   13958 N  N     . MET D 2 95  ? 140.728 92.847  133.820 1.00 26.67 ?  74  MET D N     1 
ATOM   13959 C  CA    . MET D 2 95  ? 139.293 93.085  133.687 1.00 26.00 ?  74  MET D CA    1 
ATOM   13960 C  C     . MET D 2 95  ? 138.496 91.785  133.707 1.00 25.25 ?  74  MET D C     1 
ATOM   13961 O  O     . MET D 2 95  ? 137.467 91.728  134.367 1.00 24.97 ?  74  MET D O     1 
ATOM   13962 C  CB    . MET D 2 95  ? 138.942 93.931  132.457 1.00 26.00 ?  74  MET D CB    1 
ATOM   13963 C  CG    . MET D 2 95  ? 139.169 95.411  132.649 1.00 26.40 ?  74  MET D CG    1 
ATOM   13964 S  SD    . MET D 2 95  ? 138.175 96.146  133.971 1.00 28.10 ?  74  MET D SD    1 
ATOM   13965 C  CE    . MET D 2 95  ? 138.881 97.789  133.979 1.00 28.95 ?  74  MET D CE    1 
ATOM   13966 N  N     . PRO D 2 96  ? 138.957 90.747  132.984 1.00 24.98 ?  75  PRO D N     1 
ATOM   13967 C  CA    . PRO D 2 96  ? 138.129 89.527  133.024 1.00 24.59 ?  75  PRO D CA    1 
ATOM   13968 C  C     . PRO D 2 96  ? 138.059 88.862  134.396 1.00 23.90 ?  75  PRO D C     1 
ATOM   13969 O  O     . PRO D 2 96  ? 137.036 88.266  134.714 1.00 23.45 ?  75  PRO D O     1 
ATOM   13970 C  CB    . PRO D 2 96  ? 138.816 88.590  132.022 1.00 24.80 ?  75  PRO D CB    1 
ATOM   13971 C  CG    . PRO D 2 96  ? 139.543 89.518  131.075 1.00 25.75 ?  75  PRO D CG    1 
ATOM   13972 C  CD    . PRO D 2 96  ? 139.991 90.675  131.929 1.00 25.07 ?  75  PRO D CD    1 
ATOM   13973 N  N     . ILE D 2 97  ? 139.128 88.947  135.193 1.00 23.36 ?  76  ILE D N     1 
ATOM   13974 C  CA    . ILE D 2 97  ? 139.122 88.303  136.502 1.00 23.48 ?  76  ILE D CA    1 
ATOM   13975 C  C     . ILE D 2 97  ? 138.186 89.028  137.455 1.00 23.30 ?  76  ILE D C     1 
ATOM   13976 O  O     . ILE D 2 97  ? 137.504 88.391  138.255 1.00 23.45 ?  76  ILE D O     1 
ATOM   13977 C  CB    . ILE D 2 97  ? 140.546 88.140  137.104 1.00 23.96 ?  76  ILE D CB    1 
ATOM   13978 C  CG1   . ILE D 2 97  ? 140.587 86.972  138.084 1.00 24.71 ?  76  ILE D CG1   1 
ATOM   13979 C  CG2   . ILE D 2 97  ? 141.057 89.443  137.766 1.00 24.02 ?  76  ILE D CG2   1 
ATOM   13980 C  CD1   . ILE D 2 97  ? 141.954 86.244  138.081 1.00 29.17 ?  76  ILE D CD1   1 
ATOM   13981 N  N     . VAL D 2 98  ? 138.144 90.356  137.360 1.00 22.71 ?  77  VAL D N     1 
ATOM   13982 C  CA    . VAL D 2 98  ? 137.230 91.153  138.194 1.00 22.78 ?  77  VAL D CA    1 
ATOM   13983 C  C     . VAL D 2 98  ? 135.778 90.906  137.779 1.00 22.89 ?  77  VAL D C     1 
ATOM   13984 O  O     . VAL D 2 98  ? 134.904 90.732  138.628 1.00 23.72 ?  77  VAL D O     1 
ATOM   13985 C  CB    . VAL D 2 98  ? 137.605 92.661  138.177 1.00 22.49 ?  77  VAL D CB    1 
ATOM   13986 C  CG1   . VAL D 2 98  ? 136.526 93.524  138.855 1.00 21.91 ?  77  VAL D CG1   1 
ATOM   13987 C  CG2   . VAL D 2 98  ? 138.940 92.864  138.874 1.00 23.02 ?  77  VAL D CG2   1 
ATOM   13988 N  N     . ALA D 2 99  ? 135.529 90.853  136.472 1.00 23.19 ?  78  ALA D N     1 
ATOM   13989 C  CA    . ALA D 2 99  ? 134.185 90.544  135.962 1.00 23.05 ?  78  ALA D CA    1 
ATOM   13990 C  C     . ALA D 2 99  ? 133.707 89.179  136.466 1.00 23.52 ?  78  ALA D C     1 
ATOM   13991 O  O     . ALA D 2 99  ? 132.530 88.992  136.790 1.00 23.68 ?  78  ALA D O     1 
ATOM   13992 C  CB    . ALA D 2 99  ? 134.169 90.599  134.444 1.00 22.81 ?  78  ALA D CB    1 
ATOM   13993 N  N     . GLU D 2 100 ? 134.628 88.222  136.540 1.00 23.68 ?  79  GLU D N     1 
ATOM   13994 C  CA    . GLU D 2 100 ? 134.302 86.885  137.031 1.00 24.14 ?  79  GLU D CA    1 
ATOM   13995 C  C     . GLU D 2 100 ? 133.841 86.850  138.498 1.00 23.66 ?  79  GLU D C     1 
ATOM   13996 O  O     . GLU D 2 100 ? 132.887 86.144  138.839 1.00 22.94 ?  79  GLU D O     1 
ATOM   13997 C  CB    . GLU D 2 100 ? 135.502 85.960  136.832 1.00 24.47 ?  79  GLU D CB    1 
ATOM   13998 C  CG    . GLU D 2 100 ? 135.202 84.496  137.087 1.00 27.90 ?  79  GLU D CG    1 
ATOM   13999 C  CD    . GLU D 2 100 ? 136.448 83.630  137.055 1.00 32.30 ?  79  GLU D CD    1 
ATOM   14000 O  OE1   . GLU D 2 100 ? 137.433 84.008  136.381 1.00 32.88 ?  79  GLU D OE1   1 
ATOM   14001 O  OE2   . GLU D 2 100 ? 136.438 82.570  137.714 1.00 34.74 -1 79  GLU D OE2   1 
ATOM   14002 N  N     . HIS D 2 101 ? 134.521 87.600  139.363 1.00 23.62 ?  80  HIS D N     1 
ATOM   14003 C  CA    . HIS D 2 101 ? 134.232 87.557  140.809 1.00 23.99 ?  80  HIS D CA    1 
ATOM   14004 C  C     . HIS D 2 101 ? 133.189 88.557  141.325 1.00 24.35 ?  80  HIS D C     1 
ATOM   14005 O  O     . HIS D 2 101 ? 132.655 88.378  142.421 1.00 24.21 ?  80  HIS D O     1 
ATOM   14006 C  CB    . HIS D 2 101 ? 135.534 87.657  141.617 1.00 24.13 ?  80  HIS D CB    1 
ATOM   14007 C  CG    . HIS D 2 101 ? 136.443 86.479  141.428 1.00 24.76 ?  80  HIS D CG    1 
ATOM   14008 N  ND1   . HIS D 2 101 ? 136.432 85.387  142.271 1.00 25.68 ?  80  HIS D ND1   1 
ATOM   14009 C  CD2   . HIS D 2 101 ? 137.370 86.211  140.479 1.00 25.75 ?  80  HIS D CD2   1 
ATOM   14010 C  CE1   . HIS D 2 101 ? 137.319 84.500  141.850 1.00 26.21 ?  80  HIS D CE1   1 
ATOM   14011 N  NE2   . HIS D 2 101 ? 137.902 84.977  140.765 1.00 25.35 ?  80  HIS D NE2   1 
ATOM   14012 N  N     . VAL D 2 102 ? 132.907 89.608  140.557 1.00 24.50 ?  81  VAL D N     1 
ATOM   14013 C  CA    . VAL D 2 102 ? 131.887 90.585  140.937 1.00 25.50 ?  81  VAL D CA    1 
ATOM   14014 C  C     . VAL D 2 102 ? 130.483 90.007  140.694 1.00 26.14 ?  81  VAL D C     1 
ATOM   14015 O  O     . VAL D 2 102 ? 130.232 89.426  139.641 1.00 26.96 ?  81  VAL D O     1 
ATOM   14016 C  CB    . VAL D 2 102 ? 132.067 91.920  140.158 1.00 25.30 ?  81  VAL D CB    1 
ATOM   14017 C  CG1   . VAL D 2 102 ? 130.868 92.822  140.337 1.00 27.08 ?  81  VAL D CG1   1 
ATOM   14018 C  CG2   . VAL D 2 102 ? 133.318 92.642  140.630 1.00 25.41 ?  81  VAL D CG2   1 
ATOM   14019 N  N     . ASP D 2 103 ? 129.592 90.154  141.671 1.00 26.45 ?  82  ASP D N     1 
ATOM   14020 C  CA    . ASP D 2 103 ? 128.194 89.745  141.516 1.00 27.15 ?  82  ASP D CA    1 
ATOM   14021 C  C     . ASP D 2 103 ? 127.358 90.891  140.965 1.00 26.39 ?  82  ASP D C     1 
ATOM   14022 O  O     . ASP D 2 103 ? 127.554 92.056  141.335 1.00 26.40 ?  82  ASP D O     1 
ATOM   14023 C  CB    . ASP D 2 103 ? 127.600 89.280  142.850 1.00 27.72 ?  82  ASP D CB    1 
ATOM   14024 C  CG    . ASP D 2 103 ? 128.297 88.051  143.421 1.00 31.46 ?  82  ASP D CG    1 
ATOM   14025 O  OD1   . ASP D 2 103 ? 128.786 87.186  142.645 1.00 34.26 ?  82  ASP D OD1   1 
ATOM   14026 O  OD2   . ASP D 2 103 ? 128.350 87.943  144.667 1.00 35.52 -1 82  ASP D OD2   1 
ATOM   14027 N  N     . GLY D 2 104 ? 126.414 90.551  140.093 1.00 25.52 ?  83  GLY D N     1 
ATOM   14028 C  CA    . GLY D 2 104 ? 125.506 91.538  139.511 1.00 24.31 ?  83  GLY D CA    1 
ATOM   14029 C  C     . GLY D 2 104 ? 125.603 91.481  137.991 1.00 23.27 ?  83  GLY D C     1 
ATOM   14030 O  O     . GLY D 2 104 ? 126.687 91.620  137.425 1.00 22.38 ?  83  GLY D O     1 
ATOM   14031 N  N     . HIS D 2 105 ? 124.471 91.259  137.331 1.00 22.46 ?  84  HIS D N     1 
ATOM   14032 C  CA    . HIS D 2 105 ? 124.451 91.173  135.869 1.00 22.17 ?  84  HIS D CA    1 
ATOM   14033 C  C     . HIS D 2 105 ? 124.891 92.456  135.182 1.00 21.13 ?  84  HIS D C     1 
ATOM   14034 O  O     . HIS D 2 105 ? 125.597 92.407  134.177 1.00 20.91 ?  84  HIS D O     1 
ATOM   14035 C  CB    . HIS D 2 105 ? 123.061 90.756  135.369 1.00 22.07 ?  84  HIS D CB    1 
ATOM   14036 C  CG    . HIS D 2 105 ? 122.621 89.431  135.905 1.00 23.85 ?  84  HIS D CG    1 
ATOM   14037 N  ND1   . HIS D 2 105 ? 123.408 88.302  135.817 1.00 24.86 ?  84  HIS D ND1   1 
ATOM   14038 C  CD2   . HIS D 2 105 ? 121.500 89.060  136.565 1.00 25.19 ?  84  HIS D CD2   1 
ATOM   14039 C  CE1   . HIS D 2 105 ? 122.780 87.287  136.382 1.00 24.94 ?  84  HIS D CE1   1 
ATOM   14040 N  NE2   . HIS D 2 105 ? 121.623 87.723  136.848 1.00 26.41 ?  84  HIS D NE2   1 
ATOM   14041 N  N     . GLN D 2 106 ? 124.477 93.594  135.718 1.00 20.66 ?  85  GLN D N     1 
ATOM   14042 C  CA    . GLN D 2 106 ? 124.753 94.865  135.053 1.00 20.70 ?  85  GLN D CA    1 
ATOM   14043 C  C     . GLN D 2 106 ? 126.228 95.232  135.209 1.00 20.46 ?  85  GLN D C     1 
ATOM   14044 O  O     . GLN D 2 106 ? 126.843 95.733  134.269 1.00 20.72 ?  85  GLN D O     1 
ATOM   14045 C  CB    . GLN D 2 106 ? 123.789 95.966  135.525 1.00 20.60 ?  85  GLN D CB    1 
ATOM   14046 C  CG    . GLN D 2 106 ? 122.304 95.642  135.206 1.00 20.74 ?  85  GLN D CG    1 
ATOM   14047 C  CD    . GLN D 2 106 ? 121.295 96.613  135.833 1.00 22.11 ?  85  GLN D CD    1 
ATOM   14048 O  OE1   . GLN D 2 106 ? 121.595 97.780  136.059 1.00 22.88 ?  85  GLN D OE1   1 
ATOM   14049 N  NE2   . GLN D 2 106 ? 120.087 96.124  136.100 1.00 21.64 ?  85  GLN D NE2   1 
ATOM   14050 N  N     . ARG D 2 107 ? 126.798 94.930  136.378 1.00 20.17 ?  86  ARG D N     1 
ATOM   14051 C  CA    . ARG D 2 107 ? 128.224 95.153  136.621 1.00 20.29 ?  86  ARG D CA    1 
ATOM   14052 C  C     . ARG D 2 107 ? 129.070 94.267  135.721 1.00 20.07 ?  86  ARG D C     1 
ATOM   14053 O  O     . ARG D 2 107 ? 130.066 94.719  135.171 1.00 19.53 ?  86  ARG D O     1 
ATOM   14054 C  CB    . ARG D 2 107 ? 128.584 94.869  138.077 1.00 20.88 ?  86  ARG D CB    1 
ATOM   14055 C  CG    . ARG D 2 107 ? 127.818 95.713  139.043 1.00 22.56 ?  86  ARG D CG    1 
ATOM   14056 C  CD    . ARG D 2 107 ? 127.954 95.178  140.446 1.00 27.21 ?  86  ARG D CD    1 
ATOM   14057 N  NE    . ARG D 2 107 ? 127.652 96.278  141.342 1.00 31.70 ?  86  ARG D NE    1 
ATOM   14058 C  CZ    . ARG D 2 107 ? 128.019 96.354  142.604 1.00 32.23 ?  86  ARG D CZ    1 
ATOM   14059 N  NH1   . ARG D 2 107 ? 128.716 95.370  143.170 1.00 34.27 1  86  ARG D NH1   1 
ATOM   14060 N  NH2   . ARG D 2 107 ? 127.684 97.432  143.289 1.00 33.79 ?  86  ARG D NH2   1 
ATOM   14061 N  N     . LYS D 2 108 ? 128.677 92.999  135.587 1.00 19.61 ?  87  LYS D N     1 
ATOM   14062 C  CA    . LYS D 2 108 ? 129.394 92.090  134.695 1.00 19.92 ?  87  LYS D CA    1 
ATOM   14063 C  C     . LYS D 2 108 ? 129.379 92.589  133.246 1.00 20.08 ?  87  LYS D C     1 
ATOM   14064 O  O     . LYS D 2 108 ? 130.355 92.403  132.511 1.00 20.38 ?  87  LYS D O     1 
ATOM   14065 C  CB    . LYS D 2 108 ? 128.852 90.661  134.782 1.00 19.54 ?  87  LYS D CB    1 
ATOM   14066 C  CG    . LYS D 2 108 ? 129.096 89.982  136.116 1.00 20.55 ?  87  LYS D CG    1 
ATOM   14067 C  CD    . LYS D 2 108 ? 128.555 88.550  136.121 1.00 21.09 ?  87  LYS D CD    1 
ATOM   14068 C  CE    . LYS D 2 108 ? 128.828 87.837  137.441 1.00 22.98 ?  87  LYS D CE    1 
ATOM   14069 N  NZ    . LYS D 2 108 ? 130.295 87.496  137.579 1.00 22.30 1  87  LYS D NZ    1 
ATOM   14070 N  N     . ALA D 2 109 ? 128.273 93.210  132.836 1.00 19.72 ?  88  ALA D N     1 
ATOM   14071 C  CA    . ALA D 2 109 ? 128.160 93.727  131.478 1.00 19.83 ?  88  ALA D CA    1 
ATOM   14072 C  C     . ALA D 2 109 ? 129.096 94.915  131.254 1.00 19.84 ?  88  ALA D C     1 
ATOM   14073 O  O     . ALA D 2 109 ? 129.802 94.976  130.241 1.00 19.96 ?  88  ALA D O     1 
ATOM   14074 C  CB    . ALA D 2 109 ? 126.702 94.093  131.149 1.00 19.65 ?  88  ALA D CB    1 
ATOM   14075 N  N     . VAL D 2 110 ? 129.121 95.843  132.208 1.00 19.33 ?  89  VAL D N     1 
ATOM   14076 C  CA    . VAL D 2 110 ? 130.014 97.008  132.121 1.00 19.22 ?  89  VAL D CA    1 
ATOM   14077 C  C     . VAL D 2 110 ? 131.475 96.522  132.105 1.00 19.45 ?  89  VAL D C     1 
ATOM   14078 O  O     . VAL D 2 110 ? 132.254 96.878  131.210 1.00 18.97 ?  89  VAL D O     1 
ATOM   14079 C  CB    . VAL D 2 110 ? 129.714 98.032  133.254 1.00 19.01 ?  89  VAL D CB    1 
ATOM   14080 C  CG1   . VAL D 2 110 ? 130.771 99.175  133.299 1.00 19.90 ?  89  VAL D CG1   1 
ATOM   14081 C  CG2   . VAL D 2 110 ? 128.338 98.622  133.048 1.00 19.69 ?  89  VAL D CG2   1 
ATOM   14082 N  N     . LEU D 2 111 ? 131.817 95.647  133.053 1.00 19.27 ?  90  LEU D N     1 
ATOM   14083 C  CA    . LEU D 2 111 ? 133.163 95.073  133.092 1.00 19.96 ?  90  LEU D CA    1 
ATOM   14084 C  C     . LEU D 2 111 ? 133.555 94.344  131.800 1.00 20.30 ?  90  LEU D C     1 
ATOM   14085 O  O     . LEU D 2 111 ? 134.685 94.493  131.327 1.00 19.88 ?  90  LEU D O     1 
ATOM   14086 C  CB    . LEU D 2 111 ? 133.359 94.192  134.334 1.00 19.87 ?  90  LEU D CB    1 
ATOM   14087 C  CG    . LEU D 2 111 ? 133.339 94.983  135.643 1.00 20.24 ?  90  LEU D CG    1 
ATOM   14088 C  CD1   . LEU D 2 111 ? 133.182 94.087  136.882 1.00 21.85 ?  90  LEU D CD1   1 
ATOM   14089 C  CD2   . LEU D 2 111 ? 134.579 95.890  135.762 1.00 20.29 ?  90  LEU D CD2   1 
ATOM   14090 N  N     . ASN D 2 112 ? 132.622 93.585  131.221 1.00 20.92 ?  91  ASN D N     1 
ATOM   14091 C  CA    . ASN D 2 112 ? 132.839 92.968  129.891 1.00 20.70 ?  91  ASN D CA    1 
ATOM   14092 C  C     . ASN D 2 112 ? 133.123 93.986  128.802 1.00 20.57 ?  91  ASN D C     1 
ATOM   14093 O  O     . ASN D 2 112 ? 133.936 93.737  127.896 1.00 20.45 ?  91  ASN D O     1 
ATOM   14094 C  CB    . ASN D 2 112 ? 131.612 92.176  129.437 1.00 21.16 ?  91  ASN D CB    1 
ATOM   14095 C  CG    . ASN D 2 112 ? 131.707 90.697  129.755 1.00 21.98 ?  91  ASN D CG    1 
ATOM   14096 O  OD1   . ASN D 2 112 ? 132.649 90.234  130.406 1.00 25.37 ?  91  ASN D OD1   1 
ATOM   14097 N  ND2   . ASN D 2 112 ? 130.712 89.949  129.314 1.00 21.12 ?  91  ASN D ND2   1 
ATOM   14098 N  N     . PHE D 2 113 ? 132.389 95.095  128.839 1.00 19.70 ?  92  PHE D N     1 
ATOM   14099 C  CA    . PHE D 2 113 ? 132.600 96.155  127.877 1.00 20.02 ?  92  PHE D CA    1 
ATOM   14100 C  C     . PHE D 2 113 ? 134.012 96.744  128.015 1.00 19.97 ?  92  PHE D C     1 
ATOM   14101 O  O     . PHE D 2 113 ? 134.707 96.954  127.015 1.00 19.22 ?  92  PHE D O     1 
ATOM   14102 C  CB    . PHE D 2 113 ? 131.528 97.254  127.981 1.00 20.09 ?  92  PHE D CB    1 
ATOM   14103 C  CG    . PHE D 2 113 ? 131.627 98.261  126.888 1.00 20.54 ?  92  PHE D CG    1 
ATOM   14104 C  CD1   . PHE D 2 113 ? 130.947 98.069  125.685 1.00 20.14 ?  92  PHE D CD1   1 
ATOM   14105 C  CD2   . PHE D 2 113 ? 132.455 99.375  127.034 1.00 20.77 ?  92  PHE D CD2   1 
ATOM   14106 C  CE1   . PHE D 2 113 ? 131.068 98.992  124.650 1.00 20.54 ?  92  PHE D CE1   1 
ATOM   14107 C  CE2   . PHE D 2 113 ? 132.588 100.300 125.999 1.00 21.23 ?  92  PHE D CE2   1 
ATOM   14108 C  CZ    . PHE D 2 113 ? 131.890 100.099 124.801 1.00 20.92 ?  92  PHE D CZ    1 
ATOM   14109 N  N     . MET D 2 114 ? 134.429 96.994  129.253 1.00 19.67 ?  93  MET D N     1 
ATOM   14110 C  CA    . MET D 2 114 ? 135.775 97.490  129.511 1.00 20.55 ?  93  MET D CA    1 
ATOM   14111 C  C     . MET D 2 114 ? 136.853 96.508  129.049 1.00 20.82 ?  93  MET D C     1 
ATOM   14112 O  O     . MET D 2 114 ? 137.831 96.939  128.453 1.00 20.43 ?  93  MET D O     1 
ATOM   14113 C  CB    . MET D 2 114 ? 135.956 97.837  130.984 1.00 20.24 ?  93  MET D CB    1 
ATOM   14114 C  CG    . MET D 2 114 ? 134.938 98.865  131.437 1.00 22.05 ?  93  MET D CG    1 
ATOM   14115 S  SD    . MET D 2 114 ? 134.946 99.189  133.185 1.00 25.85 ?  93  MET D SD    1 
ATOM   14116 C  CE    . MET D 2 114 ? 134.217 100.834 133.184 1.00 27.57 ?  93  MET D CE    1 
ATOM   14117 N  N     . ALA D 2 115 ? 136.667 95.208  129.322 1.00 21.19 ?  94  ALA D N     1 
ATOM   14118 C  CA    . ALA D 2 115 ? 137.609 94.174  128.850 1.00 21.53 ?  94  ALA D CA    1 
ATOM   14119 C  C     . ALA D 2 115 ? 137.691 94.170  127.325 1.00 21.75 ?  94  ALA D C     1 
ATOM   14120 O  O     . ALA D 2 115 ? 138.785 94.092  126.765 1.00 22.18 ?  94  ALA D O     1 
ATOM   14121 C  CB    . ALA D 2 115 ? 137.229 92.786  129.378 1.00 21.32 ?  94  ALA D CB    1 
ATOM   14122 N  N     . MET D 2 116 ? 136.539 94.286  126.661 1.00 21.47 ?  95  MET D N     1 
ATOM   14123 C  CA    . MET D 2 116 ? 136.489 94.397  125.206 1.00 21.83 ?  95  MET D CA    1 
ATOM   14124 C  C     . MET D 2 116 ? 137.348 95.569  124.692 1.00 22.15 ?  95  MET D C     1 
ATOM   14125 O  O     . MET D 2 116 ? 138.119 95.404  123.750 1.00 22.09 ?  95  MET D O     1 
ATOM   14126 C  CB    . MET D 2 116 ? 135.035 94.526  124.722 1.00 21.72 ?  95  MET D CB    1 
ATOM   14127 C  CG    . MET D 2 116 ? 134.870 94.753  123.211 1.00 22.57 ?  95  MET D CG    1 
ATOM   14128 S  SD    . MET D 2 116 ? 135.165 96.456  122.667 1.00 22.75 ?  95  MET D SD    1 
ATOM   14129 C  CE    . MET D 2 116 ? 133.795 97.324  123.430 1.00 22.96 ?  95  MET D CE    1 
ATOM   14130 N  N     . MET D 2 117 ? 137.207 96.741  125.315 1.00 22.04 ?  96  MET D N     1 
ATOM   14131 C  CA    . MET D 2 117 ? 137.976 97.930  124.911 1.00 22.45 ?  96  MET D CA    1 
ATOM   14132 C  C     . MET D 2 117 ? 139.492 97.693  125.021 1.00 22.39 ?  96  MET D C     1 
ATOM   14133 O  O     . MET D 2 117 ? 140.255 98.110  124.148 1.00 21.88 ?  96  MET D O     1 
ATOM   14134 C  CB    . MET D 2 117 ? 137.551 99.173  125.720 1.00 22.00 ?  96  MET D CB    1 
ATOM   14135 C  CG    . MET D 2 117 ? 136.148 99.716  125.339 1.00 23.25 ?  96  MET D CG    1 
ATOM   14136 S  SD    . MET D 2 117 ? 135.991 100.178 123.598 1.00 24.28 ?  96  MET D SD    1 
ATOM   14137 C  CE    . MET D 2 117 ? 136.955 101.684 123.534 1.00 24.59 ?  96  MET D CE    1 
ATOM   14138 N  N     . GLU D 2 118 ? 139.918 97.004  126.079 1.00 22.66 ?  97  GLU D N     1 
ATOM   14139 C  CA    . GLU D 2 118 ? 141.337 96.669  126.250 1.00 23.52 ?  97  GLU D CA    1 
ATOM   14140 C  C     . GLU D 2 118 ? 141.851 95.811  125.107 1.00 24.25 ?  97  GLU D C     1 
ATOM   14141 O  O     . GLU D 2 118 ? 142.873 96.139  124.501 1.00 25.05 ?  97  GLU D O     1 
ATOM   14142 C  CB    . GLU D 2 118 ? 141.618 95.953  127.592 1.00 23.11 ?  97  GLU D CB    1 
ATOM   14143 C  CG    . GLU D 2 118 ? 140.938 96.542  128.835 1.00 23.08 ?  97  GLU D CG    1 
ATOM   14144 C  CD    . GLU D 2 118 ? 141.472 97.900  129.262 1.00 24.08 ?  97  GLU D CD    1 
ATOM   14145 O  OE1   . GLU D 2 118 ? 142.153 98.559  128.462 1.00 26.39 ?  97  GLU D OE1   1 
ATOM   14146 O  OE2   . GLU D 2 118 ? 141.184 98.325  130.400 1.00 27.52 -1 97  GLU D OE2   1 
ATOM   14147 N  N     . ASN D 2 119 ? 141.127 94.735  124.807 1.00 25.47 ?  98  ASN D N     1 
ATOM   14148 C  CA    . ASN D 2 119 ? 141.579 93.690  123.866 1.00 26.32 ?  98  ASN D CA    1 
ATOM   14149 C  C     . ASN D 2 119 ? 141.319 93.986  122.392 1.00 26.22 ?  98  ASN D C     1 
ATOM   14150 O  O     . ASN D 2 119 ? 142.146 93.652  121.519 1.00 26.54 ?  98  ASN D O     1 
ATOM   14151 C  CB    . ASN D 2 119 ? 140.944 92.335  124.227 1.00 26.72 ?  98  ASN D CB    1 
ATOM   14152 C  CG    . ASN D 2 119 ? 141.420 91.811  125.582 1.00 29.12 ?  98  ASN D CG    1 
ATOM   14153 O  OD1   . ASN D 2 119 ? 142.625 91.697  125.832 1.00 32.07 ?  98  ASN D OD1   1 
ATOM   14154 N  ND2   . ASN D 2 119 ? 140.474 91.522  126.470 1.00 29.12 ?  98  ASN D ND2   1 
ATOM   14155 N  N     . ALA D 2 120 ? 140.163 94.585  122.121 1.00 25.46 ?  99  ALA D N     1 
ATOM   14156 C  CA    . ALA D 2 120 ? 139.717 94.820  120.749 1.00 25.77 ?  99  ALA D CA    1 
ATOM   14157 C  C     . ALA D 2 120 ? 140.078 96.205  120.222 1.00 25.51 ?  99  ALA D C     1 
ATOM   14158 O  O     . ALA D 2 120 ? 140.232 96.384  119.011 1.00 26.64 ?  99  ALA D O     1 
ATOM   14159 C  CB    . ALA D 2 120 ? 138.202 94.585  120.625 1.00 25.75 ?  99  ALA D CB    1 
ATOM   14160 N  N     . VAL D 2 121 ? 140.203 97.182  121.115 1.00 24.40 ?  100 VAL D N     1 
ATOM   14161 C  CA    . VAL D 2 121 ? 140.394 98.561  120.681 1.00 24.15 ?  100 VAL D CA    1 
ATOM   14162 C  C     . VAL D 2 121 ? 141.781 99.089  121.056 1.00 23.94 ?  100 VAL D C     1 
ATOM   14163 O  O     . VAL D 2 121 ? 142.565 99.465  120.178 1.00 23.75 ?  100 VAL D O     1 
ATOM   14164 C  CB    . VAL D 2 121 ? 139.261 99.495  121.207 1.00 23.68 ?  100 VAL D CB    1 
ATOM   14165 C  CG1   . VAL D 2 121 ? 139.460 100.925 120.706 1.00 23.76 ?  100 VAL D CG1   1 
ATOM   14166 C  CG2   . VAL D 2 121 ? 137.895 98.969  120.756 1.00 23.99 ?  100 VAL D CG2   1 
ATOM   14167 N  N     . HIS D 2 122 ? 142.079 99.106  122.353 1.00 23.68 ?  101 HIS D N     1 
ATOM   14168 C  CA    . HIS D 2 122 ? 143.365 99.608  122.840 1.00 24.02 ?  101 HIS D CA    1 
ATOM   14169 C  C     . HIS D 2 122 ? 144.551 98.832  122.291 1.00 24.39 ?  101 HIS D C     1 
ATOM   14170 O  O     . HIS D 2 122 ? 145.513 99.438  121.827 1.00 24.71 ?  101 HIS D O     1 
ATOM   14171 C  CB    . HIS D 2 122 ? 143.422 99.647  124.372 1.00 23.20 ?  101 HIS D CB    1 
ATOM   14172 C  CG    . HIS D 2 122 ? 142.439 100.592 124.992 1.00 22.82 ?  101 HIS D CG    1 
ATOM   14173 N  ND1   . HIS D 2 122 ? 142.295 100.721 126.355 1.00 20.48 ?  101 HIS D ND1   1 
ATOM   14174 C  CD2   . HIS D 2 122 ? 141.534 101.433 124.435 1.00 21.03 ?  101 HIS D CD2   1 
ATOM   14175 C  CE1   . HIS D 2 122 ? 141.355 101.612 126.613 1.00 19.88 ?  101 HIS D CE1   1 
ATOM   14176 N  NE2   . HIS D 2 122 ? 140.878 102.061 125.465 1.00 21.62 ?  101 HIS D NE2   1 
ATOM   14177 N  N     . ALA D 2 123 ? 144.484 97.501  122.331 1.00 25.30 ?  102 ALA D N     1 
ATOM   14178 C  CA    . ALA D 2 123 ? 145.620 96.677  121.893 1.00 25.77 ?  102 ALA D CA    1 
ATOM   14179 C  C     . ALA D 2 123 ? 145.928 96.856  120.403 1.00 26.37 ?  102 ALA D C     1 
ATOM   14180 O  O     . ALA D 2 123 ? 147.097 96.909  120.001 1.00 25.87 ?  102 ALA D O     1 
ATOM   14181 C  CB    . ALA D 2 123 ? 145.387 95.198  122.229 1.00 26.43 ?  102 ALA D CB    1 
ATOM   14182 N  N     . LYS D 2 124 ? 144.873 96.950  119.593 1.00 26.51 ?  103 LYS D N     1 
ATOM   14183 C  CA    . LYS D 2 124 ? 145.020 97.180  118.162 1.00 27.22 ?  103 LYS D CA    1 
ATOM   14184 C  C     . LYS D 2 124 ? 145.576 98.585  117.895 1.00 26.63 ?  103 LYS D C     1 
ATOM   14185 O  O     . LYS D 2 124 ? 146.372 98.771  116.974 1.00 26.07 ?  103 LYS D O     1 
ATOM   14186 C  CB    . LYS D 2 124 ? 143.676 96.965  117.437 1.00 27.51 ?  103 LYS D CB    1 
ATOM   14187 C  CG    . LYS D 2 124 ? 143.682 97.265  115.922 1.00 30.58 ?  103 LYS D CG    1 
ATOM   14188 C  CD    . LYS D 2 124 ? 144.536 96.278  115.140 1.00 35.72 ?  103 LYS D CD    1 
ATOM   14189 C  CE    . LYS D 2 124 ? 144.567 96.596  113.644 1.00 37.33 ?  103 LYS D CE    1 
ATOM   14190 N  NZ    . LYS D 2 124 ? 143.220 96.411  113.041 1.00 40.73 1  103 LYS D NZ    1 
ATOM   14191 N  N     . SER D 2 125 ? 145.166 99.554  118.719 1.00 26.02 ?  104 SER D N     1 
ATOM   14192 C  CA    . SER D 2 125 ? 145.605 100.946 118.588 1.00 26.16 ?  104 SER D CA    1 
ATOM   14193 C  C     . SER D 2 125 ? 147.101 101.109 118.855 1.00 26.18 ?  104 SER D C     1 
ATOM   14194 O  O     . SER D 2 125 ? 147.791 101.823 118.118 1.00 26.06 ?  104 SER D O     1 
ATOM   14195 C  CB    . SER D 2 125 ? 144.807 101.864 119.516 1.00 26.10 ?  104 SER D CB    1 
ATOM   14196 O  OG    . SER D 2 125 ? 143.447 101.899 119.120 1.00 26.58 ?  104 SER D OG    1 
ATOM   14197 N  N     . TYR D 2 126 ? 147.590 100.450 119.904 1.00 25.68 ?  105 TYR D N     1 
ATOM   14198 C  CA    . TYR D 2 126 ? 149.021 100.468 120.236 1.00 26.12 ?  105 TYR D CA    1 
ATOM   14199 C  C     . TYR D 2 126 ? 149.842 99.807  119.123 1.00 26.38 ?  105 TYR D C     1 
ATOM   14200 O  O     . TYR D 2 126 ? 150.884 100.325 118.715 1.00 26.83 ?  105 TYR D O     1 
ATOM   14201 C  CB    . TYR D 2 126 ? 149.295 99.762  121.577 1.00 25.35 ?  105 TYR D CB    1 
ATOM   14202 C  CG    . TYR D 2 126 ? 148.976 100.580 122.814 1.00 25.46 ?  105 TYR D CG    1 
ATOM   14203 C  CD1   . TYR D 2 126 ? 149.543 101.841 123.003 1.00 25.41 ?  105 TYR D CD1   1 
ATOM   14204 C  CD2   . TYR D 2 126 ? 148.130 100.080 123.816 1.00 24.77 ?  105 TYR D CD2   1 
ATOM   14205 C  CE1   . TYR D 2 126 ? 149.261 102.601 124.136 1.00 25.89 ?  105 TYR D CE1   1 
ATOM   14206 C  CE2   . TYR D 2 126 ? 147.840 100.839 124.961 1.00 23.11 ?  105 TYR D CE2   1 
ATOM   14207 C  CZ    . TYR D 2 126 ? 148.421 102.089 125.118 1.00 25.38 ?  105 TYR D CZ    1 
ATOM   14208 O  OH    . TYR D 2 126 ? 148.160 102.860 126.230 1.00 23.31 ?  105 TYR D OH    1 
ATOM   14209 N  N     . SER D 2 127 ? 149.355 98.676  118.626 1.00 27.16 ?  106 SER D N     1 
ATOM   14210 C  CA    . SER D 2 127 ? 150.009 97.965  117.523 1.00 27.83 ?  106 SER D CA    1 
ATOM   14211 C  C     . SER D 2 127 ? 150.108 98.852  116.273 1.00 28.21 ?  106 SER D C     1 
ATOM   14212 O  O     . SER D 2 127 ? 151.182 98.951  115.666 1.00 28.30 ?  106 SER D O     1 
ATOM   14213 C  CB    . SER D 2 127 ? 149.273 96.650  117.218 1.00 28.37 ?  106 SER D CB    1 
ATOM   14214 O  OG    . SER D 2 127 ? 149.824 95.994  116.077 1.00 29.33 ?  106 SER D OG    1 
ATOM   14215 N  N     . ASN D 2 128 ? 148.993 99.493  115.910 1.00 28.27 ?  107 ASN D N     1 
ATOM   14216 C  CA    . ASN D 2 128 ? 148.933 100.451 114.795 1.00 28.79 ?  107 ASN D CA    1 
ATOM   14217 C  C     . ASN D 2 128 ? 149.941 101.591 114.905 1.00 28.53 ?  107 ASN D C     1 
ATOM   14218 O  O     . ASN D 2 128 ? 150.600 101.931 113.917 1.00 28.03 ?  107 ASN D O     1 
ATOM   14219 C  CB    . ASN D 2 128 ? 147.521 101.042 114.630 1.00 29.05 ?  107 ASN D CB    1 
ATOM   14220 C  CG    . ASN D 2 128 ? 146.505 100.021 114.109 1.00 30.48 ?  107 ASN D CG    1 
ATOM   14221 O  OD1   . ASN D 2 128 ? 146.867 98.928  113.681 1.00 32.19 ?  107 ASN D OD1   1 
ATOM   14222 N  ND2   . ASN D 2 128 ? 145.226 100.378 114.164 1.00 31.59 ?  107 ASN D ND2   1 
ATOM   14223 N  N     . ILE D 2 129 ? 150.041 102.196 116.091 1.00 28.21 ?  108 ILE D N     1 
ATOM   14224 C  CA    . ILE D 2 129 ? 151.037 103.252 116.318 1.00 28.76 ?  108 ILE D CA    1 
ATOM   14225 C  C     . ILE D 2 129 ? 152.461 102.724 116.068 1.00 29.83 ?  108 ILE D C     1 
ATOM   14226 O  O     . ILE D 2 129 ? 153.249 103.354 115.350 1.00 29.99 ?  108 ILE D O     1 
ATOM   14227 C  CB    . ILE D 2 129 ? 150.919 103.900 117.735 1.00 28.28 ?  108 ILE D CB    1 
ATOM   14228 C  CG1   . ILE D 2 129 ? 149.566 104.607 117.904 1.00 27.94 ?  108 ILE D CG1   1 
ATOM   14229 C  CG2   . ILE D 2 129 ? 152.060 104.901 117.967 1.00 27.52 ?  108 ILE D CG2   1 
ATOM   14230 C  CD1   . ILE D 2 129 ? 149.214 104.945 119.347 1.00 27.98 ?  108 ILE D CD1   1 
ATOM   14231 N  N     . PHE D 2 130 ? 152.783 101.574 116.654 1.00 30.86 ?  109 PHE D N     1 
ATOM   14232 C  CA    . PHE D 2 130 ? 154.092 100.956 116.462 1.00 32.76 ?  109 PHE D CA    1 
ATOM   14233 C  C     . PHE D 2 130 ? 154.428 100.691 114.991 1.00 34.37 ?  109 PHE D C     1 
ATOM   14234 O  O     . PHE D 2 130 ? 155.480 101.109 114.513 1.00 34.61 ?  109 PHE D O     1 
ATOM   14235 C  CB    . PHE D 2 130 ? 154.205 99.658  117.258 1.00 32.81 ?  109 PHE D CB    1 
ATOM   14236 C  CG    . PHE D 2 130 ? 154.862 99.821  118.599 1.00 33.84 ?  109 PHE D CG    1 
ATOM   14237 C  CD1   . PHE D 2 130 ? 156.215 100.138 118.690 1.00 34.61 ?  109 PHE D CD1   1 
ATOM   14238 C  CD2   . PHE D 2 130 ? 154.137 99.625  119.767 1.00 35.74 ?  109 PHE D CD2   1 
ATOM   14239 C  CE1   . PHE D 2 130 ? 156.836 100.279 119.931 1.00 36.99 ?  109 PHE D CE1   1 
ATOM   14240 C  CE2   . PHE D 2 130 ? 154.745 99.763  121.021 1.00 36.96 ?  109 PHE D CE2   1 
ATOM   14241 C  CZ    . PHE D 2 130 ? 156.098 100.090 121.104 1.00 36.91 ?  109 PHE D CZ    1 
ATOM   14242 N  N     . MET D 2 131 ? 153.521 100.013 114.288 1.00 35.90 ?  110 MET D N     1 
ATOM   14243 C  CA    . MET D 2 131 ? 153.714 99.645  112.885 1.00 37.94 ?  110 MET D CA    1 
ATOM   14244 C  C     . MET D 2 131 ? 153.897 100.860 111.986 1.00 38.05 ?  110 MET D C     1 
ATOM   14245 O  O     . MET D 2 131 ? 154.559 100.771 110.958 1.00 38.20 ?  110 MET D O     1 
ATOM   14246 C  CB    . MET D 2 131 ? 152.550 98.783  112.368 1.00 38.63 ?  110 MET D CB    1 
ATOM   14247 C  CG    . MET D 2 131 ? 152.466 97.379  112.988 1.00 42.34 ?  110 MET D CG    1 
ATOM   14248 S  SD    . MET D 2 131 ? 151.091 96.356  112.366 1.00 50.15 ?  110 MET D SD    1 
ATOM   14249 C  CE    . MET D 2 131 ? 149.642 97.172  113.051 1.00 48.14 ?  110 MET D CE    1 
ATOM   14250 N  N     . THR D 2 132 ? 153.310 101.990 112.379 1.00 38.12 ?  111 THR D N     1 
ATOM   14251 C  CA    . THR D 2 132 ? 153.451 103.234 111.621 1.00 38.79 ?  111 THR D CA    1 
ATOM   14252 C  C     . THR D 2 132 ? 154.845 103.865 111.790 1.00 38.81 ?  111 THR D C     1 
ATOM   14253 O  O     . THR D 2 132 ? 155.437 104.332 110.811 1.00 39.26 ?  111 THR D O     1 
ATOM   14254 C  CB    . THR D 2 132 ? 152.350 104.246 111.997 1.00 38.78 ?  111 THR D CB    1 
ATOM   14255 O  OG1   . THR D 2 132 ? 151.065 103.652 111.779 1.00 39.32 ?  111 THR D OG1   1 
ATOM   14256 C  CG2   . THR D 2 132 ? 152.449 105.507 111.145 1.00 39.75 ?  111 THR D CG2   1 
ATOM   14257 N  N     . LEU D 2 133 ? 155.358 103.860 113.021 1.00 38.34 ?  112 LEU D N     1 
ATOM   14258 C  CA    . LEU D 2 133 ? 156.585 104.581 113.375 1.00 38.36 ?  112 LEU D CA    1 
ATOM   14259 C  C     . LEU D 2 133 ? 157.879 103.775 113.238 1.00 38.94 ?  112 LEU D C     1 
ATOM   14260 O  O     . LEU D 2 133 ? 158.932 104.342 112.951 1.00 39.14 ?  112 LEU D O     1 
ATOM   14261 C  CB    . LEU D 2 133 ? 156.490 105.137 114.805 1.00 37.62 ?  112 LEU D CB    1 
ATOM   14262 C  CG    . LEU D 2 133 ? 155.300 106.032 115.164 1.00 36.50 ?  112 LEU D CG    1 
ATOM   14263 C  CD1   . LEU D 2 133 ? 155.251 106.274 116.676 1.00 35.80 ?  112 LEU D CD1   1 
ATOM   14264 C  CD2   . LEU D 2 133 ? 155.318 107.345 114.401 1.00 35.32 ?  112 LEU D CD2   1 
ATOM   14265 N  N     . ALA D 2 134 ? 157.817 102.468 113.454 1.00 39.41 ?  113 ALA D N     1 
ATOM   14266 C  CA    . ALA D 2 134 ? 159.039 101.657 113.404 1.00 40.33 ?  113 ALA D CA    1 
ATOM   14267 C  C     . ALA D 2 134 ? 158.927 100.482 112.437 1.00 41.05 ?  113 ALA D C     1 
ATOM   14268 O  O     . ALA D 2 134 ? 157.834 99.965  112.232 1.00 40.81 ?  113 ALA D O     1 
ATOM   14269 C  CB    . ALA D 2 134 ? 159.400 101.169 114.794 1.00 40.15 ?  113 ALA D CB    1 
ATOM   14270 N  N     . PRO D 2 135 ? 160.058 100.063 111.828 1.00 42.21 ?  114 PRO D N     1 
ATOM   14271 C  CA    . PRO D 2 135 ? 160.025 98.824  111.043 1.00 43.27 ?  114 PRO D CA    1 
ATOM   14272 C  C     . PRO D 2 135 ? 159.927 97.592  111.955 1.00 43.89 ?  114 PRO D C     1 
ATOM   14273 O  O     . PRO D 2 135 ? 160.254 97.676  113.142 1.00 43.31 ?  114 PRO D O     1 
ATOM   14274 C  CB    . PRO D 2 135 ? 161.363 98.839  110.299 1.00 43.69 ?  114 PRO D CB    1 
ATOM   14275 C  CG    . PRO D 2 135 ? 162.258 99.651  111.155 1.00 43.01 ?  114 PRO D CG    1 
ATOM   14276 C  CD    . PRO D 2 135 ? 161.393 100.692 111.811 1.00 42.16 ?  114 PRO D CD    1 
ATOM   14277 N  N     . THR D 2 136 ? 159.490 96.466  111.391 1.00 45.26 ?  115 THR D N     1 
ATOM   14278 C  CA    . THR D 2 136 ? 159.220 95.237  112.154 1.00 46.11 ?  115 THR D CA    1 
ATOM   14279 C  C     . THR D 2 136 ? 160.363 94.837  113.091 1.00 46.35 ?  115 THR D C     1 
ATOM   14280 O  O     . THR D 2 136 ? 160.122 94.522  114.262 1.00 46.25 ?  115 THR D O     1 
ATOM   14281 C  CB    . THR D 2 136 ? 158.835 94.053  111.224 1.00 46.59 ?  115 THR D CB    1 
ATOM   14282 O  OG1   . THR D 2 136 ? 157.752 94.449  110.377 1.00 47.80 ?  115 THR D OG1   1 
ATOM   14283 C  CG2   . THR D 2 136 ? 158.384 92.834  112.028 1.00 46.94 ?  115 THR D CG2   1 
ATOM   14284 N  N     . GLU D 2 137 ? 161.597 94.873  112.588 1.00 46.92 ?  116 GLU D N     1 
ATOM   14285 C  CA    . GLU D 2 137 ? 162.762 94.480  113.379 1.00 47.37 ?  116 GLU D CA    1 
ATOM   14286 C  C     . GLU D 2 137 ? 162.983 95.369  114.606 1.00 46.64 ?  116 GLU D C     1 
ATOM   14287 O  O     . GLU D 2 137 ? 163.356 94.869  115.668 1.00 46.89 ?  116 GLU D O     1 
ATOM   14288 C  CB    . GLU D 2 137 ? 164.030 94.418  112.513 1.00 48.04 ?  116 GLU D CB    1 
ATOM   14289 C  CG    . GLU D 2 137 ? 165.282 93.890  113.239 1.00 49.86 ?  116 GLU D CG    1 
ATOM   14290 C  CD    . GLU D 2 137 ? 165.237 92.387  113.556 1.00 52.40 ?  116 GLU D CD    1 
ATOM   14291 O  OE1   . GLU D 2 137 ? 164.261 91.917  114.181 1.00 52.97 ?  116 GLU D OE1   1 
ATOM   14292 O  OE2   . GLU D 2 137 ? 166.203 91.674  113.197 1.00 54.12 -1 116 GLU D OE2   1 
ATOM   14293 N  N     . THR D 2 138 ? 162.748 96.671  114.452 1.00 46.09 ?  117 THR D N     1 
ATOM   14294 C  CA    . THR D 2 138 ? 162.862 97.632  115.560 1.00 45.30 ?  117 THR D CA    1 
ATOM   14295 C  C     . THR D 2 138 ? 161.798 97.394  116.639 1.00 44.63 ?  117 THR D C     1 
ATOM   14296 O  O     . THR D 2 138 ? 162.088 97.487  117.835 1.00 44.51 ?  117 THR D O     1 
ATOM   14297 C  CB    . THR D 2 138 ? 162.785 99.092  115.053 1.00 45.20 ?  117 THR D CB    1 
ATOM   14298 O  OG1   . THR D 2 138 ? 163.804 99.310  114.072 1.00 45.69 ?  117 THR D OG1   1 
ATOM   14299 C  CG2   . THR D 2 138 ? 162.978 100.091 116.194 1.00 44.67 ?  117 THR D CG2   1 
ATOM   14300 N  N     . ILE D 2 139 ? 160.573 97.081  116.213 1.00 44.24 ?  118 ILE D N     1 
ATOM   14301 C  CA    . ILE D 2 139 ? 159.486 96.772  117.145 1.00 43.65 ?  118 ILE D CA    1 
ATOM   14302 C  C     . ILE D 2 139 ? 159.835 95.544  117.998 1.00 43.87 ?  118 ILE D C     1 
ATOM   14303 O  O     . ILE D 2 139 ? 159.727 95.582  119.226 1.00 43.36 ?  118 ILE D O     1 
ATOM   14304 C  CB    . ILE D 2 139 ? 158.134 96.597  116.406 1.00 43.68 ?  118 ILE D CB    1 
ATOM   14305 C  CG1   . ILE D 2 139 ? 157.683 97.939  115.807 1.00 43.30 ?  118 ILE D CG1   1 
ATOM   14306 C  CG2   . ILE D 2 139 ? 157.053 96.033  117.347 1.00 43.11 ?  118 ILE D CG2   1 
ATOM   14307 C  CD1   . ILE D 2 139 ? 156.602 97.838  114.739 1.00 43.41 ?  118 ILE D CD1   1 
ATOM   14308 N  N     . ASN D 2 140 ? 160.282 94.474  117.341 1.00 44.52 ?  119 ASN D N     1 
ATOM   14309 C  CA    . ASN D 2 140 ? 160.684 93.244  118.033 1.00 45.00 ?  119 ASN D CA    1 
ATOM   14310 C  C     . ASN D 2 140 ? 161.798 93.471  119.076 1.00 44.99 ?  119 ASN D C     1 
ATOM   14311 O  O     . ASN D 2 140 ? 161.752 92.903  120.175 1.00 44.61 ?  119 ASN D O     1 
ATOM   14312 C  CB    . ASN D 2 140 ? 161.082 92.154  117.021 1.00 45.74 ?  119 ASN D CB    1 
ATOM   14313 C  CG    . ASN D 2 140 ? 159.934 91.757  116.086 1.00 46.40 ?  119 ASN D CG    1 
ATOM   14314 O  OD1   . ASN D 2 140 ? 158.763 92.064  116.333 1.00 46.85 ?  119 ASN D OD1   1 
ATOM   14315 N  ND2   . ASN D 2 140 ? 160.275 91.058  115.005 1.00 48.16 ?  119 ASN D ND2   1 
ATOM   14316 N  N     . GLU D 2 141 ? 162.773 94.318  118.739 1.00 45.09 ?  120 GLU D N     1 
ATOM   14317 C  CA    . GLU D 2 141 ? 163.884 94.627  119.645 1.00 45.27 ?  120 GLU D CA    1 
ATOM   14318 C  C     . GLU D 2 141 ? 163.469 95.463  120.865 1.00 44.75 ?  120 GLU D C     1 
ATOM   14319 O  O     . GLU D 2 141 ? 163.913 95.196  121.987 1.00 44.37 ?  120 GLU D O     1 
ATOM   14320 C  CB    . GLU D 2 141 ? 165.025 95.317  118.897 1.00 45.75 ?  120 GLU D CB    1 
ATOM   14321 C  CG    . GLU D 2 141 ? 165.753 94.412  117.901 1.00 48.17 ?  120 GLU D CG    1 
ATOM   14322 C  CD    . GLU D 2 141 ? 166.918 95.096  117.215 1.00 50.15 ?  120 GLU D CD    1 
ATOM   14323 O  OE1   . GLU D 2 141 ? 167.763 95.697  117.912 1.00 50.90 ?  120 GLU D OE1   1 
ATOM   14324 O  OE2   . GLU D 2 141 ? 166.993 95.027  115.971 1.00 52.25 -1 120 GLU D OE2   1 
ATOM   14325 N  N     . VAL D 2 142 ? 162.635 96.477  120.635 1.00 44.31 ?  121 VAL D N     1 
ATOM   14326 C  CA    . VAL D 2 142 ? 162.106 97.312  121.715 1.00 43.91 ?  121 VAL D CA    1 
ATOM   14327 C  C     . VAL D 2 142 ? 161.306 96.465  122.709 1.00 43.71 ?  121 VAL D C     1 
ATOM   14328 O  O     . VAL D 2 142 ? 161.451 96.619  123.920 1.00 43.44 ?  121 VAL D O     1 
ATOM   14329 C  CB    . VAL D 2 142 ? 161.240 98.484  121.176 1.00 43.65 ?  121 VAL D CB    1 
ATOM   14330 C  CG1   . VAL D 2 142 ? 160.595 99.260  122.324 1.00 43.40 ?  121 VAL D CG1   1 
ATOM   14331 C  CG2   . VAL D 2 142 ? 162.088 99.426  120.327 1.00 43.96 ?  121 VAL D CG2   1 
ATOM   14332 N  N     . PHE D 2 143 ? 160.476 95.562  122.192 1.00 44.03 ?  122 PHE D N     1 
ATOM   14333 C  CA    . PHE D 2 143 ? 159.692 94.684  123.052 1.00 44.42 ?  122 PHE D CA    1 
ATOM   14334 C  C     . PHE D 2 143 ? 160.548 93.671  123.805 1.00 45.38 ?  122 PHE D C     1 
ATOM   14335 O  O     . PHE D 2 143 ? 160.258 93.360  124.957 1.00 45.50 ?  122 PHE D O     1 
ATOM   14336 C  CB    . PHE D 2 143 ? 158.548 94.014  122.288 1.00 44.27 ?  122 PHE D CB    1 
ATOM   14337 C  CG    . PHE D 2 143 ? 157.303 94.849  122.249 1.00 43.28 ?  122 PHE D CG    1 
ATOM   14338 C  CD1   . PHE D 2 143 ? 156.421 94.852  123.329 1.00 42.17 ?  122 PHE D CD1   1 
ATOM   14339 C  CD2   . PHE D 2 143 ? 157.028 95.659  121.156 1.00 42.76 ?  122 PHE D CD2   1 
ATOM   14340 C  CE1   . PHE D 2 143 ? 155.274 95.636  123.313 1.00 42.16 ?  122 PHE D CE1   1 
ATOM   14341 C  CE2   . PHE D 2 143 ? 155.884 96.448  121.129 1.00 42.77 ?  122 PHE D CE2   1 
ATOM   14342 C  CZ    . PHE D 2 143 ? 155.003 96.437  122.210 1.00 42.28 ?  122 PHE D CZ    1 
ATOM   14343 N  N     . GLU D 2 144 ? 161.607 93.185  123.164 1.00 46.18 ?  123 GLU D N     1 
ATOM   14344 C  CA    . GLU D 2 144 ? 162.602 92.353  123.840 1.00 47.19 ?  123 GLU D CA    1 
ATOM   14345 C  C     . GLU D 2 144 ? 163.253 93.104  125.011 1.00 46.99 ?  123 GLU D C     1 
ATOM   14346 O  O     . GLU D 2 144 ? 163.392 92.541  126.101 1.00 46.94 ?  123 GLU D O     1 
ATOM   14347 C  CB    . GLU D 2 144 ? 163.666 91.872  122.844 1.00 47.80 ?  123 GLU D CB    1 
ATOM   14348 C  CG    . GLU D 2 144 ? 164.685 90.871  123.400 1.00 49.54 ?  123 GLU D CG    1 
ATOM   14349 C  CD    . GLU D 2 144 ? 165.787 90.521  122.395 1.00 52.37 ?  123 GLU D CD    1 
ATOM   14350 O  OE1   . GLU D 2 144 ? 166.345 91.441  121.753 1.00 52.92 ?  123 GLU D OE1   1 
ATOM   14351 O  OE2   . GLU D 2 144 ? 166.102 89.320  122.251 1.00 53.55 -1 123 GLU D OE2   1 
ATOM   14352 N  N     . TRP D 2 145 ? 163.638 94.365  124.779 1.00 47.02 ?  124 TRP D N     1 
ATOM   14353 C  CA    . TRP D 2 145 ? 164.273 95.217  125.800 1.00 46.93 ?  124 TRP D CA    1 
ATOM   14354 C  C     . TRP D 2 145 ? 163.326 95.501  126.956 1.00 46.55 ?  124 TRP D C     1 
ATOM   14355 O  O     . TRP D 2 145 ? 163.677 95.295  128.115 1.00 46.42 ?  124 TRP D O     1 
ATOM   14356 C  CB    . TRP D 2 145 ? 164.750 96.547  125.196 1.00 47.07 ?  124 TRP D CB    1 
ATOM   14357 C  CG    . TRP D 2 145 ? 165.603 97.416  126.125 1.00 47.82 ?  124 TRP D CG    1 
ATOM   14358 C  CD1   . TRP D 2 145 ? 166.970 97.431  126.207 1.00 48.78 ?  124 TRP D CD1   1 
ATOM   14359 C  CD2   . TRP D 2 145 ? 165.139 98.401  127.072 1.00 47.80 ?  124 TRP D CD2   1 
ATOM   14360 N  NE1   . TRP D 2 145 ? 167.385 98.350  127.145 1.00 49.06 ?  124 TRP D NE1   1 
ATOM   14361 C  CE2   . TRP D 2 145 ? 166.285 98.958  127.693 1.00 48.24 ?  124 TRP D CE2   1 
ATOM   14362 C  CE3   . TRP D 2 145 ? 163.873 98.860  127.460 1.00 47.65 ?  124 TRP D CE3   1 
ATOM   14363 C  CZ2   . TRP D 2 145 ? 166.199 99.951  128.682 1.00 47.74 ?  124 TRP D CZ2   1 
ATOM   14364 C  CZ3   . TRP D 2 145 ? 163.786 99.848  128.444 1.00 46.92 ?  124 TRP D CZ3   1 
ATOM   14365 C  CH2   . TRP D 2 145 ? 164.948 100.382 129.042 1.00 47.88 ?  124 TRP D CH2   1 
ATOM   14366 N  N     . VAL D 2 146 ? 162.127 95.978  126.636 1.00 46.09 ?  125 VAL D N     1 
ATOM   14367 C  CA    . VAL D 2 146 ? 161.157 96.357  127.657 1.00 45.36 ?  125 VAL D CA    1 
ATOM   14368 C  C     . VAL D 2 146 ? 160.673 95.117  128.426 1.00 45.28 ?  125 VAL D C     1 
ATOM   14369 O  O     . VAL D 2 146 ? 160.404 95.192  129.631 1.00 45.29 ?  125 VAL D O     1 
ATOM   14370 C  CB    . VAL D 2 146 ? 160.019 97.242  127.055 1.00 45.33 ?  125 VAL D CB    1 
ATOM   14371 C  CG1   . VAL D 2 146 ? 158.932 97.516  128.061 1.00 44.97 ?  125 VAL D CG1   1 
ATOM   14372 C  CG2   . VAL D 2 146 ? 160.595 98.574  126.570 1.00 44.52 ?  125 VAL D CG2   1 
ATOM   14373 N  N     . LYS D 2 147 ? 160.616 93.973  127.743 1.00 44.98 ?  126 LYS D N     1 
ATOM   14374 C  CA    . LYS D 2 147 ? 160.271 92.697  128.385 1.00 44.65 ?  126 LYS D CA    1 
ATOM   14375 C  C     . LYS D 2 147 ? 161.299 92.260  129.441 1.00 44.06 ?  126 LYS D C     1 
ATOM   14376 O  O     . LYS D 2 147 ? 160.953 91.580  130.408 1.00 44.65 ?  126 LYS D O     1 
ATOM   14377 C  CB    . LYS D 2 147 ? 160.101 91.584  127.347 1.00 45.31 ?  126 LYS D CB    1 
ATOM   14378 C  CG    . LYS D 2 147 ? 158.866 90.725  127.573 1.00 46.54 ?  126 LYS D CG    1 
ATOM   14379 C  CD    . LYS D 2 147 ? 159.137 89.233  127.368 1.00 49.06 ?  126 LYS D CD    1 
ATOM   14380 C  CE    . LYS D 2 147 ? 159.636 88.574  128.661 1.00 50.46 ?  126 LYS D CE    1 
ATOM   14381 N  NZ    . LYS D 2 147 ? 159.327 87.114  128.722 1.00 51.33 1  126 LYS D NZ    1 
ATOM   14382 N  N     . GLN D 2 148 ? 162.557 92.650  129.249 1.00 42.58 ?  127 GLN D N     1 
ATOM   14383 C  CA    . GLN D 2 148 ? 163.631 92.318  130.184 1.00 41.39 ?  127 GLN D CA    1 
ATOM   14384 C  C     . GLN D 2 148 ? 163.868 93.419  131.226 1.00 39.56 ?  127 GLN D C     1 
ATOM   14385 O  O     . GLN D 2 148 ? 164.524 93.181  132.239 1.00 39.77 ?  127 GLN D O     1 
ATOM   14386 C  CB    . GLN D 2 148 ? 164.917 91.986  129.401 1.00 42.11 ?  127 GLN D CB    1 
ATOM   14387 C  CG    . GLN D 2 148 ? 166.234 92.401  130.051 1.00 44.08 ?  127 GLN D CG    1 
ATOM   14388 C  CD    . GLN D 2 148 ? 166.783 93.728  129.523 1.00 46.12 ?  127 GLN D CD    1 
ATOM   14389 O  OE1   . GLN D 2 148 ? 166.040 94.697  129.315 1.00 46.47 ?  127 GLN D OE1   1 
ATOM   14390 N  NE2   . GLN D 2 148 ? 168.100 93.779  129.319 1.00 45.69 ?  127 GLN D NE2   1 
ATOM   14391 N  N     . ASN D 2 149 ? 163.323 94.612  130.974 1.00 36.99 ?  128 ASN D N     1 
ATOM   14392 C  CA    . ASN D 2 149 ? 163.522 95.768  131.848 1.00 34.54 ?  128 ASN D CA    1 
ATOM   14393 C  C     . ASN D 2 149 ? 163.036 95.559  133.285 1.00 33.13 ?  128 ASN D C     1 
ATOM   14394 O  O     . ASN D 2 149 ? 161.882 95.210  133.518 1.00 32.62 ?  128 ASN D O     1 
ATOM   14395 C  CB    . ASN D 2 149 ? 162.862 97.014  131.255 1.00 34.24 ?  128 ASN D CB    1 
ATOM   14396 C  CG    . ASN D 2 149 ? 163.146 98.258  132.073 1.00 33.83 ?  128 ASN D CG    1 
ATOM   14397 O  OD1   . ASN D 2 149 ? 162.312 98.698  132.866 1.00 32.21 ?  128 ASN D OD1   1 
ATOM   14398 N  ND2   . ASN D 2 149 ? 164.344 98.814  131.907 1.00 33.26 ?  128 ASN D ND2   1 
ATOM   14399 N  N     . LYS D 2 150 ? 163.927 95.812  134.240 1.00 31.49 ?  129 LYS D N     1 
ATOM   14400 C  CA    . LYS D 2 150 ? 163.679 95.547  135.655 1.00 30.68 ?  129 LYS D CA    1 
ATOM   14401 C  C     . LYS D 2 150 ? 162.483 96.328  136.253 1.00 28.95 ?  129 LYS D C     1 
ATOM   14402 O  O     . LYS D 2 150 ? 161.697 95.771  137.027 1.00 27.90 ?  129 LYS D O     1 
ATOM   14403 C  CB    . LYS D 2 150 ? 164.977 95.806  136.434 1.00 31.17 ?  129 LYS D CB    1 
ATOM   14404 C  CG    . LYS D 2 150 ? 164.875 95.937  137.939 1.00 33.66 ?  129 LYS D CG    1 
ATOM   14405 C  CD    . LYS D 2 150 ? 166.268 96.220  138.522 1.00 38.08 ?  129 LYS D CD    1 
ATOM   14406 C  CE    . LYS D 2 150 ? 166.197 96.965  139.860 1.00 40.20 ?  129 LYS D CE    1 
ATOM   14407 N  NZ    . LYS D 2 150 ? 166.184 96.040  141.026 1.00 42.60 1  129 LYS D NZ    1 
ATOM   14408 N  N     . TYR D 2 151 ? 162.354 97.605  135.898 1.00 27.36 ?  130 TYR D N     1 
ATOM   14409 C  CA    . TYR D 2 151 ? 161.319 98.466  136.500 1.00 26.56 ?  130 TYR D CA    1 
ATOM   14410 C  C     . TYR D 2 151 ? 159.941 98.215  135.907 1.00 25.66 ?  130 TYR D C     1 
ATOM   14411 O  O     . TYR D 2 151 ? 158.947 98.241  136.638 1.00 25.61 ?  130 TYR D O     1 
ATOM   14412 C  CB    . TYR D 2 151 ? 161.710 99.956  136.434 1.00 26.32 ?  130 TYR D CB    1 
ATOM   14413 C  CG    . TYR D 2 151 ? 163.151 100.180 136.849 1.00 27.20 ?  130 TYR D CG    1 
ATOM   14414 C  CD1   . TYR D 2 151 ? 163.540 100.020 138.179 1.00 27.31 ?  130 TYR D CD1   1 
ATOM   14415 C  CD2   . TYR D 2 151 ? 164.131 100.495 135.908 1.00 27.22 ?  130 TYR D CD2   1 
ATOM   14416 C  CE1   . TYR D 2 151 ? 164.867 100.190 138.568 1.00 29.65 ?  130 TYR D CE1   1 
ATOM   14417 C  CE2   . TYR D 2 151 ? 165.471 100.669 136.289 1.00 28.75 ?  130 TYR D CE2   1 
ATOM   14418 C  CZ    . TYR D 2 151 ? 165.818 100.520 137.634 1.00 29.17 ?  130 TYR D CZ    1 
ATOM   14419 O  OH    . TYR D 2 151 ? 167.119 100.682 138.054 1.00 30.61 ?  130 TYR D OH    1 
ATOM   14420 N  N     . LEU D 2 152 ? 159.888 97.970  134.596 1.00 24.87 ?  131 LEU D N     1 
ATOM   14421 C  CA    . LEU D 2 152 ? 158.639 97.576  133.953 1.00 24.37 ?  131 LEU D CA    1 
ATOM   14422 C  C     . LEU D 2 152 ? 158.162 96.226  134.502 1.00 24.18 ?  131 LEU D C     1 
ATOM   14423 O  O     . LEU D 2 152 ? 157.013 96.103  134.923 1.00 23.16 ?  131 LEU D O     1 
ATOM   14424 C  CB    . LEU D 2 152 ? 158.745 97.528  132.425 1.00 24.45 ?  131 LEU D CB    1 
ATOM   14425 C  CG    . LEU D 2 152 ? 157.342 97.149  131.918 1.00 26.33 ?  131 LEU D CG    1 
ATOM   14426 C  CD1   . LEU D 2 152 ? 156.376 98.337  132.036 1.00 25.00 ?  131 LEU D CD1   1 
ATOM   14427 C  CD2   . LEU D 2 152 ? 157.327 96.551  130.542 1.00 29.15 ?  131 LEU D CD2   1 
ATOM   14428 N  N     . GLN D 2 153 ? 159.055 95.234  134.524 1.00 24.07 ?  132 GLN D N     1 
ATOM   14429 C  CA    . GLN D 2 153 ? 158.714 93.913  135.093 1.00 24.99 ?  132 GLN D CA    1 
ATOM   14430 C  C     . GLN D 2 153 ? 158.265 93.972  136.551 1.00 24.24 ?  132 GLN D C     1 
ATOM   14431 O  O     . GLN D 2 153 ? 157.269 93.330  136.933 1.00 23.75 ?  132 GLN D O     1 
ATOM   14432 C  CB    . GLN D 2 153 ? 159.857 92.900  134.911 1.00 25.84 ?  132 GLN D CB    1 
ATOM   14433 C  CG    . GLN D 2 153 ? 160.053 92.444  133.440 1.00 28.48 ?  132 GLN D CG    1 
ATOM   14434 C  CD    . GLN D 2 153 ? 158.823 91.743  132.840 1.00 30.95 ?  132 GLN D CD    1 
ATOM   14435 O  OE1   . GLN D 2 153 ? 158.117 91.014  133.527 1.00 31.78 ?  132 GLN D OE1   1 
ATOM   14436 N  NE2   . GLN D 2 153 ? 158.580 91.961  131.546 1.00 32.81 ?  132 GLN D NE2   1 
ATOM   14437 N  N     . LYS D 2 154 ? 158.973 94.740  137.375 1.00 24.00 ?  133 LYS D N     1 
ATOM   14438 C  CA    . LYS D 2 154 ? 158.590 94.811  138.784 1.00 24.43 ?  133 LYS D CA    1 
ATOM   14439 C  C     . LYS D 2 154 ? 157.114 95.204  138.942 1.00 23.40 ?  133 LYS D C     1 
ATOM   14440 O  O     . LYS D 2 154 ? 156.348 94.503  139.607 1.00 22.68 ?  133 LYS D O     1 
ATOM   14441 C  CB    . LYS D 2 154 ? 159.472 95.768  139.594 1.00 24.64 ?  133 LYS D CB    1 
ATOM   14442 C  CG    . LYS D 2 154 ? 159.055 95.781  141.076 1.00 28.01 ?  133 LYS D CG    1 
ATOM   14443 C  CD    . LYS D 2 154 ? 159.983 96.563  141.976 1.00 32.56 ?  133 LYS D CD    1 
ATOM   14444 C  CE    . LYS D 2 154 ? 161.313 95.868  142.135 1.00 34.45 ?  133 LYS D CE    1 
ATOM   14445 N  NZ    . LYS D 2 154 ? 162.219 96.665  143.021 1.00 36.11 1  133 LYS D NZ    1 
ATOM   14446 N  N     . LYS D 2 155 ? 156.716 96.319  138.328 1.00 23.07 ?  134 LYS D N     1 
ATOM   14447 C  CA    . LYS D 2 155 ? 155.326 96.752  138.436 1.00 22.70 ?  134 LYS D CA    1 
ATOM   14448 C  C     . LYS D 2 155 ? 154.358 95.799  137.736 1.00 21.96 ?  134 LYS D C     1 
ATOM   14449 O  O     . LYS D 2 155 ? 153.311 95.487  138.294 1.00 22.25 ?  134 LYS D O     1 
ATOM   14450 C  CB    . LYS D 2 155 ? 155.127 98.214  137.997 1.00 22.70 ?  134 LYS D CB    1 
ATOM   14451 C  CG    . LYS D 2 155 ? 155.389 98.527  136.537 1.00 23.62 ?  134 LYS D CG    1 
ATOM   14452 C  CD    . LYS D 2 155 ? 155.066 99.997  136.274 1.00 25.32 ?  134 LYS D CD    1 
ATOM   14453 C  CE    . LYS D 2 155 ? 156.013 100.575 135.227 1.00 27.09 ?  134 LYS D CE    1 
ATOM   14454 N  NZ    . LYS D 2 155 ? 155.652 101.989 134.917 1.00 26.65 1  134 LYS D NZ    1 
ATOM   14455 N  N     . ALA D 2 156 ? 154.701 95.307  136.545 1.00 21.76 ?  135 ALA D N     1 
ATOM   14456 C  CA    . ALA D 2 156 ? 153.789 94.388  135.839 1.00 21.83 ?  135 ALA D CA    1 
ATOM   14457 C  C     . ALA D 2 156 ? 153.494 93.140  136.689 1.00 22.30 ?  135 ALA D C     1 
ATOM   14458 O  O     . ALA D 2 156 ? 152.334 92.744  136.842 1.00 21.92 ?  135 ALA D O     1 
ATOM   14459 C  CB    . ALA D 2 156 ? 154.351 93.988  134.463 1.00 22.30 ?  135 ALA D CB    1 
ATOM   14460 N  N     . GLN D 2 157 ? 154.539 92.542  137.262 1.00 22.15 ?  136 GLN D N     1 
ATOM   14461 C  CA    . GLN D 2 157 ? 154.363 91.322  138.058 1.00 22.38 ?  136 GLN D CA    1 
ATOM   14462 C  C     . GLN D 2 157 ? 153.696 91.562  139.419 1.00 21.59 ?  136 GLN D C     1 
ATOM   14463 O  O     . GLN D 2 157 ? 152.983 90.692  139.919 1.00 21.44 ?  136 GLN D O     1 
ATOM   14464 C  CB    . GLN D 2 157 ? 155.686 90.554  138.223 1.00 22.94 ?  136 GLN D CB    1 
ATOM   14465 C  CG    . GLN D 2 157 ? 156.360 90.132  136.908 1.00 25.31 ?  136 GLN D CG    1 
ATOM   14466 C  CD    . GLN D 2 157 ? 155.400 89.510  135.889 1.00 28.02 ?  136 GLN D CD    1 
ATOM   14467 O  OE1   . GLN D 2 157 ? 154.497 88.743  136.238 1.00 27.14 ?  136 GLN D OE1   1 
ATOM   14468 N  NE2   . GLN D 2 157 ? 155.607 89.840  134.616 1.00 29.47 ?  136 GLN D NE2   1 
ATOM   14469 N  N     . MET D 2 158 ? 153.928 92.723  140.022 1.00 21.52 ?  137 MET D N     1 
ATOM   14470 C  CA    . MET D 2 158 ? 153.230 93.081  141.269 1.00 22.20 ?  137 MET D CA    1 
ATOM   14471 C  C     . MET D 2 158 ? 151.709 93.118  141.082 1.00 21.84 ?  137 MET D C     1 
ATOM   14472 O  O     . MET D 2 158 ? 150.960 92.594  141.909 1.00 21.91 ?  137 MET D O     1 
ATOM   14473 C  CB    . MET D 2 158 ? 153.716 94.423  141.815 1.00 22.52 ?  137 MET D CB    1 
ATOM   14474 C  CG    . MET D 2 158 ? 155.077 94.350  142.522 1.00 25.81 ?  137 MET D CG    1 
ATOM   14475 S  SD    . MET D 2 158 ? 155.648 95.950  143.158 1.00 31.19 ?  137 MET D SD    1 
ATOM   14476 C  CE    . MET D 2 158 ? 154.357 96.241  144.338 1.00 23.91 ?  137 MET D CE    1 
ATOM   14477 N  N     . ILE D 2 159 ? 151.272 93.740  139.988 1.00 21.41 ?  138 ILE D N     1 
ATOM   14478 C  CA    . ILE D 2 159 ? 149.852 93.867  139.675 1.00 21.51 ?  138 ILE D CA    1 
ATOM   14479 C  C     . ILE D 2 159 ? 149.244 92.489  139.369 1.00 21.77 ?  138 ILE D C     1 
ATOM   14480 O  O     . ILE D 2 159 ? 148.201 92.122  139.934 1.00 21.44 ?  138 ILE D O     1 
ATOM   14481 C  CB    . ILE D 2 159 ? 149.633 94.899  138.502 1.00 21.49 ?  138 ILE D CB    1 
ATOM   14482 C  CG1   . ILE D 2 159 ? 150.109 96.305  138.900 1.00 21.16 ?  138 ILE D CG1   1 
ATOM   14483 C  CG2   . ILE D 2 159 ? 148.175 94.931  138.027 1.00 22.34 ?  138 ILE D CG2   1 
ATOM   14484 C  CD1   . ILE D 2 159 ? 149.358 96.937  140.091 1.00 23.85 ?  138 ILE D CD1   1 
ATOM   14485 N  N     . VAL D 2 160 ? 149.913 91.735  138.488 1.00 21.96 ?  139 VAL D N     1 
ATOM   14486 C  CA    . VAL D 2 160 ? 149.474 90.399  138.059 1.00 22.59 ?  139 VAL D CA    1 
ATOM   14487 C  C     . VAL D 2 160 ? 149.408 89.436  139.254 1.00 22.36 ?  139 VAL D C     1 
ATOM   14488 O  O     . VAL D 2 160 ? 148.498 88.605  139.336 1.00 21.64 ?  139 VAL D O     1 
ATOM   14489 C  CB    . VAL D 2 160 ? 150.395 89.833  136.926 1.00 23.08 ?  139 VAL D CB    1 
ATOM   14490 C  CG1   . VAL D 2 160 ? 150.213 88.317  136.722 1.00 24.33 ?  139 VAL D CG1   1 
ATOM   14491 C  CG2   . VAL D 2 160 ? 150.145 90.578  135.605 1.00 22.87 ?  139 VAL D CG2   1 
ATOM   14492 N  N     . GLY D 2 161 ? 150.369 89.563  140.173 1.00 22.21 ?  140 GLY D N     1 
ATOM   14493 C  CA    . GLY D 2 161 ? 150.382 88.762  141.395 1.00 22.50 ?  140 GLY D CA    1 
ATOM   14494 C  C     . GLY D 2 161 ? 149.099 88.916  142.206 1.00 22.88 ?  140 GLY D C     1 
ATOM   14495 O  O     . GLY D 2 161 ? 148.539 87.923  142.692 1.00 23.54 ?  140 GLY D O     1 
ATOM   14496 N  N     . LEU D 2 162 ? 148.622 90.153  142.345 1.00 22.25 ?  141 LEU D N     1 
ATOM   14497 C  CA    . LEU D 2 162 ? 147.376 90.406  143.074 1.00 22.48 ?  141 LEU D CA    1 
ATOM   14498 C  C     . LEU D 2 162 ? 146.136 89.874  142.350 1.00 22.27 ?  141 LEU D C     1 
ATOM   14499 O  O     . LEU D 2 162 ? 145.202 89.406  143.004 1.00 22.31 ?  141 LEU D O     1 
ATOM   14500 C  CB    . LEU D 2 162 ? 147.227 91.891  143.460 1.00 22.07 ?  141 LEU D CB    1 
ATOM   14501 C  CG    . LEU D 2 162 ? 148.139 92.330  144.627 1.00 22.81 ?  141 LEU D CG    1 
ATOM   14502 C  CD1   . LEU D 2 162 ? 148.358 93.841  144.651 1.00 21.65 ?  141 LEU D CD1   1 
ATOM   14503 C  CD2   . LEU D 2 162 ? 147.662 91.806  145.986 1.00 23.35 ?  141 LEU D CD2   1 
ATOM   14504 N  N     . TYR D 2 163 ? 146.119 89.941  141.017 1.00 22.63 ?  142 TYR D N     1 
ATOM   14505 C  CA    . TYR D 2 163 ? 145.027 89.326  140.236 1.00 23.30 ?  142 TYR D CA    1 
ATOM   14506 C  C     . TYR D 2 163 ? 144.998 87.811  140.394 1.00 23.40 ?  142 TYR D C     1 
ATOM   14507 O  O     . TYR D 2 163 ? 143.934 87.220  140.492 1.00 23.75 ?  142 TYR D O     1 
ATOM   14508 C  CB    . TYR D 2 163 ? 145.155 89.617  138.748 1.00 23.22 ?  142 TYR D CB    1 
ATOM   14509 C  CG    . TYR D 2 163 ? 145.091 91.066  138.347 1.00 24.01 ?  142 TYR D CG    1 
ATOM   14510 C  CD1   . TYR D 2 163 ? 144.479 92.012  139.160 1.00 24.47 ?  142 TYR D CD1   1 
ATOM   14511 C  CD2   . TYR D 2 163 ? 145.641 91.484  137.139 1.00 24.62 ?  142 TYR D CD2   1 
ATOM   14512 C  CE1   . TYR D 2 163 ? 144.420 93.339  138.787 1.00 26.33 ?  142 TYR D CE1   1 
ATOM   14513 C  CE2   . TYR D 2 163 ? 145.577 92.811  136.748 1.00 26.07 ?  142 TYR D CE2   1 
ATOM   14514 C  CZ    . TYR D 2 163 ? 144.958 93.732  137.583 1.00 26.65 ?  142 TYR D CZ    1 
ATOM   14515 O  OH    . TYR D 2 163 ? 144.894 95.058  137.221 1.00 31.13 ?  142 TYR D OH    1 
ATOM   14516 N  N     . LYS D 2 164 ? 146.169 87.188  140.406 1.00 23.70 ?  143 LYS D N     1 
ATOM   14517 C  CA    . LYS D 2 164 ? 146.264 85.729  140.574 1.00 24.47 ?  143 LYS D CA    1 
ATOM   14518 C  C     . LYS D 2 164 ? 145.890 85.245  141.985 1.00 24.55 ?  143 LYS D C     1 
ATOM   14519 O  O     . LYS D 2 164 ? 145.607 84.063  142.187 1.00 24.49 ?  143 LYS D O     1 
ATOM   14520 C  CB    . LYS D 2 164 ? 147.673 85.253  140.214 1.00 24.98 ?  143 LYS D CB    1 
ATOM   14521 C  CG    . LYS D 2 164 ? 147.974 85.221  138.708 1.00 27.10 ?  143 LYS D CG    1 
ATOM   14522 C  CD    . LYS D 2 164 ? 149.352 84.619  138.471 1.00 30.75 ?  143 LYS D CD    1 
ATOM   14523 C  CE    . LYS D 2 164 ? 149.680 84.458  136.988 1.00 32.81 ?  143 LYS D CE    1 
ATOM   14524 N  NZ    . LYS D 2 164 ? 151.096 83.957  136.771 1.00 33.68 1  143 LYS D NZ    1 
ATOM   14525 N  N     . ALA D 2 165 ? 145.902 86.155  142.955 1.00 24.18 ?  144 ALA D N     1 
ATOM   14526 C  CA    . ALA D 2 165 ? 145.632 85.802  144.352 1.00 25.04 ?  144 ALA D CA    1 
ATOM   14527 C  C     . ALA D 2 165 ? 144.158 85.918  144.766 1.00 25.00 ?  144 ALA D C     1 
ATOM   14528 O  O     . ALA D 2 165 ? 143.814 85.610  145.917 1.00 25.50 ?  144 ALA D O     1 
ATOM   14529 C  CB    . ALA D 2 165 ? 146.520 86.627  145.298 1.00 25.02 ?  144 ALA D CB    1 
ATOM   14530 N  N     . ILE D 2 166 ? 143.291 86.359  143.851 1.00 24.60 ?  145 ILE D N     1 
ATOM   14531 C  CA    . ILE D 2 166 ? 141.858 86.427  144.139 1.00 24.40 ?  145 ILE D CA    1 
ATOM   14532 C  C     . ILE D 2 166 ? 141.325 85.009  144.391 1.00 25.75 ?  145 ILE D C     1 
ATOM   14533 O  O     . ILE D 2 166 ? 141.618 84.080  143.631 1.00 25.84 ?  145 ILE D O     1 
ATOM   14534 C  CB    . ILE D 2 166 ? 141.032 87.080  142.995 1.00 24.15 ?  145 ILE D CB    1 
ATOM   14535 C  CG1   . ILE D 2 166 ? 141.633 88.421  142.576 1.00 23.15 ?  145 ILE D CG1   1 
ATOM   14536 C  CG2   . ILE D 2 166 ? 139.577 87.262  143.426 1.00 22.72 ?  145 ILE D CG2   1 
ATOM   14537 C  CD1   . ILE D 2 166 ? 141.022 89.001  141.318 1.00 21.70 ?  145 ILE D CD1   1 
ATOM   14538 N  N     . GLN D 2 167 ? 140.577 84.850  145.475 1.00 26.52 ?  146 GLN D N     1 
ATOM   14539 C  CA    . GLN D 2 167 ? 139.960 83.570  145.796 1.00 28.77 ?  146 GLN D CA    1 
ATOM   14540 C  C     . GLN D 2 167 ? 138.444 83.661  145.676 1.00 29.20 ?  146 GLN D C     1 
ATOM   14541 O  O     . GLN D 2 167 ? 137.840 84.678  146.048 1.00 28.89 ?  146 GLN D O     1 
ATOM   14542 C  CB    . GLN D 2 167 ? 140.349 83.134  147.206 1.00 29.04 ?  146 GLN D CB    1 
ATOM   14543 C  CG    . GLN D 2 167 ? 141.830 82.846  147.356 1.00 31.87 ?  146 GLN D CG    1 
ATOM   14544 C  CD    . GLN D 2 167 ? 142.392 83.423  148.628 1.00 35.35 ?  146 GLN D CD    1 
ATOM   14545 O  OE1   . GLN D 2 167 ? 142.069 82.967  149.728 1.00 36.91 ?  146 GLN D OE1   1 
ATOM   14546 N  NE2   . GLN D 2 167 ? 143.244 84.437  148.489 1.00 36.19 ?  146 GLN D NE2   1 
ATOM   14547 N  N     . LYS D 2 168 ? 137.836 82.597  145.158 1.00 30.29 ?  147 LYS D N     1 
ATOM   14548 C  CA    . LYS D 2 168 ? 136.380 82.525  145.045 1.00 31.24 ?  147 LYS D CA    1 
ATOM   14549 C  C     . LYS D 2 168 ? 135.703 82.855  146.375 1.00 31.73 ?  147 LYS D C     1 
ATOM   14550 O  O     . LYS D 2 168 ? 136.142 82.387  147.425 1.00 31.46 ?  147 LYS D O     1 
ATOM   14551 C  CB    . LYS D 2 168 ? 135.947 81.149  144.548 1.00 31.92 ?  147 LYS D CB    1 
ATOM   14552 C  CG    . LYS D 2 168 ? 134.447 81.029  144.324 1.00 33.23 ?  147 LYS D CG    1 
ATOM   14553 C  CD    . LYS D 2 168 ? 134.088 79.737  143.607 1.00 36.06 ?  147 LYS D CD    1 
ATOM   14554 C  CE    . LYS D 2 168 ? 132.588 79.593  143.455 1.00 35.46 ?  147 LYS D CE    1 
ATOM   14555 N  NZ    . LYS D 2 168 ? 132.029 80.552  142.464 1.00 38.24 1  147 LYS D NZ    1 
ATOM   14556 N  N     . ASP D 2 169 ? 134.653 83.679  146.316 1.00 32.28 ?  148 ASP D N     1 
ATOM   14557 C  CA    . ASP D 2 169 ? 133.883 84.096  147.500 1.00 33.45 ?  148 ASP D CA    1 
ATOM   14558 C  C     . ASP D 2 169 ? 134.688 84.765  148.613 1.00 33.30 ?  148 ASP D C     1 
ATOM   14559 O  O     . ASP D 2 169 ? 134.281 84.743  149.777 1.00 34.32 ?  148 ASP D O     1 
ATOM   14560 C  CB    . ASP D 2 169 ? 133.113 82.908  148.103 1.00 34.63 ?  148 ASP D CB    1 
ATOM   14561 C  CG    . ASP D 2 169 ? 131.926 82.483  147.266 1.00 36.09 ?  148 ASP D CG    1 
ATOM   14562 O  OD1   . ASP D 2 169 ? 131.516 83.220  146.344 1.00 37.80 ?  148 ASP D OD1   1 
ATOM   14563 O  OD2   . ASP D 2 169 ? 131.396 81.389  147.549 1.00 40.47 -1 148 ASP D OD2   1 
ATOM   14564 N  N     . ASP D 2 170 ? 135.835 85.338  148.280 1.00 32.58 ?  149 ASP D N     1 
ATOM   14565 C  CA    . ASP D 2 170 ? 136.593 86.100  149.271 1.00 32.01 ?  149 ASP D CA    1 
ATOM   14566 C  C     . ASP D 2 170 ? 136.708 87.544  148.798 1.00 30.59 ?  149 ASP D C     1 
ATOM   14567 O  O     . ASP D 2 170 ? 137.495 87.858  147.905 1.00 29.11 ?  149 ASP D O     1 
ATOM   14568 C  CB    . ASP D 2 170 ? 137.964 85.469  149.529 1.00 32.93 ?  149 ASP D CB    1 
ATOM   14569 C  CG    . ASP D 2 170 ? 138.879 86.357  150.361 1.00 35.05 ?  149 ASP D CG    1 
ATOM   14570 O  OD1   . ASP D 2 170 ? 138.400 87.159  151.193 1.00 39.25 ?  149 ASP D OD1   1 
ATOM   14571 O  OD2   . ASP D 2 170 ? 140.101 86.239  150.195 1.00 39.22 -1 149 ASP D OD2   1 
ATOM   14572 N  N     . GLU D 2 171 ? 135.899 88.407  149.407 1.00 29.34 ?  150 GLU D N     1 
ATOM   14573 C  CA    . GLU D 2 171 ? 135.811 89.807  149.007 1.00 28.51 ?  150 GLU D CA    1 
ATOM   14574 C  C     . GLU D 2 171 ? 137.050 90.631  149.384 1.00 27.27 ?  150 GLU D C     1 
ATOM   14575 O  O     . GLU D 2 171 ? 137.310 91.656  148.774 1.00 26.62 ?  150 GLU D O     1 
ATOM   14576 C  CB    . GLU D 2 171 ? 134.527 90.446  149.554 1.00 29.09 ?  150 GLU D CB    1 
ATOM   14577 C  CG    . GLU D 2 171 ? 134.487 90.644  151.068 1.00 30.68 ?  150 GLU D CG    1 
ATOM   14578 C  CD    . GLU D 2 171 ? 133.124 91.110  151.557 1.00 33.92 ?  150 GLU D CD    1 
ATOM   14579 O  OE1   . GLU D 2 171 ? 132.223 91.320  150.709 1.00 36.31 ?  150 GLU D OE1   1 
ATOM   14580 O  OE2   . GLU D 2 171 ? 132.945 91.275  152.784 1.00 34.02 -1 150 GLU D OE2   1 
ATOM   14581 N  N     . ILE D 2 172 ? 137.820 90.167  150.367 1.00 26.19 ?  151 ILE D N     1 
ATOM   14582 C  CA    . ILE D 2 172 ? 139.058 90.847  150.752 1.00 25.49 ?  151 ILE D CA    1 
ATOM   14583 C  C     . ILE D 2 172 ? 140.099 90.742  149.634 1.00 24.61 ?  151 ILE D C     1 
ATOM   14584 O  O     . ILE D 2 172 ? 140.703 91.748  149.241 1.00 24.09 ?  151 ILE D O     1 
ATOM   14585 C  CB    . ILE D 2 172 ? 139.618 90.323  152.104 1.00 25.98 ?  151 ILE D CB    1 
ATOM   14586 C  CG1   . ILE D 2 172 ? 138.642 90.614  153.246 1.00 26.86 ?  151 ILE D CG1   1 
ATOM   14587 C  CG2   . ILE D 2 172 ? 141.021 90.904  152.425 1.00 26.50 ?  151 ILE D CG2   1 
ATOM   14588 C  CD1   . ILE D 2 172 ? 138.354 92.092  153.466 1.00 27.81 ?  151 ILE D CD1   1 
ATOM   14589 N  N     . SER D 2 173 ? 140.283 89.533  149.114 1.00 23.71 ?  152 SER D N     1 
ATOM   14590 C  CA    . SER D 2 173 ? 141.222 89.303  148.017 1.00 23.38 ?  152 SER D CA    1 
ATOM   14591 C  C     . SER D 2 173 ? 140.752 90.008  146.731 1.00 22.41 ?  152 SER D C     1 
ATOM   14592 O  O     . SER D 2 173 ? 141.566 90.492  145.940 1.00 21.43 ?  152 SER D O     1 
ATOM   14593 C  CB    . SER D 2 173 ? 141.447 87.803  147.788 1.00 23.90 ?  152 SER D CB    1 
ATOM   14594 O  OG    . SER D 2 173 ? 140.312 87.140  147.231 1.00 23.74 ?  152 SER D OG    1 
ATOM   14595 N  N     . LEU D 2 174 ? 139.438 90.080  146.540 1.00 21.63 ?  153 LEU D N     1 
ATOM   14596 C  CA    . LEU D 2 174 ? 138.887 90.809  145.395 1.00 20.75 ?  153 LEU D CA    1 
ATOM   14597 C  C     . LEU D 2 174 ? 139.200 92.298  145.528 1.00 20.96 ?  153 LEU D C     1 
ATOM   14598 O  O     . LEU D 2 174 ? 139.618 92.936  144.563 1.00 20.41 ?  153 LEU D O     1 
ATOM   14599 C  CB    . LEU D 2 174 ? 137.369 90.579  145.260 1.00 20.62 ?  153 LEU D CB    1 
ATOM   14600 C  CG    . LEU D 2 174 ? 136.656 91.325  144.112 1.00 19.55 ?  153 LEU D CG    1 
ATOM   14601 C  CD1   . LEU D 2 174 ? 137.343 91.050  142.769 1.00 20.44 ?  153 LEU D CD1   1 
ATOM   14602 C  CD2   . LEU D 2 174 ? 135.173 90.931  144.069 1.00 20.99 ?  153 LEU D CD2   1 
ATOM   14603 N  N     . PHE D 2 175 ? 139.001 92.845  146.727 1.00 21.07 ?  154 PHE D N     1 
ATOM   14604 C  CA    . PHE D 2 175 ? 139.281 94.256  146.980 1.00 21.32 ?  154 PHE D CA    1 
ATOM   14605 C  C     . PHE D 2 175 ? 140.746 94.600  146.682 1.00 21.08 ?  154 PHE D C     1 
ATOM   14606 O  O     . PHE D 2 175 ? 141.039 95.611  146.041 1.00 20.85 ?  154 PHE D O     1 
ATOM   14607 C  CB    . PHE D 2 175 ? 138.939 94.621  148.429 1.00 21.20 ?  154 PHE D CB    1 
ATOM   14608 C  CG    . PHE D 2 175 ? 139.445 95.969  148.851 1.00 22.46 ?  154 PHE D CG    1 
ATOM   14609 C  CD1   . PHE D 2 175 ? 138.648 97.102  148.697 1.00 21.21 ?  154 PHE D CD1   1 
ATOM   14610 C  CD2   . PHE D 2 175 ? 140.717 96.113  149.413 1.00 22.53 ?  154 PHE D CD2   1 
ATOM   14611 C  CE1   . PHE D 2 175 ? 139.099 98.345  149.092 1.00 22.11 ?  154 PHE D CE1   1 
ATOM   14612 C  CE2   . PHE D 2 175 ? 141.187 97.365  149.798 1.00 23.26 ?  154 PHE D CE2   1 
ATOM   14613 C  CZ    . PHE D 2 175 ? 140.376 98.485  149.644 1.00 22.08 ?  154 PHE D CZ    1 
ATOM   14614 N  N     . LYS D 2 176 ? 141.657 93.759  147.161 1.00 21.14 ?  155 LYS D N     1 
ATOM   14615 C  CA    . LYS D 2 176 ? 143.091 93.959  146.927 1.00 20.93 ?  155 LYS D CA    1 
ATOM   14616 C  C     . LYS D 2 176 ? 143.433 94.001  145.439 1.00 20.61 ?  155 LYS D C     1 
ATOM   14617 O  O     . LYS D 2 176 ? 144.222 94.843  144.995 1.00 20.62 ?  155 LYS D O     1 
ATOM   14618 C  CB    . LYS D 2 176 ? 143.886 92.871  147.631 1.00 21.27 ?  155 LYS D CB    1 
ATOM   14619 C  CG    . LYS D 2 176 ? 143.906 93.064  149.122 1.00 22.04 ?  155 LYS D CG    1 
ATOM   14620 C  CD    . LYS D 2 176 ? 144.607 91.930  149.852 1.00 25.24 ?  155 LYS D CD    1 
ATOM   14621 C  CE    . LYS D 2 176 ? 144.636 92.236  151.327 1.00 25.83 ?  155 LYS D CE    1 
ATOM   14622 N  NZ    . LYS D 2 176 ? 145.325 91.181  152.127 1.00 26.64 1  155 LYS D NZ    1 
ATOM   14623 N  N     . ALA D 2 177 ? 142.814 93.110  144.673 1.00 20.02 ?  156 ALA D N     1 
ATOM   14624 C  CA    . ALA D 2 177 ? 142.968 93.108  143.220 1.00 19.86 ?  156 ALA D CA    1 
ATOM   14625 C  C     . ALA D 2 177 ? 142.375 94.369  142.575 1.00 19.61 ?  156 ALA D C     1 
ATOM   14626 O  O     . ALA D 2 177 ? 142.902 94.880  141.584 1.00 19.69 ?  156 ALA D O     1 
ATOM   14627 C  CB    . ALA D 2 177 ? 142.328 91.883  142.655 1.00 19.99 ?  156 ALA D CB    1 
ATOM   14628 N  N     . MET D 2 178 ? 141.270 94.862  143.130 1.00 19.75 ?  157 MET D N     1 
ATOM   14629 C  CA    . MET D 2 178 ? 140.621 96.076  142.594 1.00 18.89 ?  157 MET D CA    1 
ATOM   14630 C  C     . MET D 2 178 ? 141.504 97.292  142.829 1.00 18.62 ?  157 MET D C     1 
ATOM   14631 O  O     . MET D 2 178 ? 141.617 98.165  141.961 1.00 18.10 ?  157 MET D O     1 
ATOM   14632 C  CB    . MET D 2 178 ? 139.249 96.287  143.227 1.00 18.82 ?  157 MET D CB    1 
ATOM   14633 C  CG    . MET D 2 178 ? 138.192 95.330  142.701 1.00 20.20 ?  157 MET D CG    1 
ATOM   14634 S  SD    . MET D 2 178 ? 136.653 95.548  143.607 1.00 23.78 ?  157 MET D SD    1 
ATOM   14635 C  CE    . MET D 2 178 ? 135.568 94.513  142.628 1.00 22.62 ?  157 MET D CE    1 
ATOM   14636 N  N     . VAL D 2 179 ? 142.146 97.324  143.999 1.00 18.34 ?  158 VAL D N     1 
ATOM   14637 C  CA    . VAL D 2 179 ? 143.115 98.360  144.322 1.00 18.75 ?  158 VAL D CA    1 
ATOM   14638 C  C     . VAL D 2 179 ? 144.259 98.346  143.316 1.00 18.86 ?  158 VAL D C     1 
ATOM   14639 O  O     . VAL D 2 179 ? 144.646 99.409  142.801 1.00 18.79 ?  158 VAL D O     1 
ATOM   14640 C  CB    . VAL D 2 179 ? 143.678 98.226  145.762 1.00 19.02 ?  158 VAL D CB    1 
ATOM   14641 C  CG1   . VAL D 2 179 ? 144.849 99.198  145.965 1.00 19.10 ?  158 VAL D CG1   1 
ATOM   14642 C  CG2   . VAL D 2 179 ? 142.574 98.470  146.803 1.00 18.94 ?  158 VAL D CG2   1 
ATOM   14643 N  N     . ALA D 2 180 ? 144.798 97.148  143.054 1.00 18.96 ?  159 ALA D N     1 
ATOM   14644 C  CA    . ALA D 2 180 ? 145.832 96.968  142.032 1.00 19.05 ?  159 ALA D CA    1 
ATOM   14645 C  C     . ALA D 2 180 ? 145.353 97.470  140.668 1.00 18.67 ?  159 ALA D C     1 
ATOM   14646 O  O     . ALA D 2 180 ? 146.081 98.192  139.976 1.00 17.72 ?  159 ALA D O     1 
ATOM   14647 C  CB    . ALA D 2 180 ? 146.267 95.494  141.947 1.00 19.43 ?  159 ALA D CB    1 
ATOM   14648 N  N     . SER D 2 181 ? 144.117 97.113  140.306 1.00 18.49 ?  160 SER D N     1 
ATOM   14649 C  CA    . SER D 2 181 ? 143.543 97.546  139.030 1.00 18.51 ?  160 SER D CA    1 
ATOM   14650 C  C     . SER D 2 181 ? 143.407 99.065  138.936 1.00 18.23 ?  160 SER D C     1 
ATOM   14651 O  O     . SER D 2 181 ? 143.784 99.662  137.936 1.00 18.18 ?  160 SER D O     1 
ATOM   14652 C  CB    . SER D 2 181 ? 142.183 96.888  138.782 1.00 18.51 ?  160 SER D CB    1 
ATOM   14653 O  OG    . SER D 2 181 ? 141.748 97.198  137.472 1.00 19.42 ?  160 SER D OG    1 
ATOM   14654 N  N     . VAL D 2 182 ? 142.874 99.687  139.986 1.00 18.43 ?  161 VAL D N     1 
ATOM   14655 C  CA    . VAL D 2 182 ? 142.774 101.150 140.025 1.00 18.09 ?  161 VAL D CA    1 
ATOM   14656 C  C     . VAL D 2 182 ? 144.158 101.802 139.933 1.00 18.41 ?  161 VAL D C     1 
ATOM   14657 O  O     . VAL D 2 182 ? 144.337 102.782 139.207 1.00 18.52 ?  161 VAL D O     1 
ATOM   14658 C  CB    . VAL D 2 182 ? 142.007 101.639 141.260 1.00 17.71 ?  161 VAL D CB    1 
ATOM   14659 C  CG1   . VAL D 2 182 ? 142.099 103.178 141.393 1.00 16.02 ?  161 VAL D CG1   1 
ATOM   14660 C  CG2   . VAL D 2 182 ? 140.540 101.200 141.156 1.00 17.78 ?  161 VAL D CG2   1 
ATOM   14661 N  N     . TYR D 2 183 ? 145.141 101.232 140.631 1.00 19.06 ?  162 TYR D N     1 
ATOM   14662 C  CA    . TYR D 2 183 ? 146.497 101.765 140.553 1.00 19.73 ?  162 TYR D CA    1 
ATOM   14663 C  C     . TYR D 2 183 ? 147.053 101.675 139.139 1.00 19.90 ?  162 TYR D C     1 
ATOM   14664 O  O     . TYR D 2 183 ? 147.765 102.568 138.711 1.00 20.73 ?  162 TYR D O     1 
ATOM   14665 C  CB    . TYR D 2 183 ? 147.455 101.110 141.565 1.00 19.84 ?  162 TYR D CB    1 
ATOM   14666 C  CG    . TYR D 2 183 ? 147.231 101.532 143.003 1.00 20.24 ?  162 TYR D CG    1 
ATOM   14667 C  CD1   . TYR D 2 183 ? 146.421 102.620 143.317 1.00 21.51 ?  162 TYR D CD1   1 
ATOM   14668 C  CD2   . TYR D 2 183 ? 147.853 100.850 144.056 1.00 20.45 ?  162 TYR D CD2   1 
ATOM   14669 C  CE1   . TYR D 2 183 ? 146.221 103.012 144.646 1.00 21.68 ?  162 TYR D CE1   1 
ATOM   14670 C  CE2   . TYR D 2 183 ? 147.676 101.249 145.388 1.00 19.97 ?  162 TYR D CE2   1 
ATOM   14671 C  CZ    . TYR D 2 183 ? 146.854 102.327 145.672 1.00 21.83 ?  162 TYR D CZ    1 
ATOM   14672 O  OH    . TYR D 2 183 ? 146.662 102.725 146.981 1.00 21.96 ?  162 TYR D OH    1 
ATOM   14673 N  N     . LEU D 2 184 ? 146.717 100.622 138.406 1.00 20.22 ?  163 LEU D N     1 
ATOM   14674 C  CA    . LEU D 2 184 ? 147.181 100.518 137.025 1.00 20.89 ?  163 LEU D CA    1 
ATOM   14675 C  C     . LEU D 2 184 ? 146.466 101.554 136.145 1.00 20.72 ?  163 LEU D C     1 
ATOM   14676 O  O     . LEU D 2 184 ? 147.117 102.358 135.484 1.00 21.07 ?  163 LEU D O     1 
ATOM   14677 C  CB    . LEU D 2 184 ? 147.043 99.080  136.487 1.00 21.16 ?  163 LEU D CB    1 
ATOM   14678 C  CG    . LEU D 2 184 ? 147.442 98.781  135.027 1.00 22.77 ?  163 LEU D CG    1 
ATOM   14679 C  CD1   . LEU D 2 184 ? 148.860 99.286  134.678 1.00 22.44 ?  163 LEU D CD1   1 
ATOM   14680 C  CD2   . LEU D 2 184 ? 147.323 97.298  134.715 1.00 24.75 ?  163 LEU D CD2   1 
ATOM   14681 N  N     . GLU D 2 185 ? 145.135 101.552 136.181 1.00 20.65 ?  164 GLU D N     1 
ATOM   14682 C  CA    . GLU D 2 185 ? 144.312 102.445 135.351 1.00 20.69 ?  164 GLU D CA    1 
ATOM   14683 C  C     . GLU D 2 185 ? 144.540 103.935 135.604 1.00 20.64 ?  164 GLU D C     1 
ATOM   14684 O  O     . GLU D 2 185 ? 144.548 104.741 134.662 1.00 20.25 ?  164 GLU D O     1 
ATOM   14685 C  CB    . GLU D 2 185 ? 142.821 102.146 135.564 1.00 21.03 ?  164 GLU D CB    1 
ATOM   14686 C  CG    . GLU D 2 185 ? 142.397 100.709 135.245 1.00 22.19 ?  164 GLU D CG    1 
ATOM   14687 C  CD    . GLU D 2 185 ? 142.119 100.460 133.765 1.00 24.19 ?  164 GLU D CD    1 
ATOM   14688 O  OE1   . GLU D 2 185 ? 142.332 101.350 132.922 1.00 27.97 ?  164 GLU D OE1   1 
ATOM   14689 O  OE2   . GLU D 2 185 ? 141.657 99.368  133.434 1.00 25.47 -1 164 GLU D OE2   1 
ATOM   14690 N  N     . SER D 2 186 ? 144.689 104.300 136.874 1.00 20.42 ?  165 SER D N     1 
ATOM   14691 C  CA    . SER D 2 186 ? 144.663 105.705 137.278 1.00 20.70 ?  165 SER D CA    1 
ATOM   14692 C  C     . SER D 2 186 ? 146.022 106.258 137.709 1.00 20.88 ?  165 SER D C     1 
ATOM   14693 O  O     . SER D 2 186 ? 146.122 107.428 138.076 1.00 21.21 ?  165 SER D O     1 
ATOM   14694 C  CB    . SER D 2 186 ? 143.641 105.922 138.408 1.00 21.25 ?  165 SER D CB    1 
ATOM   14695 O  OG    . SER D 2 186 ? 142.362 105.401 138.073 1.00 20.97 ?  165 SER D OG    1 
ATOM   14696 N  N     . PHE D 2 187 ? 147.071 105.436 137.661 1.00 20.94 ?  166 PHE D N     1 
ATOM   14697 C  CA    . PHE D 2 187 ? 148.346 105.854 138.225 1.00 21.19 ?  166 PHE D CA    1 
ATOM   14698 C  C     . PHE D 2 187 ? 149.538 105.340 137.419 1.00 21.22 ?  166 PHE D C     1 
ATOM   14699 O  O     . PHE D 2 187 ? 150.282 106.153 136.859 1.00 21.10 ?  166 PHE D O     1 
ATOM   14700 C  CB    . PHE D 2 187 ? 148.393 105.510 139.740 1.00 21.63 ?  166 PHE D CB    1 
ATOM   14701 C  CG    . PHE D 2 187 ? 149.774 105.437 140.338 1.00 24.05 ?  166 PHE D CG    1 
ATOM   14702 C  CD1   . PHE D 2 187 ? 150.635 106.534 140.306 1.00 25.52 ?  166 PHE D CD1   1 
ATOM   14703 C  CD2   . PHE D 2 187 ? 150.197 104.278 140.983 1.00 27.03 ?  166 PHE D CD2   1 
ATOM   14704 C  CE1   . PHE D 2 187 ? 151.897 106.463 140.883 1.00 26.73 ?  166 PHE D CE1   1 
ATOM   14705 C  CE2   . PHE D 2 187 ? 151.475 104.200 141.556 1.00 27.36 ?  166 PHE D CE2   1 
ATOM   14706 C  CZ    . PHE D 2 187 ? 152.317 105.292 141.500 1.00 27.87 ?  166 PHE D CZ    1 
ATOM   14707 N  N     . LEU D 2 188 ? 149.686 104.023 137.311 1.00 20.78 ?  167 LEU D N     1 
ATOM   14708 C  CA    . LEU D 2 188 ? 150.870 103.426 136.658 1.00 21.78 ?  167 LEU D CA    1 
ATOM   14709 C  C     . LEU D 2 188 ? 151.024 103.752 135.167 1.00 21.91 ?  167 LEU D C     1 
ATOM   14710 O  O     . LEU D 2 188 ? 152.148 103.853 134.675 1.00 22.87 ?  167 LEU D O     1 
ATOM   14711 C  CB    . LEU D 2 188 ? 150.899 101.911 136.854 1.00 22.32 ?  167 LEU D CB    1 
ATOM   14712 C  CG    . LEU D 2 188 ? 151.108 101.316 138.246 1.00 23.33 ?  167 LEU D CG    1 
ATOM   14713 C  CD1   . LEU D 2 188 ? 151.066 99.802  138.139 1.00 22.43 ?  167 LEU D CD1   1 
ATOM   14714 C  CD2   . LEU D 2 188 ? 152.419 101.777 138.898 1.00 25.71 ?  167 LEU D CD2   1 
ATOM   14715 N  N     . PHE D 2 189 ? 149.907 103.895 134.451 1.00 21.56 ?  168 PHE D N     1 
ATOM   14716 C  CA    . PHE D 2 189 ? 149.936 104.279 133.037 1.00 21.86 ?  168 PHE D CA    1 
ATOM   14717 C  C     . PHE D 2 189 ? 150.522 105.689 132.814 1.00 21.87 ?  168 PHE D C     1 
ATOM   14718 O  O     . PHE D 2 189 ? 151.010 106.002 131.725 1.00 21.79 ?  168 PHE D O     1 
ATOM   14719 C  CB    . PHE D 2 189 ? 148.522 104.259 132.428 1.00 21.79 ?  168 PHE D CB    1 
ATOM   14720 C  CG    . PHE D 2 189 ? 148.016 102.886 132.052 1.00 21.88 ?  168 PHE D CG    1 
ATOM   14721 C  CD1   . PHE D 2 189 ? 148.862 101.928 131.488 1.00 21.44 ?  168 PHE D CD1   1 
ATOM   14722 C  CD2   . PHE D 2 189 ? 146.670 102.568 132.234 1.00 22.82 ?  168 PHE D CD2   1 
ATOM   14723 C  CE1   . PHE D 2 189 ? 148.378 100.661 131.137 1.00 22.35 ?  168 PHE D CE1   1 
ATOM   14724 C  CE2   . PHE D 2 189 ? 146.170 101.312 131.888 1.00 22.08 ?  168 PHE D CE2   1 
ATOM   14725 C  CZ    . PHE D 2 189 ? 147.028 100.350 131.348 1.00 22.60 ?  168 PHE D CZ    1 
ATOM   14726 N  N     . TYR D 2 190 ? 150.453 106.543 133.830 1.00 21.91 ?  169 TYR D N     1 
ATOM   14727 C  CA    . TYR D 2 190 ? 150.698 107.976 133.605 1.00 22.52 ?  169 TYR D CA    1 
ATOM   14728 C  C     . TYR D 2 190 ? 152.163 108.390 133.452 1.00 22.75 ?  169 TYR D C     1 
ATOM   14729 O  O     . TYR D 2 190 ? 152.435 109.387 132.796 1.00 21.93 ?  169 TYR D O     1 
ATOM   14730 C  CB    . TYR D 2 190 ? 149.937 108.843 134.612 1.00 22.67 ?  169 TYR D CB    1 
ATOM   14731 C  CG    . TYR D 2 190 ? 148.466 108.906 134.258 1.00 24.77 ?  169 TYR D CG    1 
ATOM   14732 C  CD1   . TYR D 2 190 ? 147.617 107.823 134.511 1.00 25.65 ?  169 TYR D CD1   1 
ATOM   14733 C  CD2   . TYR D 2 190 ? 147.933 110.026 133.626 1.00 25.94 ?  169 TYR D CD2   1 
ATOM   14734 C  CE1   . TYR D 2 190 ? 146.266 107.870 134.153 1.00 26.62 ?  169 TYR D CE1   1 
ATOM   14735 C  CE2   . TYR D 2 190 ? 146.585 110.089 133.281 1.00 26.91 ?  169 TYR D CE2   1 
ATOM   14736 C  CZ    . TYR D 2 190 ? 145.761 109.012 133.542 1.00 27.39 ?  169 TYR D CZ    1 
ATOM   14737 O  OH    . TYR D 2 190 ? 144.428 109.091 133.185 1.00 27.50 ?  169 TYR D OH    1 
ATOM   14738 N  N     . SER D 2 191 ? 153.096 107.616 134.016 1.00 22.74 ?  170 SER D N     1 
ATOM   14739 C  CA    . SER D 2 191 ? 154.517 107.830 133.719 1.00 23.43 ?  170 SER D CA    1 
ATOM   14740 C  C     . SER D 2 191 ? 154.754 107.618 132.223 1.00 23.08 ?  170 SER D C     1 
ATOM   14741 O  O     . SER D 2 191 ? 155.637 108.221 131.638 1.00 23.67 ?  170 SER D O     1 
ATOM   14742 C  CB    . SER D 2 191 ? 155.426 106.907 134.545 1.00 23.39 ?  170 SER D CB    1 
ATOM   14743 O  OG    . SER D 2 191 ? 155.171 105.538 134.267 1.00 24.10 ?  170 SER D OG    1 
ATOM   14744 N  N     . GLY D 2 192 ? 153.926 106.781 131.611 1.00 22.82 ?  171 GLY D N     1 
ATOM   14745 C  CA    . GLY D 2 192 ? 153.982 106.521 130.178 1.00 22.08 ?  171 GLY D CA    1 
ATOM   14746 C  C     . GLY D 2 192 ? 153.217 107.536 129.345 1.00 22.12 ?  171 GLY D C     1 
ATOM   14747 O  O     . GLY D 2 192 ? 153.759 108.079 128.381 1.00 22.86 ?  171 GLY D O     1 
ATOM   14748 N  N     . PHE D 2 193 ? 151.963 107.797 129.712 1.00 21.48 ?  172 PHE D N     1 
ATOM   14749 C  CA    . PHE D 2 193 ? 151.120 108.774 128.997 1.00 21.06 ?  172 PHE D CA    1 
ATOM   14750 C  C     . PHE D 2 193 ? 151.780 110.149 128.894 1.00 21.13 ?  172 PHE D C     1 
ATOM   14751 O  O     . PHE D 2 193 ? 151.522 110.887 127.942 1.00 21.18 ?  172 PHE D O     1 
ATOM   14752 C  CB    . PHE D 2 193 ? 149.766 108.941 129.683 1.00 21.33 ?  172 PHE D CB    1 
ATOM   14753 C  CG    . PHE D 2 193 ? 148.831 107.764 129.526 1.00 20.93 ?  172 PHE D CG    1 
ATOM   14754 C  CD1   . PHE D 2 193 ? 148.870 106.946 128.398 1.00 20.88 ?  172 PHE D CD1   1 
ATOM   14755 C  CD2   . PHE D 2 193 ? 147.871 107.513 130.498 1.00 19.83 ?  172 PHE D CD2   1 
ATOM   14756 C  CE1   . PHE D 2 193 ? 147.981 105.872 128.267 1.00 22.31 ?  172 PHE D CE1   1 
ATOM   14757 C  CE2   . PHE D 2 193 ? 146.970 106.450 130.368 1.00 20.67 ?  172 PHE D CE2   1 
ATOM   14758 C  CZ    . PHE D 2 193 ? 147.026 105.630 129.251 1.00 21.00 ?  172 PHE D CZ    1 
ATOM   14759 N  N     . TYR D 2 194 ? 152.633 110.481 129.865 1.00 20.48 ?  173 TYR D N     1 
ATOM   14760 C  CA    . TYR D 2 194 ? 153.284 111.789 129.911 1.00 20.76 ?  173 TYR D CA    1 
ATOM   14761 C  C     . TYR D 2 194 ? 153.884 112.182 128.556 1.00 20.53 ?  173 TYR D C     1 
ATOM   14762 O  O     . TYR D 2 194 ? 153.646 113.278 128.041 1.00 19.89 ?  173 TYR D O     1 
ATOM   14763 C  CB    . TYR D 2 194 ? 154.370 111.838 131.013 1.00 20.94 ?  173 TYR D CB    1 
ATOM   14764 C  CG    . TYR D 2 194 ? 154.903 113.241 131.243 1.00 21.56 ?  173 TYR D CG    1 
ATOM   14765 C  CD1   . TYR D 2 194 ? 154.436 114.022 132.304 1.00 22.23 ?  173 TYR D CD1   1 
ATOM   14766 C  CD2   . TYR D 2 194 ? 155.858 113.800 130.385 1.00 22.00 ?  173 TYR D CD2   1 
ATOM   14767 C  CE1   . TYR D 2 194 ? 154.905 115.319 132.504 1.00 21.58 ?  173 TYR D CE1   1 
ATOM   14768 C  CE2   . TYR D 2 194 ? 156.333 115.083 130.581 1.00 20.52 ?  173 TYR D CE2   1 
ATOM   14769 C  CZ    . TYR D 2 194 ? 155.854 115.838 131.638 1.00 21.66 ?  173 TYR D CZ    1 
ATOM   14770 O  OH    . TYR D 2 194 ? 156.308 117.123 131.816 1.00 21.37 ?  173 TYR D OH    1 
ATOM   14771 N  N     . TYR D 2 195 ? 154.639 111.270 127.967 1.00 20.77 ?  174 TYR D N     1 
ATOM   14772 C  CA    . TYR D 2 195 ? 155.422 111.619 126.794 1.00 21.12 ?  174 TYR D CA    1 
ATOM   14773 C  C     . TYR D 2 195 ? 154.563 111.910 125.551 1.00 21.49 ?  174 TYR D C     1 
ATOM   14774 O  O     . TYR D 2 195 ? 154.736 112.967 124.937 1.00 21.60 ?  174 TYR D O     1 
ATOM   14775 C  CB    . TYR D 2 195 ? 156.518 110.576 126.555 1.00 21.23 ?  174 TYR D CB    1 
ATOM   14776 C  CG    . TYR D 2 195 ? 157.772 111.107 125.896 1.00 21.77 ?  174 TYR D CG    1 
ATOM   14777 C  CD1   . TYR D 2 195 ? 158.284 112.369 126.215 1.00 23.28 ?  174 TYR D CD1   1 
ATOM   14778 C  CD2   . TYR D 2 195 ? 158.463 110.332 124.968 1.00 22.87 ?  174 TYR D CD2   1 
ATOM   14779 C  CE1   . TYR D 2 195 ? 159.452 112.846 125.602 1.00 23.81 ?  174 TYR D CE1   1 
ATOM   14780 C  CE2   . TYR D 2 195 ? 159.628 110.797 124.363 1.00 24.09 ?  174 TYR D CE2   1 
ATOM   14781 C  CZ    . TYR D 2 195 ? 160.111 112.050 124.678 1.00 23.51 ?  174 TYR D CZ    1 
ATOM   14782 O  OH    . TYR D 2 195 ? 161.262 112.509 124.067 1.00 25.36 ?  174 TYR D OH    1 
ATOM   14783 N  N     . PRO D 2 196 ? 153.631 110.994 125.181 1.00 21.86 ?  175 PRO D N     1 
ATOM   14784 C  CA    . PRO D 2 196 ? 152.714 111.305 124.073 1.00 22.03 ?  175 PRO D CA    1 
ATOM   14785 C  C     . PRO D 2 196 ? 151.921 112.591 124.299 1.00 22.18 ?  175 PRO D C     1 
ATOM   14786 O  O     . PRO D 2 196 ? 151.712 113.345 123.345 1.00 23.00 ?  175 PRO D O     1 
ATOM   14787 C  CB    . PRO D 2 196 ? 151.756 110.107 124.041 1.00 21.50 ?  175 PRO D CB    1 
ATOM   14788 C  CG    . PRO D 2 196 ? 152.456 109.026 124.700 1.00 22.47 ?  175 PRO D CG    1 
ATOM   14789 C  CD    . PRO D 2 196 ? 153.525 109.583 125.593 1.00 20.91 ?  175 PRO D CD    1 
ATOM   14790 N  N     . LEU D 2 197 ? 151.496 112.846 125.538 1.00 21.70 ?  176 LEU D N     1 
ATOM   14791 C  CA    . LEU D 2 197 ? 150.796 114.096 125.867 1.00 22.40 ?  176 LEU D CA    1 
ATOM   14792 C  C     . LEU D 2 197 ? 151.696 115.326 125.725 1.00 22.58 ?  176 LEU D C     1 
ATOM   14793 O  O     . LEU D 2 197 ? 151.241 116.391 125.287 1.00 22.15 ?  176 LEU D O     1 
ATOM   14794 C  CB    . LEU D 2 197 ? 150.232 114.055 127.281 1.00 22.15 ?  176 LEU D CB    1 
ATOM   14795 C  CG    . LEU D 2 197 ? 149.036 113.144 127.587 1.00 23.08 ?  176 LEU D CG    1 
ATOM   14796 C  CD1   . LEU D 2 197 ? 148.910 113.012 129.096 1.00 21.62 ?  176 LEU D CD1   1 
ATOM   14797 C  CD2   . LEU D 2 197 ? 147.738 113.697 126.963 1.00 21.94 ?  176 LEU D CD2   1 
ATOM   14798 N  N     . TYR D 2 198 ? 152.964 115.161 126.108 1.00 22.76 ?  177 TYR D N     1 
ATOM   14799 C  CA    . TYR D 2 198 ? 153.993 116.193 125.960 1.00 23.23 ?  177 TYR D CA    1 
ATOM   14800 C  C     . TYR D 2 198 ? 154.194 116.564 124.491 1.00 23.91 ?  177 TYR D C     1 
ATOM   14801 O  O     . TYR D 2 198 ? 154.220 117.755 124.145 1.00 24.20 ?  177 TYR D O     1 
ATOM   14802 C  CB    . TYR D 2 198 ? 155.306 115.730 126.613 1.00 23.19 ?  177 TYR D CB    1 
ATOM   14803 C  CG    . TYR D 2 198 ? 156.452 116.722 126.571 1.00 23.52 ?  177 TYR D CG    1 
ATOM   14804 C  CD1   . TYR D 2 198 ? 156.395 117.911 127.284 1.00 24.85 ?  177 TYR D CD1   1 
ATOM   14805 C  CD2   . TYR D 2 198 ? 157.619 116.442 125.847 1.00 25.30 ?  177 TYR D CD2   1 
ATOM   14806 C  CE1   . TYR D 2 198 ? 157.456 118.820 127.264 1.00 26.05 ?  177 TYR D CE1   1 
ATOM   14807 C  CE2   . TYR D 2 198 ? 158.694 117.347 125.824 1.00 26.38 ?  177 TYR D CE2   1 
ATOM   14808 C  CZ    . TYR D 2 198 ? 158.598 118.527 126.537 1.00 26.68 ?  177 TYR D CZ    1 
ATOM   14809 O  OH    . TYR D 2 198 ? 159.638 119.430 126.534 1.00 30.01 ?  177 TYR D OH    1 
ATOM   14810 N  N     . PHE D 2 199 ? 154.323 115.563 123.620 1.00 24.84 ?  178 PHE D N     1 
ATOM   14811 C  CA    . PHE D 2 199 ? 154.389 115.838 122.181 1.00 25.81 ?  178 PHE D CA    1 
ATOM   14812 C  C     . PHE D 2 199 ? 153.102 116.439 121.629 1.00 26.23 ?  178 PHE D C     1 
ATOM   14813 O  O     . PHE D 2 199 ? 153.141 117.408 120.871 1.00 26.58 ?  178 PHE D O     1 
ATOM   14814 C  CB    . PHE D 2 199 ? 154.773 114.593 121.393 1.00 26.08 ?  178 PHE D CB    1 
ATOM   14815 C  CG    . PHE D 2 199 ? 156.228 114.245 121.496 1.00 28.71 ?  178 PHE D CG    1 
ATOM   14816 C  CD1   . PHE D 2 199 ? 157.202 115.224 121.348 1.00 32.03 ?  178 PHE D CD1   1 
ATOM   14817 C  CD2   . PHE D 2 199 ? 156.630 112.944 121.745 1.00 31.77 ?  178 PHE D CD2   1 
ATOM   14818 C  CE1   . PHE D 2 199 ? 158.567 114.913 121.455 1.00 32.29 ?  178 PHE D CE1   1 
ATOM   14819 C  CE2   . PHE D 2 199 ? 157.989 112.624 121.843 1.00 32.72 ?  178 PHE D CE2   1 
ATOM   14820 C  CZ    . PHE D 2 199 ? 158.953 113.616 121.696 1.00 31.91 ?  178 PHE D CZ    1 
ATOM   14821 N  N     . TYR D 2 200 ? 151.976 115.850 122.022 1.00 26.46 ?  179 TYR D N     1 
ATOM   14822 C  CA    . TYR D 2 200 ? 150.633 116.270 121.591 1.00 27.43 ?  179 TYR D CA    1 
ATOM   14823 C  C     . TYR D 2 200 ? 150.387 117.737 121.929 1.00 27.68 ?  179 TYR D C     1 
ATOM   14824 O  O     . TYR D 2 200 ? 149.807 118.472 121.131 1.00 28.71 ?  179 TYR D O     1 
ATOM   14825 C  CB    . TYR D 2 200 ? 149.608 115.392 122.300 1.00 27.27 ?  179 TYR D CB    1 
ATOM   14826 C  CG    . TYR D 2 200 ? 148.207 115.359 121.740 1.00 28.90 ?  179 TYR D CG    1 
ATOM   14827 C  CD1   . TYR D 2 200 ? 147.973 115.177 120.383 1.00 29.00 ?  179 TYR D CD1   1 
ATOM   14828 C  CD2   . TYR D 2 200 ? 147.107 115.442 122.598 1.00 30.14 ?  179 TYR D CD2   1 
ATOM   14829 C  CE1   . TYR D 2 200 ? 146.675 115.117 119.881 1.00 31.26 ?  179 TYR D CE1   1 
ATOM   14830 C  CE2   . TYR D 2 200 ? 145.811 115.372 122.113 1.00 31.86 ?  179 TYR D CE2   1 
ATOM   14831 C  CZ    . TYR D 2 200 ? 145.600 115.215 120.753 1.00 32.51 ?  179 TYR D CZ    1 
ATOM   14832 O  OH    . TYR D 2 200 ? 144.315 115.150 120.272 1.00 33.77 ?  179 TYR D OH    1 
ATOM   14833 N  N     . GLY D 2 201 ? 150.835 118.156 123.111 1.00 27.68 ?  180 GLY D N     1 
ATOM   14834 C  CA    . GLY D 2 201 ? 150.722 119.547 123.536 1.00 28.02 ?  180 GLY D CA    1 
ATOM   14835 C  C     . GLY D 2 201 ? 151.626 120.526 122.792 1.00 28.60 ?  180 GLY D C     1 
ATOM   14836 O  O     . GLY D 2 201 ? 151.428 121.730 122.888 1.00 28.44 ?  180 GLY D O     1 
ATOM   14837 N  N     . GLN D 2 202 ? 152.621 120.001 122.071 1.00 29.34 ?  181 GLN D N     1 
ATOM   14838 C  CA    . GLN D 2 202 ? 153.577 120.795 121.278 1.00 30.39 ?  181 GLN D CA    1 
ATOM   14839 C  C     . GLN D 2 202 ? 153.279 120.787 119.779 1.00 30.55 ?  181 GLN D C     1 
ATOM   14840 O  O     . GLN D 2 202 ? 153.998 121.427 119.004 1.00 31.23 ?  181 GLN D O     1 
ATOM   14841 C  CB    . GLN D 2 202 ? 154.984 120.206 121.395 1.00 30.31 ?  181 GLN D CB    1 
ATOM   14842 C  CG    . GLN D 2 202 ? 155.671 120.294 122.705 1.00 32.40 ?  181 GLN D CG    1 
ATOM   14843 C  CD    . GLN D 2 202 ? 157.040 119.651 122.623 1.00 33.85 ?  181 GLN D CD    1 
ATOM   14844 O  OE1   . GLN D 2 202 ? 157.258 118.551 123.125 1.00 33.94 ?  181 GLN D OE1   1 
ATOM   14845 N  NE2   . GLN D 2 202 ? 157.960 120.317 121.946 1.00 34.92 ?  181 GLN D NE2   1 
ATOM   14846 N  N     . GLY D 2 203 ? 152.282 120.019 119.356 1.00 30.57 ?  182 GLY D N     1 
ATOM   14847 C  CA    . GLY D 2 203 ? 151.968 119.895 117.931 1.00 30.83 ?  182 GLY D CA    1 
ATOM   14848 C  C     . GLY D 2 203 ? 152.727 118.785 117.219 1.00 30.80 ?  182 GLY D C     1 
ATOM   14849 O  O     . GLY D 2 203 ? 152.706 118.705 115.988 1.00 30.86 ?  182 GLY D O     1 
ATOM   14850 N  N     . LYS D 2 204 ? 153.390 117.924 117.992 1.00 30.14 ?  183 LYS D N     1 
ATOM   14851 C  CA    . LYS D 2 204 ? 154.131 116.789 117.433 1.00 30.35 ?  183 LYS D CA    1 
ATOM   14852 C  C     . LYS D 2 204 ? 153.384 115.471 117.629 1.00 29.52 ?  183 LYS D C     1 
ATOM   14853 O  O     . LYS D 2 204 ? 152.699 115.291 118.632 1.00 28.60 ?  183 LYS D O     1 
ATOM   14854 C  CB    . LYS D 2 204 ? 155.524 116.703 118.056 1.00 30.76 ?  183 LYS D CB    1 
ATOM   14855 C  CG    . LYS D 2 204 ? 156.426 117.890 117.704 1.00 32.95 ?  183 LYS D CG    1 
ATOM   14856 C  CD    . LYS D 2 204 ? 157.659 117.877 118.574 1.00 36.37 ?  183 LYS D CD    1 
ATOM   14857 C  CE    . LYS D 2 204 ? 158.591 119.035 118.264 1.00 38.47 ?  183 LYS D CE    1 
ATOM   14858 N  NZ    . LYS D 2 204 ? 159.640 119.088 119.326 1.00 40.21 1  183 LYS D NZ    1 
ATOM   14859 N  N     . LEU D 2 205 ? 153.534 114.555 116.668 1.00 29.47 ?  184 LEU D N     1 
ATOM   14860 C  CA    . LEU D 2 205 ? 152.875 113.240 116.702 1.00 29.06 ?  184 LEU D CA    1 
ATOM   14861 C  C     . LEU D 2 205 ? 151.402 113.349 117.150 1.00 28.96 ?  184 LEU D C     1 
ATOM   14862 O  O     . LEU D 2 205 ? 150.962 112.696 118.105 1.00 27.68 ?  184 LEU D O     1 
ATOM   14863 C  CB    . LEU D 2 205 ? 153.658 112.251 117.580 1.00 28.63 ?  184 LEU D CB    1 
ATOM   14864 C  CG    . LEU D 2 205 ? 155.134 111.997 117.238 1.00 29.00 ?  184 LEU D CG    1 
ATOM   14865 C  CD1   . LEU D 2 205 ? 155.762 111.052 118.265 1.00 28.90 ?  184 LEU D CD1   1 
ATOM   14866 C  CD2   . LEU D 2 205 ? 155.293 111.429 115.834 1.00 28.67 ?  184 LEU D CD2   1 
ATOM   14867 N  N     . MET D 2 206 ? 150.666 114.191 116.430 1.00 29.02 ?  185 MET D N     1 
ATOM   14868 C  CA    . MET D 2 206 ? 149.281 114.520 116.729 1.00 29.72 ?  185 MET D CA    1 
ATOM   14869 C  C     . MET D 2 206 ? 148.277 113.389 116.527 1.00 29.54 ?  185 MET D C     1 
ATOM   14870 O  O     . MET D 2 206 ? 147.286 113.319 117.250 1.00 29.47 ?  185 MET D O     1 
ATOM   14871 C  CB    . MET D 2 206 ? 148.852 115.743 115.908 1.00 30.69 ?  185 MET D CB    1 
ATOM   14872 C  CG    . MET D 2 206 ? 149.712 116.968 116.177 1.00 32.03 ?  185 MET D CG    1 
ATOM   14873 S  SD    . MET D 2 206 ? 149.672 117.430 117.918 1.00 36.63 ?  185 MET D SD    1 
ATOM   14874 C  CE    . MET D 2 206 ? 148.190 118.422 117.958 1.00 33.80 ?  185 MET D CE    1 
ATOM   14875 N  N     . GLN D 2 207 ? 148.516 112.530 115.538 1.00 29.56 ?  186 GLN D N     1 
ATOM   14876 C  CA    . GLN D 2 207 ? 147.602 111.422 115.239 1.00 29.17 ?  186 GLN D CA    1 
ATOM   14877 C  C     . GLN D 2 207 ? 147.693 110.345 116.316 1.00 28.26 ?  186 GLN D C     1 
ATOM   14878 O  O     . GLN D 2 207 ? 146.672 109.888 116.822 1.00 27.98 ?  186 GLN D O     1 
ATOM   14879 C  CB    . GLN D 2 207 ? 147.879 110.822 113.852 1.00 29.80 ?  186 GLN D CB    1 
ATOM   14880 C  CG    . GLN D 2 207 ? 147.868 111.833 112.706 1.00 31.75 ?  186 GLN D CG    1 
ATOM   14881 C  CD    . GLN D 2 207 ? 146.610 112.679 112.700 1.00 34.93 ?  186 GLN D CD    1 
ATOM   14882 O  OE1   . GLN D 2 207 ? 145.515 112.196 112.383 1.00 36.91 ?  186 GLN D OE1   1 
ATOM   14883 N  NE2   . GLN D 2 207 ? 146.758 113.948 113.064 1.00 36.09 ?  186 GLN D NE2   1 
ATOM   14884 N  N     . SER D 2 208 ? 148.914 109.943 116.665 0.50 27.75 ?  187 SER D N     1 
ATOM   14885 C  CA    . SER D 2 208 ? 149.108 108.958 117.723 0.50 27.12 ?  187 SER D CA    1 
ATOM   14886 C  C     . SER D 2 208 ? 148.757 109.550 119.085 0.50 26.72 ?  187 SER D C     1 
ATOM   14887 O  O     . SER D 2 208 ? 148.282 108.832 119.963 0.50 26.30 ?  187 SER D O     1 
ATOM   14888 C  CB    . SER D 2 208 ? 150.537 108.414 117.720 0.50 26.88 ?  187 SER D CB    1 
ATOM   14889 O  OG    . SER D 2 208 ? 151.472 109.470 117.737 0.50 26.59 ?  187 SER D OG    1 
ATOM   14890 N  N     . GLY D 2 209 ? 148.989 110.854 119.247 1.00 26.64 ?  188 GLY D N     1 
ATOM   14891 C  CA    . GLY D 2 209 ? 148.604 111.574 120.478 1.00 26.43 ?  188 GLY D CA    1 
ATOM   14892 C  C     . GLY D 2 209 ? 147.095 111.628 120.676 1.00 26.66 ?  188 GLY D C     1 
ATOM   14893 O  O     . GLY D 2 209 ? 146.601 111.553 121.801 1.00 26.57 ?  188 GLY D O     1 
ATOM   14894 N  N     . GLU D 2 210 ? 146.355 111.766 119.579 1.00 27.42 ?  189 GLU D N     1 
ATOM   14895 C  CA    . GLU D 2 210 ? 144.895 111.716 119.631 1.00 27.73 ?  189 GLU D CA    1 
ATOM   14896 C  C     . GLU D 2 210 ? 144.436 110.320 120.076 1.00 27.04 ?  189 GLU D C     1 
ATOM   14897 O  O     . GLU D 2 210 ? 143.579 110.190 120.951 1.00 26.57 ?  189 GLU D O     1 
ATOM   14898 C  CB    . GLU D 2 210 ? 144.276 112.106 118.277 1.00 28.28 ?  189 GLU D CB    1 
ATOM   14899 C  CG    . GLU D 2 210 ? 142.740 112.167 118.302 1.00 30.71 ?  189 GLU D CG    1 
ATOM   14900 C  CD    . GLU D 2 210 ? 142.116 112.801 117.060 1.00 35.43 ?  189 GLU D CD    1 
ATOM   14901 O  OE1   . GLU D 2 210 ? 142.835 113.072 116.066 1.00 36.89 ?  189 GLU D OE1   1 
ATOM   14902 O  OE2   . GLU D 2 210 ? 140.886 113.037 117.089 1.00 37.04 -1 189 GLU D OE2   1 
ATOM   14903 N  N     . ILE D 2 211 ? 145.020 109.286 119.480 1.00 26.80 ?  190 ILE D N     1 
ATOM   14904 C  CA    . ILE D 2 211 ? 144.748 107.912 119.892 1.00 26.92 ?  190 ILE D CA    1 
ATOM   14905 C  C     . ILE D 2 211 ? 145.038 107.715 121.374 1.00 26.45 ?  190 ILE D C     1 
ATOM   14906 O  O     . ILE D 2 211 ? 144.208 107.161 122.092 1.00 26.65 ?  190 ILE D O     1 
ATOM   14907 C  CB    . ILE D 2 211 ? 145.514 106.879 119.028 1.00 27.00 ?  190 ILE D CB    1 
ATOM   14908 C  CG1   . ILE D 2 211 ? 144.921 106.851 117.614 1.00 28.77 ?  190 ILE D CG1   1 
ATOM   14909 C  CG2   . ILE D 2 211 ? 145.446 105.479 119.661 1.00 26.82 ?  190 ILE D CG2   1 
ATOM   14910 C  CD1   . ILE D 2 211 ? 145.680 105.989 116.614 1.00 30.88 ?  190 ILE D CD1   1 
ATOM   14911 N  N     . ILE D 2 212 ? 146.196 108.189 121.841 1.00 26.49 ?  191 ILE D N     1 
ATOM   14912 C  CA    . ILE D 2 212 ? 146.578 108.003 123.242 1.00 25.73 ?  191 ILE D CA    1 
ATOM   14913 C  C     . ILE D 2 212 ? 145.592 108.712 124.173 1.00 25.48 ?  191 ILE D C     1 
ATOM   14914 O  O     . ILE D 2 212 ? 145.228 108.182 125.226 1.00 24.95 ?  191 ILE D O     1 
ATOM   14915 C  CB    . ILE D 2 212 ? 148.043 108.452 123.524 1.00 26.44 ?  191 ILE D CB    1 
ATOM   14916 C  CG1   . ILE D 2 212 ? 149.041 107.560 122.774 1.00 26.71 ?  191 ILE D CG1   1 
ATOM   14917 C  CG2   . ILE D 2 212 ? 148.342 108.462 125.039 1.00 26.01 ?  191 ILE D CG2   1 
ATOM   14918 C  CD1   . ILE D 2 212 ? 149.038 106.092 123.158 1.00 30.50 ?  191 ILE D CD1   1 
ATOM   14919 N  N     . ASN D 2 213 ? 145.147 109.897 123.764 1.00 24.79 ?  192 ASN D N     1 
ATOM   14920 C  CA    . ASN D 2 213 ? 144.175 110.652 124.542 1.00 24.80 ?  192 ASN D CA    1 
ATOM   14921 C  C     . ASN D 2 213 ? 142.828 109.913 124.685 1.00 24.44 ?  192 ASN D C     1 
ATOM   14922 O  O     . ASN D 2 213 ? 142.166 110.004 125.725 1.00 23.25 ?  192 ASN D O     1 
ATOM   14923 C  CB    . ASN D 2 213 ? 143.984 112.044 123.938 1.00 25.68 ?  192 ASN D CB    1 
ATOM   14924 C  CG    . ASN D 2 213 ? 143.799 113.119 124.993 1.00 27.89 ?  192 ASN D CG    1 
ATOM   14925 O  OD1   . ASN D 2 213 ? 144.321 113.023 126.100 1.00 31.05 ?  192 ASN D OD1   1 
ATOM   14926 N  ND2   . ASN D 2 213 ? 143.052 114.158 124.645 1.00 31.70 ?  192 ASN D ND2   1 
ATOM   14927 N  N     . LEU D 2 214 ? 142.437 109.175 123.645 1.00 23.60 ?  193 LEU D N     1 
ATOM   14928 C  CA    . LEU D 2 214 ? 141.197 108.398 123.688 1.00 23.84 ?  193 LEU D CA    1 
ATOM   14929 C  C     . LEU D 2 214 ? 141.360 107.203 124.610 1.00 23.48 ?  193 LEU D C     1 
ATOM   14930 O  O     . LEU D 2 214 ? 140.455 106.885 125.387 1.00 24.12 ?  193 LEU D O     1 
ATOM   14931 C  CB    . LEU D 2 214 ? 140.798 107.937 122.287 1.00 23.71 ?  193 LEU D CB    1 
ATOM   14932 C  CG    . LEU D 2 214 ? 140.240 109.030 121.365 1.00 25.29 ?  193 LEU D CG    1 
ATOM   14933 C  CD1   . LEU D 2 214 ? 140.020 108.479 119.956 1.00 25.41 ?  193 LEU D CD1   1 
ATOM   14934 C  CD2   . LEU D 2 214 ? 138.950 109.620 121.910 1.00 25.80 ?  193 LEU D CD2   1 
ATOM   14935 N  N     . ILE D 2 215 ? 142.522 106.555 124.524 1.00 22.89 ?  194 ILE D N     1 
ATOM   14936 C  CA    . ILE D 2 215 ? 142.853 105.435 125.393 1.00 22.25 ?  194 ILE D CA    1 
ATOM   14937 C  C     . ILE D 2 215 ? 142.840 105.908 126.843 1.00 22.55 ?  194 ILE D C     1 
ATOM   14938 O  O     . ILE D 2 215 ? 142.191 105.297 127.704 1.00 22.53 ?  194 ILE D O     1 
ATOM   14939 C  CB    . ILE D 2 215 ? 144.233 104.835 125.054 1.00 22.37 ?  194 ILE D CB    1 
ATOM   14940 C  CG1   . ILE D 2 215 ? 144.202 104.177 123.668 1.00 21.89 ?  194 ILE D CG1   1 
ATOM   14941 C  CG2   . ILE D 2 215 ? 144.676 103.844 126.150 1.00 20.25 ?  194 ILE D CG2   1 
ATOM   14942 C  CD1   . ILE D 2 215 ? 145.536 103.559 123.230 1.00 20.48 ?  194 ILE D CD1   1 
ATOM   14943 N  N     . LEU D 2 216 ? 143.544 107.005 127.103 1.00 22.35 ?  195 LEU D N     1 
ATOM   14944 C  CA    . LEU D 2 216 ? 143.662 107.542 128.456 1.00 22.51 ?  195 LEU D CA    1 
ATOM   14945 C  C     . LEU D 2 216 ? 142.278 107.866 129.026 1.00 22.30 ?  195 LEU D C     1 
ATOM   14946 O  O     . LEU D 2 216 ? 142.010 107.586 130.201 1.00 21.62 ?  195 LEU D O     1 
ATOM   14947 C  CB    . LEU D 2 216 ? 144.556 108.791 128.438 1.00 23.06 ?  195 LEU D CB    1 
ATOM   14948 C  CG    . LEU D 2 216 ? 144.800 109.682 129.666 1.00 23.98 ?  195 LEU D CG    1 
ATOM   14949 C  CD1   . LEU D 2 216 ? 146.000 110.548 129.386 1.00 24.44 ?  195 LEU D CD1   1 
ATOM   14950 C  CD2   . LEU D 2 216 ? 143.588 110.569 129.996 1.00 25.00 ?  195 LEU D CD2   1 
ATOM   14951 N  N     . ARG D 2 217 ? 141.414 108.458 128.193 1.00 21.64 ?  196 ARG D N     1 
ATOM   14952 C  CA    . ARG D 2 217 ? 140.040 108.778 128.599 1.00 22.49 ?  196 ARG D CA    1 
ATOM   14953 C  C     . ARG D 2 217 ? 139.252 107.508 129.003 1.00 21.56 ?  196 ARG D C     1 
ATOM   14954 O  O     . ARG D 2 217 ? 138.495 107.540 129.964 1.00 21.32 ?  196 ARG D O     1 
ATOM   14955 C  CB    . ARG D 2 217 ? 139.295 109.590 127.521 1.00 23.07 ?  196 ARG D CB    1 
ATOM   14956 C  CG    . ARG D 2 217 ? 137.908 110.104 127.966 1.00 25.64 ?  196 ARG D CG    1 
ATOM   14957 C  CD    . ARG D 2 217 ? 137.092 110.717 126.814 1.00 32.11 ?  196 ARG D CD    1 
ATOM   14958 N  NE    . ARG D 2 217 ? 136.862 109.762 125.721 1.00 35.06 ?  196 ARG D NE    1 
ATOM   14959 C  CZ    . ARG D 2 217 ? 136.018 109.951 124.713 1.00 37.65 ?  196 ARG D CZ    1 
ATOM   14960 N  NH1   . ARG D 2 217 ? 135.282 111.056 124.650 1.00 40.20 1  196 ARG D NH1   1 
ATOM   14961 N  NH2   . ARG D 2 217 ? 135.894 109.025 123.766 1.00 38.20 ?  196 ARG D NH2   1 
ATOM   14962 N  N     . ASP D 2 218 ? 139.439 106.403 128.278 1.00 21.34 ?  197 ASP D N     1 
ATOM   14963 C  CA    . ASP D 2 218 ? 138.877 105.108 128.690 1.00 21.09 ?  197 ASP D CA    1 
ATOM   14964 C  C     . ASP D 2 218 ? 139.469 104.623 130.029 1.00 20.65 ?  197 ASP D C     1 
ATOM   14965 O  O     . ASP D 2 218 ? 138.723 104.201 130.916 1.00 20.16 ?  197 ASP D O     1 
ATOM   14966 C  CB    . ASP D 2 218 ? 139.091 104.033 127.613 1.00 21.58 ?  197 ASP D CB    1 
ATOM   14967 C  CG    . ASP D 2 218 ? 138.302 104.301 126.331 1.00 22.60 ?  197 ASP D CG    1 
ATOM   14968 O  OD1   . ASP D 2 218 ? 137.276 105.019 126.369 1.00 24.72 ?  197 ASP D OD1   1 
ATOM   14969 O  OD2   . ASP D 2 218 ? 138.728 103.789 125.271 1.00 22.64 -1 197 ASP D OD2   1 
ATOM   14970 N  N     . GLU D 2 219 ? 140.793 104.673 130.184 1.00 20.59 ?  198 GLU D N     1 
ATOM   14971 C  CA    . GLU D 2 219 ? 141.414 104.180 131.434 1.00 20.66 ?  198 GLU D CA    1 
ATOM   14972 C  C     . GLU D 2 219 ? 140.950 104.983 132.653 1.00 20.45 ?  198 GLU D C     1 
ATOM   14973 O  O     . GLU D 2 219 ? 140.766 104.422 133.737 1.00 20.59 ?  198 GLU D O     1 
ATOM   14974 C  CB    . GLU D 2 219 ? 142.949 104.157 131.363 1.00 20.55 ?  198 GLU D CB    1 
ATOM   14975 C  CG    . GLU D 2 219 ? 143.571 103.640 130.028 1.00 21.99 ?  198 GLU D CG    1 
ATOM   14976 C  CD    . GLU D 2 219 ? 143.215 102.196 129.652 1.00 24.00 ?  198 GLU D CD    1 
ATOM   14977 O  OE1   . GLU D 2 219 ? 142.174 101.655 130.081 1.00 25.06 ?  198 GLU D OE1   1 
ATOM   14978 O  OE2   . GLU D 2 219 ? 143.980 101.593 128.880 1.00 24.49 -1 198 GLU D OE2   1 
ATOM   14979 N  N     . ALA D 2 220 ? 140.748 106.285 132.466 1.00 20.47 ?  199 ALA D N     1 
ATOM   14980 C  CA    . ALA D 2 220 ? 140.222 107.154 133.540 1.00 21.10 ?  199 ALA D CA    1 
ATOM   14981 C  C     . ALA D 2 220 ? 138.877 106.662 134.068 1.00 21.34 ?  199 ALA D C     1 
ATOM   14982 O  O     . ALA D 2 220 ? 138.732 106.442 135.269 1.00 21.19 ?  199 ALA D O     1 
ATOM   14983 C  CB    . ALA D 2 220 ? 140.134 108.612 133.085 1.00 21.09 ?  199 ALA D CB    1 
ATOM   14984 N  N     . ILE D 2 221 ? 137.909 106.463 133.171 1.00 21.31 ?  200 ILE D N     1 
ATOM   14985 C  CA    . ILE D 2 221 ? 136.618 105.913 133.577 1.00 21.80 ?  200 ILE D CA    1 
ATOM   14986 C  C     . ILE D 2 221 ? 136.705 104.470 134.118 1.00 20.90 ?  200 ILE D C     1 
ATOM   14987 O  O     . ILE D 2 221 ? 135.992 104.125 135.059 1.00 20.54 ?  200 ILE D O     1 
ATOM   14988 C  CB    . ILE D 2 221 ? 135.513 106.084 132.495 1.00 22.75 ?  200 ILE D CB    1 
ATOM   14989 C  CG1   . ILE D 2 221 ? 134.140 105.882 133.128 1.00 24.63 ?  200 ILE D CG1   1 
ATOM   14990 C  CG2   . ILE D 2 221 ? 135.694 105.102 131.340 1.00 23.38 ?  200 ILE D CG2   1 
ATOM   14991 C  CD1   . ILE D 2 221 ? 133.015 106.508 132.356 1.00 26.91 ?  200 ILE D CD1   1 
ATOM   14992 N  N     . HIS D 2 222 ? 137.599 103.645 133.560 1.00 20.31 ?  201 HIS D N     1 
ATOM   14993 C  CA    . HIS D 2 222 ? 137.813 102.301 134.105 1.00 20.25 ?  201 HIS D CA    1 
ATOM   14994 C  C     . HIS D 2 222 ? 138.250 102.384 135.565 1.00 20.51 ?  201 HIS D C     1 
ATOM   14995 O  O     . HIS D 2 222 ? 137.680 101.713 136.435 1.00 20.99 ?  201 HIS D O     1 
ATOM   14996 C  CB    . HIS D 2 222 ? 138.847 101.505 133.300 1.00 19.79 ?  201 HIS D CB    1 
ATOM   14997 C  CG    . HIS D 2 222 ? 138.469 101.253 131.873 1.00 19.25 ?  201 HIS D CG    1 
ATOM   14998 N  ND1   . HIS D 2 222 ? 139.348 100.694 130.970 1.00 18.35 ?  201 HIS D ND1   1 
ATOM   14999 C  CD2   . HIS D 2 222 ? 137.323 101.491 131.186 1.00 17.64 ?  201 HIS D CD2   1 
ATOM   15000 C  CE1   . HIS D 2 222 ? 138.760 100.583 129.792 1.00 18.28 ?  201 HIS D CE1   1 
ATOM   15001 N  NE2   . HIS D 2 222 ? 137.533 101.067 129.894 1.00 20.01 ?  201 HIS D NE2   1 
ATOM   15002 N  N     . GLY D 2 223 ? 139.248 103.228 135.833 1.00 20.33 ?  202 GLY D N     1 
ATOM   15003 C  CA    . GLY D 2 223 ? 139.746 103.451 137.197 1.00 19.94 ?  202 GLY D CA    1 
ATOM   15004 C  C     . GLY D 2 223 ? 138.678 103.942 138.167 1.00 19.80 ?  202 GLY D C     1 
ATOM   15005 O  O     . GLY D 2 223 ? 138.579 103.438 139.284 1.00 19.96 ?  202 GLY D O     1 
ATOM   15006 N  N     . VAL D 2 224 ? 137.857 104.903 137.736 1.00 19.49 ?  203 VAL D N     1 
ATOM   15007 C  CA    . VAL D 2 224 ? 136.768 105.418 138.582 1.00 18.88 ?  203 VAL D CA    1 
ATOM   15008 C  C     . VAL D 2 224 ? 135.735 104.330 138.908 1.00 18.55 ?  203 VAL D C     1 
ATOM   15009 O  O     . VAL D 2 224 ? 135.306 104.184 140.064 1.00 17.65 ?  203 VAL D O     1 
ATOM   15010 C  CB    . VAL D 2 224 ? 136.064 106.674 137.949 1.00 19.22 ?  203 VAL D CB    1 
ATOM   15011 C  CG1   . VAL D 2 224 ? 134.910 107.169 138.845 1.00 18.51 ?  203 VAL D CG1   1 
ATOM   15012 C  CG2   . VAL D 2 224 ? 137.080 107.812 137.718 1.00 19.69 ?  203 VAL D CG2   1 
ATOM   15013 N  N     . TYR D 2 225 ? 135.362 103.553 137.894 1.00 18.17 ?  204 TYR D N     1 
ATOM   15014 C  CA    . TYR D 2 225 ? 134.359 102.496 138.048 1.00 18.76 ?  204 TYR D CA    1 
ATOM   15015 C  C     . TYR D 2 225 ? 134.841 101.378 138.989 1.00 18.93 ?  204 TYR D C     1 
ATOM   15016 O  O     . TYR D 2 225 ? 134.155 101.022 139.957 1.00 18.77 ?  204 TYR D O     1 
ATOM   15017 C  CB    . TYR D 2 225 ? 133.947 101.914 136.681 1.00 18.96 ?  204 TYR D CB    1 
ATOM   15018 C  CG    . TYR D 2 225 ? 132.808 100.910 136.812 1.00 20.06 ?  204 TYR D CG    1 
ATOM   15019 C  CD1   . TYR D 2 225 ? 131.534 101.328 137.222 1.00 21.79 ?  204 TYR D CD1   1 
ATOM   15020 C  CD2   . TYR D 2 225 ? 133.008 99.549  136.561 1.00 19.51 ?  204 TYR D CD2   1 
ATOM   15021 C  CE1   . TYR D 2 225 ? 130.489 100.415 137.374 1.00 20.38 ?  204 TYR D CE1   1 
ATOM   15022 C  CE2   . TYR D 2 225 ? 131.953 98.621  136.706 1.00 19.38 ?  204 TYR D CE2   1 
ATOM   15023 C  CZ    . TYR D 2 225 ? 130.702 99.072  137.117 1.00 20.84 ?  204 TYR D CZ    1 
ATOM   15024 O  OH    . TYR D 2 225 ? 129.655 98.194  137.284 1.00 20.77 ?  204 TYR D OH    1 
ATOM   15025 N  N     . VAL D 2 226 ? 136.024 100.833 138.712 1.00 18.76 ?  205 VAL D N     1 
ATOM   15026 C  CA    . VAL D 2 226 ? 136.582 99.792  139.572 1.00 18.85 ?  205 VAL D CA    1 
ATOM   15027 C  C     . VAL D 2 226 ? 136.769 100.331 140.989 1.00 19.19 ?  205 VAL D C     1 
ATOM   15028 O  O     . VAL D 2 226 ? 136.549 99.603  141.959 1.00 19.87 ?  205 VAL D O     1 
ATOM   15029 C  CB    . VAL D 2 226 ? 137.886 99.216  139.005 1.00 19.28 ?  205 VAL D CB    1 
ATOM   15030 C  CG1   . VAL D 2 226 ? 138.492 98.160  139.968 1.00 18.22 ?  205 VAL D CG1   1 
ATOM   15031 C  CG2   . VAL D 2 226 ? 137.603 98.605  137.622 1.00 18.40 ?  205 VAL D CG2   1 
ATOM   15032 N  N     . GLY D 2 227 ? 137.143 101.608 141.098 1.00 18.53 ?  206 GLY D N     1 
ATOM   15033 C  CA    . GLY D 2 227 ? 137.239 102.288 142.403 1.00 18.74 ?  206 GLY D CA    1 
ATOM   15034 C  C     . GLY D 2 227 ? 135.954 102.265 143.212 1.00 19.17 ?  206 GLY D C     1 
ATOM   15035 O  O     . GLY D 2 227 ? 135.977 102.067 144.435 1.00 18.66 ?  206 GLY D O     1 
ATOM   15036 N  N     . LEU D 2 228 ? 134.827 102.485 142.538 1.00 19.00 ?  207 LEU D N     1 
ATOM   15037 C  CA    . LEU D 2 228 ? 133.526 102.446 143.208 1.00 19.73 ?  207 LEU D CA    1 
ATOM   15038 C  C     . LEU D 2 228 ? 133.189 101.023 143.675 1.00 19.76 ?  207 LEU D C     1 
ATOM   15039 O  O     . LEU D 2 228 ? 132.671 100.840 144.776 1.00 20.07 ?  207 LEU D O     1 
ATOM   15040 C  CB    . LEU D 2 228 ? 132.430 103.022 142.308 1.00 19.36 ?  207 LEU D CB    1 
ATOM   15041 C  CG    . LEU D 2 228 ? 132.509 104.537 142.061 1.00 20.50 ?  207 LEU D CG    1 
ATOM   15042 C  CD1   . LEU D 2 228 ? 131.554 104.950 140.957 1.00 19.87 ?  207 LEU D CD1   1 
ATOM   15043 C  CD2   . LEU D 2 228 ? 132.223 105.344 143.361 1.00 22.38 ?  207 LEU D CD2   1 
ATOM   15044 N  N     . LEU D 2 229 ? 133.523 100.022 142.862 1.00 19.27 ?  208 LEU D N     1 
ATOM   15045 C  CA    . LEU D 2 229 ? 133.349 98.614  143.266 1.00 19.47 ?  208 LEU D CA    1 
ATOM   15046 C  C     . LEU D 2 229 ? 134.211 98.232  144.476 1.00 19.67 ?  208 LEU D C     1 
ATOM   15047 O  O     . LEU D 2 229 ? 133.779 97.449  145.332 1.00 19.82 ?  208 LEU D O     1 
ATOM   15048 C  CB    . LEU D 2 229 ? 133.637 97.656  142.091 1.00 19.51 ?  208 LEU D CB    1 
ATOM   15049 C  CG    . LEU D 2 229 ? 132.784 97.744  140.815 1.00 19.48 ?  208 LEU D CG    1 
ATOM   15050 C  CD1   . LEU D 2 229 ? 133.350 96.810  139.731 1.00 20.14 ?  208 LEU D CD1   1 
ATOM   15051 C  CD2   . LEU D 2 229 ? 131.287 97.457  141.066 1.00 19.95 ?  208 LEU D CD2   1 
ATOM   15052 N  N     . ALA D 2 230 ? 135.428 98.773  144.546 1.00 19.43 ?  209 ALA D N     1 
ATOM   15053 C  CA    . ALA D 2 230 ? 136.305 98.562  145.705 1.00 20.29 ?  209 ALA D CA    1 
ATOM   15054 C  C     . ALA D 2 230 ? 135.760 99.228  146.970 1.00 21.17 ?  209 ALA D C     1 
ATOM   15055 O  O     . ALA D 2 230 ? 135.779 98.630  148.041 1.00 21.73 ?  209 ALA D O     1 
ATOM   15056 C  CB    . ALA D 2 230 ? 137.719 99.055  145.406 1.00 19.99 ?  209 ALA D CB    1 
ATOM   15057 N  N     . GLN D 2 231 ? 135.271 100.462 146.845 1.00 22.26 ?  210 GLN D N     1 
ATOM   15058 C  CA    . GLN D 2 231 ? 134.665 101.179 147.983 1.00 23.33 ?  210 GLN D CA    1 
ATOM   15059 C  C     . GLN D 2 231 ? 133.444 100.441 148.542 1.00 23.85 ?  210 GLN D C     1 
ATOM   15060 O  O     . GLN D 2 231 ? 133.228 100.426 149.751 1.00 24.91 ?  210 GLN D O     1 
ATOM   15061 C  CB    . GLN D 2 231 ? 134.261 102.603 147.591 1.00 23.49 ?  210 GLN D CB    1 
ATOM   15062 C  CG    . GLN D 2 231 ? 135.420 103.544 147.247 1.00 23.05 ?  210 GLN D CG    1 
ATOM   15063 C  CD    . GLN D 2 231 ? 134.927 104.932 146.843 1.00 24.65 ?  210 GLN D CD    1 
ATOM   15064 O  OE1   . GLN D 2 231 ? 134.134 105.543 147.560 1.00 25.85 ?  210 GLN D OE1   1 
ATOM   15065 N  NE2   . GLN D 2 231 ? 135.379 105.425 145.689 1.00 22.30 ?  210 GLN D NE2   1 
ATOM   15066 N  N     . GLU D 2 232 ? 132.642 99.850  147.660 1.00 24.36 ?  211 GLU D N     1 
ATOM   15067 C  CA    . GLU D 2 232 ? 131.521 99.012  148.079 1.00 24.83 ?  211 GLU D CA    1 
ATOM   15068 C  C     . GLU D 2 232 ? 131.969 97.877  149.007 1.00 24.34 ?  211 GLU D C     1 
ATOM   15069 O  O     . GLU D 2 232 ? 131.340 97.641  150.040 1.00 24.20 ?  211 GLU D O     1 
ATOM   15070 C  CB    . GLU D 2 232 ? 130.798 98.437  146.866 1.00 25.15 ?  211 GLU D CB    1 
ATOM   15071 C  CG    . GLU D 2 232 ? 129.482 97.780  147.193 1.00 28.55 ?  211 GLU D CG    1 
ATOM   15072 C  CD    . GLU D 2 232 ? 128.809 97.257  145.954 1.00 33.83 ?  211 GLU D CD    1 
ATOM   15073 O  OE1   . GLU D 2 232 ? 128.003 98.009  145.367 1.00 35.09 ?  211 GLU D OE1   1 
ATOM   15074 O  OE2   . GLU D 2 232 ? 129.117 96.116  145.543 1.00 35.51 -1 211 GLU D OE2   1 
ATOM   15075 N  N     . ILE D 2 233 ? 133.050 97.187  148.647 1.00 23.39 ?  212 ILE D N     1 
ATOM   15076 C  CA    . ILE D 2 233 ? 133.607 96.130  149.508 1.00 23.42 ?  212 ILE D CA    1 
ATOM   15077 C  C     . ILE D 2 233 ? 134.161 96.718  150.807 1.00 23.74 ?  212 ILE D C     1 
ATOM   15078 O  O     . ILE D 2 233 ? 133.851 96.239  151.897 1.00 24.61 ?  212 ILE D O     1 
ATOM   15079 C  CB    . ILE D 2 233 ? 134.683 95.278  148.781 1.00 22.81 ?  212 ILE D CB    1 
ATOM   15080 C  CG1   . ILE D 2 233 ? 134.049 94.482  147.632 1.00 22.94 ?  212 ILE D CG1   1 
ATOM   15081 C  CG2   . ILE D 2 233 ? 135.374 94.317  149.757 1.00 22.45 ?  212 ILE D CG2   1 
ATOM   15082 C  CD1   . ILE D 2 233 ? 135.072 93.888  146.639 1.00 22.21 ?  212 ILE D CD1   1 
ATOM   15083 N  N     . TYR D 2 234 ? 134.966 97.770  150.684 1.00 24.19 ?  213 TYR D N     1 
ATOM   15084 C  CA    . TYR D 2 234 ? 135.565 98.449  151.824 1.00 24.59 ?  213 TYR D CA    1 
ATOM   15085 C  C     . TYR D 2 234 ? 134.513 98.849  152.864 1.00 25.15 ?  213 TYR D C     1 
ATOM   15086 O  O     . TYR D 2 234 ? 134.732 98.674  154.066 1.00 24.94 ?  213 TYR D O     1 
ATOM   15087 C  CB    . TYR D 2 234 ? 136.326 99.688  151.345 1.00 24.41 ?  213 TYR D CB    1 
ATOM   15088 C  CG    . TYR D 2 234 ? 136.989 100.502 152.437 1.00 25.93 ?  213 TYR D CG    1 
ATOM   15089 C  CD1   . TYR D 2 234 ? 138.258 100.172 152.900 1.00 24.70 ?  213 TYR D CD1   1 
ATOM   15090 C  CD2   . TYR D 2 234 ? 136.344 101.611 153.001 1.00 26.11 ?  213 TYR D CD2   1 
ATOM   15091 C  CE1   . TYR D 2 234 ? 138.875 100.919 153.899 1.00 27.90 ?  213 TYR D CE1   1 
ATOM   15092 C  CE2   . TYR D 2 234 ? 136.956 102.365 153.993 1.00 27.70 ?  213 TYR D CE2   1 
ATOM   15093 C  CZ    . TYR D 2 234 ? 138.220 102.016 154.435 1.00 27.89 ?  213 TYR D CZ    1 
ATOM   15094 O  OH    . TYR D 2 234 ? 138.830 102.756 155.421 1.00 32.34 ?  213 TYR D OH    1 
ATOM   15095 N  N     . ASN D 2 235 ? 133.387 99.386  152.391 1.00 25.43 ?  214 ASN D N     1 
ATOM   15096 C  CA    . ASN D 2 235 ? 132.314 99.876  153.273 1.00 26.77 ?  214 ASN D CA    1 
ATOM   15097 C  C     . ASN D 2 235 ? 131.535 98.769  153.984 1.00 27.06 ?  214 ASN D C     1 
ATOM   15098 O  O     . ASN D 2 235 ? 130.774 99.037  154.908 1.00 27.42 ?  214 ASN D O     1 
ATOM   15099 C  CB    . ASN D 2 235 ? 131.328 100.761 152.507 1.00 26.80 ?  214 ASN D CB    1 
ATOM   15100 C  CG    . ASN D 2 235 ? 131.962 102.017 151.974 1.00 28.19 ?  214 ASN D CG    1 
ATOM   15101 O  OD1   . ASN D 2 235 ? 132.857 102.592 152.590 1.00 29.35 ?  214 ASN D OD1   1 
ATOM   15102 N  ND2   . ASN D 2 235 ? 131.491 102.460 150.820 1.00 30.84 ?  214 ASN D ND2   1 
ATOM   15103 N  N     . LYS D 2 236 ? 131.725 97.534  153.545 1.00 26.87 ?  215 LYS D N     1 
ATOM   15104 C  CA    . LYS D 2 236 ? 131.081 96.394  154.185 1.00 27.86 ?  215 LYS D CA    1 
ATOM   15105 C  C     . LYS D 2 236 ? 131.930 95.840  155.337 1.00 28.07 ?  215 LYS D C     1 
ATOM   15106 O  O     . LYS D 2 236 ? 131.517 94.907  156.024 1.00 28.22 ?  215 LYS D O     1 
ATOM   15107 C  CB    . LYS D 2 236 ? 130.790 95.298  153.158 1.00 27.52 ?  215 LYS D CB    1 
ATOM   15108 C  CG    . LYS D 2 236 ? 129.793 95.693  152.096 1.00 29.60 ?  215 LYS D CG    1 
ATOM   15109 C  CD    . LYS D 2 236 ? 129.081 94.483  151.513 1.00 34.24 ?  215 LYS D CD    1 
ATOM   15110 C  CE    . LYS D 2 236 ? 129.657 94.028  150.187 1.00 36.75 ?  215 LYS D CE    1 
ATOM   15111 N  NZ    . LYS D 2 236 ? 131.039 93.522  150.332 1.00 40.41 1  215 LYS D NZ    1 
ATOM   15112 N  N     . GLN D 2 237 ? 133.106 96.425  155.549 1.00 28.33 ?  216 GLN D N     1 
ATOM   15113 C  CA    . GLN D 2 237 ? 134.062 95.898  156.526 1.00 29.60 ?  216 GLN D CA    1 
ATOM   15114 C  C     . GLN D 2 237 ? 133.960 96.586  157.882 1.00 30.69 ?  216 GLN D C     1 
ATOM   15115 O  O     . GLN D 2 237 ? 133.453 97.709  157.982 1.00 30.85 ?  216 GLN D O     1 
ATOM   15116 C  CB    . GLN D 2 237 ? 135.509 96.012  156.002 1.00 29.08 ?  216 GLN D CB    1 
ATOM   15117 C  CG    . GLN D 2 237 ? 135.763 95.412  154.615 1.00 27.78 ?  216 GLN D CG    1 
ATOM   15118 C  CD    . GLN D 2 237 ? 135.233 93.995  154.464 1.00 28.38 ?  216 GLN D CD    1 
ATOM   15119 O  OE1   . GLN D 2 237 ? 135.509 93.124  155.287 1.00 29.30 ?  216 GLN D OE1   1 
ATOM   15120 N  NE2   . GLN D 2 237 ? 134.474 93.757  153.399 1.00 26.88 ?  216 GLN D NE2   1 
ATOM   15121 N  N     . THR D 2 238 ? 134.457 95.908  158.915 1.00 32.02 ?  217 THR D N     1 
ATOM   15122 C  CA    . THR D 2 238 ? 134.587 96.500  160.251 1.00 33.47 ?  217 THR D CA    1 
ATOM   15123 C  C     . THR D 2 238 ? 135.610 97.641  160.252 1.00 34.29 ?  217 THR D C     1 
ATOM   15124 O  O     . THR D 2 238 ? 136.352 97.836  159.275 1.00 33.78 ?  217 THR D O     1 
ATOM   15125 C  CB    . THR D 2 238 ? 135.016 95.438  161.302 1.00 34.00 ?  217 THR D CB    1 
ATOM   15126 O  OG1   . THR D 2 238 ? 136.340 94.969  161.006 1.00 34.33 ?  217 THR D OG1   1 
ATOM   15127 C  CG2   . THR D 2 238 ? 134.042 94.248  161.312 1.00 33.53 ?  217 THR D CG2   1 
ATOM   15128 N  N     . GLU D 2 239 ? 135.665 98.387  161.350 1.00 35.45 ?  218 GLU D N     1 
ATOM   15129 C  CA    . GLU D 2 239 ? 136.618 99.487  161.462 1.00 36.37 ?  218 GLU D CA    1 
ATOM   15130 C  C     . GLU D 2 239 ? 138.067 99.007  161.488 1.00 36.29 ?  218 GLU D C     1 
ATOM   15131 O  O     . GLU D 2 239 ? 138.937 99.628  160.870 1.00 36.18 ?  218 GLU D O     1 
ATOM   15132 C  CB    . GLU D 2 239 ? 136.301 100.378 162.667 1.00 37.27 ?  218 GLU D CB    1 
ATOM   15133 C  CG    . GLU D 2 239 ? 135.010 101.199 162.498 1.00 39.45 ?  218 GLU D CG    1 
ATOM   15134 C  CD    . GLU D 2 239 ? 135.008 102.074 161.246 1.00 41.22 ?  218 GLU D CD    1 
ATOM   15135 O  OE1   . GLU D 2 239 ? 136.017 102.764 160.984 1.00 42.62 ?  218 GLU D OE1   1 
ATOM   15136 O  OE2   . GLU D 2 239 ? 133.991 102.072 160.519 1.00 41.24 -1 218 GLU D OE2   1 
ATOM   15137 N  N     . GLU D 2 240 ? 138.321 97.898  162.180 1.00 36.66 ?  219 GLU D N     1 
ATOM   15138 C  CA    . GLU D 2 240 ? 139.668 97.324  162.233 1.00 37.01 ?  219 GLU D CA    1 
ATOM   15139 C  C     . GLU D 2 240 ? 140.094 96.801  160.861 1.00 35.85 ?  219 GLU D C     1 
ATOM   15140 O  O     . GLU D 2 240 ? 141.241 97.001  160.450 1.00 35.62 ?  219 GLU D O     1 
ATOM   15141 C  CB    . GLU D 2 240 ? 139.770 96.209  163.285 1.00 37.98 ?  219 GLU D CB    1 
ATOM   15142 C  CG    . GLU D 2 240 ? 141.196 95.657  163.441 1.00 40.87 ?  219 GLU D CG    1 
ATOM   15143 C  CD    . GLU D 2 240 ? 141.329 94.537  164.471 1.00 44.58 ?  219 GLU D CD    1 
ATOM   15144 O  OE1   . GLU D 2 240 ? 142.448 94.378  165.016 1.00 45.86 ?  219 GLU D OE1   1 
ATOM   15145 O  OE2   . GLU D 2 240 ? 140.333 93.818  164.733 1.00 45.75 -1 219 GLU D OE2   1 
ATOM   15146 N  N     . LYS D 2 241 ? 139.169 96.135  160.171 1.00 34.54 ?  220 LYS D N     1 
ATOM   15147 C  CA    . LYS D 2 241 ? 139.425 95.605  158.830 1.00 33.65 ?  220 LYS D CA    1 
ATOM   15148 C  C     . LYS D 2 241 ? 139.649 96.741  157.823 1.00 32.67 ?  220 LYS D C     1 
ATOM   15149 O  O     . LYS D 2 241 ? 140.505 96.624  156.950 1.00 32.05 ?  220 LYS D O     1 
ATOM   15150 C  CB    . LYS D 2 241 ? 138.292 94.679  158.377 1.00 33.30 ?  220 LYS D CB    1 
ATOM   15151 C  CG    . LYS D 2 241 ? 138.529 93.940  157.046 1.00 34.50 ?  220 LYS D CG    1 
ATOM   15152 C  CD    . LYS D 2 241 ? 139.759 93.024  157.079 1.00 36.30 ?  220 LYS D CD    1 
ATOM   15153 C  CE    . LYS D 2 241 ? 139.533 91.801  157.959 1.00 38.44 ?  220 LYS D CE    1 
ATOM   15154 N  NZ    . LYS D 2 241 ? 140.823 91.231  158.431 1.00 39.28 1  220 LYS D NZ    1 
ATOM   15155 N  N     . LYS D 2 242 ? 138.883 97.828  157.957 1.00 31.90 ?  221 LYS D N     1 
ATOM   15156 C  CA    . LYS D 2 242 ? 139.070 99.021  157.131 1.00 31.28 ?  221 LYS D CA    1 
ATOM   15157 C  C     . LYS D 2 242 ? 140.476 99.597  157.289 1.00 31.32 ?  221 LYS D C     1 
ATOM   15158 O  O     . LYS D 2 242 ? 141.149 99.851  156.298 1.00 30.72 ?  221 LYS D O     1 
ATOM   15159 C  CB    . LYS D 2 242 ? 138.027 100.100 157.455 1.00 31.38 ?  221 LYS D CB    1 
ATOM   15160 C  CG    . LYS D 2 242 ? 136.676 99.906  156.776 1.00 30.64 ?  221 LYS D CG    1 
ATOM   15161 C  CD    . LYS D 2 242 ? 135.722 101.037 157.159 1.00 32.51 ?  221 LYS D CD    1 
ATOM   15162 C  CE    . LYS D 2 242 ? 134.384 100.880 156.471 1.00 32.66 ?  221 LYS D CE    1 
ATOM   15163 N  NZ    . LYS D 2 242 ? 133.392 101.829 157.023 1.00 35.31 1  221 LYS D NZ    1 
ATOM   15164 N  N     . ALA D 2 243 ? 140.906 99.805  158.538 1.00 31.62 ?  222 ALA D N     1 
ATOM   15165 C  CA    . ALA D 2 243 ? 142.251 100.313 158.830 1.00 31.66 ?  222 ALA D CA    1 
ATOM   15166 C  C     . ALA D 2 243 ? 143.344 99.427  158.218 1.00 31.52 ?  222 ALA D C     1 
ATOM   15167 O  O     . ALA D 2 243 ? 144.375 99.922  157.753 1.00 31.41 ?  222 ALA D O     1 
ATOM   15168 C  CB    . ALA D 2 243 ? 142.451 100.462 160.342 1.00 31.89 ?  222 ALA D CB    1 
ATOM   15169 N  N     . GLU D 2 244 ? 143.087 98.123  158.209 1.00 31.35 ?  223 GLU D N     1 
ATOM   15170 C  CA    . GLU D 2 244 ? 143.987 97.124  157.655 1.00 31.54 ?  223 GLU D CA    1 
ATOM   15171 C  C     . GLU D 2 244 ? 144.041 97.197  156.111 1.00 30.63 ?  223 GLU D C     1 
ATOM   15172 O  O     . GLU D 2 244 ? 145.111 97.064  155.502 1.00 29.47 ?  223 GLU D O     1 
ATOM   15173 C  CB    . GLU D 2 244 ? 143.501 95.761  158.121 1.00 32.45 ?  223 GLU D CB    1 
ATOM   15174 C  CG    . GLU D 2 244 ? 144.436 94.607  157.931 1.00 35.31 ?  223 GLU D CG    1 
ATOM   15175 C  CD    . GLU D 2 244 ? 143.973 93.398  158.719 1.00 38.36 ?  223 GLU D CD    1 
ATOM   15176 O  OE1   . GLU D 2 244 ? 144.021 93.443  159.966 1.00 41.93 ?  223 GLU D OE1   1 
ATOM   15177 O  OE2   . GLU D 2 244 ? 143.548 92.404  158.097 1.00 39.37 -1 223 GLU D OE2   1 
ATOM   15178 N  N     . LEU D 2 245 ? 142.882 97.415  155.498 1.00 29.62 ?  224 LEU D N     1 
ATOM   15179 C  CA    . LEU D 2 245 ? 142.793 97.615  154.053 1.00 29.44 ?  224 LEU D CA    1 
ATOM   15180 C  C     . LEU D 2 245 ? 143.417 98.940  153.608 1.00 28.99 ?  224 LEU D C     1 
ATOM   15181 O  O     . LEU D 2 245 ? 144.008 99.005  152.534 1.00 28.63 ?  224 LEU D O     1 
ATOM   15182 C  CB    . LEU D 2 245 ? 141.338 97.513  153.582 1.00 29.06 ?  224 LEU D CB    1 
ATOM   15183 C  CG    . LEU D 2 245 ? 140.684 96.131  153.678 1.00 29.27 ?  224 LEU D CG    1 
ATOM   15184 C  CD1   . LEU D 2 245 ? 139.265 96.201  153.121 1.00 30.76 ?  224 LEU D CD1   1 
ATOM   15185 C  CD2   . LEU D 2 245 ? 141.486 95.066  152.937 1.00 28.11 ?  224 LEU D CD2   1 
ATOM   15186 N  N     . ARG D 2 246 ? 143.283 99.982  154.430 1.00 29.31 ?  225 ARG D N     1 
ATOM   15187 C  CA    . ARG D 2 246 ? 143.948 101.263 154.166 1.00 29.86 ?  225 ARG D CA    1 
ATOM   15188 C  C     . ARG D 2 246 ? 145.463 101.109 154.196 1.00 29.23 ?  225 ARG D C     1 
ATOM   15189 O  O     . ARG D 2 246 ? 146.156 101.632 153.335 1.00 28.95 ?  225 ARG D O     1 
ATOM   15190 C  CB    . ARG D 2 246 ? 143.548 102.341 155.180 1.00 30.56 ?  225 ARG D CB    1 
ATOM   15191 C  CG    . ARG D 2 246 ? 142.178 102.940 154.957 1.00 33.71 ?  225 ARG D CG    1 
ATOM   15192 C  CD    . ARG D 2 246 ? 142.035 104.331 155.605 1.00 37.42 ?  225 ARG D CD    1 
ATOM   15193 N  NE    . ARG D 2 246 ? 142.337 104.343 157.041 1.00 39.17 ?  225 ARG D NE    1 
ATOM   15194 C  CZ    . ARG D 2 246 ? 141.516 103.929 158.006 1.00 40.68 ?  225 ARG D CZ    1 
ATOM   15195 N  NH1   . ARG D 2 246 ? 140.312 103.440 157.721 1.00 40.28 1  225 ARG D NH1   1 
ATOM   15196 N  NH2   . ARG D 2 246 ? 141.909 103.995 159.275 1.00 41.65 ?  225 ARG D NH2   1 
ATOM   15197 N  N     . GLU D 2 247 ? 145.964 100.403 155.203 1.00 28.89 ?  226 GLU D N     1 
ATOM   15198 C  CA    . GLU D 2 247 ? 147.395 100.135 155.308 1.00 29.27 ?  226 GLU D CA    1 
ATOM   15199 C  C     . GLU D 2 247 ? 147.890 99.352  154.093 1.00 27.84 ?  226 GLU D C     1 
ATOM   15200 O  O     . GLU D 2 247 ? 148.950 99.675  153.549 1.00 27.37 ?  226 GLU D O     1 
ATOM   15201 C  CB    . GLU D 2 247 ? 147.734 99.402  156.619 1.00 30.21 ?  226 GLU D CB    1 
ATOM   15202 C  CG    . GLU D 2 247 ? 149.207 98.972  156.759 1.00 34.46 ?  226 GLU D CG    1 
ATOM   15203 C  CD    . GLU D 2 247 ? 150.182 100.146 156.693 1.00 40.77 ?  226 GLU D CD    1 
ATOM   15204 O  OE1   . GLU D 2 247 ? 150.117 101.024 157.585 1.00 44.03 ?  226 GLU D OE1   1 
ATOM   15205 O  OE2   . GLU D 2 247 ? 151.014 100.195 155.752 1.00 42.98 -1 226 GLU D OE2   1 
ATOM   15206 N  N     . PHE D 2 248 ? 147.123 98.346  153.665 1.00 26.73 ?  227 PHE D N     1 
ATOM   15207 C  CA    . PHE D 2 248 ? 147.435 97.596  152.442 1.00 26.15 ?  227 PHE D CA    1 
ATOM   15208 C  C     . PHE D 2 248 ? 147.575 98.523  151.232 1.00 25.33 ?  227 PHE D C     1 
ATOM   15209 O  O     . PHE D 2 248 ? 148.552 98.431  150.494 1.00 24.70 ?  227 PHE D O     1 
ATOM   15210 C  CB    . PHE D 2 248 ? 146.396 96.505  152.118 1.00 26.02 ?  227 PHE D CB    1 
ATOM   15211 C  CG    . PHE D 2 248 ? 146.490 95.985  150.684 1.00 25.61 ?  227 PHE D CG    1 
ATOM   15212 C  CD1   . PHE D 2 248 ? 147.370 94.959  150.356 1.00 26.51 ?  227 PHE D CD1   1 
ATOM   15213 C  CD2   . PHE D 2 248 ? 145.723 96.556  149.664 1.00 26.21 ?  227 PHE D CD2   1 
ATOM   15214 C  CE1   . PHE D 2 248 ? 147.484 94.494  149.046 1.00 26.16 ?  227 PHE D CE1   1 
ATOM   15215 C  CE2   . PHE D 2 248 ? 145.828 96.102  148.342 1.00 26.07 ?  227 PHE D CE2   1 
ATOM   15216 C  CZ    . PHE D 2 248 ? 146.716 95.067  148.036 1.00 25.82 ?  227 PHE D CZ    1 
ATOM   15217 N  N     . ALA D 2 249 ? 146.582 99.393  151.034 1.00 24.83 ?  228 ALA D N     1 
ATOM   15218 C  CA    . ALA D 2 249 ? 146.533 100.293 149.874 1.00 24.08 ?  228 ALA D CA    1 
ATOM   15219 C  C     . ALA D 2 249 ? 147.711 101.279 149.861 1.00 23.93 ?  228 ALA D C     1 
ATOM   15220 O  O     . ALA D 2 249 ? 148.325 101.508 148.817 1.00 22.51 ?  228 ALA D O     1 
ATOM   15221 C  CB    . ALA D 2 249 ? 145.204 101.056 149.858 1.00 24.18 ?  228 ALA D CB    1 
ATOM   15222 N  N     . ILE D 2 250 ? 148.012 101.858 151.023 1.00 24.20 ?  229 ILE D N     1 
ATOM   15223 C  CA    . ILE D 2 250 ? 149.111 102.819 151.143 1.00 24.86 ?  229 ILE D CA    1 
ATOM   15224 C  C     . ILE D 2 250 ? 150.466 102.126 150.961 1.00 24.68 ?  229 ILE D C     1 
ATOM   15225 O  O     . ILE D 2 250 ? 151.343 102.650 150.285 1.00 24.30 ?  229 ILE D O     1 
ATOM   15226 C  CB    . ILE D 2 250 ? 149.049 103.622 152.489 1.00 25.44 ?  229 ILE D CB    1 
ATOM   15227 C  CG1   . ILE D 2 250 ? 147.724 104.397 152.632 1.00 26.49 ?  229 ILE D CG1   1 
ATOM   15228 C  CG2   . ILE D 2 250 ? 150.247 104.570 152.638 1.00 27.13 ?  229 ILE D CG2   1 
ATOM   15229 C  CD1   . ILE D 2 250 ? 147.366 105.319 151.465 1.00 28.58 ?  229 ILE D CD1   1 
ATOM   15230 N  N     . ASP D 2 251 ? 150.626 100.946 151.562 1.00 24.90 ?  230 ASP D N     1 
ATOM   15231 C  CA    . ASP D 2 251 ? 151.847 100.160 151.421 1.00 25.04 ?  230 ASP D CA    1 
ATOM   15232 C  C     . ASP D 2 251 ? 152.092 99.785  149.948 1.00 24.25 ?  230 ASP D C     1 
ATOM   15233 O  O     . ASP D 2 251 ? 153.203 99.941  149.438 1.00 23.60 ?  230 ASP D O     1 
ATOM   15234 C  CB    . ASP D 2 251 ? 151.762 98.907  152.298 1.00 26.23 ?  230 ASP D CB    1 
ATOM   15235 C  CG    . ASP D 2 251 ? 152.936 97.971  152.109 1.00 28.91 ?  230 ASP D CG    1 
ATOM   15236 O  OD1   . ASP D 2 251 ? 154.070 98.326  152.493 1.00 32.03 ?  230 ASP D OD1   1 
ATOM   15237 O  OD2   . ASP D 2 251 ? 152.716 96.858  151.593 1.00 33.16 -1 230 ASP D OD2   1 
ATOM   15238 N  N     . LEU D 2 252 ? 151.053 99.288  149.281 1.00 23.43 ?  231 LEU D N     1 
ATOM   15239 C  CA    . LEU D 2 252 ? 151.136 98.976  147.857 1.00 22.79 ?  231 LEU D CA    1 
ATOM   15240 C  C     . LEU D 2 252 ? 151.492 100.220 147.037 1.00 22.71 ?  231 LEU D C     1 
ATOM   15241 O  O     . LEU D 2 252 ? 152.360 100.165 146.158 1.00 21.58 ?  231 LEU D O     1 
ATOM   15242 C  CB    . LEU D 2 252 ? 149.823 98.371  147.346 1.00 22.48 ?  231 LEU D CB    1 
ATOM   15243 C  CG    . LEU D 2 252 ? 149.800 97.998  145.852 1.00 21.05 ?  231 LEU D CG    1 
ATOM   15244 C  CD1   . LEU D 2 252 ? 150.916 96.993  145.491 1.00 22.94 ?  231 LEU D CD1   1 
ATOM   15245 C  CD2   . LEU D 2 252 ? 148.444 97.432  145.452 1.00 19.31 ?  231 LEU D CD2   1 
ATOM   15246 N  N     . LEU D 2 253 ? 150.818 101.334 147.326 1.00 22.90 ?  232 LEU D N     1 
ATOM   15247 C  CA    . LEU D 2 253 ? 151.095 102.589 146.612 1.00 23.78 ?  232 LEU D CA    1 
ATOM   15248 C  C     . LEU D 2 253 ? 152.568 102.989 146.755 1.00 23.75 ?  232 LEU D C     1 
ATOM   15249 O  O     . LEU D 2 253 ? 153.212 103.357 145.772 1.00 23.26 ?  232 LEU D O     1 
ATOM   15250 C  CB    . LEU D 2 253 ? 150.205 103.728 147.116 1.00 24.03 ?  232 LEU D CB    1 
ATOM   15251 C  CG    . LEU D 2 253 ? 150.591 105.122 146.589 1.00 26.46 ?  232 LEU D CG    1 
ATOM   15252 C  CD1   . LEU D 2 253 ? 150.226 105.244 145.128 1.00 26.52 ?  232 LEU D CD1   1 
ATOM   15253 C  CD2   . LEU D 2 253 ? 149.925 106.240 147.395 1.00 27.50 ?  232 LEU D CD2   1 
ATOM   15254 N  N     . ASN D 2 254 ? 153.075 102.934 147.987 1.00 24.63 ?  233 ASN D N     1 
ATOM   15255 C  CA    . ASN D 2 254 ? 154.484 103.223 148.268 1.00 25.49 ?  233 ASN D CA    1 
ATOM   15256 C  C     . ASN D 2 254 ? 155.465 102.360 147.462 1.00 24.94 ?  233 ASN D C     1 
ATOM   15257 O  O     . ASN D 2 254 ? 156.442 102.885 146.921 1.00 24.64 ?  233 ASN D O     1 
ATOM   15258 C  CB    . ASN D 2 254 ? 154.784 103.078 149.757 1.00 26.98 ?  233 ASN D CB    1 
ATOM   15259 C  CG    . ASN D 2 254 ? 154.485 104.339 150.536 1.00 29.94 ?  233 ASN D CG    1 
ATOM   15260 O  OD1   . ASN D 2 254 ? 154.760 105.456 150.077 1.00 34.55 ?  233 ASN D OD1   1 
ATOM   15261 N  ND2   . ASN D 2 254 ? 153.933 104.174 151.731 1.00 33.81 ?  233 ASN D ND2   1 
ATOM   15262 N  N     . GLN D 2 255 ? 155.211 101.053 147.397 1.00 24.08 ?  234 GLN D N     1 
ATOM   15263 C  CA    . GLN D 2 255 ? 156.082 100.145 146.645 1.00 24.35 ?  234 GLN D CA    1 
ATOM   15264 C  C     . GLN D 2 255 ? 156.084 100.523 145.175 1.00 23.26 ?  234 GLN D C     1 
ATOM   15265 O  O     . GLN D 2 255 ? 157.153 100.631 144.567 1.00 23.12 ?  234 GLN D O     1 
ATOM   15266 C  CB    . GLN D 2 255 ? 155.645 98.681  146.772 1.00 24.84 ?  234 GLN D CB    1 
ATOM   15267 C  CG    . GLN D 2 255 ? 155.900 98.027  148.112 1.00 27.45 ?  234 GLN D CG    1 
ATOM   15268 C  CD    . GLN D 2 255 ? 157.356 98.094  148.541 1.00 32.02 ?  234 GLN D CD    1 
ATOM   15269 O  OE1   . GLN D 2 255 ? 157.671 98.686  149.570 1.00 35.80 ?  234 GLN D OE1   1 
ATOM   15270 N  NE2   . GLN D 2 255 ? 158.248 97.484  147.758 1.00 32.12 ?  234 GLN D NE2   1 
ATOM   15271 N  N     . LEU D 2 256 ? 154.888 100.725 144.619 1.00 21.77 ?  235 LEU D N     1 
ATOM   15272 C  CA    . LEU D 2 256 ? 154.743 101.080 143.205 1.00 21.68 ?  235 LEU D CA    1 
ATOM   15273 C  C     . LEU D 2 256 ? 155.351 102.448 142.920 1.00 21.49 ?  235 LEU D C     1 
ATOM   15274 O  O     . LEU D 2 256 ? 156.012 102.633 141.903 1.00 20.89 ?  235 LEU D O     1 
ATOM   15275 C  CB    . LEU D 2 256 ? 153.267 101.060 142.761 1.00 20.49 ?  235 LEU D CB    1 
ATOM   15276 C  CG    . LEU D 2 256 ? 152.578 99.689  142.716 1.00 21.52 ?  235 LEU D CG    1 
ATOM   15277 C  CD1   . LEU D 2 256 ? 151.063 99.818  142.481 1.00 20.71 ?  235 LEU D CD1   1 
ATOM   15278 C  CD2   . LEU D 2 256 ? 153.192 98.784  141.658 1.00 20.74 ?  235 LEU D CD2   1 
ATOM   15279 N  N     . TYR D 2 257 ? 155.128 103.398 143.827 1.00 21.42 ?  236 TYR D N     1 
ATOM   15280 C  CA    . TYR D 2 257 ? 155.656 104.750 143.647 1.00 22.02 ?  236 TYR D CA    1 
ATOM   15281 C  C     . TYR D 2 257 ? 157.184 104.783 143.618 1.00 22.61 ?  236 TYR D C     1 
ATOM   15282 O  O     . TYR D 2 257 ? 157.776 105.460 142.776 1.00 22.19 ?  236 TYR D O     1 
ATOM   15283 C  CB    . TYR D 2 257 ? 155.112 105.699 144.710 1.00 22.06 ?  236 TYR D CB    1 
ATOM   15284 C  CG    . TYR D 2 257 ? 155.739 107.074 144.683 1.00 23.44 ?  236 TYR D CG    1 
ATOM   15285 C  CD1   . TYR D 2 257 ? 155.526 107.943 143.605 1.00 24.01 ?  236 TYR D CD1   1 
ATOM   15286 C  CD2   . TYR D 2 257 ? 156.537 107.511 145.738 1.00 25.22 ?  236 TYR D CD2   1 
ATOM   15287 C  CE1   . TYR D 2 257 ? 156.101 109.212 143.584 1.00 25.14 ?  236 TYR D CE1   1 
ATOM   15288 C  CE2   . TYR D 2 257 ? 157.125 108.773 145.722 1.00 26.71 ?  236 TYR D CE2   1 
ATOM   15289 C  CZ    . TYR D 2 257 ? 156.899 109.615 144.648 1.00 25.35 ?  236 TYR D CZ    1 
ATOM   15290 O  OH    . TYR D 2 257 ? 157.473 110.860 144.651 1.00 26.77 ?  236 TYR D OH    1 
ATOM   15291 N  N     . GLU D 2 258 ? 157.823 104.045 144.522 1.00 23.09 ?  237 GLU D N     1 
ATOM   15292 C  CA    . GLU D 2 258 ? 159.287 104.043 144.562 1.00 23.98 ?  237 GLU D CA    1 
ATOM   15293 C  C     . GLU D 2 258 ? 159.883 103.420 143.299 1.00 23.13 ?  237 GLU D C     1 
ATOM   15294 O  O     . GLU D 2 258 ? 160.885 103.906 142.782 1.00 23.02 ?  237 GLU D O     1 
ATOM   15295 C  CB    . GLU D 2 258 ? 159.817 103.377 145.840 1.00 25.20 ?  237 GLU D CB    1 
ATOM   15296 C  CG    . GLU D 2 258 ? 159.473 104.151 147.124 1.00 28.82 ?  237 GLU D CG    1 
ATOM   15297 C  CD    . GLU D 2 258 ? 160.231 105.477 147.285 1.00 34.48 ?  237 GLU D CD    1 
ATOM   15298 O  OE1   . GLU D 2 258 ? 161.375 105.608 146.775 1.00 37.75 ?  237 GLU D OE1   1 
ATOM   15299 O  OE2   . GLU D 2 258 ? 159.684 106.396 147.941 1.00 37.16 -1 237 GLU D OE2   1 
ATOM   15300 N  N     . ASN D 2 259 ? 159.246 102.372 142.793 1.00 22.12 ?  238 ASN D N     1 
ATOM   15301 C  CA    . ASN D 2 259 ? 159.623 101.791 141.504 1.00 22.35 ?  238 ASN D CA    1 
ATOM   15302 C  C     . ASN D 2 259 ? 159.345 102.729 140.299 1.00 22.11 ?  238 ASN D C     1 
ATOM   15303 O  O     . ASN D 2 259 ? 160.129 102.759 139.347 1.00 22.24 ?  238 ASN D O     1 
ATOM   15304 C  CB    . ASN D 2 259 ? 158.945 100.429 141.313 1.00 21.69 ?  238 ASN D CB    1 
ATOM   15305 C  CG    . ASN D 2 259 ? 159.342 99.759  140.010 1.00 23.38 ?  238 ASN D CG    1 
ATOM   15306 O  OD1   . ASN D 2 259 ? 160.472 99.271  139.860 1.00 23.95 ?  238 ASN D OD1   1 
ATOM   15307 N  ND2   . ASN D 2 259 ? 158.421 99.740  139.056 1.00 21.14 ?  238 ASN D ND2   1 
ATOM   15308 N  N     . GLU D 2 260 ? 158.242 103.485 140.349 1.00 21.95 ?  239 GLU D N     1 
ATOM   15309 C  CA    . GLU D 2 260 ? 157.928 104.493 139.315 1.00 22.50 ?  239 GLU D CA    1 
ATOM   15310 C  C     . GLU D 2 260 ? 159.003 105.574 139.214 1.00 22.03 ?  239 GLU D C     1 
ATOM   15311 O  O     . GLU D 2 260 ? 159.303 106.054 138.125 1.00 22.03 ?  239 GLU D O     1 
ATOM   15312 C  CB    . GLU D 2 260 ? 156.585 105.198 139.581 1.00 22.90 ?  239 GLU D CB    1 
ATOM   15313 C  CG    . GLU D 2 260 ? 155.324 104.466 139.092 1.00 25.84 ?  239 GLU D CG    1 
ATOM   15314 C  CD    . GLU D 2 260 ? 155.418 103.963 137.656 1.00 28.59 ?  239 GLU D CD    1 
ATOM   15315 O  OE1   . GLU D 2 260 ? 156.037 102.900 137.440 1.00 28.18 ?  239 GLU D OE1   1 
ATOM   15316 O  OE2   . GLU D 2 260 ? 154.840 104.606 136.749 1.00 30.32 -1 239 GLU D OE2   1 
ATOM   15317 N  N     . LEU D 2 261 ? 159.550 105.979 140.355 1.00 21.50 ?  240 LEU D N     1 
ATOM   15318 C  CA    . LEU D 2 261 ? 160.607 106.987 140.362 1.00 22.03 ?  240 LEU D CA    1 
ATOM   15319 C  C     . LEU D 2 261 ? 161.825 106.462 139.623 1.00 21.52 ?  240 LEU D C     1 
ATOM   15320 O  O     . LEU D 2 261 ? 162.414 107.182 138.816 1.00 21.44 ?  240 LEU D O     1 
ATOM   15321 C  CB    . LEU D 2 261 ? 160.985 107.402 141.782 1.00 21.57 ?  240 LEU D CB    1 
ATOM   15322 C  CG    . LEU D 2 261 ? 159.903 108.041 142.653 1.00 23.22 ?  240 LEU D CG    1 
ATOM   15323 C  CD1   . LEU D 2 261 ? 160.485 108.341 144.023 1.00 23.06 ?  240 LEU D CD1   1 
ATOM   15324 C  CD2   . LEU D 2 261 ? 159.349 109.312 142.009 1.00 23.52 ?  240 LEU D CD2   1 
ATOM   15325 N  N     . GLU D 2 262 ? 162.180 105.204 139.884 1.00 21.69 ?  241 GLU D N     1 
ATOM   15326 C  CA    . GLU D 2 262 ? 163.305 104.561 139.186 1.00 22.31 ?  241 GLU D CA    1 
ATOM   15327 C  C     . GLU D 2 262 ? 163.007 104.355 137.699 1.00 21.69 ?  241 GLU D C     1 
ATOM   15328 O  O     . GLU D 2 262 ? 163.862 104.602 136.845 1.00 21.75 ?  241 GLU D O     1 
ATOM   15329 C  CB    . GLU D 2 262 ? 163.657 103.215 139.828 1.00 22.46 ?  241 GLU D CB    1 
ATOM   15330 C  CG    . GLU D 2 262 ? 164.109 103.273 141.289 1.00 25.63 ?  241 GLU D CG    1 
ATOM   15331 C  CD    . GLU D 2 262 ? 164.526 101.897 141.792 1.00 29.83 ?  241 GLU D CD    1 
ATOM   15332 O  OE1   . GLU D 2 262 ? 163.639 101.084 142.127 1.00 33.22 ?  241 GLU D OE1   1 
ATOM   15333 O  OE2   . GLU D 2 262 ? 165.737 101.613 141.825 1.00 33.36 -1 241 GLU D OE2   1 
ATOM   15334 N  N     . TYR D 2 263 ? 161.799 103.882 137.397 1.00 21.42 ?  242 TYR D N     1 
ATOM   15335 C  CA    . TYR D 2 263 ? 161.333 103.712 136.016 1.00 21.04 ?  242 TYR D CA    1 
ATOM   15336 C  C     . TYR D 2 263 ? 161.441 105.041 135.257 1.00 21.15 ?  242 TYR D C     1 
ATOM   15337 O  O     . TYR D 2 263 ? 161.870 105.082 134.103 1.00 20.32 ?  242 TYR D O     1 
ATOM   15338 C  CB    . TYR D 2 263 ? 159.875 103.225 136.025 1.00 20.95 ?  242 TYR D CB    1 
ATOM   15339 C  CG    . TYR D 2 263 ? 159.215 103.096 134.664 1.00 21.86 ?  242 TYR D CG    1 
ATOM   15340 C  CD1   . TYR D 2 263 ? 159.445 101.980 133.860 1.00 23.53 ?  242 TYR D CD1   1 
ATOM   15341 C  CD2   . TYR D 2 263 ? 158.360 104.092 134.181 1.00 21.20 ?  242 TYR D CD2   1 
ATOM   15342 C  CE1   . TYR D 2 263 ? 158.842 101.856 132.617 1.00 23.34 ?  242 TYR D CE1   1 
ATOM   15343 C  CE2   . TYR D 2 263 ? 157.752 103.974 132.935 1.00 23.11 ?  242 TYR D CE2   1 
ATOM   15344 C  CZ    . TYR D 2 263 ? 158.004 102.856 132.158 1.00 23.27 ?  242 TYR D CZ    1 
ATOM   15345 O  OH    . TYR D 2 263 ? 157.404 102.735 130.923 1.00 27.07 ?  242 TYR D OH    1 
ATOM   15346 N  N     . THR D 2 264 ? 161.028 106.114 135.928 1.00 21.12 ?  243 THR D N     1 
ATOM   15347 C  CA    . THR D 2 264 ? 160.997 107.456 135.354 1.00 21.98 ?  243 THR D CA    1 
ATOM   15348 C  C     . THR D 2 264 ? 162.401 107.949 135.008 1.00 22.32 ?  243 THR D C     1 
ATOM   15349 O  O     . THR D 2 264 ? 162.642 108.375 133.880 1.00 21.78 ?  243 THR D O     1 
ATOM   15350 C  CB    . THR D 2 264 ? 160.268 108.443 136.294 1.00 21.68 ?  243 THR D CB    1 
ATOM   15351 O  OG1   . THR D 2 264 ? 158.891 108.064 136.382 1.00 23.29 ?  243 THR D OG1   1 
ATOM   15352 C  CG2   . THR D 2 264 ? 160.367 109.899 135.800 1.00 23.16 ?  243 THR D CG2   1 
ATOM   15353 N  N     . GLU D 2 265 ? 163.325 107.865 135.964 1.00 22.48 ?  244 GLU D N     1 
ATOM   15354 C  CA    . GLU D 2 265 ? 164.703 108.289 135.703 1.00 23.73 ?  244 GLU D CA    1 
ATOM   15355 C  C     . GLU D 2 265 ? 165.332 107.477 134.582 1.00 23.85 ?  244 GLU D C     1 
ATOM   15356 O  O     . GLU D 2 265 ? 166.021 108.033 133.736 1.00 24.40 ?  244 GLU D O     1 
ATOM   15357 C  CB    . GLU D 2 265 ? 165.552 108.201 136.962 1.00 23.19 ?  244 GLU D CB    1 
ATOM   15358 C  CG    . GLU D 2 265 ? 165.222 109.296 137.941 1.00 25.08 ?  244 GLU D CG    1 
ATOM   15359 C  CD    . GLU D 2 265 ? 165.925 109.135 139.272 1.00 27.30 ?  244 GLU D CD    1 
ATOM   15360 O  OE1   . GLU D 2 265 ? 166.832 108.288 139.383 1.00 27.77 ?  244 GLU D OE1   1 
ATOM   15361 O  OE2   . GLU D 2 265 ? 165.562 109.867 140.210 1.00 28.63 -1 244 GLU D OE2   1 
ATOM   15362 N  N     . ASP D 2 266 ? 165.056 106.172 134.569 1.00 24.13 ?  245 ASP D N     1 
ATOM   15363 C  CA    . ASP D 2 266 ? 165.587 105.251 133.559 1.00 25.22 ?  245 ASP D CA    1 
ATOM   15364 C  C     . ASP D 2 266 ? 165.198 105.656 132.120 1.00 24.84 ?  245 ASP D C     1 
ATOM   15365 O  O     . ASP D 2 266 ? 166.001 105.509 131.193 1.00 25.64 ?  245 ASP D O     1 
ATOM   15366 C  CB    . ASP D 2 266 ? 165.114 103.823 133.878 1.00 25.79 ?  245 ASP D CB    1 
ATOM   15367 C  CG    . ASP D 2 266 ? 165.727 102.771 132.964 1.00 27.71 ?  245 ASP D CG    1 
ATOM   15368 O  OD1   . ASP D 2 266 ? 166.963 102.698 132.887 1.00 31.57 ?  245 ASP D OD1   1 
ATOM   15369 O  OD2   . ASP D 2 266 ? 164.973 101.995 132.340 1.00 30.29 -1 245 ASP D OD2   1 
ATOM   15370 N  N     . LEU D 2 267 ? 163.988 106.178 131.947 1.00 24.07 ?  246 LEU D N     1 
ATOM   15371 C  CA    . LEU D 2 267 ? 163.472 106.539 130.624 1.00 23.98 ?  246 LEU D CA    1 
ATOM   15372 C  C     . LEU D 2 267 ? 163.637 108.014 130.255 1.00 22.83 ?  246 LEU D C     1 
ATOM   15373 O  O     . LEU D 2 267 ? 163.929 108.333 129.096 1.00 23.00 ?  246 LEU D O     1 
ATOM   15374 C  CB    . LEU D 2 267 ? 161.983 106.167 130.501 1.00 23.82 ?  246 LEU D CB    1 
ATOM   15375 C  CG    . LEU D 2 267 ? 161.651 104.669 130.455 1.00 26.05 ?  246 LEU D CG    1 
ATOM   15376 C  CD1   . LEU D 2 267 ? 160.212 104.458 130.071 1.00 26.74 ?  246 LEU D CD1   1 
ATOM   15377 C  CD2   . LEU D 2 267 ? 162.552 103.922 129.491 1.00 28.00 ?  246 LEU D CD2   1 
ATOM   15378 N  N     . TYR D 2 268 ? 163.446 108.897 131.236 1.00 21.68 ?  247 TYR D N     1 
ATOM   15379 C  CA    . TYR D 2 268 ? 163.314 110.333 130.970 1.00 20.95 ?  247 TYR D CA    1 
ATOM   15380 C  C     . TYR D 2 268 ? 164.543 111.209 131.246 1.00 21.43 ?  247 TYR D C     1 
ATOM   15381 O  O     . TYR D 2 268 ? 164.589 112.343 130.772 1.00 20.73 ?  247 TYR D O     1 
ATOM   15382 C  CB    . TYR D 2 268 ? 162.108 110.914 131.713 1.00 20.27 ?  247 TYR D CB    1 
ATOM   15383 C  CG    . TYR D 2 268 ? 160.759 110.482 131.166 1.00 19.54 ?  247 TYR D CG    1 
ATOM   15384 C  CD1   . TYR D 2 268 ? 160.017 109.490 131.799 1.00 18.52 ?  247 TYR D CD1   1 
ATOM   15385 C  CD2   . TYR D 2 268 ? 160.231 111.069 130.007 1.00 20.62 ?  247 TYR D CD2   1 
ATOM   15386 C  CE1   . TYR D 2 268 ? 158.750 109.088 131.301 1.00 18.33 ?  247 TYR D CE1   1 
ATOM   15387 C  CE2   . TYR D 2 268 ? 158.971 110.677 129.498 1.00 20.79 ?  247 TYR D CE2   1 
ATOM   15388 C  CZ    . TYR D 2 268 ? 158.242 109.697 130.158 1.00 20.23 ?  247 TYR D CZ    1 
ATOM   15389 O  OH    . TYR D 2 268 ? 157.013 109.323 129.651 1.00 20.50 ?  247 TYR D OH    1 
ATOM   15390 N  N     . ASP D 2 269 ? 165.520 110.716 132.016 1.00 21.65 ?  248 ASP D N     1 
ATOM   15391 C  CA    . ASP D 2 269 ? 166.755 111.489 132.192 1.00 22.30 ?  248 ASP D CA    1 
ATOM   15392 C  C     . ASP D 2 269 ? 167.432 111.846 130.847 1.00 22.54 ?  248 ASP D C     1 
ATOM   15393 O  O     . ASP D 2 269 ? 167.954 112.953 130.694 1.00 22.49 ?  248 ASP D O     1 
ATOM   15394 C  CB    . ASP D 2 269 ? 167.744 110.782 133.121 1.00 22.83 ?  248 ASP D CB    1 
ATOM   15395 C  CG    . ASP D 2 269 ? 167.423 110.996 134.596 1.00 23.55 ?  248 ASP D CG    1 
ATOM   15396 O  OD1   . ASP D 2 269 ? 166.533 111.811 134.911 1.00 24.95 ?  248 ASP D OD1   1 
ATOM   15397 O  OD2   . ASP D 2 269 ? 168.067 110.342 135.448 1.00 24.47 -1 248 ASP D OD2   1 
ATOM   15398 N  N     . GLN D 2 270 ? 167.413 110.920 129.886 1.00 22.79 ?  249 GLN D N     1 
ATOM   15399 C  CA    . GLN D 2 270 ? 168.061 111.144 128.588 1.00 23.41 ?  249 GLN D CA    1 
ATOM   15400 C  C     . GLN D 2 270 ? 167.397 112.240 127.748 1.00 22.83 ?  249 GLN D C     1 
ATOM   15401 O  O     . GLN D 2 270 ? 167.992 112.726 126.788 1.00 23.75 ?  249 GLN D O     1 
ATOM   15402 C  CB    . GLN D 2 270 ? 168.173 109.848 127.778 1.00 24.02 ?  249 GLN D CB    1 
ATOM   15403 C  CG    . GLN D 2 270 ? 166.837 109.295 127.250 1.00 25.40 ?  249 GLN D CG    1 
ATOM   15404 C  CD    . GLN D 2 270 ? 166.957 107.872 126.734 1.00 29.23 ?  249 GLN D CD    1 
ATOM   15405 O  OE1   . GLN D 2 270 ? 167.769 107.088 127.227 1.00 31.31 ?  249 GLN D OE1   1 
ATOM   15406 N  NE2   . GLN D 2 270 ? 166.137 107.525 125.744 1.00 30.04 ?  249 GLN D NE2   1 
ATOM   15407 N  N     . VAL D 2 271 ? 166.165 112.611 128.097 1.00 21.93 ?  250 VAL D N     1 
ATOM   15408 C  CA    . VAL D 2 271 ? 165.479 113.723 127.433 1.00 21.29 ?  250 VAL D CA    1 
ATOM   15409 C  C     . VAL D 2 271 ? 165.160 114.876 128.403 1.00 21.16 ?  250 VAL D C     1 
ATOM   15410 O  O     . VAL D 2 271 ? 164.401 115.789 128.066 1.00 21.54 ?  250 VAL D O     1 
ATOM   15411 C  CB    . VAL D 2 271 ? 164.205 113.237 126.669 1.00 21.62 ?  250 VAL D CB    1 
ATOM   15412 C  CG1   . VAL D 2 271 ? 164.594 112.295 125.530 1.00 21.36 ?  250 VAL D CG1   1 
ATOM   15413 C  CG2   . VAL D 2 271 ? 163.204 112.558 127.622 1.00 21.17 ?  250 VAL D CG2   1 
ATOM   15414 N  N     . GLY D 2 272 ? 165.727 114.812 129.614 1.00 20.92 ?  251 GLY D N     1 
ATOM   15415 C  CA    . GLY D 2 272 ? 165.678 115.914 130.595 1.00 20.61 ?  251 GLY D CA    1 
ATOM   15416 C  C     . GLY D 2 272 ? 164.333 116.249 131.237 1.00 20.77 ?  251 GLY D C     1 
ATOM   15417 O  O     . GLY D 2 272 ? 164.114 117.386 131.681 1.00 20.28 ?  251 GLY D O     1 
ATOM   15418 N  N     . LEU D 2 273 ? 163.440 115.266 131.314 1.00 19.85 ?  252 LEU D N     1 
ATOM   15419 C  CA    . LEU D 2 273 ? 162.066 115.544 131.735 1.00 20.09 ?  252 LEU D CA    1 
ATOM   15420 C  C     . LEU D 2 273 ? 161.645 114.982 133.095 1.00 19.88 ?  252 LEU D C     1 
ATOM   15421 O  O     . LEU D 2 273 ? 160.538 115.259 133.546 1.00 20.04 ?  252 LEU D O     1 
ATOM   15422 C  CB    . LEU D 2 273 ? 161.089 115.026 130.665 1.00 19.97 ?  252 LEU D CB    1 
ATOM   15423 C  CG    . LEU D 2 273 ? 161.234 115.600 129.264 1.00 20.26 ?  252 LEU D CG    1 
ATOM   15424 C  CD1   . LEU D 2 273 ? 160.117 115.040 128.412 1.00 18.98 ?  252 LEU D CD1   1 
ATOM   15425 C  CD2   . LEU D 2 273 ? 161.206 117.154 129.263 1.00 21.03 ?  252 LEU D CD2   1 
ATOM   15426 N  N     . SER D 2 274 ? 162.528 114.217 133.739 0.50 19.54 ?  253 SER D N     1 
ATOM   15427 C  CA    . SER D 2 274 ? 162.160 113.405 134.909 0.50 19.34 ?  253 SER D CA    1 
ATOM   15428 C  C     . SER D 2 274 ? 161.502 114.176 136.059 0.50 20.05 ?  253 SER D C     1 
ATOM   15429 O  O     . SER D 2 274 ? 160.539 113.692 136.653 0.50 20.31 ?  253 SER D O     1 
ATOM   15430 C  CB    . SER D 2 274 ? 163.360 112.597 135.421 0.50 18.97 ?  253 SER D CB    1 
ATOM   15431 O  OG    . SER D 2 274 ? 163.911 111.788 134.398 0.50 15.35 ?  253 SER D OG    1 
ATOM   15432 N  N     . HIS D 2 275 ? 162.026 115.360 136.375 1.00 20.77 ?  254 HIS D N     1 
ATOM   15433 C  CA    . HIS D 2 275 ? 161.443 116.215 137.430 1.00 21.18 ?  254 HIS D CA    1 
ATOM   15434 C  C     . HIS D 2 275 ? 159.938 116.458 137.215 1.00 21.50 ?  254 HIS D C     1 
ATOM   15435 O  O     . HIS D 2 275 ? 159.128 116.261 138.136 1.00 19.88 ?  254 HIS D O     1 
ATOM   15436 C  CB    . HIS D 2 275 ? 162.189 117.554 137.552 1.00 21.60 ?  254 HIS D CB    1 
ATOM   15437 C  CG    . HIS D 2 275 ? 161.553 118.505 138.521 1.00 22.43 ?  254 HIS D CG    1 
ATOM   15438 N  ND1   . HIS D 2 275 ? 161.862 118.520 139.867 1.00 22.77 ?  254 HIS D ND1   1 
ATOM   15439 C  CD2   . HIS D 2 275 ? 160.610 119.463 138.339 1.00 22.50 ?  254 HIS D CD2   1 
ATOM   15440 C  CE1   . HIS D 2 275 ? 161.140 119.452 140.468 1.00 24.05 ?  254 HIS D CE1   1 
ATOM   15441 N  NE2   . HIS D 2 275 ? 160.369 120.033 139.565 1.00 23.22 ?  254 HIS D NE2   1 
ATOM   15442 N  N     . ASP D 2 276 ? 159.578 116.868 135.998 1.00 22.34 ?  255 ASP D N     1 
ATOM   15443 C  CA    . ASP D 2 276 ? 158.183 117.147 135.668 1.00 23.19 ?  255 ASP D CA    1 
ATOM   15444 C  C     . ASP D 2 276 ? 157.334 115.885 135.600 1.00 22.17 ?  255 ASP D C     1 
ATOM   15445 O  O     . ASP D 2 276 ? 156.165 115.920 135.958 1.00 21.87 ?  255 ASP D O     1 
ATOM   15446 C  CB    . ASP D 2 276 ? 158.059 117.921 134.345 1.00 24.33 ?  255 ASP D CB    1 
ATOM   15447 C  CG    . ASP D 2 276 ? 158.152 119.438 134.526 1.00 27.58 ?  255 ASP D CG    1 
ATOM   15448 O  OD1   . ASP D 2 276 ? 157.858 119.951 135.629 1.00 31.10 ?  255 ASP D OD1   1 
ATOM   15449 O  OD2   . ASP D 2 276 ? 158.527 120.120 133.545 1.00 29.88 -1 255 ASP D OD2   1 
ATOM   15450 N  N     . VAL D 2 277 ? 157.908 114.788 135.108 1.00 21.21 ?  256 VAL D N     1 
ATOM   15451 C  CA    . VAL D 2 277 ? 157.190 113.510 135.079 1.00 20.51 ?  256 VAL D CA    1 
ATOM   15452 C  C     . VAL D 2 277 ? 156.836 113.040 136.495 1.00 20.32 ?  256 VAL D C     1 
ATOM   15453 O  O     . VAL D 2 277 ? 155.734 112.550 136.726 1.00 19.81 ?  256 VAL D O     1 
ATOM   15454 C  CB    . VAL D 2 277 ? 157.975 112.400 134.322 1.00 20.30 ?  256 VAL D CB    1 
ATOM   15455 C  CG1   . VAL D 2 277 ? 157.226 111.080 134.382 1.00 21.16 ?  256 VAL D CG1   1 
ATOM   15456 C  CG2   . VAL D 2 277 ? 158.196 112.802 132.874 1.00 19.06 ?  256 VAL D CG2   1 
ATOM   15457 N  N     . LYS D 2 278 ? 157.769 113.216 137.430 1.00 19.84 ?  257 LYS D N     1 
ATOM   15458 C  CA    . LYS D 2 278 ? 157.539 112.864 138.831 1.00 20.27 ?  257 LYS D CA    1 
ATOM   15459 C  C     . LYS D 2 278 ? 156.353 113.621 139.443 1.00 20.16 ?  257 LYS D C     1 
ATOM   15460 O  O     . LYS D 2 278 ? 155.558 113.021 140.162 1.00 19.88 ?  257 LYS D O     1 
ATOM   15461 C  CB    . LYS D 2 278 ? 158.809 113.045 139.667 1.00 20.20 ?  257 LYS D CB    1 
ATOM   15462 C  CG    . LYS D 2 278 ? 159.859 111.971 139.402 1.00 21.60 ?  257 LYS D CG    1 
ATOM   15463 C  CD    . LYS D 2 278 ? 161.202 112.323 140.030 1.00 21.53 ?  257 LYS D CD    1 
ATOM   15464 C  CE    . LYS D 2 278 ? 162.247 111.321 139.602 1.00 24.52 ?  257 LYS D CE    1 
ATOM   15465 N  NZ    . LYS D 2 278 ? 163.570 111.628 140.239 1.00 26.32 1  257 LYS D NZ    1 
ATOM   15466 N  N     . LYS D 2 279 ? 156.226 114.916 139.134 1.00 19.67 ?  258 LYS D N     1 
ATOM   15467 C  CA    . LYS D 2 279 ? 155.060 115.694 139.579 1.00 20.10 ?  258 LYS D CA    1 
ATOM   15468 C  C     . LYS D 2 279 ? 153.755 115.096 139.038 1.00 19.12 ?  258 LYS D C     1 
ATOM   15469 O  O     . LYS D 2 279 ? 152.761 115.023 139.761 1.00 18.59 ?  258 LYS D O     1 
ATOM   15470 C  CB    . LYS D 2 279 ? 155.169 117.178 139.178 1.00 20.54 ?  258 LYS D CB    1 
ATOM   15471 C  CG    . LYS D 2 279 ? 156.367 117.918 139.770 1.00 22.84 ?  258 LYS D CG    1 
ATOM   15472 C  CD    . LYS D 2 279 ? 156.142 119.447 139.833 1.00 24.16 ?  258 LYS D CD    1 
ATOM   15473 C  CE    . LYS D 2 279 ? 156.054 120.088 138.451 1.00 25.61 ?  258 LYS D CE    1 
ATOM   15474 N  NZ    . LYS D 2 279 ? 155.840 121.586 138.523 1.00 24.70 1  258 LYS D NZ    1 
ATOM   15475 N  N     . PHE D 2 280 ? 153.787 114.656 137.776 1.00 19.04 ?  259 PHE D N     1 
ATOM   15476 C  CA    . PHE D 2 280 ? 152.626 114.057 137.093 1.00 19.31 ?  259 PHE D CA    1 
ATOM   15477 C  C     . PHE D 2 280 ? 152.222 112.699 137.678 1.00 19.25 ?  259 PHE D C     1 
ATOM   15478 O  O     . PHE D 2 280 ? 151.030 112.390 137.798 1.00 19.71 ?  259 PHE D O     1 
ATOM   15479 C  CB    . PHE D 2 280 ? 152.925 113.907 135.601 1.00 19.04 ?  259 PHE D CB    1 
ATOM   15480 C  CG    . PHE D 2 280 ? 151.703 113.675 134.731 1.00 20.15 ?  259 PHE D CG    1 
ATOM   15481 C  CD1   . PHE D 2 280 ? 150.639 114.563 134.742 1.00 21.63 ?  259 PHE D CD1   1 
ATOM   15482 C  CD2   . PHE D 2 280 ? 151.659 112.584 133.861 1.00 19.95 ?  259 PHE D CD2   1 
ATOM   15483 C  CE1   . PHE D 2 280 ? 149.523 114.362 133.899 1.00 22.56 ?  259 PHE D CE1   1 
ATOM   15484 C  CE2   . PHE D 2 280 ? 150.567 112.370 133.022 1.00 20.29 ?  259 PHE D CE2   1 
ATOM   15485 C  CZ    . PHE D 2 280 ? 149.493 113.261 133.043 1.00 21.30 ?  259 PHE D CZ    1 
ATOM   15486 N  N     . ILE D 2 281 ? 153.212 111.883 138.027 1.00 19.36 ?  260 ILE D N     1 
ATOM   15487 C  CA    . ILE D 2 281 ? 152.968 110.630 138.747 1.00 19.45 ?  260 ILE D CA    1 
ATOM   15488 C  C     . ILE D 2 281 ? 152.239 110.856 140.090 1.00 19.61 ?  260 ILE D C     1 
ATOM   15489 O  O     . ILE D 2 281 ? 151.255 110.170 140.376 1.00 19.72 ?  260 ILE D O     1 
ATOM   15490 C  CB    . ILE D 2 281 ? 154.300 109.862 138.949 1.00 19.49 ?  260 ILE D CB    1 
ATOM   15491 C  CG1   . ILE D 2 281 ? 154.848 109.417 137.590 1.00 20.10 ?  260 ILE D CG1   1 
ATOM   15492 C  CG2   . ILE D 2 281 ? 154.159 108.682 139.936 1.00 20.53 ?  260 ILE D CG2   1 
ATOM   15493 C  CD1   . ILE D 2 281 ? 156.308 108.960 137.670 1.00 21.17 ?  260 ILE D CD1   1 
ATOM   15494 N  N     . ARG D 2 282 ? 152.711 111.812 140.892 1.00 19.75 ?  261 ARG D N     1 
ATOM   15495 C  CA    . ARG D 2 282 ? 152.122 112.072 142.220 1.00 20.34 ?  261 ARG D CA    1 
ATOM   15496 C  C     . ARG D 2 282 ? 150.696 112.601 142.115 1.00 21.18 ?  261 ARG D C     1 
ATOM   15497 O  O     . ARG D 2 282 ? 149.810 112.214 142.890 1.00 21.68 ?  261 ARG D O     1 
ATOM   15498 C  CB    . ARG D 2 282 ? 152.994 113.030 143.041 1.00 20.20 ?  261 ARG D CB    1 
ATOM   15499 C  CG    . ARG D 2 282 ? 154.297 112.417 143.521 1.00 20.57 ?  261 ARG D CG    1 
ATOM   15500 C  CD    . ARG D 2 282 ? 155.040 113.360 144.470 1.00 23.15 ?  261 ARG D CD    1 
ATOM   15501 N  NE    . ARG D 2 282 ? 155.667 114.498 143.795 1.00 23.46 ?  261 ARG D NE    1 
ATOM   15502 C  CZ    . ARG D 2 282 ? 156.898 114.492 143.285 1.00 22.84 ?  261 ARG D CZ    1 
ATOM   15503 N  NH1   . ARG D 2 282 ? 157.644 113.396 143.332 1.00 23.37 1  261 ARG D NH1   1 
ATOM   15504 N  NH2   . ARG D 2 282 ? 157.380 115.588 142.714 1.00 22.27 ?  261 ARG D NH2   1 
ATOM   15505 N  N     . TYR D 2 283 ? 150.492 113.503 141.162 1.00 21.46 ?  262 TYR D N     1 
ATOM   15506 C  CA    . TYR D 2 283 ? 149.171 114.059 140.874 1.00 22.97 ?  262 TYR D CA    1 
ATOM   15507 C  C     . TYR D 2 283 ? 148.184 112.931 140.496 1.00 22.12 ?  262 TYR D C     1 
ATOM   15508 O  O     . TYR D 2 283 ? 147.045 112.905 140.968 1.00 22.00 ?  262 TYR D O     1 
ATOM   15509 C  CB    . TYR D 2 283 ? 149.317 115.114 139.771 1.00 23.37 ?  262 TYR D CB    1 
ATOM   15510 C  CG    . TYR D 2 283 ? 148.047 115.561 139.087 1.00 27.31 ?  262 TYR D CG    1 
ATOM   15511 C  CD1   . TYR D 2 283 ? 147.280 116.603 139.609 1.00 30.79 ?  262 TYR D CD1   1 
ATOM   15512 C  CD2   . TYR D 2 283 ? 147.637 114.972 137.891 1.00 30.31 ?  262 TYR D CD2   1 
ATOM   15513 C  CE1   . TYR D 2 283 ? 146.103 117.026 138.969 1.00 33.18 ?  262 TYR D CE1   1 
ATOM   15514 C  CE2   . TYR D 2 283 ? 146.474 115.391 137.238 1.00 33.20 ?  262 TYR D CE2   1 
ATOM   15515 C  CZ    . TYR D 2 283 ? 145.718 116.422 137.782 1.00 34.74 ?  262 TYR D CZ    1 
ATOM   15516 O  OH    . TYR D 2 283 ? 144.573 116.839 137.131 1.00 37.63 ?  262 TYR D OH    1 
ATOM   15517 N  N     . ASN D 2 284 ? 148.638 111.975 139.691 1.00 21.63 ?  263 ASN D N     1 
ATOM   15518 C  CA    . ASN D 2 284 ? 147.779 110.862 139.294 1.00 21.41 ?  263 ASN D CA    1 
ATOM   15519 C  C     . ASN D 2 284 ? 147.616 109.796 140.382 1.00 20.86 ?  263 ASN D C     1 
ATOM   15520 O  O     . ASN D 2 284 ? 146.568 109.167 140.468 1.00 20.92 ?  263 ASN D O     1 
ATOM   15521 C  CB    . ASN D 2 284 ? 148.218 110.270 137.953 1.00 21.15 ?  263 ASN D CB    1 
ATOM   15522 C  CG    . ASN D 2 284 ? 147.837 111.166 136.782 1.00 22.59 ?  263 ASN D CG    1 
ATOM   15523 O  OD1   . ASN D 2 284 ? 146.661 111.275 136.428 1.00 22.35 ?  263 ASN D OD1   1 
ATOM   15524 N  ND2   . ASN D 2 284 ? 148.828 111.823 136.185 1.00 22.93 ?  263 ASN D ND2   1 
ATOM   15525 N  N     . ALA D 2 285 ? 148.644 109.607 141.209 1.00 20.92 ?  264 ALA D N     1 
ATOM   15526 C  CA    . ALA D 2 285 ? 148.523 108.781 142.423 1.00 20.77 ?  264 ALA D CA    1 
ATOM   15527 C  C     . ALA D 2 285 ? 147.400 109.281 143.339 1.00 21.13 ?  264 ALA D C     1 
ATOM   15528 O  O     . ALA D 2 285 ? 146.611 108.481 143.857 1.00 19.92 ?  264 ALA D O     1 
ATOM   15529 C  CB    . ALA D 2 285 ? 149.857 108.724 143.182 1.00 20.68 ?  264 ALA D CB    1 
ATOM   15530 N  N     . ASN D 2 286 ? 147.332 110.604 143.526 1.00 21.38 ?  265 ASN D N     1 
ATOM   15531 C  CA    . ASN D 2 286 ? 146.263 111.234 144.305 1.00 21.94 ?  265 ASN D CA    1 
ATOM   15532 C  C     . ASN D 2 286 ? 144.870 110.984 143.699 1.00 22.13 ?  265 ASN D C     1 
ATOM   15533 O  O     . ASN D 2 286 ? 143.912 110.754 144.427 1.00 21.95 ?  265 ASN D O     1 
ATOM   15534 C  CB    . ASN D 2 286 ? 146.500 112.739 144.442 1.00 22.22 ?  265 ASN D CB    1 
ATOM   15535 C  CG    . ASN D 2 286 ? 147.531 113.095 145.510 1.00 22.80 ?  265 ASN D CG    1 
ATOM   15536 O  OD1   . ASN D 2 286 ? 147.926 112.267 146.339 1.00 22.57 ?  265 ASN D OD1   1 
ATOM   15537 N  ND2   . ASN D 2 286 ? 147.974 114.346 145.483 1.00 23.91 ?  265 ASN D ND2   1 
ATOM   15538 N  N     . LYS D 2 287 ? 144.765 111.020 142.373 1.00 22.51 ?  266 LYS D N     1 
ATOM   15539 C  CA    . LYS D 2 287 ? 143.491 110.711 141.707 1.00 22.91 ?  266 LYS D CA    1 
ATOM   15540 C  C     . LYS D 2 287 ? 143.076 109.255 141.951 1.00 22.33 ?  266 LYS D C     1 
ATOM   15541 O  O     . LYS D 2 287 ? 141.912 108.984 142.217 1.00 22.24 ?  266 LYS D O     1 
ATOM   15542 C  CB    . LYS D 2 287 ? 143.559 111.008 140.203 1.00 23.65 ?  266 LYS D CB    1 
ATOM   15543 C  CG    . LYS D 2 287 ? 143.512 112.499 139.865 1.00 26.50 ?  266 LYS D CG    1 
ATOM   15544 C  CD    . LYS D 2 287 ? 143.569 112.714 138.341 1.00 31.30 ?  266 LYS D CD    1 
ATOM   15545 C  CE    . LYS D 2 287 ? 143.029 114.087 137.982 1.00 35.08 ?  266 LYS D CE    1 
ATOM   15546 N  NZ    . LYS D 2 287 ? 143.016 114.363 136.514 1.00 37.66 1  266 LYS D NZ    1 
ATOM   15547 N  N     . ALA D 2 288 ? 144.041 108.337 141.871 1.00 21.41 ?  267 ALA D N     1 
ATOM   15548 C  CA    . ALA D 2 288 ? 143.818 106.913 142.125 1.00 21.53 ?  267 ALA D CA    1 
ATOM   15549 C  C     . ALA D 2 288 ? 143.320 106.664 143.559 1.00 21.77 ?  267 ALA D C     1 
ATOM   15550 O  O     . ALA D 2 288 ? 142.367 105.898 143.786 1.00 21.59 ?  267 ALA D O     1 
ATOM   15551 C  CB    . ALA D 2 288 ? 145.098 106.113 141.842 1.00 21.33 ?  267 ALA D CB    1 
ATOM   15552 N  N     . LEU D 2 289 ? 143.949 107.328 144.520 1.00 21.71 ?  268 LEU D N     1 
ATOM   15553 C  CA    . LEU D 2 289 ? 143.496 107.257 145.903 1.00 22.36 ?  268 LEU D CA    1 
ATOM   15554 C  C     . LEU D 2 289 ? 142.080 107.797 146.046 1.00 23.01 ?  268 LEU D C     1 
ATOM   15555 O  O     . LEU D 2 289 ? 141.234 107.170 146.688 1.00 23.14 ?  268 LEU D O     1 
ATOM   15556 C  CB    . LEU D 2 289 ? 144.470 107.982 146.840 1.00 22.61 ?  268 LEU D CB    1 
ATOM   15557 C  CG    . LEU D 2 289 ? 145.837 107.292 147.037 1.00 21.22 ?  268 LEU D CG    1 
ATOM   15558 C  CD1   . LEU D 2 289 ? 146.826 108.231 147.713 1.00 20.77 ?  268 LEU D CD1   1 
ATOM   15559 C  CD2   . LEU D 2 289 ? 145.712 105.973 147.831 1.00 21.40 ?  268 LEU D CD2   1 
ATOM   15560 N  N     . MET D 2 290 ? 141.800 108.941 145.431 1.00 23.87 ?  269 MET D N     1 
ATOM   15561 C  CA    . MET D 2 290 ? 140.446 109.483 145.506 1.00 25.26 ?  269 MET D CA    1 
ATOM   15562 C  C     . MET D 2 290 ? 139.412 108.535 144.874 1.00 24.37 ?  269 MET D C     1 
ATOM   15563 O  O     . MET D 2 290 ? 138.321 108.385 145.416 1.00 23.97 ?  269 MET D O     1 
ATOM   15564 C  CB    . MET D 2 290 ? 140.386 110.911 144.976 1.00 25.94 ?  269 MET D CB    1 
ATOM   15565 C  CG    . MET D 2 290 ? 140.905 111.914 146.026 1.00 31.08 ?  269 MET D CG    1 
ATOM   15566 S  SD    . MET D 2 290 ? 140.904 113.637 145.483 1.00 41.28 ?  269 MET D SD    1 
ATOM   15567 C  CE    . MET D 2 290 ? 139.194 113.838 144.920 1.00 38.56 ?  269 MET D CE    1 
ATOM   15568 N  N     . ASN D 2 291 ? 139.773 107.863 143.776 1.00 23.66 ?  270 ASN D N     1 
ATOM   15569 C  CA    . ASN D 2 291 ? 138.915 106.803 143.196 1.00 23.17 ?  270 ASN D CA    1 
ATOM   15570 C  C     . ASN D 2 291 ? 138.560 105.676 144.170 1.00 23.22 ?  270 ASN D C     1 
ATOM   15571 O  O     . ASN D 2 291 ? 137.495 105.070 144.063 1.00 22.68 ?  270 ASN D O     1 
ATOM   15572 C  CB    . ASN D 2 291 ? 139.541 106.195 141.931 1.00 22.41 ?  270 ASN D CB    1 
ATOM   15573 C  CG    . ASN D 2 291 ? 139.554 107.158 140.766 1.00 21.93 ?  270 ASN D CG    1 
ATOM   15574 O  OD1   . ASN D 2 291 ? 138.885 108.196 140.793 1.00 20.94 ?  270 ASN D OD1   1 
ATOM   15575 N  ND2   . ASN D 2 291 ? 140.317 106.821 139.729 1.00 19.20 ?  270 ASN D ND2   1 
ATOM   15576 N  N     . LEU D 2 292 ? 139.467 105.409 145.109 1.00 23.53 ?  271 LEU D N     1 
ATOM   15577 C  CA    . LEU D 2 292 ? 139.274 104.379 146.132 1.00 24.21 ?  271 LEU D CA    1 
ATOM   15578 C  C     . LEU D 2 292 ? 138.678 104.952 147.422 1.00 25.14 ?  271 LEU D C     1 
ATOM   15579 O  O     . LEU D 2 292 ? 138.616 104.265 148.454 1.00 25.14 ?  271 LEU D O     1 
ATOM   15580 C  CB    . LEU D 2 292 ? 140.605 103.651 146.418 1.00 23.71 ?  271 LEU D CB    1 
ATOM   15581 C  CG    . LEU D 2 292 ? 141.234 102.843 145.274 1.00 23.37 ?  271 LEU D CG    1 
ATOM   15582 C  CD1   . LEU D 2 292 ? 142.703 102.529 145.568 1.00 23.28 ?  271 LEU D CD1   1 
ATOM   15583 C  CD2   . LEU D 2 292 ? 140.445 101.550 144.988 1.00 23.06 ?  271 LEU D CD2   1 
ATOM   15584 N  N     . GLY D 2 293 ? 138.232 106.208 147.353 1.00 25.82 ?  272 GLY D N     1 
ATOM   15585 C  CA    . GLY D 2 293 ? 137.629 106.887 148.493 1.00 27.13 ?  272 GLY D CA    1 
ATOM   15586 C  C     . GLY D 2 293 ? 138.604 107.258 149.592 1.00 27.99 ?  272 GLY D C     1 
ATOM   15587 O  O     . GLY D 2 293 ? 138.191 107.505 150.722 1.00 27.97 ?  272 GLY D O     1 
ATOM   15588 N  N     . PHE D 2 294 ? 139.899 107.295 149.264 1.00 28.02 ?  273 PHE D N     1 
ATOM   15589 C  CA    . PHE D 2 294 ? 140.946 107.652 150.229 1.00 28.75 ?  273 PHE D CA    1 
ATOM   15590 C  C     . PHE D 2 294 ? 141.440 109.093 150.051 1.00 29.00 ?  273 PHE D C     1 
ATOM   15591 O  O     . PHE D 2 294 ? 141.265 109.688 148.990 1.00 28.74 ?  273 PHE D O     1 
ATOM   15592 C  CB    . PHE D 2 294 ? 142.138 106.687 150.109 1.00 28.32 ?  273 PHE D CB    1 
ATOM   15593 C  CG    . PHE D 2 294 ? 141.813 105.265 150.475 1.00 28.66 ?  273 PHE D CG    1 
ATOM   15594 C  CD1   . PHE D 2 294 ? 141.012 104.977 151.580 1.00 30.23 ?  273 PHE D CD1   1 
ATOM   15595 C  CD2   . PHE D 2 294 ? 142.322 104.214 149.724 1.00 26.94 ?  273 PHE D CD2   1 
ATOM   15596 C  CE1   . PHE D 2 294 ? 140.712 103.654 151.922 1.00 31.04 ?  273 PHE D CE1   1 
ATOM   15597 C  CE2   . PHE D 2 294 ? 142.036 102.896 150.053 1.00 27.39 ?  273 PHE D CE2   1 
ATOM   15598 C  CZ    . PHE D 2 294 ? 141.235 102.607 151.151 1.00 29.80 ?  273 PHE D CZ    1 
ATOM   15599 N  N     . ASP D 2 295 ? 142.053 109.644 151.098 1.00 29.60 ?  274 ASP D N     1 
ATOM   15600 C  CA    . ASP D 2 295 ? 142.628 110.985 151.047 1.00 30.40 ?  274 ASP D CA    1 
ATOM   15601 C  C     . ASP D 2 295 ? 143.880 111.033 150.150 1.00 29.58 ?  274 ASP D C     1 
ATOM   15602 O  O     . ASP D 2 295 ? 144.577 110.028 150.004 1.00 28.68 ?  274 ASP D O     1 
ATOM   15603 C  CB    . ASP D 2 295 ? 142.988 111.475 152.456 1.00 31.44 ?  274 ASP D CB    1 
ATOM   15604 C  CG    . ASP D 2 295 ? 141.768 111.666 153.351 1.00 34.27 ?  274 ASP D CG    1 
ATOM   15605 O  OD1   . ASP D 2 295 ? 140.661 111.957 152.835 1.00 36.43 ?  274 ASP D OD1   1 
ATOM   15606 O  OD2   . ASP D 2 295 ? 141.928 111.527 154.583 1.00 38.03 -1 274 ASP D OD2   1 
ATOM   15607 N  N     . PRO D 2 296 ? 144.171 112.207 149.557 1.00 29.59 ?  275 PRO D N     1 
ATOM   15608 C  CA    . PRO D 2 296 ? 145.405 112.314 148.774 1.00 29.09 ?  275 PRO D CA    1 
ATOM   15609 C  C     . PRO D 2 296 ? 146.631 112.082 149.656 1.00 29.26 ?  275 PRO D C     1 
ATOM   15610 O  O     . PRO D 2 296 ? 146.632 112.450 150.832 1.00 29.36 ?  275 PRO D O     1 
ATOM   15611 C  CB    . PRO D 2 296 ? 145.382 113.759 148.256 1.00 29.49 ?  275 PRO D CB    1 
ATOM   15612 C  CG    . PRO D 2 296 ? 144.405 114.488 149.138 1.00 30.28 ?  275 PRO D CG    1 
ATOM   15613 C  CD    . PRO D 2 296 ? 143.399 113.465 149.565 1.00 29.63 ?  275 PRO D CD    1 
ATOM   15614 N  N     . TYR D 2 297 ? 147.655 111.457 149.095 1.00 28.97 ?  276 TYR D N     1 
ATOM   15615 C  CA    . TYR D 2 297 ? 148.865 111.134 149.842 1.00 29.63 ?  276 TYR D CA    1 
ATOM   15616 C  C     . TYR D 2 297 ? 149.929 112.232 149.690 1.00 29.55 ?  276 TYR D C     1 
ATOM   15617 O  O     . TYR D 2 297 ? 150.694 112.516 150.621 1.00 30.12 ?  276 TYR D O     1 
ATOM   15618 C  CB    . TYR D 2 297 ? 149.413 109.800 149.334 1.00 29.49 ?  276 TYR D CB    1 
ATOM   15619 C  CG    . TYR D 2 297 ? 150.469 109.165 150.199 1.00 31.19 ?  276 TYR D CG    1 
ATOM   15620 C  CD1   . TYR D 2 297 ? 150.176 108.767 151.508 1.00 31.93 ?  276 TYR D CD1   1 
ATOM   15621 C  CD2   . TYR D 2 297 ? 151.754 108.935 149.706 1.00 31.98 ?  276 TYR D CD2   1 
ATOM   15622 C  CE1   . TYR D 2 297 ? 151.140 108.172 152.310 1.00 33.86 ?  276 TYR D CE1   1 
ATOM   15623 C  CE2   . TYR D 2 297 ? 152.729 108.332 150.503 1.00 33.88 ?  276 TYR D CE2   1 
ATOM   15624 C  CZ    . TYR D 2 297 ? 152.407 107.952 151.801 1.00 34.42 ?  276 TYR D CZ    1 
ATOM   15625 O  OH    . TYR D 2 297 ? 153.352 107.364 152.602 1.00 37.63 ?  276 TYR D OH    1 
ATOM   15626 N  N     . PHE D 2 298 ? 149.961 112.835 148.507 1.00 29.10 ?  277 PHE D N     1 
ATOM   15627 C  CA    . PHE D 2 298 ? 150.987 113.799 148.124 1.00 28.97 ?  277 PHE D CA    1 
ATOM   15628 C  C     . PHE D 2 298 ? 150.426 115.226 148.133 1.00 29.77 ?  277 PHE D C     1 
ATOM   15629 O  O     . PHE D 2 298 ? 149.243 115.437 147.853 1.00 29.07 ?  277 PHE D O     1 
ATOM   15630 C  CB    . PHE D 2 298 ? 151.521 113.469 146.726 1.00 27.99 ?  277 PHE D CB    1 
ATOM   15631 C  CG    . PHE D 2 298 ? 152.168 112.108 146.618 1.00 27.61 ?  277 PHE D CG    1 
ATOM   15632 C  CD1   . PHE D 2 298 ? 151.537 111.075 145.939 1.00 25.91 ?  277 PHE D CD1   1 
ATOM   15633 C  CD2   . PHE D 2 298 ? 153.423 111.871 147.183 1.00 27.32 ?  277 PHE D CD2   1 
ATOM   15634 C  CE1   . PHE D 2 298 ? 152.134 109.830 145.832 1.00 26.65 ?  277 PHE D CE1   1 
ATOM   15635 C  CE2   . PHE D 2 298 ? 154.032 110.633 147.083 1.00 25.38 ?  277 PHE D CE2   1 
ATOM   15636 C  CZ    . PHE D 2 298 ? 153.390 109.606 146.417 1.00 26.20 ?  277 PHE D CZ    1 
ATOM   15637 N  N     . GLU D 2 299 ? 151.283 116.192 148.461 1.00 31.10 ?  278 GLU D N     1 
ATOM   15638 C  CA    . GLU D 2 299 ? 150.927 117.612 148.383 1.00 32.86 ?  278 GLU D CA    1 
ATOM   15639 C  C     . GLU D 2 299 ? 150.581 117.983 146.934 1.00 33.04 ?  278 GLU D C     1 
ATOM   15640 O  O     . GLU D 2 299 ? 151.104 117.385 145.989 1.00 32.23 ?  278 GLU D O     1 
ATOM   15641 C  CB    . GLU D 2 299 ? 152.072 118.492 148.912 1.00 33.45 ?  278 GLU D CB    1 
ATOM   15642 C  CG    . GLU D 2 299 ? 153.373 118.361 148.106 1.00 36.27 ?  278 GLU D CG    1 
ATOM   15643 C  CD    . GLU D 2 299 ? 154.477 119.321 148.525 1.00 40.47 ?  278 GLU D CD    1 
ATOM   15644 O  OE1   . GLU D 2 299 ? 154.671 119.549 149.741 1.00 41.72 ?  278 GLU D OE1   1 
ATOM   15645 O  OE2   . GLU D 2 299 ? 155.174 119.824 147.616 1.00 42.65 -1 278 GLU D OE2   1 
ATOM   15646 N  N     . GLU D 2 300 ? 149.696 118.966 146.780 1.00 34.09 ?  279 GLU D N     1 
ATOM   15647 C  CA    . GLU D 2 300 ? 149.281 119.456 145.472 1.00 35.06 ?  279 GLU D CA    1 
ATOM   15648 C  C     . GLU D 2 300 ? 150.450 120.146 144.768 1.00 34.97 ?  279 GLU D C     1 
ATOM   15649 O  O     . GLU D 2 300 ? 151.181 120.929 145.378 1.00 34.96 ?  279 GLU D O     1 
ATOM   15650 C  CB    . GLU D 2 300 ? 148.087 120.415 145.621 1.00 35.81 ?  279 GLU D CB    1 
ATOM   15651 C  CG    . GLU D 2 300 ? 147.451 120.840 144.296 1.00 38.58 ?  279 GLU D CG    1 
ATOM   15652 C  CD    . GLU D 2 300 ? 145.991 121.266 144.440 1.00 43.09 ?  279 GLU D CD    1 
ATOM   15653 O  OE1   . GLU D 2 300 ? 145.131 120.674 143.748 1.00 44.69 ?  279 GLU D OE1   1 
ATOM   15654 O  OE2   . GLU D 2 300 ? 145.702 122.181 145.245 1.00 44.94 -1 279 GLU D OE2   1 
ATOM   15655 N  N     . GLU D 2 301 ? 150.629 119.821 143.492 1.00 34.73 ?  280 GLU D N     1 
ATOM   15656 C  CA    . GLU D 2 301 ? 151.674 120.414 142.666 1.00 35.16 ?  280 GLU D CA    1 
ATOM   15657 C  C     . GLU D 2 301 ? 151.069 120.846 141.341 1.00 35.23 ?  280 GLU D C     1 
ATOM   15658 O  O     . GLU D 2 301 ? 150.078 120.268 140.884 1.00 34.92 ?  280 GLU D O     1 
ATOM   15659 C  CB    . GLU D 2 301 ? 152.795 119.400 142.407 1.00 35.10 ?  280 GLU D CB    1 
ATOM   15660 C  CG    . GLU D 2 301 ? 153.802 119.249 143.545 1.00 36.62 ?  280 GLU D CG    1 
ATOM   15661 C  CD    . GLU D 2 301 ? 154.731 118.048 143.362 1.00 37.59 ?  280 GLU D CD    1 
ATOM   15662 O  OE1   . GLU D 2 301 ? 154.232 116.910 143.234 1.00 38.10 ?  280 GLU D OE1   1 
ATOM   15663 O  OE2   . GLU D 2 301 ? 155.962 118.237 143.371 1.00 38.93 -1 280 GLU D OE2   1 
ATOM   15664 N  N     . ASP D 2 302 ? 151.661 121.859 140.721 1.00 35.60 ?  281 ASP D N     1 
ATOM   15665 C  CA    . ASP D 2 302 ? 151.232 122.268 139.389 1.00 35.96 ?  281 ASP D CA    1 
ATOM   15666 C  C     . ASP D 2 302 ? 151.848 121.319 138.369 1.00 35.01 ?  281 ASP D C     1 
ATOM   15667 O  O     . ASP D 2 302 ? 152.901 120.734 138.624 1.00 35.52 ?  281 ASP D O     1 
ATOM   15668 C  CB    . ASP D 2 302 ? 151.590 123.739 139.111 1.00 36.82 ?  281 ASP D CB    1 
ATOM   15669 C  CG    . ASP D 2 302 ? 153.106 124.009 139.102 1.00 39.01 ?  281 ASP D CG    1 
ATOM   15670 O  OD1   . ASP D 2 302 ? 153.900 123.223 139.678 1.00 40.83 ?  281 ASP D OD1   1 
ATOM   15671 O  OD2   . ASP D 2 302 ? 153.500 125.043 138.525 1.00 41.13 -1 281 ASP D OD2   1 
ATOM   15672 N  N     . ILE D 2 303 ? 151.182 121.130 137.239 1.00 33.94 ?  282 ILE D N     1 
ATOM   15673 C  CA    . ILE D 2 303 ? 151.685 120.226 136.207 1.00 33.00 ?  282 ILE D CA    1 
ATOM   15674 C  C     . ILE D 2 303 ? 152.254 120.985 135.001 1.00 31.59 ?  282 ILE D C     1 
ATOM   15675 O  O     . ILE D 2 303 ? 151.832 122.106 134.710 1.00 31.14 ?  282 ILE D O     1 
ATOM   15676 C  CB    . ILE D 2 303 ? 150.610 119.165 135.805 1.00 33.44 ?  282 ILE D CB    1 
ATOM   15677 C  CG1   . ILE D 2 303 ? 150.758 118.723 134.344 1.00 34.29 ?  282 ILE D CG1   1 
ATOM   15678 C  CG2   . ILE D 2 303 ? 149.210 119.684 136.088 1.00 35.47 ?  282 ILE D CG2   1 
ATOM   15679 C  CD1   . ILE D 2 303 ? 149.626 117.850 133.841 1.00 36.30 ?  282 ILE D CD1   1 
ATOM   15680 N  N     . ASN D 2 304 ? 153.228 120.375 134.326 1.00 29.53 ?  283 ASN D N     1 
ATOM   15681 C  CA    . ASN D 2 304 ? 153.799 120.939 133.106 1.00 28.49 ?  283 ASN D CA    1 
ATOM   15682 C  C     . ASN D 2 304 ? 152.700 121.439 132.144 1.00 27.87 ?  283 ASN D C     1 
ATOM   15683 O  O     . ASN D 2 304 ? 151.805 120.678 131.782 1.00 27.02 ?  283 ASN D O     1 
ATOM   15684 C  CB    . ASN D 2 304 ? 154.684 119.900 132.415 1.00 28.20 ?  283 ASN D CB    1 
ATOM   15685 C  CG    . ASN D 2 304 ? 155.377 120.454 131.198 1.00 28.17 ?  283 ASN D CG    1 
ATOM   15686 O  OD1   . ASN D 2 304 ? 154.813 120.465 130.108 1.00 29.01 ?  283 ASN D OD1   1 
ATOM   15687 N  ND2   . ASN D 2 304 ? 156.605 120.916 131.371 1.00 27.24 ?  283 ASN D ND2   1 
ATOM   15688 N  N     . PRO D 2 305 ? 152.759 122.726 131.744 1.00 28.00 ?  284 PRO D N     1 
ATOM   15689 C  CA    . PRO D 2 305 ? 151.685 123.310 130.925 1.00 27.58 ?  284 PRO D CA    1 
ATOM   15690 C  C     . PRO D 2 305 ? 151.560 122.718 129.520 1.00 27.01 ?  284 PRO D C     1 
ATOM   15691 O  O     . PRO D 2 305 ? 150.483 122.766 128.934 1.00 26.66 ?  284 PRO D O     1 
ATOM   15692 C  CB    . PRO D 2 305 ? 152.059 124.797 130.845 1.00 28.21 ?  284 PRO D CB    1 
ATOM   15693 C  CG    . PRO D 2 305 ? 153.487 124.865 131.169 1.00 28.80 ?  284 PRO D CG    1 
ATOM   15694 C  CD    . PRO D 2 305 ? 153.739 123.748 132.157 1.00 28.11 ?  284 PRO D CD    1 
ATOM   15695 N  N     . ILE D 2 306 ? 152.645 122.162 128.990 1.00 26.52 ?  285 ILE D N     1 
ATOM   15696 C  CA    . ILE D 2 306 ? 152.601 121.521 127.680 1.00 26.50 ?  285 ILE D CA    1 
ATOM   15697 C  C     . ILE D 2 306 ? 151.785 120.223 127.759 1.00 26.43 ?  285 ILE D C     1 
ATOM   15698 O  O     . ILE D 2 306 ? 150.887 119.980 126.940 1.00 26.00 ?  285 ILE D O     1 
ATOM   15699 C  CB    . ILE D 2 306 ? 154.019 121.289 127.103 1.00 26.88 ?  285 ILE D CB    1 
ATOM   15700 C  CG1   . ILE D 2 306 ? 154.743 122.639 126.942 1.00 26.98 ?  285 ILE D CG1   1 
ATOM   15701 C  CG2   . ILE D 2 306 ? 153.927 120.530 125.779 1.00 24.94 ?  285 ILE D CG2   1 
ATOM   15702 C  CD1   . ILE D 2 306 ? 156.196 122.543 126.566 1.00 26.65 ?  285 ILE D CD1   1 
ATOM   15703 N  N     . VAL D 2 307 ? 152.081 119.415 128.771 1.00 26.36 ?  286 VAL D N     1 
ATOM   15704 C  CA    . VAL D 2 307 ? 151.284 118.232 129.069 1.00 26.71 ?  286 VAL D CA    1 
ATOM   15705 C  C     . VAL D 2 307 ? 149.827 118.594 129.376 1.00 27.68 ?  286 VAL D C     1 
ATOM   15706 O  O     . VAL D 2 307 ? 148.920 117.919 128.889 1.00 27.92 ?  286 VAL D O     1 
ATOM   15707 C  CB    . VAL D 2 307 ? 151.930 117.372 130.189 1.00 26.37 ?  286 VAL D CB    1 
ATOM   15708 C  CG1   . VAL D 2 307 ? 150.976 116.270 130.677 1.00 25.48 ?  286 VAL D CG1   1 
ATOM   15709 C  CG2   . VAL D 2 307 ? 153.187 116.757 129.666 1.00 25.55 ?  286 VAL D CG2   1 
ATOM   15710 N  N     . LEU D 2 308 ? 149.595 119.669 130.136 1.00 28.80 ?  287 LEU D N     1 
ATOM   15711 C  CA    . LEU D 2 308 ? 148.221 120.144 130.362 1.00 30.07 ?  287 LEU D CA    1 
ATOM   15712 C  C     . LEU D 2 308 ? 147.494 120.486 129.057 1.00 30.38 ?  287 LEU D C     1 
ATOM   15713 O  O     . LEU D 2 308 ? 146.315 120.159 128.884 1.00 30.71 ?  287 LEU D O     1 
ATOM   15714 C  CB    . LEU D 2 308 ? 148.187 121.344 131.313 1.00 30.86 ?  287 LEU D CB    1 
ATOM   15715 C  CG    . LEU D 2 308 ? 148.194 121.010 132.809 1.00 32.62 ?  287 LEU D CG    1 
ATOM   15716 C  CD1   . LEU D 2 308 ? 148.368 122.264 133.637 1.00 33.97 ?  287 LEU D CD1   1 
ATOM   15717 C  CD2   . LEU D 2 308 ? 146.919 120.254 133.225 1.00 34.73 ?  287 LEU D CD2   1 
ATOM   15718 N  N     . ASN D 2 309 ? 148.198 121.134 128.136 1.00 30.81 ?  288 ASN D N     1 
ATOM   15719 C  CA    . ASN D 2 309 ? 147.617 121.464 126.839 1.00 31.25 ?  288 ASN D CA    1 
ATOM   15720 C  C     . ASN D 2 309 ? 147.276 120.207 126.036 1.00 31.83 ?  288 ASN D C     1 
ATOM   15721 O  O     . ASN D 2 309 ? 146.287 120.183 125.298 1.00 31.73 ?  288 ASN D O     1 
ATOM   15722 C  CB    . ASN D 2 309 ? 148.523 122.404 126.037 1.00 31.21 ?  288 ASN D CB    1 
ATOM   15723 C  CG    . ASN D 2 309 ? 147.849 122.918 124.775 1.00 31.41 ?  288 ASN D CG    1 
ATOM   15724 O  OD1   . ASN D 2 309 ? 146.677 123.311 124.801 1.00 31.88 ?  288 ASN D OD1   1 
ATOM   15725 N  ND2   . ASN D 2 309 ? 148.579 122.910 123.665 1.00 29.12 ?  288 ASN D ND2   1 
ATOM   15726 N  N     . GLY D 2 310 ? 148.097 119.168 126.194 1.00 32.04 ?  289 GLY D N     1 
ATOM   15727 C  CA    . GLY D 2 310 ? 147.814 117.859 125.616 1.00 33.04 ?  289 GLY D CA    1 
ATOM   15728 C  C     . GLY D 2 310 ? 146.574 117.231 126.239 1.00 33.85 ?  289 GLY D C     1 
ATOM   15729 O  O     . GLY D 2 310 ? 145.697 116.748 125.524 1.00 34.05 ?  289 GLY D O     1 
ATOM   15730 N  N     . LEU D 2 311 ? 146.504 117.245 127.570 1.00 34.33 ?  290 LEU D N     1 
ATOM   15731 C  CA    . LEU D 2 311 ? 145.384 116.662 128.314 1.00 35.77 ?  290 LEU D CA    1 
ATOM   15732 C  C     . LEU D 2 311 ? 144.044 117.323 128.007 1.00 37.01 ?  290 LEU D C     1 
ATOM   15733 O  O     . LEU D 2 311 ? 143.024 116.643 127.889 1.00 37.18 ?  290 LEU D O     1 
ATOM   15734 C  CB    . LEU D 2 311 ? 145.637 116.749 129.825 1.00 35.50 ?  290 LEU D CB    1 
ATOM   15735 C  CG    . LEU D 2 311 ? 146.346 115.633 130.584 1.00 35.45 ?  290 LEU D CG    1 
ATOM   15736 C  CD1   . LEU D 2 311 ? 146.616 116.095 132.025 1.00 35.28 ?  290 LEU D CD1   1 
ATOM   15737 C  CD2   . LEU D 2 311 ? 145.544 114.328 130.583 1.00 34.16 ?  290 LEU D CD2   1 
ATOM   15738 N  N     . LYS D 2 330 ? 119.838 115.832 148.066 1.00 42.55 ?  309 LYS D N     1 
ATOM   15739 C  CA    . LYS D 2 330 ? 118.438 115.607 147.728 1.00 44.90 ?  309 LYS D CA    1 
ATOM   15740 C  C     . LYS D 2 330 ? 117.625 115.171 148.942 1.00 43.76 ?  309 LYS D C     1 
ATOM   15741 O  O     . LYS D 2 330 ? 117.522 113.981 149.237 1.00 44.28 ?  309 LYS D O     1 
ATOM   15742 C  CB    . LYS D 2 330 ? 118.317 114.558 146.619 1.00 40.63 ?  309 LYS D CB    1 
ATOM   15743 C  CG    . LYS D 2 330 ? 116.943 114.499 145.967 1.00 43.98 ?  309 LYS D CG    1 
ATOM   15744 C  CD    . LYS D 2 330 ? 116.589 115.809 145.282 1.00 43.19 ?  309 LYS D CD    1 
ATOM   15745 C  CE    . LYS D 2 330 ? 116.585 115.656 143.770 1.00 45.38 ?  309 LYS D CE    1 
ATOM   15746 N  NZ    . LYS D 2 330 ? 116.536 116.973 143.078 1.00 43.90 1  309 LYS D NZ    1 
ATOM   15747 N  N     . ALA D 2 331 ? 117.052 116.144 149.645 1.00 41.98 ?  310 ALA D N     1 
ATOM   15748 C  CA    . ALA D 2 331 ? 116.162 115.843 150.753 1.00 42.36 ?  310 ALA D CA    1 
ATOM   15749 C  C     . ALA D 2 331 ? 114.834 115.302 150.231 1.00 42.70 ?  310 ALA D C     1 
ATOM   15750 O  O     . ALA D 2 331 ? 114.446 115.536 149.083 1.00 44.14 ?  310 ALA D O     1 
ATOM   15751 C  CB    . ALA D 2 331 ? 115.925 117.084 151.613 1.00 39.32 ?  310 ALA D CB    1 
ATOM   15752 N  N     . THR D 2 332 ? 114.138 114.568 151.093 1.00 33.29 ?  311 THR D N     1 
ATOM   15753 C  CA    . THR D 2 332 ? 112.880 113.927 150.719 1.00 32.46 ?  311 THR D CA    1 
ATOM   15754 C  C     . THR D 2 332 ? 111.841 115.004 150.438 1.00 32.78 ?  311 THR D C     1 
ATOM   15755 O  O     . THR D 2 332 ? 111.538 115.833 151.298 1.00 35.85 ?  311 THR D O     1 
ATOM   15756 C  CB    . THR D 2 332 ? 112.412 112.983 151.822 1.00 36.71 ?  311 THR D CB    1 
ATOM   15757 O  OG1   . THR D 2 332 ? 113.121 111.743 151.722 1.00 39.19 ?  311 THR D OG1   1 
ATOM   15758 C  CG2   . THR D 2 332 ? 110.920 112.707 151.689 1.00 34.82 ?  311 THR D CG2   1 
ATOM   15759 N  N     . VAL D 2 333 ? 111.301 115.006 149.222 1.00 30.31 ?  312 VAL D N     1 
ATOM   15760 C  CA    . VAL D 2 333 ? 110.274 115.967 148.842 1.00 24.24 ?  312 VAL D CA    1 
ATOM   15761 C  C     . VAL D 2 333 ? 108.942 115.526 149.430 1.00 30.13 ?  312 VAL D C     1 
ATOM   15762 O  O     . VAL D 2 333 ? 108.418 114.462 149.080 1.00 35.56 ?  312 VAL D O     1 
ATOM   15763 C  CB    . VAL D 2 333 ? 110.183 116.116 147.313 1.00 29.05 ?  312 VAL D CB    1 
ATOM   15764 C  CG1   . VAL D 2 333 ? 109.210 117.224 146.947 1.00 31.60 ?  312 VAL D CG1   1 
ATOM   15765 C  CG2   . VAL D 2 333 ? 111.558 116.387 146.725 1.00 29.59 ?  312 VAL D CG2   1 
ATOM   15766 N  N     . GLU D 2 334 ? 108.387 116.336 150.325 1.00 28.79 ?  313 GLU D N     1 
ATOM   15767 C  CA    . GLU D 2 334 ? 107.107 116.044 150.955 1.00 29.66 ?  313 GLU D CA    1 
ATOM   15768 C  C     . GLU D 2 334 ? 106.165 117.215 150.712 1.00 31.26 ?  313 GLU D C     1 
ATOM   15769 O  O     . GLU D 2 334 ? 106.497 118.356 151.077 1.00 34.83 ?  313 GLU D O     1 
ATOM   15770 C  CB    . GLU D 2 334 ? 107.280 115.788 152.454 1.00 29.26 ?  313 GLU D CB    1 
ATOM   15771 C  CG    . GLU D 2 334 ? 105.986 115.797 153.244 1.00 33.58 ?  313 GLU D CG    1 
ATOM   15772 C  CD    . GLU D 2 334 ? 106.184 115.365 154.684 1.00 35.28 ?  313 GLU D CD    1 
ATOM   15773 O  OE1   . GLU D 2 334 ? 107.270 115.626 155.240 1.00 33.47 ?  313 GLU D OE1   1 
ATOM   15774 O  OE2   . GLU D 2 334 ? 105.253 114.761 155.260 1.00 31.19 -1 313 GLU D OE2   1 
ATOM   15775 N  N     . PRO D 2 335 ? 105.003 116.997 150.099 1.00 31.21 ?  314 PRO D N     1 
ATOM   15776 C  CA    . PRO D 2 335 ? 104.125 118.119 149.752 1.00 33.35 ?  314 PRO D CA    1 
ATOM   15777 C  C     . PRO D 2 335 ? 103.601 118.833 150.990 1.00 33.18 ?  314 PRO D C     1 
ATOM   15778 O  O     . PRO D 2 335 ? 103.431 118.234 152.054 1.00 33.38 ?  314 PRO D O     1 
ATOM   15779 C  CB    . PRO D 2 335 ? 102.990 117.450 148.969 1.00 30.11 ?  314 PRO D CB    1 
ATOM   15780 C  CG    . PRO D 2 335 ? 103.030 116.016 149.395 1.00 31.03 ?  314 PRO D CG    1 
ATOM   15781 C  CD    . PRO D 2 335 ? 104.477 115.714 149.607 1.00 33.22 ?  314 PRO D CD    1 
ATOM   15782 N  N     . LEU D 2 336 ? 103.350 120.131 150.843 1.00 30.38 ?  315 LEU D N     1 
ATOM   15783 C  CA    . LEU D 2 336 ? 102.722 120.902 151.903 1.00 26.61 ?  315 LEU D CA    1 
ATOM   15784 C  C     . LEU D 2 336 ? 101.274 120.463 152.073 1.00 27.64 ?  315 LEU D C     1 
ATOM   15785 O  O     . LEU D 2 336 ? 100.500 120.412 151.114 1.00 34.77 ?  315 LEU D O     1 
ATOM   15786 C  CB    . LEU D 2 336 ? 102.793 122.397 151.591 1.00 22.39 ?  315 LEU D CB    1 
ATOM   15787 C  CG    . LEU D 2 336 ? 104.096 123.099 151.979 1.00 25.97 ?  315 LEU D CG    1 
ATOM   15788 C  CD1   . LEU D 2 336 ? 104.087 124.545 151.512 1.00 19.59 ?  315 LEU D CD1   1 
ATOM   15789 C  CD2   . LEU D 2 336 ? 104.334 123.018 153.479 1.00 27.01 ?  315 LEU D CD2   1 
ATOM   15790 N  N     . LYS D 2 337 ? 100.912 120.145 153.315 1.00 28.30 ?  316 LYS D N     1 
ATOM   15791 C  CA    . LYS D 2 337 ? 99.630  119.518 153.619 1.00 36.46 ?  316 LYS D CA    1 
ATOM   15792 C  C     . LYS D 2 337 ? 98.580  120.507 154.104 1.00 36.32 ?  316 LYS D C     1 
ATOM   15793 O  O     . LYS D 2 337 ? 97.537  120.078 154.611 1.00 40.02 ?  316 LYS D O     1 
ATOM   15794 C  CB    . LYS D 2 337 ? 99.815  118.419 154.669 1.00 33.57 ?  316 LYS D CB    1 
ATOM   15795 C  CG    . LYS D 2 337 ? 101.011 117.520 154.428 1.00 36.47 ?  316 LYS D CG    1 
ATOM   15796 C  CD    . LYS D 2 337 ? 100.642 116.060 154.612 1.00 38.79 ?  316 LYS D CD    1 
ATOM   15797 C  CE    . LYS D 2 337 ? 101.882 115.189 154.678 1.00 37.56 ?  316 LYS D CE    1 
ATOM   15798 N  NZ    . LYS D 2 337 ? 102.725 115.355 153.465 1.00 36.72 1  316 LYS D NZ    1 
ATOM   15799 N  N     . ASP D 2 338 ? 98.837  121.813 153.981 1.00 24.38 ?  317 ASP D N     1 
ATOM   15800 C  CA    . ASP D 2 338 ? 98.004  122.860 154.568 1.00 29.04 ?  317 ASP D CA    1 
ATOM   15801 C  C     . ASP D 2 338 ? 98.042  122.756 156.089 1.00 28.87 ?  317 ASP D C     1 
ATOM   15802 O  O     . ASP D 2 338 ? 98.507  121.750 156.636 1.00 33.66 ?  317 ASP D O     1 
ATOM   15803 C  CB    . ASP D 2 338 ? 96.566  122.795 154.040 1.00 31.69 ?  317 ASP D CB    1 
ATOM   15804 C  CG    . ASP D 2 338 ? 95.770  124.044 154.361 1.00 32.42 ?  317 ASP D CG    1 
ATOM   15805 O  OD1   . ASP D 2 338 ? 96.391  125.093 154.626 1.00 34.34 ?  317 ASP D OD1   1 
ATOM   15806 O  OD2   . ASP D 2 338 ? 94.523  123.977 154.346 1.00 28.35 -1 317 ASP D OD2   1 
ATOM   15807 N  N     . ASP D 2 339 ? 97.604  123.813 156.777 1.00 22.82 ?  318 ASP D N     1 
ATOM   15808 C  CA    . ASP D 2 339 ? 97.735  123.947 158.227 1.00 24.73 ?  318 ASP D CA    1 
ATOM   15809 C  C     . ASP D 2 339 ? 99.206  124.069 158.612 1.00 24.49 ?  318 ASP D C     1 
ATOM   15810 O  O     . ASP D 2 339 ? 99.537  124.214 159.793 1.00 31.22 ?  318 ASP D O     1 
ATOM   15811 C  CB    . ASP D 2 339 ? 97.068  122.781 158.964 1.00 23.30 ?  318 ASP D CB    1 
ATOM   15812 C  CG    . ASP D 2 339 ? 95.697  122.450 158.409 1.00 31.35 ?  318 ASP D CG    1 
ATOM   15813 O  OD1   . ASP D 2 339 ? 94.799  123.316 158.484 1.00 29.84 ?  318 ASP D OD1   1 
ATOM   15814 O  OD2   . ASP D 2 339 ? 95.517  121.327 157.893 1.00 30.37 -1 318 ASP D OD2   1 
ATOM   15815 N  N     . ASP D 2 340 ? 100.091 124.007 157.619 1.00 24.54 ?  319 ASP D N     1 
ATOM   15816 C  CA    . ASP D 2 340 ? 101.480 124.413 157.760 1.00 16.40 ?  319 ASP D CA    1 
ATOM   15817 C  C     . ASP D 2 340 ? 101.645 125.909 157.556 1.00 13.50 ?  319 ASP D C     1 
ATOM   15818 O  O     . ASP D 2 340 ? 102.734 126.444 157.783 1.00 33.12 ?  319 ASP D O     1 
ATOM   15819 C  CB    . ASP D 2 340 ? 102.356 123.651 156.763 1.00 15.31 ?  319 ASP D CB    1 
ATOM   15820 C  CG    . ASP D 2 340 ? 102.455 122.174 157.082 1.00 20.12 ?  319 ASP D CG    1 
ATOM   15821 O  OD1   . ASP D 2 340 ? 102.380 121.814 158.275 1.00 32.00 ?  319 ASP D OD1   1 
ATOM   15822 O  OD2   . ASP D 2 340 ? 102.607 121.372 156.137 1.00 22.25 -1 319 ASP D OD2   1 
ATOM   15823 N  N     . PHE D 2 341 ? 100.579 126.587 157.127 1.00 10.33 ?  320 PHE D N     1 
ATOM   15824 C  CA    . PHE D 2 341 ? 100.564 128.030 156.952 1.00 15.27 ?  320 PHE D CA    1 
ATOM   15825 C  C     . PHE D 2 341 ? 99.952  128.732 158.156 1.00 19.34 ?  320 PHE D C     1 
ATOM   15826 O  O     . PHE D 2 341 ? 99.851  129.964 158.157 1.00 16.81 ?  320 PHE D O     1 
ATOM   15827 C  CB    . PHE D 2 341 ? 99.782  128.404 155.688 1.00 19.36 ?  320 PHE D CB    1 
ATOM   15828 C  CG    . PHE D 2 341 ? 100.405 127.905 154.418 1.00 13.21 ?  320 PHE D CG    1 
ATOM   15829 C  CD1   . PHE D 2 341 ? 101.311 128.683 153.720 1.00 12.45 ?  320 PHE D CD1   1 
ATOM   15830 C  CD2   . PHE D 2 341 ? 100.083 126.653 153.922 1.00 11.41 ?  320 PHE D CD2   1 
ATOM   15831 C  CE1   . PHE D 2 341 ? 101.881 128.223 152.549 1.00 11.53 ?  320 PHE D CE1   1 
ATOM   15832 C  CE2   . PHE D 2 341 ? 100.652 126.189 152.755 1.00 15.13 ?  320 PHE D CE2   1 
ATOM   15833 C  CZ    . PHE D 2 341 ? 101.552 126.975 152.068 1.00 8.25  ?  320 PHE D CZ    1 
ATOM   15834 N  N     . TYR D 2 342 ? 99.539  127.981 159.173 1.00 12.30 ?  321 TYR D N     1 
ATOM   15835 C  CA    . TYR D 2 342 ? 98.863  128.525 160.339 1.00 16.33 ?  321 TYR D CA    1 
ATOM   15836 C  C     . TYR D 2 342 ? 99.611  128.094 161.590 1.00 22.82 ?  321 TYR D C     1 
ATOM   15837 O  O     . TYR D 2 342 ? 100.114 126.969 161.666 1.00 19.28 ?  321 TYR D O     1 
ATOM   15838 C  CB    . TYR D 2 342 ? 97.407  128.052 160.402 1.00 12.46 ?  321 TYR D CB    1 
ATOM   15839 C  CG    . TYR D 2 342 ? 96.593  128.453 159.194 1.00 15.87 ?  321 TYR D CG    1 
ATOM   15840 C  CD1   . TYR D 2 342 ? 96.002  129.706 159.114 1.00 18.56 ?  321 TYR D CD1   1 
ATOM   15841 C  CD2   . TYR D 2 342 ? 96.422  127.579 158.129 1.00 15.63 ?  321 TYR D CD2   1 
ATOM   15842 C  CE1   . TYR D 2 342 ? 95.260  130.076 158.009 1.00 14.14 ?  321 TYR D CE1   1 
ATOM   15843 C  CE2   . TYR D 2 342 ? 95.682  127.940 157.020 1.00 15.01 ?  321 TYR D CE2   1 
ATOM   15844 C  CZ    . TYR D 2 342 ? 95.103  129.189 156.965 1.00 17.53 ?  321 TYR D CZ    1 
ATOM   15845 O  OH    . TYR D 2 342 ? 94.364  129.553 155.864 1.00 21.36 ?  321 TYR D OH    1 
ATOM   15846 N  N     . PHE D 2 343 ? 99.688  128.995 162.563 1.00 12.45 ?  322 PHE D N     1 
ATOM   15847 C  CA    . PHE D 2 343 ? 100.474 128.750 163.764 1.00 16.01 ?  322 PHE D CA    1 
ATOM   15848 C  C     . PHE D 2 343 ? 99.744  129.244 165.008 1.00 27.60 ?  322 PHE D C     1 
ATOM   15849 O  O     . PHE D 2 343 ? 98.908  130.145 164.936 1.00 22.19 ?  322 PHE D O     1 
ATOM   15850 C  CB    . PHE D 2 343 ? 101.842 129.427 163.645 1.00 18.28 ?  322 PHE D CB    1 
ATOM   15851 C  CG    . PHE D 2 343 ? 102.534 129.164 162.337 1.00 19.26 ?  322 PHE D CG    1 
ATOM   15852 C  CD1   . PHE D 2 343 ? 103.318 128.037 162.164 1.00 20.02 ?  322 PHE D CD1   1 
ATOM   15853 C  CD2   . PHE D 2 343 ? 102.384 130.037 161.272 1.00 13.80 ?  322 PHE D CD2   1 
ATOM   15854 C  CE1   . PHE D 2 343 ? 103.946 127.791 160.960 1.00 12.20 ?  322 PHE D CE1   1 
ATOM   15855 C  CE2   . PHE D 2 343 ? 103.008 129.795 160.067 1.00 9.90  ?  322 PHE D CE2   1 
ATOM   15856 C  CZ    . PHE D 2 343 ? 103.790 128.671 159.910 1.00 11.36 ?  322 PHE D CZ    1 
HETATM 15857 P  PG    . ATP E 3 .   ? 103.658 141.548 83.115  1.00 68.91 ?  801 ATP A PG    1 
HETATM 15858 O  O1G   . ATP E 3 .   ? 102.398 141.941 82.420  1.00 61.99 ?  801 ATP A O1G   1 
HETATM 15859 O  O2G   . ATP E 3 .   ? 104.808 142.541 82.914  1.00 61.48 -1 801 ATP A O2G   1 
HETATM 15860 O  O3G   . ATP E 3 .   ? 103.478 141.289 84.615  1.00 57.91 ?  801 ATP A O3G   1 
HETATM 15861 P  PB    . ATP E 3 .   ? 105.367 139.623 81.579  1.00 68.42 ?  801 ATP A PB    1 
HETATM 15862 O  O1B   . ATP E 3 .   ? 105.160 140.033 80.175  1.00 59.48 -1 801 ATP A O1B   1 
HETATM 15863 O  O2B   . ATP E 3 .   ? 106.701 140.040 82.199  1.00 59.06 ?  801 ATP A O2B   1 
HETATM 15864 O  O3B   . ATP E 3 .   ? 104.215 140.165 82.533  1.00 62.04 ?  801 ATP A O3B   1 
HETATM 15865 P  PA    . ATP E 3 .   ? 105.460 136.992 82.933  1.00 63.87 ?  801 ATP A PA    1 
HETATM 15866 O  O1A   . ATP E 3 .   ? 106.653 136.159 82.681  1.00 60.02 -1 801 ATP A O1A   1 
HETATM 15867 O  O2A   . ATP E 3 .   ? 104.155 136.214 83.099  1.00 58.33 ?  801 ATP A O2A   1 
HETATM 15868 O  O3A   . ATP E 3 .   ? 105.230 138.048 81.764  1.00 62.45 ?  801 ATP A O3A   1 
HETATM 15869 O  "O5'" . ATP E 3 .   ? 105.658 137.906 84.204  1.00 59.78 ?  801 ATP A "O5'" 1 
HETATM 15870 C  "C5'" . ATP E 3 .   ? 104.613 138.059 85.187  1.00 58.13 ?  801 ATP A "C5'" 1 
HETATM 15871 C  "C4'" . ATP E 3 .   ? 105.139 138.886 86.332  1.00 59.51 ?  801 ATP A "C4'" 1 
HETATM 15872 O  "O4'" . ATP E 3 .   ? 105.709 138.014 87.334  1.00 62.13 ?  801 ATP A "O4'" 1 
HETATM 15873 C  "C3'" . ATP E 3 .   ? 106.248 139.869 85.969  1.00 57.82 ?  801 ATP A "C3'" 1 
HETATM 15874 O  "O3'" . ATP E 3 .   ? 105.710 141.127 85.578  1.00 58.51 ?  801 ATP A "O3'" 1 
HETATM 15875 C  "C2'" . ATP E 3 .   ? 107.030 139.977 87.278  1.00 58.31 ?  801 ATP A "C2'" 1 
HETATM 15876 O  "O2'" . ATP E 3 .   ? 106.417 140.883 88.186  1.00 58.66 ?  801 ATP A "O2'" 1 
HETATM 15877 C  "C1'" . ATP E 3 .   ? 106.938 138.542 87.802  1.00 58.50 ?  801 ATP A "C1'" 1 
HETATM 15878 N  N9    . ATP E 3 .   ? 108.016 137.671 87.345  1.00 58.48 ?  801 ATP A N9    1 
HETATM 15879 C  C8    . ATP E 3 .   ? 107.906 136.569 86.538  1.00 58.26 ?  801 ATP A C8    1 
HETATM 15880 N  N7    . ATP E 3 .   ? 109.046 135.973 86.288  1.00 56.05 ?  801 ATP A N7    1 
HETATM 15881 C  C5    . ATP E 3 .   ? 109.975 136.737 86.980  1.00 58.55 ?  801 ATP A C5    1 
HETATM 15882 C  C6    . ATP E 3 .   ? 111.371 136.635 87.124  1.00 56.46 ?  801 ATP A C6    1 
HETATM 15883 N  N6    . ATP E 3 .   ? 112.112 135.680 86.553  1.00 55.74 ?  801 ATP A N6    1 
HETATM 15884 N  N1    . ATP E 3 .   ? 111.993 137.562 87.886  1.00 57.23 ?  801 ATP A N1    1 
HETATM 15885 C  C2    . ATP E 3 .   ? 111.262 138.523 88.456  1.00 55.67 ?  801 ATP A C2    1 
HETATM 15886 N  N3    . ATP E 3 .   ? 109.943 138.718 88.393  1.00 57.17 ?  801 ATP A N3    1 
HETATM 15887 C  C4    . ATP E 3 .   ? 109.354 137.788 87.636  1.00 59.07 ?  801 ATP A C4    1 
HETATM 15888 P  PB    . GDP F 4 .   ? 100.523 154.716 86.858  1.00 70.96 ?  802 GDP A PB    1 
HETATM 15889 O  O1B   . GDP F 4 .   ? 101.711 154.105 86.156  1.00 59.03 ?  802 GDP A O1B   1 
HETATM 15890 O  O2B   . GDP F 4 .   ? 99.919  155.786 85.982  1.00 60.98 -1 802 GDP A O2B   1 
HETATM 15891 O  O3B   . GDP F 4 .   ? 99.492  153.646 87.134  1.00 60.51 ?  802 GDP A O3B   1 
HETATM 15892 O  O3A   . GDP F 4 .   ? 101.023 155.382 88.233  1.00 58.04 ?  802 GDP A O3A   1 
HETATM 15893 P  PA    . GDP F 4 .   ? 101.564 154.483 89.453  1.00 62.53 ?  802 GDP A PA    1 
HETATM 15894 O  O1A   . GDP F 4 .   ? 101.178 155.094 90.778  1.00 60.36 -1 802 GDP A O1A   1 
HETATM 15895 O  O2A   . GDP F 4 .   ? 101.054 153.065 89.362  1.00 57.51 ?  802 GDP A O2A   1 
HETATM 15896 O  "O5'" . GDP F 4 .   ? 103.162 154.530 89.257  1.00 58.41 ?  802 GDP A "O5'" 1 
HETATM 15897 C  "C5'" . GDP F 4 .   ? 104.015 154.353 90.381  1.00 58.74 ?  802 GDP A "C5'" 1 
HETATM 15898 C  "C4'" . GDP F 4 .   ? 105.144 153.393 90.048  1.00 56.36 ?  802 GDP A "C4'" 1 
HETATM 15899 O  "O4'" . GDP F 4 .   ? 105.510 152.709 91.248  1.00 56.52 ?  802 GDP A "O4'" 1 
HETATM 15900 C  "C3'" . GDP F 4 .   ? 104.701 152.355 89.032  1.00 58.64 ?  802 GDP A "C3'" 1 
HETATM 15901 O  "O3'" . GDP F 4 .   ? 105.544 152.412 87.878  1.00 59.90 ?  802 GDP A "O3'" 1 
HETATM 15902 C  "C2'" . GDP F 4 .   ? 104.846 151.008 89.707  1.00 57.17 ?  802 GDP A "C2'" 1 
HETATM 15903 O  "O2'" . GDP F 4 .   ? 105.676 150.150 88.921  1.00 58.14 ?  802 GDP A "O2'" 1 
HETATM 15904 C  "C1'" . GDP F 4 .   ? 105.507 151.294 91.046  1.00 54.02 ?  802 GDP A "C1'" 1 
HETATM 15905 N  N9    . GDP F 4 .   ? 104.829 150.607 92.179  1.00 54.87 ?  802 GDP A N9    1 
HETATM 15906 C  C8    . GDP F 4 .   ? 105.473 150.039 93.213  1.00 56.62 ?  802 GDP A C8    1 
HETATM 15907 N  N7    . GDP F 4 .   ? 104.608 149.492 94.100  1.00 56.41 ?  802 GDP A N7    1 
HETATM 15908 C  C5    . GDP F 4 .   ? 103.366 149.721 93.641  1.00 56.75 ?  802 GDP A C5    1 
HETATM 15909 C  C6    . GDP F 4 .   ? 101.992 149.413 94.101  1.00 57.45 ?  802 GDP A C6    1 
HETATM 15910 O  O6    . GDP F 4 .   ? 101.797 148.789 95.166  1.00 57.90 ?  802 GDP A O6    1 
HETATM 15911 N  N1    . GDP F 4 .   ? 100.969 149.820 93.342  1.00 57.76 ?  802 GDP A N1    1 
HETATM 15912 C  C2    . GDP F 4 .   ? 101.153 150.493 92.193  1.00 56.48 ?  802 GDP A C2    1 
HETATM 15913 N  N2    . GDP F 4 .   ? 100.065 150.870 91.482  1.00 57.02 ?  802 GDP A N2    1 
HETATM 15914 N  N3    . GDP F 4 .   ? 102.383 150.810 91.712  1.00 58.50 ?  802 GDP A N3    1 
HETATM 15915 C  C4    . GDP F 4 .   ? 103.512 150.459 92.377  1.00 57.68 ?  802 GDP A C4    1 
HETATM 15916 P  PA    . TTP G 5 .   ? 143.441 148.379 135.805 1.00 19.24 ?  803 TTP A PA    1 
HETATM 15917 O  O1A   . TTP G 5 .   ? 142.012 148.165 136.233 1.00 19.64 -1 803 TTP A O1A   1 
HETATM 15918 O  O2A   . TTP G 5 .   ? 143.617 149.720 135.139 1.00 31.54 ?  803 TTP A O2A   1 
HETATM 15919 O  O3A   . TTP G 5 .   ? 144.458 148.225 137.040 1.00 30.64 ?  803 TTP A O3A   1 
HETATM 15920 P  PB    . TTP G 5 .   ? 144.663 149.388 138.128 1.00 31.57 ?  803 TTP A PB    1 
HETATM 15921 O  O1B   . TTP G 5 .   ? 144.443 150.760 137.543 1.00 27.79 -1 803 TTP A O1B   1 
HETATM 15922 O  O2B   . TTP G 5 .   ? 143.754 149.165 139.310 1.00 31.36 ?  803 TTP A O2B   1 
HETATM 15923 O  O3B   . TTP G 5 .   ? 146.198 149.174 138.553 1.00 27.98 ?  803 TTP A O3B   1 
HETATM 15924 P  PG    . TTP G 5 .   ? 147.382 149.324 137.473 1.00 26.76 ?  803 TTP A PG    1 
HETATM 15925 O  O1G   . TTP G 5 .   ? 147.004 150.338 136.421 1.00 32.07 ?  803 TTP A O1G   1 
HETATM 15926 O  O2G   . TTP G 5 .   ? 148.650 149.758 138.163 1.00 34.92 -1 803 TTP A O2G   1 
HETATM 15927 O  O3G   . TTP G 5 .   ? 147.617 147.987 136.819 1.00 18.37 ?  803 TTP A O3G   1 
HETATM 15928 O  "O5'" . TTP G 5 .   ? 143.933 147.200 134.836 1.00 23.88 ?  803 TTP A "O5'" 1 
HETATM 15929 C  "C5'" . TTP G 5 .   ? 144.475 146.016 135.409 1.00 21.43 ?  803 TTP A "C5'" 1 
HETATM 15930 C  "C4'" . TTP G 5 .   ? 144.484 144.912 134.367 1.00 24.35 ?  803 TTP A "C4'" 1 
HETATM 15931 O  "O4'" . TTP G 5 .   ? 144.320 143.667 135.044 1.00 31.28 ?  803 TTP A "O4'" 1 
HETATM 15932 C  "C3'" . TTP G 5 .   ? 143.326 145.082 133.404 1.00 26.08 ?  803 TTP A "C3'" 1 
HETATM 15933 O  "O3'" . TTP G 5 .   ? 143.807 145.194 132.062 1.00 24.00 ?  803 TTP A "O3'" 1 
HETATM 15934 C  "C2'" . TTP G 5 .   ? 142.481 143.835 133.538 1.00 25.88 ?  803 TTP A "C2'" 1 
HETATM 15935 C  "C1'" . TTP G 5 .   ? 143.186 142.951 134.554 1.00 25.26 ?  803 TTP A "C1'" 1 
HETATM 15936 N  N1    . TTP G 5 .   ? 142.287 142.664 135.670 1.00 25.70 ?  803 TTP A N1    1 
HETATM 15937 C  C2    . TTP G 5 .   ? 141.963 141.327 135.986 1.00 25.54 ?  803 TTP A C2    1 
HETATM 15938 O  O2    . TTP G 5 .   ? 142.450 140.400 135.304 1.00 22.46 ?  803 TTP A O2    1 
HETATM 15939 N  N3    . TTP G 5 .   ? 141.144 141.032 137.003 1.00 24.38 ?  803 TTP A N3    1 
HETATM 15940 C  C4    . TTP G 5 .   ? 140.609 142.002 137.748 1.00 29.17 ?  803 TTP A C4    1 
HETATM 15941 O  O4    . TTP G 5 .   ? 139.846 141.725 138.697 1.00 37.02 ?  803 TTP A O4    1 
HETATM 15942 C  C5    . TTP G 5 .   ? 140.934 143.414 137.438 1.00 28.26 ?  803 TTP A C5    1 
HETATM 15943 C  C5M   . TTP G 5 .   ? 140.353 144.535 138.255 1.00 26.39 ?  803 TTP A C5M   1 
HETATM 15944 C  C6    . TTP G 5 .   ? 141.785 143.680 136.378 1.00 27.03 ?  803 TTP A C6    1 
HETATM 15945 MG MG    . MG  H 6 .   ? 145.318 150.865 134.834 1.00 18.30 ?  804 MG  A MG    1 
HETATM 15946 P  PA    . TTP I 5 .   ? 116.878 148.287 126.079 1.00 24.11 ?  801 TTP B PA    1 
HETATM 15947 O  O1A   . TTP I 5 .   ? 118.326 148.687 126.198 1.00 30.19 -1 801 TTP B O1A   1 
HETATM 15948 O  O2A   . TTP I 5 .   ? 116.001 149.176 126.924 1.00 22.18 ?  801 TTP B O2A   1 
HETATM 15949 O  O3A   . TTP I 5 .   ? 116.416 148.267 124.541 1.00 32.55 ?  801 TTP B O3A   1 
HETATM 15950 P  PB    . TTP I 5 .   ? 115.587 149.483 123.893 1.00 29.61 ?  801 TTP B PB    1 
HETATM 15951 O  O1B   . TTP I 5 .   ? 115.577 150.713 124.765 1.00 32.07 -1 801 TTP B O1B   1 
HETATM 15952 O  O2B   . TTP I 5 .   ? 116.149 149.812 122.533 1.00 29.33 ?  801 TTP B O2B   1 
HETATM 15953 O  O3B   . TTP I 5 .   ? 114.123 148.826 123.776 1.00 19.28 ?  801 TTP B O3B   1 
HETATM 15954 P  PG    . TTP I 5 .   ? 112.871 149.441 124.579 1.00 31.34 ?  801 TTP B PG    1 
HETATM 15955 O  O1G   . TTP I 5 .   ? 112.460 150.753 123.959 1.00 34.07 ?  801 TTP B O1G   1 
HETATM 15956 O  O2G   . TTP I 5 .   ? 111.715 148.473 124.518 1.00 23.32 -1 801 TTP B O2G   1 
HETATM 15957 O  O3G   . TTP I 5 .   ? 113.257 149.663 126.020 1.00 34.53 ?  801 TTP B O3G   1 
HETATM 15958 O  "O5'" . TTP I 5 .   ? 116.664 146.752 126.502 1.00 24.93 ?  801 TTP B "O5'" 1 
HETATM 15959 C  "C5'" . TTP I 5 .   ? 115.711 146.450 127.514 1.00 24.44 ?  801 TTP B "C5'" 1 
HETATM 15960 C  "C4'" . TTP I 5 .   ? 115.762 144.971 127.858 1.00 24.00 ?  801 TTP B "C4'" 1 
HETATM 15961 O  "O4'" . TTP I 5 .   ? 115.964 144.195 126.679 1.00 28.53 ?  801 TTP B "O4'" 1 
HETATM 15962 C  "C3'" . TTP I 5 .   ? 116.923 144.652 128.781 1.00 27.23 ?  801 TTP B "C3'" 1 
HETATM 15963 O  "O3'" . TTP I 5 .   ? 116.480 144.559 130.137 1.00 27.74 ?  801 TTP B "O3'" 1 
HETATM 15964 C  "C2'" . TTP I 5 .   ? 117.445 143.312 128.305 1.00 27.40 ?  801 TTP B "C2'" 1 
HETATM 15965 C  "C1'" . TTP I 5 .   ? 116.735 143.032 126.990 1.00 29.90 ?  801 TTP B "C1'" 1 
HETATM 15966 N  N1    . TTP I 5 .   ? 117.722 142.769 125.944 1.00 28.87 ?  801 TTP B N1    1 
HETATM 15967 C  C2    . TTP I 5 .   ? 118.137 141.441 125.710 1.00 27.67 ?  801 TTP B C2    1 
HETATM 15968 O  O2    . TTP I 5 .   ? 117.644 140.520 126.394 1.00 29.22 ?  801 TTP B O2    1 
HETATM 15969 N  N3    . TTP I 5 .   ? 119.040 141.145 124.766 1.00 25.56 ?  801 TTP B N3    1 
HETATM 15970 C  C4    . TTP I 5 .   ? 119.579 142.110 124.021 1.00 29.58 ?  801 TTP B C4    1 
HETATM 15971 O  O4    . TTP I 5 .   ? 120.422 141.833 123.142 1.00 38.14 ?  801 TTP B O4    1 
HETATM 15972 C  C5    . TTP I 5 .   ? 119.165 143.516 124.250 1.00 24.40 ?  801 TTP B C5    1 
HETATM 15973 C  C5M   . TTP I 5 .   ? 119.751 144.632 123.429 1.00 26.91 ?  801 TTP B C5M   1 
HETATM 15974 C  C6    . TTP I 5 .   ? 118.228 143.783 125.236 1.00 27.32 ?  801 TTP B C6    1 
HETATM 15975 MG MG    . MG  J 6 .   ? 114.764 150.780 127.129 1.00 37.62 ?  802 MG  B MG    1 
HETATM 15976 P  PG    . ATP K 3 .   ? 154.383 139.112 179.821 1.00 70.08 ?  803 ATP B PG    1 
HETATM 15977 O  O1G   . ATP K 3 .   ? 154.305 139.703 178.454 1.00 62.41 ?  803 ATP B O1G   1 
HETATM 15978 O  O2G   . ATP K 3 .   ? 154.337 140.156 180.942 1.00 61.28 -1 803 ATP B O2G   1 
HETATM 15979 O  O3G   . ATP K 3 .   ? 153.322 138.040 180.091 1.00 60.15 ?  803 ATP B O3G   1 
HETATM 15980 P  PB    . ATP K 3 .   ? 156.351 136.893 180.274 1.00 67.84 ?  803 ATP B PB    1 
HETATM 15981 O  O1B   . ATP K 3 .   ? 157.633 136.677 179.573 1.00 59.55 -1 803 ATP B O1B   1 
HETATM 15982 O  O2B   . ATP K 3 .   ? 156.370 136.659 181.785 1.00 61.48 ?  803 ATP B O2B   1 
HETATM 15983 O  O3B   . ATP K 3 .   ? 155.780 138.360 180.031 1.00 62.14 ?  803 ATP B O3B   1 
HETATM 15984 P  PA    . ATP K 3 .   ? 154.816 135.376 178.248 1.00 67.77 ?  803 ATP B PA    1 
HETATM 15985 O  O1A   . ATP K 3 .   ? 153.386 135.574 177.939 1.00 60.17 -1 803 ATP B O1A   1 
HETATM 15986 O  O2A   . ATP K 3 .   ? 155.287 133.922 178.240 1.00 60.55 ?  803 ATP B O2A   1 
HETATM 15987 O  O3A   . ATP K 3 .   ? 155.193 135.983 179.670 1.00 61.79 ?  803 ATP B O3A   1 
HETATM 15988 O  "O5'" . ATP K 3 .   ? 155.732 136.200 177.261 1.00 60.51 ?  803 ATP B "O5'" 1 
HETATM 15989 C  "C5'" . ATP K 3 .   ? 155.852 135.833 175.869 1.00 57.17 ?  803 ATP B "C5'" 1 
HETATM 15990 C  "C4'" . ATP K 3 .   ? 155.334 136.966 175.018 1.00 59.72 ?  803 ATP B "C4'" 1 
HETATM 15991 O  "O4'" . ATP K 3 .   ? 154.652 136.427 173.864 1.00 60.83 ?  803 ATP B "O4'" 1 
HETATM 15992 C  "C3'" . ATP K 3 .   ? 154.325 137.884 175.701 1.00 58.64 ?  803 ATP B "C3'" 1 
HETATM 15993 O  "O3'" . ATP K 3 .   ? 154.980 138.967 176.352 1.00 58.59 ?  803 ATP B "O3'" 1 
HETATM 15994 C  "C2'" . ATP K 3 .   ? 153.469 138.365 174.529 1.00 58.56 ?  803 ATP B "C2'" 1 
HETATM 15995 O  "O2'" . ATP K 3 .   ? 154.080 139.447 173.835 1.00 59.99 ?  803 ATP B "O2'" 1 
HETATM 15996 C  "C1'" . ATP K 3 .   ? 153.432 137.114 173.649 1.00 57.94 ?  803 ATP B "C1'" 1 
HETATM 15997 N  N9    . ATP K 3 .   ? 152.333 136.204 173.954 1.00 59.22 ?  803 ATP B N9    1 
HETATM 15998 C  C8    . ATP K 3 .   ? 152.407 134.998 174.601 1.00 57.41 ?  803 ATP B C8    1 
HETATM 15999 N  N7    . ATP K 3 .   ? 151.254 134.391 174.737 1.00 58.19 ?  803 ATP B N7    1 
HETATM 16000 C  C5    . ATP K 3 .   ? 150.355 135.258 174.138 1.00 58.18 ?  803 ATP B C5    1 
HETATM 16001 C  C6    . ATP K 3 .   ? 148.961 135.200 173.945 1.00 55.35 ?  803 ATP B C6    1 
HETATM 16002 N  N6    . ATP K 3 .   ? 148.194 134.186 174.357 1.00 55.86 ?  803 ATP B N6    1 
HETATM 16003 N  N1    . ATP K 3 .   ? 148.371 136.233 173.306 1.00 57.37 ?  803 ATP B N1    1 
HETATM 16004 C  C2    . ATP K 3 .   ? 149.129 137.252 172.893 1.00 55.85 ?  803 ATP B C2    1 
HETATM 16005 N  N3    . ATP K 3 .   ? 150.447 137.416 173.016 1.00 57.67 ?  803 ATP B N3    1 
HETATM 16006 C  C4    . ATP K 3 .   ? 151.005 136.380 173.650 1.00 59.74 ?  803 ATP B C4    1 
HETATM 16007 P  PB    . GDP L 4 .   ? 160.242 153.721 174.470 1.00 69.13 ?  804 GDP B PB    1 
HETATM 16008 O  O1B   . GDP L 4 .   ? 161.053 152.449 174.458 1.00 61.24 ?  804 GDP B O1B   1 
HETATM 16009 O  O2B   . GDP L 4 .   ? 160.281 154.328 175.852 1.00 59.98 -1 804 GDP B O2B   1 
HETATM 16010 O  O3B   . GDP L 4 .   ? 160.816 154.696 173.469 1.00 59.87 ?  804 GDP B O3B   1 
HETATM 16011 O  O3A   . GDP L 4 .   ? 158.715 153.389 174.092 1.00 58.19 ?  804 GDP B O3A   1 
HETATM 16012 P  PA    . GDP L 4 .   ? 158.285 152.903 172.619 1.00 64.69 ?  804 GDP B PA    1 
HETATM 16013 O  O1A   . GDP L 4 .   ? 158.386 154.021 171.610 1.00 59.39 -1 804 GDP B O1A   1 
HETATM 16014 O  O2A   . GDP L 4 .   ? 159.116 151.721 172.180 1.00 58.30 ?  804 GDP B O2A   1 
HETATM 16015 O  "O5'" . GDP L 4 .   ? 156.753 152.476 172.854 1.00 61.40 ?  804 GDP B "O5'" 1 
HETATM 16016 C  "C5'" . GDP L 4 .   ? 155.746 152.759 171.887 1.00 57.46 ?  804 GDP B "C5'" 1 
HETATM 16017 C  "C4'" . GDP L 4 .   ? 154.600 151.779 172.084 1.00 55.92 ?  804 GDP B "C4'" 1 
HETATM 16018 O  "O4'" . GDP L 4 .   ? 154.336 151.156 170.828 1.00 58.58 ?  804 GDP B "O4'" 1 
HETATM 16019 C  "C3'" . GDP L 4 .   ? 154.990 150.695 173.075 1.00 59.02 ?  804 GDP B "C3'" 1 
HETATM 16020 O  "O3'" . GDP L 4 .   ? 153.977 150.547 174.075 1.00 58.82 ?  804 GDP B "O3'" 1 
HETATM 16021 C  "C2'" . GDP L 4 .   ? 155.110 149.420 172.271 1.00 56.94 ?  804 GDP B "C2'" 1 
HETATM 16022 O  "O2'" . GDP L 4 .   ? 154.433 148.348 172.932 1.00 59.26 ?  804 GDP B "O2'" 1 
HETATM 16023 C  "C1'" . GDP L 4 .   ? 154.447 149.735 170.940 1.00 55.87 ?  804 GDP B "C1'" 1 
HETATM 16024 N  N9    . GDP L 4 .   ? 155.187 149.184 169.775 1.00 56.16 ?  804 GDP B N9    1 
HETATM 16025 C  C8    . GDP L 4 .   ? 154.599 148.685 168.673 1.00 57.86 ?  804 GDP B C8    1 
HETATM 16026 N  N7    . GDP L 4 .   ? 155.516 148.262 167.772 1.00 59.36 ?  804 GDP B N7    1 
HETATM 16027 C  C5    . GDP L 4 .   ? 156.731 148.505 168.290 1.00 59.05 ?  804 GDP B C5    1 
HETATM 16028 C  C6    . GDP L 4 .   ? 158.133 148.303 167.854 1.00 58.07 ?  804 GDP B C6    1 
HETATM 16029 O  O6    . GDP L 4 .   ? 158.390 147.788 166.744 1.00 59.08 ?  804 GDP B O6    1 
HETATM 16030 N  N1    . GDP L 4 .   ? 159.111 148.687 168.681 1.00 57.10 ?  804 GDP B N1    1 
HETATM 16031 C  C2    . GDP L 4 .   ? 158.859 149.243 169.879 1.00 57.92 ?  804 GDP B C2    1 
HETATM 16032 N  N2    . GDP L 4 .   ? 159.904 149.605 170.662 1.00 58.60 ?  804 GDP B N2    1 
HETATM 16033 N  N3    . GDP L 4 .   ? 157.603 149.457 170.341 1.00 60.62 ?  804 GDP B N3    1 
HETATM 16034 C  C4    . GDP L 4 .   ? 156.515 149.117 169.610 1.00 59.26 ?  804 GDP B C4    1 
HETATM 16035 MN MN    . MN  M 7 .   ? 126.098 84.823  120.649 0.85 25.05 ?  401 MN  C MN    1 
HETATM 16036 MN MN    . MN  N 7 .   ? 123.427 87.052  122.011 0.85 26.37 ?  402 MN  C MN    1 
HETATM 16037 MN MN    . MN  O 7 .   ? 141.565 100.015 131.210 1.00 22.51 ?  401 MN  D MN    1 
HETATM 16038 MN MN    . MN  P 7 .   ? 143.555 99.832  127.848 1.00 24.72 ?  402 MN  D MN    1 
# 
