data_9BY8
# 
_entry.id   9BY8 
# 
_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   9BY8         pdb_00009by8 10.2210/pdb9by8/pdb 
WWPDB D_1000284367 ?            ?                   
EMDB  EMD-45021    ?            ?                   
# 
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                        9BY8 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB .                                                                                           EMD-45018 'consensus EM volume'  
EMDB 'Class 9 model for product condition of Bacillus subtilis ribonucleotide reductase complex' EMD-45021 'associated EM volume' 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              nozomi.ando@cornell.edu 
_pdbx_contact_author.name_first         Nozomi 
_pdbx_contact_author.name_last          Ando 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7062-1644 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, D.'       1 0000-0002-3879-039X 
'Thomas, W.C.' 2 0000-0001-5490-4900 
'Burnim, A.A.' 3 0000-0002-9962-1397 
'Ando, N.'     4 0000-0001-7062-1644 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                2458 
_citation.page_last                 2458 
_citation.title                     
'Conformational landscapes of a class I ribonucleotide reductase complex during turnover reveal intrinsic dynamics and asymmetry.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57735-4 
_citation.pdbx_database_id_PubMed   40075098 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xu, D.'       1 ? 
primary 'Thomas, W.C.' 2 ? 
primary 'Burnim, A.A.' 3 ? 
primary 'Ando, N.'     4 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Ribonucleoside-diphosphate reductase subunit alpha' 80791.469 2 1.17.4.1 ? ? ? 
2 polymer     man 'Ribonucleoside-diphosphate reductase subunit beta'  40720.992 2 1.17.4.1 ? ? ? 
3 non-polymer syn "THYMIDINE-5'-TRIPHOSPHATE"                          482.168   2 ?        ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                      24.305    2 ?        ? ? ? 
5 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"                          507.181   2 ?        ? ? ? 
6 non-polymer syn "2'-DEOXYGUANOSINE-5'-DIPHOSPHATE"                   427.201   2 ?        ? ? ? 
7 non-polymer syn 'MANGANESE (II) ION'                                 54.938    4 ?        ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Ribonucleotide reductase large subunit' 
2 'Ribonucleotide reductase small subunit' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MSQNQVPKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVFFHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEV
FKTAYAKKFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVALFFANGDTEKAKEYVNLMINQEYQPSTPTFLNAG
RKRRGELVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKLRAKGEAIKDVENATKGVVGVMKLLDNAFRYADQM
GQRQGSGAAYLNIFHRDINDFLDTKKISADEDVRVKTLSIGVVIPDKFVELAREDKAAYVFYPHTIYKEYGQHMDEMDMN
EMYDKFVDNPRVKKEKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNHISKVKFSNLCSEVLQASQVSSYTDYDEE
DEIGLDISCNLGSLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRANKAMKSIGLGAMNLHGYLAQNGIAYE
SPEARDFANTFFMMVNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYVSTDFSPKYEKIANLFEGMHIPTTEDWKK
LKAFVAEHGMYHSYRLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYPMPGLASNNWFFYKEAYDMDMFKVVDM
IATIQQHIDQGISFTLFLKDTMTTRDLNRIDLYAHHRGIKTIYYARTKDTGQDSCLSCVV
;
;MSQNQVPKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVFFHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEV
FKTAYAKKFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVALFFANGDTEKAKEYVNLMINQEYQPSTPTFLNAG
RKRRGELVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKLRAKGEAIKDVENATKGVVGVMKLLDNAFRYADQM
GQRQGSGAAYLNIFHRDINDFLDTKKISADEDVRVKTLSIGVVIPDKFVELAREDKAAYVFYPHTIYKEYGQHMDEMDMN
EMYDKFVDNPRVKKEKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNHISKVKFSNLCSEVLQASQVSSYTDYDEE
DEIGLDISCNLGSLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRANKAMKSIGLGAMNLHGYLAQNGIAYE
SPEARDFANTFFMMVNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYVSTDFSPKYEKIANLFEGMHIPTTEDWKK
LKAFVAEHGMYHSYRLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYPMPGLASNNWFFYKEAYDMDMFKVVDM
IATIQQHIDQGISFTLFLKDTMTTRDLNRIDLYAHHRGIKTIYYARTKDTGQDSCLSCVV
;
A,B ? 
2 'polypeptide(L)' no no 
;MGSSHHHHHHSSGLVPRGSHMMTKIYDAANWSKHEDDFTQMFYNQNVKQFWLPEEIALNGDLLTWKYLGKNEQDTYMKVL
AGLTLLDTEQGNTGMPIVAEHVDGHQRKAVLNFMAMMENAVHAKSYSNIFMTLAPTETINEVFEWVKQNKYLQKKAQMIV
GLYKAIQKDDEISLFKAMVASVYLESFLFYSGFYYPLYFYGQGKLMQSGEIINLILRDEAIHGVYVGLLAQEIYNKQTEE
KKAELREFAIDLLNQLYENELEYTEDLYDQVGLSHDVKKFIRYNANKALMNLGFDPYFEEEDINPIVLNGLNTKTKSHDF
FSMKGNGYKKATVEPLKDDDFYFEDEKEQI
;
;MGSSHHHHHHSSGLVPRGSHMMTKIYDAANWSKHEDDFTQMFYNQNVKQFWLPEEIALNGDLLTWKYLGKNEQDTYMKVL
AGLTLLDTEQGNTGMPIVAEHVDGHQRKAVLNFMAMMENAVHAKSYSNIFMTLAPTETINEVFEWVKQNKYLQKKAQMIV
GLYKAIQKDDEISLFKAMVASVYLESFLFYSGFYYPLYFYGQGKLMQSGEIINLILRDEAIHGVYVGLLAQEIYNKQTEE
KKAELREFAIDLLNQLYENELEYTEDLYDQVGLSHDVKKFIRYNANKALMNLGFDPYFEEEDINPIVLNGLNTKTKSHDF
FSMKGNGYKKATVEPLKDDDFYFEDEKEQI
;
C,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 "THYMIDINE-5'-TRIPHOSPHATE"        TTP 
4 'MAGNESIUM ION'                    MG  
5 "ADENOSINE-5'-TRIPHOSPHATE"        ATP 
6 "2'-DEOXYGUANOSINE-5'-DIPHOSPHATE" DGI 
7 'MANGANESE (II) ION'               MN  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   GLN n 
1 4   ASN n 
1 5   GLN n 
1 6   VAL n 
1 7   PRO n 
1 8   LYS n 
1 9   TRP n 
1 10  ILE n 
1 11  GLN n 
1 12  LEU n 
1 13  ASN n 
1 14  ASN n 
1 15  GLU n 
1 16  ILE n 
1 17  MET n 
1 18  ILE n 
1 19  GLN n 
1 20  LYS n 
1 21  ASP n 
1 22  GLY n 
1 23  LYS n 
1 24  PHE n 
1 25  GLN n 
1 26  PHE n 
1 27  ASP n 
1 28  LYS n 
1 29  ASP n 
1 30  LYS n 
1 31  GLU n 
1 32  ALA n 
1 33  VAL n 
1 34  HIS n 
1 35  SER n 
1 36  TYR n 
1 37  PHE n 
1 38  VAL n 
1 39  ASP n 
1 40  TYR n 
1 41  ILE n 
1 42  ASN n 
1 43  GLN n 
1 44  ASN n 
1 45  THR n 
1 46  VAL n 
1 47  PHE n 
1 48  PHE n 
1 49  HIS n 
1 50  ASN n 
1 51  LEU n 
1 52  LYS n 
1 53  GLU n 
1 54  LYS n 
1 55  LEU n 
1 56  ASP n 
1 57  TYR n 
1 58  LEU n 
1 59  VAL n 
1 60  GLU n 
1 61  ASN n 
1 62  GLN n 
1 63  TYR n 
1 64  TYR n 
1 65  GLU n 
1 66  GLU n 
1 67  GLU n 
1 68  PHE n 
1 69  LEU n 
1 70  SER n 
1 71  LEU n 
1 72  TYR n 
1 73  SER n 
1 74  PHE n 
1 75  GLU n 
1 76  ASP n 
1 77  ILE n 
1 78  LYS n 
1 79  GLU n 
1 80  VAL n 
1 81  PHE n 
1 82  LYS n 
1 83  THR n 
1 84  ALA n 
1 85  TYR n 
1 86  ALA n 
1 87  LYS n 
1 88  LYS n 
1 89  PHE n 
1 90  ARG n 
1 91  PHE n 
1 92  PRO n 
1 93  SER n 
1 94  PHE n 
1 95  MET n 
1 96  SER n 
1 97  ALA n 
1 98  PHE n 
1 99  LYS n 
1 100 PHE n 
1 101 TYR n 
1 102 ASN n 
1 103 ASP n 
1 104 TYR n 
1 105 ALA n 
1 106 LEU n 
1 107 LYS n 
1 108 THR n 
1 109 ASN n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 ILE n 
1 115 LEU n 
1 116 GLU n 
1 117 ARG n 
1 118 TYR n 
1 119 GLU n 
1 120 ASP n 
1 121 ARG n 
1 122 ILE n 
1 123 SER n 
1 124 ILE n 
1 125 VAL n 
1 126 ALA n 
1 127 LEU n 
1 128 PHE n 
1 129 PHE n 
1 130 ALA n 
1 131 ASN n 
1 132 GLY n 
1 133 ASP n 
1 134 THR n 
1 135 GLU n 
1 136 LYS n 
1 137 ALA n 
1 138 LYS n 
1 139 GLU n 
1 140 TYR n 
1 141 VAL n 
1 142 ASN n 
1 143 LEU n 
1 144 MET n 
1 145 ILE n 
1 146 ASN n 
1 147 GLN n 
1 148 GLU n 
1 149 TYR n 
1 150 GLN n 
1 151 PRO n 
1 152 SER n 
1 153 THR n 
1 154 PRO n 
1 155 THR n 
1 156 PHE n 
1 157 LEU n 
1 158 ASN n 
1 159 ALA n 
1 160 GLY n 
1 161 ARG n 
1 162 LYS n 
1 163 ARG n 
1 164 ARG n 
1 165 GLY n 
1 166 GLU n 
1 167 LEU n 
1 168 VAL n 
1 169 SER n 
1 170 CYS n 
1 171 PHE n 
1 172 LEU n 
1 173 LEU n 
1 174 GLU n 
1 175 VAL n 
1 176 ASN n 
1 177 ASP n 
1 178 SER n 
1 179 LEU n 
1 180 ASN n 
1 181 ASP n 
1 182 ILE n 
1 183 SER n 
1 184 ARG n 
1 185 ALA n 
1 186 ILE n 
1 187 ASP n 
1 188 ILE n 
1 189 SER n 
1 190 MET n 
1 191 GLN n 
1 192 LEU n 
1 193 SER n 
1 194 LYS n 
1 195 LEU n 
1 196 GLY n 
1 197 GLY n 
1 198 GLY n 
1 199 VAL n 
1 200 SER n 
1 201 LEU n 
1 202 ASN n 
1 203 LEU n 
1 204 SER n 
1 205 LYS n 
1 206 LEU n 
1 207 ARG n 
1 208 ALA n 
1 209 LYS n 
1 210 GLY n 
1 211 GLU n 
1 212 ALA n 
1 213 ILE n 
1 214 LYS n 
1 215 ASP n 
1 216 VAL n 
1 217 GLU n 
1 218 ASN n 
1 219 ALA n 
1 220 THR n 
1 221 LYS n 
1 222 GLY n 
1 223 VAL n 
1 224 VAL n 
1 225 GLY n 
1 226 VAL n 
1 227 MET n 
1 228 LYS n 
1 229 LEU n 
1 230 LEU n 
1 231 ASP n 
1 232 ASN n 
1 233 ALA n 
1 234 PHE n 
1 235 ARG n 
1 236 TYR n 
1 237 ALA n 
1 238 ASP n 
1 239 GLN n 
1 240 MET n 
1 241 GLY n 
1 242 GLN n 
1 243 ARG n 
1 244 GLN n 
1 245 GLY n 
1 246 SER n 
1 247 GLY n 
1 248 ALA n 
1 249 ALA n 
1 250 TYR n 
1 251 LEU n 
1 252 ASN n 
1 253 ILE n 
1 254 PHE n 
1 255 HIS n 
1 256 ARG n 
1 257 ASP n 
1 258 ILE n 
1 259 ASN n 
1 260 ASP n 
1 261 PHE n 
1 262 LEU n 
1 263 ASP n 
1 264 THR n 
1 265 LYS n 
1 266 LYS n 
1 267 ILE n 
1 268 SER n 
1 269 ALA n 
1 270 ASP n 
1 271 GLU n 
1 272 ASP n 
1 273 VAL n 
1 274 ARG n 
1 275 VAL n 
1 276 LYS n 
1 277 THR n 
1 278 LEU n 
1 279 SER n 
1 280 ILE n 
1 281 GLY n 
1 282 VAL n 
1 283 VAL n 
1 284 ILE n 
1 285 PRO n 
1 286 ASP n 
1 287 LYS n 
1 288 PHE n 
1 289 VAL n 
1 290 GLU n 
1 291 LEU n 
1 292 ALA n 
1 293 ARG n 
1 294 GLU n 
1 295 ASP n 
1 296 LYS n 
1 297 ALA n 
1 298 ALA n 
1 299 TYR n 
1 300 VAL n 
1 301 PHE n 
1 302 TYR n 
1 303 PRO n 
1 304 HIS n 
1 305 THR n 
1 306 ILE n 
1 307 TYR n 
1 308 LYS n 
1 309 GLU n 
1 310 TYR n 
1 311 GLY n 
1 312 GLN n 
1 313 HIS n 
1 314 MET n 
1 315 ASP n 
1 316 GLU n 
1 317 MET n 
1 318 ASP n 
1 319 MET n 
1 320 ASN n 
1 321 GLU n 
1 322 MET n 
1 323 TYR n 
1 324 ASP n 
1 325 LYS n 
1 326 PHE n 
1 327 VAL n 
1 328 ASP n 
1 329 ASN n 
1 330 PRO n 
1 331 ARG n 
1 332 VAL n 
1 333 LYS n 
1 334 LYS n 
1 335 GLU n 
1 336 LYS n 
1 337 ILE n 
1 338 ASN n 
1 339 PRO n 
1 340 ARG n 
1 341 LYS n 
1 342 LEU n 
1 343 LEU n 
1 344 GLU n 
1 345 LYS n 
1 346 LEU n 
1 347 ALA n 
1 348 MET n 
1 349 LEU n 
1 350 ARG n 
1 351 SER n 
1 352 GLU n 
1 353 SER n 
1 354 GLY n 
1 355 TYR n 
1 356 PRO n 
1 357 TYR n 
1 358 ILE n 
1 359 MET n 
1 360 PHE n 
1 361 GLN n 
1 362 ASP n 
1 363 ASN n 
1 364 VAL n 
1 365 ASN n 
1 366 LYS n 
1 367 VAL n 
1 368 HIS n 
1 369 ALA n 
1 370 ASN n 
1 371 ASN n 
1 372 HIS n 
1 373 ILE n 
1 374 SER n 
1 375 LYS n 
1 376 VAL n 
1 377 LYS n 
1 378 PHE n 
1 379 SER n 
1 380 ASN n 
1 381 LEU n 
1 382 CYS n 
1 383 SER n 
1 384 GLU n 
1 385 VAL n 
1 386 LEU n 
1 387 GLN n 
1 388 ALA n 
1 389 SER n 
1 390 GLN n 
1 391 VAL n 
1 392 SER n 
1 393 SER n 
1 394 TYR n 
1 395 THR n 
1 396 ASP n 
1 397 TYR n 
1 398 ASP n 
1 399 GLU n 
1 400 GLU n 
1 401 ASP n 
1 402 GLU n 
1 403 ILE n 
1 404 GLY n 
1 405 LEU n 
1 406 ASP n 
1 407 ILE n 
1 408 SER n 
1 409 CYS n 
1 410 ASN n 
1 411 LEU n 
1 412 GLY n 
1 413 SER n 
1 414 LEU n 
1 415 ASN n 
1 416 ILE n 
1 417 LEU n 
1 418 ASN n 
1 419 VAL n 
1 420 MET n 
1 421 GLU n 
1 422 HIS n 
1 423 LYS n 
1 424 SER n 
1 425 ILE n 
1 426 GLU n 
1 427 LYS n 
1 428 THR n 
1 429 VAL n 
1 430 LYS n 
1 431 LEU n 
1 432 ALA n 
1 433 THR n 
1 434 ASP n 
1 435 SER n 
1 436 LEU n 
1 437 THR n 
1 438 HIS n 
1 439 VAL n 
1 440 SER n 
1 441 GLU n 
1 442 THR n 
1 443 THR n 
1 444 ASP n 
1 445 ILE n 
1 446 ARG n 
1 447 ASN n 
1 448 ALA n 
1 449 PRO n 
1 450 ALA n 
1 451 VAL n 
1 452 ARG n 
1 453 ARG n 
1 454 ALA n 
1 455 ASN n 
1 456 LYS n 
1 457 ALA n 
1 458 MET n 
1 459 LYS n 
1 460 SER n 
1 461 ILE n 
1 462 GLY n 
1 463 LEU n 
1 464 GLY n 
1 465 ALA n 
1 466 MET n 
1 467 ASN n 
1 468 LEU n 
1 469 HIS n 
1 470 GLY n 
1 471 TYR n 
1 472 LEU n 
1 473 ALA n 
1 474 GLN n 
1 475 ASN n 
1 476 GLY n 
1 477 ILE n 
1 478 ALA n 
1 479 TYR n 
1 480 GLU n 
1 481 SER n 
1 482 PRO n 
1 483 GLU n 
1 484 ALA n 
1 485 ARG n 
1 486 ASP n 
1 487 PHE n 
1 488 ALA n 
1 489 ASN n 
1 490 THR n 
1 491 PHE n 
1 492 PHE n 
1 493 MET n 
1 494 MET n 
1 495 VAL n 
1 496 ASN n 
1 497 PHE n 
1 498 TYR n 
1 499 SER n 
1 500 ILE n 
1 501 GLN n 
1 502 ARG n 
1 503 SER n 
1 504 ALA n 
1 505 GLU n 
1 506 ILE n 
1 507 ALA n 
1 508 LYS n 
1 509 GLU n 
1 510 LYS n 
1 511 GLY n 
1 512 GLU n 
1 513 THR n 
1 514 PHE n 
1 515 ASP n 
1 516 GLN n 
1 517 TYR n 
1 518 GLU n 
1 519 GLY n 
1 520 SER n 
1 521 THR n 
1 522 TYR n 
1 523 ALA n 
1 524 THR n 
1 525 GLY n 
1 526 GLU n 
1 527 TYR n 
1 528 PHE n 
1 529 ASP n 
1 530 LYS n 
1 531 TYR n 
1 532 VAL n 
1 533 SER n 
1 534 THR n 
1 535 ASP n 
1 536 PHE n 
1 537 SER n 
1 538 PRO n 
1 539 LYS n 
1 540 TYR n 
1 541 GLU n 
1 542 LYS n 
1 543 ILE n 
1 544 ALA n 
1 545 ASN n 
1 546 LEU n 
1 547 PHE n 
1 548 GLU n 
1 549 GLY n 
1 550 MET n 
1 551 HIS n 
1 552 ILE n 
1 553 PRO n 
1 554 THR n 
1 555 THR n 
1 556 GLU n 
1 557 ASP n 
1 558 TRP n 
1 559 LYS n 
1 560 LYS n 
1 561 LEU n 
1 562 LYS n 
1 563 ALA n 
1 564 PHE n 
1 565 VAL n 
1 566 ALA n 
1 567 GLU n 
1 568 HIS n 
1 569 GLY n 
1 570 MET n 
1 571 TYR n 
1 572 HIS n 
1 573 SER n 
1 574 TYR n 
1 575 ARG n 
1 576 LEU n 
1 577 CYS n 
1 578 ILE n 
1 579 ALA n 
1 580 PRO n 
1 581 THR n 
1 582 GLY n 
1 583 SER n 
1 584 ILE n 
1 585 SER n 
1 586 TYR n 
1 587 VAL n 
1 588 GLN n 
1 589 SER n 
1 590 SER n 
1 591 THR n 
1 592 ALA n 
1 593 SER n 
1 594 VAL n 
1 595 MET n 
1 596 PRO n 
1 597 ILE n 
1 598 MET n 
1 599 GLU n 
1 600 ARG n 
1 601 ILE n 
1 602 GLU n 
1 603 GLU n 
1 604 ARG n 
1 605 THR n 
1 606 TYR n 
1 607 GLY n 
1 608 ASN n 
1 609 SER n 
1 610 LYS n 
1 611 THR n 
1 612 TYR n 
1 613 TYR n 
1 614 PRO n 
1 615 MET n 
1 616 PRO n 
1 617 GLY n 
1 618 LEU n 
1 619 ALA n 
1 620 SER n 
1 621 ASN n 
1 622 ASN n 
1 623 TRP n 
1 624 PHE n 
1 625 PHE n 
1 626 TYR n 
1 627 LYS n 
1 628 GLU n 
1 629 ALA n 
1 630 TYR n 
1 631 ASP n 
1 632 MET n 
1 633 ASP n 
1 634 MET n 
1 635 PHE n 
1 636 LYS n 
1 637 VAL n 
1 638 VAL n 
1 639 ASP n 
1 640 MET n 
1 641 ILE n 
1 642 ALA n 
1 643 THR n 
1 644 ILE n 
1 645 GLN n 
1 646 GLN n 
1 647 HIS n 
1 648 ILE n 
1 649 ASP n 
1 650 GLN n 
1 651 GLY n 
1 652 ILE n 
1 653 SER n 
1 654 PHE n 
1 655 THR n 
1 656 LEU n 
1 657 PHE n 
1 658 LEU n 
1 659 LYS n 
1 660 ASP n 
1 661 THR n 
1 662 MET n 
1 663 THR n 
1 664 THR n 
1 665 ARG n 
1 666 ASP n 
1 667 LEU n 
1 668 ASN n 
1 669 ARG n 
1 670 ILE n 
1 671 ASP n 
1 672 LEU n 
1 673 TYR n 
1 674 ALA n 
1 675 HIS n 
1 676 HIS n 
1 677 ARG n 
1 678 GLY n 
1 679 ILE n 
1 680 LYS n 
1 681 THR n 
1 682 ILE n 
1 683 TYR n 
1 684 TYR n 
1 685 ALA n 
1 686 ARG n 
1 687 THR n 
1 688 LYS n 
1 689 ASP n 
1 690 THR n 
1 691 GLY n 
1 692 GLN n 
1 693 ASP n 
1 694 SER n 
1 695 CYS n 
1 696 LEU n 
1 697 SER n 
1 698 CYS n 
1 699 VAL n 
1 700 VAL n 
2 1   MET n 
2 2   GLY n 
2 3   SER n 
2 4   SER n 
2 5   HIS n 
2 6   HIS n 
2 7   HIS n 
2 8   HIS n 
2 9   HIS n 
2 10  HIS n 
2 11  SER n 
2 12  SER n 
2 13  GLY n 
2 14  LEU n 
2 15  VAL n 
2 16  PRO n 
2 17  ARG n 
2 18  GLY n 
2 19  SER n 
2 20  HIS n 
2 21  MET n 
2 22  MET n 
2 23  THR n 
2 24  LYS n 
2 25  ILE n 
2 26  TYR n 
2 27  ASP n 
2 28  ALA n 
2 29  ALA n 
2 30  ASN n 
2 31  TRP n 
2 32  SER n 
2 33  LYS n 
2 34  HIS n 
2 35  GLU n 
2 36  ASP n 
2 37  ASP n 
2 38  PHE n 
2 39  THR n 
2 40  GLN n 
2 41  MET n 
2 42  PHE n 
2 43  TYR n 
2 44  ASN n 
2 45  GLN n 
2 46  ASN n 
2 47  VAL n 
2 48  LYS n 
2 49  GLN n 
2 50  PHE n 
2 51  TRP n 
2 52  LEU n 
2 53  PRO n 
2 54  GLU n 
2 55  GLU n 
2 56  ILE n 
2 57  ALA n 
2 58  LEU n 
2 59  ASN n 
2 60  GLY n 
2 61  ASP n 
2 62  LEU n 
2 63  LEU n 
2 64  THR n 
2 65  TRP n 
2 66  LYS n 
2 67  TYR n 
2 68  LEU n 
2 69  GLY n 
2 70  LYS n 
2 71  ASN n 
2 72  GLU n 
2 73  GLN n 
2 74  ASP n 
2 75  THR n 
2 76  TYR n 
2 77  MET n 
2 78  LYS n 
2 79  VAL n 
2 80  LEU n 
2 81  ALA n 
2 82  GLY n 
2 83  LEU n 
2 84  THR n 
2 85  LEU n 
2 86  LEU n 
2 87  ASP n 
2 88  THR n 
2 89  GLU n 
2 90  GLN n 
2 91  GLY n 
2 92  ASN n 
2 93  THR n 
2 94  GLY n 
2 95  MET n 
2 96  PRO n 
2 97  ILE n 
2 98  VAL n 
2 99  ALA n 
2 100 GLU n 
2 101 HIS n 
2 102 VAL n 
2 103 ASP n 
2 104 GLY n 
2 105 HIS n 
2 106 GLN n 
2 107 ARG n 
2 108 LYS n 
2 109 ALA n 
2 110 VAL n 
2 111 LEU n 
2 112 ASN n 
2 113 PHE n 
2 114 MET n 
2 115 ALA n 
2 116 MET n 
2 117 MET n 
2 118 GLU n 
2 119 ASN n 
2 120 ALA n 
2 121 VAL n 
2 122 HIS n 
2 123 ALA n 
2 124 LYS n 
2 125 SER n 
2 126 TYR n 
2 127 SER n 
2 128 ASN n 
2 129 ILE n 
2 130 PHE n 
2 131 MET n 
2 132 THR n 
2 133 LEU n 
2 134 ALA n 
2 135 PRO n 
2 136 THR n 
2 137 GLU n 
2 138 THR n 
2 139 ILE n 
2 140 ASN n 
2 141 GLU n 
2 142 VAL n 
2 143 PHE n 
2 144 GLU n 
2 145 TRP n 
2 146 VAL n 
2 147 LYS n 
2 148 GLN n 
2 149 ASN n 
2 150 LYS n 
2 151 TYR n 
2 152 LEU n 
2 153 GLN n 
2 154 LYS n 
2 155 LYS n 
2 156 ALA n 
2 157 GLN n 
2 158 MET n 
2 159 ILE n 
2 160 VAL n 
2 161 GLY n 
2 162 LEU n 
2 163 TYR n 
2 164 LYS n 
2 165 ALA n 
2 166 ILE n 
2 167 GLN n 
2 168 LYS n 
2 169 ASP n 
2 170 ASP n 
2 171 GLU n 
2 172 ILE n 
2 173 SER n 
2 174 LEU n 
2 175 PHE n 
2 176 LYS n 
2 177 ALA n 
2 178 MET n 
2 179 VAL n 
2 180 ALA n 
2 181 SER n 
2 182 VAL n 
2 183 TYR n 
2 184 LEU n 
2 185 GLU n 
2 186 SER n 
2 187 PHE n 
2 188 LEU n 
2 189 PHE n 
2 190 TYR n 
2 191 SER n 
2 192 GLY n 
2 193 PHE n 
2 194 TYR n 
2 195 TYR n 
2 196 PRO n 
2 197 LEU n 
2 198 TYR n 
2 199 PHE n 
2 200 TYR n 
2 201 GLY n 
2 202 GLN n 
2 203 GLY n 
2 204 LYS n 
2 205 LEU n 
2 206 MET n 
2 207 GLN n 
2 208 SER n 
2 209 GLY n 
2 210 GLU n 
2 211 ILE n 
2 212 ILE n 
2 213 ASN n 
2 214 LEU n 
2 215 ILE n 
2 216 LEU n 
2 217 ARG n 
2 218 ASP n 
2 219 GLU n 
2 220 ALA n 
2 221 ILE n 
2 222 HIS n 
2 223 GLY n 
2 224 VAL n 
2 225 TYR n 
2 226 VAL n 
2 227 GLY n 
2 228 LEU n 
2 229 LEU n 
2 230 ALA n 
2 231 GLN n 
2 232 GLU n 
2 233 ILE n 
2 234 TYR n 
2 235 ASN n 
2 236 LYS n 
2 237 GLN n 
2 238 THR n 
2 239 GLU n 
2 240 GLU n 
2 241 LYS n 
2 242 LYS n 
2 243 ALA n 
2 244 GLU n 
2 245 LEU n 
2 246 ARG n 
2 247 GLU n 
2 248 PHE n 
2 249 ALA n 
2 250 ILE n 
2 251 ASP n 
2 252 LEU n 
2 253 LEU n 
2 254 ASN n 
2 255 GLN n 
2 256 LEU n 
2 257 TYR n 
2 258 GLU n 
2 259 ASN n 
2 260 GLU n 
2 261 LEU n 
2 262 GLU n 
2 263 TYR n 
2 264 THR n 
2 265 GLU n 
2 266 ASP n 
2 267 LEU n 
2 268 TYR n 
2 269 ASP n 
2 270 GLN n 
2 271 VAL n 
2 272 GLY n 
2 273 LEU n 
2 274 SER n 
2 275 HIS n 
2 276 ASP n 
2 277 VAL n 
2 278 LYS n 
2 279 LYS n 
2 280 PHE n 
2 281 ILE n 
2 282 ARG n 
2 283 TYR n 
2 284 ASN n 
2 285 ALA n 
2 286 ASN n 
2 287 LYS n 
2 288 ALA n 
2 289 LEU n 
2 290 MET n 
2 291 ASN n 
2 292 LEU n 
2 293 GLY n 
2 294 PHE n 
2 295 ASP n 
2 296 PRO n 
2 297 TYR n 
2 298 PHE n 
2 299 GLU n 
2 300 GLU n 
2 301 GLU n 
2 302 ASP n 
2 303 ILE n 
2 304 ASN n 
2 305 PRO n 
2 306 ILE n 
2 307 VAL n 
2 308 LEU n 
2 309 ASN n 
2 310 GLY n 
2 311 LEU n 
2 312 ASN n 
2 313 THR n 
2 314 LYS n 
2 315 THR n 
2 316 LYS n 
2 317 SER n 
2 318 HIS n 
2 319 ASP n 
2 320 PHE n 
2 321 PHE n 
2 322 SER n 
2 323 MET n 
2 324 LYS n 
2 325 GLY n 
2 326 ASN n 
2 327 GLY n 
2 328 TYR n 
2 329 LYS n 
2 330 LYS n 
2 331 ALA n 
2 332 THR n 
2 333 VAL n 
2 334 GLU n 
2 335 PRO n 
2 336 LEU n 
2 337 LYS n 
2 338 ASP n 
2 339 ASP n 
2 340 ASP n 
2 341 PHE n 
2 342 TYR n 
2 343 PHE n 
2 344 GLU n 
2 345 ASP n 
2 346 GLU n 
2 347 LYS n 
2 348 GLU n 
2 349 GLN n 
2 350 ILE n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 700 ? ? 'nrdE, nrdA, BSU17380' ? ? ? ? ? ? 'Bacillus subtilis' 1423 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 350 ? ? 'nrdF, BSU17390'       ? ? ? ? ? ? 'Bacillus subtilis' 1423 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                            ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                           ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                         ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                    ? 'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE"        ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                           ? 'C3 H7 N O2 S'      121.158 
DGI 'DNA linking'       n "2'-DEOXYGUANOSINE-5'-DIPHOSPHATE" ? 'C10 H15 N5 O10 P2' 427.201 
GLN 'L-peptide linking' y GLUTAMINE                          ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                    ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                            ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                          ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                         ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                            ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                             ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                         ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'                    ? 'Mg 2'              24.305  
MN  non-polymer         . 'MANGANESE (II) ION'               ? 'Mn 2'              54.938  
PHE 'L-peptide linking' y PHENYLALANINE                      ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                            ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                             ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                          ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                         ? 'C11 H12 N2 O2'     204.225 
TTP non-polymer         . "THYMIDINE-5'-TRIPHOSPHATE"        ? 'C10 H17 N2 O14 P3' 482.168 
TYR 'L-peptide linking' y TYROSINE                           ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                             ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   GLN 3   3   ?   ?   ?   A . n 
A 1 4   ASN 4   4   ?   ?   ?   A . n 
A 1 5   GLN 5   5   ?   ?   ?   A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   PRO 7   7   7   PRO PRO A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   TRP 9   9   9   TRP TRP A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  GLN 11  11  11  GLN GLN A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  HIS 34  34  34  HIS HIS A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  TYR 36  36  36  TYR TYR A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  ASN 42  42  42  ASN ASN A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  PHE 47  47  47  PHE PHE A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  HIS 49  49  49  HIS HIS A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  TYR 57  57  57  TYR TYR A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  TYR 63  63  63  TYR TYR A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  PHE 68  68  68  PHE PHE A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  ILE 77  77  77  ILE ILE A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  PHE 81  81  81  PHE PHE A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  THR 83  83  83  THR THR A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  PHE 91  91  91  PHE PHE A . n 
A 1 92  PRO 92  92  92  PRO PRO A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  MET 95  95  95  MET MET A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 PHE 100 100 100 PHE PHE A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 TYR 104 104 104 TYR TYR A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 ARG 117 117 117 ARG ARG A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 PHE 129 129 129 PHE PHE A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 MET 144 144 144 MET MET A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 ASN 146 146 146 ASN ASN A . n 
A 1 147 GLN 147 147 147 GLN GLN A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 TYR 149 149 149 TYR TYR A . n 
A 1 150 GLN 150 150 150 GLN GLN A . n 
A 1 151 PRO 151 151 151 PRO PRO A . n 
A 1 152 SER 152 152 152 SER SER A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 THR 155 155 155 THR THR A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 ASN 158 158 158 ASN ASN A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 CYS 170 170 170 CYS CYS A . n 
A 1 171 PHE 171 171 171 PHE PHE A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 GLU 174 174 174 GLU GLU A . n 
A 1 175 VAL 175 175 175 VAL VAL A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 ASP 177 177 177 ASP ASP A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 ILE 182 182 182 ILE ILE A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ILE 188 188 188 ILE ILE A . n 
A 1 189 SER 189 189 189 SER SER A . n 
A 1 190 MET 190 190 190 MET MET A . n 
A 1 191 GLN 191 191 191 GLN GLN A . n 
A 1 192 LEU 192 192 192 LEU LEU A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 SER 200 200 200 SER SER A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 ASN 202 202 202 ASN ASN A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 ARG 207 207 207 ARG ARG A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 LYS 209 209 209 LYS LYS A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 GLU 211 211 211 GLU GLU A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 LYS 214 214 214 LYS LYS A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 THR 220 220 220 THR THR A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 GLY 222 222 222 GLY GLY A . n 
A 1 223 VAL 223 223 223 VAL VAL A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 GLY 225 225 225 GLY GLY A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 MET 227 227 227 MET MET A . n 
A 1 228 LYS 228 228 228 LYS LYS A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 ASP 231 231 231 ASP ASP A . n 
A 1 232 ASN 232 232 232 ASN ASN A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 PHE 234 234 234 PHE PHE A . n 
A 1 235 ARG 235 235 235 ARG ARG A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 GLN 239 239 239 GLN GLN A . n 
A 1 240 MET 240 240 240 MET MET A . n 
A 1 241 GLY 241 241 241 GLY GLY A . n 
A 1 242 GLN 242 242 242 GLN GLN A . n 
A 1 243 ARG 243 243 243 ARG ARG A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 TYR 250 250 250 TYR TYR A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 ILE 253 253 253 ILE ILE A . n 
A 1 254 PHE 254 254 254 PHE PHE A . n 
A 1 255 HIS 255 255 255 HIS HIS A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 ASP 257 257 257 ASP ASP A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 ASN 259 259 259 ASN ASN A . n 
A 1 260 ASP 260 260 260 ASP ASP A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 THR 264 264 264 THR THR A . n 
A 1 265 LYS 265 265 265 LYS LYS A . n 
A 1 266 LYS 266 266 266 LYS LYS A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 SER 268 268 268 SER SER A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 ASP 270 270 270 ASP ASP A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 ASP 272 272 272 ASP ASP A . n 
A 1 273 VAL 273 273 273 VAL VAL A . n 
A 1 274 ARG 274 274 274 ARG ARG A . n 
A 1 275 VAL 275 275 275 VAL VAL A . n 
A 1 276 LYS 276 276 276 LYS LYS A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 SER 279 279 279 SER SER A . n 
A 1 280 ILE 280 280 280 ILE ILE A . n 
A 1 281 GLY 281 281 281 GLY GLY A . n 
A 1 282 VAL 282 282 282 VAL VAL A . n 
A 1 283 VAL 283 283 283 VAL VAL A . n 
A 1 284 ILE 284 284 284 ILE ILE A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 ASP 286 286 286 ASP ASP A . n 
A 1 287 LYS 287 287 287 LYS LYS A . n 
A 1 288 PHE 288 288 288 PHE PHE A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 LEU 291 291 291 LEU LEU A . n 
A 1 292 ALA 292 292 292 ALA ALA A . n 
A 1 293 ARG 293 293 293 ARG ARG A . n 
A 1 294 GLU 294 294 294 GLU GLU A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 LYS 296 296 296 LYS LYS A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 ALA 298 298 298 ALA ALA A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 VAL 300 300 300 VAL VAL A . n 
A 1 301 PHE 301 301 301 PHE PHE A . n 
A 1 302 TYR 302 302 302 TYR TYR A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 HIS 304 304 304 HIS HIS A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 ILE 306 306 306 ILE ILE A . n 
A 1 307 TYR 307 307 307 TYR TYR A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 GLU 309 309 309 GLU GLU A . n 
A 1 310 TYR 310 310 310 TYR TYR A . n 
A 1 311 GLY 311 311 311 GLY GLY A . n 
A 1 312 GLN 312 312 312 GLN GLN A . n 
A 1 313 HIS 313 313 313 HIS HIS A . n 
A 1 314 MET 314 314 314 MET MET A . n 
A 1 315 ASP 315 315 315 ASP ASP A . n 
A 1 316 GLU 316 316 316 GLU GLU A . n 
A 1 317 MET 317 317 317 MET MET A . n 
A 1 318 ASP 318 318 318 ASP ASP A . n 
A 1 319 MET 319 319 319 MET MET A . n 
A 1 320 ASN 320 320 320 ASN ASN A . n 
A 1 321 GLU 321 321 321 GLU GLU A . n 
A 1 322 MET 322 322 322 MET MET A . n 
A 1 323 TYR 323 323 323 TYR TYR A . n 
A 1 324 ASP 324 324 324 ASP ASP A . n 
A 1 325 LYS 325 325 325 LYS LYS A . n 
A 1 326 PHE 326 326 326 PHE PHE A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 ASP 328 328 328 ASP ASP A . n 
A 1 329 ASN 329 329 329 ASN ASN A . n 
A 1 330 PRO 330 330 330 PRO PRO A . n 
A 1 331 ARG 331 331 331 ARG ARG A . n 
A 1 332 VAL 332 332 332 VAL VAL A . n 
A 1 333 LYS 333 333 333 LYS LYS A . n 
A 1 334 LYS 334 334 334 LYS LYS A . n 
A 1 335 GLU 335 335 335 GLU GLU A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 ASN 338 338 338 ASN ASN A . n 
A 1 339 PRO 339 339 339 PRO PRO A . n 
A 1 340 ARG 340 340 340 ARG ARG A . n 
A 1 341 LYS 341 341 341 LYS LYS A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 LEU 343 343 343 LEU LEU A . n 
A 1 344 GLU 344 344 344 GLU GLU A . n 
A 1 345 LYS 345 345 345 LYS LYS A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 MET 348 348 348 MET MET A . n 
A 1 349 LEU 349 349 349 LEU LEU A . n 
A 1 350 ARG 350 350 350 ARG ARG A . n 
A 1 351 SER 351 351 351 SER SER A . n 
A 1 352 GLU 352 352 352 GLU GLU A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 TYR 355 355 355 TYR TYR A . n 
A 1 356 PRO 356 356 356 PRO PRO A . n 
A 1 357 TYR 357 357 357 TYR TYR A . n 
A 1 358 ILE 358 358 358 ILE ILE A . n 
A 1 359 MET 359 359 359 MET MET A . n 
A 1 360 PHE 360 360 360 PHE PHE A . n 
A 1 361 GLN 361 361 361 GLN GLN A . n 
A 1 362 ASP 362 362 362 ASP ASP A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 VAL 364 364 364 VAL VAL A . n 
A 1 365 ASN 365 365 365 ASN ASN A . n 
A 1 366 LYS 366 366 366 LYS LYS A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 HIS 368 368 368 HIS HIS A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 ASN 370 370 370 ASN ASN A . n 
A 1 371 ASN 371 371 371 ASN ASN A . n 
A 1 372 HIS 372 372 372 HIS HIS A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 SER 374 374 374 SER SER A . n 
A 1 375 LYS 375 375 375 LYS LYS A . n 
A 1 376 VAL 376 376 376 VAL VAL A . n 
A 1 377 LYS 377 377 377 LYS LYS A . n 
A 1 378 PHE 378 378 378 PHE PHE A . n 
A 1 379 SER 379 379 379 SER SER A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 LEU 381 381 381 LEU LEU A . n 
A 1 382 CYS 382 382 382 CYS CYS A . n 
A 1 383 SER 383 383 383 SER SER A . n 
A 1 384 GLU 384 384 384 GLU GLU A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 GLN 387 387 387 GLN GLN A . n 
A 1 388 ALA 388 388 388 ALA ALA A . n 
A 1 389 SER 389 389 389 SER SER A . n 
A 1 390 GLN 390 390 390 GLN GLN A . n 
A 1 391 VAL 391 391 391 VAL VAL A . n 
A 1 392 SER 392 392 392 SER SER A . n 
A 1 393 SER 393 393 393 SER SER A . n 
A 1 394 TYR 394 394 394 TYR TYR A . n 
A 1 395 THR 395 395 395 THR THR A . n 
A 1 396 ASP 396 396 396 ASP ASP A . n 
A 1 397 TYR 397 397 397 TYR TYR A . n 
A 1 398 ASP 398 398 398 ASP ASP A . n 
A 1 399 GLU 399 399 399 GLU GLU A . n 
A 1 400 GLU 400 400 400 GLU GLU A . n 
A 1 401 ASP 401 401 401 ASP ASP A . n 
A 1 402 GLU 402 402 402 GLU GLU A . n 
A 1 403 ILE 403 403 403 ILE ILE A . n 
A 1 404 GLY 404 404 404 GLY GLY A . n 
A 1 405 LEU 405 405 405 LEU LEU A . n 
A 1 406 ASP 406 406 406 ASP ASP A . n 
A 1 407 ILE 407 407 407 ILE ILE A . n 
A 1 408 SER 408 408 408 SER SER A . n 
A 1 409 CYS 409 409 409 CYS CYS A . n 
A 1 410 ASN 410 410 410 ASN ASN A . n 
A 1 411 LEU 411 411 411 LEU LEU A . n 
A 1 412 GLY 412 412 412 GLY GLY A . n 
A 1 413 SER 413 413 413 SER SER A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 ASN 415 415 415 ASN ASN A . n 
A 1 416 ILE 416 416 416 ILE ILE A . n 
A 1 417 LEU 417 417 417 LEU LEU A . n 
A 1 418 ASN 418 418 418 ASN ASN A . n 
A 1 419 VAL 419 419 419 VAL VAL A . n 
A 1 420 MET 420 420 420 MET MET A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 HIS 422 422 422 HIS HIS A . n 
A 1 423 LYS 423 423 423 LYS LYS A . n 
A 1 424 SER 424 424 424 SER SER A . n 
A 1 425 ILE 425 425 425 ILE ILE A . n 
A 1 426 GLU 426 426 426 GLU GLU A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 THR 428 428 428 THR THR A . n 
A 1 429 VAL 429 429 429 VAL VAL A . n 
A 1 430 LYS 430 430 430 LYS LYS A . n 
A 1 431 LEU 431 431 431 LEU LEU A . n 
A 1 432 ALA 432 432 432 ALA ALA A . n 
A 1 433 THR 433 433 433 THR THR A . n 
A 1 434 ASP 434 434 434 ASP ASP A . n 
A 1 435 SER 435 435 435 SER SER A . n 
A 1 436 LEU 436 436 436 LEU LEU A . n 
A 1 437 THR 437 437 437 THR THR A . n 
A 1 438 HIS 438 438 438 HIS HIS A . n 
A 1 439 VAL 439 439 439 VAL VAL A . n 
A 1 440 SER 440 440 440 SER SER A . n 
A 1 441 GLU 441 441 441 GLU GLU A . n 
A 1 442 THR 442 442 442 THR THR A . n 
A 1 443 THR 443 443 443 THR THR A . n 
A 1 444 ASP 444 444 444 ASP ASP A . n 
A 1 445 ILE 445 445 445 ILE ILE A . n 
A 1 446 ARG 446 446 446 ARG ARG A . n 
A 1 447 ASN 447 447 447 ASN ASN A . n 
A 1 448 ALA 448 448 448 ALA ALA A . n 
A 1 449 PRO 449 449 449 PRO PRO A . n 
A 1 450 ALA 450 450 450 ALA ALA A . n 
A 1 451 VAL 451 451 451 VAL VAL A . n 
A 1 452 ARG 452 452 452 ARG ARG A . n 
A 1 453 ARG 453 453 453 ARG ARG A . n 
A 1 454 ALA 454 454 454 ALA ALA A . n 
A 1 455 ASN 455 455 455 ASN ASN A . n 
A 1 456 LYS 456 456 456 LYS LYS A . n 
A 1 457 ALA 457 457 457 ALA ALA A . n 
A 1 458 MET 458 458 458 MET MET A . n 
A 1 459 LYS 459 459 459 LYS LYS A . n 
A 1 460 SER 460 460 460 SER SER A . n 
A 1 461 ILE 461 461 461 ILE ILE A . n 
A 1 462 GLY 462 462 462 GLY GLY A . n 
A 1 463 LEU 463 463 463 LEU LEU A . n 
A 1 464 GLY 464 464 464 GLY GLY A . n 
A 1 465 ALA 465 465 465 ALA ALA A . n 
A 1 466 MET 466 466 466 MET MET A . n 
A 1 467 ASN 467 467 467 ASN ASN A . n 
A 1 468 LEU 468 468 468 LEU LEU A . n 
A 1 469 HIS 469 469 469 HIS HIS A . n 
A 1 470 GLY 470 470 470 GLY GLY A . n 
A 1 471 TYR 471 471 471 TYR TYR A . n 
A 1 472 LEU 472 472 472 LEU LEU A . n 
A 1 473 ALA 473 473 473 ALA ALA A . n 
A 1 474 GLN 474 474 474 GLN GLN A . n 
A 1 475 ASN 475 475 475 ASN ASN A . n 
A 1 476 GLY 476 476 476 GLY GLY A . n 
A 1 477 ILE 477 477 477 ILE ILE A . n 
A 1 478 ALA 478 478 478 ALA ALA A . n 
A 1 479 TYR 479 479 479 TYR TYR A . n 
A 1 480 GLU 480 480 480 GLU GLU A . n 
A 1 481 SER 481 481 481 SER SER A . n 
A 1 482 PRO 482 482 482 PRO PRO A . n 
A 1 483 GLU 483 483 483 GLU GLU A . n 
A 1 484 ALA 484 484 484 ALA ALA A . n 
A 1 485 ARG 485 485 485 ARG ARG A . n 
A 1 486 ASP 486 486 486 ASP ASP A . n 
A 1 487 PHE 487 487 487 PHE PHE A . n 
A 1 488 ALA 488 488 488 ALA ALA A . n 
A 1 489 ASN 489 489 489 ASN ASN A . n 
A 1 490 THR 490 490 490 THR THR A . n 
A 1 491 PHE 491 491 491 PHE PHE A . n 
A 1 492 PHE 492 492 492 PHE PHE A . n 
A 1 493 MET 493 493 493 MET MET A . n 
A 1 494 MET 494 494 494 MET MET A . n 
A 1 495 VAL 495 495 495 VAL VAL A . n 
A 1 496 ASN 496 496 496 ASN ASN A . n 
A 1 497 PHE 497 497 497 PHE PHE A . n 
A 1 498 TYR 498 498 498 TYR TYR A . n 
A 1 499 SER 499 499 499 SER SER A . n 
A 1 500 ILE 500 500 500 ILE ILE A . n 
A 1 501 GLN 501 501 501 GLN GLN A . n 
A 1 502 ARG 502 502 502 ARG ARG A . n 
A 1 503 SER 503 503 503 SER SER A . n 
A 1 504 ALA 504 504 504 ALA ALA A . n 
A 1 505 GLU 505 505 505 GLU GLU A . n 
A 1 506 ILE 506 506 506 ILE ILE A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 LYS 508 508 508 LYS LYS A . n 
A 1 509 GLU 509 509 509 GLU GLU A . n 
A 1 510 LYS 510 510 510 LYS LYS A . n 
A 1 511 GLY 511 511 511 GLY GLY A . n 
A 1 512 GLU 512 512 512 GLU GLU A . n 
A 1 513 THR 513 513 513 THR THR A . n 
A 1 514 PHE 514 514 514 PHE PHE A . n 
A 1 515 ASP 515 515 515 ASP ASP A . n 
A 1 516 GLN 516 516 516 GLN GLN A . n 
A 1 517 TYR 517 517 517 TYR TYR A . n 
A 1 518 GLU 518 518 518 GLU GLU A . n 
A 1 519 GLY 519 519 519 GLY GLY A . n 
A 1 520 SER 520 520 520 SER SER A . n 
A 1 521 THR 521 521 521 THR THR A . n 
A 1 522 TYR 522 522 522 TYR TYR A . n 
A 1 523 ALA 523 523 523 ALA ALA A . n 
A 1 524 THR 524 524 524 THR THR A . n 
A 1 525 GLY 525 525 525 GLY GLY A . n 
A 1 526 GLU 526 526 526 GLU GLU A . n 
A 1 527 TYR 527 527 527 TYR TYR A . n 
A 1 528 PHE 528 528 528 PHE PHE A . n 
A 1 529 ASP 529 529 529 ASP ASP A . n 
A 1 530 LYS 530 530 530 LYS LYS A . n 
A 1 531 TYR 531 531 531 TYR TYR A . n 
A 1 532 VAL 532 532 532 VAL VAL A . n 
A 1 533 SER 533 533 533 SER SER A . n 
A 1 534 THR 534 534 534 THR THR A . n 
A 1 535 ASP 535 535 535 ASP ASP A . n 
A 1 536 PHE 536 536 536 PHE PHE A . n 
A 1 537 SER 537 537 537 SER SER A . n 
A 1 538 PRO 538 538 538 PRO PRO A . n 
A 1 539 LYS 539 539 539 LYS LYS A . n 
A 1 540 TYR 540 540 540 TYR TYR A . n 
A 1 541 GLU 541 541 541 GLU GLU A . n 
A 1 542 LYS 542 542 542 LYS LYS A . n 
A 1 543 ILE 543 543 543 ILE ILE A . n 
A 1 544 ALA 544 544 544 ALA ALA A . n 
A 1 545 ASN 545 545 545 ASN ASN A . n 
A 1 546 LEU 546 546 546 LEU LEU A . n 
A 1 547 PHE 547 547 547 PHE PHE A . n 
A 1 548 GLU 548 548 548 GLU GLU A . n 
A 1 549 GLY 549 549 549 GLY GLY A . n 
A 1 550 MET 550 550 550 MET MET A . n 
A 1 551 HIS 551 551 551 HIS HIS A . n 
A 1 552 ILE 552 552 552 ILE ILE A . n 
A 1 553 PRO 553 553 553 PRO PRO A . n 
A 1 554 THR 554 554 554 THR THR A . n 
A 1 555 THR 555 555 555 THR THR A . n 
A 1 556 GLU 556 556 556 GLU GLU A . n 
A 1 557 ASP 557 557 557 ASP ASP A . n 
A 1 558 TRP 558 558 558 TRP TRP A . n 
A 1 559 LYS 559 559 559 LYS LYS A . n 
A 1 560 LYS 560 560 560 LYS LYS A . n 
A 1 561 LEU 561 561 561 LEU LEU A . n 
A 1 562 LYS 562 562 562 LYS LYS A . n 
A 1 563 ALA 563 563 563 ALA ALA A . n 
A 1 564 PHE 564 564 564 PHE PHE A . n 
A 1 565 VAL 565 565 565 VAL VAL A . n 
A 1 566 ALA 566 566 566 ALA ALA A . n 
A 1 567 GLU 567 567 567 GLU GLU A . n 
A 1 568 HIS 568 568 568 HIS HIS A . n 
A 1 569 GLY 569 569 569 GLY GLY A . n 
A 1 570 MET 570 570 570 MET MET A . n 
A 1 571 TYR 571 571 571 TYR TYR A . n 
A 1 572 HIS 572 572 572 HIS HIS A . n 
A 1 573 SER 573 573 573 SER SER A . n 
A 1 574 TYR 574 574 574 TYR TYR A . n 
A 1 575 ARG 575 575 575 ARG ARG A . n 
A 1 576 LEU 576 576 576 LEU LEU A . n 
A 1 577 CYS 577 577 577 CYS CYS A . n 
A 1 578 ILE 578 578 578 ILE ILE A . n 
A 1 579 ALA 579 579 579 ALA ALA A . n 
A 1 580 PRO 580 580 580 PRO PRO A . n 
A 1 581 THR 581 581 581 THR THR A . n 
A 1 582 GLY 582 582 582 GLY GLY A . n 
A 1 583 SER 583 583 583 SER SER A . n 
A 1 584 ILE 584 584 584 ILE ILE A . n 
A 1 585 SER 585 585 585 SER SER A . n 
A 1 586 TYR 586 586 586 TYR TYR A . n 
A 1 587 VAL 587 587 587 VAL VAL A . n 
A 1 588 GLN 588 588 588 GLN GLN A . n 
A 1 589 SER 589 589 589 SER SER A . n 
A 1 590 SER 590 590 590 SER SER A . n 
A 1 591 THR 591 591 591 THR THR A . n 
A 1 592 ALA 592 592 592 ALA ALA A . n 
A 1 593 SER 593 593 593 SER SER A . n 
A 1 594 VAL 594 594 594 VAL VAL A . n 
A 1 595 MET 595 595 595 MET MET A . n 
A 1 596 PRO 596 596 596 PRO PRO A . n 
A 1 597 ILE 597 597 597 ILE ILE A . n 
A 1 598 MET 598 598 598 MET MET A . n 
A 1 599 GLU 599 599 599 GLU GLU A . n 
A 1 600 ARG 600 600 600 ARG ARG A . n 
A 1 601 ILE 601 601 601 ILE ILE A . n 
A 1 602 GLU 602 602 602 GLU GLU A . n 
A 1 603 GLU 603 603 603 GLU GLU A . n 
A 1 604 ARG 604 604 604 ARG ARG A . n 
A 1 605 THR 605 605 605 THR THR A . n 
A 1 606 TYR 606 606 606 TYR TYR A . n 
A 1 607 GLY 607 607 607 GLY GLY A . n 
A 1 608 ASN 608 608 608 ASN ASN A . n 
A 1 609 SER 609 609 609 SER SER A . n 
A 1 610 LYS 610 610 610 LYS LYS A . n 
A 1 611 THR 611 611 611 THR THR A . n 
A 1 612 TYR 612 612 612 TYR TYR A . n 
A 1 613 TYR 613 613 613 TYR TYR A . n 
A 1 614 PRO 614 614 614 PRO PRO A . n 
A 1 615 MET 615 615 615 MET MET A . n 
A 1 616 PRO 616 616 616 PRO PRO A . n 
A 1 617 GLY 617 617 617 GLY GLY A . n 
A 1 618 LEU 618 618 618 LEU LEU A . n 
A 1 619 ALA 619 619 619 ALA ALA A . n 
A 1 620 SER 620 620 620 SER SER A . n 
A 1 621 ASN 621 621 621 ASN ASN A . n 
A 1 622 ASN 622 622 622 ASN ASN A . n 
A 1 623 TRP 623 623 623 TRP TRP A . n 
A 1 624 PHE 624 624 624 PHE PHE A . n 
A 1 625 PHE 625 625 625 PHE PHE A . n 
A 1 626 TYR 626 626 626 TYR TYR A . n 
A 1 627 LYS 627 627 627 LYS LYS A . n 
A 1 628 GLU 628 628 628 GLU GLU A . n 
A 1 629 ALA 629 629 629 ALA ALA A . n 
A 1 630 TYR 630 630 630 TYR TYR A . n 
A 1 631 ASP 631 631 631 ASP ASP A . n 
A 1 632 MET 632 632 632 MET MET A . n 
A 1 633 ASP 633 633 633 ASP ASP A . n 
A 1 634 MET 634 634 634 MET MET A . n 
A 1 635 PHE 635 635 635 PHE PHE A . n 
A 1 636 LYS 636 636 636 LYS LYS A . n 
A 1 637 VAL 637 637 637 VAL VAL A . n 
A 1 638 VAL 638 638 638 VAL VAL A . n 
A 1 639 ASP 639 639 639 ASP ASP A . n 
A 1 640 MET 640 640 640 MET MET A . n 
A 1 641 ILE 641 641 641 ILE ILE A . n 
A 1 642 ALA 642 642 642 ALA ALA A . n 
A 1 643 THR 643 643 643 THR THR A . n 
A 1 644 ILE 644 644 644 ILE ILE A . n 
A 1 645 GLN 645 645 645 GLN GLN A . n 
A 1 646 GLN 646 646 646 GLN GLN A . n 
A 1 647 HIS 647 647 647 HIS HIS A . n 
A 1 648 ILE 648 648 648 ILE ILE A . n 
A 1 649 ASP 649 649 649 ASP ASP A . n 
A 1 650 GLN 650 650 650 GLN GLN A . n 
A 1 651 GLY 651 651 651 GLY GLY A . n 
A 1 652 ILE 652 652 652 ILE ILE A . n 
A 1 653 SER 653 653 653 SER SER A . n 
A 1 654 PHE 654 654 654 PHE PHE A . n 
A 1 655 THR 655 655 655 THR THR A . n 
A 1 656 LEU 656 656 656 LEU LEU A . n 
A 1 657 PHE 657 657 657 PHE PHE A . n 
A 1 658 LEU 658 658 658 LEU LEU A . n 
A 1 659 LYS 659 659 659 LYS LYS A . n 
A 1 660 ASP 660 660 660 ASP ASP A . n 
A 1 661 THR 661 661 661 THR THR A . n 
A 1 662 MET 662 662 662 MET MET A . n 
A 1 663 THR 663 663 663 THR THR A . n 
A 1 664 THR 664 664 664 THR THR A . n 
A 1 665 ARG 665 665 665 ARG ARG A . n 
A 1 666 ASP 666 666 666 ASP ASP A . n 
A 1 667 LEU 667 667 667 LEU LEU A . n 
A 1 668 ASN 668 668 668 ASN ASN A . n 
A 1 669 ARG 669 669 669 ARG ARG A . n 
A 1 670 ILE 670 670 670 ILE ILE A . n 
A 1 671 ASP 671 671 671 ASP ASP A . n 
A 1 672 LEU 672 672 672 LEU LEU A . n 
A 1 673 TYR 673 673 673 TYR TYR A . n 
A 1 674 ALA 674 674 674 ALA ALA A . n 
A 1 675 HIS 675 675 675 HIS HIS A . n 
A 1 676 HIS 676 676 676 HIS HIS A . n 
A 1 677 ARG 677 677 677 ARG ARG A . n 
A 1 678 GLY 678 678 678 GLY GLY A . n 
A 1 679 ILE 679 679 679 ILE ILE A . n 
A 1 680 LYS 680 680 680 LYS LYS A . n 
A 1 681 THR 681 681 681 THR THR A . n 
A 1 682 ILE 682 682 682 ILE ILE A . n 
A 1 683 TYR 683 683 683 TYR TYR A . n 
A 1 684 TYR 684 684 684 TYR TYR A . n 
A 1 685 ALA 685 685 685 ALA ALA A . n 
A 1 686 ARG 686 686 686 ARG ARG A . n 
A 1 687 THR 687 687 687 THR THR A . n 
A 1 688 LYS 688 688 688 LYS LYS A . n 
A 1 689 ASP 689 689 ?   ?   ?   A . n 
A 1 690 THR 690 690 ?   ?   ?   A . n 
A 1 691 GLY 691 691 ?   ?   ?   A . n 
A 1 692 GLN 692 692 ?   ?   ?   A . n 
A 1 693 ASP 693 693 ?   ?   ?   A . n 
A 1 694 SER 694 694 ?   ?   ?   A . n 
A 1 695 CYS 695 695 ?   ?   ?   A . n 
A 1 696 LEU 696 696 ?   ?   ?   A . n 
A 1 697 SER 697 697 ?   ?   ?   A . n 
A 1 698 CYS 698 698 ?   ?   ?   A . n 
A 1 699 VAL 699 699 ?   ?   ?   A . n 
A 1 700 VAL 700 700 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   GLN 3   3   ?   ?   ?   B . n 
B 1 4   ASN 4   4   ?   ?   ?   B . n 
B 1 5   GLN 5   5   ?   ?   ?   B . n 
B 1 6   VAL 6   6   6   VAL VAL B . n 
B 1 7   PRO 7   7   7   PRO PRO B . n 
B 1 8   LYS 8   8   8   LYS LYS B . n 
B 1 9   TRP 9   9   9   TRP TRP B . n 
B 1 10  ILE 10  10  10  ILE ILE B . n 
B 1 11  GLN 11  11  11  GLN GLN B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  ASN 14  14  14  ASN ASN B . n 
B 1 15  GLU 15  15  15  GLU GLU B . n 
B 1 16  ILE 16  16  16  ILE ILE B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  LYS 20  20  20  LYS LYS B . n 
B 1 21  ASP 21  21  21  ASP ASP B . n 
B 1 22  GLY 22  22  22  GLY GLY B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  PHE 24  24  24  PHE PHE B . n 
B 1 25  GLN 25  25  25  GLN GLN B . n 
B 1 26  PHE 26  26  26  PHE PHE B . n 
B 1 27  ASP 27  27  27  ASP ASP B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  ASP 29  29  29  ASP ASP B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  GLU 31  31  31  GLU GLU B . n 
B 1 32  ALA 32  32  32  ALA ALA B . n 
B 1 33  VAL 33  33  33  VAL VAL B . n 
B 1 34  HIS 34  34  34  HIS HIS B . n 
B 1 35  SER 35  35  35  SER SER B . n 
B 1 36  TYR 36  36  36  TYR TYR B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  VAL 38  38  38  VAL VAL B . n 
B 1 39  ASP 39  39  39  ASP ASP B . n 
B 1 40  TYR 40  40  40  TYR TYR B . n 
B 1 41  ILE 41  41  41  ILE ILE B . n 
B 1 42  ASN 42  42  42  ASN ASN B . n 
B 1 43  GLN 43  43  43  GLN GLN B . n 
B 1 44  ASN 44  44  44  ASN ASN B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  VAL 46  46  46  VAL VAL B . n 
B 1 47  PHE 47  47  47  PHE PHE B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  HIS 49  49  49  HIS HIS B . n 
B 1 50  ASN 50  50  50  ASN ASN B . n 
B 1 51  LEU 51  51  51  LEU LEU B . n 
B 1 52  LYS 52  52  52  LYS LYS B . n 
B 1 53  GLU 53  53  53  GLU GLU B . n 
B 1 54  LYS 54  54  54  LYS LYS B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  TYR 57  57  57  TYR TYR B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  ASN 61  61  61  ASN ASN B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  TYR 63  63  63  TYR TYR B . n 
B 1 64  TYR 64  64  64  TYR TYR B . n 
B 1 65  GLU 65  65  65  GLU GLU B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  GLU 67  67  67  GLU GLU B . n 
B 1 68  PHE 68  68  68  PHE PHE B . n 
B 1 69  LEU 69  69  69  LEU LEU B . n 
B 1 70  SER 70  70  70  SER SER B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  TYR 72  72  72  TYR TYR B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  PHE 74  74  74  PHE PHE B . n 
B 1 75  GLU 75  75  75  GLU GLU B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  ILE 77  77  77  ILE ILE B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  GLU 79  79  79  GLU GLU B . n 
B 1 80  VAL 80  80  80  VAL VAL B . n 
B 1 81  PHE 81  81  81  PHE PHE B . n 
B 1 82  LYS 82  82  82  LYS LYS B . n 
B 1 83  THR 83  83  83  THR THR B . n 
B 1 84  ALA 84  84  84  ALA ALA B . n 
B 1 85  TYR 85  85  85  TYR TYR B . n 
B 1 86  ALA 86  86  86  ALA ALA B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  PHE 89  89  89  PHE PHE B . n 
B 1 90  ARG 90  90  90  ARG ARG B . n 
B 1 91  PHE 91  91  91  PHE PHE B . n 
B 1 92  PRO 92  92  92  PRO PRO B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  PHE 94  94  94  PHE PHE B . n 
B 1 95  MET 95  95  95  MET MET B . n 
B 1 96  SER 96  96  96  SER SER B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  PHE 98  98  98  PHE PHE B . n 
B 1 99  LYS 99  99  99  LYS LYS B . n 
B 1 100 PHE 100 100 100 PHE PHE B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 ASN 102 102 102 ASN ASN B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 TYR 104 104 104 TYR TYR B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 LYS 107 107 107 LYS LYS B . n 
B 1 108 THR 108 108 108 THR THR B . n 
B 1 109 ASN 109 109 109 ASN ASN B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 LYS 112 112 112 LYS LYS B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 ILE 114 114 114 ILE ILE B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 GLU 116 116 116 GLU GLU B . n 
B 1 117 ARG 117 117 117 ARG ARG B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 GLU 119 119 119 GLU GLU B . n 
B 1 120 ASP 120 120 120 ASP ASP B . n 
B 1 121 ARG 121 121 121 ARG ARG B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 ALA 126 126 126 ALA ALA B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 PHE 128 128 128 PHE PHE B . n 
B 1 129 PHE 129 129 129 PHE PHE B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLY 132 132 132 GLY GLY B . n 
B 1 133 ASP 133 133 133 ASP ASP B . n 
B 1 134 THR 134 134 134 THR THR B . n 
B 1 135 GLU 135 135 135 GLU GLU B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 LYS 138 138 138 LYS LYS B . n 
B 1 139 GLU 139 139 139 GLU GLU B . n 
B 1 140 TYR 140 140 140 TYR TYR B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 MET 144 144 144 MET MET B . n 
B 1 145 ILE 145 145 145 ILE ILE B . n 
B 1 146 ASN 146 146 146 ASN ASN B . n 
B 1 147 GLN 147 147 147 GLN GLN B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 TYR 149 149 149 TYR TYR B . n 
B 1 150 GLN 150 150 150 GLN GLN B . n 
B 1 151 PRO 151 151 151 PRO PRO B . n 
B 1 152 SER 152 152 152 SER SER B . n 
B 1 153 THR 153 153 153 THR THR B . n 
B 1 154 PRO 154 154 154 PRO PRO B . n 
B 1 155 THR 155 155 155 THR THR B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 LEU 157 157 157 LEU LEU B . n 
B 1 158 ASN 158 158 158 ASN ASN B . n 
B 1 159 ALA 159 159 159 ALA ALA B . n 
B 1 160 GLY 160 160 160 GLY GLY B . n 
B 1 161 ARG 161 161 161 ARG ARG B . n 
B 1 162 LYS 162 162 162 LYS LYS B . n 
B 1 163 ARG 163 163 163 ARG ARG B . n 
B 1 164 ARG 164 164 164 ARG ARG B . n 
B 1 165 GLY 165 165 165 GLY GLY B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 CYS 170 170 170 CYS CYS B . n 
B 1 171 PHE 171 171 171 PHE PHE B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 LEU 173 173 173 LEU LEU B . n 
B 1 174 GLU 174 174 174 GLU GLU B . n 
B 1 175 VAL 175 175 175 VAL VAL B . n 
B 1 176 ASN 176 176 176 ASN ASN B . n 
B 1 177 ASP 177 177 177 ASP ASP B . n 
B 1 178 SER 178 178 178 SER SER B . n 
B 1 179 LEU 179 179 179 LEU LEU B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 ASP 181 181 181 ASP ASP B . n 
B 1 182 ILE 182 182 182 ILE ILE B . n 
B 1 183 SER 183 183 183 SER SER B . n 
B 1 184 ARG 184 184 184 ARG ARG B . n 
B 1 185 ALA 185 185 185 ALA ALA B . n 
B 1 186 ILE 186 186 186 ILE ILE B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ILE 188 188 188 ILE ILE B . n 
B 1 189 SER 189 189 189 SER SER B . n 
B 1 190 MET 190 190 190 MET MET B . n 
B 1 191 GLN 191 191 191 GLN GLN B . n 
B 1 192 LEU 192 192 192 LEU LEU B . n 
B 1 193 SER 193 193 193 SER SER B . n 
B 1 194 LYS 194 194 194 LYS LYS B . n 
B 1 195 LEU 195 195 195 LEU LEU B . n 
B 1 196 GLY 196 196 196 GLY GLY B . n 
B 1 197 GLY 197 197 197 GLY GLY B . n 
B 1 198 GLY 198 198 198 GLY GLY B . n 
B 1 199 VAL 199 199 199 VAL VAL B . n 
B 1 200 SER 200 200 200 SER SER B . n 
B 1 201 LEU 201 201 201 LEU LEU B . n 
B 1 202 ASN 202 202 202 ASN ASN B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 SER 204 204 204 SER SER B . n 
B 1 205 LYS 205 205 205 LYS LYS B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 ARG 207 207 207 ARG ARG B . n 
B 1 208 ALA 208 208 208 ALA ALA B . n 
B 1 209 LYS 209 209 209 LYS LYS B . n 
B 1 210 GLY 210 210 210 GLY GLY B . n 
B 1 211 GLU 211 211 211 GLU GLU B . n 
B 1 212 ALA 212 212 212 ALA ALA B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 LYS 214 214 214 LYS LYS B . n 
B 1 215 ASP 215 215 215 ASP ASP B . n 
B 1 216 VAL 216 216 216 VAL VAL B . n 
B 1 217 GLU 217 217 217 GLU GLU B . n 
B 1 218 ASN 218 218 218 ASN ASN B . n 
B 1 219 ALA 219 219 219 ALA ALA B . n 
B 1 220 THR 220 220 220 THR THR B . n 
B 1 221 LYS 221 221 221 LYS LYS B . n 
B 1 222 GLY 222 222 222 GLY GLY B . n 
B 1 223 VAL 223 223 223 VAL VAL B . n 
B 1 224 VAL 224 224 224 VAL VAL B . n 
B 1 225 GLY 225 225 225 GLY GLY B . n 
B 1 226 VAL 226 226 226 VAL VAL B . n 
B 1 227 MET 227 227 227 MET MET B . n 
B 1 228 LYS 228 228 228 LYS LYS B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 ASP 231 231 231 ASP ASP B . n 
B 1 232 ASN 232 232 232 ASN ASN B . n 
B 1 233 ALA 233 233 233 ALA ALA B . n 
B 1 234 PHE 234 234 234 PHE PHE B . n 
B 1 235 ARG 235 235 235 ARG ARG B . n 
B 1 236 TYR 236 236 236 TYR TYR B . n 
B 1 237 ALA 237 237 237 ALA ALA B . n 
B 1 238 ASP 238 238 238 ASP ASP B . n 
B 1 239 GLN 239 239 239 GLN GLN B . n 
B 1 240 MET 240 240 240 MET MET B . n 
B 1 241 GLY 241 241 241 GLY GLY B . n 
B 1 242 GLN 242 242 242 GLN GLN B . n 
B 1 243 ARG 243 243 243 ARG ARG B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 GLY 245 245 245 GLY GLY B . n 
B 1 246 SER 246 246 246 SER SER B . n 
B 1 247 GLY 247 247 247 GLY GLY B . n 
B 1 248 ALA 248 248 248 ALA ALA B . n 
B 1 249 ALA 249 249 249 ALA ALA B . n 
B 1 250 TYR 250 250 250 TYR TYR B . n 
B 1 251 LEU 251 251 251 LEU LEU B . n 
B 1 252 ASN 252 252 252 ASN ASN B . n 
B 1 253 ILE 253 253 253 ILE ILE B . n 
B 1 254 PHE 254 254 254 PHE PHE B . n 
B 1 255 HIS 255 255 255 HIS HIS B . n 
B 1 256 ARG 256 256 256 ARG ARG B . n 
B 1 257 ASP 257 257 257 ASP ASP B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 ASN 259 259 259 ASN ASN B . n 
B 1 260 ASP 260 260 260 ASP ASP B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 THR 264 264 264 THR THR B . n 
B 1 265 LYS 265 265 265 LYS LYS B . n 
B 1 266 LYS 266 266 266 LYS LYS B . n 
B 1 267 ILE 267 267 267 ILE ILE B . n 
B 1 268 SER 268 268 268 SER SER B . n 
B 1 269 ALA 269 269 269 ALA ALA B . n 
B 1 270 ASP 270 270 270 ASP ASP B . n 
B 1 271 GLU 271 271 271 GLU GLU B . n 
B 1 272 ASP 272 272 272 ASP ASP B . n 
B 1 273 VAL 273 273 273 VAL VAL B . n 
B 1 274 ARG 274 274 274 ARG ARG B . n 
B 1 275 VAL 275 275 275 VAL VAL B . n 
B 1 276 LYS 276 276 276 LYS LYS B . n 
B 1 277 THR 277 277 277 THR THR B . n 
B 1 278 LEU 278 278 278 LEU LEU B . n 
B 1 279 SER 279 279 279 SER SER B . n 
B 1 280 ILE 280 280 280 ILE ILE B . n 
B 1 281 GLY 281 281 281 GLY GLY B . n 
B 1 282 VAL 282 282 282 VAL VAL B . n 
B 1 283 VAL 283 283 283 VAL VAL B . n 
B 1 284 ILE 284 284 284 ILE ILE B . n 
B 1 285 PRO 285 285 285 PRO PRO B . n 
B 1 286 ASP 286 286 286 ASP ASP B . n 
B 1 287 LYS 287 287 287 LYS LYS B . n 
B 1 288 PHE 288 288 288 PHE PHE B . n 
B 1 289 VAL 289 289 289 VAL VAL B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 LEU 291 291 291 LEU LEU B . n 
B 1 292 ALA 292 292 292 ALA ALA B . n 
B 1 293 ARG 293 293 293 ARG ARG B . n 
B 1 294 GLU 294 294 294 GLU GLU B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 LYS 296 296 296 LYS LYS B . n 
B 1 297 ALA 297 297 297 ALA ALA B . n 
B 1 298 ALA 298 298 298 ALA ALA B . n 
B 1 299 TYR 299 299 299 TYR TYR B . n 
B 1 300 VAL 300 300 300 VAL VAL B . n 
B 1 301 PHE 301 301 301 PHE PHE B . n 
B 1 302 TYR 302 302 302 TYR TYR B . n 
B 1 303 PRO 303 303 303 PRO PRO B . n 
B 1 304 HIS 304 304 304 HIS HIS B . n 
B 1 305 THR 305 305 305 THR THR B . n 
B 1 306 ILE 306 306 306 ILE ILE B . n 
B 1 307 TYR 307 307 307 TYR TYR B . n 
B 1 308 LYS 308 308 308 LYS LYS B . n 
B 1 309 GLU 309 309 309 GLU GLU B . n 
B 1 310 TYR 310 310 310 TYR TYR B . n 
B 1 311 GLY 311 311 311 GLY GLY B . n 
B 1 312 GLN 312 312 312 GLN GLN B . n 
B 1 313 HIS 313 313 313 HIS HIS B . n 
B 1 314 MET 314 314 314 MET MET B . n 
B 1 315 ASP 315 315 315 ASP ASP B . n 
B 1 316 GLU 316 316 316 GLU GLU B . n 
B 1 317 MET 317 317 317 MET MET B . n 
B 1 318 ASP 318 318 318 ASP ASP B . n 
B 1 319 MET 319 319 319 MET MET B . n 
B 1 320 ASN 320 320 320 ASN ASN B . n 
B 1 321 GLU 321 321 321 GLU GLU B . n 
B 1 322 MET 322 322 322 MET MET B . n 
B 1 323 TYR 323 323 323 TYR TYR B . n 
B 1 324 ASP 324 324 324 ASP ASP B . n 
B 1 325 LYS 325 325 325 LYS LYS B . n 
B 1 326 PHE 326 326 326 PHE PHE B . n 
B 1 327 VAL 327 327 327 VAL VAL B . n 
B 1 328 ASP 328 328 328 ASP ASP B . n 
B 1 329 ASN 329 329 329 ASN ASN B . n 
B 1 330 PRO 330 330 330 PRO PRO B . n 
B 1 331 ARG 331 331 331 ARG ARG B . n 
B 1 332 VAL 332 332 332 VAL VAL B . n 
B 1 333 LYS 333 333 333 LYS LYS B . n 
B 1 334 LYS 334 334 334 LYS LYS B . n 
B 1 335 GLU 335 335 335 GLU GLU B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 ILE 337 337 337 ILE ILE B . n 
B 1 338 ASN 338 338 338 ASN ASN B . n 
B 1 339 PRO 339 339 339 PRO PRO B . n 
B 1 340 ARG 340 340 340 ARG ARG B . n 
B 1 341 LYS 341 341 341 LYS LYS B . n 
B 1 342 LEU 342 342 342 LEU LEU B . n 
B 1 343 LEU 343 343 343 LEU LEU B . n 
B 1 344 GLU 344 344 344 GLU GLU B . n 
B 1 345 LYS 345 345 345 LYS LYS B . n 
B 1 346 LEU 346 346 346 LEU LEU B . n 
B 1 347 ALA 347 347 347 ALA ALA B . n 
B 1 348 MET 348 348 348 MET MET B . n 
B 1 349 LEU 349 349 349 LEU LEU B . n 
B 1 350 ARG 350 350 350 ARG ARG B . n 
B 1 351 SER 351 351 351 SER SER B . n 
B 1 352 GLU 352 352 352 GLU GLU B . n 
B 1 353 SER 353 353 353 SER SER B . n 
B 1 354 GLY 354 354 354 GLY GLY B . n 
B 1 355 TYR 355 355 355 TYR TYR B . n 
B 1 356 PRO 356 356 356 PRO PRO B . n 
B 1 357 TYR 357 357 357 TYR TYR B . n 
B 1 358 ILE 358 358 358 ILE ILE B . n 
B 1 359 MET 359 359 359 MET MET B . n 
B 1 360 PHE 360 360 360 PHE PHE B . n 
B 1 361 GLN 361 361 361 GLN GLN B . n 
B 1 362 ASP 362 362 362 ASP ASP B . n 
B 1 363 ASN 363 363 363 ASN ASN B . n 
B 1 364 VAL 364 364 364 VAL VAL B . n 
B 1 365 ASN 365 365 365 ASN ASN B . n 
B 1 366 LYS 366 366 366 LYS LYS B . n 
B 1 367 VAL 367 367 367 VAL VAL B . n 
B 1 368 HIS 368 368 368 HIS HIS B . n 
B 1 369 ALA 369 369 369 ALA ALA B . n 
B 1 370 ASN 370 370 370 ASN ASN B . n 
B 1 371 ASN 371 371 371 ASN ASN B . n 
B 1 372 HIS 372 372 372 HIS HIS B . n 
B 1 373 ILE 373 373 373 ILE ILE B . n 
B 1 374 SER 374 374 374 SER SER B . n 
B 1 375 LYS 375 375 375 LYS LYS B . n 
B 1 376 VAL 376 376 376 VAL VAL B . n 
B 1 377 LYS 377 377 377 LYS LYS B . n 
B 1 378 PHE 378 378 378 PHE PHE B . n 
B 1 379 SER 379 379 379 SER SER B . n 
B 1 380 ASN 380 380 380 ASN ASN B . n 
B 1 381 LEU 381 381 381 LEU LEU B . n 
B 1 382 CYS 382 382 382 CYS CYS B . n 
B 1 383 SER 383 383 383 SER SER B . n 
B 1 384 GLU 384 384 384 GLU GLU B . n 
B 1 385 VAL 385 385 385 VAL VAL B . n 
B 1 386 LEU 386 386 386 LEU LEU B . n 
B 1 387 GLN 387 387 387 GLN GLN B . n 
B 1 388 ALA 388 388 388 ALA ALA B . n 
B 1 389 SER 389 389 389 SER SER B . n 
B 1 390 GLN 390 390 390 GLN GLN B . n 
B 1 391 VAL 391 391 391 VAL VAL B . n 
B 1 392 SER 392 392 392 SER SER B . n 
B 1 393 SER 393 393 393 SER SER B . n 
B 1 394 TYR 394 394 394 TYR TYR B . n 
B 1 395 THR 395 395 395 THR THR B . n 
B 1 396 ASP 396 396 396 ASP ASP B . n 
B 1 397 TYR 397 397 397 TYR TYR B . n 
B 1 398 ASP 398 398 398 ASP ASP B . n 
B 1 399 GLU 399 399 399 GLU GLU B . n 
B 1 400 GLU 400 400 400 GLU GLU B . n 
B 1 401 ASP 401 401 401 ASP ASP B . n 
B 1 402 GLU 402 402 402 GLU GLU B . n 
B 1 403 ILE 403 403 403 ILE ILE B . n 
B 1 404 GLY 404 404 404 GLY GLY B . n 
B 1 405 LEU 405 405 405 LEU LEU B . n 
B 1 406 ASP 406 406 406 ASP ASP B . n 
B 1 407 ILE 407 407 407 ILE ILE B . n 
B 1 408 SER 408 408 408 SER SER B . n 
B 1 409 CYS 409 409 409 CYS CYS B . n 
B 1 410 ASN 410 410 410 ASN ASN B . n 
B 1 411 LEU 411 411 411 LEU LEU B . n 
B 1 412 GLY 412 412 412 GLY GLY B . n 
B 1 413 SER 413 413 413 SER SER B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 ASN 415 415 415 ASN ASN B . n 
B 1 416 ILE 416 416 416 ILE ILE B . n 
B 1 417 LEU 417 417 417 LEU LEU B . n 
B 1 418 ASN 418 418 418 ASN ASN B . n 
B 1 419 VAL 419 419 419 VAL VAL B . n 
B 1 420 MET 420 420 420 MET MET B . n 
B 1 421 GLU 421 421 421 GLU GLU B . n 
B 1 422 HIS 422 422 422 HIS HIS B . n 
B 1 423 LYS 423 423 423 LYS LYS B . n 
B 1 424 SER 424 424 424 SER SER B . n 
B 1 425 ILE 425 425 425 ILE ILE B . n 
B 1 426 GLU 426 426 426 GLU GLU B . n 
B 1 427 LYS 427 427 427 LYS LYS B . n 
B 1 428 THR 428 428 428 THR THR B . n 
B 1 429 VAL 429 429 429 VAL VAL B . n 
B 1 430 LYS 430 430 430 LYS LYS B . n 
B 1 431 LEU 431 431 431 LEU LEU B . n 
B 1 432 ALA 432 432 432 ALA ALA B . n 
B 1 433 THR 433 433 433 THR THR B . n 
B 1 434 ASP 434 434 434 ASP ASP B . n 
B 1 435 SER 435 435 435 SER SER B . n 
B 1 436 LEU 436 436 436 LEU LEU B . n 
B 1 437 THR 437 437 437 THR THR B . n 
B 1 438 HIS 438 438 438 HIS HIS B . n 
B 1 439 VAL 439 439 439 VAL VAL B . n 
B 1 440 SER 440 440 440 SER SER B . n 
B 1 441 GLU 441 441 441 GLU GLU B . n 
B 1 442 THR 442 442 442 THR THR B . n 
B 1 443 THR 443 443 443 THR THR B . n 
B 1 444 ASP 444 444 444 ASP ASP B . n 
B 1 445 ILE 445 445 445 ILE ILE B . n 
B 1 446 ARG 446 446 446 ARG ARG B . n 
B 1 447 ASN 447 447 447 ASN ASN B . n 
B 1 448 ALA 448 448 448 ALA ALA B . n 
B 1 449 PRO 449 449 449 PRO PRO B . n 
B 1 450 ALA 450 450 450 ALA ALA B . n 
B 1 451 VAL 451 451 451 VAL VAL B . n 
B 1 452 ARG 452 452 452 ARG ARG B . n 
B 1 453 ARG 453 453 453 ARG ARG B . n 
B 1 454 ALA 454 454 454 ALA ALA B . n 
B 1 455 ASN 455 455 455 ASN ASN B . n 
B 1 456 LYS 456 456 456 LYS LYS B . n 
B 1 457 ALA 457 457 457 ALA ALA B . n 
B 1 458 MET 458 458 458 MET MET B . n 
B 1 459 LYS 459 459 459 LYS LYS B . n 
B 1 460 SER 460 460 460 SER SER B . n 
B 1 461 ILE 461 461 461 ILE ILE B . n 
B 1 462 GLY 462 462 462 GLY GLY B . n 
B 1 463 LEU 463 463 463 LEU LEU B . n 
B 1 464 GLY 464 464 464 GLY GLY B . n 
B 1 465 ALA 465 465 465 ALA ALA B . n 
B 1 466 MET 466 466 466 MET MET B . n 
B 1 467 ASN 467 467 467 ASN ASN B . n 
B 1 468 LEU 468 468 468 LEU LEU B . n 
B 1 469 HIS 469 469 469 HIS HIS B . n 
B 1 470 GLY 470 470 470 GLY GLY B . n 
B 1 471 TYR 471 471 471 TYR TYR B . n 
B 1 472 LEU 472 472 472 LEU LEU B . n 
B 1 473 ALA 473 473 473 ALA ALA B . n 
B 1 474 GLN 474 474 474 GLN GLN B . n 
B 1 475 ASN 475 475 475 ASN ASN B . n 
B 1 476 GLY 476 476 476 GLY GLY B . n 
B 1 477 ILE 477 477 477 ILE ILE B . n 
B 1 478 ALA 478 478 478 ALA ALA B . n 
B 1 479 TYR 479 479 479 TYR TYR B . n 
B 1 480 GLU 480 480 480 GLU GLU B . n 
B 1 481 SER 481 481 481 SER SER B . n 
B 1 482 PRO 482 482 482 PRO PRO B . n 
B 1 483 GLU 483 483 483 GLU GLU B . n 
B 1 484 ALA 484 484 484 ALA ALA B . n 
B 1 485 ARG 485 485 485 ARG ARG B . n 
B 1 486 ASP 486 486 486 ASP ASP B . n 
B 1 487 PHE 487 487 487 PHE PHE B . n 
B 1 488 ALA 488 488 488 ALA ALA B . n 
B 1 489 ASN 489 489 489 ASN ASN B . n 
B 1 490 THR 490 490 490 THR THR B . n 
B 1 491 PHE 491 491 491 PHE PHE B . n 
B 1 492 PHE 492 492 492 PHE PHE B . n 
B 1 493 MET 493 493 493 MET MET B . n 
B 1 494 MET 494 494 494 MET MET B . n 
B 1 495 VAL 495 495 495 VAL VAL B . n 
B 1 496 ASN 496 496 496 ASN ASN B . n 
B 1 497 PHE 497 497 497 PHE PHE B . n 
B 1 498 TYR 498 498 498 TYR TYR B . n 
B 1 499 SER 499 499 499 SER SER B . n 
B 1 500 ILE 500 500 500 ILE ILE B . n 
B 1 501 GLN 501 501 501 GLN GLN B . n 
B 1 502 ARG 502 502 502 ARG ARG B . n 
B 1 503 SER 503 503 503 SER SER B . n 
B 1 504 ALA 504 504 504 ALA ALA B . n 
B 1 505 GLU 505 505 505 GLU GLU B . n 
B 1 506 ILE 506 506 506 ILE ILE B . n 
B 1 507 ALA 507 507 507 ALA ALA B . n 
B 1 508 LYS 508 508 508 LYS LYS B . n 
B 1 509 GLU 509 509 509 GLU GLU B . n 
B 1 510 LYS 510 510 510 LYS LYS B . n 
B 1 511 GLY 511 511 511 GLY GLY B . n 
B 1 512 GLU 512 512 512 GLU GLU B . n 
B 1 513 THR 513 513 513 THR THR B . n 
B 1 514 PHE 514 514 514 PHE PHE B . n 
B 1 515 ASP 515 515 515 ASP ASP B . n 
B 1 516 GLN 516 516 516 GLN GLN B . n 
B 1 517 TYR 517 517 517 TYR TYR B . n 
B 1 518 GLU 518 518 518 GLU GLU B . n 
B 1 519 GLY 519 519 519 GLY GLY B . n 
B 1 520 SER 520 520 520 SER SER B . n 
B 1 521 THR 521 521 521 THR THR B . n 
B 1 522 TYR 522 522 522 TYR TYR B . n 
B 1 523 ALA 523 523 523 ALA ALA B . n 
B 1 524 THR 524 524 524 THR THR B . n 
B 1 525 GLY 525 525 525 GLY GLY B . n 
B 1 526 GLU 526 526 526 GLU GLU B . n 
B 1 527 TYR 527 527 527 TYR TYR B . n 
B 1 528 PHE 528 528 528 PHE PHE B . n 
B 1 529 ASP 529 529 529 ASP ASP B . n 
B 1 530 LYS 530 530 530 LYS LYS B . n 
B 1 531 TYR 531 531 531 TYR TYR B . n 
B 1 532 VAL 532 532 532 VAL VAL B . n 
B 1 533 SER 533 533 533 SER SER B . n 
B 1 534 THR 534 534 534 THR THR B . n 
B 1 535 ASP 535 535 535 ASP ASP B . n 
B 1 536 PHE 536 536 536 PHE PHE B . n 
B 1 537 SER 537 537 537 SER SER B . n 
B 1 538 PRO 538 538 538 PRO PRO B . n 
B 1 539 LYS 539 539 539 LYS LYS B . n 
B 1 540 TYR 540 540 540 TYR TYR B . n 
B 1 541 GLU 541 541 541 GLU GLU B . n 
B 1 542 LYS 542 542 542 LYS LYS B . n 
B 1 543 ILE 543 543 543 ILE ILE B . n 
B 1 544 ALA 544 544 544 ALA ALA B . n 
B 1 545 ASN 545 545 545 ASN ASN B . n 
B 1 546 LEU 546 546 546 LEU LEU B . n 
B 1 547 PHE 547 547 547 PHE PHE B . n 
B 1 548 GLU 548 548 548 GLU GLU B . n 
B 1 549 GLY 549 549 549 GLY GLY B . n 
B 1 550 MET 550 550 550 MET MET B . n 
B 1 551 HIS 551 551 551 HIS HIS B . n 
B 1 552 ILE 552 552 552 ILE ILE B . n 
B 1 553 PRO 553 553 553 PRO PRO B . n 
B 1 554 THR 554 554 554 THR THR B . n 
B 1 555 THR 555 555 555 THR THR B . n 
B 1 556 GLU 556 556 556 GLU GLU B . n 
B 1 557 ASP 557 557 557 ASP ASP B . n 
B 1 558 TRP 558 558 558 TRP TRP B . n 
B 1 559 LYS 559 559 559 LYS LYS B . n 
B 1 560 LYS 560 560 560 LYS LYS B . n 
B 1 561 LEU 561 561 561 LEU LEU B . n 
B 1 562 LYS 562 562 562 LYS LYS B . n 
B 1 563 ALA 563 563 563 ALA ALA B . n 
B 1 564 PHE 564 564 564 PHE PHE B . n 
B 1 565 VAL 565 565 565 VAL VAL B . n 
B 1 566 ALA 566 566 566 ALA ALA B . n 
B 1 567 GLU 567 567 567 GLU GLU B . n 
B 1 568 HIS 568 568 568 HIS HIS B . n 
B 1 569 GLY 569 569 569 GLY GLY B . n 
B 1 570 MET 570 570 570 MET MET B . n 
B 1 571 TYR 571 571 571 TYR TYR B . n 
B 1 572 HIS 572 572 572 HIS HIS B . n 
B 1 573 SER 573 573 573 SER SER B . n 
B 1 574 TYR 574 574 574 TYR TYR B . n 
B 1 575 ARG 575 575 575 ARG ARG B . n 
B 1 576 LEU 576 576 576 LEU LEU B . n 
B 1 577 CYS 577 577 577 CYS CYS B . n 
B 1 578 ILE 578 578 578 ILE ILE B . n 
B 1 579 ALA 579 579 579 ALA ALA B . n 
B 1 580 PRO 580 580 580 PRO PRO B . n 
B 1 581 THR 581 581 581 THR THR B . n 
B 1 582 GLY 582 582 582 GLY GLY B . n 
B 1 583 SER 583 583 583 SER SER B . n 
B 1 584 ILE 584 584 584 ILE ILE B . n 
B 1 585 SER 585 585 585 SER SER B . n 
B 1 586 TYR 586 586 586 TYR TYR B . n 
B 1 587 VAL 587 587 587 VAL VAL B . n 
B 1 588 GLN 588 588 588 GLN GLN B . n 
B 1 589 SER 589 589 589 SER SER B . n 
B 1 590 SER 590 590 590 SER SER B . n 
B 1 591 THR 591 591 591 THR THR B . n 
B 1 592 ALA 592 592 592 ALA ALA B . n 
B 1 593 SER 593 593 593 SER SER B . n 
B 1 594 VAL 594 594 594 VAL VAL B . n 
B 1 595 MET 595 595 595 MET MET B . n 
B 1 596 PRO 596 596 596 PRO PRO B . n 
B 1 597 ILE 597 597 597 ILE ILE B . n 
B 1 598 MET 598 598 598 MET MET B . n 
B 1 599 GLU 599 599 599 GLU GLU B . n 
B 1 600 ARG 600 600 600 ARG ARG B . n 
B 1 601 ILE 601 601 601 ILE ILE B . n 
B 1 602 GLU 602 602 602 GLU GLU B . n 
B 1 603 GLU 603 603 603 GLU GLU B . n 
B 1 604 ARG 604 604 604 ARG ARG B . n 
B 1 605 THR 605 605 605 THR THR B . n 
B 1 606 TYR 606 606 606 TYR TYR B . n 
B 1 607 GLY 607 607 607 GLY GLY B . n 
B 1 608 ASN 608 608 608 ASN ASN B . n 
B 1 609 SER 609 609 609 SER SER B . n 
B 1 610 LYS 610 610 610 LYS LYS B . n 
B 1 611 THR 611 611 611 THR THR B . n 
B 1 612 TYR 612 612 612 TYR TYR B . n 
B 1 613 TYR 613 613 613 TYR TYR B . n 
B 1 614 PRO 614 614 614 PRO PRO B . n 
B 1 615 MET 615 615 615 MET MET B . n 
B 1 616 PRO 616 616 616 PRO PRO B . n 
B 1 617 GLY 617 617 617 GLY GLY B . n 
B 1 618 LEU 618 618 618 LEU LEU B . n 
B 1 619 ALA 619 619 619 ALA ALA B . n 
B 1 620 SER 620 620 620 SER SER B . n 
B 1 621 ASN 621 621 621 ASN ASN B . n 
B 1 622 ASN 622 622 622 ASN ASN B . n 
B 1 623 TRP 623 623 623 TRP TRP B . n 
B 1 624 PHE 624 624 624 PHE PHE B . n 
B 1 625 PHE 625 625 625 PHE PHE B . n 
B 1 626 TYR 626 626 626 TYR TYR B . n 
B 1 627 LYS 627 627 627 LYS LYS B . n 
B 1 628 GLU 628 628 628 GLU GLU B . n 
B 1 629 ALA 629 629 629 ALA ALA B . n 
B 1 630 TYR 630 630 630 TYR TYR B . n 
B 1 631 ASP 631 631 631 ASP ASP B . n 
B 1 632 MET 632 632 632 MET MET B . n 
B 1 633 ASP 633 633 633 ASP ASP B . n 
B 1 634 MET 634 634 634 MET MET B . n 
B 1 635 PHE 635 635 635 PHE PHE B . n 
B 1 636 LYS 636 636 636 LYS LYS B . n 
B 1 637 VAL 637 637 637 VAL VAL B . n 
B 1 638 VAL 638 638 638 VAL VAL B . n 
B 1 639 ASP 639 639 639 ASP ASP B . n 
B 1 640 MET 640 640 640 MET MET B . n 
B 1 641 ILE 641 641 641 ILE ILE B . n 
B 1 642 ALA 642 642 642 ALA ALA B . n 
B 1 643 THR 643 643 643 THR THR B . n 
B 1 644 ILE 644 644 644 ILE ILE B . n 
B 1 645 GLN 645 645 645 GLN GLN B . n 
B 1 646 GLN 646 646 646 GLN GLN B . n 
B 1 647 HIS 647 647 647 HIS HIS B . n 
B 1 648 ILE 648 648 648 ILE ILE B . n 
B 1 649 ASP 649 649 649 ASP ASP B . n 
B 1 650 GLN 650 650 650 GLN GLN B . n 
B 1 651 GLY 651 651 651 GLY GLY B . n 
B 1 652 ILE 652 652 652 ILE ILE B . n 
B 1 653 SER 653 653 653 SER SER B . n 
B 1 654 PHE 654 654 654 PHE PHE B . n 
B 1 655 THR 655 655 655 THR THR B . n 
B 1 656 LEU 656 656 656 LEU LEU B . n 
B 1 657 PHE 657 657 657 PHE PHE B . n 
B 1 658 LEU 658 658 658 LEU LEU B . n 
B 1 659 LYS 659 659 659 LYS LYS B . n 
B 1 660 ASP 660 660 660 ASP ASP B . n 
B 1 661 THR 661 661 661 THR THR B . n 
B 1 662 MET 662 662 662 MET MET B . n 
B 1 663 THR 663 663 663 THR THR B . n 
B 1 664 THR 664 664 664 THR THR B . n 
B 1 665 ARG 665 665 665 ARG ARG B . n 
B 1 666 ASP 666 666 666 ASP ASP B . n 
B 1 667 LEU 667 667 667 LEU LEU B . n 
B 1 668 ASN 668 668 668 ASN ASN B . n 
B 1 669 ARG 669 669 669 ARG ARG B . n 
B 1 670 ILE 670 670 670 ILE ILE B . n 
B 1 671 ASP 671 671 671 ASP ASP B . n 
B 1 672 LEU 672 672 672 LEU LEU B . n 
B 1 673 TYR 673 673 673 TYR TYR B . n 
B 1 674 ALA 674 674 674 ALA ALA B . n 
B 1 675 HIS 675 675 675 HIS HIS B . n 
B 1 676 HIS 676 676 676 HIS HIS B . n 
B 1 677 ARG 677 677 677 ARG ARG B . n 
B 1 678 GLY 678 678 678 GLY GLY B . n 
B 1 679 ILE 679 679 679 ILE ILE B . n 
B 1 680 LYS 680 680 680 LYS LYS B . n 
B 1 681 THR 681 681 681 THR THR B . n 
B 1 682 ILE 682 682 682 ILE ILE B . n 
B 1 683 TYR 683 683 683 TYR TYR B . n 
B 1 684 TYR 684 684 684 TYR TYR B . n 
B 1 685 ALA 685 685 685 ALA ALA B . n 
B 1 686 ARG 686 686 686 ARG ARG B . n 
B 1 687 THR 687 687 687 THR THR B . n 
B 1 688 LYS 688 688 688 LYS LYS B . n 
B 1 689 ASP 689 689 ?   ?   ?   B . n 
B 1 690 THR 690 690 ?   ?   ?   B . n 
B 1 691 GLY 691 691 ?   ?   ?   B . n 
B 1 692 GLN 692 692 ?   ?   ?   B . n 
B 1 693 ASP 693 693 ?   ?   ?   B . n 
B 1 694 SER 694 694 ?   ?   ?   B . n 
B 1 695 CYS 695 695 ?   ?   ?   B . n 
B 1 696 LEU 696 696 ?   ?   ?   B . n 
B 1 697 SER 697 697 ?   ?   ?   B . n 
B 1 698 CYS 698 698 ?   ?   ?   B . n 
B 1 699 VAL 699 699 ?   ?   ?   B . n 
B 1 700 VAL 700 700 ?   ?   ?   B . n 
C 2 1   MET 1   -20 ?   ?   ?   C . n 
C 2 2   GLY 2   -19 ?   ?   ?   C . n 
C 2 3   SER 3   -18 ?   ?   ?   C . n 
C 2 4   SER 4   -17 ?   ?   ?   C . n 
C 2 5   HIS 5   -16 ?   ?   ?   C . n 
C 2 6   HIS 6   -15 ?   ?   ?   C . n 
C 2 7   HIS 7   -14 ?   ?   ?   C . n 
C 2 8   HIS 8   -13 ?   ?   ?   C . n 
C 2 9   HIS 9   -12 ?   ?   ?   C . n 
C 2 10  HIS 10  -11 ?   ?   ?   C . n 
C 2 11  SER 11  -10 ?   ?   ?   C . n 
C 2 12  SER 12  -9  ?   ?   ?   C . n 
C 2 13  GLY 13  -8  ?   ?   ?   C . n 
C 2 14  LEU 14  -7  ?   ?   ?   C . n 
C 2 15  VAL 15  -6  ?   ?   ?   C . n 
C 2 16  PRO 16  -5  ?   ?   ?   C . n 
C 2 17  ARG 17  -4  ?   ?   ?   C . n 
C 2 18  GLY 18  -3  ?   ?   ?   C . n 
C 2 19  SER 19  -2  ?   ?   ?   C . n 
C 2 20  HIS 20  -1  ?   ?   ?   C . n 
C 2 21  MET 21  0   ?   ?   ?   C . n 
C 2 22  MET 22  1   ?   ?   ?   C . n 
C 2 23  THR 23  2   ?   ?   ?   C . n 
C 2 24  LYS 24  3   ?   ?   ?   C . n 
C 2 25  ILE 25  4   ?   ?   ?   C . n 
C 2 26  TYR 26  5   ?   ?   ?   C . n 
C 2 27  ASP 27  6   ?   ?   ?   C . n 
C 2 28  ALA 28  7   ?   ?   ?   C . n 
C 2 29  ALA 29  8   ?   ?   ?   C . n 
C 2 30  ASN 30  9   ?   ?   ?   C . n 
C 2 31  TRP 31  10  ?   ?   ?   C . n 
C 2 32  SER 32  11  ?   ?   ?   C . n 
C 2 33  LYS 33  12  ?   ?   ?   C . n 
C 2 34  HIS 34  13  ?   ?   ?   C . n 
C 2 35  GLU 35  14  ?   ?   ?   C . n 
C 2 36  ASP 36  15  ?   ?   ?   C . n 
C 2 37  ASP 37  16  16  ASP ASP C . n 
C 2 38  PHE 38  17  17  PHE PHE C . n 
C 2 39  THR 39  18  18  THR THR C . n 
C 2 40  GLN 40  19  19  GLN GLN C . n 
C 2 41  MET 41  20  20  MET MET C . n 
C 2 42  PHE 42  21  21  PHE PHE C . n 
C 2 43  TYR 43  22  22  TYR TYR C . n 
C 2 44  ASN 44  23  23  ASN ASN C . n 
C 2 45  GLN 45  24  24  GLN GLN C . n 
C 2 46  ASN 46  25  25  ASN ASN C . n 
C 2 47  VAL 47  26  26  VAL VAL C . n 
C 2 48  LYS 48  27  27  LYS LYS C . n 
C 2 49  GLN 49  28  28  GLN GLN C . n 
C 2 50  PHE 50  29  29  PHE PHE C . n 
C 2 51  TRP 51  30  30  TRP TRP C . n 
C 2 52  LEU 52  31  31  LEU LEU C . n 
C 2 53  PRO 53  32  32  PRO PRO C . n 
C 2 54  GLU 54  33  33  GLU GLU C . n 
C 2 55  GLU 55  34  34  GLU GLU C . n 
C 2 56  ILE 56  35  35  ILE ILE C . n 
C 2 57  ALA 57  36  36  ALA ALA C . n 
C 2 58  LEU 58  37  37  LEU LEU C . n 
C 2 59  ASN 59  38  38  ASN ASN C . n 
C 2 60  GLY 60  39  39  GLY GLY C . n 
C 2 61  ASP 61  40  40  ASP ASP C . n 
C 2 62  LEU 62  41  41  LEU LEU C . n 
C 2 63  LEU 63  42  42  LEU LEU C . n 
C 2 64  THR 64  43  43  THR THR C . n 
C 2 65  TRP 65  44  44  TRP TRP C . n 
C 2 66  LYS 66  45  45  LYS LYS C . n 
C 2 67  TYR 67  46  46  TYR TYR C . n 
C 2 68  LEU 68  47  47  LEU LEU C . n 
C 2 69  GLY 69  48  48  GLY GLY C . n 
C 2 70  LYS 70  49  49  LYS LYS C . n 
C 2 71  ASN 71  50  50  ASN ASN C . n 
C 2 72  GLU 72  51  51  GLU GLU C . n 
C 2 73  GLN 73  52  52  GLN GLN C . n 
C 2 74  ASP 74  53  53  ASP ASP C . n 
C 2 75  THR 75  54  54  THR THR C . n 
C 2 76  TYR 76  55  55  TYR TYR C . n 
C 2 77  MET 77  56  56  MET MET C . n 
C 2 78  LYS 78  57  57  LYS LYS C . n 
C 2 79  VAL 79  58  58  VAL VAL C . n 
C 2 80  LEU 80  59  59  LEU LEU C . n 
C 2 81  ALA 81  60  60  ALA ALA C . n 
C 2 82  GLY 82  61  61  GLY GLY C . n 
C 2 83  LEU 83  62  62  LEU LEU C . n 
C 2 84  THR 84  63  63  THR THR C . n 
C 2 85  LEU 85  64  64  LEU LEU C . n 
C 2 86  LEU 86  65  65  LEU LEU C . n 
C 2 87  ASP 87  66  66  ASP ASP C . n 
C 2 88  THR 88  67  67  THR THR C . n 
C 2 89  GLU 89  68  68  GLU GLU C . n 
C 2 90  GLN 90  69  69  GLN GLN C . n 
C 2 91  GLY 91  70  70  GLY GLY C . n 
C 2 92  ASN 92  71  71  ASN ASN C . n 
C 2 93  THR 93  72  72  THR THR C . n 
C 2 94  GLY 94  73  73  GLY GLY C . n 
C 2 95  MET 95  74  74  MET MET C . n 
C 2 96  PRO 96  75  75  PRO PRO C . n 
C 2 97  ILE 97  76  76  ILE ILE C . n 
C 2 98  VAL 98  77  77  VAL VAL C . n 
C 2 99  ALA 99  78  78  ALA ALA C . n 
C 2 100 GLU 100 79  79  GLU GLU C . n 
C 2 101 HIS 101 80  80  HIS HIS C . n 
C 2 102 VAL 102 81  81  VAL VAL C . n 
C 2 103 ASP 103 82  82  ASP ASP C . n 
C 2 104 GLY 104 83  83  GLY GLY C . n 
C 2 105 HIS 105 84  84  HIS HIS C . n 
C 2 106 GLN 106 85  85  GLN GLN C . n 
C 2 107 ARG 107 86  86  ARG ARG C . n 
C 2 108 LYS 108 87  87  LYS LYS C . n 
C 2 109 ALA 109 88  88  ALA ALA C . n 
C 2 110 VAL 110 89  89  VAL VAL C . n 
C 2 111 LEU 111 90  90  LEU LEU C . n 
C 2 112 ASN 112 91  91  ASN ASN C . n 
C 2 113 PHE 113 92  92  PHE PHE C . n 
C 2 114 MET 114 93  93  MET MET C . n 
C 2 115 ALA 115 94  94  ALA ALA C . n 
C 2 116 MET 116 95  95  MET MET C . n 
C 2 117 MET 117 96  96  MET MET C . n 
C 2 118 GLU 118 97  97  GLU GLU C . n 
C 2 119 ASN 119 98  98  ASN ASN C . n 
C 2 120 ALA 120 99  99  ALA ALA C . n 
C 2 121 VAL 121 100 100 VAL VAL C . n 
C 2 122 HIS 122 101 101 HIS HIS C . n 
C 2 123 ALA 123 102 102 ALA ALA C . n 
C 2 124 LYS 124 103 103 LYS LYS C . n 
C 2 125 SER 125 104 104 SER SER C . n 
C 2 126 TYR 126 105 105 TYR TYR C . n 
C 2 127 SER 127 106 106 SER SER C . n 
C 2 128 ASN 128 107 107 ASN ASN C . n 
C 2 129 ILE 129 108 108 ILE ILE C . n 
C 2 130 PHE 130 109 109 PHE PHE C . n 
C 2 131 MET 131 110 110 MET MET C . n 
C 2 132 THR 132 111 111 THR THR C . n 
C 2 133 LEU 133 112 112 LEU LEU C . n 
C 2 134 ALA 134 113 113 ALA ALA C . n 
C 2 135 PRO 135 114 114 PRO PRO C . n 
C 2 136 THR 136 115 115 THR THR C . n 
C 2 137 GLU 137 116 116 GLU GLU C . n 
C 2 138 THR 138 117 117 THR THR C . n 
C 2 139 ILE 139 118 118 ILE ILE C . n 
C 2 140 ASN 140 119 119 ASN ASN C . n 
C 2 141 GLU 141 120 120 GLU GLU C . n 
C 2 142 VAL 142 121 121 VAL VAL C . n 
C 2 143 PHE 143 122 122 PHE PHE C . n 
C 2 144 GLU 144 123 123 GLU GLU C . n 
C 2 145 TRP 145 124 124 TRP TRP C . n 
C 2 146 VAL 146 125 125 VAL VAL C . n 
C 2 147 LYS 147 126 126 LYS LYS C . n 
C 2 148 GLN 148 127 127 GLN GLN C . n 
C 2 149 ASN 149 128 128 ASN ASN C . n 
C 2 150 LYS 150 129 129 LYS LYS C . n 
C 2 151 TYR 151 130 130 TYR TYR C . n 
C 2 152 LEU 152 131 131 LEU LEU C . n 
C 2 153 GLN 153 132 132 GLN GLN C . n 
C 2 154 LYS 154 133 133 LYS LYS C . n 
C 2 155 LYS 155 134 134 LYS LYS C . n 
C 2 156 ALA 156 135 135 ALA ALA C . n 
C 2 157 GLN 157 136 136 GLN GLN C . n 
C 2 158 MET 158 137 137 MET MET C . n 
C 2 159 ILE 159 138 138 ILE ILE C . n 
C 2 160 VAL 160 139 139 VAL VAL C . n 
C 2 161 GLY 161 140 140 GLY GLY C . n 
C 2 162 LEU 162 141 141 LEU LEU C . n 
C 2 163 TYR 163 142 142 TYR TYR C . n 
C 2 164 LYS 164 143 143 LYS LYS C . n 
C 2 165 ALA 165 144 144 ALA ALA C . n 
C 2 166 ILE 166 145 145 ILE ILE C . n 
C 2 167 GLN 167 146 146 GLN GLN C . n 
C 2 168 LYS 168 147 147 LYS LYS C . n 
C 2 169 ASP 169 148 148 ASP ASP C . n 
C 2 170 ASP 170 149 149 ASP ASP C . n 
C 2 171 GLU 171 150 150 GLU GLU C . n 
C 2 172 ILE 172 151 151 ILE ILE C . n 
C 2 173 SER 173 152 152 SER SER C . n 
C 2 174 LEU 174 153 153 LEU LEU C . n 
C 2 175 PHE 175 154 154 PHE PHE C . n 
C 2 176 LYS 176 155 155 LYS LYS C . n 
C 2 177 ALA 177 156 156 ALA ALA C . n 
C 2 178 MET 178 157 157 MET MET C . n 
C 2 179 VAL 179 158 158 VAL VAL C . n 
C 2 180 ALA 180 159 159 ALA ALA C . n 
C 2 181 SER 181 160 160 SER SER C . n 
C 2 182 VAL 182 161 161 VAL VAL C . n 
C 2 183 TYR 183 162 162 TYR TYR C . n 
C 2 184 LEU 184 163 163 LEU LEU C . n 
C 2 185 GLU 185 164 164 GLU GLU C . n 
C 2 186 SER 186 165 165 SER SER C . n 
C 2 187 PHE 187 166 166 PHE PHE C . n 
C 2 188 LEU 188 167 167 LEU LEU C . n 
C 2 189 PHE 189 168 168 PHE PHE C . n 
C 2 190 TYR 190 169 169 TYR TYR C . n 
C 2 191 SER 191 170 170 SER SER C . n 
C 2 192 GLY 192 171 171 GLY GLY C . n 
C 2 193 PHE 193 172 172 PHE PHE C . n 
C 2 194 TYR 194 173 173 TYR TYR C . n 
C 2 195 TYR 195 174 174 TYR TYR C . n 
C 2 196 PRO 196 175 175 PRO PRO C . n 
C 2 197 LEU 197 176 176 LEU LEU C . n 
C 2 198 TYR 198 177 177 TYR TYR C . n 
C 2 199 PHE 199 178 178 PHE PHE C . n 
C 2 200 TYR 200 179 179 TYR TYR C . n 
C 2 201 GLY 201 180 180 GLY GLY C . n 
C 2 202 GLN 202 181 181 GLN GLN C . n 
C 2 203 GLY 203 182 182 GLY GLY C . n 
C 2 204 LYS 204 183 183 LYS LYS C . n 
C 2 205 LEU 205 184 184 LEU LEU C . n 
C 2 206 MET 206 185 185 MET MET C . n 
C 2 207 GLN 207 186 186 GLN GLN C . n 
C 2 208 SER 208 187 187 SER SER C . n 
C 2 209 GLY 209 188 188 GLY GLY C . n 
C 2 210 GLU 210 189 189 GLU GLU C . n 
C 2 211 ILE 211 190 190 ILE ILE C . n 
C 2 212 ILE 212 191 191 ILE ILE C . n 
C 2 213 ASN 213 192 192 ASN ASN C . n 
C 2 214 LEU 214 193 193 LEU LEU C . n 
C 2 215 ILE 215 194 194 ILE ILE C . n 
C 2 216 LEU 216 195 195 LEU LEU C . n 
C 2 217 ARG 217 196 196 ARG ARG C . n 
C 2 218 ASP 218 197 197 ASP ASP C . n 
C 2 219 GLU 219 198 198 GLU GLU C . n 
C 2 220 ALA 220 199 199 ALA ALA C . n 
C 2 221 ILE 221 200 200 ILE ILE C . n 
C 2 222 HIS 222 201 201 HIS HIS C . n 
C 2 223 GLY 223 202 202 GLY GLY C . n 
C 2 224 VAL 224 203 203 VAL VAL C . n 
C 2 225 TYR 225 204 204 TYR TYR C . n 
C 2 226 VAL 226 205 205 VAL VAL C . n 
C 2 227 GLY 227 206 206 GLY GLY C . n 
C 2 228 LEU 228 207 207 LEU LEU C . n 
C 2 229 LEU 229 208 208 LEU LEU C . n 
C 2 230 ALA 230 209 209 ALA ALA C . n 
C 2 231 GLN 231 210 210 GLN GLN C . n 
C 2 232 GLU 232 211 211 GLU GLU C . n 
C 2 233 ILE 233 212 212 ILE ILE C . n 
C 2 234 TYR 234 213 213 TYR TYR C . n 
C 2 235 ASN 235 214 214 ASN ASN C . n 
C 2 236 LYS 236 215 215 LYS LYS C . n 
C 2 237 GLN 237 216 216 GLN GLN C . n 
C 2 238 THR 238 217 217 THR THR C . n 
C 2 239 GLU 239 218 218 GLU GLU C . n 
C 2 240 GLU 240 219 219 GLU GLU C . n 
C 2 241 LYS 241 220 220 LYS LYS C . n 
C 2 242 LYS 242 221 221 LYS LYS C . n 
C 2 243 ALA 243 222 222 ALA ALA C . n 
C 2 244 GLU 244 223 223 GLU GLU C . n 
C 2 245 LEU 245 224 224 LEU LEU C . n 
C 2 246 ARG 246 225 225 ARG ARG C . n 
C 2 247 GLU 247 226 226 GLU GLU C . n 
C 2 248 PHE 248 227 227 PHE PHE C . n 
C 2 249 ALA 249 228 228 ALA ALA C . n 
C 2 250 ILE 250 229 229 ILE ILE C . n 
C 2 251 ASP 251 230 230 ASP ASP C . n 
C 2 252 LEU 252 231 231 LEU LEU C . n 
C 2 253 LEU 253 232 232 LEU LEU C . n 
C 2 254 ASN 254 233 233 ASN ASN C . n 
C 2 255 GLN 255 234 234 GLN GLN C . n 
C 2 256 LEU 256 235 235 LEU LEU C . n 
C 2 257 TYR 257 236 236 TYR TYR C . n 
C 2 258 GLU 258 237 237 GLU GLU C . n 
C 2 259 ASN 259 238 238 ASN ASN C . n 
C 2 260 GLU 260 239 239 GLU GLU C . n 
C 2 261 LEU 261 240 240 LEU LEU C . n 
C 2 262 GLU 262 241 241 GLU GLU C . n 
C 2 263 TYR 263 242 242 TYR TYR C . n 
C 2 264 THR 264 243 243 THR THR C . n 
C 2 265 GLU 265 244 244 GLU GLU C . n 
C 2 266 ASP 266 245 245 ASP ASP C . n 
C 2 267 LEU 267 246 246 LEU LEU C . n 
C 2 268 TYR 268 247 247 TYR TYR C . n 
C 2 269 ASP 269 248 248 ASP ASP C . n 
C 2 270 GLN 270 249 249 GLN GLN C . n 
C 2 271 VAL 271 250 250 VAL VAL C . n 
C 2 272 GLY 272 251 251 GLY GLY C . n 
C 2 273 LEU 273 252 252 LEU LEU C . n 
C 2 274 SER 274 253 253 SER SER C . n 
C 2 275 HIS 275 254 254 HIS HIS C . n 
C 2 276 ASP 276 255 255 ASP ASP C . n 
C 2 277 VAL 277 256 256 VAL VAL C . n 
C 2 278 LYS 278 257 257 LYS LYS C . n 
C 2 279 LYS 279 258 258 LYS LYS C . n 
C 2 280 PHE 280 259 259 PHE PHE C . n 
C 2 281 ILE 281 260 260 ILE ILE C . n 
C 2 282 ARG 282 261 261 ARG ARG C . n 
C 2 283 TYR 283 262 262 TYR TYR C . n 
C 2 284 ASN 284 263 263 ASN ASN C . n 
C 2 285 ALA 285 264 264 ALA ALA C . n 
C 2 286 ASN 286 265 265 ASN ASN C . n 
C 2 287 LYS 287 266 266 LYS LYS C . n 
C 2 288 ALA 288 267 267 ALA ALA C . n 
C 2 289 LEU 289 268 268 LEU LEU C . n 
C 2 290 MET 290 269 269 MET MET C . n 
C 2 291 ASN 291 270 270 ASN ASN C . n 
C 2 292 LEU 292 271 271 LEU LEU C . n 
C 2 293 GLY 293 272 272 GLY GLY C . n 
C 2 294 PHE 294 273 273 PHE PHE C . n 
C 2 295 ASP 295 274 274 ASP ASP C . n 
C 2 296 PRO 296 275 275 PRO PRO C . n 
C 2 297 TYR 297 276 276 TYR TYR C . n 
C 2 298 PHE 298 277 277 PHE PHE C . n 
C 2 299 GLU 299 278 278 GLU GLU C . n 
C 2 300 GLU 300 279 279 GLU GLU C . n 
C 2 301 GLU 301 280 280 GLU GLU C . n 
C 2 302 ASP 302 281 281 ASP ASP C . n 
C 2 303 ILE 303 282 282 ILE ILE C . n 
C 2 304 ASN 304 283 283 ASN ASN C . n 
C 2 305 PRO 305 284 284 PRO PRO C . n 
C 2 306 ILE 306 285 285 ILE ILE C . n 
C 2 307 VAL 307 286 286 VAL VAL C . n 
C 2 308 LEU 308 287 287 LEU LEU C . n 
C 2 309 ASN 309 288 288 ASN ASN C . n 
C 2 310 GLY 310 289 289 GLY GLY C . n 
C 2 311 LEU 311 290 290 LEU LEU C . n 
C 2 312 ASN 312 291 ?   ?   ?   C . n 
C 2 313 THR 313 292 ?   ?   ?   C . n 
C 2 314 LYS 314 293 ?   ?   ?   C . n 
C 2 315 THR 315 294 ?   ?   ?   C . n 
C 2 316 LYS 316 295 ?   ?   ?   C . n 
C 2 317 SER 317 296 ?   ?   ?   C . n 
C 2 318 HIS 318 297 ?   ?   ?   C . n 
C 2 319 ASP 319 298 ?   ?   ?   C . n 
C 2 320 PHE 320 299 ?   ?   ?   C . n 
C 2 321 PHE 321 300 ?   ?   ?   C . n 
C 2 322 SER 322 301 ?   ?   ?   C . n 
C 2 323 MET 323 302 ?   ?   ?   C . n 
C 2 324 LYS 324 303 ?   ?   ?   C . n 
C 2 325 GLY 325 304 ?   ?   ?   C . n 
C 2 326 ASN 326 305 ?   ?   ?   C . n 
C 2 327 GLY 327 306 ?   ?   ?   C . n 
C 2 328 TYR 328 307 ?   ?   ?   C . n 
C 2 329 LYS 329 308 ?   ?   ?   C . n 
C 2 330 LYS 330 309 309 LYS LYS C . n 
C 2 331 ALA 331 310 310 ALA ALA C . n 
C 2 332 THR 332 311 311 THR THR C . n 
C 2 333 VAL 333 312 312 VAL VAL C . n 
C 2 334 GLU 334 313 313 GLU GLU C . n 
C 2 335 PRO 335 314 314 PRO PRO C . n 
C 2 336 LEU 336 315 315 LEU LEU C . n 
C 2 337 LYS 337 316 316 LYS LYS C . n 
C 2 338 ASP 338 317 317 ASP ASP C . n 
C 2 339 ASP 339 318 318 ASP ASP C . n 
C 2 340 ASP 340 319 319 ASP ASP C . n 
C 2 341 PHE 341 320 320 PHE PHE C . n 
C 2 342 TYR 342 321 321 TYR TYR C . n 
C 2 343 PHE 343 322 322 PHE PHE C . n 
C 2 344 GLU 344 323 ?   ?   ?   C . n 
C 2 345 ASP 345 324 ?   ?   ?   C . n 
C 2 346 GLU 346 325 ?   ?   ?   C . n 
C 2 347 LYS 347 326 ?   ?   ?   C . n 
C 2 348 GLU 348 327 ?   ?   ?   C . n 
C 2 349 GLN 349 328 ?   ?   ?   C . n 
C 2 350 ILE 350 329 ?   ?   ?   C . n 
D 2 1   MET 1   -20 ?   ?   ?   D . n 
D 2 2   GLY 2   -19 ?   ?   ?   D . n 
D 2 3   SER 3   -18 ?   ?   ?   D . n 
D 2 4   SER 4   -17 ?   ?   ?   D . n 
D 2 5   HIS 5   -16 ?   ?   ?   D . n 
D 2 6   HIS 6   -15 ?   ?   ?   D . n 
D 2 7   HIS 7   -14 ?   ?   ?   D . n 
D 2 8   HIS 8   -13 ?   ?   ?   D . n 
D 2 9   HIS 9   -12 ?   ?   ?   D . n 
D 2 10  HIS 10  -11 ?   ?   ?   D . n 
D 2 11  SER 11  -10 ?   ?   ?   D . n 
D 2 12  SER 12  -9  ?   ?   ?   D . n 
D 2 13  GLY 13  -8  ?   ?   ?   D . n 
D 2 14  LEU 14  -7  ?   ?   ?   D . n 
D 2 15  VAL 15  -6  ?   ?   ?   D . n 
D 2 16  PRO 16  -5  ?   ?   ?   D . n 
D 2 17  ARG 17  -4  ?   ?   ?   D . n 
D 2 18  GLY 18  -3  ?   ?   ?   D . n 
D 2 19  SER 19  -2  ?   ?   ?   D . n 
D 2 20  HIS 20  -1  ?   ?   ?   D . n 
D 2 21  MET 21  0   ?   ?   ?   D . n 
D 2 22  MET 22  1   ?   ?   ?   D . n 
D 2 23  THR 23  2   ?   ?   ?   D . n 
D 2 24  LYS 24  3   ?   ?   ?   D . n 
D 2 25  ILE 25  4   ?   ?   ?   D . n 
D 2 26  TYR 26  5   ?   ?   ?   D . n 
D 2 27  ASP 27  6   ?   ?   ?   D . n 
D 2 28  ALA 28  7   ?   ?   ?   D . n 
D 2 29  ALA 29  8   ?   ?   ?   D . n 
D 2 30  ASN 30  9   ?   ?   ?   D . n 
D 2 31  TRP 31  10  ?   ?   ?   D . n 
D 2 32  SER 32  11  ?   ?   ?   D . n 
D 2 33  LYS 33  12  ?   ?   ?   D . n 
D 2 34  HIS 34  13  ?   ?   ?   D . n 
D 2 35  GLU 35  14  ?   ?   ?   D . n 
D 2 36  ASP 36  15  ?   ?   ?   D . n 
D 2 37  ASP 37  16  16  ASP ASP D . n 
D 2 38  PHE 38  17  17  PHE PHE D . n 
D 2 39  THR 39  18  18  THR THR D . n 
D 2 40  GLN 40  19  19  GLN GLN D . n 
D 2 41  MET 41  20  20  MET MET D . n 
D 2 42  PHE 42  21  21  PHE PHE D . n 
D 2 43  TYR 43  22  22  TYR TYR D . n 
D 2 44  ASN 44  23  23  ASN ASN D . n 
D 2 45  GLN 45  24  24  GLN GLN D . n 
D 2 46  ASN 46  25  25  ASN ASN D . n 
D 2 47  VAL 47  26  26  VAL VAL D . n 
D 2 48  LYS 48  27  27  LYS LYS D . n 
D 2 49  GLN 49  28  28  GLN GLN D . n 
D 2 50  PHE 50  29  29  PHE PHE D . n 
D 2 51  TRP 51  30  30  TRP TRP D . n 
D 2 52  LEU 52  31  31  LEU LEU D . n 
D 2 53  PRO 53  32  32  PRO PRO D . n 
D 2 54  GLU 54  33  33  GLU GLU D . n 
D 2 55  GLU 55  34  34  GLU GLU D . n 
D 2 56  ILE 56  35  35  ILE ILE D . n 
D 2 57  ALA 57  36  36  ALA ALA D . n 
D 2 58  LEU 58  37  37  LEU LEU D . n 
D 2 59  ASN 59  38  38  ASN ASN D . n 
D 2 60  GLY 60  39  39  GLY GLY D . n 
D 2 61  ASP 61  40  40  ASP ASP D . n 
D 2 62  LEU 62  41  41  LEU LEU D . n 
D 2 63  LEU 63  42  42  LEU LEU D . n 
D 2 64  THR 64  43  43  THR THR D . n 
D 2 65  TRP 65  44  44  TRP TRP D . n 
D 2 66  LYS 66  45  45  LYS LYS D . n 
D 2 67  TYR 67  46  46  TYR TYR D . n 
D 2 68  LEU 68  47  47  LEU LEU D . n 
D 2 69  GLY 69  48  48  GLY GLY D . n 
D 2 70  LYS 70  49  49  LYS LYS D . n 
D 2 71  ASN 71  50  50  ASN ASN D . n 
D 2 72  GLU 72  51  51  GLU GLU D . n 
D 2 73  GLN 73  52  52  GLN GLN D . n 
D 2 74  ASP 74  53  53  ASP ASP D . n 
D 2 75  THR 75  54  54  THR THR D . n 
D 2 76  TYR 76  55  55  TYR TYR D . n 
D 2 77  MET 77  56  56  MET MET D . n 
D 2 78  LYS 78  57  57  LYS LYS D . n 
D 2 79  VAL 79  58  58  VAL VAL D . n 
D 2 80  LEU 80  59  59  LEU LEU D . n 
D 2 81  ALA 81  60  60  ALA ALA D . n 
D 2 82  GLY 82  61  61  GLY GLY D . n 
D 2 83  LEU 83  62  62  LEU LEU D . n 
D 2 84  THR 84  63  63  THR THR D . n 
D 2 85  LEU 85  64  64  LEU LEU D . n 
D 2 86  LEU 86  65  65  LEU LEU D . n 
D 2 87  ASP 87  66  66  ASP ASP D . n 
D 2 88  THR 88  67  67  THR THR D . n 
D 2 89  GLU 89  68  68  GLU GLU D . n 
D 2 90  GLN 90  69  69  GLN GLN D . n 
D 2 91  GLY 91  70  70  GLY GLY D . n 
D 2 92  ASN 92  71  71  ASN ASN D . n 
D 2 93  THR 93  72  72  THR THR D . n 
D 2 94  GLY 94  73  73  GLY GLY D . n 
D 2 95  MET 95  74  74  MET MET D . n 
D 2 96  PRO 96  75  75  PRO PRO D . n 
D 2 97  ILE 97  76  76  ILE ILE D . n 
D 2 98  VAL 98  77  77  VAL VAL D . n 
D 2 99  ALA 99  78  78  ALA ALA D . n 
D 2 100 GLU 100 79  79  GLU GLU D . n 
D 2 101 HIS 101 80  80  HIS HIS D . n 
D 2 102 VAL 102 81  81  VAL VAL D . n 
D 2 103 ASP 103 82  82  ASP ASP D . n 
D 2 104 GLY 104 83  83  GLY GLY D . n 
D 2 105 HIS 105 84  84  HIS HIS D . n 
D 2 106 GLN 106 85  85  GLN GLN D . n 
D 2 107 ARG 107 86  86  ARG ARG D . n 
D 2 108 LYS 108 87  87  LYS LYS D . n 
D 2 109 ALA 109 88  88  ALA ALA D . n 
D 2 110 VAL 110 89  89  VAL VAL D . n 
D 2 111 LEU 111 90  90  LEU LEU D . n 
D 2 112 ASN 112 91  91  ASN ASN D . n 
D 2 113 PHE 113 92  92  PHE PHE D . n 
D 2 114 MET 114 93  93  MET MET D . n 
D 2 115 ALA 115 94  94  ALA ALA D . n 
D 2 116 MET 116 95  95  MET MET D . n 
D 2 117 MET 117 96  96  MET MET D . n 
D 2 118 GLU 118 97  97  GLU GLU D . n 
D 2 119 ASN 119 98  98  ASN ASN D . n 
D 2 120 ALA 120 99  99  ALA ALA D . n 
D 2 121 VAL 121 100 100 VAL VAL D . n 
D 2 122 HIS 122 101 101 HIS HIS D . n 
D 2 123 ALA 123 102 102 ALA ALA D . n 
D 2 124 LYS 124 103 103 LYS LYS D . n 
D 2 125 SER 125 104 104 SER SER D . n 
D 2 126 TYR 126 105 105 TYR TYR D . n 
D 2 127 SER 127 106 106 SER SER D . n 
D 2 128 ASN 128 107 107 ASN ASN D . n 
D 2 129 ILE 129 108 108 ILE ILE D . n 
D 2 130 PHE 130 109 109 PHE PHE D . n 
D 2 131 MET 131 110 110 MET MET D . n 
D 2 132 THR 132 111 111 THR THR D . n 
D 2 133 LEU 133 112 112 LEU LEU D . n 
D 2 134 ALA 134 113 113 ALA ALA D . n 
D 2 135 PRO 135 114 114 PRO PRO D . n 
D 2 136 THR 136 115 115 THR THR D . n 
D 2 137 GLU 137 116 116 GLU GLU D . n 
D 2 138 THR 138 117 117 THR THR D . n 
D 2 139 ILE 139 118 118 ILE ILE D . n 
D 2 140 ASN 140 119 119 ASN ASN D . n 
D 2 141 GLU 141 120 120 GLU GLU D . n 
D 2 142 VAL 142 121 121 VAL VAL D . n 
D 2 143 PHE 143 122 122 PHE PHE D . n 
D 2 144 GLU 144 123 123 GLU GLU D . n 
D 2 145 TRP 145 124 124 TRP TRP D . n 
D 2 146 VAL 146 125 125 VAL VAL D . n 
D 2 147 LYS 147 126 126 LYS LYS D . n 
D 2 148 GLN 148 127 127 GLN GLN D . n 
D 2 149 ASN 149 128 128 ASN ASN D . n 
D 2 150 LYS 150 129 129 LYS LYS D . n 
D 2 151 TYR 151 130 130 TYR TYR D . n 
D 2 152 LEU 152 131 131 LEU LEU D . n 
D 2 153 GLN 153 132 132 GLN GLN D . n 
D 2 154 LYS 154 133 133 LYS LYS D . n 
D 2 155 LYS 155 134 134 LYS LYS D . n 
D 2 156 ALA 156 135 135 ALA ALA D . n 
D 2 157 GLN 157 136 136 GLN GLN D . n 
D 2 158 MET 158 137 137 MET MET D . n 
D 2 159 ILE 159 138 138 ILE ILE D . n 
D 2 160 VAL 160 139 139 VAL VAL D . n 
D 2 161 GLY 161 140 140 GLY GLY D . n 
D 2 162 LEU 162 141 141 LEU LEU D . n 
D 2 163 TYR 163 142 142 TYR TYR D . n 
D 2 164 LYS 164 143 143 LYS LYS D . n 
D 2 165 ALA 165 144 144 ALA ALA D . n 
D 2 166 ILE 166 145 145 ILE ILE D . n 
D 2 167 GLN 167 146 146 GLN GLN D . n 
D 2 168 LYS 168 147 147 LYS LYS D . n 
D 2 169 ASP 169 148 148 ASP ASP D . n 
D 2 170 ASP 170 149 149 ASP ASP D . n 
D 2 171 GLU 171 150 150 GLU GLU D . n 
D 2 172 ILE 172 151 151 ILE ILE D . n 
D 2 173 SER 173 152 152 SER SER D . n 
D 2 174 LEU 174 153 153 LEU LEU D . n 
D 2 175 PHE 175 154 154 PHE PHE D . n 
D 2 176 LYS 176 155 155 LYS LYS D . n 
D 2 177 ALA 177 156 156 ALA ALA D . n 
D 2 178 MET 178 157 157 MET MET D . n 
D 2 179 VAL 179 158 158 VAL VAL D . n 
D 2 180 ALA 180 159 159 ALA ALA D . n 
D 2 181 SER 181 160 160 SER SER D . n 
D 2 182 VAL 182 161 161 VAL VAL D . n 
D 2 183 TYR 183 162 162 TYR TYR D . n 
D 2 184 LEU 184 163 163 LEU LEU D . n 
D 2 185 GLU 185 164 164 GLU GLU D . n 
D 2 186 SER 186 165 165 SER SER D . n 
D 2 187 PHE 187 166 166 PHE PHE D . n 
D 2 188 LEU 188 167 167 LEU LEU D . n 
D 2 189 PHE 189 168 168 PHE PHE D . n 
D 2 190 TYR 190 169 169 TYR TYR D . n 
D 2 191 SER 191 170 170 SER SER D . n 
D 2 192 GLY 192 171 171 GLY GLY D . n 
D 2 193 PHE 193 172 172 PHE PHE D . n 
D 2 194 TYR 194 173 173 TYR TYR D . n 
D 2 195 TYR 195 174 174 TYR TYR D . n 
D 2 196 PRO 196 175 175 PRO PRO D . n 
D 2 197 LEU 197 176 176 LEU LEU D . n 
D 2 198 TYR 198 177 177 TYR TYR D . n 
D 2 199 PHE 199 178 178 PHE PHE D . n 
D 2 200 TYR 200 179 179 TYR TYR D . n 
D 2 201 GLY 201 180 180 GLY GLY D . n 
D 2 202 GLN 202 181 181 GLN GLN D . n 
D 2 203 GLY 203 182 182 GLY GLY D . n 
D 2 204 LYS 204 183 183 LYS LYS D . n 
D 2 205 LEU 205 184 184 LEU LEU D . n 
D 2 206 MET 206 185 185 MET MET D . n 
D 2 207 GLN 207 186 186 GLN GLN D . n 
D 2 208 SER 208 187 187 SER SER D . n 
D 2 209 GLY 209 188 188 GLY GLY D . n 
D 2 210 GLU 210 189 189 GLU GLU D . n 
D 2 211 ILE 211 190 190 ILE ILE D . n 
D 2 212 ILE 212 191 191 ILE ILE D . n 
D 2 213 ASN 213 192 192 ASN ASN D . n 
D 2 214 LEU 214 193 193 LEU LEU D . n 
D 2 215 ILE 215 194 194 ILE ILE D . n 
D 2 216 LEU 216 195 195 LEU LEU D . n 
D 2 217 ARG 217 196 196 ARG ARG D . n 
D 2 218 ASP 218 197 197 ASP ASP D . n 
D 2 219 GLU 219 198 198 GLU GLU D . n 
D 2 220 ALA 220 199 199 ALA ALA D . n 
D 2 221 ILE 221 200 200 ILE ILE D . n 
D 2 222 HIS 222 201 201 HIS HIS D . n 
D 2 223 GLY 223 202 202 GLY GLY D . n 
D 2 224 VAL 224 203 203 VAL VAL D . n 
D 2 225 TYR 225 204 204 TYR TYR D . n 
D 2 226 VAL 226 205 205 VAL VAL D . n 
D 2 227 GLY 227 206 206 GLY GLY D . n 
D 2 228 LEU 228 207 207 LEU LEU D . n 
D 2 229 LEU 229 208 208 LEU LEU D . n 
D 2 230 ALA 230 209 209 ALA ALA D . n 
D 2 231 GLN 231 210 210 GLN GLN D . n 
D 2 232 GLU 232 211 211 GLU GLU D . n 
D 2 233 ILE 233 212 212 ILE ILE D . n 
D 2 234 TYR 234 213 213 TYR TYR D . n 
D 2 235 ASN 235 214 214 ASN ASN D . n 
D 2 236 LYS 236 215 215 LYS LYS D . n 
D 2 237 GLN 237 216 216 GLN GLN D . n 
D 2 238 THR 238 217 217 THR THR D . n 
D 2 239 GLU 239 218 218 GLU GLU D . n 
D 2 240 GLU 240 219 219 GLU GLU D . n 
D 2 241 LYS 241 220 220 LYS LYS D . n 
D 2 242 LYS 242 221 221 LYS LYS D . n 
D 2 243 ALA 243 222 222 ALA ALA D . n 
D 2 244 GLU 244 223 223 GLU GLU D . n 
D 2 245 LEU 245 224 224 LEU LEU D . n 
D 2 246 ARG 246 225 225 ARG ARG D . n 
D 2 247 GLU 247 226 226 GLU GLU D . n 
D 2 248 PHE 248 227 227 PHE PHE D . n 
D 2 249 ALA 249 228 228 ALA ALA D . n 
D 2 250 ILE 250 229 229 ILE ILE D . n 
D 2 251 ASP 251 230 230 ASP ASP D . n 
D 2 252 LEU 252 231 231 LEU LEU D . n 
D 2 253 LEU 253 232 232 LEU LEU D . n 
D 2 254 ASN 254 233 233 ASN ASN D . n 
D 2 255 GLN 255 234 234 GLN GLN D . n 
D 2 256 LEU 256 235 235 LEU LEU D . n 
D 2 257 TYR 257 236 236 TYR TYR D . n 
D 2 258 GLU 258 237 237 GLU GLU D . n 
D 2 259 ASN 259 238 238 ASN ASN D . n 
D 2 260 GLU 260 239 239 GLU GLU D . n 
D 2 261 LEU 261 240 240 LEU LEU D . n 
D 2 262 GLU 262 241 241 GLU GLU D . n 
D 2 263 TYR 263 242 242 TYR TYR D . n 
D 2 264 THR 264 243 243 THR THR D . n 
D 2 265 GLU 265 244 244 GLU GLU D . n 
D 2 266 ASP 266 245 245 ASP ASP D . n 
D 2 267 LEU 267 246 246 LEU LEU D . n 
D 2 268 TYR 268 247 247 TYR TYR D . n 
D 2 269 ASP 269 248 248 ASP ASP D . n 
D 2 270 GLN 270 249 249 GLN GLN D . n 
D 2 271 VAL 271 250 250 VAL VAL D . n 
D 2 272 GLY 272 251 251 GLY GLY D . n 
D 2 273 LEU 273 252 252 LEU LEU D . n 
D 2 274 SER 274 253 253 SER SER D . n 
D 2 275 HIS 275 254 254 HIS HIS D . n 
D 2 276 ASP 276 255 255 ASP ASP D . n 
D 2 277 VAL 277 256 256 VAL VAL D . n 
D 2 278 LYS 278 257 257 LYS LYS D . n 
D 2 279 LYS 279 258 258 LYS LYS D . n 
D 2 280 PHE 280 259 259 PHE PHE D . n 
D 2 281 ILE 281 260 260 ILE ILE D . n 
D 2 282 ARG 282 261 261 ARG ARG D . n 
D 2 283 TYR 283 262 262 TYR TYR D . n 
D 2 284 ASN 284 263 263 ASN ASN D . n 
D 2 285 ALA 285 264 264 ALA ALA D . n 
D 2 286 ASN 286 265 265 ASN ASN D . n 
D 2 287 LYS 287 266 266 LYS LYS D . n 
D 2 288 ALA 288 267 267 ALA ALA D . n 
D 2 289 LEU 289 268 268 LEU LEU D . n 
D 2 290 MET 290 269 269 MET MET D . n 
D 2 291 ASN 291 270 270 ASN ASN D . n 
D 2 292 LEU 292 271 271 LEU LEU D . n 
D 2 293 GLY 293 272 272 GLY GLY D . n 
D 2 294 PHE 294 273 273 PHE PHE D . n 
D 2 295 ASP 295 274 274 ASP ASP D . n 
D 2 296 PRO 296 275 275 PRO PRO D . n 
D 2 297 TYR 297 276 276 TYR TYR D . n 
D 2 298 PHE 298 277 277 PHE PHE D . n 
D 2 299 GLU 299 278 278 GLU GLU D . n 
D 2 300 GLU 300 279 279 GLU GLU D . n 
D 2 301 GLU 301 280 280 GLU GLU D . n 
D 2 302 ASP 302 281 281 ASP ASP D . n 
D 2 303 ILE 303 282 282 ILE ILE D . n 
D 2 304 ASN 304 283 283 ASN ASN D . n 
D 2 305 PRO 305 284 284 PRO PRO D . n 
D 2 306 ILE 306 285 285 ILE ILE D . n 
D 2 307 VAL 307 286 286 VAL VAL D . n 
D 2 308 LEU 308 287 287 LEU LEU D . n 
D 2 309 ASN 309 288 288 ASN ASN D . n 
D 2 310 GLY 310 289 289 GLY GLY D . n 
D 2 311 LEU 311 290 290 LEU LEU D . n 
D 2 312 ASN 312 291 ?   ?   ?   D . n 
D 2 313 THR 313 292 ?   ?   ?   D . n 
D 2 314 LYS 314 293 ?   ?   ?   D . n 
D 2 315 THR 315 294 ?   ?   ?   D . n 
D 2 316 LYS 316 295 ?   ?   ?   D . n 
D 2 317 SER 317 296 ?   ?   ?   D . n 
D 2 318 HIS 318 297 ?   ?   ?   D . n 
D 2 319 ASP 319 298 ?   ?   ?   D . n 
D 2 320 PHE 320 299 ?   ?   ?   D . n 
D 2 321 PHE 321 300 ?   ?   ?   D . n 
D 2 322 SER 322 301 ?   ?   ?   D . n 
D 2 323 MET 323 302 ?   ?   ?   D . n 
D 2 324 LYS 324 303 ?   ?   ?   D . n 
D 2 325 GLY 325 304 ?   ?   ?   D . n 
D 2 326 ASN 326 305 ?   ?   ?   D . n 
D 2 327 GLY 327 306 ?   ?   ?   D . n 
D 2 328 TYR 328 307 ?   ?   ?   D . n 
D 2 329 LYS 329 308 ?   ?   ?   D . n 
D 2 330 LYS 330 309 309 LYS LYS D . n 
D 2 331 ALA 331 310 310 ALA ALA D . n 
D 2 332 THR 332 311 311 THR THR D . n 
D 2 333 VAL 333 312 312 VAL VAL D . n 
D 2 334 GLU 334 313 313 GLU GLU D . n 
D 2 335 PRO 335 314 314 PRO PRO D . n 
D 2 336 LEU 336 315 315 LEU LEU D . n 
D 2 337 LYS 337 316 316 LYS LYS D . n 
D 2 338 ASP 338 317 317 ASP ASP D . n 
D 2 339 ASP 339 318 318 ASP ASP D . n 
D 2 340 ASP 340 319 319 ASP ASP D . n 
D 2 341 PHE 341 320 320 PHE PHE D . n 
D 2 342 TYR 342 321 321 TYR TYR D . n 
D 2 343 PHE 343 322 322 PHE PHE D . n 
D 2 344 GLU 344 323 ?   ?   ?   D . n 
D 2 345 ASP 345 324 ?   ?   ?   D . n 
D 2 346 GLU 346 325 ?   ?   ?   D . n 
D 2 347 LYS 347 326 ?   ?   ?   D . n 
D 2 348 GLU 348 327 ?   ?   ?   D . n 
D 2 349 GLN 349 328 ?   ?   ?   D . n 
D 2 350 ILE 350 329 ?   ?   ?   D . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 DGI ? ? DGI ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
4 MN  ? ? MN  ? ? 'SUBJECT OF INVESTIGATION' ? 
5 TTP ? ? TTP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 TTP 1 801 801 TTP TTP A . 
F 4 MG  1 802 802 MG  MG  A . 
G 5 ATP 1 803 803 ATP ATP A . 
H 6 DGI 1 804 804 DGI DGI A . 
I 3 TTP 1 801 801 TTP TTP B . 
J 4 MG  1 802 802 MG  MG  B . 
K 5 ATP 1 803 803 ATP ATP B . 
L 6 DGI 1 804 804 DGI DGI B . 
M 7 MN  1 401 401 MN  MN  C . 
N 7 MN  1 402 402 MN  MN  C . 
O 7 MN  1 401 401 MN  MN  D . 
P 7 MN  1 402 402 MN  MN  D . 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BY8 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BY8 
_struct.title                        'Class 9 model for product condition of Bacillus subtilis ribonucleotide reductase complex' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BY8 
_struct_keywords.text            'Ribonucleotide Reductase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 6 ? 
M N N 7 ? 
N N N 7 ? 
O N N 7 ? 
P N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP RIR1_BACSU P50620 ? 1 
;MSQNQVPKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVFFHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEV
FKTAYAKKFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVALFFANGDTEKAKEYVNLMINQEYQPSTPTFLNAG
RKRRGELVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKLRAKGEAIKDVENATKGVVGVMKLLDNAFRYADQM
GQRQGSGAAYLNIFHRDINDFLDTKKISADEDVRVKTLSIGVVIPDKFVELAREDKAAYVFYPHTIYKEYGQHMDEMDMN
EMYDKFVDNPRVKKEKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNHISKVKFSNLCSEVLQASQVSSYTDYDEE
DEIGLDISCNLGSLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRANKAMKSIGLGAMNLHGYLAQNGIAYE
SPEARDFANTFFMMVNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYVSTDFSPKYEKIANLFEGMHIPTTEDWKK
LKAFVAEHGMYHSYRLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYPMPGLASNNWFFYKEAYDMDMFKVVDM
IATIQQHIDQGISFTLFLKDTMTTRDLNRIDLYAHHRGIKTIYYARTKDTGQDSCLSCVV
;
1 
2 UNP RIR2_BACSU P50621 ? 2 
;MTKIYDAANWSKHEDDFTQMFYNQNVKQFWLPEEIALNGDLLTWKYLGKNEQDTYMKVLAGLTLLDTEQGNTGMPIVAEH
VDGHQRKAVLNFMAMMENAVHAKSYSNIFMTLAPTETINEVFEWVKQNKYLQKKAQMIVGLYKAIQKDDEISLFKAMVAS
VYLESFLFYSGFYYPLYFYGQGKLMQSGEIINLILRDEAIHGVYVGLLAQEIYNKQTEEKKAELREFAIDLLNQLYENEL
EYTEDLYDQVGLSHDVKKFIRYNANKALMNLGFDPYFEEEDINPIVLNGLNTKTKSHDFFSMKGNGYKKATVEPLKDDDF
YFEDEKEQI
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9BY8 A 1  ? 700 ? P50620 1 ? 700 ? 1 700 
2 1 9BY8 B 1  ? 700 ? P50620 1 ? 700 ? 1 700 
3 2 9BY8 C 22 ? 350 ? P50621 1 ? 329 ? 1 329 
4 2 9BY8 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 9BY8 MET C 1  ? UNP P50621 ? ? 'initiating methionine' -20 1  
3 9BY8 GLY C 2  ? UNP P50621 ? ? 'expression tag'        -19 2  
3 9BY8 SER C 3  ? UNP P50621 ? ? 'expression tag'        -18 3  
3 9BY8 SER C 4  ? UNP P50621 ? ? 'expression tag'        -17 4  
3 9BY8 HIS C 5  ? UNP P50621 ? ? 'expression tag'        -16 5  
3 9BY8 HIS C 6  ? UNP P50621 ? ? 'expression tag'        -15 6  
3 9BY8 HIS C 7  ? UNP P50621 ? ? 'expression tag'        -14 7  
3 9BY8 HIS C 8  ? UNP P50621 ? ? 'expression tag'        -13 8  
3 9BY8 HIS C 9  ? UNP P50621 ? ? 'expression tag'        -12 9  
3 9BY8 HIS C 10 ? UNP P50621 ? ? 'expression tag'        -11 10 
3 9BY8 SER C 11 ? UNP P50621 ? ? 'expression tag'        -10 11 
3 9BY8 SER C 12 ? UNP P50621 ? ? 'expression tag'        -9  12 
3 9BY8 GLY C 13 ? UNP P50621 ? ? 'expression tag'        -8  13 
3 9BY8 LEU C 14 ? UNP P50621 ? ? 'expression tag'        -7  14 
3 9BY8 VAL C 15 ? UNP P50621 ? ? 'expression tag'        -6  15 
3 9BY8 PRO C 16 ? UNP P50621 ? ? 'expression tag'        -5  16 
3 9BY8 ARG C 17 ? UNP P50621 ? ? 'expression tag'        -4  17 
3 9BY8 GLY C 18 ? UNP P50621 ? ? 'expression tag'        -3  18 
3 9BY8 SER C 19 ? UNP P50621 ? ? 'expression tag'        -2  19 
3 9BY8 HIS C 20 ? UNP P50621 ? ? 'expression tag'        -1  20 
3 9BY8 MET C 21 ? UNP P50621 ? ? 'expression tag'        0   21 
4 9BY8 MET D 1  ? UNP P50621 ? ? 'initiating methionine' -20 22 
4 9BY8 GLY D 2  ? UNP P50621 ? ? 'expression tag'        -19 23 
4 9BY8 SER D 3  ? UNP P50621 ? ? 'expression tag'        -18 24 
4 9BY8 SER D 4  ? UNP P50621 ? ? 'expression tag'        -17 25 
4 9BY8 HIS D 5  ? UNP P50621 ? ? 'expression tag'        -16 26 
4 9BY8 HIS D 6  ? UNP P50621 ? ? 'expression tag'        -15 27 
4 9BY8 HIS D 7  ? UNP P50621 ? ? 'expression tag'        -14 28 
4 9BY8 HIS D 8  ? UNP P50621 ? ? 'expression tag'        -13 29 
4 9BY8 HIS D 9  ? UNP P50621 ? ? 'expression tag'        -12 30 
4 9BY8 HIS D 10 ? UNP P50621 ? ? 'expression tag'        -11 31 
4 9BY8 SER D 11 ? UNP P50621 ? ? 'expression tag'        -10 32 
4 9BY8 SER D 12 ? UNP P50621 ? ? 'expression tag'        -9  33 
4 9BY8 GLY D 13 ? UNP P50621 ? ? 'expression tag'        -8  34 
4 9BY8 LEU D 14 ? UNP P50621 ? ? 'expression tag'        -7  35 
4 9BY8 VAL D 15 ? UNP P50621 ? ? 'expression tag'        -6  36 
4 9BY8 PRO D 16 ? UNP P50621 ? ? 'expression tag'        -5  37 
4 9BY8 ARG D 17 ? UNP P50621 ? ? 'expression tag'        -4  38 
4 9BY8 GLY D 18 ? UNP P50621 ? ? 'expression tag'        -3  39 
4 9BY8 SER D 19 ? UNP P50621 ? ? 'expression tag'        -2  40 
4 9BY8 HIS D 20 ? UNP P50621 ? ? 'expression tag'        -1  41 
4 9BY8 MET D 21 ? UNP P50621 ? ? 'expression tag'        0   42 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 7   ? ASN A 14  ? PRO A 7   ASN A 14  1 ? 8  
HELX_P HELX_P2  AA2 GLU A 15  ? MET A 17  ? GLU A 15  MET A 17  5 ? 3  
HELX_P HELX_P3  AA3 ASP A 27  ? TYR A 40  ? ASP A 27  TYR A 40  1 ? 14 
HELX_P HELX_P4  AA4 TYR A 40  ? THR A 45  ? TYR A 40  THR A 45  1 ? 6  
HELX_P HELX_P5  AA5 ASN A 50  ? ASN A 61  ? ASN A 50  ASN A 61  1 ? 12 
HELX_P HELX_P6  AA6 GLU A 65  ? SER A 70  ? GLU A 65  SER A 70  1 ? 6  
HELX_P HELX_P7  AA7 SER A 73  ? LYS A 87  ? SER A 73  LYS A 87  1 ? 15 
HELX_P HELX_P8  AA8 SER A 93  ? TYR A 104 ? SER A 93  TYR A 104 1 ? 12 
HELX_P HELX_P9  AA9 ARG A 117 ? ASN A 131 ? ARG A 117 ASN A 131 1 ? 15 
HELX_P HELX_P10 AB1 ASP A 133 ? ASN A 146 ? ASP A 133 ASN A 146 1 ? 14 
HELX_P HELX_P11 AB2 SER A 152 ? ALA A 159 ? SER A 152 ALA A 159 1 ? 8  
HELX_P HELX_P12 AB3 SER A 178 ? LEU A 195 ? SER A 178 LEU A 195 1 ? 18 
HELX_P HELX_P13 AB4 GLY A 222 ? ALA A 237 ? GLY A 222 ALA A 237 1 ? 16 
HELX_P HELX_P14 AB5 ASP A 238 ? GLN A 242 ? ASP A 238 GLN A 242 5 ? 5  
HELX_P HELX_P15 AB6 ASP A 257 ? THR A 264 ? ASP A 257 THR A 264 1 ? 8  
HELX_P HELX_P16 AB7 PRO A 285 ? GLU A 294 ? PRO A 285 GLU A 294 1 ? 10 
HELX_P HELX_P17 AB8 TYR A 302 ? GLY A 311 ? TYR A 302 GLY A 311 1 ? 10 
HELX_P HELX_P18 AB9 HIS A 313 ? MET A 317 ? HIS A 313 MET A 317 5 ? 5  
HELX_P HELX_P19 AC1 ASP A 318 ? ASN A 329 ? ASP A 318 ASN A 329 1 ? 12 
HELX_P HELX_P20 AC2 ASN A 338 ? GLY A 354 ? ASN A 338 GLY A 354 1 ? 17 
HELX_P HELX_P21 AC3 GLN A 361 ? LYS A 366 ? GLN A 361 LYS A 366 1 ? 6  
HELX_P HELX_P22 AC4 ILE A 416 ? LYS A 423 ? ILE A 416 LYS A 423 1 ? 8  
HELX_P HELX_P23 AC5 SER A 424 ? THR A 443 ? SER A 424 THR A 443 1 ? 20 
HELX_P HELX_P24 AC6 ALA A 448 ? LYS A 459 ? ALA A 448 LYS A 459 1 ? 12 
HELX_P HELX_P25 AC7 ASN A 467 ? GLN A 474 ? ASN A 467 GLN A 474 1 ? 8  
HELX_P HELX_P26 AC8 SER A 481 ? GLY A 511 ? SER A 481 GLY A 511 1 ? 31 
HELX_P HELX_P27 AC9 SER A 520 ? GLY A 525 ? SER A 520 GLY A 525 1 ? 6  
HELX_P HELX_P28 AD1 PHE A 528 ? THR A 534 ? PHE A 528 THR A 534 1 ? 7  
HELX_P HELX_P29 AD2 TYR A 540 ? PHE A 547 ? TYR A 540 PHE A 547 1 ? 8  
HELX_P HELX_P30 AD3 THR A 554 ? GLY A 569 ? THR A 554 GLY A 569 1 ? 16 
HELX_P HELX_P31 AD4 SER A 583 ? GLN A 588 ? SER A 583 GLN A 588 1 ? 6  
HELX_P HELX_P32 AD5 GLU A 628 ? MET A 632 ? GLU A 628 MET A 632 5 ? 5  
HELX_P HELX_P33 AD6 ASP A 633 ? GLN A 646 ? ASP A 633 GLN A 646 1 ? 14 
HELX_P HELX_P34 AD7 THR A 663 ? ARG A 677 ? THR A 663 ARG A 677 1 ? 15 
HELX_P HELX_P35 AD8 PRO B 7   ? GLU B 15  ? PRO B 7   GLU B 15  1 ? 9  
HELX_P HELX_P36 AD9 ASP B 27  ? THR B 45  ? ASP B 27  THR B 45  1 ? 19 
HELX_P HELX_P37 AE1 ASN B 50  ? ASN B 61  ? ASN B 50  ASN B 61  1 ? 12 
HELX_P HELX_P38 AE2 GLU B 65  ? SER B 70  ? GLU B 65  SER B 70  1 ? 6  
HELX_P HELX_P39 AE3 SER B 73  ? LYS B 87  ? SER B 73  LYS B 87  1 ? 15 
HELX_P HELX_P40 AE4 SER B 93  ? TYR B 104 ? SER B 93  TYR B 104 1 ? 12 
HELX_P HELX_P41 AE5 ARG B 117 ? ASN B 131 ? ARG B 117 ASN B 131 1 ? 15 
HELX_P HELX_P42 AE6 ASP B 133 ? ASN B 146 ? ASP B 133 ASN B 146 1 ? 14 
HELX_P HELX_P43 AE7 SER B 152 ? ALA B 159 ? SER B 152 ALA B 159 1 ? 8  
HELX_P HELX_P44 AE8 SER B 178 ? LEU B 195 ? SER B 178 LEU B 195 1 ? 18 
HELX_P HELX_P45 AE9 GLY B 222 ? ALA B 237 ? GLY B 222 ALA B 237 1 ? 16 
HELX_P HELX_P46 AF1 ASP B 257 ? THR B 264 ? ASP B 257 THR B 264 1 ? 8  
HELX_P HELX_P47 AF2 PRO B 285 ? GLU B 294 ? PRO B 285 GLU B 294 1 ? 10 
HELX_P HELX_P48 AF3 TYR B 302 ? GLY B 311 ? TYR B 302 GLY B 311 1 ? 10 
HELX_P HELX_P49 AF4 HIS B 313 ? MET B 317 ? HIS B 313 MET B 317 5 ? 5  
HELX_P HELX_P50 AF5 ASP B 318 ? ASN B 329 ? ASP B 318 ASN B 329 1 ? 12 
HELX_P HELX_P51 AF6 ASN B 338 ? GLY B 354 ? ASN B 338 GLY B 354 1 ? 17 
HELX_P HELX_P52 AF7 GLN B 361 ? LYS B 366 ? GLN B 361 LYS B 366 1 ? 6  
HELX_P HELX_P53 AF8 ILE B 416 ? LYS B 423 ? ILE B 416 LYS B 423 1 ? 8  
HELX_P HELX_P54 AF9 SER B 424 ? THR B 443 ? SER B 424 THR B 443 1 ? 20 
HELX_P HELX_P55 AG1 ALA B 448 ? LYS B 459 ? ALA B 448 LYS B 459 1 ? 12 
HELX_P HELX_P56 AG2 ASN B 467 ? GLN B 474 ? ASN B 467 GLN B 474 1 ? 8  
HELX_P HELX_P57 AG3 SER B 481 ? GLY B 511 ? SER B 481 GLY B 511 1 ? 31 
HELX_P HELX_P58 AG4 SER B 520 ? GLY B 525 ? SER B 520 GLY B 525 1 ? 6  
HELX_P HELX_P59 AG5 PHE B 528 ? THR B 534 ? PHE B 528 THR B 534 1 ? 7  
HELX_P HELX_P60 AG6 TYR B 540 ? PHE B 547 ? TYR B 540 PHE B 547 1 ? 8  
HELX_P HELX_P61 AG7 THR B 554 ? GLY B 569 ? THR B 554 GLY B 569 1 ? 16 
HELX_P HELX_P62 AG8 SER B 583 ? GLN B 588 ? SER B 583 GLN B 588 1 ? 6  
HELX_P HELX_P63 AG9 ASP B 633 ? GLN B 646 ? ASP B 633 GLN B 646 1 ? 14 
HELX_P HELX_P64 AH1 THR B 663 ? ARG B 677 ? THR B 663 ARG B 677 1 ? 15 
HELX_P HELX_P65 AH2 PHE C 38  ? GLN C 49  ? PHE C 17  GLN C 28  1 ? 12 
HELX_P HELX_P66 AH3 LEU C 52  ? ILE C 56  ? LEU C 31  ILE C 35  5 ? 5  
HELX_P HELX_P67 AH4 LEU C 58  ? GLY C 60  ? LEU C 37  GLY C 39  5 ? 3  
HELX_P HELX_P68 AH5 ASP C 61  ? TYR C 67  ? ASP C 40  TYR C 46  1 ? 7  
HELX_P HELX_P69 AH6 GLY C 69  ? THR C 93  ? GLY C 48  THR C 72  1 ? 25 
HELX_P HELX_P70 AH7 THR C 93  ? VAL C 102 ? THR C 72  VAL C 81  1 ? 10 
HELX_P HELX_P71 AH8 GLY C 104 ? VAL C 121 ? GLY C 83  VAL C 100 1 ? 18 
HELX_P HELX_P72 AH9 VAL C 121 ? ALA C 134 ? VAL C 100 ALA C 113 1 ? 14 
HELX_P HELX_P73 AI1 PRO C 135 ? ASN C 149 ? PRO C 114 ASN C 128 1 ? 15 
HELX_P HELX_P74 AI2 ASN C 149 ? ALA C 165 ? ASN C 128 ALA C 144 1 ? 17 
HELX_P HELX_P75 AI3 ASP C 170 ? PHE C 187 ? ASP C 149 PHE C 166 1 ? 18 
HELX_P HELX_P76 AI4 PHE C 189 ? GLY C 201 ? PHE C 168 GLY C 180 1 ? 13 
HELX_P HELX_P77 AI5 LEU C 205 ? ASN C 235 ? LEU C 184 ASN C 214 1 ? 31 
HELX_P HELX_P78 AI6 THR C 238 ? ASP C 269 ? THR C 217 ASP C 248 1 ? 32 
HELX_P HELX_P79 AI7 GLN C 270 ? GLY C 272 ? GLN C 249 GLY C 251 5 ? 3  
HELX_P HELX_P80 AI8 LEU C 273 ? LEU C 292 ? LEU C 252 LEU C 271 1 ? 20 
HELX_P HELX_P81 AI9 ASN C 304 ? GLY C 310 ? ASN C 283 GLY C 289 1 ? 7  
HELX_P HELX_P82 AJ1 LYS C 337 ? TYR C 342 ? LYS C 316 TYR C 321 5 ? 6  
HELX_P HELX_P83 AJ2 PHE D 38  ? GLN D 49  ? PHE D 17  GLN D 28  1 ? 12 
HELX_P HELX_P84 AJ3 LEU D 52  ? ILE D 56  ? LEU D 31  ILE D 35  5 ? 5  
HELX_P HELX_P85 AJ4 LEU D 58  ? GLY D 60  ? LEU D 37  GLY D 39  5 ? 3  
HELX_P HELX_P86 AJ5 ASP D 61  ? LYS D 66  ? ASP D 40  LYS D 45  1 ? 6  
HELX_P HELX_P87 AJ6 GLY D 69  ? THR D 93  ? GLY D 48  THR D 72  1 ? 25 
HELX_P HELX_P88 AJ7 THR D 93  ? VAL D 102 ? THR D 72  VAL D 81  1 ? 10 
HELX_P HELX_P89 AJ8 GLY D 104 ? VAL D 121 ? GLY D 83  VAL D 100 1 ? 18 
HELX_P HELX_P90 AJ9 VAL D 121 ? ALA D 134 ? VAL D 100 ALA D 113 1 ? 14 
HELX_P HELX_P91 AK1 PRO D 135 ? ASN D 149 ? PRO D 114 ASN D 128 1 ? 15 
HELX_P HELX_P92 AK2 ASN D 149 ? ALA D 165 ? ASN D 128 ALA D 144 1 ? 17 
HELX_P HELX_P93 AK3 ASP D 170 ? PHE D 187 ? ASP D 149 PHE D 166 1 ? 18 
HELX_P HELX_P94 AK4 PHE D 189 ? GLY D 201 ? PHE D 168 GLY D 180 1 ? 13 
HELX_P HELX_P95 AK5 LEU D 205 ? ASN D 235 ? LEU D 184 ASN D 214 1 ? 31 
HELX_P HELX_P96 AK6 THR D 238 ? ASP D 269 ? THR D 217 ASP D 248 1 ? 32 
HELX_P HELX_P97 AK7 GLN D 270 ? GLY D 272 ? GLN D 249 GLY D 251 5 ? 3  
HELX_P HELX_P98 AK8 LEU D 273 ? LEU D 292 ? LEU D 252 LEU D 271 1 ? 20 
HELX_P HELX_P99 AK9 ASN D 304 ? LEU D 311 ? ASN D 283 LEU D 290 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? E TTP .   O2A ? ? ? 1_555 F MG . MG ? ? A TTP 801 A MG 802 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc2  metalc ? ? E TTP .   O2B ? ? ? 1_555 F MG . MG ? ? A TTP 801 A MG 802 1_555 ? ? ? ? ? ? ? 2.471 ? ? 
metalc3  metalc ? ? E TTP .   O1G ? ? ? 1_555 F MG . MG ? ? A TTP 801 A MG 802 1_555 ? ? ? ? ? ? ? 2.483 ? ? 
metalc4  metalc ? ? I TTP .   O2A ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc5  metalc ? ? I TTP .   O3G ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.104 ? ? 
metalc6  metalc ? ? C ASP 87  OD1 ? ? ? 1_555 N MN . MN ? ? C ASP 66  C MN 402 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc7  metalc ? ? C GLU 118 OE2 ? ? ? 1_555 M MN . MN ? ? C GLU 97  C MN 401 1_555 ? ? ? ? ? ? ? 1.961 ? ? 
metalc8  metalc ? ? C GLU 118 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 97  C MN 402 1_555 ? ? ? ? ? ? ? 2.112 ? ? 
metalc9  metalc ? ? C HIS 122 ND1 ? ? ? 1_555 N MN . MN ? ? C HIS 101 C MN 402 1_555 ? ? ? ? ? ? ? 2.177 ? ? 
metalc10 metalc ? ? C GLU 185 OE1 ? ? ? 1_555 M MN . MN ? ? C GLU 164 C MN 401 1_555 ? ? ? ? ? ? ? 2.129 ? ? 
metalc11 metalc ? ? C GLU 185 OE2 ? ? ? 1_555 M MN . MN ? ? C GLU 164 C MN 401 1_555 ? ? ? ? ? ? ? 1.964 ? ? 
metalc12 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 M MN . MN ? ? C GLU 198 C MN 401 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc13 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.711 ? ? 
metalc14 metalc ? ? C GLU 219 OE2 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
metalc15 metalc ? ? C HIS 222 ND1 ? ? ? 1_555 M MN . MN ? ? C HIS 201 C MN 401 1_555 ? ? ? ? ? ? ? 2.408 ? ? 
metalc16 metalc ? ? D ASP 87  OD1 ? ? ? 1_555 P MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc17 metalc ? ? D ASP 87  OD2 ? ? ? 1_555 P MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.157 ? ? 
metalc18 metalc ? ? D GLU 118 OE2 ? ? ? 1_555 O MN . MN ? ? D GLU 97  D MN 401 1_555 ? ? ? ? ? ? ? 1.911 ? ? 
metalc19 metalc ? ? D GLU 118 OE1 ? ? ? 1_555 P MN . MN ? ? D GLU 97  D MN 402 1_555 ? ? ? ? ? ? ? 1.991 ? ? 
metalc20 metalc ? ? D HIS 122 ND1 ? ? ? 1_555 P MN . MN ? ? D HIS 101 D MN 402 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc21 metalc ? ? D GLU 185 OE1 ? ? ? 1_555 O MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.303 ? ? 
metalc22 metalc ? ? D GLU 185 OE2 ? ? ? 1_555 O MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc23 metalc ? ? D GLU 219 OE1 ? ? ? 1_555 O MN . MN ? ? D GLU 198 D MN 401 1_555 ? ? ? ? ? ? ? 2.083 ? ? 
metalc24 metalc ? ? D GLU 219 OE2 ? ? ? 1_555 P MN . MN ? ? D GLU 198 D MN 402 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc25 metalc ? ? D HIS 222 ND1 ? ? ? 1_555 O MN . MN ? ? D HIS 201 D MN 401 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O2A ? E TTP .   ? A TTP 801 ? 1_555 MG ? F MG . ? A MG 802 ? 1_555 O2B ? E TTP .   ? A TTP 801 ? 1_555 71.9  ? 
2  O2A ? E TTP .   ? A TTP 801 ? 1_555 MG ? F MG . ? A MG 802 ? 1_555 O1G ? E TTP .   ? A TTP 801 ? 1_555 88.9  ? 
3  O2B ? E TTP .   ? A TTP 801 ? 1_555 MG ? F MG . ? A MG 802 ? 1_555 O1G ? E TTP .   ? A TTP 801 ? 1_555 68.1  ? 
4  O2A ? I TTP .   ? B TTP 801 ? 1_555 MG ? J MG . ? B MG 802 ? 1_555 O3G ? I TTP .   ? B TTP 801 ? 1_555 102.3 ? 
5  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 118 ? C GLU 97  ? 1_555 89.6  ? 
6  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 120.6 ? 
7  OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 90.1  ? 
8  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 138.4 ? 
9  OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 85.1  ? 
10 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 100.7 ? 
11 OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 117.3 ? 
12 OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 137.9 ? 
13 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 101.2 ? 
14 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 53.0  ? 
15 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 141.6 ? 
16 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 87.2  ? 
17 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 64.8  ? 
18 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 120.1 ? 
19 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 78.3  ? 
20 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 142.1 ? 
21 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 97.1  ? 
22 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 114.2 ? 
23 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 104.0 ? 
24 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 MN ? M MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 98.4  ? 
25 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 58.6  ? 
26 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 93.4  ? 
27 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 119.5 ? 
28 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 165.7 ? 
29 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 107.1 ? 
30 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 93.8  ? 
31 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 90.2  ? 
32 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 111.3 ? 
33 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 122.0 ? 
34 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 96.5  ? 
35 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 153.3 ? 
36 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 99.6  ? 
37 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 55.6  ? 
38 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 121.7 ? 
39 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 81.3  ? 
40 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 136.7 ? 
41 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 91.4  ? 
42 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 103.0 ? 
43 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 102.6 ? 
44 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 MN ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 89.6  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 355 A . ? TYR 355 A PRO 356 A ? PRO 356 A 1 1.33  
2 TYR 355 B . ? TYR 355 B PRO 356 B ? PRO 356 B 1 -0.33 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 6 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 149 ? PRO A 151 ? TYR A 149 PRO A 151 
AA1 2 ASN A 410 ? ASN A 415 ? ASN A 410 ASN A 415 
AA1 3 ILE A 461 ? MET A 466 ? ILE A 461 MET A 466 
AA2 1 ILE A 407 ? SER A 408 ? ILE A 407 SER A 408 
AA2 2 CYS A 170 ? GLU A 174 ? CYS A 170 GLU A 174 
AA2 3 GLY A 198 ? ASN A 202 ? GLY A 198 ASN A 202 
AA2 4 GLY A 247 ? ASN A 252 ? GLY A 247 ASN A 252 
AA2 5 LEU A 278 ? ILE A 284 ? LEU A 278 ILE A 284 
AA2 6 TYR A 357 ? PHE A 360 ? TYR A 357 PHE A 360 
AA2 7 THR A 681 ? ILE A 682 ? THR A 681 ILE A 682 
AA3 1 ALA A 298 ? PHE A 301 ? ALA A 298 PHE A 301 
AA3 2 LYS A 334 ? ILE A 337 ? LYS A 334 ILE A 337 
AA4 1 ILE A 601 ? TYR A 606 ? ILE A 601 TYR A 606 
AA4 2 SER A 609 ? PRO A 614 ? SER A 609 PRO A 614 
AA5 1 THR A 655 ? LEU A 658 ? THR A 655 LEU A 658 
AA5 2 TYR A 684 ? THR A 687 ? TYR A 684 THR A 687 
AA6 1 TYR B 149 ? PRO B 151 ? TYR B 149 PRO B 151 
AA6 2 ASN B 410 ? ASN B 415 ? ASN B 410 ASN B 415 
AA6 3 ILE B 461 ? MET B 466 ? ILE B 461 MET B 466 
AA7 1 CYS B 170 ? GLU B 174 ? CYS B 170 GLU B 174 
AA7 2 GLY B 198 ? ASN B 202 ? GLY B 198 ASN B 202 
AA7 3 GLY B 247 ? ASN B 252 ? GLY B 247 ASN B 252 
AA7 4 LEU B 278 ? ILE B 284 ? LEU B 278 ILE B 284 
AA7 5 TYR B 357 ? PHE B 360 ? TYR B 357 PHE B 360 
AA7 6 THR B 681 ? ILE B 682 ? THR B 681 ILE B 682 
AA8 1 ALA B 298 ? PHE B 301 ? ALA B 298 PHE B 301 
AA8 2 LYS B 334 ? ILE B 337 ? LYS B 334 ILE B 337 
AA9 1 ILE B 601 ? TYR B 606 ? ILE B 601 TYR B 606 
AA9 2 SER B 609 ? PRO B 614 ? SER B 609 PRO B 614 
AB1 1 THR B 655 ? LEU B 658 ? THR B 655 LEU B 658 
AB1 2 TYR B 684 ? THR B 687 ? TYR B 684 THR B 687 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 150 ? N GLN A 150 O SER A 413 ? O SER A 413 
AA1 2 3 N GLY A 412 ? N GLY A 412 O GLY A 464 ? O GLY A 464 
AA2 1 2 O ILE A 407 ? O ILE A 407 N LEU A 172 ? N LEU A 172 
AA2 2 3 N LEU A 173 ? N LEU A 173 O SER A 200 ? O SER A 200 
AA2 3 4 N LEU A 201 ? N LEU A 201 O ALA A 248 ? O ALA A 248 
AA2 4 5 N GLY A 247 ? N GLY A 247 O SER A 279 ? O SER A 279 
AA2 5 6 N VAL A 282 ? N VAL A 282 O TYR A 357 ? O TYR A 357 
AA2 6 7 N ILE A 358 ? N ILE A 358 O ILE A 682 ? O ILE A 682 
AA3 1 2 N VAL A 300 ? N VAL A 300 O GLU A 335 ? O GLU A 335 
AA4 1 2 N GLU A 602 ? N GLU A 602 O TYR A 613 ? O TYR A 613 
AA5 1 2 N LEU A 656 ? N LEU A 656 O TYR A 684 ? O TYR A 684 
AA6 1 2 N GLN B 150 ? N GLN B 150 O SER B 413 ? O SER B 413 
AA6 2 3 N GLY B 412 ? N GLY B 412 O GLY B 464 ? O GLY B 464 
AA7 1 2 N LEU B 173 ? N LEU B 173 O SER B 200 ? O SER B 200 
AA7 2 3 N LEU B 201 ? N LEU B 201 O TYR B 250 ? O TYR B 250 
AA7 3 4 N GLY B 247 ? N GLY B 247 O SER B 279 ? O SER B 279 
AA7 4 5 N VAL B 282 ? N VAL B 282 O TYR B 357 ? O TYR B 357 
AA7 5 6 N ILE B 358 ? N ILE B 358 O ILE B 682 ? O ILE B 682 
AA8 1 2 N ALA B 298 ? N ALA B 298 O ILE B 337 ? O ILE B 337 
AA9 1 2 N ARG B 604 ? N ARG B 604 O THR B 611 ? O THR B 611 
AB1 1 2 N LEU B 656 ? N LEU B 656 O TYR B 684 ? O TYR B 684 
# 
_pdbx_entry_details.entry_id                   9BY8 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A CYS 382 ? ? OG  A SER 653 ? ? 2.13 
2 1 O   B PRO 616 ? ? OH  B TYR 626 ? ? 2.13 
3 1 O   A PRO 616 ? ? OH  A TYR 626 ? ? 2.14 
4 1 NH2 D ARG 86  ? ? OE1 D GLU 211 ? ? 2.18 
5 1 O   B CYS 382 ? ? OG  B SER 653 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 MET A 240 ? ? 72.07   -7.44   
2  1 SER A 593 ? ? 59.74   -154.81 
3  1 SER A 653 ? ? -68.90  99.22   
4  1 ASP B 215 ? ? 79.68   -0.87   
5  1 ASP B 238 ? ? -95.48  31.27   
6  1 SER B 408 ? ? -160.51 113.44  
7  1 SER B 593 ? ? 58.49   -151.27 
8  1 THR C 72  ? ? -128.07 -59.05  
9  1 ASP C 148 ? ? 58.01   15.69   
10 1 PHE C 166 ? ? -125.59 -60.78  
11 1 THR D 72  ? ? -128.21 -58.37  
12 1 PHE D 166 ? ? -144.18 -61.13  
13 1 THR D 311 ? ? -168.67 116.06  
14 1 ASP D 317 ? ? 61.62   167.64  
15 1 ASP D 318 ? ? 67.22   -4.13   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BY8 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'RIGID BODY FIT' 
# 
loop_
_em_3d_fitting_list.id 
_em_3d_fitting_list.3d_fitting_id 
_em_3d_fitting_list.pdb_entry_id 
_em_3d_fitting_list.pdb_chain_id 
_em_3d_fitting_list.pdb_chain_residue_range 
_em_3d_fitting_list.details 
_em_3d_fitting_list.chain_id 
_em_3d_fitting_list.chain_residue_range 
_em_3d_fitting_list.source_name 
_em_3d_fitting_list.type 
_em_3d_fitting_list.accession_code 
_em_3d_fitting_list.initial_refinement_model_id 
1 1 9BY1 ? ?      'Rigid-body docking of consensus model 9BY1 containing alpha subunits and beta C-terminal tails' ? ?      PDB 
'experimental model' 9BY1 1 
2 1 4DR0 ? 16-290 'Rigid-body docking of residues 16-290 from beta dimer model 4DR0'                               ? 16-290 PDB 
'experimental model' 4DR0 2 
# 
_em_3d_reconstruction.entry_id                    9BY8 
_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                  3.88 
_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               29000 
_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                        9BY8 
_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              9BY8 
_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                9BY8 
_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              9BY8 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A SER 2   ? A SER 2   
3   1 Y 1 A GLN 3   ? A GLN 3   
4   1 Y 1 A ASN 4   ? A ASN 4   
5   1 Y 1 A GLN 5   ? A GLN 5   
6   1 Y 1 A ASP 689 ? A ASP 689 
7   1 Y 1 A THR 690 ? A THR 690 
8   1 Y 1 A GLY 691 ? A GLY 691 
9   1 Y 1 A GLN 692 ? A GLN 692 
10  1 Y 1 A ASP 693 ? A ASP 693 
11  1 Y 1 A SER 694 ? A SER 694 
12  1 Y 1 A CYS 695 ? A CYS 695 
13  1 Y 1 A LEU 696 ? A LEU 696 
14  1 Y 1 A SER 697 ? A SER 697 
15  1 Y 1 A CYS 698 ? A CYS 698 
16  1 Y 1 A VAL 699 ? A VAL 699 
17  1 Y 1 A VAL 700 ? A VAL 700 
18  1 Y 1 B MET 1   ? B MET 1   
19  1 Y 1 B SER 2   ? B SER 2   
20  1 Y 1 B GLN 3   ? B GLN 3   
21  1 Y 1 B ASN 4   ? B ASN 4   
22  1 Y 1 B GLN 5   ? B GLN 5   
23  1 Y 1 B ASP 689 ? B ASP 689 
24  1 Y 1 B THR 690 ? B THR 690 
25  1 Y 1 B GLY 691 ? B GLY 691 
26  1 Y 1 B GLN 692 ? B GLN 692 
27  1 Y 1 B ASP 693 ? B ASP 693 
28  1 Y 1 B SER 694 ? B SER 694 
29  1 Y 1 B CYS 695 ? B CYS 695 
30  1 Y 1 B LEU 696 ? B LEU 696 
31  1 Y 1 B SER 697 ? B SER 697 
32  1 Y 1 B CYS 698 ? B CYS 698 
33  1 Y 1 B VAL 699 ? B VAL 699 
34  1 Y 1 B VAL 700 ? B VAL 700 
35  1 Y 1 C MET -20 ? C MET 1   
36  1 Y 1 C GLY -19 ? C GLY 2   
37  1 Y 1 C SER -18 ? C SER 3   
38  1 Y 1 C SER -17 ? C SER 4   
39  1 Y 1 C HIS -16 ? C HIS 5   
40  1 Y 1 C HIS -15 ? C HIS 6   
41  1 Y 1 C HIS -14 ? C HIS 7   
42  1 Y 1 C HIS -13 ? C HIS 8   
43  1 Y 1 C HIS -12 ? C HIS 9   
44  1 Y 1 C HIS -11 ? C HIS 10  
45  1 Y 1 C SER -10 ? C SER 11  
46  1 Y 1 C SER -9  ? C SER 12  
47  1 Y 1 C GLY -8  ? C GLY 13  
48  1 Y 1 C LEU -7  ? C LEU 14  
49  1 Y 1 C VAL -6  ? C VAL 15  
50  1 Y 1 C PRO -5  ? C PRO 16  
51  1 Y 1 C ARG -4  ? C ARG 17  
52  1 Y 1 C GLY -3  ? C GLY 18  
53  1 Y 1 C SER -2  ? C SER 19  
54  1 Y 1 C HIS -1  ? C HIS 20  
55  1 Y 1 C MET 0   ? C MET 21  
56  1 Y 1 C MET 1   ? C MET 22  
57  1 Y 1 C THR 2   ? C THR 23  
58  1 Y 1 C LYS 3   ? C LYS 24  
59  1 Y 1 C ILE 4   ? C ILE 25  
60  1 Y 1 C TYR 5   ? C TYR 26  
61  1 Y 1 C ASP 6   ? C ASP 27  
62  1 Y 1 C ALA 7   ? C ALA 28  
63  1 Y 1 C ALA 8   ? C ALA 29  
64  1 Y 1 C ASN 9   ? C ASN 30  
65  1 Y 1 C TRP 10  ? C TRP 31  
66  1 Y 1 C SER 11  ? C SER 32  
67  1 Y 1 C LYS 12  ? C LYS 33  
68  1 Y 1 C HIS 13  ? C HIS 34  
69  1 Y 1 C GLU 14  ? C GLU 35  
70  1 Y 1 C ASP 15  ? C ASP 36  
71  1 Y 1 C ASN 291 ? C ASN 312 
72  1 Y 1 C THR 292 ? C THR 313 
73  1 Y 1 C LYS 293 ? C LYS 314 
74  1 Y 1 C THR 294 ? C THR 315 
75  1 Y 1 C LYS 295 ? C LYS 316 
76  1 Y 1 C SER 296 ? C SER 317 
77  1 Y 1 C HIS 297 ? C HIS 318 
78  1 Y 1 C ASP 298 ? C ASP 319 
79  1 Y 1 C PHE 299 ? C PHE 320 
80  1 Y 1 C PHE 300 ? C PHE 321 
81  1 Y 1 C SER 301 ? C SER 322 
82  1 Y 1 C MET 302 ? C MET 323 
83  1 Y 1 C LYS 303 ? C LYS 324 
84  1 Y 1 C GLY 304 ? C GLY 325 
85  1 Y 1 C ASN 305 ? C ASN 326 
86  1 Y 1 C GLY 306 ? C GLY 327 
87  1 Y 1 C TYR 307 ? C TYR 328 
88  1 Y 1 C LYS 308 ? C LYS 329 
89  1 Y 1 C GLU 323 ? C GLU 344 
90  1 Y 1 C ASP 324 ? C ASP 345 
91  1 Y 1 C GLU 325 ? C GLU 346 
92  1 Y 1 C LYS 326 ? C LYS 347 
93  1 Y 1 C GLU 327 ? C GLU 348 
94  1 Y 1 C GLN 328 ? C GLN 349 
95  1 Y 1 C ILE 329 ? C ILE 350 
96  1 Y 1 D MET -20 ? D MET 1   
97  1 Y 1 D GLY -19 ? D GLY 2   
98  1 Y 1 D SER -18 ? D SER 3   
99  1 Y 1 D SER -17 ? D SER 4   
100 1 Y 1 D HIS -16 ? D HIS 5   
101 1 Y 1 D HIS -15 ? D HIS 6   
102 1 Y 1 D HIS -14 ? D HIS 7   
103 1 Y 1 D HIS -13 ? D HIS 8   
104 1 Y 1 D HIS -12 ? D HIS 9   
105 1 Y 1 D HIS -11 ? D HIS 10  
106 1 Y 1 D SER -10 ? D SER 11  
107 1 Y 1 D SER -9  ? D SER 12  
108 1 Y 1 D GLY -8  ? D GLY 13  
109 1 Y 1 D LEU -7  ? D LEU 14  
110 1 Y 1 D VAL -6  ? D VAL 15  
111 1 Y 1 D PRO -5  ? D PRO 16  
112 1 Y 1 D ARG -4  ? D ARG 17  
113 1 Y 1 D GLY -3  ? D GLY 18  
114 1 Y 1 D SER -2  ? D SER 19  
115 1 Y 1 D HIS -1  ? D HIS 20  
116 1 Y 1 D MET 0   ? D MET 21  
117 1 Y 1 D MET 1   ? D MET 22  
118 1 Y 1 D THR 2   ? D THR 23  
119 1 Y 1 D LYS 3   ? D LYS 24  
120 1 Y 1 D ILE 4   ? D ILE 25  
121 1 Y 1 D TYR 5   ? D TYR 26  
122 1 Y 1 D ASP 6   ? D ASP 27  
123 1 Y 1 D ALA 7   ? D ALA 28  
124 1 Y 1 D ALA 8   ? D ALA 29  
125 1 Y 1 D ASN 9   ? D ASN 30  
126 1 Y 1 D TRP 10  ? D TRP 31  
127 1 Y 1 D SER 11  ? D SER 32  
128 1 Y 1 D LYS 12  ? D LYS 33  
129 1 Y 1 D HIS 13  ? D HIS 34  
130 1 Y 1 D GLU 14  ? D GLU 35  
131 1 Y 1 D ASP 15  ? D ASP 36  
132 1 Y 1 D ASN 291 ? D ASN 312 
133 1 Y 1 D THR 292 ? D THR 313 
134 1 Y 1 D LYS 293 ? D LYS 314 
135 1 Y 1 D THR 294 ? D THR 315 
136 1 Y 1 D LYS 295 ? D LYS 316 
137 1 Y 1 D SER 296 ? D SER 317 
138 1 Y 1 D HIS 297 ? D HIS 318 
139 1 Y 1 D ASP 298 ? D ASP 319 
140 1 Y 1 D PHE 299 ? D PHE 320 
141 1 Y 1 D PHE 300 ? D PHE 321 
142 1 Y 1 D SER 301 ? D SER 322 
143 1 Y 1 D MET 302 ? D MET 323 
144 1 Y 1 D LYS 303 ? D LYS 324 
145 1 Y 1 D GLY 304 ? D GLY 325 
146 1 Y 1 D ASN 305 ? D ASN 326 
147 1 Y 1 D GLY 306 ? D GLY 327 
148 1 Y 1 D TYR 307 ? D TYR 328 
149 1 Y 1 D LYS 308 ? D LYS 329 
150 1 Y 1 D GLU 323 ? D GLU 344 
151 1 Y 1 D ASP 324 ? D ASP 345 
152 1 Y 1 D GLU 325 ? D GLU 346 
153 1 Y 1 D LYS 326 ? D LYS 347 
154 1 Y 1 D GLU 327 ? D GLU 348 
155 1 Y 1 D GLN 328 ? D GLN 349 
156 1 Y 1 D ILE 329 ? D ILE 350 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
ATP PG     P  N N 74  
ATP O1G    O  N N 75  
ATP O2G    O  N N 76  
ATP O3G    O  N N 77  
ATP PB     P  N R 78  
ATP O1B    O  N N 79  
ATP O2B    O  N N 80  
ATP O3B    O  N N 81  
ATP PA     P  N R 82  
ATP O1A    O  N N 83  
ATP O2A    O  N N 84  
ATP O3A    O  N N 85  
ATP "O5'"  O  N N 86  
ATP "C5'"  C  N N 87  
ATP "C4'"  C  N R 88  
ATP "O4'"  O  N N 89  
ATP "C3'"  C  N S 90  
ATP "O3'"  O  N N 91  
ATP "C2'"  C  N R 92  
ATP "O2'"  O  N N 93  
ATP "C1'"  C  N R 94  
ATP N9     N  Y N 95  
ATP C8     C  Y N 96  
ATP N7     N  Y N 97  
ATP C5     C  Y N 98  
ATP C6     C  Y N 99  
ATP N6     N  N N 100 
ATP N1     N  Y N 101 
ATP C2     C  Y N 102 
ATP N3     N  Y N 103 
ATP C4     C  Y N 104 
ATP HOG2   H  N N 105 
ATP HOG3   H  N N 106 
ATP HOB2   H  N N 107 
ATP HOA2   H  N N 108 
ATP "H5'1" H  N N 109 
ATP "H5'2" H  N N 110 
ATP "H4'"  H  N N 111 
ATP "H3'"  H  N N 112 
ATP "HO3'" H  N N 113 
ATP "H2'"  H  N N 114 
ATP "HO2'" H  N N 115 
ATP "H1'"  H  N N 116 
ATP H8     H  N N 117 
ATP HN61   H  N N 118 
ATP HN62   H  N N 119 
ATP H2     H  N N 120 
CYS N      N  N N 121 
CYS CA     C  N R 122 
CYS C      C  N N 123 
CYS O      O  N N 124 
CYS CB     C  N N 125 
CYS SG     S  N N 126 
CYS OXT    O  N N 127 
CYS H      H  N N 128 
CYS H2     H  N N 129 
CYS HA     H  N N 130 
CYS HB2    H  N N 131 
CYS HB3    H  N N 132 
CYS HG     H  N N 133 
CYS HXT    H  N N 134 
DGI O1B    O  N N 135 
DGI PB     P  N N 136 
DGI O2B    O  N N 137 
DGI O3B    O  N N 138 
DGI O3A    O  N N 139 
DGI PA     P  N S 140 
DGI O1A    O  N N 141 
DGI O2A    O  N N 142 
DGI "O5'"  O  N N 143 
DGI "C5'"  C  N N 144 
DGI "C4'"  C  N R 145 
DGI "O4'"  O  N N 146 
DGI "C3'"  C  N S 147 
DGI "O3'"  O  N N 148 
DGI "C2'"  C  N N 149 
DGI "C1'"  C  N R 150 
DGI N9     N  Y N 151 
DGI C8     C  Y N 152 
DGI N7     N  Y N 153 
DGI C5     C  Y N 154 
DGI C4     C  Y N 155 
DGI N3     N  N N 156 
DGI C2     C  N N 157 
DGI N2     N  N N 158 
DGI N1     N  N N 159 
DGI C6     C  N N 160 
DGI O6     O  N N 161 
DGI HOB2   H  N N 162 
DGI HOB3   H  N N 163 
DGI HOA2   H  N N 164 
DGI "H5'"  H  N N 165 
DGI "H5''" H  N N 166 
DGI "H4'"  H  N N 167 
DGI "H3'"  H  N N 168 
DGI "HO3'" H  N N 169 
DGI "H2'"  H  N N 170 
DGI "H2''" H  N N 171 
DGI "H1'"  H  N N 172 
DGI H8     H  N N 173 
DGI HN21   H  N N 174 
DGI HN22   H  N N 175 
DGI HN1    H  N N 176 
GLN N      N  N N 177 
GLN CA     C  N S 178 
GLN C      C  N N 179 
GLN O      O  N N 180 
GLN CB     C  N N 181 
GLN CG     C  N N 182 
GLN CD     C  N N 183 
GLN OE1    O  N N 184 
GLN NE2    N  N N 185 
GLN OXT    O  N N 186 
GLN H      H  N N 187 
GLN H2     H  N N 188 
GLN HA     H  N N 189 
GLN HB2    H  N N 190 
GLN HB3    H  N N 191 
GLN HG2    H  N N 192 
GLN HG3    H  N N 193 
GLN HE21   H  N N 194 
GLN HE22   H  N N 195 
GLN HXT    H  N N 196 
GLU N      N  N N 197 
GLU CA     C  N S 198 
GLU C      C  N N 199 
GLU O      O  N N 200 
GLU CB     C  N N 201 
GLU CG     C  N N 202 
GLU CD     C  N N 203 
GLU OE1    O  N N 204 
GLU OE2    O  N N 205 
GLU OXT    O  N N 206 
GLU H      H  N N 207 
GLU H2     H  N N 208 
GLU HA     H  N N 209 
GLU HB2    H  N N 210 
GLU HB3    H  N N 211 
GLU HG2    H  N N 212 
GLU HG3    H  N N 213 
GLU HE2    H  N N 214 
GLU HXT    H  N N 215 
GLY N      N  N N 216 
GLY CA     C  N N 217 
GLY C      C  N N 218 
GLY O      O  N N 219 
GLY OXT    O  N N 220 
GLY H      H  N N 221 
GLY H2     H  N N 222 
GLY HA2    H  N N 223 
GLY HA3    H  N N 224 
GLY HXT    H  N N 225 
HIS N      N  N N 226 
HIS CA     C  N S 227 
HIS C      C  N N 228 
HIS O      O  N N 229 
HIS CB     C  N N 230 
HIS CG     C  Y N 231 
HIS ND1    N  Y N 232 
HIS CD2    C  Y N 233 
HIS CE1    C  Y N 234 
HIS NE2    N  Y N 235 
HIS OXT    O  N N 236 
HIS H      H  N N 237 
HIS H2     H  N N 238 
HIS HA     H  N N 239 
HIS HB2    H  N N 240 
HIS HB3    H  N N 241 
HIS HD1    H  N N 242 
HIS HD2    H  N N 243 
HIS HE1    H  N N 244 
HIS HE2    H  N N 245 
HIS HXT    H  N N 246 
ILE N      N  N N 247 
ILE CA     C  N S 248 
ILE C      C  N N 249 
ILE O      O  N N 250 
ILE CB     C  N S 251 
ILE CG1    C  N N 252 
ILE CG2    C  N N 253 
ILE CD1    C  N N 254 
ILE OXT    O  N N 255 
ILE H      H  N N 256 
ILE H2     H  N N 257 
ILE HA     H  N N 258 
ILE HB     H  N N 259 
ILE HG12   H  N N 260 
ILE HG13   H  N N 261 
ILE HG21   H  N N 262 
ILE HG22   H  N N 263 
ILE HG23   H  N N 264 
ILE HD11   H  N N 265 
ILE HD12   H  N N 266 
ILE HD13   H  N N 267 
ILE HXT    H  N N 268 
LEU N      N  N N 269 
LEU CA     C  N S 270 
LEU C      C  N N 271 
LEU O      O  N N 272 
LEU CB     C  N N 273 
LEU CG     C  N N 274 
LEU CD1    C  N N 275 
LEU CD2    C  N N 276 
LEU OXT    O  N N 277 
LEU H      H  N N 278 
LEU H2     H  N N 279 
LEU HA     H  N N 280 
LEU HB2    H  N N 281 
LEU HB3    H  N N 282 
LEU HG     H  N N 283 
LEU HD11   H  N N 284 
LEU HD12   H  N N 285 
LEU HD13   H  N N 286 
LEU HD21   H  N N 287 
LEU HD22   H  N N 288 
LEU HD23   H  N N 289 
LEU HXT    H  N N 290 
LYS N      N  N N 291 
LYS CA     C  N S 292 
LYS C      C  N N 293 
LYS O      O  N N 294 
LYS CB     C  N N 295 
LYS CG     C  N N 296 
LYS CD     C  N N 297 
LYS CE     C  N N 298 
LYS NZ     N  N N 299 
LYS OXT    O  N N 300 
LYS H      H  N N 301 
LYS H2     H  N N 302 
LYS HA     H  N N 303 
LYS HB2    H  N N 304 
LYS HB3    H  N N 305 
LYS HG2    H  N N 306 
LYS HG3    H  N N 307 
LYS HD2    H  N N 308 
LYS HD3    H  N N 309 
LYS HE2    H  N N 310 
LYS HE3    H  N N 311 
LYS HZ1    H  N N 312 
LYS HZ2    H  N N 313 
LYS HZ3    H  N N 314 
LYS HXT    H  N N 315 
MET N      N  N N 316 
MET CA     C  N S 317 
MET C      C  N N 318 
MET O      O  N N 319 
MET CB     C  N N 320 
MET CG     C  N N 321 
MET SD     S  N N 322 
MET CE     C  N N 323 
MET OXT    O  N N 324 
MET H      H  N N 325 
MET H2     H  N N 326 
MET HA     H  N N 327 
MET HB2    H  N N 328 
MET HB3    H  N N 329 
MET HG2    H  N N 330 
MET HG3    H  N N 331 
MET HE1    H  N N 332 
MET HE2    H  N N 333 
MET HE3    H  N N 334 
MET HXT    H  N N 335 
MG  MG     MG N N 336 
MN  MN     MN N N 337 
PHE N      N  N N 338 
PHE CA     C  N S 339 
PHE C      C  N N 340 
PHE O      O  N N 341 
PHE CB     C  N N 342 
PHE CG     C  Y N 343 
PHE CD1    C  Y N 344 
PHE CD2    C  Y N 345 
PHE CE1    C  Y N 346 
PHE CE2    C  Y N 347 
PHE CZ     C  Y N 348 
PHE OXT    O  N N 349 
PHE H      H  N N 350 
PHE H2     H  N N 351 
PHE HA     H  N N 352 
PHE HB2    H  N N 353 
PHE HB3    H  N N 354 
PHE HD1    H  N N 355 
PHE HD2    H  N N 356 
PHE HE1    H  N N 357 
PHE HE2    H  N N 358 
PHE HZ     H  N N 359 
PHE HXT    H  N N 360 
PRO N      N  N N 361 
PRO CA     C  N S 362 
PRO C      C  N N 363 
PRO O      O  N N 364 
PRO CB     C  N N 365 
PRO CG     C  N N 366 
PRO CD     C  N N 367 
PRO OXT    O  N N 368 
PRO H      H  N N 369 
PRO HA     H  N N 370 
PRO HB2    H  N N 371 
PRO HB3    H  N N 372 
PRO HG2    H  N N 373 
PRO HG3    H  N N 374 
PRO HD2    H  N N 375 
PRO HD3    H  N N 376 
PRO HXT    H  N N 377 
SER N      N  N N 378 
SER CA     C  N S 379 
SER C      C  N N 380 
SER O      O  N N 381 
SER CB     C  N N 382 
SER OG     O  N N 383 
SER OXT    O  N N 384 
SER H      H  N N 385 
SER H2     H  N N 386 
SER HA     H  N N 387 
SER HB2    H  N N 388 
SER HB3    H  N N 389 
SER HG     H  N N 390 
SER HXT    H  N N 391 
THR N      N  N N 392 
THR CA     C  N S 393 
THR C      C  N N 394 
THR O      O  N N 395 
THR CB     C  N R 396 
THR OG1    O  N N 397 
THR CG2    C  N N 398 
THR OXT    O  N N 399 
THR H      H  N N 400 
THR H2     H  N N 401 
THR HA     H  N N 402 
THR HB     H  N N 403 
THR HG1    H  N N 404 
THR HG21   H  N N 405 
THR HG22   H  N N 406 
THR HG23   H  N N 407 
THR HXT    H  N N 408 
TRP N      N  N N 409 
TRP CA     C  N S 410 
TRP C      C  N N 411 
TRP O      O  N N 412 
TRP CB     C  N N 413 
TRP CG     C  Y N 414 
TRP CD1    C  Y N 415 
TRP CD2    C  Y N 416 
TRP NE1    N  Y N 417 
TRP CE2    C  Y N 418 
TRP CE3    C  Y N 419 
TRP CZ2    C  Y N 420 
TRP CZ3    C  Y N 421 
TRP CH2    C  Y N 422 
TRP OXT    O  N N 423 
TRP H      H  N N 424 
TRP H2     H  N N 425 
TRP HA     H  N N 426 
TRP HB2    H  N N 427 
TRP HB3    H  N N 428 
TRP HD1    H  N N 429 
TRP HE1    H  N N 430 
TRP HE3    H  N N 431 
TRP HZ2    H  N N 432 
TRP HZ3    H  N N 433 
TRP HH2    H  N N 434 
TRP HXT    H  N N 435 
TTP PA     P  N S 436 
TTP O1A    O  N N 437 
TTP O2A    O  N N 438 
TTP O3A    O  N N 439 
TTP PB     P  N S 440 
TTP O1B    O  N N 441 
TTP O2B    O  N N 442 
TTP O3B    O  N N 443 
TTP PG     P  N N 444 
TTP O1G    O  N N 445 
TTP O2G    O  N N 446 
TTP O3G    O  N N 447 
TTP "O5'"  O  N N 448 
TTP "C5'"  C  N N 449 
TTP "C4'"  C  N R 450 
TTP "O4'"  O  N N 451 
TTP "C3'"  C  N S 452 
TTP "O3'"  O  N N 453 
TTP "C2'"  C  N N 454 
TTP "C1'"  C  N R 455 
TTP N1     N  N N 456 
TTP C2     C  N N 457 
TTP O2     O  N N 458 
TTP N3     N  N N 459 
TTP C4     C  N N 460 
TTP O4     O  N N 461 
TTP C5     C  N N 462 
TTP C5M    C  N N 463 
TTP C6     C  N N 464 
TTP HOA2   H  N N 465 
TTP HOB2   H  N N 466 
TTP HOG2   H  N N 467 
TTP HOG3   H  N N 468 
TTP "H5'1" H  N N 469 
TTP "H5'2" H  N N 470 
TTP "H4'"  H  N N 471 
TTP "H3'"  H  N N 472 
TTP "HO3'" H  N N 473 
TTP "H2'1" H  N N 474 
TTP "H2'2" H  N N 475 
TTP "H1'"  H  N N 476 
TTP HN3    H  N N 477 
TTP HM51   H  N N 478 
TTP HM52   H  N N 479 
TTP HM53   H  N N 480 
TTP H6     H  N N 481 
TYR N      N  N N 482 
TYR CA     C  N S 483 
TYR C      C  N N 484 
TYR O      O  N N 485 
TYR CB     C  N N 486 
TYR CG     C  Y N 487 
TYR CD1    C  Y N 488 
TYR CD2    C  Y N 489 
TYR CE1    C  Y N 490 
TYR CE2    C  Y N 491 
TYR CZ     C  Y N 492 
TYR OH     O  N N 493 
TYR OXT    O  N N 494 
TYR H      H  N N 495 
TYR H2     H  N N 496 
TYR HA     H  N N 497 
TYR HB2    H  N N 498 
TYR HB3    H  N N 499 
TYR HD1    H  N N 500 
TYR HD2    H  N N 501 
TYR HE1    H  N N 502 
TYR HE2    H  N N 503 
TYR HH     H  N N 504 
TYR HXT    H  N N 505 
VAL N      N  N N 506 
VAL CA     C  N S 507 
VAL C      C  N N 508 
VAL O      O  N N 509 
VAL CB     C  N N 510 
VAL CG1    C  N N 511 
VAL CG2    C  N N 512 
VAL OXT    O  N N 513 
VAL H      H  N N 514 
VAL H2     H  N N 515 
VAL HA     H  N N 516 
VAL HB     H  N N 517 
VAL HG11   H  N N 518 
VAL HG12   H  N N 519 
VAL HG13   H  N N 520 
VAL HG21   H  N N 521 
VAL HG22   H  N N 522 
VAL HG23   H  N N 523 
VAL HXT    H  N N 524 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
ATP PG    O1G    doub N N 70  
ATP PG    O2G    sing N N 71  
ATP PG    O3G    sing N N 72  
ATP PG    O3B    sing N N 73  
ATP O2G   HOG2   sing N N 74  
ATP O3G   HOG3   sing N N 75  
ATP PB    O1B    doub N N 76  
ATP PB    O2B    sing N N 77  
ATP PB    O3B    sing N N 78  
ATP PB    O3A    sing N N 79  
ATP O2B   HOB2   sing N N 80  
ATP PA    O1A    doub N N 81  
ATP PA    O2A    sing N N 82  
ATP PA    O3A    sing N N 83  
ATP PA    "O5'"  sing N N 84  
ATP O2A   HOA2   sing N N 85  
ATP "O5'" "C5'"  sing N N 86  
ATP "C5'" "C4'"  sing N N 87  
ATP "C5'" "H5'1" sing N N 88  
ATP "C5'" "H5'2" sing N N 89  
ATP "C4'" "O4'"  sing N N 90  
ATP "C4'" "C3'"  sing N N 91  
ATP "C4'" "H4'"  sing N N 92  
ATP "O4'" "C1'"  sing N N 93  
ATP "C3'" "O3'"  sing N N 94  
ATP "C3'" "C2'"  sing N N 95  
ATP "C3'" "H3'"  sing N N 96  
ATP "O3'" "HO3'" sing N N 97  
ATP "C2'" "O2'"  sing N N 98  
ATP "C2'" "C1'"  sing N N 99  
ATP "C2'" "H2'"  sing N N 100 
ATP "O2'" "HO2'" sing N N 101 
ATP "C1'" N9     sing N N 102 
ATP "C1'" "H1'"  sing N N 103 
ATP N9    C8     sing Y N 104 
ATP N9    C4     sing Y N 105 
ATP C8    N7     doub Y N 106 
ATP C8    H8     sing N N 107 
ATP N7    C5     sing Y N 108 
ATP C5    C6     sing Y N 109 
ATP C5    C4     doub Y N 110 
ATP C6    N6     sing N N 111 
ATP C6    N1     doub Y N 112 
ATP N6    HN61   sing N N 113 
ATP N6    HN62   sing N N 114 
ATP N1    C2     sing Y N 115 
ATP C2    N3     doub Y N 116 
ATP C2    H2     sing N N 117 
ATP N3    C4     sing Y N 118 
CYS N     CA     sing N N 119 
CYS N     H      sing N N 120 
CYS N     H2     sing N N 121 
CYS CA    C      sing N N 122 
CYS CA    CB     sing N N 123 
CYS CA    HA     sing N N 124 
CYS C     O      doub N N 125 
CYS C     OXT    sing N N 126 
CYS CB    SG     sing N N 127 
CYS CB    HB2    sing N N 128 
CYS CB    HB3    sing N N 129 
CYS SG    HG     sing N N 130 
CYS OXT   HXT    sing N N 131 
DGI O1B   PB     doub N N 132 
DGI PB    O2B    sing N N 133 
DGI PB    O3B    sing N N 134 
DGI PB    O3A    sing N N 135 
DGI O2B   HOB2   sing N N 136 
DGI O3B   HOB3   sing N N 137 
DGI O3A   PA     sing N N 138 
DGI PA    O1A    doub N N 139 
DGI PA    O2A    sing N N 140 
DGI PA    "O5'"  sing N N 141 
DGI O2A   HOA2   sing N N 142 
DGI "O5'" "C5'"  sing N N 143 
DGI "C5'" "C4'"  sing N N 144 
DGI "C5'" "H5'"  sing N N 145 
DGI "C5'" "H5''" sing N N 146 
DGI "C4'" "O4'"  sing N N 147 
DGI "C4'" "C3'"  sing N N 148 
DGI "C4'" "H4'"  sing N N 149 
DGI "O4'" "C1'"  sing N N 150 
DGI "C3'" "O3'"  sing N N 151 
DGI "C3'" "C2'"  sing N N 152 
DGI "C3'" "H3'"  sing N N 153 
DGI "O3'" "HO3'" sing N N 154 
DGI "C2'" "C1'"  sing N N 155 
DGI "C2'" "H2'"  sing N N 156 
DGI "C2'" "H2''" sing N N 157 
DGI "C1'" N9     sing N N 158 
DGI "C1'" "H1'"  sing N N 159 
DGI N9    C8     sing Y N 160 
DGI N9    C4     sing Y N 161 
DGI C8    N7     doub Y N 162 
DGI C8    H8     sing N N 163 
DGI N7    C5     sing Y N 164 
DGI C5    C4     doub Y N 165 
DGI C5    C6     sing N N 166 
DGI C4    N3     sing N N 167 
DGI N3    C2     doub N N 168 
DGI C2    N2     sing N N 169 
DGI C2    N1     sing N N 170 
DGI N2    HN21   sing N N 171 
DGI N2    HN22   sing N N 172 
DGI N1    C6     sing N N 173 
DGI N1    HN1    sing N N 174 
DGI C6    O6     doub N N 175 
GLN N     CA     sing N N 176 
GLN N     H      sing N N 177 
GLN N     H2     sing N N 178 
GLN CA    C      sing N N 179 
GLN CA    CB     sing N N 180 
GLN CA    HA     sing N N 181 
GLN C     O      doub N N 182 
GLN C     OXT    sing N N 183 
GLN CB    CG     sing N N 184 
GLN CB    HB2    sing N N 185 
GLN CB    HB3    sing N N 186 
GLN CG    CD     sing N N 187 
GLN CG    HG2    sing N N 188 
GLN CG    HG3    sing N N 189 
GLN CD    OE1    doub N N 190 
GLN CD    NE2    sing N N 191 
GLN NE2   HE21   sing N N 192 
GLN NE2   HE22   sing N N 193 
GLN OXT   HXT    sing N N 194 
GLU N     CA     sing N N 195 
GLU N     H      sing N N 196 
GLU N     H2     sing N N 197 
GLU CA    C      sing N N 198 
GLU CA    CB     sing N N 199 
GLU CA    HA     sing N N 200 
GLU C     O      doub N N 201 
GLU C     OXT    sing N N 202 
GLU CB    CG     sing N N 203 
GLU CB    HB2    sing N N 204 
GLU CB    HB3    sing N N 205 
GLU CG    CD     sing N N 206 
GLU CG    HG2    sing N N 207 
GLU CG    HG3    sing N N 208 
GLU CD    OE1    doub N N 209 
GLU CD    OE2    sing N N 210 
GLU OE2   HE2    sing N N 211 
GLU OXT   HXT    sing N N 212 
GLY N     CA     sing N N 213 
GLY N     H      sing N N 214 
GLY N     H2     sing N N 215 
GLY CA    C      sing N N 216 
GLY CA    HA2    sing N N 217 
GLY CA    HA3    sing N N 218 
GLY C     O      doub N N 219 
GLY C     OXT    sing N N 220 
GLY OXT   HXT    sing N N 221 
HIS N     CA     sing N N 222 
HIS N     H      sing N N 223 
HIS N     H2     sing N N 224 
HIS CA    C      sing N N 225 
HIS CA    CB     sing N N 226 
HIS CA    HA     sing N N 227 
HIS C     O      doub N N 228 
HIS C     OXT    sing N N 229 
HIS CB    CG     sing N N 230 
HIS CB    HB2    sing N N 231 
HIS CB    HB3    sing N N 232 
HIS CG    ND1    sing Y N 233 
HIS CG    CD2    doub Y N 234 
HIS ND1   CE1    doub Y N 235 
HIS ND1   HD1    sing N N 236 
HIS CD2   NE2    sing Y N 237 
HIS CD2   HD2    sing N N 238 
HIS CE1   NE2    sing Y N 239 
HIS CE1   HE1    sing N N 240 
HIS NE2   HE2    sing N N 241 
HIS OXT   HXT    sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TTP PA    O1A    doub N N 425 
TTP PA    O2A    sing N N 426 
TTP PA    O3A    sing N N 427 
TTP PA    "O5'"  sing N N 428 
TTP O2A   HOA2   sing N N 429 
TTP O3A   PB     sing N N 430 
TTP PB    O1B    doub N N 431 
TTP PB    O2B    sing N N 432 
TTP PB    O3B    sing N N 433 
TTP O2B   HOB2   sing N N 434 
TTP O3B   PG     sing N N 435 
TTP PG    O1G    doub N N 436 
TTP PG    O2G    sing N N 437 
TTP PG    O3G    sing N N 438 
TTP O2G   HOG2   sing N N 439 
TTP O3G   HOG3   sing N N 440 
TTP "O5'" "C5'"  sing N N 441 
TTP "C5'" "C4'"  sing N N 442 
TTP "C5'" "H5'1" sing N N 443 
TTP "C5'" "H5'2" sing N N 444 
TTP "C4'" "O4'"  sing N N 445 
TTP "C4'" "C3'"  sing N N 446 
TTP "C4'" "H4'"  sing N N 447 
TTP "O4'" "C1'"  sing N N 448 
TTP "C3'" "O3'"  sing N N 449 
TTP "C3'" "C2'"  sing N N 450 
TTP "C3'" "H3'"  sing N N 451 
TTP "O3'" "HO3'" sing N N 452 
TTP "C2'" "C1'"  sing N N 453 
TTP "C2'" "H2'1" sing N N 454 
TTP "C2'" "H2'2" sing N N 455 
TTP "C1'" N1     sing N N 456 
TTP "C1'" "H1'"  sing N N 457 
TTP N1    C2     sing N N 458 
TTP N1    C6     sing N N 459 
TTP C2    O2     doub N N 460 
TTP C2    N3     sing N N 461 
TTP N3    C4     sing N N 462 
TTP N3    HN3    sing N N 463 
TTP C4    O4     doub N N 464 
TTP C4    C5     sing N N 465 
TTP C5    C5M    sing N N 466 
TTP C5    C6     doub N N 467 
TTP C5M   HM51   sing N N 468 
TTP C5M   HM52   sing N N 469 
TTP C5M   HM53   sing N N 470 
TTP C6    H6     sing N N 471 
TYR N     CA     sing N N 472 
TYR N     H      sing N N 473 
TYR N     H2     sing N N 474 
TYR CA    C      sing N N 475 
TYR CA    CB     sing N N 476 
TYR CA    HA     sing N N 477 
TYR C     O      doub N N 478 
TYR C     OXT    sing N N 479 
TYR CB    CG     sing N N 480 
TYR CB    HB2    sing N N 481 
TYR CB    HB3    sing N N 482 
TYR CG    CD1    doub Y N 483 
TYR CG    CD2    sing Y N 484 
TYR CD1   CE1    sing Y N 485 
TYR CD1   HD1    sing N N 486 
TYR CD2   CE2    doub Y N 487 
TYR CD2   HD2    sing N N 488 
TYR CE1   CZ     doub Y N 489 
TYR CE1   HE1    sing N N 490 
TYR CE2   CZ     sing Y N 491 
TYR CE2   HE2    sing N N 492 
TYR CZ    OH     sing N N 493 
TYR OH    HH     sing N N 494 
TYR OXT   HXT    sing N N 495 
VAL N     CA     sing N N 496 
VAL N     H      sing N N 497 
VAL N     H2     sing N N 498 
VAL CA    C      sing N N 499 
VAL CA    CB     sing N N 500 
VAL CA    HA     sing N N 501 
VAL C     O      doub N N 502 
VAL C     OXT    sing N N 503 
VAL CB    CG1    sing N N 504 
VAL CB    CG2    sing N N 505 
VAL CB    HB     sing N N 506 
VAL CG1   HG11   sing N N 507 
VAL CG1   HG12   sing N N 508 
VAL CG1   HG13   sing N N 509 
VAL CG2   HG21   sing N N 510 
VAL CG2   HG22   sing N N 511 
VAL CG2   HG23   sing N N 512 
VAL OXT   HXT    sing N N 513 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-23 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BY8 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'Class 9 model for product condition of Bacillus subtilis ribonucleotide reductase complex' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          1423 
_em_entity_assembly_naturalsource.organism             'Bacillus subtilis' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       COUNTING 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    20 
_em_imaging_optics.energyfilter_name          ? 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ?               ? 
'IMAGE ACQUISITION'        ? 2  ? ? ? ?               ? 
MASKING                    ? 3  ? ? ? ?               ? 
'CTF CORRECTION'           ? 4  1 ? ? ?               ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ?               ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?               ? 
'MODEL FITTING'            ? 7  ? 1 ? 'UCSF ChimeraX' ? 
OTHER                      ? 8  ? ? ? ?               ? 
'INITIAL EULER ASSIGNMENT' ? 9  1 ? ? RELION          ? 
'FINAL EULER ASSIGNMENT'   ? 10 1 ? ? RELION          ? 
CLASSIFICATION             ? 11 1 ? ? ?               ? 
RECONSTRUCTION             ? 12 1 ? ? RELION          ? 
'MODEL REFINEMENT'         ? 13 ? 1 ? ?               ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)' 'United States' MCB-1942668 1 
'National Science Foundation (NSF, United States)' 'United States' DMR-1719875 2 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
1 'experimental model' PDB 9BY1 
2 'experimental model' PDB 4DR0 
# 
_atom_sites.entry_id                    9BY8 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
MN 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . VAL A 1 6   ? 104.361 118.126 97.268  1.00 63.04 ?  6   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 6   ? 105.670 118.642 96.893  1.00 62.74 ?  6   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 6   ? 105.498 119.830 95.945  1.00 63.36 ?  6   VAL A C     1 
ATOM   4     O  O     . VAL A 1 6   ? 104.601 119.833 95.098  1.00 63.20 ?  6   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 6   ? 106.550 117.522 96.271  1.00 64.24 ?  6   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 6   ? 106.296 117.370 94.775  1.00 62.93 ?  6   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 6   ? 108.022 117.773 96.549  1.00 61.49 ?  6   VAL A CG2   1 
ATOM   8     N  N     . PRO A 1 7   ? 106.319 120.866 96.123  1.00 58.77 ?  7   PRO A N     1 
ATOM   9     C  CA    . PRO A 1 7   ? 106.281 121.996 95.189  1.00 54.02 ?  7   PRO A CA    1 
ATOM   10    C  C     . PRO A 1 7   ? 106.657 121.557 93.784  1.00 56.48 ?  7   PRO A C     1 
ATOM   11    O  O     . PRO A 1 7   ? 107.491 120.671 93.587  1.00 60.50 ?  7   PRO A O     1 
ATOM   12    C  CB    . PRO A 1 7   ? 107.312 122.969 95.768  1.00 55.37 ?  7   PRO A CB    1 
ATOM   13    C  CG    . PRO A 1 7   ? 107.360 122.636 97.216  1.00 57.08 ?  7   PRO A CG    1 
ATOM   14    C  CD    . PRO A 1 7   ? 107.170 121.148 97.290  1.00 57.20 ?  7   PRO A CD    1 
ATOM   15    N  N     . LYS A 1 8   ? 106.021 122.188 92.796  1.00 58.03 ?  8   LYS A N     1 
ATOM   16    C  CA    . LYS A 1 8   ? 106.283 121.828 91.407  1.00 56.12 ?  8   LYS A CA    1 
ATOM   17    C  C     . LYS A 1 8   ? 107.712 122.166 91.007  1.00 57.08 ?  8   LYS A C     1 
ATOM   18    O  O     . LYS A 1 8   ? 108.350 121.416 90.259  1.00 57.57 ?  8   LYS A O     1 
ATOM   19    C  CB    . LYS A 1 8   ? 105.289 122.531 90.483  1.00 55.64 ?  8   LYS A CB    1 
ATOM   20    C  CG    . LYS A 1 8   ? 105.147 121.870 89.123  1.00 56.25 ?  8   LYS A CG    1 
ATOM   21    C  CD    . LYS A 1 8   ? 104.906 122.894 88.030  1.00 57.80 ?  8   LYS A CD    1 
ATOM   22    C  CE    . LYS A 1 8   ? 105.119 122.289 86.654  1.00 57.13 ?  8   LYS A CE    1 
ATOM   23    N  NZ    . LYS A 1 8   ? 105.641 123.290 85.684  1.00 58.95 1  8   LYS A NZ    1 
ATOM   24    N  N     . TRP A 1 9   ? 108.231 123.294 91.494  1.00 57.42 ?  9   TRP A N     1 
ATOM   25    C  CA    . TRP A 1 9   ? 109.556 123.732 91.072  1.00 52.16 ?  9   TRP A CA    1 
ATOM   26    C  C     . TRP A 1 9   ? 110.650 122.839 91.642  1.00 54.06 ?  9   TRP A C     1 
ATOM   27    O  O     . TRP A 1 9   ? 111.631 122.543 90.950  1.00 57.94 ?  9   TRP A O     1 
ATOM   28    C  CB    . TRP A 1 9   ? 109.781 125.191 91.461  1.00 53.77 ?  9   TRP A CB    1 
ATOM   29    C  CG    . TRP A 1 9   ? 109.464 125.523 92.879  1.00 50.50 ?  9   TRP A CG    1 
ATOM   30    C  CD1   . TRP A 1 9   ? 110.302 125.427 93.945  1.00 51.38 ?  9   TRP A CD1   1 
ATOM   31    C  CD2   . TRP A 1 9   ? 108.223 126.020 93.387  1.00 51.33 ?  9   TRP A CD2   1 
ATOM   32    N  NE1   . TRP A 1 9   ? 109.661 125.826 95.091  1.00 52.90 ?  9   TRP A NE1   1 
ATOM   33    C  CE2   . TRP A 1 9   ? 108.381 126.197 94.775  1.00 52.26 ?  9   TRP A CE2   1 
ATOM   34    C  CE3   . TRP A 1 9   ? 106.992 126.330 92.804  1.00 51.69 ?  9   TRP A CE3   1 
ATOM   35    C  CZ2   . TRP A 1 9   ? 107.357 126.668 95.588  1.00 52.47 ?  9   TRP A CZ2   1 
ATOM   36    C  CZ3   . TRP A 1 9   ? 105.978 126.797 93.611  1.00 55.31 ?  9   TRP A CZ3   1 
ATOM   37    C  CH2   . TRP A 1 9   ? 106.165 126.963 94.988  1.00 54.90 ?  9   TRP A CH2   1 
ATOM   38    N  N     . ILE A 1 10  ? 110.509 122.391 92.893  1.00 54.45 ?  10  ILE A N     1 
ATOM   39    C  CA    . ILE A 1 10  ? 111.508 121.470 93.426  1.00 57.23 ?  10  ILE A CA    1 
ATOM   40    C  C     . ILE A 1 10  ? 111.329 120.066 92.868  1.00 55.75 ?  10  ILE A C     1 
ATOM   41    O  O     . ILE A 1 10  ? 112.290 119.287 92.856  1.00 59.01 ?  10  ILE A O     1 
ATOM   42    C  CB    . ILE A 1 10  ? 111.509 121.409 94.965  1.00 56.46 ?  10  ILE A CB    1 
ATOM   43    C  CG1   . ILE A 1 10  ? 110.537 120.350 95.483  1.00 58.14 ?  10  ILE A CG1   1 
ATOM   44    C  CG2   . ILE A 1 10  ? 111.199 122.761 95.570  1.00 55.14 ?  10  ILE A CG2   1 
ATOM   45    C  CD1   . ILE A 1 10  ? 110.739 120.024 96.941  1.00 58.28 ?  10  ILE A CD1   1 
ATOM   46    N  N     . GLN A 1 11  ? 110.127 119.716 92.409  1.00 57.10 ?  11  GLN A N     1 
ATOM   47    C  CA    . GLN A 1 11  ? 109.959 118.454 91.699  1.00 57.23 ?  11  GLN A CA    1 
ATOM   48    C  C     . GLN A 1 11  ? 110.669 118.493 90.352  1.00 56.41 ?  11  GLN A C     1 
ATOM   49    O  O     . GLN A 1 11  ? 111.330 117.525 89.964  1.00 58.51 ?  11  GLN A O     1 
ATOM   50    C  CB    . GLN A 1 11  ? 108.473 118.142 91.528  1.00 59.25 ?  11  GLN A CB    1 
ATOM   51    C  CG    . GLN A 1 11  ? 108.175 117.045 90.526  1.00 60.60 ?  11  GLN A CG    1 
ATOM   52    C  CD    . GLN A 1 11  ? 107.389 117.551 89.334  1.00 61.60 ?  11  GLN A CD    1 
ATOM   53    O  OE1   . GLN A 1 11  ? 106.397 118.261 89.488  1.00 60.15 ?  11  GLN A OE1   1 
ATOM   54    N  NE2   . GLN A 1 11  ? 107.833 117.189 88.136  1.00 60.38 ?  11  GLN A NE2   1 
ATOM   55    N  N     . LEU A 1 12  ? 110.550 119.613 89.634  1.00 56.36 ?  12  LEU A N     1 
ATOM   56    C  CA    . LEU A 1 12  ? 111.284 119.783 88.384  1.00 55.06 ?  12  LEU A CA    1 
ATOM   57    C  C     . LEU A 1 12  ? 112.787 119.832 88.629  1.00 57.48 ?  12  LEU A C     1 
ATOM   58    O  O     . LEU A 1 12  ? 113.572 119.316 87.825  1.00 59.89 ?  12  LEU A O     1 
ATOM   59    C  CB    . LEU A 1 12  ? 110.820 121.052 87.674  1.00 55.96 ?  12  LEU A CB    1 
ATOM   60    C  CG    . LEU A 1 12  ? 109.722 120.906 86.622  1.00 56.90 ?  12  LEU A CG    1 
ATOM   61    C  CD1   . LEU A 1 12  ? 108.959 122.211 86.474  1.00 55.45 ?  12  LEU A CD1   1 
ATOM   62    C  CD2   . LEU A 1 12  ? 110.312 120.473 85.292  1.00 57.52 ?  12  LEU A CD2   1 
ATOM   63    N  N     . ASN A 1 13  ? 113.206 120.461 89.729  1.00 56.01 ?  13  ASN A N     1 
ATOM   64    C  CA    . ASN A 1 13  ? 114.626 120.567 90.040  1.00 52.82 ?  13  ASN A CA    1 
ATOM   65    C  C     . ASN A 1 13  ? 115.229 119.212 90.384  1.00 54.86 ?  13  ASN A C     1 
ATOM   66    O  O     . ASN A 1 13  ? 116.429 119.000 90.182  1.00 60.62 ?  13  ASN A O     1 
ATOM   67    C  CB    . ASN A 1 13  ? 114.831 121.553 91.191  1.00 56.25 ?  13  ASN A CB    1 
ATOM   68    C  CG    . ASN A 1 13  ? 116.276 121.642 91.633  1.00 56.13 ?  13  ASN A CG    1 
ATOM   69    O  OD1   . ASN A 1 13  ? 116.660 121.071 92.653  1.00 54.72 ?  13  ASN A OD1   1 
ATOM   70    N  ND2   . ASN A 1 13  ? 117.086 122.363 90.868  1.00 55.92 ?  13  ASN A ND2   1 
ATOM   71    N  N     . ASN A 1 14  ? 114.420 118.287 90.900  1.00 57.72 ?  14  ASN A N     1 
ATOM   72    C  CA    . ASN A 1 14  ? 114.903 116.948 91.208  1.00 58.51 ?  14  ASN A CA    1 
ATOM   73    C  C     . ASN A 1 14  ? 115.000 116.057 89.977  1.00 57.77 ?  14  ASN A C     1 
ATOM   74    O  O     . ASN A 1 14  ? 115.587 114.975 90.063  1.00 60.03 ?  14  ASN A O     1 
ATOM   75    C  CB    . ASN A 1 14  ? 114.000 116.289 92.253  1.00 56.46 ?  14  ASN A CB    1 
ATOM   76    C  CG    . ASN A 1 14  ? 114.248 116.817 93.650  1.00 58.69 ?  14  ASN A CG    1 
ATOM   77    O  OD1   . ASN A 1 14  ? 114.576 117.988 93.833  1.00 60.90 ?  14  ASN A OD1   1 
ATOM   78    N  ND2   . ASN A 1 14  ? 114.090 115.954 94.646  1.00 59.30 ?  14  ASN A ND2   1 
ATOM   79    N  N     . GLU A 1 15  ? 114.446 116.481 88.842  1.00 57.87 ?  15  GLU A N     1 
ATOM   80    C  CA    . GLU A 1 15  ? 114.577 115.731 87.601  1.00 59.07 ?  15  GLU A CA    1 
ATOM   81    C  C     . GLU A 1 15  ? 115.944 115.903 86.952  1.00 61.72 ?  15  GLU A C     1 
ATOM   82    O  O     . GLU A 1 15  ? 116.208 115.266 85.927  1.00 63.52 ?  15  GLU A O     1 
ATOM   83    C  CB    . GLU A 1 15  ? 113.480 116.142 86.613  1.00 59.34 ?  15  GLU A CB    1 
ATOM   84    C  CG    . GLU A 1 15  ? 112.099 116.240 87.232  1.00 60.15 ?  15  GLU A CG    1 
ATOM   85    C  CD    . GLU A 1 15  ? 110.989 116.243 86.200  1.00 63.73 ?  15  GLU A CD    1 
ATOM   86    O  OE1   . GLU A 1 15  ? 111.293 116.368 84.997  1.00 63.57 ?  15  GLU A OE1   1 
ATOM   87    O  OE2   . GLU A 1 15  ? 109.810 116.121 86.594  1.00 63.84 -1 15  GLU A OE2   1 
ATOM   88    N  N     . ILE A 1 16  ? 116.805 116.754 87.514  1.00 59.98 ?  16  ILE A N     1 
ATOM   89    C  CA    . ILE A 1 16  ? 118.173 116.866 87.015  1.00 59.72 ?  16  ILE A CA    1 
ATOM   90    C  C     . ILE A 1 16  ? 118.920 115.557 87.223  1.00 59.78 ?  16  ILE A C     1 
ATOM   91    O  O     . ILE A 1 16  ? 119.647 115.090 86.338  1.00 61.09 ?  16  ILE A O     1 
ATOM   92    C  CB    . ILE A 1 16  ? 118.896 118.043 87.696  1.00 58.93 ?  16  ILE A CB    1 
ATOM   93    C  CG1   . ILE A 1 16  ? 118.165 119.357 87.420  1.00 57.54 ?  16  ILE A CG1   1 
ATOM   94    C  CG2   . ILE A 1 16  ? 120.341 118.131 87.227  1.00 59.58 ?  16  ILE A CG2   1 
ATOM   95    C  CD1   . ILE A 1 16  ? 118.646 120.509 88.270  1.00 56.90 ?  16  ILE A CD1   1 
ATOM   96    N  N     . MET A 1 17  ? 118.747 114.940 88.393  1.00 60.50 ?  17  MET A N     1 
ATOM   97    C  CA    . MET A 1 17  ? 119.465 113.716 88.719  1.00 61.98 ?  17  MET A CA    1 
ATOM   98    C  C     . MET A 1 17  ? 118.901 112.490 88.017  1.00 62.80 ?  17  MET A C     1 
ATOM   99    O  O     . MET A 1 17  ? 119.602 111.478 87.914  1.00 63.98 ?  17  MET A O     1 
ATOM   100   C  CB    . MET A 1 17  ? 119.452 113.493 90.230  1.00 61.29 ?  17  MET A CB    1 
ATOM   101   C  CG    . MET A 1 17  ? 119.899 114.703 91.015  1.00 61.55 ?  17  MET A CG    1 
ATOM   102   S  SD    . MET A 1 17  ? 121.438 115.412 90.397  1.00 68.12 ?  17  MET A SD    1 
ATOM   103   C  CE    . MET A 1 17  ? 122.644 114.406 91.257  1.00 61.05 ?  17  MET A CE    1 
ATOM   104   N  N     . ILE A 1 18  ? 117.660 112.548 87.538  1.00 62.62 ?  18  ILE A N     1 
ATOM   105   C  CA    . ILE A 1 18  ? 117.106 111.442 86.763  1.00 64.44 ?  18  ILE A CA    1 
ATOM   106   C  C     . ILE A 1 18  ? 117.851 111.403 85.432  1.00 65.28 ?  18  ILE A C     1 
ATOM   107   O  O     . ILE A 1 18  ? 117.660 112.271 84.575  1.00 66.44 ?  18  ILE A O     1 
ATOM   108   C  CB    . ILE A 1 18  ? 115.590 111.576 86.557  1.00 65.30 ?  18  ILE A CB    1 
ATOM   109   C  CG1   . ILE A 1 18  ? 114.775 111.271 87.832  1.00 64.60 ?  18  ILE A CG1   1 
ATOM   110   C  CG2   . ILE A 1 18  ? 115.119 110.655 85.437  1.00 64.87 ?  18  ILE A CG2   1 
ATOM   111   C  CD1   . ILE A 1 18  ? 115.217 111.921 89.129  1.00 64.07 ?  18  ILE A CD1   1 
ATOM   112   N  N     . GLN A 1 19  ? 118.716 110.408 85.266  1.00 68.96 ?  19  GLN A N     1 
ATOM   113   C  CA    . GLN A 1 19  ? 119.588 110.339 84.102  1.00 70.00 ?  19  GLN A CA    1 
ATOM   114   C  C     . GLN A 1 19  ? 118.813 109.793 82.910  1.00 69.78 ?  19  GLN A C     1 
ATOM   115   O  O     . GLN A 1 19  ? 118.393 108.631 82.911  1.00 71.76 ?  19  GLN A O     1 
ATOM   116   C  CB    . GLN A 1 19  ? 120.806 109.469 84.401  1.00 72.02 ?  19  GLN A CB    1 
ATOM   117   C  CG    . GLN A 1 19  ? 121.764 110.081 85.413  1.00 70.29 ?  19  GLN A CG    1 
ATOM   118   C  CD    . GLN A 1 19  ? 122.990 109.222 85.652  1.00 71.59 ?  19  GLN A CD    1 
ATOM   119   O  OE1   . GLN A 1 19  ? 123.134 108.148 85.070  1.00 71.28 ?  19  GLN A OE1   1 
ATOM   120   N  NE2   . GLN A 1 19  ? 123.882 109.694 86.516  1.00 71.39 ?  19  GLN A NE2   1 
ATOM   121   N  N     . LYS A 1 20  ? 118.623 110.633 81.897  1.00 71.28 ?  20  LYS A N     1 
ATOM   122   C  CA    . LYS A 1 20  ? 117.951 110.252 80.664  1.00 73.11 ?  20  LYS A CA    1 
ATOM   123   C  C     . LYS A 1 20  ? 118.997 110.135 79.564  1.00 73.64 ?  20  LYS A C     1 
ATOM   124   O  O     . LYS A 1 20  ? 119.740 111.089 79.310  1.00 73.55 ?  20  LYS A O     1 
ATOM   125   C  CB    . LYS A 1 20  ? 116.875 111.270 80.289  1.00 71.82 ?  20  LYS A CB    1 
ATOM   126   C  CG    . LYS A 1 20  ? 116.284 111.069 78.904  1.00 72.49 ?  20  LYS A CG    1 
ATOM   127   C  CD    . LYS A 1 20  ? 116.095 112.395 78.188  1.00 73.53 ?  20  LYS A CD    1 
ATOM   128   C  CE    . LYS A 1 20  ? 117.356 113.241 78.248  1.00 73.84 ?  20  LYS A CE    1 
ATOM   129   N  NZ    . LYS A 1 20  ? 118.508 112.568 77.590  1.00 73.93 1  20  LYS A NZ    1 
ATOM   130   N  N     . ASP A 1 21  ? 119.050 108.967 78.922  1.00 72.18 ?  21  ASP A N     1 
ATOM   131   C  CA    . ASP A 1 21  ? 120.040 108.674 77.884  1.00 73.50 ?  21  ASP A CA    1 
ATOM   132   C  C     . ASP A 1 21  ? 121.464 108.814 78.420  1.00 74.05 ?  21  ASP A C     1 
ATOM   133   O  O     . ASP A 1 21  ? 122.372 109.258 77.715  1.00 72.09 ?  21  ASP A O     1 
ATOM   134   C  CB    . ASP A 1 21  ? 119.832 109.558 76.652  1.00 73.43 ?  21  ASP A CB    1 
ATOM   135   C  CG    . ASP A 1 21  ? 118.378 109.634 76.230  1.00 74.57 ?  21  ASP A CG    1 
ATOM   136   O  OD1   . ASP A 1 21  ? 117.676 108.605 76.318  1.00 72.61 ?  21  ASP A OD1   1 
ATOM   137   O  OD2   . ASP A 1 21  ? 117.937 110.726 75.812  1.00 74.27 -1 21  ASP A OD2   1 
ATOM   138   N  N     . GLY A 1 22  ? 121.659 108.432 79.680  1.00 73.98 ?  22  GLY A N     1 
ATOM   139   C  CA    . GLY A 1 22  ? 122.977 108.442 80.283  1.00 74.01 ?  22  GLY A CA    1 
ATOM   140   C  C     . GLY A 1 22  ? 123.511 109.804 80.663  1.00 73.96 ?  22  GLY A C     1 
ATOM   141   O  O     . GLY A 1 22  ? 124.700 109.914 80.982  1.00 72.73 ?  22  GLY A O     1 
ATOM   142   N  N     . LYS A 1 23  ? 122.679 110.843 80.644  1.00 70.77 ?  23  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 23  ? 123.114 112.195 80.957  1.00 68.48 ?  23  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 23  ? 122.171 112.828 81.967  1.00 69.58 ?  23  LYS A C     1 
ATOM   145   O  O     . LYS A 1 23  ? 120.973 112.532 81.992  1.00 70.55 ?  23  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 23  ? 123.172 113.074 79.700  1.00 68.39 ?  23  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 23  ? 124.262 112.700 78.713  1.00 68.46 ?  23  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 23  ? 124.286 113.681 77.552  1.00 68.57 ?  23  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 23  ? 125.289 113.271 76.491  1.00 68.95 ?  23  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 23  ? 125.263 114.199 75.327  1.00 67.63 1  23  LYS A NZ    1 
ATOM   151   N  N     . PHE A 1 24  ? 122.726 113.702 82.802  1.00 63.30 ?  24  PHE A N     1 
ATOM   152   C  CA    . PHE A 1 24  ? 121.905 114.499 83.701  1.00 60.09 ?  24  PHE A CA    1 
ATOM   153   C  C     . PHE A 1 24  ? 121.036 115.460 82.901  1.00 60.84 ?  24  PHE A C     1 
ATOM   154   O  O     . PHE A 1 24  ? 121.473 116.030 81.899  1.00 59.40 ?  24  PHE A O     1 
ATOM   155   C  CB    . PHE A 1 24  ? 122.782 115.284 84.676  1.00 58.54 ?  24  PHE A CB    1 
ATOM   156   C  CG    . PHE A 1 24  ? 123.440 114.435 85.722  1.00 59.92 ?  24  PHE A CG    1 
ATOM   157   C  CD1   . PHE A 1 24  ? 122.760 114.083 86.874  1.00 60.45 ?  24  PHE A CD1   1 
ATOM   158   C  CD2   . PHE A 1 24  ? 124.741 113.994 85.555  1.00 59.89 ?  24  PHE A CD2   1 
ATOM   159   C  CE1   . PHE A 1 24  ? 123.366 113.304 87.839  1.00 60.18 ?  24  PHE A CE1   1 
ATOM   160   C  CE2   . PHE A 1 24  ? 125.351 113.216 86.517  1.00 59.21 ?  24  PHE A CE2   1 
ATOM   161   C  CZ    . PHE A 1 24  ? 124.662 112.870 87.660  1.00 60.10 ?  24  PHE A CZ    1 
ATOM   162   N  N     . GLN A 1 25  ? 119.794 115.637 83.350  1.00 61.85 ?  25  GLN A N     1 
ATOM   163   C  CA    . GLN A 1 25  ? 118.863 116.555 82.695  1.00 59.76 ?  25  GLN A CA    1 
ATOM   164   C  C     . GLN A 1 25  ? 119.089 117.949 83.271  1.00 60.95 ?  25  GLN A C     1 
ATOM   165   O  O     . GLN A 1 25  ? 118.374 118.421 84.157  1.00 61.19 ?  25  GLN A O     1 
ATOM   166   C  CB    . GLN A 1 25  ? 117.426 116.084 82.876  1.00 61.01 ?  25  GLN A CB    1 
ATOM   167   C  CG    . GLN A 1 25  ? 117.161 114.690 82.337  1.00 61.65 ?  25  GLN A CG    1 
ATOM   168   C  CD    . GLN A 1 25  ? 115.709 114.283 82.470  1.00 62.47 ?  25  GLN A CD    1 
ATOM   169   O  OE1   . GLN A 1 25  ? 114.895 114.550 81.586  1.00 62.18 ?  25  GLN A OE1   1 
ATOM   170   N  NE2   . GLN A 1 25  ? 115.376 113.631 83.577  1.00 60.78 ?  25  GLN A NE2   1 
ATOM   171   N  N     . PHE A 1 26  ? 120.119 118.616 82.746  1.00 57.38 ?  26  PHE A N     1 
ATOM   172   C  CA    . PHE A 1 26  ? 120.490 119.931 83.257  1.00 55.95 ?  26  PHE A CA    1 
ATOM   173   C  C     . PHE A 1 26  ? 119.466 120.994 82.884  1.00 57.41 ?  26  PHE A C     1 
ATOM   174   O  O     . PHE A 1 26  ? 119.306 121.978 83.614  1.00 56.88 ?  26  PHE A O     1 
ATOM   175   C  CB    . PHE A 1 26  ? 121.874 120.322 82.739  1.00 53.29 ?  26  PHE A CB    1 
ATOM   176   C  CG    . PHE A 1 26  ? 122.990 119.511 83.331  1.00 54.17 ?  26  PHE A CG    1 
ATOM   177   C  CD1   . PHE A 1 26  ? 123.159 119.438 84.703  1.00 54.44 ?  26  PHE A CD1   1 
ATOM   178   C  CD2   . PHE A 1 26  ? 123.869 118.820 82.517  1.00 55.39 ?  26  PHE A CD2   1 
ATOM   179   C  CE1   . PHE A 1 26  ? 124.183 118.692 85.249  1.00 53.11 ?  26  PHE A CE1   1 
ATOM   180   C  CE2   . PHE A 1 26  ? 124.895 118.074 83.059  1.00 54.08 ?  26  PHE A CE2   1 
ATOM   181   C  CZ    . PHE A 1 26  ? 125.052 118.010 84.427  1.00 51.66 ?  26  PHE A CZ    1 
ATOM   182   N  N     . ASP A 1 27  ? 118.766 120.819 81.761  1.00 62.63 ?  27  ASP A N     1 
ATOM   183   C  CA    . ASP A 1 27  ? 117.768 121.790 81.330  1.00 61.91 ?  27  ASP A CA    1 
ATOM   184   C  C     . ASP A 1 27  ? 116.554 121.840 82.247  1.00 62.06 ?  27  ASP A C     1 
ATOM   185   O  O     . ASP A 1 27  ? 115.743 122.764 82.118  1.00 62.82 ?  27  ASP A O     1 
ATOM   186   C  CB    . ASP A 1 27  ? 117.320 121.484 79.901  1.00 61.74 ?  27  ASP A CB    1 
ATOM   187   C  CG    . ASP A 1 27  ? 117.295 122.718 79.021  1.00 65.25 ?  27  ASP A CG    1 
ATOM   188   O  OD1   . ASP A 1 27  ? 117.297 122.568 77.781  1.00 66.74 ?  27  ASP A OD1   1 
ATOM   189   O  OD2   . ASP A 1 27  ? 117.272 123.839 79.570  1.00 65.33 -1 27  ASP A OD2   1 
ATOM   190   N  N     . LYS A 1 28  ? 116.402 120.874 83.154  1.00 58.49 ?  28  LYS A N     1 
ATOM   191   C  CA    . LYS A 1 28  ? 115.278 120.903 84.082  1.00 59.07 ?  28  LYS A CA    1 
ATOM   192   C  C     . LYS A 1 28  ? 115.367 122.084 85.038  1.00 59.76 ?  28  LYS A C     1 
ATOM   193   O  O     . LYS A 1 28  ? 114.335 122.563 85.523  1.00 62.05 ?  28  LYS A O     1 
ATOM   194   C  CB    . LYS A 1 28  ? 115.210 119.594 84.868  1.00 58.92 ?  28  LYS A CB    1 
ATOM   195   C  CG    . LYS A 1 28  ? 114.877 118.385 84.018  1.00 60.16 ?  28  LYS A CG    1 
ATOM   196   C  CD    . LYS A 1 28  ? 113.420 118.394 83.595  1.00 61.07 ?  28  LYS A CD    1 
ATOM   197   C  CE    . LYS A 1 28  ? 113.152 117.347 82.529  1.00 60.92 ?  28  LYS A CE    1 
ATOM   198   N  NZ    . LYS A 1 28  ? 111.704 117.249 82.204  1.00 61.66 1  28  LYS A NZ    1 
ATOM   199   N  N     . ASP A 1 29  ? 116.580 122.565 85.324  1.00 56.42 ?  29  ASP A N     1 
ATOM   200   C  CA    . ASP A 1 29  ? 116.732 123.681 86.249  1.00 54.47 ?  29  ASP A CA    1 
ATOM   201   C  C     . ASP A 1 29  ? 116.179 124.975 85.667  1.00 53.46 ?  29  ASP A C     1 
ATOM   202   O  O     . ASP A 1 29  ? 115.713 125.839 86.419  1.00 55.08 ?  29  ASP A O     1 
ATOM   203   C  CB    . ASP A 1 29  ? 118.200 123.851 86.631  1.00 52.84 ?  29  ASP A CB    1 
ATOM   204   C  CG    . ASP A 1 29  ? 118.394 124.033 88.121  1.00 56.37 ?  29  ASP A CG    1 
ATOM   205   O  OD1   . ASP A 1 29  ? 117.516 123.594 88.892  1.00 56.68 ?  29  ASP A OD1   1 
ATOM   206   O  OD2   . ASP A 1 29  ? 119.427 124.605 88.524  1.00 55.59 -1 29  ASP A OD2   1 
ATOM   207   N  N     . LYS A 1 30  ? 116.232 125.135 84.344  1.00 54.13 ?  30  LYS A N     1 
ATOM   208   C  CA    . LYS A 1 30  ? 115.565 126.269 83.713  1.00 56.39 ?  30  LYS A CA    1 
ATOM   209   C  C     . LYS A 1 30  ? 114.054 126.162 83.874  1.00 55.12 ?  30  LYS A C     1 
ATOM   210   O  O     . LYS A 1 30  ? 113.382 127.137 84.236  1.00 59.35 ?  30  LYS A O     1 
ATOM   211   C  CB    . LYS A 1 30  ? 115.950 126.347 82.236  1.00 55.60 ?  30  LYS A CB    1 
ATOM   212   C  CG    . LYS A 1 30  ? 115.352 127.529 81.496  1.00 57.24 ?  30  LYS A CG    1 
ATOM   213   C  CD    . LYS A 1 30  ? 116.351 128.131 80.522  1.00 57.04 ?  30  LYS A CD    1 
ATOM   214   C  CE    . LYS A 1 30  ? 115.777 129.353 79.826  1.00 57.35 ?  30  LYS A CE    1 
ATOM   215   N  NZ    . LYS A 1 30  ? 115.273 129.027 78.463  1.00 56.39 1  30  LYS A NZ    1 
ATOM   216   N  N     . GLU A 1 31  ? 113.503 124.972 83.626  1.00 52.94 ?  31  GLU A N     1 
ATOM   217   C  CA    . GLU A 1 31  ? 112.090 124.746 83.898  1.00 53.56 ?  31  GLU A CA    1 
ATOM   218   C  C     . GLU A 1 31  ? 111.799 124.869 85.386  1.00 54.66 ?  31  GLU A C     1 
ATOM   219   O  O     . GLU A 1 31  ? 110.737 125.364 85.780  1.00 56.52 ?  31  GLU A O     1 
ATOM   220   C  CB    . GLU A 1 31  ? 111.667 123.373 83.378  1.00 55.25 ?  31  GLU A CB    1 
ATOM   221   C  CG    . GLU A 1 31  ? 111.208 123.370 81.932  1.00 56.83 ?  31  GLU A CG    1 
ATOM   222   C  CD    . GLU A 1 31  ? 111.518 122.067 81.225  1.00 60.89 ?  31  GLU A CD    1 
ATOM   223   O  OE1   . GLU A 1 31  ? 112.237 121.230 81.809  1.00 60.98 ?  31  GLU A OE1   1 
ATOM   224   O  OE2   . GLU A 1 31  ? 111.042 121.878 80.086  1.00 58.42 -1 31  GLU A OE2   1 
ATOM   225   N  N     . ALA A 1 32  ? 112.736 124.431 86.229  1.00 50.02 ?  32  ALA A N     1 
ATOM   226   C  CA    . ALA A 1 32  ? 112.541 124.538 87.670  1.00 49.58 ?  32  ALA A CA    1 
ATOM   227   C  C     . ALA A 1 32  ? 112.417 125.991 88.106  1.00 52.01 ?  32  ALA A C     1 
ATOM   228   O  O     . ALA A 1 32  ? 111.520 126.335 88.880  1.00 51.91 ?  32  ALA A O     1 
ATOM   229   C  CB    . ALA A 1 32  ? 113.687 123.853 88.412  1.00 48.80 ?  32  ALA A CB    1 
ATOM   230   N  N     . VAL A 1 33  ? 113.294 126.864 87.607  1.00 53.52 ?  33  VAL A N     1 
ATOM   231   C  CA    . VAL A 1 33  ? 113.235 128.268 88.005  1.00 52.03 ?  33  VAL A CA    1 
ATOM   232   C  C     . VAL A 1 33  ? 112.028 128.959 87.376  1.00 52.95 ?  33  VAL A C     1 
ATOM   233   O  O     . VAL A 1 33  ? 111.407 129.832 87.995  1.00 54.60 ?  33  VAL A O     1 
ATOM   234   C  CB    . VAL A 1 33  ? 114.558 128.986 87.673  1.00 49.44 ?  33  VAL A CB    1 
ATOM   235   C  CG1   . VAL A 1 33  ? 114.722 129.202 86.179  1.00 51.09 ?  33  VAL A CG1   1 
ATOM   236   C  CG2   . VAL A 1 33  ? 114.643 130.309 88.415  1.00 49.46 ?  33  VAL A CG2   1 
ATOM   237   N  N     . HIS A 1 34  ? 111.666 128.575 86.149  1.00 50.73 ?  34  HIS A N     1 
ATOM   238   C  CA    . HIS A 1 34  ? 110.481 129.149 85.519  1.00 50.74 ?  34  HIS A CA    1 
ATOM   239   C  C     . HIS A 1 34  ? 109.229 128.816 86.326  1.00 52.66 ?  34  HIS A C     1 
ATOM   240   O  O     . HIS A 1 34  ? 108.391 129.689 86.592  1.00 53.04 ?  34  HIS A O     1 
ATOM   241   C  CB    . HIS A 1 34  ? 110.374 128.638 84.079  1.00 53.19 ?  34  HIS A CB    1 
ATOM   242   C  CG    . HIS A 1 34  ? 109.284 129.278 83.270  1.00 55.22 ?  34  HIS A CG    1 
ATOM   243   N  ND1   . HIS A 1 34  ? 108.041 129.578 83.783  1.00 54.82 ?  34  HIS A ND1   1 
ATOM   244   C  CD2   . HIS A 1 34  ? 109.262 129.675 81.977  1.00 54.74 ?  34  HIS A CD2   1 
ATOM   245   C  CE1   . HIS A 1 34  ? 107.298 130.128 82.839  1.00 55.21 ?  34  HIS A CE1   1 
ATOM   246   N  NE2   . HIS A 1 34  ? 108.018 130.202 81.734  1.00 55.54 ?  34  HIS A NE2   1 
ATOM   247   N  N     . SER A 1 35  ? 109.096 127.550 86.735  1.00 54.59 ?  35  SER A N     1 
ATOM   248   C  CA    . SER A 1 35  ? 107.973 127.151 87.573  1.00 51.97 ?  35  SER A CA    1 
ATOM   249   C  C     . SER A 1 35  ? 108.034 127.830 88.933  1.00 52.12 ?  35  SER A C     1 
ATOM   250   O  O     . SER A 1 35  ? 107.005 128.269 89.459  1.00 54.74 ?  35  SER A O     1 
ATOM   251   C  CB    . SER A 1 35  ? 107.953 125.632 87.735  1.00 51.86 ?  35  SER A CB    1 
ATOM   252   O  OG    . SER A 1 35  ? 107.159 125.253 88.844  1.00 54.09 ?  35  SER A OG    1 
ATOM   253   N  N     . TYR A 1 36  ? 109.231 127.927 89.517  1.00 51.70 ?  36  TYR A N     1 
ATOM   254   C  CA    . TYR A 1 36  ? 109.392 128.610 90.794  1.00 51.33 ?  36  TYR A CA    1 
ATOM   255   C  C     . TYR A 1 36  ? 108.834 130.018 90.722  1.00 48.41 ?  36  TYR A C     1 
ATOM   256   O  O     . TYR A 1 36  ? 108.016 130.418 91.556  1.00 48.38 ?  36  TYR A O     1 
ATOM   257   C  CB    . TYR A 1 36  ? 110.869 128.636 91.188  1.00 47.92 ?  36  TYR A CB    1 
ATOM   258   C  CG    . TYR A 1 36  ? 111.166 129.408 92.453  1.00 49.41 ?  36  TYR A CG    1 
ATOM   259   C  CD1   . TYR A 1 36  ? 110.601 129.038 93.666  1.00 47.81 ?  36  TYR A CD1   1 
ATOM   260   C  CD2   . TYR A 1 36  ? 112.018 130.503 92.435  1.00 48.66 ?  36  TYR A CD2   1 
ATOM   261   C  CE1   . TYR A 1 36  ? 110.876 129.738 94.822  1.00 46.14 ?  36  TYR A CE1   1 
ATOM   262   C  CE2   . TYR A 1 36  ? 112.297 131.210 93.585  1.00 46.68 ?  36  TYR A CE2   1 
ATOM   263   C  CZ    . TYR A 1 36  ? 111.724 130.823 94.775  1.00 48.10 ?  36  TYR A CZ    1 
ATOM   264   O  OH    . TYR A 1 36  ? 112.001 131.526 95.924  1.00 50.06 ?  36  TYR A OH    1 
ATOM   265   N  N     . PHE A 1 37  ? 109.219 130.764 89.689  1.00 52.38 ?  37  PHE A N     1 
ATOM   266   C  CA    . PHE A 1 37  ? 108.709 132.119 89.543  1.00 52.15 ?  37  PHE A CA    1 
ATOM   267   C  C     . PHE A 1 37  ? 107.200 132.114 89.351  1.00 53.54 ?  37  PHE A C     1 
ATOM   268   O  O     . PHE A 1 37  ? 106.462 132.584 90.222  1.00 56.56 ?  37  PHE A O     1 
ATOM   269   C  CB    . PHE A 1 37  ? 109.416 132.834 88.396  1.00 54.60 ?  37  PHE A CB    1 
ATOM   270   C  CG    . PHE A 1 37  ? 110.680 133.509 88.819  1.00 53.80 ?  37  PHE A CG    1 
ATOM   271   C  CD1   . PHE A 1 37  ? 110.642 134.756 89.415  1.00 51.23 ?  37  PHE A CD1   1 
ATOM   272   C  CD2   . PHE A 1 37  ? 111.902 132.886 88.656  1.00 53.12 ?  37  PHE A CD2   1 
ATOM   273   C  CE1   . PHE A 1 37  ? 111.799 135.377 89.821  1.00 52.41 ?  37  PHE A CE1   1 
ATOM   274   C  CE2   . PHE A 1 37  ? 113.060 133.503 89.059  1.00 52.36 ?  37  PHE A CE2   1 
ATOM   275   C  CZ    . PHE A 1 37  ? 113.010 134.748 89.645  1.00 52.98 ?  37  PHE A CZ    1 
ATOM   276   N  N     . VAL A 1 38  ? 106.721 131.498 88.264  1.00 56.41 ?  38  VAL A N     1 
ATOM   277   C  CA    . VAL A 1 38  ? 105.310 131.611 87.905  1.00 55.88 ?  38  VAL A CA    1 
ATOM   278   C  C     . VAL A 1 38  ? 104.370 130.897 88.863  1.00 55.62 ?  38  VAL A C     1 
ATOM   279   O  O     . VAL A 1 38  ? 103.150 130.985 88.686  1.00 57.68 ?  38  VAL A O     1 
ATOM   280   C  CB    . VAL A 1 38  ? 105.055 131.087 86.478  1.00 54.03 ?  38  VAL A CB    1 
ATOM   281   C  CG1   . VAL A 1 38  ? 105.991 131.763 85.494  1.00 55.29 ?  38  VAL A CG1   1 
ATOM   282   C  CG2   . VAL A 1 38  ? 105.198 129.575 86.429  1.00 52.16 ?  38  VAL A CG2   1 
ATOM   283   N  N     . ASP A 1 39  ? 104.885 130.193 89.874  1.00 54.34 ?  39  ASP A N     1 
ATOM   284   C  CA    . ASP A 1 39  ? 104.019 129.548 90.847  1.00 53.08 ?  39  ASP A CA    1 
ATOM   285   C  C     . ASP A 1 39  ? 104.199 130.037 92.275  1.00 57.49 ?  39  ASP A C     1 
ATOM   286   O  O     . ASP A 1 39  ? 103.288 129.844 93.086  1.00 61.79 ?  39  ASP A O     1 
ATOM   287   C  CB    . ASP A 1 39  ? 104.225 128.025 90.820  1.00 55.36 ?  39  ASP A CB    1 
ATOM   288   C  CG    . ASP A 1 39  ? 103.970 127.426 89.451  1.00 58.49 ?  39  ASP A CG    1 
ATOM   289   O  OD1   . ASP A 1 39  ? 103.132 127.976 88.707  1.00 59.03 ?  39  ASP A OD1   1 
ATOM   290   O  OD2   . ASP A 1 39  ? 104.603 126.402 89.118  1.00 58.25 -1 39  ASP A OD2   1 
ATOM   291   N  N     . TYR A 1 40  ? 105.332 130.650 92.616  1.00 56.20 ?  40  TYR A N     1 
ATOM   292   C  CA    . TYR A 1 40  ? 105.543 131.188 93.952  1.00 55.34 ?  40  TYR A CA    1 
ATOM   293   C  C     . TYR A 1 40  ? 105.828 132.680 93.945  1.00 59.10 ?  40  TYR A C     1 
ATOM   294   O  O     . TYR A 1 40  ? 105.217 133.427 94.717  1.00 61.95 ?  40  TYR A O     1 
ATOM   295   C  CB    . TYR A 1 40  ? 106.697 130.440 94.637  1.00 54.12 ?  40  TYR A CB    1 
ATOM   296   C  CG    . TYR A 1 40  ? 106.824 130.725 96.113  1.00 54.91 ?  40  TYR A CG    1 
ATOM   297   C  CD1   . TYR A 1 40  ? 105.794 130.419 96.991  1.00 55.80 ?  40  TYR A CD1   1 
ATOM   298   C  CD2   . TYR A 1 40  ? 107.974 131.305 96.629  1.00 55.91 ?  40  TYR A CD2   1 
ATOM   299   C  CE1   . TYR A 1 40  ? 105.908 130.680 98.342  1.00 57.94 ?  40  TYR A CE1   1 
ATOM   300   C  CE2   . TYR A 1 40  ? 108.097 131.570 97.977  1.00 58.46 ?  40  TYR A CE2   1 
ATOM   301   C  CZ    . TYR A 1 40  ? 107.061 131.257 98.829  1.00 60.69 ?  40  TYR A CZ    1 
ATOM   302   O  OH    . TYR A 1 40  ? 107.178 131.519 100.174 1.00 61.32 ?  40  TYR A OH    1 
ATOM   303   N  N     . ILE A 1 41  ? 106.730 133.140 93.078  1.00 55.06 ?  41  ILE A N     1 
ATOM   304   C  CA    . ILE A 1 41  ? 107.302 134.471 93.244  1.00 54.10 ?  41  ILE A CA    1 
ATOM   305   C  C     . ILE A 1 41  ? 106.338 135.539 92.751  1.00 53.77 ?  41  ILE A C     1 
ATOM   306   O  O     . ILE A 1 41  ? 106.037 136.500 93.467  1.00 56.11 ?  41  ILE A O     1 
ATOM   307   C  CB    . ILE A 1 41  ? 108.661 134.558 92.524  1.00 53.23 ?  41  ILE A CB    1 
ATOM   308   C  CG1   . ILE A 1 41  ? 109.675 133.621 93.181  1.00 51.97 ?  41  ILE A CG1   1 
ATOM   309   C  CG2   . ILE A 1 41  ? 109.179 135.985 92.539  1.00 52.91 ?  41  ILE A CG2   1 
ATOM   310   C  CD1   . ILE A 1 41  ? 109.948 133.933 94.628  1.00 49.09 ?  41  ILE A CD1   1 
ATOM   311   N  N     . ASN A 1 42  ? 105.835 135.386 91.524  1.00 55.14 ?  42  ASN A N     1 
ATOM   312   C  CA    . ASN A 1 42  ? 104.873 136.349 91.001  1.00 57.04 ?  42  ASN A CA    1 
ATOM   313   C  C     . ASN A 1 42  ? 103.591 136.356 91.821  1.00 60.67 ?  42  ASN A C     1 
ATOM   314   O  O     . ASN A 1 42  ? 102.909 137.384 91.899  1.00 60.98 ?  42  ASN A O     1 
ATOM   315   C  CB    . ASN A 1 42  ? 104.573 136.041 89.534  1.00 56.57 ?  42  ASN A CB    1 
ATOM   316   C  CG    . ASN A 1 42  ? 105.817 136.067 88.668  1.00 57.49 ?  42  ASN A CG    1 
ATOM   317   O  OD1   . ASN A 1 42  ? 106.858 136.579 89.075  1.00 61.31 ?  42  ASN A OD1   1 
ATOM   318   N  ND2   . ASN A 1 42  ? 105.713 135.514 87.466  1.00 57.43 ?  42  ASN A ND2   1 
ATOM   319   N  N     . GLN A 1 43  ? 103.245 135.223 92.434  1.00 62.95 ?  43  GLN A N     1 
ATOM   320   C  CA    . GLN A 1 43  ? 102.071 135.177 93.298  1.00 61.34 ?  43  GLN A CA    1 
ATOM   321   C  C     . GLN A 1 43  ? 102.320 135.908 94.611  1.00 59.55 ?  43  GLN A C     1 
ATOM   322   O  O     . GLN A 1 43  ? 101.461 136.665 95.080  1.00 62.85 ?  43  GLN A O     1 
ATOM   323   C  CB    . GLN A 1 43  ? 101.668 133.726 93.559  1.00 60.93 ?  43  GLN A CB    1 
ATOM   324   C  CG    . GLN A 1 43  ? 101.868 132.792 92.373  1.00 61.60 ?  43  GLN A CG    1 
ATOM   325   C  CD    . GLN A 1 43  ? 100.829 132.983 91.282  1.00 64.24 ?  43  GLN A CD    1 
ATOM   326   O  OE1   . GLN A 1 43  ? 100.780 134.026 90.628  1.00 62.89 ?  43  GLN A OE1   1 
ATOM   327   N  NE2   . GLN A 1 43  ? 99.995  131.971 91.079  1.00 62.68 ?  43  GLN A NE2   1 
ATOM   328   N  N     . ASN A 1 44  ? 103.488 135.702 95.217  1.00 54.88 ?  44  ASN A N     1 
ATOM   329   C  CA    . ASN A 1 44  ? 103.814 136.287 96.510  1.00 56.20 ?  44  ASN A CA    1 
ATOM   330   C  C     . ASN A 1 44  ? 104.434 137.674 96.403  1.00 56.44 ?  44  ASN A C     1 
ATOM   331   O  O     . ASN A 1 44  ? 104.786 138.257 97.433  1.00 57.09 ?  44  ASN A O     1 
ATOM   332   C  CB    . ASN A 1 44  ? 104.759 135.361 97.283  1.00 56.48 ?  44  ASN A CB    1 
ATOM   333   C  CG    . ASN A 1 44  ? 104.049 134.151 97.857  1.00 59.38 ?  44  ASN A CG    1 
ATOM   334   O  OD1   . ASN A 1 44  ? 103.674 134.136 99.028  1.00 60.88 ?  44  ASN A OD1   1 
ATOM   335   N  ND2   . ASN A 1 44  ? 103.859 133.129 97.031  1.00 58.08 ?  44  ASN A ND2   1 
ATOM   336   N  N     . THR A 1 45  ? 104.581 138.212 95.197  1.00 58.13 ?  45  THR A N     1 
ATOM   337   C  CA    . THR A 1 45  ? 105.158 139.535 95.008  1.00 59.07 ?  45  THR A CA    1 
ATOM   338   C  C     . THR A 1 45  ? 104.080 140.600 95.146  1.00 59.02 ?  45  THR A C     1 
ATOM   339   O  O     . THR A 1 45  ? 103.041 140.531 94.481  1.00 60.05 ?  45  THR A O     1 
ATOM   340   C  CB    . THR A 1 45  ? 105.826 139.647 93.638  1.00 58.07 ?  45  THR A CB    1 
ATOM   341   O  OG1   . THR A 1 45  ? 106.895 138.697 93.548  1.00 59.58 ?  45  THR A OG1   1 
ATOM   342   C  CG2   . THR A 1 45  ? 106.377 141.047 93.427  1.00 55.65 ?  45  THR A CG2   1 
ATOM   343   N  N     . VAL A 1 46  ? 104.331 141.582 96.010  1.00 60.32 ?  46  VAL A N     1 
ATOM   344   C  CA    . VAL A 1 46  ? 103.451 142.741 96.106  1.00 60.71 ?  46  VAL A CA    1 
ATOM   345   C  C     . VAL A 1 46  ? 103.695 143.632 94.897  1.00 60.62 ?  46  VAL A C     1 
ATOM   346   O  O     . VAL A 1 46  ? 104.828 144.060 94.643  1.00 62.72 ?  46  VAL A O     1 
ATOM   347   C  CB    . VAL A 1 46  ? 103.684 143.505 97.415  1.00 60.03 ?  46  VAL A CB    1 
ATOM   348   C  CG1   . VAL A 1 46  ? 102.627 144.579 97.596  1.00 60.24 ?  46  VAL A CG1   1 
ATOM   349   C  CG2   . VAL A 1 46  ? 103.685 142.551 98.592  1.00 59.25 ?  46  VAL A CG2   1 
ATOM   350   N  N     . PHE A 1 47  ? 102.637 143.919 94.147  1.00 64.09 ?  47  PHE A N     1 
ATOM   351   C  CA    . PHE A 1 47  ? 102.725 144.750 92.956  1.00 66.23 ?  47  PHE A CA    1 
ATOM   352   C  C     . PHE A 1 47  ? 101.912 146.017 93.167  1.00 67.45 ?  47  PHE A C     1 
ATOM   353   O  O     . PHE A 1 47  ? 100.760 145.956 93.608  1.00 67.74 ?  47  PHE A O     1 
ATOM   354   C  CB    . PHE A 1 47  ? 102.233 144.000 91.715  1.00 67.11 ?  47  PHE A CB    1 
ATOM   355   C  CG    . PHE A 1 47  ? 102.371 144.785 90.441  1.00 68.09 ?  47  PHE A CG    1 
ATOM   356   C  CD1   . PHE A 1 47  ? 103.582 144.836 89.772  1.00 67.12 ?  47  PHE A CD1   1 
ATOM   357   C  CD2   . PHE A 1 47  ? 101.288 145.466 89.910  1.00 66.60 ?  47  PHE A CD2   1 
ATOM   358   C  CE1   . PHE A 1 47  ? 103.713 145.557 88.600  1.00 67.08 ?  47  PHE A CE1   1 
ATOM   359   C  CE2   . PHE A 1 47  ? 101.412 146.187 88.738  1.00 67.40 ?  47  PHE A CE2   1 
ATOM   360   C  CZ    . PHE A 1 47  ? 102.626 146.233 88.082  1.00 68.47 ?  47  PHE A CZ    1 
ATOM   361   N  N     . PHE A 1 48  ? 102.518 147.156 92.856  1.00 66.92 ?  48  PHE A N     1 
ATOM   362   C  CA    . PHE A 1 48  ? 101.894 148.459 93.008  1.00 64.94 ?  48  PHE A CA    1 
ATOM   363   C  C     . PHE A 1 48  ? 101.538 149.017 91.638  1.00 65.55 ?  48  PHE A C     1 
ATOM   364   O  O     . PHE A 1 48  ? 102.084 148.599 90.613  1.00 67.21 ?  48  PHE A O     1 
ATOM   365   C  CB    . PHE A 1 48  ? 102.817 149.428 93.756  1.00 63.60 ?  48  PHE A CB    1 
ATOM   366   C  CG    . PHE A 1 48  ? 103.258 148.930 95.107  1.00 63.28 ?  48  PHE A CG    1 
ATOM   367   C  CD1   . PHE A 1 48  ? 102.736 149.478 96.264  1.00 64.12 ?  48  PHE A CD1   1 
ATOM   368   C  CD2   . PHE A 1 48  ? 104.214 147.933 95.219  1.00 63.11 ?  48  PHE A CD2   1 
ATOM   369   C  CE1   . PHE A 1 48  ? 103.140 149.027 97.502  1.00 65.24 ?  48  PHE A CE1   1 
ATOM   370   C  CE2   . PHE A 1 48  ? 104.621 147.480 96.455  1.00 63.83 ?  48  PHE A CE2   1 
ATOM   371   C  CZ    . PHE A 1 48  ? 104.085 148.027 97.596  1.00 64.21 ?  48  PHE A CZ    1 
ATOM   372   N  N     . HIS A 1 49  ? 100.602 149.969 91.630  1.00 68.07 ?  49  HIS A N     1 
ATOM   373   C  CA    . HIS A 1 49  ? 100.146 150.542 90.367  1.00 70.19 ?  49  HIS A CA    1 
ATOM   374   C  C     . HIS A 1 49  ? 101.286 151.232 89.629  1.00 69.96 ?  49  HIS A C     1 
ATOM   375   O  O     . HIS A 1 49  ? 101.427 151.082 88.410  1.00 70.21 ?  49  HIS A O     1 
ATOM   376   C  CB    . HIS A 1 49  ? 98.995  151.516 90.617  1.00 69.80 ?  49  HIS A CB    1 
ATOM   377   C  CG    . HIS A 1 49  ? 97.834  150.906 91.337  1.00 71.45 ?  49  HIS A CG    1 
ATOM   378   N  ND1   . HIS A 1 49  ? 97.860  150.618 92.685  1.00 71.84 ?  49  HIS A ND1   1 
ATOM   379   C  CD2   . HIS A 1 49  ? 96.611  150.528 90.897  1.00 70.55 ?  49  HIS A CD2   1 
ATOM   380   C  CE1   . HIS A 1 49  ? 96.704  150.089 93.043  1.00 69.89 ?  49  HIS A CE1   1 
ATOM   381   N  NE2   . HIS A 1 49  ? 95.929  150.023 91.977  1.00 71.70 ?  49  HIS A NE2   1 
ATOM   382   N  N     . ASN A 1 50  ? 102.111 151.988 90.349  1.00 67.49 ?  50  ASN A N     1 
ATOM   383   C  CA    . ASN A 1 50  ? 103.277 152.632 89.767  1.00 66.95 ?  50  ASN A CA    1 
ATOM   384   C  C     . ASN A 1 50  ? 104.421 152.583 90.770  1.00 65.92 ?  50  ASN A C     1 
ATOM   385   O  O     . ASN A 1 50  ? 104.226 152.295 91.952  1.00 67.91 ?  50  ASN A O     1 
ATOM   386   C  CB    . ASN A 1 50  ? 102.983 154.080 89.346  1.00 66.30 ?  50  ASN A CB    1 
ATOM   387   C  CG    . ASN A 1 50  ? 102.388 154.909 90.467  1.00 66.97 ?  50  ASN A CG    1 
ATOM   388   O  OD1   . ASN A 1 50  ? 102.265 154.449 91.601  1.00 66.48 ?  50  ASN A OD1   1 
ATOM   389   N  ND2   . ASN A 1 50  ? 102.017 156.144 90.153  1.00 66.32 ?  50  ASN A ND2   1 
ATOM   390   N  N     . LEU A 1 51  ? 105.630 152.859 90.273  1.00 60.19 ?  51  LEU A N     1 
ATOM   391   C  CA    . LEU A 1 51  ? 106.807 152.830 91.134  1.00 60.44 ?  51  LEU A CA    1 
ATOM   392   C  C     . LEU A 1 51  ? 106.725 153.877 92.238  1.00 62.18 ?  51  LEU A C     1 
ATOM   393   O  O     . LEU A 1 51  ? 107.299 153.685 93.316  1.00 64.40 ?  51  LEU A O     1 
ATOM   394   C  CB    . LEU A 1 51  ? 108.070 153.034 90.297  1.00 61.12 ?  51  LEU A CB    1 
ATOM   395   C  CG    . LEU A 1 51  ? 109.405 153.067 91.046  1.00 58.98 ?  51  LEU A CG    1 
ATOM   396   C  CD1   . LEU A 1 51  ? 109.682 151.728 91.705  1.00 58.21 ?  51  LEU A CD1   1 
ATOM   397   C  CD2   . LEU A 1 51  ? 110.535 153.462 90.115  1.00 58.63 ?  51  LEU A CD2   1 
ATOM   398   N  N     . LYS A 1 52  ? 106.026 154.988 91.990  1.00 62.24 ?  52  LYS A N     1 
ATOM   399   C  CA    . LYS A 1 52  ? 105.890 156.020 93.014  1.00 60.33 ?  52  LYS A CA    1 
ATOM   400   C  C     . LYS A 1 52  ? 105.155 155.490 94.236  1.00 61.87 ?  52  LYS A C     1 
ATOM   401   O  O     . LYS A 1 52  ? 105.575 155.729 95.375  1.00 61.87 ?  52  LYS A O     1 
ATOM   402   C  CB    . LYS A 1 52  ? 105.167 157.237 92.440  1.00 59.33 ?  52  LYS A CB    1 
ATOM   403   C  CG    . LYS A 1 52  ? 105.434 158.529 93.192  1.00 62.17 ?  52  LYS A CG    1 
ATOM   404   C  CD    . LYS A 1 52  ? 105.322 159.733 92.271  1.00 63.90 ?  52  LYS A CD    1 
ATOM   405   C  CE    . LYS A 1 52  ? 106.197 160.881 92.748  1.00 63.03 ?  52  LYS A CE    1 
ATOM   406   N  NZ    . LYS A 1 52  ? 106.425 160.836 94.218  1.00 61.51 1  52  LYS A NZ    1 
ATOM   407   N  N     . GLU A 1 53  ? 104.059 154.760 94.019  1.00 65.07 ?  53  GLU A N     1 
ATOM   408   C  CA    . GLU A 1 53  ? 103.329 154.171 95.135  1.00 65.62 ?  53  GLU A CA    1 
ATOM   409   C  C     . GLU A 1 53  ? 104.192 153.157 95.873  1.00 64.75 ?  53  GLU A C     1 
ATOM   410   O  O     . GLU A 1 53  ? 104.170 153.096 97.106  1.00 65.93 ?  53  GLU A O     1 
ATOM   411   C  CB    . GLU A 1 53  ? 102.039 153.522 94.633  1.00 65.41 ?  53  GLU A CB    1 
ATOM   412   C  CG    . GLU A 1 53  ? 101.339 152.639 95.653  1.00 67.11 ?  53  GLU A CG    1 
ATOM   413   C  CD    . GLU A 1 53  ? 100.099 151.972 95.088  1.00 69.03 ?  53  GLU A CD    1 
ATOM   414   O  OE1   . GLU A 1 53  ? 99.643  152.384 94.001  1.00 69.01 ?  53  GLU A OE1   1 
ATOM   415   O  OE2   . GLU A 1 53  ? 99.581  151.036 95.732  1.00 68.53 -1 53  GLU A OE2   1 
ATOM   416   N  N     . LYS A 1 54  ? 104.970 152.364 95.134  1.00 60.53 ?  54  LYS A N     1 
ATOM   417   C  CA    . LYS A 1 54  ? 105.850 151.383 95.761  1.00 62.09 ?  54  LYS A CA    1 
ATOM   418   C  C     . LYS A 1 54  ? 106.883 152.057 96.653  1.00 58.42 ?  54  LYS A C     1 
ATOM   419   O  O     . LYS A 1 54  ? 107.089 151.652 97.805  1.00 60.89 ?  54  LYS A O     1 
ATOM   420   C  CB    . LYS A 1 54  ? 106.538 150.545 94.684  1.00 61.73 ?  54  LYS A CB    1 
ATOM   421   C  CG    . LYS A 1 54  ? 107.625 149.630 95.212  1.00 59.32 ?  54  LYS A CG    1 
ATOM   422   C  CD    . LYS A 1 54  ? 107.961 148.545 94.210  1.00 59.69 ?  54  LYS A CD    1 
ATOM   423   C  CE    . LYS A 1 54  ? 108.878 147.503 94.817  1.00 60.84 ?  54  LYS A CE    1 
ATOM   424   N  NZ    . LYS A 1 54  ? 108.827 146.218 94.069  1.00 61.90 1  54  LYS A NZ    1 
ATOM   425   N  N     . LEU A 1 55  ? 107.543 153.094 96.137  1.00 56.48 ?  55  LEU A N     1 
ATOM   426   C  CA    . LEU A 1 55  ? 108.572 153.776 96.915  1.00 58.32 ?  55  LEU A CA    1 
ATOM   427   C  C     . LEU A 1 55  ? 107.972 154.492 98.117  1.00 61.53 ?  55  LEU A C     1 
ATOM   428   O  O     . LEU A 1 55  ? 108.560 154.482 99.205  1.00 63.78 ?  55  LEU A O     1 
ATOM   429   C  CB    . LEU A 1 55  ? 109.342 154.751 96.029  1.00 59.39 ?  55  LEU A CB    1 
ATOM   430   C  CG    . LEU A 1 55  ? 110.223 154.093 94.967  1.00 59.74 ?  55  LEU A CG    1 
ATOM   431   C  CD1   . LEU A 1 55  ? 110.869 155.144 94.089  1.00 59.60 ?  55  LEU A CD1   1 
ATOM   432   C  CD2   . LEU A 1 55  ? 111.274 153.207 95.615  1.00 59.41 ?  55  LEU A CD2   1 
ATOM   433   N  N     . ASP A 1 56  ? 106.805 155.119 97.946  1.00 65.92 ?  56  ASP A N     1 
ATOM   434   C  CA    . ASP A 1 56  ? 106.147 155.763 99.076  1.00 64.75 ?  56  ASP A CA    1 
ATOM   435   C  C     . ASP A 1 56  ? 105.768 154.744 100.143 1.00 64.19 ?  56  ASP A C     1 
ATOM   436   O  O     . ASP A 1 56  ? 105.956 154.988 101.340 1.00 65.16 ?  56  ASP A O     1 
ATOM   437   C  CB    . ASP A 1 56  ? 104.914 156.526 98.595  1.00 65.50 ?  56  ASP A CB    1 
ATOM   438   C  CG    . ASP A 1 56  ? 105.270 157.783 97.826  1.00 68.31 ?  56  ASP A CG    1 
ATOM   439   O  OD1   . ASP A 1 56  ? 106.394 158.295 98.010  1.00 67.57 ?  56  ASP A OD1   1 
ATOM   440   O  OD2   . ASP A 1 56  ? 104.428 158.260 97.037  1.00 67.50 -1 56  ASP A OD2   1 
ATOM   441   N  N     . TYR A 1 57  ? 105.248 153.588 99.724  1.00 59.50 ?  57  TYR A N     1 
ATOM   442   C  CA    . TYR A 1 57  ? 104.885 152.540 100.669 1.00 62.04 ?  57  TYR A CA    1 
ATOM   443   C  C     . TYR A 1 57  ? 106.106 152.033 101.423 1.00 61.86 ?  57  TYR A C     1 
ATOM   444   O  O     . TYR A 1 57  ? 106.041 151.783 102.632 1.00 63.68 ?  57  TYR A O     1 
ATOM   445   C  CB    . TYR A 1 57  ? 104.208 151.392 99.918  1.00 61.52 ?  57  TYR A CB    1 
ATOM   446   C  CG    . TYR A 1 57  ? 103.955 150.155 100.746 1.00 62.14 ?  57  TYR A CG    1 
ATOM   447   C  CD1   . TYR A 1 57  ? 102.886 150.092 101.627 1.00 62.07 ?  57  TYR A CD1   1 
ATOM   448   C  CD2   . TYR A 1 57  ? 104.799 149.056 100.664 1.00 63.16 ?  57  TYR A CD2   1 
ATOM   449   C  CE1   . TYR A 1 57  ? 102.649 148.961 102.379 1.00 62.91 ?  57  TYR A CE1   1 
ATOM   450   C  CE2   . TYR A 1 57  ? 104.575 147.927 101.421 1.00 63.73 ?  57  TYR A CE2   1 
ATOM   451   C  CZ    . TYR A 1 57  ? 103.501 147.885 102.279 1.00 63.36 ?  57  TYR A CZ    1 
ATOM   452   O  OH    . TYR A 1 57  ? 103.275 146.758 103.035 1.00 62.05 ?  57  TYR A OH    1 
ATOM   453   N  N     . LEU A 1 58  ? 107.230 151.869 100.721 1.00 56.04 ?  58  LEU A N     1 
ATOM   454   C  CA    . LEU A 1 58  ? 108.425 151.332 101.362 1.00 54.62 ?  58  LEU A CA    1 
ATOM   455   C  C     . LEU A 1 58  ? 109.060 152.346 102.306 1.00 55.12 ?  58  LEU A C     1 
ATOM   456   O  O     . LEU A 1 58  ? 109.564 151.977 103.372 1.00 58.06 ?  58  LEU A O     1 
ATOM   457   C  CB    . LEU A 1 58  ? 109.426 150.877 100.301 1.00 56.32 ?  58  LEU A CB    1 
ATOM   458   C  CG    . LEU A 1 58  ? 108.980 149.671 99.474  1.00 56.27 ?  58  LEU A CG    1 
ATOM   459   C  CD1   . LEU A 1 58  ? 109.761 149.588 98.179  1.00 55.04 ?  58  LEU A CD1   1 
ATOM   460   C  CD2   . LEU A 1 58  ? 109.124 148.390 100.270 1.00 56.23 ?  58  LEU A CD2   1 
ATOM   461   N  N     . VAL A 1 59  ? 109.054 153.627 101.933 1.00 60.11 ?  59  VAL A N     1 
ATOM   462   C  CA    . VAL A 1 59  ? 109.631 154.650 102.800 1.00 62.24 ?  59  VAL A CA    1 
ATOM   463   C  C     . VAL A 1 59  ? 108.759 154.862 104.032 1.00 64.10 ?  59  VAL A C     1 
ATOM   464   O  O     . VAL A 1 59  ? 109.260 154.947 105.159 1.00 63.20 ?  59  VAL A O     1 
ATOM   465   C  CB    . VAL A 1 59  ? 109.839 155.961 102.021 1.00 62.74 ?  59  VAL A CB    1 
ATOM   466   C  CG1   . VAL A 1 59  ? 110.255 157.077 102.962 1.00 60.59 ?  59  VAL A CG1   1 
ATOM   467   C  CG2   . VAL A 1 59  ? 110.885 155.769 100.934 1.00 62.18 ?  59  VAL A CG2   1 
ATOM   468   N  N     . GLU A 1 60  ? 107.440 154.946 103.837 1.00 64.88 ?  60  GLU A N     1 
ATOM   469   C  CA    . GLU A 1 60  ? 106.543 155.252 104.947 1.00 64.28 ?  60  GLU A CA    1 
ATOM   470   C  C     . GLU A 1 60  ? 106.529 154.140 105.988 1.00 65.21 ?  60  GLU A C     1 
ATOM   471   O  O     . GLU A 1 60  ? 106.487 154.414 107.194 1.00 67.47 ?  60  GLU A O     1 
ATOM   472   C  CB    . GLU A 1 60  ? 105.132 155.515 104.420 1.00 64.16 ?  60  GLU A CB    1 
ATOM   473   C  CG    . GLU A 1 60  ? 104.986 156.840 103.685 1.00 65.72 ?  60  GLU A CG    1 
ATOM   474   C  CD    . GLU A 1 60  ? 103.800 156.858 102.739 1.00 69.17 ?  60  GLU A CD    1 
ATOM   475   O  OE1   . GLU A 1 60  ? 102.969 155.927 102.804 1.00 68.12 ?  60  GLU A OE1   1 
ATOM   476   O  OE2   . GLU A 1 60  ? 103.698 157.803 101.929 1.00 67.57 -1 60  GLU A OE2   1 
ATOM   477   N  N     . ASN A 1 61  ? 106.563 152.882 105.552 1.00 59.25 ?  61  ASN A N     1 
ATOM   478   C  CA    . ASN A 1 61  ? 106.492 151.754 106.474 1.00 60.01 ?  61  ASN A CA    1 
ATOM   479   C  C     . ASN A 1 61  ? 107.856 151.282 106.952 1.00 61.33 ?  61  ASN A C     1 
ATOM   480   O  O     . ASN A 1 61  ? 108.001 150.098 107.282 1.00 64.86 ?  61  ASN A O     1 
ATOM   481   C  CB    . ASN A 1 61  ? 105.729 150.593 105.838 1.00 60.81 ?  61  ASN A CB    1 
ATOM   482   C  CG    . ASN A 1 61  ? 104.370 151.008 105.326 1.00 62.46 ?  61  ASN A CG    1 
ATOM   483   O  OD1   . ASN A 1 61  ? 104.065 152.196 105.236 1.00 63.19 ?  61  ASN A OD1   1 
ATOM   484   N  ND2   . ASN A 1 61  ? 103.529 150.031 105.031 1.00 61.88 ?  61  ASN A ND2   1 
ATOM   485   N  N     . GLN A 1 62  ? 108.848 152.173 106.981 1.00 57.49 ?  62  GLN A N     1 
ATOM   486   C  CA    . GLN A 1 62  ? 110.142 151.909 107.612 1.00 58.44 ?  62  GLN A CA    1 
ATOM   487   C  C     . GLN A 1 62  ? 110.894 150.768 106.934 1.00 57.89 ?  62  GLN A C     1 
ATOM   488   O  O     . GLN A 1 62  ? 111.664 150.051 107.578 1.00 58.51 ?  62  GLN A O     1 
ATOM   489   C  CB    . GLN A 1 62  ? 109.976 151.618 109.107 1.00 58.21 ?  62  GLN A CB    1 
ATOM   490   C  CG    . GLN A 1 62  ? 109.266 152.715 109.889 1.00 57.65 ?  62  GLN A CG    1 
ATOM   491   C  CD    . GLN A 1 62  ? 109.877 154.084 109.675 1.00 60.19 ?  62  GLN A CD    1 
ATOM   492   O  OE1   . GLN A 1 62  ? 110.837 154.463 110.346 1.00 59.91 ?  62  GLN A OE1   1 
ATOM   493   N  NE2   . GLN A 1 62  ? 109.324 154.836 108.730 1.00 58.82 ?  62  GLN A NE2   1 
ATOM   494   N  N     . TYR A 1 63  ? 110.678 150.583 105.632 1.00 55.04 ?  63  TYR A N     1 
ATOM   495   C  CA    . TYR A 1 63  ? 111.433 149.586 104.884 1.00 53.55 ?  63  TYR A CA    1 
ATOM   496   C  C     . TYR A 1 63  ? 112.693 150.172 104.263 1.00 53.47 ?  63  TYR A C     1 
ATOM   497   O  O     . TYR A 1 63  ? 113.745 149.524 104.271 1.00 52.88 ?  63  TYR A O     1 
ATOM   498   C  CB    . TYR A 1 63  ? 110.560 148.962 103.792 1.00 52.78 ?  63  TYR A CB    1 
ATOM   499   C  CG    . TYR A 1 63  ? 109.515 148.006 104.315 1.00 53.89 ?  63  TYR A CG    1 
ATOM   500   C  CD1   . TYR A 1 63  ? 109.865 146.958 105.156 1.00 52.87 ?  63  TYR A CD1   1 
ATOM   501   C  CD2   . TYR A 1 63  ? 108.180 148.148 103.966 1.00 55.05 ?  63  TYR A CD2   1 
ATOM   502   C  CE1   . TYR A 1 63  ? 108.913 146.082 105.636 1.00 53.91 ?  63  TYR A CE1   1 
ATOM   503   C  CE2   . TYR A 1 63  ? 107.221 147.277 104.441 1.00 55.36 ?  63  TYR A CE2   1 
ATOM   504   C  CZ    . TYR A 1 63  ? 107.594 146.246 105.276 1.00 56.36 ?  63  TYR A CZ    1 
ATOM   505   O  OH    . TYR A 1 63  ? 106.641 145.376 105.750 1.00 55.76 ?  63  TYR A OH    1 
ATOM   506   N  N     . TYR A 1 64  ? 112.606 151.385 103.732 1.00 49.94 ?  64  TYR A N     1 
ATOM   507   C  CA    . TYR A 1 64  ? 113.728 152.062 103.103 1.00 48.26 ?  64  TYR A CA    1 
ATOM   508   C  C     . TYR A 1 64  ? 114.163 153.253 103.945 1.00 50.88 ?  64  TYR A C     1 
ATOM   509   O  O     . TYR A 1 64  ? 113.543 153.597 104.953 1.00 53.87 ?  64  TYR A O     1 
ATOM   510   C  CB    . TYR A 1 64  ? 113.361 152.527 101.691 1.00 47.96 ?  64  TYR A CB    1 
ATOM   511   C  CG    . TYR A 1 64  ? 113.409 151.436 100.650 1.00 50.04 ?  64  TYR A CG    1 
ATOM   512   C  CD1   . TYR A 1 64  ? 113.860 150.163 100.969 1.00 48.97 ?  64  TYR A CD1   1 
ATOM   513   C  CD2   . TYR A 1 64  ? 113.005 151.681 99.348  1.00 49.89 ?  64  TYR A CD2   1 
ATOM   514   C  CE1   . TYR A 1 64  ? 113.903 149.165 100.020 1.00 45.60 ?  64  TYR A CE1   1 
ATOM   515   C  CE2   . TYR A 1 64  ? 113.047 150.692 98.393  1.00 48.10 ?  64  TYR A CE2   1 
ATOM   516   C  CZ    . TYR A 1 64  ? 113.495 149.436 98.733  1.00 47.41 ?  64  TYR A CZ    1 
ATOM   517   O  OH    . TYR A 1 64  ? 113.533 148.450 97.778  1.00 50.79 ?  64  TYR A OH    1 
ATOM   518   N  N     . GLU A 1 65  ? 115.247 153.885 103.511 1.00 53.79 ?  65  GLU A N     1 
ATOM   519   C  CA    . GLU A 1 65  ? 115.724 155.123 104.109 1.00 52.12 ?  65  GLU A CA    1 
ATOM   520   C  C     . GLU A 1 65  ? 115.355 156.285 103.200 1.00 55.07 ?  65  GLU A C     1 
ATOM   521   O  O     . GLU A 1 65  ? 115.584 156.229 101.987 1.00 56.78 ?  65  GLU A O     1 
ATOM   522   C  CB    . GLU A 1 65  ? 117.235 155.082 104.336 1.00 52.60 ?  65  GLU A CB    1 
ATOM   523   C  CG    . GLU A 1 65  ? 117.718 153.852 105.080 1.00 51.39 ?  65  GLU A CG    1 
ATOM   524   C  CD    . GLU A 1 65  ? 119.230 153.789 105.177 1.00 55.09 ?  65  GLU A CD    1 
ATOM   525   O  OE1   . GLU A 1 65  ? 119.907 154.205 104.213 1.00 57.01 ?  65  GLU A OE1   1 
ATOM   526   O  OE2   . GLU A 1 65  ? 119.740 153.326 106.218 1.00 54.12 -1 65  GLU A OE2   1 
ATOM   527   N  N     . GLU A 1 66  ? 114.776 157.333 103.786 1.00 58.01 ?  66  GLU A N     1 
ATOM   528   C  CA    . GLU A 1 66  ? 114.364 158.490 103.002 1.00 56.33 ?  66  GLU A CA    1 
ATOM   529   C  C     . GLU A 1 66  ? 115.545 159.339 102.557 1.00 56.91 ?  66  GLU A C     1 
ATOM   530   O  O     . GLU A 1 66  ? 115.475 159.969 101.496 1.00 57.92 ?  66  GLU A O     1 
ATOM   531   C  CB    . GLU A 1 66  ? 113.377 159.335 103.813 1.00 57.09 ?  66  GLU A CB    1 
ATOM   532   C  CG    . GLU A 1 66  ? 112.944 160.640 103.157 1.00 59.42 ?  66  GLU A CG    1 
ATOM   533   C  CD    . GLU A 1 66  ? 112.034 160.427 101.961 1.00 61.01 ?  66  GLU A CD    1 
ATOM   534   O  OE1   . GLU A 1 66  ? 110.831 160.748 102.066 1.00 58.42 ?  66  GLU A OE1   1 
ATOM   535   O  OE2   . GLU A 1 66  ? 112.520 159.953 100.912 1.00 62.31 -1 66  GLU A OE2   1 
ATOM   536   N  N     . GLU A 1 67  ? 116.631 159.359 103.334 1.00 58.05 ?  67  GLU A N     1 
ATOM   537   C  CA    . GLU A 1 67  ? 117.727 160.286 103.070 1.00 56.47 ?  67  GLU A CA    1 
ATOM   538   C  C     . GLU A 1 67  ? 118.385 160.017 101.721 1.00 57.31 ?  67  GLU A C     1 
ATOM   539   O  O     . GLU A 1 67  ? 118.641 160.949 100.951 1.00 57.76 ?  67  GLU A O     1 
ATOM   540   C  CB    . GLU A 1 67  ? 118.757 160.208 104.197 1.00 56.92 ?  67  GLU A CB    1 
ATOM   541   C  CG    . GLU A 1 67  ? 118.862 158.839 104.847 1.00 58.91 ?  67  GLU A CG    1 
ATOM   542   C  CD    . GLU A 1 67  ? 118.054 158.738 106.125 1.00 59.42 ?  67  GLU A CD    1 
ATOM   543   O  OE1   . GLU A 1 67  ? 116.808 158.721 106.044 1.00 57.57 ?  67  GLU A OE1   1 
ATOM   544   O  OE2   . GLU A 1 67  ? 118.665 158.680 107.212 1.00 62.17 -1 67  GLU A OE2   1 
ATOM   545   N  N     . PHE A 1 68  ? 118.667 158.750 101.413 1.00 54.61 ?  68  PHE A N     1 
ATOM   546   C  CA    . PHE A 1 68  ? 119.365 158.448 100.168 1.00 52.02 ?  68  PHE A CA    1 
ATOM   547   C  C     . PHE A 1 68  ? 118.442 158.537 98.960  1.00 51.81 ?  68  PHE A C     1 
ATOM   548   O  O     . PHE A 1 68  ? 118.899 158.878 97.864  1.00 55.05 ?  68  PHE A O     1 
ATOM   549   C  CB    . PHE A 1 68  ? 120.027 157.068 100.250 1.00 51.38 ?  68  PHE A CB    1 
ATOM   550   C  CG    . PHE A 1 68  ? 119.155 155.934 99.788  1.00 50.85 ?  68  PHE A CG    1 
ATOM   551   C  CD1   . PHE A 1 68  ? 118.240 155.354 100.646 1.00 51.28 ?  68  PHE A CD1   1 
ATOM   552   C  CD2   . PHE A 1 68  ? 119.276 155.428 98.504  1.00 48.03 ?  68  PHE A CD2   1 
ATOM   553   C  CE1   . PHE A 1 68  ? 117.444 154.308 100.225 1.00 48.97 ?  68  PHE A CE1   1 
ATOM   554   C  CE2   . PHE A 1 68  ? 118.485 154.382 98.080  1.00 46.98 ?  68  PHE A CE2   1 
ATOM   555   C  CZ    . PHE A 1 68  ? 117.571 153.819 98.942  1.00 48.15 ?  68  PHE A CZ    1 
ATOM   556   N  N     . LEU A 1 69  ? 117.153 158.243 99.134  1.00 50.98 ?  69  LEU A N     1 
ATOM   557   C  CA    . LEU A 1 69  ? 116.207 158.383 98.035  1.00 53.18 ?  69  LEU A CA    1 
ATOM   558   C  C     . LEU A 1 69  ? 115.844 159.835 97.767  1.00 53.68 ?  69  LEU A C     1 
ATOM   559   O  O     . LEU A 1 69  ? 115.317 160.141 96.692  1.00 54.19 ?  69  LEU A O     1 
ATOM   560   C  CB    . LEU A 1 69  ? 114.939 157.578 98.322  1.00 54.09 ?  69  LEU A CB    1 
ATOM   561   C  CG    . LEU A 1 69  ? 115.021 156.071 98.083  1.00 52.44 ?  69  LEU A CG    1 
ATOM   562   C  CD1   . LEU A 1 69  ? 113.804 155.367 98.656  1.00 51.87 ?  69  LEU A CD1   1 
ATOM   563   C  CD2   . LEU A 1 69  ? 115.169 155.772 96.603  1.00 50.13 ?  69  LEU A CD2   1 
ATOM   564   N  N     . SER A 1 70  ? 116.114 160.735 98.713  1.00 55.83 ?  70  SER A N     1 
ATOM   565   C  CA    . SER A 1 70  ? 115.780 162.144 98.550  1.00 54.06 ?  70  SER A CA    1 
ATOM   566   C  C     . SER A 1 70  ? 116.794 162.905 97.710  1.00 53.45 ?  70  SER A C     1 
ATOM   567   O  O     . SER A 1 70  ? 116.532 164.058 97.353  1.00 56.79 ?  70  SER A O     1 
ATOM   568   C  CB    . SER A 1 70  ? 115.647 162.813 99.920  1.00 54.37 ?  70  SER A CB    1 
ATOM   569   O  OG    . SER A 1 70  ? 116.908 162.937 100.551 1.00 54.27 ?  70  SER A OG    1 
ATOM   570   N  N     . LEU A 1 71  ? 117.937 162.300 97.388  1.00 50.47 ?  71  LEU A N     1 
ATOM   571   C  CA    . LEU A 1 71  ? 118.934 162.957 96.555  1.00 50.14 ?  71  LEU A CA    1 
ATOM   572   C  C     . LEU A 1 71  ? 118.615 162.869 95.070  1.00 50.99 ?  71  LEU A C     1 
ATOM   573   O  O     . LEU A 1 71  ? 119.311 163.497 94.265  1.00 50.24 ?  71  LEU A O     1 
ATOM   574   C  CB    . LEU A 1 71  ? 120.319 162.358 96.815  1.00 48.19 ?  71  LEU A CB    1 
ATOM   575   C  CG    . LEU A 1 71  ? 120.646 162.026 98.271  1.00 49.88 ?  71  LEU A CG    1 
ATOM   576   C  CD1   . LEU A 1 71  ? 121.663 160.904 98.345  1.00 51.77 ?  71  LEU A CD1   1 
ATOM   577   C  CD2   . LEU A 1 71  ? 121.154 163.262 98.992  1.00 51.24 ?  71  LEU A CD2   1 
ATOM   578   N  N     . TYR A 1 72  ? 117.589 162.113 94.690  1.00 48.11 ?  72  TYR A N     1 
ATOM   579   C  CA    . TYR A 1 72  ? 117.173 161.981 93.304  1.00 50.38 ?  72  TYR A CA    1 
ATOM   580   C  C     . TYR A 1 72  ? 115.733 162.445 93.153  1.00 52.50 ?  72  TYR A C     1 
ATOM   581   O  O     . TYR A 1 72  ? 114.884 162.145 93.998  1.00 52.67 ?  72  TYR A O     1 
ATOM   582   C  CB    . TYR A 1 72  ? 117.275 160.531 92.812  1.00 48.01 ?  72  TYR A CB    1 
ATOM   583   C  CG    . TYR A 1 72  ? 118.565 159.822 93.139  1.00 47.76 ?  72  TYR A CG    1 
ATOM   584   C  CD1   . TYR A 1 72  ? 118.741 159.186 94.360  1.00 46.66 ?  72  TYR A CD1   1 
ATOM   585   C  CD2   . TYR A 1 72  ? 119.596 159.757 92.213  1.00 46.11 ?  72  TYR A CD2   1 
ATOM   586   C  CE1   . TYR A 1 72  ? 119.912 158.528 94.658  1.00 44.18 ?  72  TYR A CE1   1 
ATOM   587   C  CE2   . TYR A 1 72  ? 120.769 159.098 92.500  1.00 42.59 ?  72  TYR A CE2   1 
ATOM   588   C  CZ    . TYR A 1 72  ? 120.922 158.487 93.724  1.00 44.18 ?  72  TYR A CZ    1 
ATOM   589   O  OH    . TYR A 1 72  ? 122.092 157.829 94.016  1.00 49.45 ?  72  TYR A OH    1 
ATOM   590   N  N     . SER A 1 73  ? 115.461 163.174 92.076  1.00 55.03 ?  73  SER A N     1 
ATOM   591   C  CA    . SER A 1 73  ? 114.083 163.392 91.671  1.00 56.45 ?  73  SER A CA    1 
ATOM   592   C  C     . SER A 1 73  ? 113.481 162.068 91.217  1.00 57.84 ?  73  SER A C     1 
ATOM   593   O  O     . SER A 1 73  ? 114.185 161.183 90.723  1.00 58.76 ?  73  SER A O     1 
ATOM   594   C  CB    . SER A 1 73  ? 114.005 164.425 90.548  1.00 57.18 ?  73  SER A CB    1 
ATOM   595   O  OG    . SER A 1 73  ? 114.221 163.825 89.285  1.00 57.54 ?  73  SER A OG    1 
ATOM   596   N  N     . PHE A 1 74  ? 112.165 161.927 91.399  1.00 58.15 ?  74  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 74  ? 111.532 160.652 91.083  1.00 55.90 ?  74  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 74  ? 111.678 160.268 89.618  1.00 58.32 ?  74  PHE A C     1 
ATOM   599   O  O     . PHE A 1 74  ? 111.620 159.077 89.297  1.00 60.17 ?  74  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 74  ? 110.050 160.658 91.452  1.00 58.40 ?  74  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 74  ? 109.372 159.351 91.171  1.00 58.85 ?  74  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 74  ? 109.611 158.248 91.970  1.00 57.77 ?  74  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 74  ? 108.530 159.215 90.080  1.00 58.58 ?  74  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 74  ? 109.007 157.039 91.699  1.00 59.26 ?  74  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 74  ? 107.922 158.010 89.806  1.00 59.84 ?  74  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 74  ? 108.162 156.921 90.614  1.00 61.18 ?  74  PHE A CZ    1 
ATOM   607   N  N     . GLU A 1 75  ? 111.867 161.236 88.721  1.00 61.63 ?  75  GLU A N     1 
ATOM   608   C  CA    . GLU A 1 75  ? 112.134 160.887 87.331  1.00 61.08 ?  75  GLU A CA    1 
ATOM   609   C  C     . GLU A 1 75  ? 113.455 160.138 87.203  1.00 62.99 ?  75  GLU A C     1 
ATOM   610   O  O     . GLU A 1 75  ? 113.564 159.180 86.431  1.00 62.51 ?  75  GLU A O     1 
ATOM   611   C  CB    . GLU A 1 75  ? 112.132 162.143 86.462  1.00 60.87 ?  75  GLU A CB    1 
ATOM   612   C  CG    . GLU A 1 75  ? 110.746 162.727 86.243  1.00 62.72 ?  75  GLU A CG    1 
ATOM   613   C  CD    . GLU A 1 75  ? 109.739 161.685 85.794  1.00 65.19 ?  75  GLU A CD    1 
ATOM   614   O  OE1   . GLU A 1 75  ? 109.949 161.073 84.725  1.00 65.33 ?  75  GLU A OE1   1 
ATOM   615   O  OE2   . GLU A 1 75  ? 108.738 161.475 86.510  1.00 64.89 -1 75  GLU A OE2   1 
ATOM   616   N  N     . ASP A 1 76  ? 114.466 160.551 87.970  1.00 58.05 ?  76  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 76  ? 115.750 159.858 87.947  1.00 55.77 ?  76  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 76  ? 115.638 158.451 88.523  1.00 55.43 ?  76  ASP A C     1 
ATOM   619   O  O     . ASP A 1 76  ? 116.228 157.505 87.986  1.00 60.04 ?  76  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 76  ? 116.789 160.671 88.714  1.00 57.42 ?  76  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 76  ? 116.986 162.056 88.132  1.00 60.39 ?  76  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 76  ? 116.973 162.187 86.890  1.00 59.97 ?  76  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 76  ? 117.155 163.014 88.915  1.00 59.16 -1 76  ASP A OD2   1 
ATOM   624   N  N     . ILE A 1 77  ? 114.895 158.292 89.621  1.00 51.09 ?  77  ILE A N     1 
ATOM   625   C  CA    . ILE A 1 77  ? 114.691 156.964 90.195  1.00 51.47 ?  77  ILE A CA    1 
ATOM   626   C  C     . ILE A 1 77  ? 113.939 156.076 89.215  1.00 51.41 ?  77  ILE A C     1 
ATOM   627   O  O     . ILE A 1 77  ? 114.242 154.884 89.068  1.00 53.07 ?  77  ILE A O     1 
ATOM   628   C  CB    . ILE A 1 77  ? 113.952 157.071 91.541  1.00 52.51 ?  77  ILE A CB    1 
ATOM   629   C  CG1   . ILE A 1 77  ? 114.629 158.105 92.439  1.00 52.79 ?  77  ILE A CG1   1 
ATOM   630   C  CG2   . ILE A 1 77  ? 113.901 155.716 92.224  1.00 51.51 ?  77  ILE A CG2   1 
ATOM   631   C  CD1   . ILE A 1 77  ? 114.197 158.039 93.884  1.00 52.94 ?  77  ILE A CD1   1 
ATOM   632   N  N     . LYS A 1 78  ? 112.940 156.641 88.536  1.00 54.77 ?  78  LYS A N     1 
ATOM   633   C  CA    . LYS A 1 78  ? 112.212 155.899 87.516  1.00 54.72 ?  78  LYS A CA    1 
ATOM   634   C  C     . LYS A 1 78  ? 113.137 155.472 86.387  1.00 54.66 ?  78  LYS A C     1 
ATOM   635   O  O     . LYS A 1 78  ? 113.051 154.340 85.905  1.00 57.65 ?  78  LYS A O     1 
ATOM   636   C  CB    . LYS A 1 78  ? 111.062 156.749 86.979  1.00 57.81 ?  78  LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 78  ? 109.832 155.961 86.567  1.00 56.70 ?  78  LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 78  ? 108.811 156.866 85.902  1.00 56.73 ?  78  LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 78  ? 108.033 156.128 84.829  1.00 57.73 ?  78  LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 78  ? 106.598 155.978 85.196  1.00 57.58 1  78  LYS A NZ    1 
ATOM   641   N  N     . GLU A 1 79  ? 114.029 156.364 85.951  1.00 55.66 ?  79  GLU A N     1 
ATOM   642   C  CA    . GLU A 1 79  ? 114.987 156.012 84.907  1.00 55.52 ?  79  GLU A CA    1 
ATOM   643   C  C     . GLU A 1 79  ? 115.905 154.884 85.360  1.00 52.99 ?  79  GLU A C     1 
ATOM   644   O  O     . GLU A 1 79  ? 116.214 153.973 84.584  1.00 55.14 ?  79  GLU A O     1 
ATOM   645   C  CB    . GLU A 1 79  ? 115.809 157.239 84.514  1.00 56.06 ?  79  GLU A CB    1 
ATOM   646   C  CG    . GLU A 1 79  ? 115.070 158.245 83.653  1.00 56.91 ?  79  GLU A CG    1 
ATOM   647   C  CD    . GLU A 1 79  ? 115.931 159.438 83.291  1.00 60.38 ?  79  GLU A CD    1 
ATOM   648   O  OE1   . GLU A 1 79  ? 116.972 159.242 82.630  1.00 60.58 ?  79  GLU A OE1   1 
ATOM   649   O  OE2   . GLU A 1 79  ? 115.572 160.571 83.673  1.00 61.84 -1 79  GLU A OE2   1 
ATOM   650   N  N     . VAL A 1 80  ? 116.353 154.933 86.614  1.00 45.61 ?  80  VAL A N     1 
ATOM   651   C  CA    . VAL A 1 80  ? 117.206 153.872 87.148  1.00 43.99 ?  80  VAL A CA    1 
ATOM   652   C  C     . VAL A 1 80  ? 116.465 152.539 87.149  1.00 48.77 ?  80  VAL A C     1 
ATOM   653   O  O     . VAL A 1 80  ? 117.010 151.503 86.743  1.00 49.84 ?  80  VAL A O     1 
ATOM   654   C  CB    . VAL A 1 80  ? 117.698 154.254 88.556  1.00 43.52 ?  80  VAL A CB    1 
ATOM   655   C  CG1   . VAL A 1 80  ? 118.272 153.048 89.272  1.00 45.04 ?  80  VAL A CG1   1 
ATOM   656   C  CG2   . VAL A 1 80  ? 118.730 155.363 88.468  1.00 44.18 ?  80  VAL A CG2   1 
ATOM   657   N  N     . PHE A 1 81  ? 115.207 152.547 87.595  1.00 48.14 ?  81  PHE A N     1 
ATOM   658   C  CA    . PHE A 1 81  ? 114.429 151.313 87.628  1.00 44.30 ?  81  PHE A CA    1 
ATOM   659   C  C     . PHE A 1 81  ? 114.145 150.792 86.223  1.00 47.34 ?  81  PHE A C     1 
ATOM   660   O  O     . PHE A 1 81  ? 114.119 149.576 86.000  1.00 49.22 ?  81  PHE A O     1 
ATOM   661   C  CB    . PHE A 1 81  ? 113.131 151.533 88.401  1.00 44.78 ?  81  PHE A CB    1 
ATOM   662   C  CG    . PHE A 1 81  ? 113.247 151.244 89.871  1.00 44.53 ?  81  PHE A CG    1 
ATOM   663   C  CD1   . PHE A 1 81  ? 113.842 152.158 90.723  1.00 45.67 ?  81  PHE A CD1   1 
ATOM   664   C  CD2   . PHE A 1 81  ? 112.762 150.062 90.399  1.00 46.79 ?  81  PHE A CD2   1 
ATOM   665   C  CE1   . PHE A 1 81  ? 113.951 151.897 92.075  1.00 45.99 ?  81  PHE A CE1   1 
ATOM   666   C  CE2   . PHE A 1 81  ? 112.868 149.797 91.750  1.00 45.17 ?  81  PHE A CE2   1 
ATOM   667   C  CZ    . PHE A 1 81  ? 113.463 150.715 92.588  1.00 43.40 ?  81  PHE A CZ    1 
ATOM   668   N  N     . LYS A 1 82  ? 113.922 151.693 85.261  1.00 47.06 ?  82  LYS A N     1 
ATOM   669   C  CA    . LYS A 1 82  ? 113.794 151.266 83.870  1.00 50.44 ?  82  LYS A CA    1 
ATOM   670   C  C     . LYS A 1 82  ? 115.078 150.616 83.380  1.00 50.45 ?  82  LYS A C     1 
ATOM   671   O  O     . LYS A 1 82  ? 115.040 149.597 82.682  1.00 52.83 ?  82  LYS A O     1 
ATOM   672   C  CB    . LYS A 1 82  ? 113.431 152.447 82.967  1.00 51.75 ?  82  LYS A CB    1 
ATOM   673   C  CG    . LYS A 1 82  ? 112.140 153.170 83.307  1.00 53.41 ?  82  LYS A CG    1 
ATOM   674   C  CD    . LYS A 1 82  ? 110.946 152.242 83.280  1.00 53.59 ?  82  LYS A CD    1 
ATOM   675   C  CE    . LYS A 1 82  ? 109.869 152.766 82.346  1.00 54.29 ?  82  LYS A CE    1 
ATOM   676   N  NZ    . LYS A 1 82  ? 110.410 153.059 80.989  1.00 52.75 1  82  LYS A NZ    1 
ATOM   677   N  N     . THR A 1 83  ? 116.225 151.196 83.735  1.00 43.33 ?  83  THR A N     1 
ATOM   678   C  CA    . THR A 1 83  ? 117.503 150.612 83.342  1.00 45.07 ?  83  THR A CA    1 
ATOM   679   C  C     . THR A 1 83  ? 117.665 149.213 83.920  1.00 46.81 ?  83  THR A C     1 
ATOM   680   O  O     . THR A 1 83  ? 118.164 148.307 83.242  1.00 47.75 ?  83  THR A O     1 
ATOM   681   C  CB    . THR A 1 83  ? 118.652 151.518 83.788  1.00 46.72 ?  83  THR A CB    1 
ATOM   682   O  OG1   . THR A 1 83  ? 118.437 152.842 83.287  1.00 50.88 ?  83  THR A OG1   1 
ATOM   683   C  CG2   . THR A 1 83  ? 119.976 151.000 83.258  1.00 46.24 ?  83  THR A CG2   1 
ATOM   684   N  N     . ALA A 1 84  ? 117.246 149.016 85.171  1.00 46.18 ?  84  ALA A N     1 
ATOM   685   C  CA    . ALA A 1 84  ? 117.317 147.684 85.766  1.00 41.53 ?  84  ALA A CA    1 
ATOM   686   C  C     . ALA A 1 84  ? 116.402 146.701 85.048  1.00 42.96 ?  84  ALA A C     1 
ATOM   687   O  O     . ALA A 1 84  ? 116.806 145.571 84.749  1.00 47.86 ?  84  ALA A O     1 
ATOM   688   C  CB    . ALA A 1 84  ? 116.966 147.751 87.250  1.00 43.85 ?  84  ALA A CB    1 
ATOM   689   N  N     . TYR A 1 85  ? 115.166 147.111 84.759  1.00 47.92 ?  85  TYR A N     1 
ATOM   690   C  CA    . TYR A 1 85  ? 114.202 146.211 84.141  1.00 47.31 ?  85  TYR A CA    1 
ATOM   691   C  C     . TYR A 1 85  ? 114.384 146.082 82.635  1.00 46.51 ?  85  TYR A C     1 
ATOM   692   O  O     . TYR A 1 85  ? 113.842 145.146 82.040  1.00 49.04 ?  85  TYR A O     1 
ATOM   693   C  CB    . TYR A 1 85  ? 112.777 146.675 84.450  1.00 47.59 ?  85  TYR A CB    1 
ATOM   694   C  CG    . TYR A 1 85  ? 112.295 146.290 85.830  1.00 48.42 ?  85  TYR A CG    1 
ATOM   695   C  CD1   . TYR A 1 85  ? 112.520 147.116 86.922  1.00 47.29 ?  85  TYR A CD1   1 
ATOM   696   C  CD2   . TYR A 1 85  ? 111.617 145.098 86.041  1.00 46.70 ?  85  TYR A CD2   1 
ATOM   697   C  CE1   . TYR A 1 85  ? 112.082 146.769 88.184  1.00 46.62 ?  85  TYR A CE1   1 
ATOM   698   C  CE2   . TYR A 1 85  ? 111.175 144.742 87.298  1.00 46.81 ?  85  TYR A CE2   1 
ATOM   699   C  CZ    . TYR A 1 85  ? 111.411 145.580 88.365  1.00 47.28 ?  85  TYR A CZ    1 
ATOM   700   O  OH    . TYR A 1 85  ? 110.972 145.227 89.619  1.00 49.55 ?  85  TYR A OH    1 
ATOM   701   N  N     . ALA A 1 86  ? 115.129 146.995 82.004  1.00 45.11 ?  86  ALA A N     1 
ATOM   702   C  CA    . ALA A 1 86  ? 115.361 146.888 80.568  1.00 44.63 ?  86  ALA A CA    1 
ATOM   703   C  C     . ALA A 1 86  ? 116.212 145.674 80.224  1.00 47.07 ?  86  ALA A C     1 
ATOM   704   O  O     . ALA A 1 86  ? 116.079 145.114 79.131  1.00 48.77 ?  86  ALA A O     1 
ATOM   705   C  CB    . ALA A 1 86  ? 116.023 148.160 80.040  1.00 44.19 ?  86  ALA A CB    1 
ATOM   706   N  N     . LYS A 1 87  ? 117.093 145.261 81.137  1.00 46.25 ?  87  LYS A N     1 
ATOM   707   C  CA    . LYS A 1 87  ? 117.925 144.090 80.889  1.00 45.97 ?  87  LYS A CA    1 
ATOM   708   C  C     . LYS A 1 87  ? 117.086 142.821 80.795  1.00 45.92 ?  87  LYS A C     1 
ATOM   709   O  O     . LYS A 1 87  ? 117.460 141.884 80.080  1.00 45.76 ?  87  LYS A O     1 
ATOM   710   C  CB    . LYS A 1 87  ? 118.982 143.966 81.991  1.00 42.62 ?  87  LYS A CB    1 
ATOM   711   C  CG    . LYS A 1 87  ? 119.576 142.577 82.165  1.00 44.03 ?  87  LYS A CG    1 
ATOM   712   C  CD    . LYS A 1 87  ? 120.950 142.472 81.525  1.00 45.15 ?  87  LYS A CD    1 
ATOM   713   C  CE    . LYS A 1 87  ? 121.575 141.114 81.793  1.00 45.16 ?  87  LYS A CE    1 
ATOM   714   N  NZ    . LYS A 1 87  ? 122.922 140.987 81.173  1.00 42.00 1  87  LYS A NZ    1 
ATOM   715   N  N     . LYS A 1 88  ? 115.940 142.790 81.475  1.00 48.62 ?  88  LYS A N     1 
ATOM   716   C  CA    . LYS A 1 88  ? 115.098 141.598 81.561  1.00 47.59 ?  88  LYS A CA    1 
ATOM   717   C  C     . LYS A 1 88  ? 115.909 140.406 82.061  1.00 43.20 ?  88  LYS A C     1 
ATOM   718   O  O     . LYS A 1 88  ? 115.968 139.349 81.431  1.00 46.03 ?  88  LYS A O     1 
ATOM   719   C  CB    . LYS A 1 88  ? 114.432 141.290 80.218  1.00 49.47 ?  88  LYS A CB    1 
ATOM   720   C  CG    . LYS A 1 88  ? 113.120 142.024 79.991  1.00 49.24 ?  88  LYS A CG    1 
ATOM   721   C  CD    . LYS A 1 88  ? 112.712 142.003 78.525  1.00 47.96 ?  88  LYS A CD    1 
ATOM   722   C  CE    . LYS A 1 88  ? 113.914 142.116 77.603  1.00 49.54 ?  88  LYS A CE    1 
ATOM   723   N  NZ    . LYS A 1 88  ? 113.513 142.116 76.170  1.00 47.96 1  88  LYS A NZ    1 
ATOM   724   N  N     . PHE A 1 89  ? 116.553 140.598 83.210  1.00 42.48 ?  89  PHE A N     1 
ATOM   725   C  CA    . PHE A 1 89  ? 117.395 139.558 83.781  1.00 38.98 ?  89  PHE A CA    1 
ATOM   726   C  C     . PHE A 1 89  ? 116.560 138.347 84.169  1.00 41.01 ?  89  PHE A C     1 
ATOM   727   O  O     . PHE A 1 89  ? 115.476 138.474 84.742  1.00 44.65 ?  89  PHE A O     1 
ATOM   728   C  CB    . PHE A 1 89  ? 118.146 140.095 85.000  1.00 35.95 ?  89  PHE A CB    1 
ATOM   729   C  CG    . PHE A 1 89  ? 118.847 139.034 85.799  1.00 37.82 ?  89  PHE A CG    1 
ATOM   730   C  CD1   . PHE A 1 89  ? 120.117 138.615 85.451  1.00 35.27 ?  89  PHE A CD1   1 
ATOM   731   C  CD2   . PHE A 1 89  ? 118.236 138.457 86.901  1.00 35.78 ?  89  PHE A CD2   1 
ATOM   732   C  CE1   . PHE A 1 89  ? 120.762 137.640 86.180  1.00 37.73 ?  89  PHE A CE1   1 
ATOM   733   C  CE2   . PHE A 1 89  ? 118.878 137.482 87.632  1.00 35.76 ?  89  PHE A CE2   1 
ATOM   734   C  CZ    . PHE A 1 89  ? 120.141 137.074 87.273  1.00 38.16 ?  89  PHE A CZ    1 
ATOM   735   N  N     . ARG A 1 90  ? 117.076 137.163 83.852  1.00 41.13 ?  90  ARG A N     1 
ATOM   736   C  CA    . ARG A 1 90  ? 116.441 135.907 84.219  1.00 40.95 ?  90  ARG A CA    1 
ATOM   737   C  C     . ARG A 1 90  ? 117.453 135.044 84.954  1.00 41.23 ?  90  ARG A C     1 
ATOM   738   O  O     . ARG A 1 90  ? 118.580 134.867 84.481  1.00 43.62 ?  90  ARG A O     1 
ATOM   739   C  CB    . ARG A 1 90  ? 115.905 135.169 82.989  1.00 42.51 ?  90  ARG A CB    1 
ATOM   740   C  CG    . ARG A 1 90  ? 114.943 135.986 82.147  1.00 42.59 ?  90  ARG A CG    1 
ATOM   741   C  CD    . ARG A 1 90  ? 113.527 135.901 82.690  1.00 45.13 ?  90  ARG A CD    1 
ATOM   742   N  NE    . ARG A 1 90  ? 112.642 136.863 82.047  1.00 45.28 ?  90  ARG A NE    1 
ATOM   743   C  CZ    . ARG A 1 90  ? 112.408 138.087 82.503  1.00 47.41 ?  90  ARG A CZ    1 
ATOM   744   N  NH1   . ARG A 1 90  ? 112.962 138.526 83.620  1.00 46.93 1  90  ARG A NH1   1 
ATOM   745   N  NH2   . ARG A 1 90  ? 111.596 138.888 81.820  1.00 44.82 ?  90  ARG A NH2   1 
ATOM   746   N  N     . PHE A 1 91  ? 117.054 134.521 86.102  1.00 36.44 ?  91  PHE A N     1 
ATOM   747   C  CA    . PHE A 1 91  ? 117.917 133.618 86.846  1.00 36.22 ?  91  PHE A CA    1 
ATOM   748   C  C     . PHE A 1 91  ? 118.106 132.329 86.053  1.00 42.87 ?  91  PHE A C     1 
ATOM   749   O  O     . PHE A 1 91  ? 117.119 131.727 85.614  1.00 45.07 ?  91  PHE A O     1 
ATOM   750   C  CB    . PHE A 1 91  ? 117.319 133.320 88.216  1.00 35.20 ?  91  PHE A CB    1 
ATOM   751   C  CG    . PHE A 1 91  ? 117.400 134.473 89.174  1.00 39.44 ?  91  PHE A CG    1 
ATOM   752   C  CD1   . PHE A 1 91  ? 118.543 134.690 89.925  1.00 42.42 ?  91  PHE A CD1   1 
ATOM   753   C  CD2   . PHE A 1 91  ? 116.336 135.344 89.322  1.00 39.20 ?  91  PHE A CD2   1 
ATOM   754   C  CE1   . PHE A 1 91  ? 118.619 135.748 90.807  1.00 38.91 ?  91  PHE A CE1   1 
ATOM   755   C  CE2   . PHE A 1 91  ? 116.407 136.405 90.202  1.00 39.18 ?  91  PHE A CE2   1 
ATOM   756   C  CZ    . PHE A 1 91  ? 117.550 136.606 90.946  1.00 38.29 ?  91  PHE A CZ    1 
ATOM   757   N  N     . PRO A 1 92  ? 119.346 131.877 85.842  1.00 41.57 ?  92  PRO A N     1 
ATOM   758   C  CA    . PRO A 1 92  ? 119.555 130.680 85.018  1.00 37.12 ?  92  PRO A CA    1 
ATOM   759   C  C     . PRO A 1 92  ? 119.247 129.381 85.734  1.00 38.04 ?  92  PRO A C     1 
ATOM   760   O  O     . PRO A 1 92  ? 119.098 128.348 85.067  1.00 40.67 ?  92  PRO A O     1 
ATOM   761   C  CB    . PRO A 1 92  ? 121.042 130.769 84.657  1.00 38.47 ?  92  PRO A CB    1 
ATOM   762   C  CG    . PRO A 1 92  ? 121.650 131.453 85.833  1.00 39.59 ?  92  PRO A CG    1 
ATOM   763   C  CD    . PRO A 1 92  ? 120.611 132.405 86.382  1.00 40.78 ?  92  PRO A CD    1 
ATOM   764   N  N     . SER A 1 93  ? 119.145 129.393 87.060  1.00 39.30 ?  93  SER A N     1 
ATOM   765   C  CA    . SER A 1 93  ? 118.937 128.182 87.832  1.00 42.91 ?  93  SER A CA    1 
ATOM   766   C  C     . SER A 1 93  ? 117.951 128.467 88.954  1.00 44.00 ?  93  SER A C     1 
ATOM   767   O  O     . SER A 1 93  ? 117.737 129.616 89.344  1.00 46.31 ?  93  SER A O     1 
ATOM   768   C  CB    . SER A 1 93  ? 120.258 127.651 88.404  1.00 41.29 ?  93  SER A CB    1 
ATOM   769   O  OG    . SER A 1 93  ? 120.671 128.411 89.525  1.00 40.49 ?  93  SER A OG    1 
ATOM   770   N  N     . PHE A 1 94  ? 117.345 127.396 89.467  1.00 41.93 ?  94  PHE A N     1 
ATOM   771   C  CA    . PHE A 1 94  ? 116.407 127.545 90.575  1.00 42.32 ?  94  PHE A CA    1 
ATOM   772   C  C     . PHE A 1 94  ? 117.112 128.020 91.838  1.00 43.88 ?  94  PHE A C     1 
ATOM   773   O  O     . PHE A 1 94  ? 116.548 128.801 92.611  1.00 46.67 ?  94  PHE A O     1 
ATOM   774   C  CB    . PHE A 1 94  ? 115.673 126.231 90.835  1.00 41.55 ?  94  PHE A CB    1 
ATOM   775   C  CG    . PHE A 1 94  ? 115.021 126.165 92.185  1.00 43.53 ?  94  PHE A CG    1 
ATOM   776   C  CD1   . PHE A 1 94  ? 113.910 126.939 92.468  1.00 44.19 ?  94  PHE A CD1   1 
ATOM   777   C  CD2   . PHE A 1 94  ? 115.518 125.334 93.172  1.00 44.94 ?  94  PHE A CD2   1 
ATOM   778   C  CE1   . PHE A 1 94  ? 113.311 126.888 93.708  1.00 43.92 ?  94  PHE A CE1   1 
ATOM   779   C  CE2   . PHE A 1 94  ? 114.921 125.278 94.415  1.00 46.60 ?  94  PHE A CE2   1 
ATOM   780   C  CZ    . PHE A 1 94  ? 113.817 126.057 94.683  1.00 44.64 ?  94  PHE A CZ    1 
ATOM   781   N  N     . MET A 1 95  ? 118.339 127.550 92.073  1.00 41.38 ?  95  MET A N     1 
ATOM   782   C  CA    . MET A 1 95  ? 119.048 127.917 93.294  1.00 36.23 ?  95  MET A CA    1 
ATOM   783   C  C     . MET A 1 95  ? 119.338 129.410 93.352  1.00 39.46 ?  95  MET A C     1 
ATOM   784   O  O     . MET A 1 95  ? 119.260 130.016 94.423  1.00 45.02 ?  95  MET A O     1 
ATOM   785   C  CB    . MET A 1 95  ? 120.346 127.120 93.418  1.00 42.26 ?  95  MET A CB    1 
ATOM   786   C  CG    . MET A 1 95  ? 120.752 126.701 94.839  1.00 44.32 ?  95  MET A CG    1 
ATOM   787   S  SD    . MET A 1 95  ? 119.495 126.369 96.102  1.00 53.46 ?  95  MET A SD    1 
ATOM   788   C  CE    . MET A 1 95  ? 118.349 125.285 95.253  1.00 45.67 ?  95  MET A CE    1 
ATOM   789   N  N     . SER A 1 96  ? 119.682 130.020 92.217  1.00 35.10 ?  96  SER A N     1 
ATOM   790   C  CA    . SER A 1 96  ? 119.975 131.450 92.209  1.00 33.05 ?  96  SER A CA    1 
ATOM   791   C  C     . SER A 1 96  ? 118.779 132.257 92.698  1.00 34.07 ?  96  SER A C     1 
ATOM   792   O  O     . SER A 1 96  ? 118.887 133.049 93.646  1.00 34.98 ?  96  SER A O     1 
ATOM   793   C  CB    . SER A 1 96  ? 120.371 131.883 90.799  1.00 35.24 ?  96  SER A CB    1 
ATOM   794   O  OG    . SER A 1 96  ? 121.153 130.887 90.166  1.00 38.59 ?  96  SER A OG    1 
ATOM   795   N  N     . ALA A 1 97  ? 117.620 132.042 92.075  1.00 40.03 ?  97  ALA A N     1 
ATOM   796   C  CA    . ALA A 1 97  ? 116.419 132.778 92.450  1.00 37.07 ?  97  ALA A CA    1 
ATOM   797   C  C     . ALA A 1 97  ? 115.967 132.421 93.858  1.00 37.56 ?  97  ALA A C     1 
ATOM   798   O  O     . ALA A 1 97  ? 115.519 133.291 94.609  1.00 45.57 ?  97  ALA A O     1 
ATOM   799   C  CB    . ALA A 1 97  ? 115.306 132.501 91.445  1.00 36.46 ?  97  ALA A CB    1 
ATOM   800   N  N     . PHE A 1 98  ? 116.064 131.143 94.228  1.00 33.25 ?  98  PHE A N     1 
ATOM   801   C  CA    . PHE A 1 98  ? 115.646 130.729 95.561  1.00 35.49 ?  98  PHE A CA    1 
ATOM   802   C  C     . PHE A 1 98  ? 116.493 131.404 96.629  1.00 37.06 ?  98  PHE A C     1 
ATOM   803   O  O     . PHE A 1 98  ? 115.965 131.939 97.610  1.00 45.07 ?  98  PHE A O     1 
ATOM   804   C  CB    . PHE A 1 98  ? 115.730 129.208 95.686  1.00 40.98 ?  98  PHE A CB    1 
ATOM   805   C  CG    . PHE A 1 98  ? 115.546 128.708 97.088  1.00 42.29 ?  98  PHE A CG    1 
ATOM   806   C  CD1   . PHE A 1 98  ? 114.279 128.605 97.636  1.00 41.66 ?  98  PHE A CD1   1 
ATOM   807   C  CD2   . PHE A 1 98  ? 116.636 128.350 97.861  1.00 42.38 ?  98  PHE A CD2   1 
ATOM   808   C  CE1   . PHE A 1 98  ? 114.104 128.152 98.924  1.00 41.14 ?  98  PHE A CE1   1 
ATOM   809   C  CE2   . PHE A 1 98  ? 116.466 127.897 99.152  1.00 42.94 ?  98  PHE A CE2   1 
ATOM   810   C  CZ    . PHE A 1 98  ? 115.198 127.796 99.684  1.00 42.27 ?  98  PHE A CZ    1 
ATOM   811   N  N     . LYS A 1 99  ? 117.813 131.400 96.446  1.00 39.01 ?  99  LYS A N     1 
ATOM   812   C  CA    . LYS A 1 99  ? 118.698 132.040 97.408  1.00 38.77 ?  99  LYS A CA    1 
ATOM   813   C  C     . LYS A 1 99  ? 118.442 133.537 97.475  1.00 39.03 ?  99  LYS A C     1 
ATOM   814   O  O     . LYS A 1 99  ? 118.401 134.112 98.569  1.00 41.24 ?  99  LYS A O     1 
ATOM   815   C  CB    . LYS A 1 99  ? 120.157 131.756 97.052  1.00 38.86 ?  99  LYS A CB    1 
ATOM   816   C  CG    . LYS A 1 99  ? 120.595 130.333 97.348  1.00 41.35 ?  99  LYS A CG    1 
ATOM   817   C  CD    . LYS A 1 99  ? 120.187 129.906 98.745  1.00 43.43 ?  99  LYS A CD    1 
ATOM   818   C  CE    . LYS A 1 99  ? 121.340 129.248 99.477  1.00 41.25 ?  99  LYS A CE    1 
ATOM   819   N  NZ    . LYS A 1 99  ? 121.220 129.414 100.950 1.00 42.13 1  99  LYS A NZ    1 
ATOM   820   N  N     . PHE A 1 100 ? 118.242 134.188 96.324  1.00 34.65 ?  100 PHE A N     1 
ATOM   821   C  CA    . PHE A 1 100 ? 117.967 135.619 96.364  1.00 34.54 ?  100 PHE A CA    1 
ATOM   822   C  C     . PHE A 1 100 ? 116.676 135.911 97.115  1.00 36.68 ?  100 PHE A C     1 
ATOM   823   O  O     . PHE A 1 100 ? 116.660 136.713 98.055  1.00 42.14 ?  100 PHE A O     1 
ATOM   824   C  CB    . PHE A 1 100 ? 117.894 136.212 94.960  1.00 36.23 ?  100 PHE A CB    1 
ATOM   825   C  CG    . PHE A 1 100 ? 117.479 137.652 94.960  1.00 36.68 ?  100 PHE A CG    1 
ATOM   826   C  CD1   . PHE A 1 100 ? 118.358 138.632 95.387  1.00 37.98 ?  100 PHE A CD1   1 
ATOM   827   C  CD2   . PHE A 1 100 ? 116.202 138.024 94.581  1.00 36.45 ?  100 PHE A CD2   1 
ATOM   828   C  CE1   . PHE A 1 100 ? 117.980 139.956 95.414  1.00 38.96 ?  100 PHE A CE1   1 
ATOM   829   C  CE2   . PHE A 1 100 ? 115.818 139.347 94.605  1.00 39.45 ?  100 PHE A CE2   1 
ATOM   830   C  CZ    . PHE A 1 100 ? 116.709 140.315 95.023  1.00 39.03 ?  100 PHE A CZ    1 
ATOM   831   N  N     . TYR A 1 101 ? 115.583 135.254 96.733  1.00 41.22 ?  101 TYR A N     1 
ATOM   832   C  CA    . TYR A 1 101 ? 114.287 135.561 97.320  1.00 38.44 ?  101 TYR A CA    1 
ATOM   833   C  C     . TYR A 1 101 ? 114.116 134.993 98.719  1.00 40.02 ?  101 TYR A C     1 
ATOM   834   O  O     . TYR A 1 101 ? 113.109 135.289 99.369  1.00 46.64 ?  101 TYR A O     1 
ATOM   835   C  CB    . TYR A 1 101 ? 113.168 135.068 96.400  1.00 38.76 ?  101 TYR A CB    1 
ATOM   836   C  CG    . TYR A 1 101 ? 113.023 135.917 95.158  1.00 36.64 ?  101 TYR A CG    1 
ATOM   837   C  CD1   . TYR A 1 101 ? 112.496 137.198 95.230  1.00 39.62 ?  101 TYR A CD1   1 
ATOM   838   C  CD2   . TYR A 1 101 ? 113.436 135.449 93.920  1.00 35.22 ?  101 TYR A CD2   1 
ATOM   839   C  CE1   . TYR A 1 101 ? 112.372 137.984 94.102  1.00 39.29 ?  101 TYR A CE1   1 
ATOM   840   C  CE2   . TYR A 1 101 ? 113.316 136.226 92.788  1.00 39.50 ?  101 TYR A CE2   1 
ATOM   841   C  CZ    . TYR A 1 101 ? 112.784 137.493 92.883  1.00 41.13 ?  101 TYR A CZ    1 
ATOM   842   O  OH    . TYR A 1 101 ? 112.664 138.270 91.755  1.00 39.45 ?  101 TYR A OH    1 
ATOM   843   N  N     . ASN A 1 102 ? 115.065 134.190 99.200  1.00 40.55 ?  102 ASN A N     1 
ATOM   844   C  CA    . ASN A 1 102 ? 115.036 133.728 100.579 1.00 41.46 ?  102 ASN A CA    1 
ATOM   845   C  C     . ASN A 1 102 ? 115.992 134.478 101.495 1.00 43.05 ?  102 ASN A C     1 
ATOM   846   O  O     . ASN A 1 102 ? 115.750 134.522 102.706 1.00 45.65 ?  102 ASN A O     1 
ATOM   847   C  CB    . ASN A 1 102 ? 115.360 132.230 100.642 1.00 42.60 ?  102 ASN A CB    1 
ATOM   848   C  CG    . ASN A 1 102 ? 114.119 131.363 100.608 1.00 44.82 ?  102 ASN A CG    1 
ATOM   849   O  OD1   . ASN A 1 102 ? 113.224 131.570 99.789  1.00 46.40 ?  102 ASN A OD1   1 
ATOM   850   N  ND2   . ASN A 1 102 ? 114.057 130.385 101.503 1.00 44.73 ?  102 ASN A ND2   1 
ATOM   851   N  N     . ASP A 1 103 ? 117.062 135.067 100.965 1.00 43.44 ?  103 ASP A N     1 
ATOM   852   C  CA    . ASP A 1 103 ? 118.070 135.716 101.795 1.00 41.09 ?  103 ASP A CA    1 
ATOM   853   C  C     . ASP A 1 103 ? 118.148 137.222 101.614 1.00 41.31 ?  103 ASP A C     1 
ATOM   854   O  O     . ASP A 1 103 ? 118.343 137.941 102.595 1.00 47.96 ?  103 ASP A O     1 
ATOM   855   C  CB    . ASP A 1 103 ? 119.450 135.112 101.511 1.00 44.45 ?  103 ASP A CB    1 
ATOM   856   C  CG    . ASP A 1 103 ? 119.554 133.662 101.938 1.00 46.42 ?  103 ASP A CG    1 
ATOM   857   O  OD1   . ASP A 1 103 ? 118.544 133.105 102.417 1.00 47.25 ?  103 ASP A OD1   1 
ATOM   858   O  OD2   . ASP A 1 103 ? 120.646 133.076 101.792 1.00 48.74 -1 103 ASP A OD2   1 
ATOM   859   N  N     . TYR A 1 104 ? 118.005 137.729 100.387 1.00 31.26 ?  104 TYR A N     1 
ATOM   860   C  CA    . TYR A 1 104 ? 118.269 139.130 100.103 1.00 37.51 ?  104 TYR A CA    1 
ATOM   861   C  C     . TYR A 1 104 ? 117.047 139.922 99.664  1.00 39.68 ?  104 TYR A C     1 
ATOM   862   O  O     . TYR A 1 104 ? 117.048 141.148 99.811  1.00 44.70 ?  104 TYR A O     1 
ATOM   863   C  CB    . TYR A 1 104 ? 119.351 139.254 99.021  1.00 36.23 ?  104 TYR A CB    1 
ATOM   864   C  CG    . TYR A 1 104 ? 120.627 138.525 99.366  1.00 39.20 ?  104 TYR A CG    1 
ATOM   865   C  CD1   . TYR A 1 104 ? 121.601 139.126 100.150 1.00 34.99 ?  104 TYR A CD1   1 
ATOM   866   C  CD2   . TYR A 1 104 ? 120.853 137.231 98.917  1.00 34.27 ?  104 TYR A CD2   1 
ATOM   867   C  CE1   . TYR A 1 104 ? 122.764 138.461 100.473 1.00 36.30 ?  104 TYR A CE1   1 
ATOM   868   C  CE2   . TYR A 1 104 ? 122.014 136.557 99.236  1.00 34.79 ?  104 TYR A CE2   1 
ATOM   869   C  CZ    . TYR A 1 104 ? 122.967 137.178 100.015 1.00 39.47 ?  104 TYR A CZ    1 
ATOM   870   O  OH    . TYR A 1 104 ? 124.126 136.514 100.338 1.00 37.58 ?  104 TYR A OH    1 
ATOM   871   N  N     . ALA A 1 105 ? 116.020 139.271 99.128  1.00 39.31 ?  105 ALA A N     1 
ATOM   872   C  CA    . ALA A 1 105 ? 114.833 139.995 98.699  1.00 40.02 ?  105 ALA A CA    1 
ATOM   873   C  C     . ALA A 1 105 ? 114.083 140.550 99.903  1.00 43.24 ?  105 ALA A C     1 
ATOM   874   O  O     . ALA A 1 105 ? 113.904 139.865 100.914 1.00 41.64 ?  105 ALA A O     1 
ATOM   875   C  CB    . ALA A 1 105 ? 113.915 139.088 97.884  1.00 37.86 ?  105 ALA A CB    1 
ATOM   876   N  N     . LEU A 1 106 ? 113.654 141.803 99.793  1.00 47.41 ?  106 LEU A N     1 
ATOM   877   C  CA    . LEU A 1 106 ? 112.898 142.428 100.867 1.00 45.87 ?  106 LEU A CA    1 
ATOM   878   C  C     . LEU A 1 106 ? 111.525 141.783 100.998 1.00 47.88 ?  106 LEU A C     1 
ATOM   879   O  O     . LEU A 1 106 ? 110.833 141.545 100.006 1.00 46.17 ?  106 LEU A O     1 
ATOM   880   C  CB    . LEU A 1 106 ? 112.753 143.928 100.615 1.00 46.17 ?  106 LEU A CB    1 
ATOM   881   C  CG    . LEU A 1 106 ? 112.105 144.752 101.728 1.00 44.92 ?  106 LEU A CG    1 
ATOM   882   C  CD1   . LEU A 1 106 ? 113.002 144.799 102.952 1.00 43.99 ?  106 LEU A CD1   1 
ATOM   883   C  CD2   . LEU A 1 106 ? 111.803 146.151 101.237 1.00 45.17 ?  106 LEU A CD2   1 
ATOM   884   N  N     . LYS A 1 107 ? 111.135 141.505 102.236 1.00 54.76 ?  107 LYS A N     1 
ATOM   885   C  CA    . LYS A 1 107 ? 109.847 140.909 102.543 1.00 53.91 ?  107 LYS A CA    1 
ATOM   886   C  C     . LYS A 1 107 ? 109.092 141.801 103.517 1.00 54.18 ?  107 LYS A C     1 
ATOM   887   O  O     . LYS A 1 107 ? 109.676 142.650 104.196 1.00 54.39 ?  107 LYS A O     1 
ATOM   888   C  CB    . LYS A 1 107 ? 110.011 139.502 103.134 1.00 51.79 ?  107 LYS A CB    1 
ATOM   889   C  CG    . LYS A 1 107 ? 110.441 138.456 102.123 1.00 50.81 ?  107 LYS A CG    1 
ATOM   890   C  CD    . LYS A 1 107 ? 110.735 137.128 102.796 1.00 55.44 ?  107 LYS A CD    1 
ATOM   891   C  CE    . LYS A 1 107 ? 111.123 136.071 101.778 1.00 54.96 ?  107 LYS A CE    1 
ATOM   892   N  NZ    . LYS A 1 107 ? 111.734 134.873 102.419 1.00 51.84 1  107 LYS A NZ    1 
ATOM   893   N  N     . THR A 1 108 ? 107.777 141.605 103.569 1.00 60.48 ?  108 THR A N     1 
ATOM   894   C  CA    . THR A 1 108 ? 106.943 142.370 104.479 1.00 61.10 ?  108 THR A CA    1 
ATOM   895   C  C     . THR A 1 108 ? 107.337 142.080 105.929 1.00 62.03 ?  108 THR A C     1 
ATOM   896   O  O     . THR A 1 108 ? 108.079 141.142 106.227 1.00 60.42 ?  108 THR A O     1 
ATOM   897   C  CB    . THR A 1 108 ? 105.468 142.050 104.250 1.00 60.24 ?  108 THR A CB    1 
ATOM   898   O  OG1   . THR A 1 108 ? 105.305 140.639 104.067 1.00 62.28 ?  108 THR A OG1   1 
ATOM   899   C  CG2   . THR A 1 108 ? 104.954 142.776 103.016 1.00 59.01 ?  108 THR A CG2   1 
ATOM   900   N  N     . ASN A 1 109 ? 106.822 142.911 106.838 1.00 63.53 ?  109 ASN A N     1 
ATOM   901   C  CA    . ASN A 1 109 ? 107.235 142.833 108.236 1.00 62.62 ?  109 ASN A CA    1 
ATOM   902   C  C     . ASN A 1 109 ? 106.902 141.484 108.858 1.00 64.06 ?  109 ASN A C     1 
ATOM   903   O  O     . ASN A 1 109 ? 107.571 141.057 109.806 1.00 65.05 ?  109 ASN A O     1 
ATOM   904   C  CB    . ASN A 1 109 ? 106.584 143.961 109.035 1.00 62.62 ?  109 ASN A CB    1 
ATOM   905   C  CG    . ASN A 1 109 ? 107.332 145.270 108.903 1.00 62.85 ?  109 ASN A CG    1 
ATOM   906   O  OD1   . ASN A 1 109 ? 108.555 145.288 108.780 1.00 64.74 ?  109 ASN A OD1   1 
ATOM   907   N  ND2   . ASN A 1 109 ? 106.598 146.376 108.925 1.00 63.04 ?  109 ASN A ND2   1 
ATOM   908   N  N     . ASP A 1 110 ? 105.884 140.797 108.345 1.00 68.70 ?  110 ASP A N     1 
ATOM   909   C  CA    . ASP A 1 110 ? 105.508 139.478 108.831 1.00 67.94 ?  110 ASP A CA    1 
ATOM   910   C  C     . ASP A 1 110 ? 106.161 138.353 108.038 1.00 68.31 ?  110 ASP A C     1 
ATOM   911   O  O     . ASP A 1 110 ? 105.800 137.188 108.226 1.00 69.86 ?  110 ASP A O     1 
ATOM   912   C  CB    . ASP A 1 110 ? 103.985 139.322 108.806 1.00 67.40 ?  110 ASP A CB    1 
ATOM   913   C  CG    . ASP A 1 110 ? 103.360 139.909 107.558 1.00 68.90 ?  110 ASP A CG    1 
ATOM   914   O  OD1   . ASP A 1 110 ? 103.988 140.789 106.935 1.00 69.20 ?  110 ASP A OD1   1 
ATOM   915   O  OD2   . ASP A 1 110 ? 102.240 139.491 107.199 1.00 70.98 -1 110 ASP A OD2   1 
ATOM   916   N  N     . LYS A 1 111 ? 107.113 138.680 107.159 1.00 66.46 ?  111 LYS A N     1 
ATOM   917   C  CA    . LYS A 1 111 ? 107.800 137.693 106.322 1.00 65.58 ?  111 LYS A CA    1 
ATOM   918   C  C     . LYS A 1 111 ? 106.807 136.885 105.491 1.00 65.91 ?  111 LYS A C     1 
ATOM   919   O  O     . LYS A 1 111 ? 106.959 135.677 105.306 1.00 67.92 ?  111 LYS A O     1 
ATOM   920   C  CB    . LYS A 1 111 ? 108.683 136.763 107.161 1.00 65.10 ?  111 LYS A CB    1 
ATOM   921   C  CG    . LYS A 1 111 ? 109.833 137.441 107.898 1.00 65.13 ?  111 LYS A CG    1 
ATOM   922   C  CD    . LYS A 1 111 ? 110.395 138.627 107.131 1.00 66.65 ?  111 LYS A CD    1 
ATOM   923   C  CE    . LYS A 1 111 ? 110.384 139.886 107.983 1.00 66.83 ?  111 LYS A CE    1 
ATOM   924   N  NZ    . LYS A 1 111 ? 110.875 141.073 107.229 1.00 64.70 1  111 LYS A NZ    1 
ATOM   925   N  N     . LYS A 1 112 ? 105.777 137.561 104.982 1.00 64.63 ?  112 LYS A N     1 
ATOM   926   C  CA    . LYS A 1 112 ? 104.686 136.901 104.276 1.00 66.88 ?  112 LYS A CA    1 
ATOM   927   C  C     . LYS A 1 112 ? 104.795 137.034 102.763 1.00 66.69 ?  112 LYS A C     1 
ATOM   928   O  O     . LYS A 1 112 ? 104.768 136.028 102.050 1.00 68.00 ?  112 LYS A O     1 
ATOM   929   C  CB    . LYS A 1 112 ? 103.342 137.463 104.754 1.00 66.48 ?  112 LYS A CB    1 
ATOM   930   C  CG    . LYS A 1 112 ? 102.142 136.616 104.368 1.00 67.80 ?  112 LYS A CG    1 
ATOM   931   C  CD    . LYS A 1 112 ? 102.132 135.291 105.116 1.00 68.20 ?  112 LYS A CD    1 
ATOM   932   C  CE    . LYS A 1 112 ? 102.272 135.494 106.619 1.00 68.46 ?  112 LYS A CE    1 
ATOM   933   N  NZ    . LYS A 1 112 ? 101.252 136.436 107.155 1.00 66.80 1  112 LYS A NZ    1 
ATOM   934   N  N     . LYS A 1 113 ? 104.916 138.255 102.260 1.00 59.74 ?  113 LYS A N     1 
ATOM   935   C  CA    . LYS A 1 113 ? 104.979 138.525 100.834 1.00 57.63 ?  113 LYS A CA    1 
ATOM   936   C  C     . LYS A 1 113 ? 106.354 139.078 100.471 1.00 57.10 ?  113 LYS A C     1 
ATOM   937   O  O     . LYS A 1 113 ? 107.217 139.285 101.328 1.00 58.08 ?  113 LYS A O     1 
ATOM   938   C  CB    . LYS A 1 113 ? 103.865 139.491 100.425 1.00 58.63 ?  113 LYS A CB    1 
ATOM   939   C  CG    . LYS A 1 113 ? 102.467 138.903 100.522 1.00 58.57 ?  113 LYS A CG    1 
ATOM   940   C  CD    . LYS A 1 113 ? 102.199 137.927 99.390  1.00 61.20 ?  113 LYS A CD    1 
ATOM   941   C  CE    . LYS A 1 113 ? 100.783 137.380 99.451  1.00 59.99 ?  113 LYS A CE    1 
ATOM   942   N  NZ    . LYS A 1 113 ? 100.536 136.369 98.387  1.00 58.80 1  113 LYS A NZ    1 
ATOM   943   N  N     . ILE A 1 114 ? 106.551 139.322 99.178  1.00 53.70 ?  114 ILE A N     1 
ATOM   944   C  CA    . ILE A 1 114 ? 107.829 139.768 98.636  1.00 52.40 ?  114 ILE A CA    1 
ATOM   945   C  C     . ILE A 1 114 ? 107.649 141.182 98.101  1.00 50.13 ?  114 ILE A C     1 
ATOM   946   O  O     . ILE A 1 114 ? 106.766 141.432 97.271  1.00 52.75 ?  114 ILE A O     1 
ATOM   947   C  CB    . ILE A 1 114 ? 108.338 138.822 97.538  1.00 52.98 ?  114 ILE A CB    1 
ATOM   948   C  CG1   . ILE A 1 114 ? 108.864 137.525 98.155  1.00 51.59 ?  114 ILE A CG1   1 
ATOM   949   C  CG2   . ILE A 1 114 ? 109.421 139.489 96.709  1.00 52.71 ?  114 ILE A CG2   1 
ATOM   950   C  CD1   . ILE A 1 114 ? 108.953 136.382 97.175  1.00 51.35 ?  114 ILE A CD1   1 
ATOM   951   N  N     . LEU A 1 115 ? 108.484 142.104 98.575  1.00 49.22 ?  115 LEU A N     1 
ATOM   952   C  CA    . LEU A 1 115 ? 108.432 143.498 98.153  1.00 51.09 ?  115 LEU A CA    1 
ATOM   953   C  C     . LEU A 1 115 ? 109.416 143.823 97.040  1.00 51.90 ?  115 LEU A C     1 
ATOM   954   O  O     . LEU A 1 115 ? 109.085 144.594 96.136  1.00 52.05 ?  115 LEU A O     1 
ATOM   955   C  CB    . LEU A 1 115 ? 108.697 144.422 99.345  1.00 50.85 ?  115 LEU A CB    1 
ATOM   956   C  CG    . LEU A 1 115 ? 107.637 144.411 100.444 1.00 49.79 ?  115 LEU A CG    1 
ATOM   957   C  CD1   . LEU A 1 115 ? 108.249 144.791 101.780 1.00 50.56 ?  115 LEU A CD1   1 
ATOM   958   C  CD2   . LEU A 1 115 ? 106.499 145.344 100.081 1.00 50.74 ?  115 LEU A CD2   1 
ATOM   959   N  N     . GLU A 1 116 ? 110.613 143.250 97.080  1.00 49.12 ?  116 GLU A N     1 
ATOM   960   C  CA    . GLU A 1 116 ? 111.672 143.561 96.131  1.00 45.80 ?  116 GLU A CA    1 
ATOM   961   C  C     . GLU A 1 116 ? 111.884 142.396 95.178  1.00 46.41 ?  116 GLU A C     1 
ATOM   962   O  O     . GLU A 1 116 ? 111.948 141.240 95.607  1.00 50.13 ?  116 GLU A O     1 
ATOM   963   C  CB    . GLU A 1 116 ? 112.983 143.873 96.854  1.00 44.75 ?  116 GLU A CB    1 
ATOM   964   C  CG    . GLU A 1 116 ? 113.262 145.345 97.045  1.00 44.63 ?  116 GLU A CG    1 
ATOM   965   C  CD    . GLU A 1 116 ? 114.496 145.590 97.885  1.00 47.03 ?  116 GLU A CD    1 
ATOM   966   O  OE1   . GLU A 1 116 ? 114.993 144.626 98.501  1.00 46.08 ?  116 GLU A OE1   1 
ATOM   967   O  OE2   . GLU A 1 116 ? 114.970 146.744 97.929  1.00 48.24 -1 116 GLU A OE2   1 
ATOM   968   N  N     . ARG A 1 117 ? 111.991 142.704 93.890  1.00 42.37 ?  117 ARG A N     1 
ATOM   969   C  CA    . ARG A 1 117 ? 112.507 141.758 92.916  1.00 42.21 ?  117 ARG A CA    1 
ATOM   970   C  C     . ARG A 1 117 ? 114.025 141.918 92.856  1.00 43.77 ?  117 ARG A C     1 
ATOM   971   O  O     . ARG A 1 117 ? 114.620 142.678 93.624  1.00 47.51 ?  117 ARG A O     1 
ATOM   972   C  CB    . ARG A 1 117 ? 111.846 141.973 91.556  1.00 42.43 ?  117 ARG A CB    1 
ATOM   973   C  CG    . ARG A 1 117 ? 110.327 141.966 91.587  1.00 44.77 ?  117 ARG A CG    1 
ATOM   974   C  CD    . ARG A 1 117 ? 109.791 140.737 92.305  1.00 49.50 ?  117 ARG A CD    1 
ATOM   975   N  NE    . ARG A 1 117 ? 109.906 139.529 91.497  1.00 47.61 ?  117 ARG A NE    1 
ATOM   976   C  CZ    . ARG A 1 117 ? 109.100 139.217 90.491  1.00 47.19 ?  117 ARG A CZ    1 
ATOM   977   N  NH1   . ARG A 1 117 ? 108.096 140.003 90.140  1.00 48.28 1  117 ARG A NH1   1 
ATOM   978   N  NH2   . ARG A 1 117 ? 109.305 138.086 89.823  1.00 47.65 ?  117 ARG A NH2   1 
ATOM   979   N  N     . TYR A 1 118 ? 114.677 141.192 91.947  1.00 42.19 ?  118 TYR A N     1 
ATOM   980   C  CA    . TYR A 1 118 ? 116.111 141.375 91.762  1.00 36.17 ?  118 TYR A CA    1 
ATOM   981   C  C     . TYR A 1 118 ? 116.415 142.768 91.226  1.00 37.76 ?  118 TYR A C     1 
ATOM   982   O  O     . TYR A 1 118 ? 117.358 143.430 91.680  1.00 40.66 ?  118 TYR A O     1 
ATOM   983   C  CB    . TYR A 1 118 ? 116.655 140.300 90.822  1.00 36.88 ?  118 TYR A CB    1 
ATOM   984   C  CG    . TYR A 1 118 ? 118.156 140.153 90.844  1.00 36.73 ?  118 TYR A CG    1 
ATOM   985   C  CD1   . TYR A 1 118 ? 118.833 139.930 92.034  1.00 36.21 ?  118 TYR A CD1   1 
ATOM   986   C  CD2   . TYR A 1 118 ? 118.896 140.229 89.675  1.00 36.96 ?  118 TYR A CD2   1 
ATOM   987   C  CE1   . TYR A 1 118 ? 120.203 139.792 92.057  1.00 35.71 ?  118 TYR A CE1   1 
ATOM   988   C  CE2   . TYR A 1 118 ? 120.265 140.086 89.687  1.00 31.19 ?  118 TYR A CE2   1 
ATOM   989   C  CZ    . TYR A 1 118 ? 120.914 139.869 90.880  1.00 35.72 ?  118 TYR A CZ    1 
ATOM   990   O  OH    . TYR A 1 118 ? 122.282 139.732 90.896  1.00 45.66 ?  118 TYR A OH    1 
ATOM   991   N  N     . GLU A 1 119 ? 115.609 143.237 90.271  1.00 41.38 ?  119 GLU A N     1 
ATOM   992   C  CA    . GLU A 1 119 ? 115.813 144.563 89.704  1.00 38.57 ?  119 GLU A CA    1 
ATOM   993   C  C     . GLU A 1 119 ? 115.586 145.655 90.742  1.00 40.41 ?  119 GLU A C     1 
ATOM   994   O  O     . GLU A 1 119 ? 116.307 146.656 90.757  1.00 43.54 ?  119 GLU A O     1 
ATOM   995   C  CB    . GLU A 1 119 ? 114.895 144.764 88.501  1.00 40.57 ?  119 GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 119 ? 115.369 144.066 87.242  1.00 41.16 ?  119 GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 119 ? 114.812 142.664 87.102  1.00 43.69 ?  119 GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 119 ? 114.386 142.084 88.123  1.00 43.92 ?  119 GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 119 ? 114.807 142.139 85.970  1.00 44.72 -1 119 GLU A OE2   1 
ATOM   1000  N  N     . ASP A 1 120 ? 114.591 145.484 91.615  1.00 42.16 ?  120 ASP A N     1 
ATOM   1001  C  CA    . ASP A 1 120 ? 114.336 146.485 92.646  1.00 38.20 ?  120 ASP A CA    1 
ATOM   1002  C  C     . ASP A 1 120 ? 115.504 146.583 93.618  1.00 38.64 ?  120 ASP A C     1 
ATOM   1003  O  O     . ASP A 1 120 ? 115.960 147.685 93.948  1.00 45.44 ?  120 ASP A O     1 
ATOM   1004  C  CB    . ASP A 1 120 ? 113.045 146.153 93.395  1.00 42.51 ?  120 ASP A CB    1 
ATOM   1005  C  CG    . ASP A 1 120 ? 111.876 145.924 92.463  1.00 47.73 ?  120 ASP A CG    1 
ATOM   1006  O  OD1   . ASP A 1 120 ? 111.794 146.621 91.431  1.00 46.98 ?  120 ASP A OD1   1 
ATOM   1007  O  OD2   . ASP A 1 120 ? 111.038 145.049 92.762  1.00 51.12 -1 120 ASP A OD2   1 
ATOM   1008  N  N     . ARG A 1 121 ? 116.001 145.437 94.088  1.00 33.43 ?  121 ARG A N     1 
ATOM   1009  C  CA    . ARG A 1 121 ? 117.141 145.438 94.997  1.00 32.95 ?  121 ARG A CA    1 
ATOM   1010  C  C     . ARG A 1 121 ? 118.370 146.043 94.335  1.00 34.25 ?  121 ARG A C     1 
ATOM   1011  O  O     . ARG A 1 121 ? 119.086 146.842 94.951  1.00 41.31 ?  121 ARG A O     1 
ATOM   1012  C  CB    . ARG A 1 121 ? 117.435 144.014 95.470  1.00 34.34 ?  121 ARG A CB    1 
ATOM   1013  C  CG    . ARG A 1 121 ? 118.587 143.906 96.453  1.00 32.95 ?  121 ARG A CG    1 
ATOM   1014  C  CD    . ARG A 1 121 ? 118.095 144.000 97.885  1.00 33.48 ?  121 ARG A CD    1 
ATOM   1015  N  NE    . ARG A 1 121 ? 118.949 144.851 98.703  1.00 38.02 ?  121 ARG A NE    1 
ATOM   1016  C  CZ    . ARG A 1 121 ? 118.658 146.099 99.044  1.00 37.23 ?  121 ARG A CZ    1 
ATOM   1017  N  NH1   . ARG A 1 121 ? 117.541 146.683 98.645  1.00 36.19 1  121 ARG A NH1   1 
ATOM   1018  N  NH2   . ARG A 1 121 ? 119.511 146.779 99.804  1.00 34.72 ?  121 ARG A NH2   1 
ATOM   1019  N  N     . ILE A 1 122 ? 118.624 145.686 93.075  1.00 33.17 ?  122 ILE A N     1 
ATOM   1020  C  CA    . ILE A 1 122 ? 119.789 146.219 92.377  1.00 29.12 ?  122 ILE A CA    1 
ATOM   1021  C  C     . ILE A 1 122 ? 119.661 147.725 92.188  1.00 30.95 ?  122 ILE A C     1 
ATOM   1022  O  O     . ILE A 1 122 ? 120.631 148.468 92.372  1.00 36.66 ?  122 ILE A O     1 
ATOM   1023  C  CB    . ILE A 1 122 ? 119.992 145.483 91.041  1.00 32.31 ?  122 ILE A CB    1 
ATOM   1024  C  CG1   . ILE A 1 122 ? 120.740 144.174 91.283  1.00 27.19 ?  122 ILE A CG1   1 
ATOM   1025  C  CG2   . ILE A 1 122 ? 120.749 146.352 90.048  1.00 33.57 ?  122 ILE A CG2   1 
ATOM   1026  C  CD1   . ILE A 1 122 ? 121.068 143.432 90.030  1.00 33.73 ?  122 ILE A CD1   1 
ATOM   1027  N  N     . SER A 1 123 ? 118.468 148.204 91.827  1.00 34.94 ?  123 SER A N     1 
ATOM   1028  C  CA    . SER A 1 123 ? 118.266 149.638 91.648  1.00 32.04 ?  123 SER A CA    1 
ATOM   1029  C  C     . SER A 1 123 ? 118.451 150.392 92.955  1.00 31.85 ?  123 SER A C     1 
ATOM   1030  O  O     . SER A 1 123 ? 119.038 151.479 92.974  1.00 39.19 ?  123 SER A O     1 
ATOM   1031  C  CB    . SER A 1 123 ? 116.872 149.903 91.080  1.00 34.60 ?  123 SER A CB    1 
ATOM   1032  O  OG    . SER A 1 123 ? 116.537 148.950 90.093  1.00 39.38 ?  123 SER A OG    1 
ATOM   1033  N  N     . ILE A 1 124 ? 117.947 149.839 94.060  1.00 31.75 ?  124 ILE A N     1 
ATOM   1034  C  CA    . ILE A 1 124 ? 118.114 150.498 95.350  1.00 34.84 ?  124 ILE A CA    1 
ATOM   1035  C  C     . ILE A 1 124 ? 119.586 150.543 95.743  1.00 36.09 ?  124 ILE A C     1 
ATOM   1036  O  O     . ILE A 1 124 ? 120.084 151.573 96.214  1.00 39.49 ?  124 ILE A O     1 
ATOM   1037  C  CB    . ILE A 1 124 ? 117.253 149.806 96.419  1.00 38.69 ?  124 ILE A CB    1 
ATOM   1038  C  CG1   . ILE A 1 124 ? 115.771 150.057 96.136  1.00 39.24 ?  124 ILE A CG1   1 
ATOM   1039  C  CG2   . ILE A 1 124 ? 117.616 150.299 97.807  1.00 33.39 ?  124 ILE A CG2   1 
ATOM   1040  C  CD1   . ILE A 1 124 ? 115.446 151.506 95.837  1.00 37.19 ?  124 ILE A CD1   1 
ATOM   1041  N  N     . VAL A 1 125 ? 120.308 149.437 95.544  1.00 32.10 ?  125 VAL A N     1 
ATOM   1042  C  CA    . VAL A 1 125 ? 121.733 149.413 95.861  1.00 29.01 ?  125 VAL A CA    1 
ATOM   1043  C  C     . VAL A 1 125 ? 122.494 150.408 94.989  1.00 28.32 ?  125 VAL A C     1 
ATOM   1044  O  O     . VAL A 1 125 ? 123.417 151.084 95.454  1.00 39.80 ?  125 VAL A O     1 
ATOM   1045  C  CB    . VAL A 1 125 ? 122.285 147.982 95.715  1.00 33.53 ?  125 VAL A CB    1 
ATOM   1046  C  CG1   . VAL A 1 125 ? 123.789 147.969 95.862  1.00 30.75 ?  125 VAL A CG1   1 
ATOM   1047  C  CG2   . VAL A 1 125 ? 121.659 147.070 96.753  1.00 28.67 ?  125 VAL A CG2   1 
ATOM   1048  N  N     . ALA A 1 126 ? 122.102 150.530 93.720  1.00 26.22 ?  126 ALA A N     1 
ATOM   1049  C  CA    . ALA A 1 126 ? 122.780 151.452 92.816  1.00 26.65 ?  126 ALA A CA    1 
ATOM   1050  C  C     . ALA A 1 126 ? 122.518 152.903 93.192  1.00 34.15 ?  126 ALA A C     1 
ATOM   1051  O  O     . ALA A 1 126 ? 123.432 153.735 93.155  1.00 39.43 ?  126 ALA A O     1 
ATOM   1052  C  CB    . ALA A 1 126 ? 122.336 151.189 91.381  1.00 29.39 ?  126 ALA A CB    1 
ATOM   1053  N  N     . LEU A 1 127 ? 121.272 153.231 93.542  1.00 36.11 ?  127 LEU A N     1 
ATOM   1054  C  CA    . LEU A 1 127 ? 120.960 154.586 93.979  1.00 32.17 ?  127 LEU A CA    1 
ATOM   1055  C  C     . LEU A 1 127 ? 121.647 154.912 95.298  1.00 30.19 ?  127 LEU A C     1 
ATOM   1056  O  O     . LEU A 1 127 ? 122.020 156.068 95.531  1.00 35.16 ?  127 LEU A O     1 
ATOM   1057  C  CB    . LEU A 1 127 ? 119.448 154.763 94.103  1.00 33.59 ?  127 LEU A CB    1 
ATOM   1058  C  CG    . LEU A 1 127 ? 118.662 154.746 92.791  1.00 34.25 ?  127 LEU A CG    1 
ATOM   1059  C  CD1   . LEU A 1 127 ? 117.226 154.321 93.032  1.00 36.24 ?  127 LEU A CD1   1 
ATOM   1060  C  CD2   . LEU A 1 127 ? 118.711 156.099 92.109  1.00 34.84 ?  127 LEU A CD2   1 
ATOM   1061  N  N     . PHE A 1 128 ? 121.811 153.917 96.170  1.00 32.75 ?  128 PHE A N     1 
ATOM   1062  C  CA    . PHE A 1 128 ? 122.592 154.114 97.384  1.00 32.86 ?  128 PHE A CA    1 
ATOM   1063  C  C     . PHE A 1 128 ? 124.058 154.383 97.060  1.00 30.93 ?  128 PHE A C     1 
ATOM   1064  O  O     . PHE A 1 128 ? 124.680 155.267 97.658  1.00 38.78 ?  128 PHE A O     1 
ATOM   1065  C  CB    . PHE A 1 128 ? 122.449 152.890 98.288  1.00 30.53 ?  128 PHE A CB    1 
ATOM   1066  C  CG    . PHE A 1 128 ? 123.310 152.933 99.516  1.00 35.69 ?  128 PHE A CG    1 
ATOM   1067  C  CD1   . PHE A 1 128 ? 122.870 153.573 100.661 1.00 37.91 ?  128 PHE A CD1   1 
ATOM   1068  C  CD2   . PHE A 1 128 ? 124.551 152.321 99.530  1.00 33.56 ?  128 PHE A CD2   1 
ATOM   1069  C  CE1   . PHE A 1 128 ? 123.657 153.609 101.793 1.00 38.80 ?  128 PHE A CE1   1 
ATOM   1070  C  CE2   . PHE A 1 128 ? 125.342 152.360 100.656 1.00 33.60 ?  128 PHE A CE2   1 
ATOM   1071  C  CZ    . PHE A 1 128 ? 124.894 153.001 101.790 1.00 35.48 ?  128 PHE A CZ    1 
ATOM   1072  N  N     . PHE A 1 129 ? 124.625 153.626 96.117  1.00 28.02 ?  129 PHE A N     1 
ATOM   1073  C  CA    . PHE A 1 129 ? 126.029 153.805 95.756  1.00 25.55 ?  129 PHE A CA    1 
ATOM   1074  C  C     . PHE A 1 129 ? 126.280 155.165 95.120  1.00 29.30 ?  129 PHE A C     1 
ATOM   1075  O  O     . PHE A 1 129 ? 127.274 155.829 95.434  1.00 33.20 ?  129 PHE A O     1 
ATOM   1076  C  CB    . PHE A 1 129 ? 126.474 152.699 94.799  1.00 26.16 ?  129 PHE A CB    1 
ATOM   1077  C  CG    . PHE A 1 129 ? 126.709 151.376 95.458  1.00 25.05 ?  129 PHE A CG    1 
ATOM   1078  C  CD1   . PHE A 1 129 ? 126.854 151.283 96.829  1.00 27.59 ?  129 PHE A CD1   1 
ATOM   1079  C  CD2   . PHE A 1 129 ? 126.799 150.223 94.699  1.00 26.52 ?  129 PHE A CD2   1 
ATOM   1080  C  CE1   . PHE A 1 129 ? 127.071 150.064 97.431  1.00 24.89 ?  129 PHE A CE1   1 
ATOM   1081  C  CE2   . PHE A 1 129 ? 127.022 149.003 95.296  1.00 26.00 ?  129 PHE A CE2   1 
ATOM   1082  C  CZ    . PHE A 1 129 ? 127.158 148.924 96.664  1.00 27.59 ?  129 PHE A CZ    1 
ATOM   1083  N  N     . ALA A 1 130 ? 125.395 155.593 94.219  1.00 35.43 ?  130 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 130 ? 125.666 156.783 93.421  1.00 35.20 ?  130 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 130 ? 125.614 158.058 94.251  1.00 42.34 ?  130 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 130 ? 126.316 159.026 93.934  1.00 47.09 ?  130 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 130 ? 124.680 156.867 92.262  1.00 34.43 ?  130 ALA A CB    1 
ATOM   1088  N  N     . ASN A 1 131 ? 124.789 158.084 95.299  1.00 42.79 ?  131 ASN A N     1 
ATOM   1089  C  CA    . ASN A 1 131 ? 124.709 159.217 96.222  1.00 43.74 ?  131 ASN A CA    1 
ATOM   1090  C  C     . ASN A 1 131 ? 124.324 160.507 95.494  1.00 43.29 ?  131 ASN A C     1 
ATOM   1091  O  O     . ASN A 1 131 ? 124.993 161.536 95.605  1.00 47.94 ?  131 ASN A O     1 
ATOM   1092  C  CB    . ASN A 1 131 ? 126.023 159.387 96.990  1.00 43.48 ?  131 ASN A CB    1 
ATOM   1093  C  CG    . ASN A 1 131 ? 125.862 160.222 98.243  1.00 48.16 ?  131 ASN A CG    1 
ATOM   1094  O  OD1   . ASN A 1 131 ? 124.908 160.049 99.001  1.00 44.83 ?  131 ASN A OD1   1 
ATOM   1095  N  ND2   . ASN A 1 131 ? 126.799 161.134 98.469  1.00 46.49 ?  131 ASN A ND2   1 
ATOM   1096  N  N     . GLY A 1 132 ? 123.228 160.443 94.741  1.00 41.46 ?  132 GLY A N     1 
ATOM   1097  C  CA    . GLY A 1 132 ? 122.673 161.596 94.071  1.00 41.96 ?  132 GLY A CA    1 
ATOM   1098  C  C     . GLY A 1 132 ? 122.939 161.669 92.581  1.00 44.87 ?  132 GLY A C     1 
ATOM   1099  O  O     . GLY A 1 132 ? 122.271 162.445 91.889  1.00 49.08 ?  132 GLY A O     1 
ATOM   1100  N  N     . ASP A 1 133 ? 123.884 160.887 92.067  1.00 47.04 ?  133 ASP A N     1 
ATOM   1101  C  CA    . ASP A 1 133 ? 124.236 160.922 90.653  1.00 46.05 ?  133 ASP A CA    1 
ATOM   1102  C  C     . ASP A 1 133 ? 123.356 159.942 89.884  1.00 49.14 ?  133 ASP A C     1 
ATOM   1103  O  O     . ASP A 1 133 ? 123.348 158.744 90.179  1.00 49.71 ?  133 ASP A O     1 
ATOM   1104  C  CB    . ASP A 1 133 ? 125.714 160.589 90.460  1.00 48.23 ?  133 ASP A CB    1 
ATOM   1105  C  CG    . ASP A 1 133 ? 126.278 161.154 89.171  1.00 53.27 ?  133 ASP A CG    1 
ATOM   1106  O  OD1   . ASP A 1 133 ? 125.498 161.373 88.220  1.00 52.24 ?  133 ASP A OD1   1 
ATOM   1107  O  OD2   . ASP A 1 133 ? 127.504 161.381 89.109  1.00 52.57 -1 133 ASP A OD2   1 
ATOM   1108  N  N     . THR A 1 134 ? 122.616 160.453 88.899  1.00 48.73 ?  134 THR A N     1 
ATOM   1109  C  CA    . THR A 1 134 ? 121.728 159.591 88.124  1.00 47.99 ?  134 THR A CA    1 
ATOM   1110  C  C     . THR A 1 134 ? 122.509 158.717 87.150  1.00 49.88 ?  134 THR A C     1 
ATOM   1111  O  O     . THR A 1 134 ? 122.237 157.517 87.026  1.00 51.80 ?  134 THR A O     1 
ATOM   1112  C  CB    . THR A 1 134 ? 120.703 160.443 87.378  1.00 52.41 ?  134 THR A CB    1 
ATOM   1113  O  OG1   . THR A 1 134 ? 119.851 161.092 88.327  1.00 53.72 ?  134 THR A OG1   1 
ATOM   1114  C  CG2   . THR A 1 134 ? 119.855 159.579 86.459  1.00 51.31 ?  134 THR A CG2   1 
ATOM   1115  N  N     . GLU A 1 135 ? 123.486 159.302 86.451  1.00 47.24 ?  135 GLU A N     1 
ATOM   1116  C  CA    . GLU A 1 135 ? 124.279 158.532 85.499  1.00 47.75 ?  135 GLU A CA    1 
ATOM   1117  C  C     . GLU A 1 135 ? 125.107 157.466 86.205  1.00 48.60 ?  135 GLU A C     1 
ATOM   1118  O  O     . GLU A 1 135 ? 125.235 156.341 85.709  1.00 51.03 ?  135 GLU A O     1 
ATOM   1119  C  CB    . GLU A 1 135 ? 125.178 159.465 84.692  1.00 49.48 ?  135 GLU A CB    1 
ATOM   1120  C  CG    . GLU A 1 135 ? 124.419 160.493 83.875  1.00 48.79 ?  135 GLU A CG    1 
ATOM   1121  C  CD    . GLU A 1 135 ? 123.323 159.870 83.035  1.00 54.08 ?  135 GLU A CD    1 
ATOM   1122  O  OE1   . GLU A 1 135 ? 123.637 159.001 82.195  1.00 54.31 ?  135 GLU A OE1   1 
ATOM   1123  O  OE2   . GLU A 1 135 ? 122.146 160.247 83.218  1.00 55.23 -1 135 GLU A OE2   1 
ATOM   1124  N  N     . LYS A 1 136 ? 125.681 157.803 87.362  1.00 40.59 ?  136 LYS A N     1 
ATOM   1125  C  CA    . LYS A 1 136 ? 126.420 156.812 88.134  1.00 40.58 ?  136 LYS A CA    1 
ATOM   1126  C  C     . LYS A 1 136 ? 125.498 155.706 88.631  1.00 41.54 ?  136 LYS A C     1 
ATOM   1127  O  O     . LYS A 1 136 ? 125.888 154.535 88.673  1.00 44.71 ?  136 LYS A O     1 
ATOM   1128  C  CB    . LYS A 1 136 ? 127.137 157.489 89.302  1.00 45.00 ?  136 LYS A CB    1 
ATOM   1129  C  CG    . LYS A 1 136 ? 128.297 156.694 89.867  1.00 42.10 ?  136 LYS A CG    1 
ATOM   1130  C  CD    . LYS A 1 136 ? 129.512 156.780 88.965  1.00 43.50 ?  136 LYS A CD    1 
ATOM   1131  C  CE    . LYS A 1 136 ? 130.790 156.482 89.729  1.00 46.23 ?  136 LYS A CE    1 
ATOM   1132  N  NZ    . LYS A 1 136 ? 131.996 156.722 88.891  1.00 47.84 1  136 LYS A NZ    1 
ATOM   1133  N  N     . ALA A 1 137 ? 124.270 156.061 89.017  1.00 39.31 ?  137 ALA A N     1 
ATOM   1134  C  CA    . ALA A 1 137 ? 123.306 155.047 89.429  1.00 34.47 ?  137 ALA A CA    1 
ATOM   1135  C  C     . ALA A 1 137 ? 122.969 154.109 88.277  1.00 36.75 ?  137 ALA A C     1 
ATOM   1136  O  O     . ALA A 1 137 ? 122.855 152.894 88.470  1.00 39.98 ?  137 ALA A O     1 
ATOM   1137  C  CB    . ALA A 1 137 ? 122.042 155.712 89.971  1.00 36.06 ?  137 ALA A CB    1 
ATOM   1138  N  N     . LYS A 1 138 ? 122.807 154.657 87.071  1.00 40.72 ?  138 LYS A N     1 
ATOM   1139  C  CA    . LYS A 1 138 ? 122.567 153.812 85.904  1.00 40.87 ?  138 LYS A CA    1 
ATOM   1140  C  C     . LYS A 1 138 ? 123.768 152.924 85.605  1.00 41.41 ?  138 LYS A C     1 
ATOM   1141  O  O     . LYS A 1 138 ? 123.606 151.762 85.214  1.00 43.37 ?  138 LYS A O     1 
ATOM   1142  C  CB    . LYS A 1 138 ? 122.218 154.676 84.693  1.00 45.21 ?  138 LYS A CB    1 
ATOM   1143  C  CG    . LYS A 1 138 ? 120.798 155.213 84.704  1.00 44.02 ?  138 LYS A CG    1 
ATOM   1144  C  CD    . LYS A 1 138 ? 120.687 156.494 83.901  1.00 43.87 ?  138 LYS A CD    1 
ATOM   1145  C  CE    . LYS A 1 138 ? 120.443 156.202 82.431  1.00 47.11 ?  138 LYS A CE    1 
ATOM   1146  N  NZ    . LYS A 1 138 ? 120.458 157.442 81.610  1.00 48.97 1  138 LYS A NZ    1 
ATOM   1147  N  N     . GLU A 1 139 ? 124.980 153.455 85.773  1.00 40.08 ?  139 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 139 ? 126.179 152.645 85.579  1.00 36.52 ?  139 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 139 ? 126.238 151.493 86.576  1.00 34.97 ?  139 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 139 ? 126.575 150.362 86.212  1.00 40.47 ?  139 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 139 ? 127.427 153.520 85.697  1.00 38.10 ?  139 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 139 ? 127.797 154.254 84.421  1.00 41.30 ?  139 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 139 ? 128.909 155.260 84.631  1.00 48.31 ?  139 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 139 ? 128.958 155.878 85.715  1.00 45.67 ?  139 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 139 ? 129.737 155.436 83.713  1.00 48.32 -1 139 GLU A OE2   1 
ATOM   1156  N  N     . TYR A 1 140 ? 125.914 151.764 87.842  1.00 32.51 ?  140 TYR A N     1 
ATOM   1157  C  CA    . TYR A 1 140 ? 125.884 150.705 88.848  1.00 30.56 ?  140 TYR A CA    1 
ATOM   1158  C  C     . TYR A 1 140 ? 124.802 149.678 88.533  1.00 33.75 ?  140 TYR A C     1 
ATOM   1159  O  O     . TYR A 1 140 ? 124.998 148.474 88.739  1.00 34.13 ?  140 TYR A O     1 
ATOM   1160  C  CB    . TYR A 1 140 ? 125.653 151.300 90.234  1.00 32.61 ?  140 TYR A CB    1 
ATOM   1161  C  CG    . TYR A 1 140 ? 126.860 151.951 90.860  1.00 32.42 ?  140 TYR A CG    1 
ATOM   1162  C  CD1   . TYR A 1 140 ? 128.037 151.243 91.053  1.00 34.45 ?  140 TYR A CD1   1 
ATOM   1163  C  CD2   . TYR A 1 140 ? 126.814 153.271 91.275  1.00 33.15 ?  140 TYR A CD2   1 
ATOM   1164  C  CE1   . TYR A 1 140 ? 129.136 151.839 91.633  1.00 34.20 ?  140 TYR A CE1   1 
ATOM   1165  C  CE2   . TYR A 1 140 ? 127.905 153.875 91.851  1.00 35.74 ?  140 TYR A CE2   1 
ATOM   1166  C  CZ    . TYR A 1 140 ? 129.062 153.158 92.029  1.00 30.78 ?  140 TYR A CZ    1 
ATOM   1167  O  OH    . TYR A 1 140 ? 130.144 153.770 92.609  1.00 33.69 ?  140 TYR A OH    1 
ATOM   1168  N  N     . VAL A 1 141 ? 123.646 150.143 88.052  1.00 33.86 ?  141 VAL A N     1 
ATOM   1169  C  CA    . VAL A 1 141 ? 122.579 149.230 87.655  1.00 33.00 ?  141 VAL A CA    1 
ATOM   1170  C  C     . VAL A 1 141 ? 123.050 148.317 86.536  1.00 35.02 ?  141 VAL A C     1 
ATOM   1171  O  O     . VAL A 1 141 ? 122.818 147.105 86.567  1.00 39.42 ?  141 VAL A O     1 
ATOM   1172  C  CB    . VAL A 1 141 ? 121.323 150.020 87.244  1.00 36.37 ?  141 VAL A CB    1 
ATOM   1173  C  CG1   . VAL A 1 141 ? 120.439 149.169 86.369  1.00 36.42 ?  141 VAL A CG1   1 
ATOM   1174  C  CG2   . VAL A 1 141 ? 120.558 150.450 88.464  1.00 35.34 ?  141 VAL A CG2   1 
ATOM   1175  N  N     . ASN A 1 142 ? 123.719 148.880 85.530  1.00 35.68 ?  142 ASN A N     1 
ATOM   1176  C  CA    . ASN A 1 142 ? 124.245 148.058 84.446  1.00 31.75 ?  142 ASN A CA    1 
ATOM   1177  C  C     . ASN A 1 142 ? 125.286 147.076 84.963  1.00 33.91 ?  142 ASN A C     1 
ATOM   1178  O  O     . ASN A 1 142 ? 125.331 145.921 84.528  1.00 40.10 ?  142 ASN A O     1 
ATOM   1179  C  CB    . ASN A 1 142 ? 124.838 148.946 83.355  1.00 32.37 ?  142 ASN A CB    1 
ATOM   1180  C  CG    . ASN A 1 142 ? 123.782 149.516 82.437  1.00 38.00 ?  142 ASN A CG    1 
ATOM   1181  O  OD1   . ASN A 1 142 ? 122.899 148.801 81.968  1.00 37.20 ?  142 ASN A OD1   1 
ATOM   1182  N  ND2   . ASN A 1 142 ? 123.866 150.815 82.176  1.00 36.90 ?  142 ASN A ND2   1 
ATOM   1183  N  N     . LEU A 1 143 ? 126.135 147.522 85.890  1.00 34.59 ?  143 LEU A N     1 
ATOM   1184  C  CA    . LEU A 1 143 ? 127.180 146.658 86.425  1.00 27.88 ?  143 LEU A CA    1 
ATOM   1185  C  C     . LEU A 1 143 ? 126.597 145.469 87.181  1.00 29.22 ?  143 LEU A C     1 
ATOM   1186  O  O     . LEU A 1 143 ? 127.080 144.340 87.042  1.00 29.56 ?  143 LEU A O     1 
ATOM   1187  C  CB    . LEU A 1 143 ? 128.101 147.471 87.333  1.00 27.94 ?  143 LEU A CB    1 
ATOM   1188  C  CG    . LEU A 1 143 ? 129.529 146.964 87.503  1.00 32.99 ?  143 LEU A CG    1 
ATOM   1189  C  CD1   . LEU A 1 143 ? 130.322 147.238 86.243  1.00 33.82 ?  143 LEU A CD1   1 
ATOM   1190  C  CD2   . LEU A 1 143 ? 130.169 147.640 88.694  1.00 28.96 ?  143 LEU A CD2   1 
ATOM   1191  N  N     . MET A 1 144 ? 125.563 145.700 87.992  1.00 33.23 ?  144 MET A N     1 
ATOM   1192  C  CA    . MET A 1 144 ? 125.038 144.618 88.820  1.00 27.56 ?  144 MET A CA    1 
ATOM   1193  C  C     . MET A 1 144 ? 124.016 143.760 88.081  1.00 28.03 ?  144 MET A C     1 
ATOM   1194  O  O     . MET A 1 144 ? 123.931 142.553 88.328  1.00 31.91 ?  144 MET A O     1 
ATOM   1195  C  CB    . MET A 1 144 ? 124.437 145.176 90.108  1.00 28.77 ?  144 MET A CB    1 
ATOM   1196  C  CG    . MET A 1 144 ? 125.418 145.966 90.955  1.00 30.13 ?  144 MET A CG    1 
ATOM   1197  S  SD    . MET A 1 144 ? 124.722 146.447 92.543  1.00 44.79 ?  144 MET A SD    1 
ATOM   1198  C  CE    . MET A 1 144 ? 123.960 148.004 92.113  1.00 33.81 ?  144 MET A CE    1 
ATOM   1199  N  N     . ILE A 1 145 ? 123.218 144.356 87.191  1.00 28.21 ?  145 ILE A N     1 
ATOM   1200  C  CA    . ILE A 1 145 ? 122.247 143.573 86.432  1.00 30.79 ?  145 ILE A CA    1 
ATOM   1201  C  C     . ILE A 1 145 ? 122.951 142.692 85.407  1.00 33.87 ?  145 ILE A C     1 
ATOM   1202  O  O     . ILE A 1 145 ? 122.481 141.590 85.100  1.00 37.32 ?  145 ILE A O     1 
ATOM   1203  C  CB    . ILE A 1 145 ? 121.187 144.490 85.787  1.00 31.53 ?  145 ILE A CB    1 
ATOM   1204  C  CG1   . ILE A 1 145 ? 119.868 143.736 85.617  1.00 30.46 ?  145 ILE A CG1   1 
ATOM   1205  C  CG2   . ILE A 1 145 ? 121.654 145.039 84.446  1.00 30.98 ?  145 ILE A CG2   1 
ATOM   1206  C  CD1   . ILE A 1 145 ? 119.193 143.370 86.916  1.00 28.31 ?  145 ILE A CD1   1 
ATOM   1207  N  N     . ASN A 1 146 ? 124.080 143.151 84.862  1.00 29.04 ?  146 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 146 ? 124.939 142.272 84.082  1.00 27.56 ?  146 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 146 ? 125.688 141.289 84.965  1.00 29.54 ?  146 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 146 ? 126.343 140.383 84.441  1.00 36.63 ?  146 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 146 ? 125.938 143.087 83.260  1.00 29.11 ?  146 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 146 ? 125.264 143.964 82.226  1.00 33.00 ?  146 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 146 ? 124.100 143.759 81.887  1.00 34.73 ?  146 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 146 ? 125.996 144.947 81.719  1.00 35.28 ?  146 ASN A ND2   1 
ATOM   1215  N  N     . GLN A 1 147 ? 125.603 141.460 86.285  1.00 28.22 ?  147 GLN A N     1 
ATOM   1216  C  CA    . GLN A 1 147 ? 126.265 140.601 87.260  1.00 24.26 ?  147 GLN A CA    1 
ATOM   1217  C  C     . GLN A 1 147 ? 127.773 140.588 87.061  1.00 27.66 ?  147 GLN A C     1 
ATOM   1218  O  O     . GLN A 1 147 ? 128.428 139.571 87.276  1.00 34.10 ?  147 GLN A O     1 
ATOM   1219  C  CB    . GLN A 1 147 ? 125.691 139.182 87.226  1.00 24.18 ?  147 GLN A CB    1 
ATOM   1220  C  CG    . GLN A 1 147 ? 124.248 139.108 87.693  1.00 23.63 ?  147 GLN A CG    1 
ATOM   1221  C  CD    . GLN A 1 147 ? 123.818 137.706 88.054  1.00 27.67 ?  147 GLN A CD    1 
ATOM   1222  O  OE1   . GLN A 1 147 ? 123.158 137.489 89.070  1.00 31.18 ?  147 GLN A OE1   1 
ATOM   1223  N  NE2   . GLN A 1 147 ? 124.181 136.743 87.217  1.00 35.38 ?  147 GLN A NE2   1 
ATOM   1224  N  N     . GLU A 1 148 ? 128.332 141.721 86.630  1.00 26.16 ?  148 GLU A N     1 
ATOM   1225  C  CA    . GLU A 1 148 ? 129.780 141.866 86.553  1.00 22.83 ?  148 GLU A CA    1 
ATOM   1226  C  C     . GLU A 1 148 ? 130.394 142.112 87.922  1.00 26.73 ?  148 GLU A C     1 
ATOM   1227  O  O     . GLU A 1 148 ? 131.516 141.667 88.186  1.00 28.77 ?  148 GLU A O     1 
ATOM   1228  C  CB    . GLU A 1 148 ? 130.142 143.006 85.603  1.00 21.54 ?  148 GLU A CB    1 
ATOM   1229  C  CG    . GLU A 1 148 ? 129.627 142.815 84.191  1.00 25.93 ?  148 GLU A CG    1 
ATOM   1230  C  CD    . GLU A 1 148 ? 129.774 144.061 83.347  1.00 32.88 ?  148 GLU A CD    1 
ATOM   1231  O  OE1   . GLU A 1 148 ? 128.842 144.891 83.340  1.00 33.79 ?  148 GLU A OE1   1 
ATOM   1232  O  OE2   . GLU A 1 148 ? 130.825 144.215 82.692  1.00 36.84 -1 148 GLU A OE2   1 
ATOM   1233  N  N     . TYR A 1 149 ? 129.683 142.818 88.797  1.00 24.71 ?  149 TYR A N     1 
ATOM   1234  C  CA    . TYR A 1 149 ? 130.132 143.083 90.154  1.00 19.22 ?  149 TYR A CA    1 
ATOM   1235  C  C     . TYR A 1 149 ? 129.007 142.761 91.122  1.00 22.08 ?  149 TYR A C     1 
ATOM   1236  O  O     . TYR A 1 149 ? 127.840 143.057 90.853  1.00 27.63 ?  149 TYR A O     1 
ATOM   1237  C  CB    . TYR A 1 149 ? 130.570 144.540 90.321  1.00 19.77 ?  149 TYR A CB    1 
ATOM   1238  C  CG    . TYR A 1 149 ? 130.755 144.975 91.757  1.00 24.10 ?  149 TYR A CG    1 
ATOM   1239  C  CD1   . TYR A 1 149 ? 131.761 144.432 92.544  1.00 16.11 ?  149 TYR A CD1   1 
ATOM   1240  C  CD2   . TYR A 1 149 ? 129.923 145.928 92.324  1.00 21.98 ?  149 TYR A CD2   1 
ATOM   1241  C  CE1   . TYR A 1 149 ? 131.932 144.829 93.853  1.00 16.16 ?  149 TYR A CE1   1 
ATOM   1242  C  CE2   . TYR A 1 149 ? 130.085 146.328 93.631  1.00 21.75 ?  149 TYR A CE2   1 
ATOM   1243  C  CZ    . TYR A 1 149 ? 131.092 145.777 94.391  1.00 18.88 ?  149 TYR A CZ    1 
ATOM   1244  O  OH    . TYR A 1 149 ? 131.256 146.174 95.696  1.00 21.26 ?  149 TYR A OH    1 
ATOM   1245  N  N     . GLN A 1 150 ? 129.362 142.148 92.242  1.00 18.57 ?  150 GLN A N     1 
ATOM   1246  C  CA    . GLN A 1 150 ? 128.394 141.798 93.278  1.00 14.00 ?  150 GLN A CA    1 
ATOM   1247  C  C     . GLN A 1 150 ? 128.831 142.380 94.611  1.00 16.18 ?  150 GLN A C     1 
ATOM   1248  O  O     . GLN A 1 150 ? 129.872 141.964 95.154  1.00 23.41 ?  150 GLN A O     1 
ATOM   1249  C  CB    . GLN A 1 150 ? 128.247 140.281 93.381  1.00 19.28 ?  150 GLN A CB    1 
ATOM   1250  C  CG    . GLN A 1 150 ? 127.493 139.794 94.604  1.00 21.38 ?  150 GLN A CG    1 
ATOM   1251  C  CD    . GLN A 1 150 ? 126.057 140.269 94.639  1.00 16.86 ?  150 GLN A CD    1 
ATOM   1252  O  OE1   . GLN A 1 150 ? 125.240 139.871 93.812  1.00 29.61 ?  150 GLN A OE1   1 
ATOM   1253  N  NE2   . GLN A 1 150 ? 125.742 141.122 95.602  1.00 14.13 ?  150 GLN A NE2   1 
ATOM   1254  N  N     . PRO A 1 151 ? 128.096 143.341 95.168  1.00 25.42 ?  151 PRO A N     1 
ATOM   1255  C  CA    . PRO A 1 151 ? 128.397 143.798 96.528  1.00 16.72 ?  151 PRO A CA    1 
ATOM   1256  C  C     . PRO A 1 151 ? 128.229 142.664 97.527  1.00 18.06 ?  151 PRO A C     1 
ATOM   1257  O  O     . PRO A 1 151 ? 127.444 141.737 97.322  1.00 24.62 ?  151 PRO A O     1 
ATOM   1258  C  CB    . PRO A 1 151 ? 127.374 144.913 96.765  1.00 15.05 ?  151 PRO A CB    1 
ATOM   1259  C  CG    . PRO A 1 151 ? 126.948 145.340 95.401  1.00 20.42 ?  151 PRO A CG    1 
ATOM   1260  C  CD    . PRO A 1 151 ? 127.012 144.117 94.548  1.00 22.10 ?  151 PRO A CD    1 
ATOM   1261  N  N     . SER A 1 152 ? 128.992 142.742 98.613  1.00 20.26 ?  152 SER A N     1 
ATOM   1262  C  CA    . SER A 1 152 ? 128.976 141.691 99.617  1.00 16.72 ?  152 SER A CA    1 
ATOM   1263  C  C     . SER A 1 152 ? 127.581 141.531 100.217 1.00 23.77 ?  152 SER A C     1 
ATOM   1264  O  O     . SER A 1 152 ? 126.701 142.379 100.057 1.00 26.90 ?  152 SER A O     1 
ATOM   1265  C  CB    . SER A 1 152 ? 129.986 141.992 100.721 1.00 25.81 ?  152 SER A CB    1 
ATOM   1266  O  OG    . SER A 1 152 ? 129.568 143.095 101.504 1.00 28.95 ?  152 SER A OG    1 
ATOM   1267  N  N     . THR A 1 153 ? 127.388 140.410 100.912 1.00 30.12 ?  153 THR A N     1 
ATOM   1268  C  CA    . THR A 1 153 ? 126.107 140.125 101.557 1.00 23.96 ?  153 THR A CA    1 
ATOM   1269  C  C     . THR A 1 153 ? 125.626 141.247 102.470 1.00 30.26 ?  153 THR A C     1 
ATOM   1270  O  O     . THR A 1 153 ? 124.444 141.613 102.378 1.00 27.34 ?  153 THR A O     1 
ATOM   1271  C  CB    . THR A 1 153 ? 126.209 138.792 102.314 1.00 23.09 ?  153 THR A CB    1 
ATOM   1272  O  OG1   . THR A 1 153 ? 126.268 137.712 101.375 1.00 35.60 ?  153 THR A OG1   1 
ATOM   1273  C  CG2   . THR A 1 153 ? 125.013 138.592 103.232 1.00 24.13 ?  153 THR A CG2   1 
ATOM   1274  N  N     . PRO A 1 154 ? 126.452 141.840 103.343 1.00 29.45 ?  154 PRO A N     1 
ATOM   1275  C  CA    . PRO A 1 154 ? 125.948 142.974 104.139 1.00 21.01 ?  154 PRO A CA    1 
ATOM   1276  C  C     . PRO A 1 154 ? 125.502 144.152 103.291 1.00 22.76 ?  154 PRO A C     1 
ATOM   1277  O  O     . PRO A 1 154 ? 124.403 144.683 103.497 1.00 30.56 ?  154 PRO A O     1 
ATOM   1278  C  CB    . PRO A 1 154 ? 127.144 143.331 105.030 1.00 23.98 ?  154 PRO A CB    1 
ATOM   1279  C  CG    . PRO A 1 154 ? 127.964 142.112 105.070 1.00 21.87 ?  154 PRO A CG    1 
ATOM   1280  C  CD    . PRO A 1 154 ? 127.826 141.481 103.735 1.00 22.33 ?  154 PRO A CD    1 
ATOM   1281  N  N     . THR A 1 155 ? 126.326 144.574 102.331 1.00 22.52 ?  155 THR A N     1 
ATOM   1282  C  CA    . THR A 1 155 ? 125.971 145.720 101.499 1.00 22.76 ?  155 THR A CA    1 
ATOM   1283  C  C     . THR A 1 155 ? 124.764 145.412 100.623 1.00 25.20 ?  155 THR A C     1 
ATOM   1284  O  O     . THR A 1 155 ? 123.800 146.182 100.590 1.00 25.43 ?  155 THR A O     1 
ATOM   1285  C  CB    . THR A 1 155 ? 127.165 146.135 100.642 1.00 21.27 ?  155 THR A CB    1 
ATOM   1286  O  OG1   . THR A 1 155 ? 128.283 146.429 101.485 1.00 27.97 ?  155 THR A OG1   1 
ATOM   1287  C  CG2   . THR A 1 155 ? 126.825 147.364 99.822  1.00 16.40 ?  155 THR A CG2   1 
ATOM   1288  N  N     . PHE A 1 156 ? 124.794 144.282 99.916  1.00 27.54 ?  156 PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 156 ? 123.690 143.937 99.025  1.00 25.07 ?  156 PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 156 ? 122.393 143.739 99.798  1.00 27.98 ?  156 PHE A C     1 
ATOM   1291  O  O     . PHE A 1 156 ? 121.307 144.042 99.292  1.00 29.53 ?  156 PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 156 ? 124.036 142.679 98.228  1.00 25.40 ?  156 PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 156 ? 123.169 142.467 97.022  1.00 27.47 ?  156 PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 156 ? 123.074 143.440 96.043  1.00 24.32 ?  156 PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 156 ? 122.452 141.294 96.867  1.00 26.19 ?  156 PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 156 ? 122.279 143.246 94.932  1.00 28.99 ?  156 PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 156 ? 121.656 141.095 95.759  1.00 24.92 ?  156 PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 156 ? 121.570 142.073 94.790  1.00 29.97 ?  156 PHE A CZ    1 
ATOM   1299  N  N     . LEU A 1 157 ? 122.487 143.233 101.026 1.00 31.66 ?  157 LEU A N     1 
ATOM   1300  C  CA    . LEU A 1 157 ? 121.301 142.970 101.831 1.00 28.13 ?  157 LEU A CA    1 
ATOM   1301  C  C     . LEU A 1 157 ? 120.747 144.226 102.490 1.00 29.68 ?  157 LEU A C     1 
ATOM   1302  O  O     . LEU A 1 157 ? 119.529 144.341 102.654 1.00 37.88 ?  157 LEU A O     1 
ATOM   1303  C  CB    . LEU A 1 157 ? 121.626 141.919 102.894 1.00 31.34 ?  157 LEU A CB    1 
ATOM   1304  C  CG    . LEU A 1 157 ? 120.524 141.542 103.885 1.00 31.00 ?  157 LEU A CG    1 
ATOM   1305  C  CD1   . LEU A 1 157 ? 119.332 140.956 103.160 1.00 29.27 ?  157 LEU A CD1   1 
ATOM   1306  C  CD2   . LEU A 1 157 ? 121.052 140.567 104.922 1.00 28.33 ?  157 LEU A CD2   1 
ATOM   1307  N  N     . ASN A 1 158 ? 121.603 145.174 102.867 1.00 32.61 ?  158 ASN A N     1 
ATOM   1308  C  CA    . ASN A 1 158 ? 121.184 146.282 103.712 1.00 26.65 ?  158 ASN A CA    1 
ATOM   1309  C  C     . ASN A 1 158 ? 121.254 147.644 103.033 1.00 31.48 ?  158 ASN A C     1 
ATOM   1310  O  O     . ASN A 1 158 ? 120.851 148.637 103.644 1.00 38.42 ?  158 ASN A O     1 
ATOM   1311  C  CB    . ASN A 1 158 ? 122.028 146.304 104.990 1.00 29.21 ?  158 ASN A CB    1 
ATOM   1312  C  CG    . ASN A 1 158 ? 122.009 144.979 105.723 1.00 36.03 ?  158 ASN A CG    1 
ATOM   1313  O  OD1   . ASN A 1 158 ? 120.976 144.318 105.806 1.00 38.85 ?  158 ASN A OD1   1 
ATOM   1314  N  ND2   . ASN A 1 158 ? 123.157 144.582 106.257 1.00 32.53 ?  158 ASN A ND2   1 
ATOM   1315  N  N     . ALA A 1 159 ? 121.747 147.728 101.798 1.00 33.82 ?  159 ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 159 ? 121.875 149.026 101.144 1.00 29.94 ?  159 ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 159 ? 120.513 149.670 100.924 1.00 36.52 ?  159 ALA A C     1 
ATOM   1318  O  O     . ALA A 1 159 ? 119.697 149.166 100.147 1.00 42.82 ?  159 ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 159 ? 122.611 148.897 99.811  1.00 34.55 ?  159 ALA A CB    1 
ATOM   1320  N  N     . GLY A 1 160 ? 120.261 150.783 101.607 1.00 43.17 ?  160 GLY A N     1 
ATOM   1321  C  CA    . GLY A 1 160 ? 119.019 151.508 101.458 1.00 40.60 ?  160 GLY A CA    1 
ATOM   1322  C  C     . GLY A 1 160 ? 117.879 151.054 102.340 1.00 44.10 ?  160 GLY A C     1 
ATOM   1323  O  O     . GLY A 1 160 ? 116.759 151.545 102.170 1.00 45.10 ?  160 GLY A O     1 
ATOM   1324  N  N     . ARG A 1 161 ? 118.121 150.137 103.272 1.00 44.10 ?  161 ARG A N     1 
ATOM   1325  C  CA    . ARG A 1 161 ? 117.092 149.658 104.183 1.00 43.77 ?  161 ARG A CA    1 
ATOM   1326  C  C     . ARG A 1 161 ? 117.192 150.389 105.514 1.00 45.82 ?  161 ARG A C     1 
ATOM   1327  O  O     . ARG A 1 161 ? 118.292 150.681 105.991 1.00 48.53 ?  161 ARG A O     1 
ATOM   1328  C  CB    . ARG A 1 161 ? 117.212 148.149 104.399 1.00 41.51 ?  161 ARG A CB    1 
ATOM   1329  C  CG    . ARG A 1 161 ? 116.969 147.333 103.143 1.00 42.22 ?  161 ARG A CG    1 
ATOM   1330  C  CD    . ARG A 1 161 ? 116.744 145.867 103.460 1.00 41.57 ?  161 ARG A CD    1 
ATOM   1331  N  NE    . ARG A 1 161 ? 116.772 145.047 102.255 1.00 45.49 ?  161 ARG A NE    1 
ATOM   1332  C  CZ    . ARG A 1 161 ? 116.652 143.727 102.241 1.00 45.46 ?  161 ARG A CZ    1 
ATOM   1333  N  NH1   . ARG A 1 161 ? 116.490 143.035 103.357 1.00 43.98 1  161 ARG A NH1   1 
ATOM   1334  N  NH2   . ARG A 1 161 ? 116.704 143.084 101.078 1.00 42.72 ?  161 ARG A NH2   1 
ATOM   1335  N  N     . LYS A 1 162 ? 116.034 150.690 106.108 1.00 53.82 ?  162 LYS A N     1 
ATOM   1336  C  CA    . LYS A 1 162 ? 116.017 151.441 107.359 1.00 52.61 ?  162 LYS A CA    1 
ATOM   1337  C  C     . LYS A 1 162 ? 116.478 150.580 108.528 1.00 54.80 ?  162 LYS A C     1 
ATOM   1338  O  O     . LYS A 1 162 ? 117.492 150.876 109.170 1.00 55.62 ?  162 LYS A O     1 
ATOM   1339  C  CB    . LYS A 1 162 ? 114.615 151.991 107.620 1.00 52.45 ?  162 LYS A CB    1 
ATOM   1340  C  CG    . LYS A 1 162 ? 114.594 153.401 108.183 1.00 55.20 ?  162 LYS A CG    1 
ATOM   1341  C  CD    . LYS A 1 162 ? 113.210 154.018 108.077 1.00 55.29 ?  162 LYS A CD    1 
ATOM   1342  C  CE    . LYS A 1 162 ? 113.274 155.535 108.133 1.00 54.69 ?  162 LYS A CE    1 
ATOM   1343  N  NZ    . LYS A 1 162 ? 114.478 156.011 108.868 1.00 55.20 1  162 LYS A NZ    1 
ATOM   1344  N  N     . ARG A 1 163 ? 115.745 149.508 108.817 1.00 57.23 ?  163 ARG A N     1 
ATOM   1345  C  CA    . ARG A 1 163 ? 116.086 148.608 109.917 1.00 57.25 ?  163 ARG A CA    1 
ATOM   1346  C  C     . ARG A 1 163 ? 117.100 147.578 109.424 1.00 58.83 ?  163 ARG A C     1 
ATOM   1347  O  O     . ARG A 1 163 ? 116.782 146.432 109.103 1.00 57.95 ?  163 ARG A O     1 
ATOM   1348  C  CB    . ARG A 1 163 ? 114.826 147.953 110.474 1.00 60.18 ?  163 ARG A CB    1 
ATOM   1349  C  CG    . ARG A 1 163 ? 113.843 148.944 111.078 1.00 58.41 ?  163 ARG A CG    1 
ATOM   1350  C  CD    . ARG A 1 163 ? 112.492 148.302 111.331 1.00 58.40 ?  163 ARG A CD    1 
ATOM   1351  N  NE    . ARG A 1 163 ? 111.843 147.910 110.087 1.00 60.59 ?  163 ARG A NE    1 
ATOM   1352  C  CZ    . ARG A 1 163 ? 110.738 147.181 110.016 1.00 62.32 ?  163 ARG A CZ    1 
ATOM   1353  N  NH1   . ARG A 1 163 ? 110.121 146.754 111.106 1.00 61.42 1  163 ARG A NH1   1 
ATOM   1354  N  NH2   . ARG A 1 163 ? 110.238 146.874 108.822 1.00 59.59 ?  163 ARG A NH2   1 
ATOM   1355  N  N     . ARG A 1 164 ? 118.349 148.025 109.372 1.00 53.64 ?  164 ARG A N     1 
ATOM   1356  C  CA    . ARG A 1 164 ? 119.435 147.279 108.763 1.00 50.73 ?  164 ARG A CA    1 
ATOM   1357  C  C     . ARG A 1 164 ? 120.620 147.188 109.714 1.00 51.26 ?  164 ARG A C     1 
ATOM   1358  O  O     . ARG A 1 164 ? 120.767 147.987 110.642 1.00 52.65 ?  164 ARG A O     1 
ATOM   1359  C  CB    . ARG A 1 164 ? 119.889 147.942 107.457 1.00 49.66 ?  164 ARG A CB    1 
ATOM   1360  C  CG    . ARG A 1 164 ? 120.638 149.252 107.674 1.00 46.69 ?  164 ARG A CG    1 
ATOM   1361  C  CD    . ARG A 1 164 ? 121.541 149.575 106.502 1.00 49.28 ?  164 ARG A CD    1 
ATOM   1362  N  NE    . ARG A 1 164 ? 122.329 150.784 106.713 1.00 50.57 ?  164 ARG A NE    1 
ATOM   1363  C  CZ    . ARG A 1 164 ? 122.553 151.700 105.782 1.00 51.84 ?  164 ARG A CZ    1 
ATOM   1364  N  NH1   . ARG A 1 164 ? 122.049 151.585 104.563 1.00 47.62 1  164 ARG A NH1   1 
ATOM   1365  N  NH2   . ARG A 1 164 ? 123.301 152.759 106.079 1.00 50.81 ?  164 ARG A NH2   1 
ATOM   1366  N  N     . GLY A 1 165 ? 121.464 146.191 109.471 1.00 45.41 ?  165 GLY A N     1 
ATOM   1367  C  CA    . GLY A 1 165 ? 122.765 146.124 110.094 1.00 42.70 ?  165 GLY A CA    1 
ATOM   1368  C  C     . GLY A 1 165 ? 123.771 146.965 109.333 1.00 47.81 ?  165 GLY A C     1 
ATOM   1369  O  O     . GLY A 1 165 ? 123.438 147.723 108.421 1.00 44.98 ?  165 GLY A O     1 
ATOM   1370  N  N     . GLU A 1 166 ? 125.032 146.824 109.724 1.00 45.86 ?  166 GLU A N     1 
ATOM   1371  C  CA    . GLU A 1 166 ? 126.084 147.557 109.041 1.00 39.66 ?  166 GLU A CA    1 
ATOM   1372  C  C     . GLU A 1 166 ? 126.392 146.917 107.691 1.00 37.91 ?  166 GLU A C     1 
ATOM   1373  O  O     . GLU A 1 166 ? 126.114 145.739 107.450 1.00 38.58 ?  166 GLU A O     1 
ATOM   1374  C  CB    . GLU A 1 166 ? 127.348 147.614 109.898 1.00 37.81 ?  166 GLU A CB    1 
ATOM   1375  C  CG    . GLU A 1 166 ? 127.274 148.610 111.042 1.00 41.94 ?  166 GLU A CG    1 
ATOM   1376  C  CD    . GLU A 1 166 ? 127.043 150.036 110.573 1.00 47.92 ?  166 GLU A CD    1 
ATOM   1377  O  OE1   . GLU A 1 166 ? 127.482 150.381 109.456 1.00 46.33 ?  166 GLU A OE1   1 
ATOM   1378  O  OE2   . GLU A 1 166 ? 126.421 150.814 111.326 1.00 45.41 -1 166 GLU A OE2   1 
ATOM   1379  N  N     . LEU A 1 167 ? 126.973 147.719 106.800 1.00 33.25 ?  167 LEU A N     1 
ATOM   1380  C  CA    . LEU A 1 167 ? 127.395 147.227 105.496 1.00 25.75 ?  167 LEU A CA    1 
ATOM   1381  C  C     . LEU A 1 167 ? 128.740 146.519 105.546 1.00 30.06 ?  167 LEU A C     1 
ATOM   1382  O  O     . LEU A 1 167 ? 129.150 145.930 104.542 1.00 32.58 ?  167 LEU A O     1 
ATOM   1383  C  CB    . LEU A 1 167 ? 127.460 148.380 104.493 1.00 27.51 ?  167 LEU A CB    1 
ATOM   1384  C  CG    . LEU A 1 167 ? 126.168 149.145 104.199 1.00 28.18 ?  167 LEU A CG    1 
ATOM   1385  C  CD1   . LEU A 1 167 ? 126.266 149.829 102.853 1.00 31.34 ?  167 LEU A CD1   1 
ATOM   1386  C  CD2   . LEU A 1 167 ? 124.966 148.226 104.232 1.00 28.89 ?  167 LEU A CD2   1 
ATOM   1387  N  N     . VAL A 1 168 ? 129.429 146.565 106.681 1.00 33.17 ?  168 VAL A N     1 
ATOM   1388  C  CA    . VAL A 1 168 ? 130.685 145.860 106.889 1.00 26.44 ?  168 VAL A CA    1 
ATOM   1389  C  C     . VAL A 1 168 ? 130.445 144.756 107.908 1.00 30.61 ?  168 VAL A C     1 
ATOM   1390  O  O     . VAL A 1 168 ? 129.795 144.980 108.936 1.00 36.41 ?  168 VAL A O     1 
ATOM   1391  C  CB    . VAL A 1 168 ? 131.797 146.817 107.363 1.00 26.26 ?  168 VAL A CB    1 
ATOM   1392  C  CG1   . VAL A 1 168 ? 133.110 146.074 107.524 1.00 29.07 ?  168 VAL A CG1   1 
ATOM   1393  C  CG2   . VAL A 1 168 ? 131.949 147.971 106.389 1.00 31.34 ?  168 VAL A CG2   1 
ATOM   1394  N  N     . SER A 1 169 ? 130.964 143.564 107.625 1.00 29.13 ?  169 SER A N     1 
ATOM   1395  C  CA    . SER A 1 169 ? 130.787 142.427 108.514 1.00 30.02 ?  169 SER A CA    1 
ATOM   1396  C  C     . SER A 1 169 ? 132.094 141.811 108.990 1.00 25.74 ?  169 SER A C     1 
ATOM   1397  O  O     . SER A 1 169 ? 132.057 140.877 109.798 1.00 31.17 ?  169 SER A O     1 
ATOM   1398  C  CB    . SER A 1 169 ? 129.937 141.343 107.841 1.00 33.72 ?  169 SER A CB    1 
ATOM   1399  O  OG    . SER A 1 169 ? 128.566 141.510 108.160 1.00 37.71 ?  169 SER A OG    1 
ATOM   1400  N  N     . CYS A 1 170 ? 133.239 142.290 108.521 1.00 28.39 ?  170 CYS A N     1 
ATOM   1401  C  CA    . CYS A 1 170 ? 134.531 141.801 108.982 1.00 26.92 ?  170 CYS A CA    1 
ATOM   1402  C  C     . CYS A 1 170 ? 135.199 142.895 109.802 1.00 25.20 ?  170 CYS A C     1 
ATOM   1403  O  O     . CYS A 1 170 ? 135.377 144.019 109.320 1.00 27.42 ?  170 CYS A O     1 
ATOM   1404  C  CB    . CYS A 1 170 ? 135.412 141.362 107.809 1.00 33.70 ?  170 CYS A CB    1 
ATOM   1405  S  SG    . CYS A 1 170 ? 135.969 142.664 106.681 1.00 51.33 ?  170 CYS A SG    1 
ATOM   1406  N  N     . PHE A 1 171 ? 135.537 142.573 111.046 1.00 22.44 ?  171 PHE A N     1 
ATOM   1407  C  CA    . PHE A 1 171 ? 136.227 143.486 111.942 1.00 16.13 ?  171 PHE A CA    1 
ATOM   1408  C  C     . PHE A 1 171 ? 137.387 142.759 112.600 1.00 16.35 ?  171 PHE A C     1 
ATOM   1409  O  O     . PHE A 1 171 ? 137.280 141.576 112.934 1.00 27.33 ?  171 PHE A O     1 
ATOM   1410  C  CB    . PHE A 1 171 ? 135.284 144.046 113.013 1.00 17.63 ?  171 PHE A CB    1 
ATOM   1411  C  CG    . PHE A 1 171 ? 134.057 144.702 112.454 1.00 17.41 ?  171 PHE A CG    1 
ATOM   1412  C  CD1   . PHE A 1 171 ? 134.106 146.000 111.980 1.00 16.60 ?  171 PHE A CD1   1 
ATOM   1413  C  CD2   . PHE A 1 171 ? 132.854 144.020 112.403 1.00 16.10 ?  171 PHE A CD2   1 
ATOM   1414  C  CE1   . PHE A 1 171 ? 132.982 146.604 111.465 1.00 15.99 ?  171 PHE A CE1   1 
ATOM   1415  C  CE2   . PHE A 1 171 ? 131.728 144.621 111.889 1.00 16.69 ?  171 PHE A CE2   1 
ATOM   1416  C  CZ    . PHE A 1 171 ? 131.791 145.914 111.421 1.00 14.78 ?  171 PHE A CZ    1 
ATOM   1417  N  N     . LEU A 1 172 ? 138.495 143.471 112.774 1.00 17.80 ?  172 LEU A N     1 
ATOM   1418  C  CA    . LEU A 1 172 ? 139.696 142.929 113.393 1.00 7.46  ?  172 LEU A CA    1 
ATOM   1419  C  C     . LEU A 1 172 ? 140.076 143.827 114.557 1.00 13.17 ?  172 LEU A C     1 
ATOM   1420  O  O     . LEU A 1 172 ? 140.239 145.037 114.380 1.00 17.99 ?  172 LEU A O     1 
ATOM   1421  C  CB    . LEU A 1 172 ? 140.851 142.840 112.388 1.00 12.46 ?  172 LEU A CB    1 
ATOM   1422  C  CG    . LEU A 1 172 ? 140.774 141.810 111.261 1.00 7.26  ?  172 LEU A CG    1 
ATOM   1423  C  CD1   . LEU A 1 172 ? 139.886 142.301 110.131 1.00 11.37 ?  172 LEU A CD1   1 
ATOM   1424  C  CD2   . LEU A 1 172 ? 142.164 141.501 110.744 1.00 11.04 ?  172 LEU A CD2   1 
ATOM   1425  N  N     . LEU A 1 173 ? 140.219 143.239 115.741 1.00 22.03 ?  173 LEU A N     1 
ATOM   1426  C  CA    . LEU A 1 173 ? 140.490 143.987 116.959 1.00 9.24  ?  173 LEU A CA    1 
ATOM   1427  C  C     . LEU A 1 173 ? 141.824 143.566 117.555 1.00 16.79 ?  173 LEU A C     1 
ATOM   1428  O  O     . LEU A 1 173 ? 142.124 142.373 117.651 1.00 26.59 ?  173 LEU A O     1 
ATOM   1429  C  CB    . LEU A 1 173 ? 139.388 143.780 118.000 1.00 14.56 ?  173 LEU A CB    1 
ATOM   1430  C  CG    . LEU A 1 173 ? 137.935 144.012 117.593 1.00 16.55 ?  173 LEU A CG    1 
ATOM   1431  C  CD1   . LEU A 1 173 ? 137.039 143.834 118.803 1.00 20.59 ?  173 LEU A CD1   1 
ATOM   1432  C  CD2   . LEU A 1 173 ? 137.744 145.383 116.974 1.00 15.88 ?  173 LEU A CD2   1 
ATOM   1433  N  N     . GLU A 1 174 ? 142.617 144.552 117.958 1.00 23.22 ?  174 GLU A N     1 
ATOM   1434  C  CA    . GLU A 1 174 ? 143.842 144.320 118.708 1.00 19.58 ?  174 GLU A CA    1 
ATOM   1435  C  C     . GLU A 1 174 ? 143.541 144.502 120.190 1.00 17.36 ?  174 GLU A C     1 
ATOM   1436  O  O     . GLU A 1 174 ? 143.001 145.537 120.593 1.00 29.19 ?  174 GLU A O     1 
ATOM   1437  C  CB    . GLU A 1 174 ? 144.950 145.274 118.264 1.00 22.04 ?  174 GLU A CB    1 
ATOM   1438  C  CG    . GLU A 1 174 ? 145.506 144.992 116.887 1.00 20.41 ?  174 GLU A CG    1 
ATOM   1439  C  CD    . GLU A 1 174 ? 146.986 144.678 116.917 1.00 19.96 ?  174 GLU A CD    1 
ATOM   1440  O  OE1   . GLU A 1 174 ? 147.795 145.626 116.950 1.00 22.11 ?  174 GLU A OE1   1 
ATOM   1441  O  OE2   . GLU A 1 174 ? 147.341 143.482 116.904 1.00 32.00 -1 174 GLU A OE2   1 
ATOM   1442  N  N     . VAL A 1 175 ? 143.887 143.504 120.994 1.00 18.09 ?  175 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 175 ? 143.629 143.524 122.429 1.00 21.78 ?  175 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 175 ? 144.944 143.775 123.151 1.00 19.70 ?  175 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 175 ? 145.907 143.016 122.986 1.00 21.46 ?  175 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 175 ? 142.982 142.213 122.903 1.00 21.89 ?  175 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 175 ? 142.317 142.406 124.255 1.00 15.48 ?  175 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 175 ? 141.982 141.712 121.876 1.00 17.38 ?  175 VAL A CG2   1 
ATOM   1449  N  N     . ASN A 1 176 ? 144.988 144.837 123.950 1.00 15.24 ?  176 ASN A N     1 
ATOM   1450  C  CA    . ASN A 1 176 ? 146.168 145.138 124.742 1.00 18.20 ?  176 ASN A CA    1 
ATOM   1451  C  C     . ASN A 1 176 ? 146.178 144.307 126.021 1.00 21.81 ?  176 ASN A C     1 
ATOM   1452  O  O     . ASN A 1 176 ? 145.160 143.755 126.447 1.00 21.13 ?  176 ASN A O     1 
ATOM   1453  C  CB    . ASN A 1 176 ? 146.226 146.627 125.078 1.00 18.41 ?  176 ASN A CB    1 
ATOM   1454  C  CG    . ASN A 1 176 ? 147.625 147.187 125.000 1.00 23.52 ?  176 ASN A CG    1 
ATOM   1455  O  OD1   . ASN A 1 176 ? 148.605 146.453 125.109 1.00 27.38 ?  176 ASN A OD1   1 
ATOM   1456  N  ND2   . ASN A 1 176 ? 147.728 148.494 124.803 1.00 21.82 ?  176 ASN A ND2   1 
ATOM   1457  N  N     . ASP A 1 177 ? 147.355 144.230 126.642 1.00 29.34 ?  177 ASP A N     1 
ATOM   1458  C  CA    . ASP A 1 177 ? 147.569 143.370 127.806 1.00 22.42 ?  177 ASP A CA    1 
ATOM   1459  C  C     . ASP A 1 177 ? 147.144 144.099 129.082 1.00 22.88 ?  177 ASP A C     1 
ATOM   1460  O  O     . ASP A 1 177 ? 147.952 144.498 129.920 1.00 27.43 ?  177 ASP A O     1 
ATOM   1461  C  CB    . ASP A 1 177 ? 149.026 142.929 127.870 1.00 21.20 ?  177 ASP A CB    1 
ATOM   1462  C  CG    . ASP A 1 177 ? 149.264 141.858 128.911 1.00 27.82 ?  177 ASP A CG    1 
ATOM   1463  O  OD1   . ASP A 1 177 ? 148.368 141.015 129.112 1.00 30.56 ?  177 ASP A OD1   1 
ATOM   1464  O  OD2   . ASP A 1 177 ? 150.352 141.857 129.523 1.00 29.71 -1 177 ASP A OD2   1 
ATOM   1465  N  N     . SER A 1 178 ? 145.831 144.264 129.217 1.00 22.26 ?  178 SER A N     1 
ATOM   1466  C  CA    . SER A 1 178 ? 145.269 144.890 130.405 1.00 18.11 ?  178 SER A CA    1 
ATOM   1467  C  C     . SER A 1 178 ? 143.829 144.431 130.569 1.00 20.63 ?  178 SER A C     1 
ATOM   1468  O  O     . SER A 1 178 ? 143.178 144.019 129.609 1.00 29.47 ?  178 SER A O     1 
ATOM   1469  C  CB    . SER A 1 178 ? 145.348 146.418 130.326 1.00 19.31 ?  178 SER A CB    1 
ATOM   1470  O  OG    . SER A 1 178 ? 144.133 146.970 129.862 1.00 25.10 ?  178 SER A OG    1 
ATOM   1471  N  N     . LEU A 1 179 ? 143.342 144.507 131.810 1.00 27.75 ?  179 LEU A N     1 
ATOM   1472  C  CA    . LEU A 1 179 ? 141.954 144.148 132.081 1.00 20.46 ?  179 LEU A CA    1 
ATOM   1473  C  C     . LEU A 1 179 ? 140.994 145.173 131.492 1.00 22.67 ?  179 LEU A C     1 
ATOM   1474  O  O     . LEU A 1 179 ? 139.901 144.816 131.040 1.00 27.44 ?  179 LEU A O     1 
ATOM   1475  C  CB    . LEU A 1 179 ? 141.726 144.009 133.586 1.00 23.33 ?  179 LEU A CB    1 
ATOM   1476  C  CG    . LEU A 1 179 ? 140.375 143.434 134.011 1.00 22.04 ?  179 LEU A CG    1 
ATOM   1477  C  CD1   . LEU A 1 179 ? 140.287 141.958 133.664 1.00 24.32 ?  179 LEU A CD1   1 
ATOM   1478  C  CD2   . LEU A 1 179 ? 140.138 143.660 135.493 1.00 21.57 ?  179 LEU A CD2   1 
ATOM   1479  N  N     . ASN A 1 180 ? 141.377 146.452 131.504 1.00 23.10 ?  180 ASN A N     1 
ATOM   1480  C  CA    . ASN A 1 180 ? 140.560 147.470 130.853 1.00 21.89 ?  180 ASN A CA    1 
ATOM   1481  C  C     . ASN A 1 180 ? 140.432 147.189 129.364 1.00 26.71 ?  180 ASN A C     1 
ATOM   1482  O  O     . ASN A 1 180 ? 139.338 147.280 128.795 1.00 30.16 ?  180 ASN A O     1 
ATOM   1483  C  CB    . ASN A 1 180 ? 141.165 148.854 131.082 1.00 22.57 ?  180 ASN A CB    1 
ATOM   1484  C  CG    . ASN A 1 180 ? 140.792 149.442 132.424 1.00 27.08 ?  180 ASN A CG    1 
ATOM   1485  O  OD1   . ASN A 1 180 ? 139.767 149.093 133.006 1.00 33.00 ?  180 ASN A OD1   1 
ATOM   1486  N  ND2   . ASN A 1 180 ? 141.627 150.344 132.922 1.00 27.92 ?  180 ASN A ND2   1 
ATOM   1487  N  N     . ASP A 1 181 ? 141.541 146.823 128.722 1.00 25.42 ?  181 ASP A N     1 
ATOM   1488  C  CA    . ASP A 1 181 ? 141.513 146.524 127.297 1.00 16.89 ?  181 ASP A CA    1 
ATOM   1489  C  C     . ASP A 1 181 ? 140.768 145.229 127.005 1.00 20.98 ?  181 ASP A C     1 
ATOM   1490  O  O     . ASP A 1 181 ? 140.106 145.126 125.971 1.00 25.91 ?  181 ASP A O     1 
ATOM   1491  C  CB    . ASP A 1 181 ? 142.936 146.468 126.752 1.00 20.00 ?  181 ASP A CB    1 
ATOM   1492  C  CG    . ASP A 1 181 ? 143.554 147.843 126.612 1.00 32.71 ?  181 ASP A CG    1 
ATOM   1493  O  OD1   . ASP A 1 181 ? 143.218 148.550 125.640 1.00 36.80 ?  181 ASP A OD1   1 
ATOM   1494  O  OD2   . ASP A 1 181 ? 144.379 148.220 127.472 1.00 30.19 -1 181 ASP A OD2   1 
ATOM   1495  N  N     . ILE A 1 182 ? 140.846 144.242 127.896 1.00 21.36 ?  182 ILE A N     1 
ATOM   1496  C  CA    . ILE A 1 182 ? 140.093 143.006 127.694 1.00 21.47 ?  182 ILE A CA    1 
ATOM   1497  C  C     . ILE A 1 182 ? 138.596 143.262 127.832 1.00 18.86 ?  182 ILE A C     1 
ATOM   1498  O  O     . ILE A 1 182 ? 137.788 142.748 127.047 1.00 24.47 ?  182 ILE A O     1 
ATOM   1499  C  CB    . ILE A 1 182 ? 140.584 141.922 128.670 1.00 24.51 ?  182 ILE A CB    1 
ATOM   1500  C  CG1   . ILE A 1 182 ? 141.947 141.395 128.223 1.00 20.55 ?  182 ILE A CG1   1 
ATOM   1501  C  CG2   . ILE A 1 182 ? 139.580 140.783 128.766 1.00 26.74 ?  182 ILE A CG2   1 
ATOM   1502  C  CD1   . ILE A 1 182 ? 142.636 140.549 129.253 1.00 22.39 ?  182 ILE A CD1   1 
ATOM   1503  N  N     . SER A 1 183 ? 138.203 144.063 128.825 1.00 22.49 ?  183 SER A N     1 
ATOM   1504  C  CA    . SER A 1 183 ? 136.798 144.426 128.974 1.00 21.31 ?  183 SER A CA    1 
ATOM   1505  C  C     . SER A 1 183 ? 136.303 145.210 127.767 1.00 24.12 ?  183 SER A C     1 
ATOM   1506  O  O     . SER A 1 183 ? 135.197 144.966 127.268 1.00 30.09 ?  183 SER A O     1 
ATOM   1507  C  CB    . SER A 1 183 ? 136.601 145.237 130.252 1.00 21.24 ?  183 SER A CB    1 
ATOM   1508  O  OG    . SER A 1 183 ? 137.209 144.605 131.362 1.00 32.18 ?  183 SER A OG    1 
ATOM   1509  N  N     . ARG A 1 184 ? 137.109 146.156 127.281 1.00 23.49 ?  184 ARG A N     1 
ATOM   1510  C  CA    . ARG A 1 184 ? 136.724 146.900 126.088 1.00 23.99 ?  184 ARG A CA    1 
ATOM   1511  C  C     . ARG A 1 184 ? 136.654 146.000 124.864 1.00 28.93 ?  184 ARG A C     1 
ATOM   1512  O  O     . ARG A 1 184 ? 135.798 146.205 124.001 1.00 33.36 ?  184 ARG A O     1 
ATOM   1513  C  CB    . ARG A 1 184 ? 137.693 148.052 125.845 1.00 23.38 ?  184 ARG A CB    1 
ATOM   1514  C  CG    . ARG A 1 184 ? 137.090 149.185 125.040 1.00 27.12 ?  184 ARG A CG    1 
ATOM   1515  C  CD    . ARG A 1 184 ? 136.510 150.250 125.947 1.00 31.20 ?  184 ARG A CD    1 
ATOM   1516  N  NE    . ARG A 1 184 ? 135.073 150.402 125.756 1.00 31.34 ?  184 ARG A NE    1 
ATOM   1517  C  CZ    . ARG A 1 184 ? 134.325 151.292 126.393 1.00 35.55 ?  184 ARG A CZ    1 
ATOM   1518  N  NH1   . ARG A 1 184 ? 134.849 152.132 127.270 1.00 33.29 1  184 ARG A NH1   1 
ATOM   1519  N  NH2   . ARG A 1 184 ? 133.021 151.341 126.143 1.00 29.20 ?  184 ARG A NH2   1 
ATOM   1520  N  N     . ALA A 1 185 ? 137.540 145.008 124.766 1.00 28.47 ?  185 ALA A N     1 
ATOM   1521  C  CA    . ALA A 1 185 ? 137.477 144.065 123.656 1.00 15.38 ?  185 ALA A CA    1 
ATOM   1522  C  C     . ALA A 1 185 ? 136.193 143.251 123.702 1.00 21.04 ?  185 ALA A C     1 
ATOM   1523  O  O     . ALA A 1 185 ? 135.554 143.037 122.670 1.00 25.07 ?  185 ALA A O     1 
ATOM   1524  C  CB    . ALA A 1 185 ? 138.697 143.147 123.678 1.00 17.48 ?  185 ALA A CB    1 
ATOM   1525  N  N     . ILE A 1 186 ? 135.798 142.796 124.892 1.00 24.51 ?  186 ILE A N     1 
ATOM   1526  C  CA    . ILE A 1 186 ? 134.541 142.063 125.027 1.00 20.17 ?  186 ILE A CA    1 
ATOM   1527  C  C     . ILE A 1 186 ? 133.364 142.950 124.639 1.00 20.92 ?  186 ILE A C     1 
ATOM   1528  O  O     . ILE A 1 186 ? 132.460 142.528 123.903 1.00 27.02 ?  186 ILE A O     1 
ATOM   1529  C  CB    . ILE A 1 186 ? 134.388 141.524 126.462 1.00 27.30 ?  186 ILE A CB    1 
ATOM   1530  C  CG1   . ILE A 1 186 ? 135.388 140.401 126.725 1.00 24.05 ?  186 ILE A CG1   1 
ATOM   1531  C  CG2   . ILE A 1 186 ? 132.967 141.040 126.708 1.00 27.00 ?  186 ILE A CG2   1 
ATOM   1532  C  CD1   . ILE A 1 186 ? 135.588 140.113 128.195 1.00 25.30 ?  186 ILE A CD1   1 
ATOM   1533  N  N     . ASP A 1 187 ? 133.363 144.194 125.121 1.00 27.48 ?  187 ASP A N     1 
ATOM   1534  C  CA    . ASP A 1 187 ? 132.276 145.117 124.812 1.00 23.22 ?  187 ASP A CA    1 
ATOM   1535  C  C     . ASP A 1 187 ? 132.188 145.384 123.316 1.00 27.24 ?  187 ASP A C     1 
ATOM   1536  O  O     . ASP A 1 187 ? 131.104 145.330 122.729 1.00 32.57 ?  187 ASP A O     1 
ATOM   1537  C  CB    . ASP A 1 187 ? 132.469 146.423 125.584 1.00 22.13 ?  187 ASP A CB    1 
ATOM   1538  C  CG    . ASP A 1 187 ? 131.615 147.553 125.044 1.00 34.84 ?  187 ASP A CG    1 
ATOM   1539  O  OD1   . ASP A 1 187 ? 130.387 147.367 124.912 1.00 36.41 ?  187 ASP A OD1   1 
ATOM   1540  O  OD2   . ASP A 1 187 ? 132.172 148.631 124.749 1.00 37.56 -1 187 ASP A OD2   1 
ATOM   1541  N  N     . ILE A 1 188 ? 133.327 145.666 122.681 1.00 25.83 ?  188 ILE A N     1 
ATOM   1542  C  CA    . ILE A 1 188 ? 133.341 145.976 121.255 1.00 22.68 ?  188 ILE A CA    1 
ATOM   1543  C  C     . ILE A 1 188 ? 132.964 144.748 120.438 1.00 22.53 ?  188 ILE A C     1 
ATOM   1544  O  O     . ILE A 1 188 ? 132.279 144.856 119.416 1.00 28.19 ?  188 ILE A O     1 
ATOM   1545  C  CB    . ILE A 1 188 ? 134.715 146.536 120.847 1.00 25.08 ?  188 ILE A CB    1 
ATOM   1546  C  CG1   . ILE A 1 188 ? 134.937 147.913 121.471 1.00 23.81 ?  188 ILE A CG1   1 
ATOM   1547  C  CG2   . ILE A 1 188 ? 134.835 146.641 119.340 1.00 21.04 ?  188 ILE A CG2   1 
ATOM   1548  C  CD1   . ILE A 1 188 ? 136.287 148.504 121.165 1.00 23.99 ?  188 ILE A CD1   1 
ATOM   1549  N  N     . SER A 1 189 ? 133.397 143.565 120.874 1.00 24.80 ?  189 SER A N     1 
ATOM   1550  C  CA    . SER A 1 189 ? 133.018 142.339 120.185 1.00 14.85 ?  189 SER A CA    1 
ATOM   1551  C  C     . SER A 1 189 ? 131.513 142.131 120.232 1.00 21.48 ?  189 SER A C     1 
ATOM   1552  O  O     . SER A 1 189 ? 130.900 141.776 119.220 1.00 28.50 ?  189 SER A O     1 
ATOM   1553  C  CB    . SER A 1 189 ? 133.745 141.144 120.802 1.00 20.15 ?  189 SER A CB    1 
ATOM   1554  O  OG    . SER A 1 189 ? 135.137 141.386 120.891 1.00 24.99 ?  189 SER A OG    1 
ATOM   1555  N  N     . MET A 1 190 ? 130.896 142.354 121.395 1.00 24.96 ?  190 MET A N     1 
ATOM   1556  C  CA    . MET A 1 190 ? 129.444 142.228 121.475 1.00 25.46 ?  190 MET A CA    1 
ATOM   1557  C  C     . MET A 1 190 ? 128.742 143.300 120.648 1.00 24.52 ?  190 MET A C     1 
ATOM   1558  O  O     . MET A 1 190 ? 127.722 143.023 120.008 1.00 25.65 ?  190 MET A O     1 
ATOM   1559  C  CB    . MET A 1 190 ? 128.978 142.275 122.929 1.00 24.20 ?  190 MET A CB    1 
ATOM   1560  C  CG    . MET A 1 190 ? 129.149 140.956 123.663 1.00 25.61 ?  190 MET A CG    1 
ATOM   1561  S  SD    . MET A 1 190 ? 128.921 141.058 125.447 1.00 39.39 ?  190 MET A SD    1 
ATOM   1562  C  CE    . MET A 1 190 ? 129.111 142.812 125.720 1.00 30.50 ?  190 MET A CE    1 
ATOM   1563  N  N     . GLN A 1 191 ? 129.270 144.526 120.644 1.00 20.97 ?  191 GLN A N     1 
ATOM   1564  C  CA    . GLN A 1 191 ? 128.659 145.590 119.851 1.00 27.46 ?  191 GLN A CA    1 
ATOM   1565  C  C     . GLN A 1 191 ? 128.710 145.277 118.361 1.00 26.57 ?  191 GLN A C     1 
ATOM   1566  O  O     . GLN A 1 191 ? 127.733 145.503 117.639 1.00 30.30 ?  191 GLN A O     1 
ATOM   1567  C  CB    . GLN A 1 191 ? 129.343 146.928 120.136 1.00 28.45 ?  191 GLN A CB    1 
ATOM   1568  C  CG    . GLN A 1 191 ? 129.189 147.428 121.560 1.00 26.96 ?  191 GLN A CG    1 
ATOM   1569  C  CD    . GLN A 1 191 ? 127.765 147.816 121.900 1.00 29.87 ?  191 GLN A CD    1 
ATOM   1570  O  OE1   . GLN A 1 191 ? 127.351 147.735 123.054 1.00 30.00 ?  191 GLN A OE1   1 
ATOM   1571  N  NE2   . GLN A 1 191 ? 127.011 148.254 120.898 1.00 30.62 ?  191 GLN A NE2   1 
ATOM   1572  N  N     . LEU A 1 192 ? 129.844 144.764 117.881 1.00 26.64 ?  192 LEU A N     1 
ATOM   1573  C  CA    . LEU A 1 192 ? 129.989 144.471 116.460 1.00 21.91 ?  192 LEU A CA    1 
ATOM   1574  C  C     . LEU A 1 192 ? 129.246 143.205 116.057 1.00 24.46 ?  192 LEU A C     1 
ATOM   1575  O  O     . LEU A 1 192 ? 128.718 143.135 114.942 1.00 33.12 ?  192 LEU A O     1 
ATOM   1576  C  CB    . LEU A 1 192 ? 131.468 144.357 116.095 1.00 21.31 ?  192 LEU A CB    1 
ATOM   1577  C  CG    . LEU A 1 192 ? 132.291 145.644 116.191 1.00 20.35 ?  192 LEU A CG    1 
ATOM   1578  C  CD1   . LEU A 1 192 ? 133.774 145.344 116.079 1.00 20.92 ?  192 LEU A CD1   1 
ATOM   1579  C  CD2   . LEU A 1 192 ? 131.864 146.643 115.131 1.00 18.19 ?  192 LEU A CD2   1 
ATOM   1580  N  N     . SER A 1 193 ? 129.194 142.201 116.935 1.00 29.05 ?  193 SER A N     1 
ATOM   1581  C  CA    . SER A 1 193 ? 128.382 141.020 116.667 1.00 26.96 ?  193 SER A CA    1 
ATOM   1582  C  C     . SER A 1 193 ? 126.901 141.371 116.653 1.00 30.56 ?  193 SER A C     1 
ATOM   1583  O  O     . SER A 1 193 ? 126.123 140.778 115.899 1.00 34.58 ?  193 SER A O     1 
ATOM   1584  C  CB    . SER A 1 193 ? 128.674 139.942 117.709 1.00 28.66 ?  193 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 193 ? 127.922 138.769 117.455 1.00 37.95 ?  193 SER A OG    1 
ATOM   1586  N  N     . LYS A 1 194 ? 126.495 142.331 117.487 1.00 33.77 ?  194 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 194 ? 125.120 142.816 117.460 1.00 31.64 ?  194 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 194 ? 124.791 143.448 116.114 1.00 36.17 ?  194 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 194 ? 123.676 143.292 115.601 1.00 39.77 ?  194 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 194 ? 124.909 143.810 118.601 1.00 29.29 ?  194 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 194 ? 123.708 144.717 118.446 1.00 33.70 ?  194 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 194 ? 123.789 145.886 119.412 1.00 36.36 ?  194 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 194 ? 122.456 146.603 119.532 1.00 34.10 ?  194 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 194 ? 122.523 147.730 120.501 1.00 34.07 1  194 LYS A NZ    1 
ATOM   1595  N  N     . LEU A 1 195 ? 125.752 144.157 115.521 1.00 34.21 ?  195 LEU A N     1 
ATOM   1596  C  CA    . LEU A 1 195 ? 125.571 144.727 114.193 1.00 31.80 ?  195 LEU A CA    1 
ATOM   1597  C  C     . LEU A 1 195 ? 125.560 143.671 113.097 1.00 34.40 ?  195 LEU A C     1 
ATOM   1598  O  O     . LEU A 1 195 ? 125.245 143.999 111.949 1.00 38.44 ?  195 LEU A O     1 
ATOM   1599  C  CB    . LEU A 1 195 ? 126.673 145.747 113.906 1.00 33.76 ?  195 LEU A CB    1 
ATOM   1600  C  CG    . LEU A 1 195 ? 126.722 146.957 114.835 1.00 34.19 ?  195 LEU A CG    1 
ATOM   1601  C  CD1   . LEU A 1 195 ? 127.975 147.775 114.573 1.00 30.68 ?  195 LEU A CD1   1 
ATOM   1602  C  CD2   . LEU A 1 195 ? 125.474 147.806 114.673 1.00 36.49 ?  195 LEU A CD2   1 
ATOM   1603  N  N     . GLY A 1 196 ? 125.899 142.425 113.418 1.00 31.78 ?  196 GLY A N     1 
ATOM   1604  C  CA    . GLY A 1 196 ? 125.917 141.352 112.450 1.00 30.65 ?  196 GLY A CA    1 
ATOM   1605  C  C     . GLY A 1 196 ? 127.280 141.017 111.891 1.00 35.94 ?  196 GLY A C     1 
ATOM   1606  O  O     . GLY A 1 196 ? 127.385 140.093 111.076 1.00 40.43 ?  196 GLY A O     1 
ATOM   1607  N  N     . GLY A 1 197 ? 128.322 141.731 112.300 1.00 30.13 ?  197 GLY A N     1 
ATOM   1608  C  CA    . GLY A 1 197 ? 129.645 141.508 111.762 1.00 24.75 ?  197 GLY A CA    1 
ATOM   1609  C  C     . GLY A 1 197 ? 130.402 140.395 112.464 1.00 24.86 ?  197 GLY A C     1 
ATOM   1610  O  O     . GLY A 1 197 ? 130.169 140.094 113.631 1.00 30.82 ?  197 GLY A O     1 
ATOM   1611  N  N     . GLY A 1 198 ? 131.320 139.780 111.721 1.00 20.05 ?  198 GLY A N     1 
ATOM   1612  C  CA    . GLY A 1 198 ? 132.243 138.817 112.291 1.00 17.92 ?  198 GLY A CA    1 
ATOM   1613  C  C     . GLY A 1 198 ? 133.464 139.538 112.824 1.00 16.53 ?  198 GLY A C     1 
ATOM   1614  O  O     . GLY A 1 198 ? 134.031 140.400 112.148 1.00 22.13 ?  198 GLY A O     1 
ATOM   1615  N  N     . VAL A 1 199 ? 133.865 139.185 114.040 1.00 20.68 ?  199 VAL A N     1 
ATOM   1616  C  CA    . VAL A 1 199 ? 134.915 139.894 114.759 1.00 16.18 ?  199 VAL A CA    1 
ATOM   1617  C  C     . VAL A 1 199 ? 136.100 138.962 114.949 1.00 11.98 ?  199 VAL A C     1 
ATOM   1618  O  O     . VAL A 1 199 ? 135.941 137.833 115.426 1.00 15.18 ?  199 VAL A O     1 
ATOM   1619  C  CB    . VAL A 1 199 ? 134.415 140.420 116.118 1.00 14.84 ?  199 VAL A CB    1 
ATOM   1620  C  CG1   . VAL A 1 199 ? 135.464 141.305 116.758 1.00 14.75 ?  199 VAL A CG1   1 
ATOM   1621  C  CG2   . VAL A 1 199 ? 133.111 141.171 115.943 1.00 18.84 ?  199 VAL A CG2   1 
ATOM   1622  N  N     . SER A 1 200 ? 137.284 139.435 114.578 1.00 16.69 ?  200 SER A N     1 
ATOM   1623  C  CA    . SER A 1 200 ? 138.531 138.734 114.833 1.00 7.23  ?  200 SER A CA    1 
ATOM   1624  C  C     . SER A 1 200 ? 139.343 139.522 115.849 1.00 12.61 ?  200 SER A C     1 
ATOM   1625  O  O     . SER A 1 200 ? 139.389 140.754 115.800 1.00 19.88 ?  200 SER A O     1 
ATOM   1626  C  CB    . SER A 1 200 ? 139.336 138.551 113.547 1.00 14.12 ?  200 SER A CB    1 
ATOM   1627  O  OG    . SER A 1 200 ? 140.281 137.508 113.685 1.00 19.62 ?  200 SER A OG    1 
ATOM   1628  N  N     . LEU A 1 201 ? 139.976 138.809 116.773 1.00 18.50 ?  201 LEU A N     1 
ATOM   1629  C  CA    . LEU A 1 201 ? 140.746 139.433 117.837 1.00 10.78 ?  201 LEU A CA    1 
ATOM   1630  C  C     . LEU A 1 201 ? 142.150 138.854 117.871 1.00 10.09 ?  201 LEU A C     1 
ATOM   1631  O  O     . LEU A 1 201 ? 142.335 137.639 117.761 1.00 15.23 ?  201 LEU A O     1 
ATOM   1632  C  CB    . LEU A 1 201 ? 140.070 139.240 119.200 1.00 14.87 ?  201 LEU A CB    1 
ATOM   1633  C  CG    . LEU A 1 201 ? 138.665 139.830 119.339 1.00 15.59 ?  201 LEU A CG    1 
ATOM   1634  C  CD1   . LEU A 1 201 ? 137.619 138.728 119.349 1.00 20.18 ?  201 LEU A CD1   1 
ATOM   1635  C  CD2   . LEU A 1 201 ? 138.562 140.684 120.586 1.00 12.72 ?  201 LEU A CD2   1 
ATOM   1636  N  N     . ASN A 1 202 ? 143.136 139.733 118.018 1.00 10.92 ?  202 ASN A N     1 
ATOM   1637  C  CA    . ASN A 1 202 ? 144.518 139.325 118.226 1.00 8.56  ?  202 ASN A CA    1 
ATOM   1638  C  C     . ASN A 1 202 ? 144.760 139.172 119.721 1.00 18.53 ?  202 ASN A C     1 
ATOM   1639  O  O     . ASN A 1 202 ? 144.582 140.126 120.485 1.00 29.15 ?  202 ASN A O     1 
ATOM   1640  C  CB    . ASN A 1 202 ? 145.482 140.345 117.626 1.00 9.92  ?  202 ASN A CB    1 
ATOM   1641  C  CG    . ASN A 1 202 ? 146.878 139.790 117.446 1.00 12.50 ?  202 ASN A CG    1 
ATOM   1642  O  OD1   . ASN A 1 202 ? 147.062 138.586 117.281 1.00 17.38 ?  202 ASN A OD1   1 
ATOM   1643  N  ND2   . ASN A 1 202 ? 147.871 140.667 117.477 1.00 10.64 ?  202 ASN A ND2   1 
ATOM   1644  N  N     . LEU A 1 203 ? 145.166 137.973 120.138 1.00 13.46 ?  203 LEU A N     1 
ATOM   1645  C  CA    . LEU A 1 203 ? 145.411 137.680 121.543 1.00 11.52 ?  203 LEU A CA    1 
ATOM   1646  C  C     . LEU A 1 203 ? 146.895 137.520 121.848 1.00 13.48 ?  203 LEU A C     1 
ATOM   1647  O  O     . LEU A 1 203 ? 147.255 137.009 122.912 1.00 21.45 ?  203 LEU A O     1 
ATOM   1648  C  CB    . LEU A 1 203 ? 144.641 136.426 121.959 1.00 17.29 ?  203 LEU A CB    1 
ATOM   1649  C  CG    . LEU A 1 203 ? 143.121 136.469 121.803 1.00 16.61 ?  203 LEU A CG    1 
ATOM   1650  C  CD1   . LEU A 1 203 ? 142.478 135.352 122.601 1.00 17.98 ?  203 LEU A CD1   1 
ATOM   1651  C  CD2   . LEU A 1 203 ? 142.559 137.817 122.228 1.00 13.98 ?  203 LEU A CD2   1 
ATOM   1652  N  N     . SER A 1 204 ? 147.765 137.956 120.937 1.00 12.80 ?  204 SER A N     1 
ATOM   1653  C  CA    . SER A 1 204 ? 149.198 137.763 121.118 1.00 15.21 ?  204 SER A CA    1 
ATOM   1654  C  C     . SER A 1 204 ? 149.788 138.720 122.145 1.00 20.30 ?  204 SER A C     1 
ATOM   1655  O  O     . SER A 1 204 ? 150.731 138.353 122.854 1.00 27.24 ?  204 SER A O     1 
ATOM   1656  C  CB    . SER A 1 204 ? 149.920 137.920 119.782 1.00 15.24 ?  204 SER A CB    1 
ATOM   1657  O  OG    . SER A 1 204 ? 149.359 137.067 118.802 1.00 22.85 ?  204 SER A OG    1 
ATOM   1658  N  N     . LYS A 1 205 ? 149.263 139.944 122.236 1.00 19.51 ?  205 LYS A N     1 
ATOM   1659  C  CA    . LYS A 1 205 ? 149.776 140.894 123.216 1.00 16.00 ?  205 LYS A CA    1 
ATOM   1660  C  C     . LYS A 1 205 ? 149.406 140.512 124.640 1.00 18.09 ?  205 LYS A C     1 
ATOM   1661  O  O     . LYS A 1 205 ? 150.058 140.978 125.579 1.00 22.70 ?  205 LYS A O     1 
ATOM   1662  C  CB    . LYS A 1 205 ? 149.270 142.302 122.910 1.00 16.09 ?  205 LYS A CB    1 
ATOM   1663  C  CG    . LYS A 1 205 ? 149.874 142.911 121.665 1.00 18.07 ?  205 LYS A CG    1 
ATOM   1664  C  CD    . LYS A 1 205 ? 149.371 144.320 121.438 1.00 23.59 ?  205 LYS A CD    1 
ATOM   1665  C  CE    . LYS A 1 205 ? 150.125 144.990 120.307 1.00 26.62 ?  205 LYS A CE    1 
ATOM   1666  N  NZ    . LYS A 1 205 ? 149.954 144.268 119.019 1.00 19.06 1  205 LYS A NZ    1 
ATOM   1667  N  N     . LEU A 1 206 ? 148.385 139.680 124.819 1.00 17.87 ?  206 LEU A N     1 
ATOM   1668  C  CA    . LEU A 1 206 ? 148.002 139.232 126.148 1.00 12.12 ?  206 LEU A CA    1 
ATOM   1669  C  C     . LEU A 1 206 ? 149.081 138.330 126.728 1.00 17.25 ?  206 LEU A C     1 
ATOM   1670  O  O     . LEU A 1 206 ? 149.601 137.446 126.040 1.00 21.62 ?  206 LEU A O     1 
ATOM   1671  C  CB    . LEU A 1 206 ? 146.670 138.490 126.090 1.00 19.76 ?  206 LEU A CB    1 
ATOM   1672  C  CG    . LEU A 1 206 ? 145.464 139.322 125.663 1.00 20.73 ?  206 LEU A CG    1 
ATOM   1673  C  CD1   . LEU A 1 206 ? 144.218 138.462 125.639 1.00 16.80 ?  206 LEU A CD1   1 
ATOM   1674  C  CD2   . LEU A 1 206 ? 145.285 140.509 126.590 1.00 23.23 ?  206 LEU A CD2   1 
ATOM   1675  N  N     . ARG A 1 207 ? 149.417 138.549 127.995 1.00 24.80 ?  207 ARG A N     1 
ATOM   1676  C  CA    . ARG A 1 207 ? 150.454 137.752 128.629 1.00 22.16 ?  207 ARG A CA    1 
ATOM   1677  C  C     . ARG A 1 207 ? 149.955 136.336 128.895 1.00 27.34 ?  207 ARG A C     1 
ATOM   1678  O  O     . ARG A 1 207 ? 148.757 136.091 129.057 1.00 27.88 ?  207 ARG A O     1 
ATOM   1679  C  CB    . ARG A 1 207 ? 150.927 138.410 129.923 1.00 22.25 ?  207 ARG A CB    1 
ATOM   1680  C  CG    . ARG A 1 207 ? 149.907 138.466 131.036 1.00 23.35 ?  207 ARG A CG    1 
ATOM   1681  C  CD    . ARG A 1 207 ? 150.420 139.335 132.166 1.00 26.39 ?  207 ARG A CD    1 
ATOM   1682  N  NE    . ARG A 1 207 ? 150.457 140.743 131.791 1.00 28.94 ?  207 ARG A NE    1 
ATOM   1683  C  CZ    . ARG A 1 207 ? 150.457 141.749 132.652 1.00 24.31 ?  207 ARG A CZ    1 
ATOM   1684  N  NH1   . ARG A 1 207 ? 150.448 141.541 133.957 1.00 28.75 1  207 ARG A NH1   1 
ATOM   1685  N  NH2   . ARG A 1 207 ? 150.463 142.997 132.192 1.00 20.66 ?  207 ARG A NH2   1 
ATOM   1686  N  N     . ALA A 1 208 ? 150.897 135.401 128.935 1.00 33.04 ?  208 ALA A N     1 
ATOM   1687  C  CA    . ALA A 1 208 ? 150.581 133.985 128.973 1.00 24.77 ?  208 ALA A CA    1 
ATOM   1688  C  C     . ALA A 1 208 ? 150.121 133.558 130.365 1.00 31.73 ?  208 ALA A C     1 
ATOM   1689  O  O     . ALA A 1 208 ? 150.118 134.336 131.322 1.00 36.14 ?  208 ALA A O     1 
ATOM   1690  C  CB    . ALA A 1 208 ? 151.791 133.165 128.536 1.00 25.67 ?  208 ALA A CB    1 
ATOM   1691  N  N     . LYS A 1 209 ? 149.712 132.297 130.463 1.00 32.25 ?  209 LYS A N     1 
ATOM   1692  C  CA    . LYS A 1 209 ? 149.298 131.734 131.739 1.00 29.35 ?  209 LYS A CA    1 
ATOM   1693  C  C     . LYS A 1 209 ? 150.490 131.610 132.678 1.00 33.86 ?  209 LYS A C     1 
ATOM   1694  O  O     . LYS A 1 209 ? 151.575 131.179 132.278 1.00 34.76 ?  209 LYS A O     1 
ATOM   1695  C  CB    . LYS A 1 209 ? 148.648 130.367 131.527 1.00 29.71 ?  209 LYS A CB    1 
ATOM   1696  C  CG    . LYS A 1 209 ? 147.707 129.943 132.638 1.00 32.21 ?  209 LYS A CG    1 
ATOM   1697  C  CD    . LYS A 1 209 ? 147.401 128.457 132.561 1.00 31.43 ?  209 LYS A CD    1 
ATOM   1698  C  CE    . LYS A 1 209 ? 148.650 127.646 132.254 1.00 35.68 ?  209 LYS A CE    1 
ATOM   1699  N  NZ    . LYS A 1 209 ? 148.319 126.271 131.786 1.00 36.68 1  209 LYS A NZ    1 
ATOM   1700  N  N     . GLY A 1 210 ? 150.280 131.988 133.936 1.00 35.89 ?  210 GLY A N     1 
ATOM   1701  C  CA    . GLY A 1 210 ? 151.349 131.945 134.911 1.00 34.31 ?  210 GLY A CA    1 
ATOM   1702  C  C     . GLY A 1 210 ? 152.233 133.166 134.947 1.00 36.82 ?  210 GLY A C     1 
ATOM   1703  O  O     . GLY A 1 210 ? 153.350 133.093 135.467 1.00 38.71 ?  210 GLY A O     1 
ATOM   1704  N  N     . GLU A 1 211 ? 151.777 134.288 134.403 1.00 37.12 ?  211 GLU A N     1 
ATOM   1705  C  CA    . GLU A 1 211 ? 152.507 135.542 134.474 1.00 33.53 ?  211 GLU A CA    1 
ATOM   1706  C  C     . GLU A 1 211 ? 151.968 136.399 135.614 1.00 36.61 ?  211 GLU A C     1 
ATOM   1707  O  O     . GLU A 1 211 ? 150.852 136.202 136.098 1.00 37.11 ?  211 GLU A O     1 
ATOM   1708  C  CB    . GLU A 1 211 ? 152.418 136.302 133.150 1.00 32.02 ?  211 GLU A CB    1 
ATOM   1709  C  CG    . GLU A 1 211 ? 152.980 135.535 131.972 1.00 32.88 ?  211 GLU A CG    1 
ATOM   1710  C  CD    . GLU A 1 211 ? 153.934 136.362 131.141 1.00 37.46 ?  211 GLU A CD    1 
ATOM   1711  O  OE1   . GLU A 1 211 ? 155.041 136.662 131.634 1.00 41.10 ?  211 GLU A OE1   1 
ATOM   1712  O  OE2   . GLU A 1 211 ? 153.588 136.701 129.991 1.00 30.94 -1 211 GLU A OE2   1 
ATOM   1713  N  N     . ALA A 1 212 ? 152.784 137.357 136.039 1.00 34.70 ?  212 ALA A N     1 
ATOM   1714  C  CA    . ALA A 1 212 ? 152.447 138.184 137.187 1.00 31.46 ?  212 ALA A CA    1 
ATOM   1715  C  C     . ALA A 1 212 ? 151.486 139.301 136.802 1.00 36.01 ?  212 ALA A C     1 
ATOM   1716  O  O     . ALA A 1 212 ? 151.562 139.859 135.704 1.00 39.23 ?  212 ALA A O     1 
ATOM   1717  C  CB    . ALA A 1 212 ? 153.713 138.779 137.803 1.00 35.89 ?  212 ALA A CB    1 
ATOM   1718  N  N     . ILE A 1 213 ? 150.577 139.620 137.715 1.00 34.91 ?  213 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 149.707 140.789 137.600 1.00 33.44 ?  213 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 150.053 141.693 138.776 1.00 35.43 ?  213 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 149.504 141.545 139.870 1.00 40.52 ?  213 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 148.222 140.425 137.597 1.00 35.77 ?  213 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 147.946 139.258 136.653 1.00 37.06 ?  213 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 147.384 141.630 137.210 1.00 32.96 ?  213 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 146.607 138.603 136.891 1.00 30.23 ?  213 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 150.953 142.651 138.552 1.00 41.20 ?  214 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 151.422 143.568 139.591 1.00 40.66 ?  214 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 152.070 142.795 140.746 1.00 44.42 ?  214 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 151.552 142.717 141.860 1.00 46.37 ?  214 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 150.284 144.470 140.086 1.00 39.51 ?  214 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 150.443 145.929 139.701 1.00 42.74 ?  214 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 149.276 146.765 140.197 1.00 42.94 ?  214 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 149.195 148.084 139.448 1.00 45.18 ?  214 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 147.825 148.665 139.482 1.00 43.21 1  214 LYS A NZ    1 
ATOM   1735  N  N     . ASP A 1 215 ? 153.198 142.174 140.406 1.00 45.21 ?  215 ASP A N     1 
ATOM   1736  C  CA    . ASP A 1 215 ? 154.167 141.552 141.309 1.00 50.42 ?  215 ASP A CA    1 
ATOM   1737  C  C     . ASP A 1 215 ? 153.605 140.386 142.121 1.00 50.21 ?  215 ASP A C     1 
ATOM   1738  O  O     . ASP A 1 215 ? 154.250 139.944 143.080 1.00 52.51 ?  215 ASP A O     1 
ATOM   1739  C  CB    . ASP A 1 215 ? 154.830 142.588 142.242 1.00 49.52 ?  215 ASP A CB    1 
ATOM   1740  C  CG    . ASP A 1 215 ? 153.916 143.071 143.360 1.00 52.69 ?  215 ASP A CG    1 
ATOM   1741  O  OD1   . ASP A 1 215 ? 153.649 142.306 144.309 1.00 51.32 ?  215 ASP A OD1   1 
ATOM   1742  O  OD2   . ASP A 1 215 ? 153.468 144.235 143.290 1.00 51.14 -1 215 ASP A OD2   1 
ATOM   1743  N  N     . VAL A 1 216 ? 152.441 139.853 141.764 1.00 43.00 ?  216 VAL A N     1 
ATOM   1744  C  CA    . VAL A 1 216 ? 151.984 138.571 142.292 1.00 45.82 ?  216 VAL A CA    1 
ATOM   1745  C  C     . VAL A 1 216 ? 152.035 137.556 141.156 1.00 47.78 ?  216 VAL A C     1 
ATOM   1746  O  O     . VAL A 1 216 ? 151.367 137.722 140.128 1.00 50.41 ?  216 VAL A O     1 
ATOM   1747  C  CB    . VAL A 1 216 ? 150.581 138.667 142.918 1.00 45.53 ?  216 VAL A CB    1 
ATOM   1748  C  CG1   . VAL A 1 216 ? 149.609 139.357 141.996 1.00 44.93 ?  216 VAL A CG1   1 
ATOM   1749  C  CG2   . VAL A 1 216 ? 150.069 137.282 143.276 1.00 45.66 ?  216 VAL A CG2   1 
ATOM   1750  N  N     . GLU A 1 217 ? 152.833 136.512 141.337 1.00 48.05 ?  217 GLU A N     1 
ATOM   1751  C  CA    . GLU A 1 217 ? 153.207 135.616 140.256 1.00 46.87 ?  217 GLU A CA    1 
ATOM   1752  C  C     . GLU A 1 217 ? 152.178 134.506 140.067 1.00 48.29 ?  217 GLU A C     1 
ATOM   1753  O  O     . GLU A 1 217 ? 151.363 134.221 140.947 1.00 49.42 ?  217 GLU A O     1 
ATOM   1754  C  CB    . GLU A 1 217 ? 154.586 135.012 140.525 1.00 48.30 ?  217 GLU A CB    1 
ATOM   1755  C  CG    . GLU A 1 217 ? 155.570 135.999 141.129 1.00 49.23 ?  217 GLU A CG    1 
ATOM   1756  C  CD    . GLU A 1 217 ? 156.454 136.652 140.086 1.00 51.51 ?  217 GLU A CD    1 
ATOM   1757  O  OE1   . GLU A 1 217 ? 156.965 135.932 139.203 1.00 53.39 ?  217 GLU A OE1   1 
ATOM   1758  O  OE2   . GLU A 1 217 ? 156.633 137.886 140.146 1.00 49.38 -1 217 GLU A OE2   1 
ATOM   1759  N  N     . ASN A 1 218 ? 152.235 133.879 138.889 1.00 45.48 ?  218 ASN A N     1 
ATOM   1760  C  CA    . ASN A 1 218 ? 151.325 132.795 138.516 1.00 43.90 ?  218 ASN A CA    1 
ATOM   1761  C  C     . ASN A 1 218 ? 149.869 133.223 138.672 1.00 47.78 ?  218 ASN A C     1 
ATOM   1762  O  O     . ASN A 1 218 ? 149.008 132.449 139.093 1.00 49.11 ?  218 ASN A O     1 
ATOM   1763  C  CB    . ASN A 1 218 ? 151.615 131.530 139.322 1.00 45.70 ?  218 ASN A CB    1 
ATOM   1764  C  CG    . ASN A 1 218 ? 152.805 130.761 138.786 1.00 48.95 ?  218 ASN A CG    1 
ATOM   1765  O  OD1   . ASN A 1 218 ? 152.662 129.911 137.908 1.00 48.93 ?  218 ASN A OD1   1 
ATOM   1766  N  ND2   . ASN A 1 218 ? 153.988 131.062 139.308 1.00 46.74 ?  218 ASN A ND2   1 
ATOM   1767  N  N     . ALA A 1 219 ? 149.593 134.478 138.324 1.00 40.88 ?  219 ALA A N     1 
ATOM   1768  C  CA    . ALA A 1 219 ? 148.281 135.069 138.534 1.00 38.59 ?  219 ALA A CA    1 
ATOM   1769  C  C     . ALA A 1 219 ? 147.442 135.147 137.270 1.00 40.39 ?  219 ALA A C     1 
ATOM   1770  O  O     . ALA A 1 219 ? 146.211 135.082 137.353 1.00 41.10 ?  219 ALA A O     1 
ATOM   1771  C  CB    . ALA A 1 219 ? 148.433 136.474 139.125 1.00 37.28 ?  219 ALA A CB    1 
ATOM   1772  N  N     . THR A 1 220 ? 148.072 135.279 136.107 1.00 37.47 ?  220 THR A N     1 
ATOM   1773  C  CA    . THR A 1 220 ? 147.340 135.447 134.862 1.00 34.68 ?  220 THR A CA    1 
ATOM   1774  C  C     . THR A 1 220 ? 146.798 134.105 134.386 1.00 35.72 ?  220 THR A C     1 
ATOM   1775  O  O     . THR A 1 220 ? 147.492 133.085 134.434 1.00 37.02 ?  220 THR A O     1 
ATOM   1776  C  CB    . THR A 1 220 ? 148.248 136.069 133.800 1.00 33.58 ?  220 THR A CB    1 
ATOM   1777  O  OG1   . THR A 1 220 ? 148.490 137.442 134.125 1.00 36.06 ?  220 THR A OG1   1 
ATOM   1778  C  CG2   . THR A 1 220 ? 147.595 136.020 132.436 1.00 35.48 ?  220 THR A CG2   1 
ATOM   1779  N  N     . LYS A 1 221 ? 145.545 134.108 133.931 1.00 37.24 ?  221 LYS A N     1 
ATOM   1780  C  CA    . LYS A 1 221 ? 144.903 132.900 133.429 1.00 32.88 ?  221 LYS A CA    1 
ATOM   1781  C  C     . LYS A 1 221 ? 145.272 132.587 131.987 1.00 38.04 ?  221 LYS A C     1 
ATOM   1782  O  O     . LYS A 1 221 ? 144.832 131.559 131.460 1.00 43.49 ?  221 LYS A O     1 
ATOM   1783  C  CB    . LYS A 1 221 ? 143.382 133.020 133.545 1.00 33.02 ?  221 LYS A CB    1 
ATOM   1784  C  CG    . LYS A 1 221 ? 142.901 133.614 134.851 1.00 37.07 ?  221 LYS A CG    1 
ATOM   1785  C  CD    . LYS A 1 221 ? 141.405 133.427 135.010 1.00 36.66 ?  221 LYS A CD    1 
ATOM   1786  C  CE    . LYS A 1 221 ? 141.062 132.022 135.467 1.00 35.69 ?  221 LYS A CE    1 
ATOM   1787  N  NZ    . LYS A 1 221 ? 141.856 131.618 136.656 1.00 37.36 1  221 LYS A NZ    1 
ATOM   1788  N  N     . GLY A 1 222 ? 146.056 133.439 131.341 1.00 32.91 ?  222 GLY A N     1 
ATOM   1789  C  CA    . GLY A 1 222 ? 146.458 133.211 129.974 1.00 30.90 ?  222 GLY A CA    1 
ATOM   1790  C  C     . GLY A 1 222 ? 145.422 133.683 128.974 1.00 30.75 ?  222 GLY A C     1 
ATOM   1791  O  O     . GLY A 1 222 ? 144.423 134.325 129.309 1.00 31.07 ?  222 GLY A O     1 
ATOM   1792  N  N     . VAL A 1 223 ? 145.678 133.347 127.710 1.00 31.96 ?  223 VAL A N     1 
ATOM   1793  C  CA    . VAL A 1 223 ? 144.762 133.741 126.646 1.00 26.30 ?  223 VAL A CA    1 
ATOM   1794  C  C     . VAL A 1 223 ? 143.511 132.877 126.615 1.00 22.89 ?  223 VAL A C     1 
ATOM   1795  O  O     . VAL A 1 223 ? 142.526 133.263 125.981 1.00 31.06 ?  223 VAL A O     1 
ATOM   1796  C  CB    . VAL A 1 223 ? 145.451 133.704 125.271 1.00 25.90 ?  223 VAL A CB    1 
ATOM   1797  C  CG1   . VAL A 1 223 ? 146.777 134.440 125.320 1.00 25.11 ?  223 VAL A CG1   1 
ATOM   1798  C  CG2   . VAL A 1 223 ? 145.641 132.272 124.800 1.00 26.84 ?  223 VAL A CG2   1 
ATOM   1799  N  N     . VAL A 1 224 ? 143.518 131.720 127.278 1.00 25.50 ?  224 VAL A N     1 
ATOM   1800  C  CA    . VAL A 1 224 ? 142.352 130.843 127.243 1.00 25.72 ?  224 VAL A CA    1 
ATOM   1801  C  C     . VAL A 1 224 ? 141.206 131.401 128.086 1.00 27.40 ?  224 VAL A C     1 
ATOM   1802  O  O     . VAL A 1 224 ? 140.034 131.214 127.744 1.00 30.19 ?  224 VAL A O     1 
ATOM   1803  C  CB    . VAL A 1 224 ? 142.747 129.423 127.682 1.00 32.71 ?  224 VAL A CB    1 
ATOM   1804  C  CG1   . VAL A 1 224 ? 141.542 128.500 127.667 1.00 31.81 ?  224 VAL A CG1   1 
ATOM   1805  C  CG2   . VAL A 1 224 ? 143.833 128.884 126.770 1.00 29.46 ?  224 VAL A CG2   1 
ATOM   1806  N  N     . GLY A 1 225 ? 141.507 132.096 129.184 1.00 24.18 ?  225 GLY A N     1 
ATOM   1807  C  CA    . GLY A 1 225 ? 140.450 132.752 129.936 1.00 21.73 ?  225 GLY A CA    1 
ATOM   1808  C  C     . GLY A 1 225 ? 139.777 133.856 129.143 1.00 22.30 ?  225 GLY A C     1 
ATOM   1809  O  O     . GLY A 1 225 ? 138.545 133.973 129.138 1.00 31.46 ?  225 GLY A O     1 
ATOM   1810  N  N     . VAL A 1 226 ? 140.573 134.673 128.453 1.00 19.34 ?  226 VAL A N     1 
ATOM   1811  C  CA    . VAL A 1 226 ? 140.016 135.679 127.556 1.00 20.35 ?  226 VAL A CA    1 
ATOM   1812  C  C     . VAL A 1 226 ? 139.261 135.014 126.419 1.00 24.85 ?  226 VAL A C     1 
ATOM   1813  O  O     . VAL A 1 226 ? 138.259 135.546 125.933 1.00 26.82 ?  226 VAL A O     1 
ATOM   1814  C  CB    . VAL A 1 226 ? 141.136 136.599 127.033 1.00 18.19 ?  226 VAL A CB    1 
ATOM   1815  C  CG1   . VAL A 1 226 ? 140.550 137.761 126.245 1.00 25.76 ?  226 VAL A CG1   1 
ATOM   1816  C  CG2   . VAL A 1 226 ? 141.981 137.098 128.185 1.00 20.82 ?  226 VAL A CG2   1 
ATOM   1817  N  N     . MET A 1 227 ? 139.728 133.848 125.975 1.00 28.39 ?  227 MET A N     1 
ATOM   1818  C  CA    . MET A 1 227 ? 139.032 133.104 124.934 1.00 22.22 ?  227 MET A CA    1 
ATOM   1819  C  C     . MET A 1 227 ? 137.651 132.668 125.398 1.00 22.95 ?  227 MET A C     1 
ATOM   1820  O  O     . MET A 1 227 ? 136.680 132.753 124.643 1.00 29.97 ?  227 MET A O     1 
ATOM   1821  C  CB    . MET A 1 227 ? 139.870 131.893 124.527 1.00 19.68 ?  227 MET A CB    1 
ATOM   1822  C  CG    . MET A 1 227 ? 140.940 132.194 123.501 1.00 17.85 ?  227 MET A CG    1 
ATOM   1823  S  SD    . MET A 1 227 ? 141.636 130.699 122.787 1.00 33.28 ?  227 MET A SD    1 
ATOM   1824  C  CE    . MET A 1 227 ? 140.349 130.256 121.637 1.00 29.81 ?  227 MET A CE    1 
ATOM   1825  N  N     . LYS A 1 228 ? 137.547 132.189 126.640 1.00 26.79 ?  228 LYS A N     1 
ATOM   1826  C  CA    . LYS A 1 228 ? 136.244 131.819 127.189 1.00 23.10 ?  228 LYS A CA    1 
ATOM   1827  C  C     . LYS A 1 228 ? 135.342 133.038 127.336 1.00 24.38 ?  228 LYS A C     1 
ATOM   1828  O  O     . LYS A 1 228 ? 134.141 132.975 127.030 1.00 26.05 ?  228 LYS A O     1 
ATOM   1829  C  CB    . LYS A 1 228 ? 136.419 131.121 128.537 1.00 23.32 ?  228 LYS A CB    1 
ATOM   1830  C  CG    . LYS A 1 228 ? 137.213 129.831 128.471 1.00 29.04 ?  228 LYS A CG    1 
ATOM   1831  C  CD    . LYS A 1 228 ? 137.276 129.154 129.827 1.00 36.78 ?  228 LYS A CD    1 
ATOM   1832  C  CE    . LYS A 1 228 ? 138.394 129.724 130.684 1.00 36.15 ?  228 LYS A CE    1 
ATOM   1833  N  NZ    . LYS A 1 228 ? 139.562 128.804 130.760 1.00 30.76 1  228 LYS A NZ    1 
ATOM   1834  N  N     . LEU A 1 229 ? 135.905 134.155 127.806 1.00 24.46 ?  229 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 229 ? 135.137 135.393 127.895 1.00 21.84 ?  229 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 229 ? 134.584 135.794 126.534 1.00 21.51 ?  229 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 229 ? 133.402 136.128 126.403 1.00 22.24 ?  229 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 229 ? 136.011 136.512 128.457 1.00 24.43 ?  229 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 229 ? 136.380 136.512 129.937 1.00 23.02 ?  229 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 229 ? 137.510 137.494 130.160 1.00 24.40 ?  229 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 229 ? 135.183 136.869 130.795 1.00 18.49 ?  229 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 230 ? 135.432 135.761 125.505 1.00 26.92 ?  230 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 230 ? 135.009 136.145 124.163 1.00 18.66 ?  230 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 230 ? 133.999 135.158 123.596 1.00 17.88 ?  230 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 230 ? 133.064 135.555 122.894 1.00 29.69 ?  230 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 230 ? 136.223 136.255 123.245 1.00 20.57 ?  230 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 230 ? 137.117 137.473 123.467 1.00 27.78 ?  230 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 230 ? 138.464 137.274 122.793 1.00 28.12 ?  230 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 230 ? 136.434 138.733 122.963 1.00 21.05 ?  230 LEU A CD2   1 
ATOM   1850  N  N     . ASP A 1 231 ? 134.176 133.868 123.879 1.00 20.37 ?  231 ASP A N     1 
ATOM   1851  C  CA    . ASP A 1 231 ? 133.233 132.868 123.398 1.00 24.19 ?  231 ASP A CA    1 
ATOM   1852  C  C     . ASP A 1 231 ? 131.848 133.097 123.983 1.00 28.73 ?  231 ASP A C     1 
ATOM   1853  O  O     . ASP A 1 231 ? 130.843 133.031 123.266 1.00 33.36 ?  231 ASP A O     1 
ATOM   1854  C  CB    . ASP A 1 231 ? 133.746 131.469 123.737 1.00 27.44 ?  231 ASP A CB    1 
ATOM   1855  C  CG    . ASP A 1 231 ? 132.813 130.376 123.268 1.00 35.91 ?  231 ASP A CG    1 
ATOM   1856  O  OD1   . ASP A 1 231 ? 132.679 130.194 122.040 1.00 39.62 ?  231 ASP A OD1   1 
ATOM   1857  O  OD2   . ASP A 1 231 ? 132.216 129.694 124.125 1.00 38.47 -1 231 ASP A OD2   1 
ATOM   1858  N  N     . ASN A 1 232 ? 131.771 133.394 125.282 1.00 29.49 ?  232 ASN A N     1 
ATOM   1859  C  CA    . ASN A 1 232 ? 130.467 133.689 125.869 1.00 27.94 ?  232 ASN A CA    1 
ATOM   1860  C  C     . ASN A 1 232 ? 129.921 135.032 125.405 1.00 28.52 ?  232 ASN A C     1 
ATOM   1861  O  O     . ASN A 1 232 ? 128.701 135.190 125.280 1.00 33.99 ?  232 ASN A O     1 
ATOM   1862  C  CB    . ASN A 1 232 ? 130.540 133.637 127.390 1.00 29.32 ?  232 ASN A CB    1 
ATOM   1863  C  CG    . ASN A 1 232 ? 130.402 132.232 127.917 1.00 36.30 ?  232 ASN A CG    1 
ATOM   1864  O  OD1   . ASN A 1 232 ? 131.301 131.407 127.765 1.00 38.87 ?  232 ASN A OD1   1 
ATOM   1865  N  ND2   . ASN A 1 232 ? 129.264 131.945 128.538 1.00 33.39 ?  232 ASN A ND2   1 
ATOM   1866  N  N     . ALA A 1 233 ? 130.794 136.005 125.140 1.00 25.87 ?  233 ALA A N     1 
ATOM   1867  C  CA    . ALA A 1 233 ? 130.333 137.279 124.602 1.00 17.88 ?  233 ALA A CA    1 
ATOM   1868  C  C     . ALA A 1 233 ? 129.721 137.102 123.219 1.00 30.07 ?  233 ALA A C     1 
ATOM   1869  O  O     . ALA A 1 233 ? 128.729 137.756 122.880 1.00 36.37 ?  233 ALA A O     1 
ATOM   1870  C  CB    . ALA A 1 233 ? 131.489 138.277 124.558 1.00 23.66 ?  233 ALA A CB    1 
ATOM   1871  N  N     . PHE A 1 234 ? 130.306 136.224 122.403 1.00 32.09 ?  234 PHE A N     1 
ATOM   1872  C  CA    . PHE A 1 234 ? 129.767 135.960 121.076 1.00 25.48 ?  234 PHE A CA    1 
ATOM   1873  C  C     . PHE A 1 234 ? 128.524 135.083 121.129 1.00 23.30 ?  234 PHE A C     1 
ATOM   1874  O  O     . PHE A 1 234 ? 127.635 135.225 120.283 1.00 29.86 ?  234 PHE A O     1 
ATOM   1875  C  CB    . PHE A 1 234 ? 130.839 135.322 120.194 1.00 24.96 ?  234 PHE A CB    1 
ATOM   1876  C  CG    . PHE A 1 234 ? 131.852 136.301 119.677 1.00 24.03 ?  234 PHE A CG    1 
ATOM   1877  C  CD1   . PHE A 1 234 ? 131.456 137.394 118.926 1.00 27.38 ?  234 PHE A CD1   1 
ATOM   1878  C  CD2   . PHE A 1 234 ? 133.196 136.141 119.953 1.00 23.01 ?  234 PHE A CD2   1 
ATOM   1879  C  CE1   . PHE A 1 234 ? 132.384 138.300 118.457 1.00 26.14 ?  234 PHE A CE1   1 
ATOM   1880  C  CE2   . PHE A 1 234 ? 134.127 137.045 119.490 1.00 24.47 ?  234 PHE A CE2   1 
ATOM   1881  C  CZ    . PHE A 1 234 ? 133.721 138.124 118.740 1.00 26.41 ?  234 PHE A CZ    1 
ATOM   1882  N  N     . ARG A 1 235 ? 128.441 134.173 122.101 1.00 31.26 ?  235 ARG A N     1 
ATOM   1883  C  CA    . ARG A 1 235 ? 127.198 133.438 122.303 1.00 26.90 ?  235 ARG A CA    1 
ATOM   1884  C  C     . ARG A 1 235 ? 126.066 134.356 122.739 1.00 32.93 ?  235 ARG A C     1 
ATOM   1885  O  O     . ARG A 1 235 ? 124.915 134.149 122.340 1.00 39.75 ?  235 ARG A O     1 
ATOM   1886  C  CB    . ARG A 1 235 ? 127.392 132.322 123.326 1.00 23.83 ?  235 ARG A CB    1 
ATOM   1887  C  CG    . ARG A 1 235 ? 127.314 130.934 122.729 1.00 35.16 ?  235 ARG A CG    1 
ATOM   1888  C  CD    . ARG A 1 235 ? 126.998 129.881 123.786 1.00 37.47 ?  235 ARG A CD    1 
ATOM   1889  N  NE    . ARG A 1 235 ? 127.890 129.918 124.941 1.00 36.06 ?  235 ARG A NE    1 
ATOM   1890  C  CZ    . ARG A 1 235 ? 129.205 129.754 124.892 1.00 36.85 ?  235 ARG A CZ    1 
ATOM   1891  N  NH1   . ARG A 1 235 ? 129.831 129.486 123.758 1.00 35.35 1  235 ARG A NH1   1 
ATOM   1892  N  NH2   . ARG A 1 235 ? 129.911 129.838 126.016 1.00 33.99 ?  235 ARG A NH2   1 
ATOM   1893  N  N     . TYR A 1 236 ? 126.364 135.362 123.562 1.00 29.33 ?  236 TYR A N     1 
ATOM   1894  C  CA    . TYR A 1 236 ? 125.321 136.276 124.009 1.00 27.39 ?  236 TYR A CA    1 
ATOM   1895  C  C     . TYR A 1 236 ? 124.814 137.141 122.861 1.00 26.88 ?  236 TYR A C     1 
ATOM   1896  O  O     . TYR A 1 236 ? 123.603 137.275 122.659 1.00 32.69 ?  236 TYR A O     1 
ATOM   1897  C  CB    . TYR A 1 236 ? 125.840 137.151 125.148 1.00 28.09 ?  236 TYR A CB    1 
ATOM   1898  C  CG    . TYR A 1 236 ? 124.784 138.061 125.720 1.00 29.84 ?  236 TYR A CG    1 
ATOM   1899  C  CD1   . TYR A 1 236 ? 123.765 137.550 126.510 1.00 26.03 ?  236 TYR A CD1   1 
ATOM   1900  C  CD2   . TYR A 1 236 ? 124.793 139.423 125.458 1.00 29.81 ?  236 TYR A CD2   1 
ATOM   1901  C  CE1   . TYR A 1 236 ? 122.794 138.368 127.029 1.00 30.09 ?  236 TYR A CE1   1 
ATOM   1902  C  CE2   . TYR A 1 236 ? 123.822 140.251 125.977 1.00 23.27 ?  236 TYR A CE2   1 
ATOM   1903  C  CZ    . TYR A 1 236 ? 122.826 139.715 126.764 1.00 24.22 ?  236 TYR A CZ    1 
ATOM   1904  O  OH    . TYR A 1 236 ? 121.851 140.524 127.290 1.00 29.49 ?  236 TYR A OH    1 
ATOM   1905  N  N     . ALA A 1 237 ? 125.729 137.738 122.098 1.00 30.76 ?  237 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 237 ? 125.359 138.598 120.975 1.00 33.92 ?  237 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 237 ? 125.251 137.731 119.724 1.00 38.01 ?  237 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 237 ? 126.194 137.573 118.947 1.00 37.56 ?  237 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 237 ? 126.367 139.726 120.804 1.00 31.93 ?  237 ALA A CB    1 
ATOM   1910  N  N     . ASP A 1 238 ? 124.066 137.153 119.539 1.00 54.09 ?  238 ASP A N     1 
ATOM   1911  C  CA    . ASP A 1 238 ? 123.824 136.203 118.463 1.00 57.14 ?  238 ASP A CA    1 
ATOM   1912  C  C     . ASP A 1 238 ? 122.723 136.637 117.505 1.00 59.65 ?  238 ASP A C     1 
ATOM   1913  O  O     . ASP A 1 238 ? 122.442 135.908 116.547 1.00 62.01 ?  238 ASP A O     1 
ATOM   1914  C  CB    . ASP A 1 238 ? 123.483 134.828 119.048 1.00 56.12 ?  238 ASP A CB    1 
ATOM   1915  C  CG    . ASP A 1 238 ? 122.246 134.859 119.920 1.00 59.17 ?  238 ASP A CG    1 
ATOM   1916  O  OD1   . ASP A 1 238 ? 121.870 135.954 120.387 1.00 58.79 ?  238 ASP A OD1   1 
ATOM   1917  O  OD2   . ASP A 1 238 ? 121.646 133.786 120.140 1.00 61.73 -1 238 ASP A OD2   1 
ATOM   1918  N  N     . GLN A 1 239 ? 122.093 137.791 117.733 1.00 61.84 ?  239 GLN A N     1 
ATOM   1919  C  CA    . GLN A 1 239 ? 121.079 138.347 116.835 1.00 63.57 ?  239 GLN A CA    1 
ATOM   1920  C  C     . GLN A 1 239 ? 119.939 137.346 116.614 1.00 64.40 ?  239 GLN A C     1 
ATOM   1921  O  O     . GLN A 1 239 ? 119.759 136.797 115.524 1.00 64.50 ?  239 GLN A O     1 
ATOM   1922  C  CB    . GLN A 1 239 ? 121.698 138.761 115.494 1.00 62.58 ?  239 GLN A CB    1 
ATOM   1923  C  CG    . GLN A 1 239 ? 123.079 139.377 115.588 1.00 60.47 ?  239 GLN A CG    1 
ATOM   1924  C  CD    . GLN A 1 239 ? 123.845 139.236 114.290 1.00 63.61 ?  239 GLN A CD    1 
ATOM   1925  O  OE1   . GLN A 1 239 ? 125.008 138.831 114.281 1.00 63.04 ?  239 GLN A OE1   1 
ATOM   1926  N  NE2   . GLN A 1 239 ? 123.195 139.567 113.182 1.00 62.96 ?  239 GLN A NE2   1 
ATOM   1927  N  N     . MET A 1 240 ? 119.210 137.087 117.706 1.00 72.88 ?  240 MET A N     1 
ATOM   1928  C  CA    . MET A 1 240 ? 118.089 136.147 117.733 1.00 74.86 ?  240 MET A CA    1 
ATOM   1929  C  C     . MET A 1 240 ? 118.554 134.697 117.648 1.00 74.66 ?  240 MET A C     1 
ATOM   1930  O  O     . MET A 1 240 ? 117.753 133.772 117.817 1.00 76.79 ?  240 MET A O     1 
ATOM   1931  C  CB    . MET A 1 240 ? 117.097 136.434 116.596 1.00 75.37 ?  240 MET A CB    1 
ATOM   1932  C  CG    . MET A 1 240 ? 115.720 135.819 116.777 1.00 74.25 ?  240 MET A CG    1 
ATOM   1933  S  SD    . MET A 1 240 ? 114.343 136.932 116.480 1.00 82.10 ?  240 MET A SD    1 
ATOM   1934  C  CE    . MET A 1 240 ? 112.982 135.770 116.574 1.00 74.95 ?  240 MET A CE    1 
ATOM   1935  N  N     . GLY A 1 241 ? 119.843 134.483 117.412 1.00 73.27 ?  241 GLY A N     1 
ATOM   1936  C  CA    . GLY A 1 241 ? 120.339 133.157 117.131 1.00 72.70 ?  241 GLY A CA    1 
ATOM   1937  C  C     . GLY A 1 241 ? 120.145 132.706 115.700 1.00 75.66 ?  241 GLY A C     1 
ATOM   1938  O  O     . GLY A 1 241 ? 120.560 131.590 115.359 1.00 74.83 ?  241 GLY A O     1 
ATOM   1939  N  N     . GLN A 1 242 ? 119.518 133.532 114.857 1.00 79.13 ?  242 GLN A N     1 
ATOM   1940  C  CA    . GLN A 1 242 ? 119.386 133.197 113.442 1.00 78.63 ?  242 GLN A CA    1 
ATOM   1941  C  C     . GLN A 1 242 ? 120.756 133.015 112.806 1.00 80.35 ?  242 GLN A C     1 
ATOM   1942  O  O     . GLN A 1 242 ? 121.002 132.037 112.091 1.00 79.65 ?  242 GLN A O     1 
ATOM   1943  C  CB    . GLN A 1 242 ? 118.601 134.293 112.718 1.00 77.99 ?  242 GLN A CB    1 
ATOM   1944  C  CG    . GLN A 1 242 ? 117.092 134.203 112.874 1.00 79.49 ?  242 GLN A CG    1 
ATOM   1945  C  CD    . GLN A 1 242 ? 116.355 135.089 111.888 1.00 79.66 ?  242 GLN A CD    1 
ATOM   1946  O  OE1   . GLN A 1 242 ? 116.970 135.757 111.057 1.00 78.67 ?  242 GLN A OE1   1 
ATOM   1947  N  NE2   . GLN A 1 242 ? 115.030 135.101 111.978 1.00 79.18 ?  242 GLN A NE2   1 
ATOM   1948  N  N     . ARG A 1 243 ? 121.664 133.953 113.064 1.00 67.57 ?  243 ARG A N     1 
ATOM   1949  C  CA    . ARG A 1 243 ? 123.081 133.806 112.752 1.00 64.53 ?  243 ARG A CA    1 
ATOM   1950  C  C     . ARG A 1 243 ? 123.842 134.096 114.037 1.00 65.13 ?  243 ARG A C     1 
ATOM   1951  O  O     . ARG A 1 243 ? 124.055 135.262 114.384 1.00 64.19 ?  243 ARG A O     1 
ATOM   1952  C  CB    . ARG A 1 243 ? 123.513 134.751 111.631 1.00 63.99 ?  243 ARG A CB    1 
ATOM   1953  C  CG    . ARG A 1 243 ? 124.933 134.513 111.144 1.00 65.11 ?  243 ARG A CG    1 
ATOM   1954  C  CD    . ARG A 1 243 ? 125.719 135.812 111.070 1.00 63.87 ?  243 ARG A CD    1 
ATOM   1955  N  NE    . ARG A 1 243 ? 126.021 136.335 112.397 1.00 65.64 ?  243 ARG A NE    1 
ATOM   1956  C  CZ    . ARG A 1 243 ? 127.088 137.067 112.690 1.00 62.31 ?  243 ARG A CZ    1 
ATOM   1957  N  NH1   . ARG A 1 243 ? 127.987 137.377 111.771 1.00 61.32 1  243 ARG A NH1   1 
ATOM   1958  N  NH2   . ARG A 1 243 ? 127.257 137.496 113.938 1.00 59.64 ?  243 ARG A NH2   1 
ATOM   1959  N  N     . GLN A 1 244 ? 124.242 133.039 114.742 1.00 62.49 ?  244 GLN A N     1 
ATOM   1960  C  CA    . GLN A 1 244 ? 124.883 133.202 116.038 1.00 60.92 ?  244 GLN A CA    1 
ATOM   1961  C  C     . GLN A 1 244 ? 126.186 133.981 115.899 1.00 61.50 ?  244 GLN A C     1 
ATOM   1962  O  O     . GLN A 1 244 ? 126.809 134.012 114.833 1.00 59.07 ?  244 GLN A O     1 
ATOM   1963  C  CB    . GLN A 1 244 ? 125.148 131.838 116.681 1.00 59.61 ?  244 GLN A CB    1 
ATOM   1964  C  CG    . GLN A 1 244 ? 126.411 131.144 116.199 1.00 61.35 ?  244 GLN A CG    1 
ATOM   1965  C  CD    . GLN A 1 244 ? 126.316 130.690 114.756 1.00 63.43 ?  244 GLN A CD    1 
ATOM   1966  O  OE1   . GLN A 1 244 ? 125.224 130.472 114.232 1.00 62.60 ?  244 GLN A OE1   1 
ATOM   1967  N  NE2   . GLN A 1 244 ? 127.464 130.547 114.103 1.00 60.79 ?  244 GLN A NE2   1 
ATOM   1968  N  N     . GLY A 1 245 ? 126.583 134.634 116.989 1.00 51.77 ?  245 GLY A N     1 
ATOM   1969  C  CA    . GLY A 1 245 ? 127.783 135.446 116.988 1.00 44.75 ?  245 GLY A CA    1 
ATOM   1970  C  C     . GLY A 1 245 ? 129.019 134.657 116.621 1.00 44.79 ?  245 GLY A C     1 
ATOM   1971  O  O     . GLY A 1 245 ? 129.324 133.634 117.241 1.00 45.23 ?  245 GLY A O     1 
ATOM   1972  N  N     . SER A 1 246 ? 129.737 135.123 115.605 1.00 39.42 ?  246 SER A N     1 
ATOM   1973  C  CA    . SER A 1 246 ? 130.919 134.445 115.097 1.00 34.17 ?  246 SER A CA    1 
ATOM   1974  C  C     . SER A 1 246 ? 132.151 135.273 115.423 1.00 31.18 ?  246 SER A C     1 
ATOM   1975  O  O     . SER A 1 246 ? 132.233 136.450 115.052 1.00 27.05 ?  246 SER A O     1 
ATOM   1976  C  CB    . SER A 1 246 ? 130.815 134.218 113.588 1.00 31.85 ?  246 SER A CB    1 
ATOM   1977  O  OG    . SER A 1 246 ? 129.823 133.254 113.286 1.00 41.80 ?  246 SER A OG    1 
ATOM   1978  N  N     . GLY A 1 247 ? 133.105 134.657 116.114 1.00 24.77 ?  247 GLY A N     1 
ATOM   1979  C  CA    . GLY A 1 247 ? 134.340 135.320 116.452 1.00 11.06 ?  247 GLY A CA    1 
ATOM   1980  C  C     . GLY A 1 247 ? 135.531 134.464 116.073 1.00 15.76 ?  247 GLY A C     1 
ATOM   1981  O  O     . GLY A 1 247 ? 135.432 133.248 115.919 1.00 22.75 ?  247 GLY A O     1 
ATOM   1982  N  N     . ALA A 1 248 ? 136.666 135.133 115.911 1.00 19.37 ?  248 ALA A N     1 
ATOM   1983  C  CA    . ALA A 1 248 ? 137.933 134.474 115.651 1.00 16.42 ?  248 ALA A CA    1 
ATOM   1984  C  C     . ALA A 1 248 ? 138.982 135.033 116.596 1.00 12.25 ?  248 ALA A C     1 
ATOM   1985  O  O     . ALA A 1 248 ? 139.004 136.234 116.872 1.00 20.81 ?  248 ALA A O     1 
ATOM   1986  C  CB    . ALA A 1 248 ? 138.383 134.656 114.198 1.00 9.18  ?  248 ALA A CB    1 
ATOM   1987  N  N     . ALA A 1 249 ? 139.839 134.155 117.099 1.00 17.17 ?  249 ALA A N     1 
ATOM   1988  C  CA    . ALA A 1 249 ? 140.969 134.545 117.925 1.00 11.41 ?  249 ALA A CA    1 
ATOM   1989  C  C     . ALA A 1 249 ? 142.252 134.149 117.216 1.00 10.22 ?  249 ALA A C     1 
ATOM   1990  O  O     . ALA A 1 249 ? 142.339 133.069 116.630 1.00 19.58 ?  249 ALA A O     1 
ATOM   1991  C  CB    . ALA A 1 249 ? 140.904 133.895 119.308 1.00 13.14 ?  249 ALA A CB    1 
ATOM   1992  N  N     . TYR A 1 250 ? 143.243 135.029 117.259 1.00 11.19 ?  250 TYR A N     1 
ATOM   1993  C  CA    . TYR A 1 250 ? 144.525 134.773 116.629 1.00 7.84  ?  250 TYR A CA    1 
ATOM   1994  C  C     . TYR A 1 250 ? 145.629 134.842 117.669 1.00 8.84  ?  250 TYR A C     1 
ATOM   1995  O  O     . TYR A 1 250 ? 145.634 135.729 118.528 1.00 13.20 ?  250 TYR A O     1 
ATOM   1996  C  CB    . TYR A 1 250 ? 144.800 135.767 115.500 1.00 10.59 ?  250 TYR A CB    1 
ATOM   1997  C  CG    . TYR A 1 250 ? 144.182 135.370 114.181 1.00 19.08 ?  250 TYR A CG    1 
ATOM   1998  C  CD1   . TYR A 1 250 ? 142.832 135.570 113.938 1.00 8.70  ?  250 TYR A CD1   1 
ATOM   1999  C  CD2   . TYR A 1 250 ? 144.946 134.780 113.182 1.00 12.91 ?  250 TYR A CD2   1 
ATOM   2000  C  CE1   . TYR A 1 250 ? 142.263 135.205 112.740 1.00 0.00  ?  250 TYR A CE1   1 
ATOM   2001  C  CE2   . TYR A 1 250 ? 144.383 134.412 111.979 1.00 7.59  ?  250 TYR A CE2   1 
ATOM   2002  C  CZ    . TYR A 1 250 ? 143.040 134.626 111.764 1.00 7.54  ?  250 TYR A CZ    1 
ATOM   2003  O  OH    . TYR A 1 250 ? 142.469 134.264 110.568 1.00 22.46 ?  250 TYR A OH    1 
ATOM   2004  N  N     . LEU A 1 251 ? 146.555 133.895 117.591 1.00 10.93 ?  251 LEU A N     1 
ATOM   2005  C  CA    . LEU A 1 251 ? 147.704 133.848 118.478 1.00 12.86 ?  251 LEU A CA    1 
ATOM   2006  C  C     . LEU A 1 251 ? 148.959 133.585 117.667 1.00 11.61 ?  251 LEU A C     1 
ATOM   2007  O  O     . LEU A 1 251 ? 148.964 132.734 116.773 1.00 17.27 ?  251 LEU A O     1 
ATOM   2008  C  CB    . LEU A 1 251 ? 147.542 132.764 119.545 1.00 18.54 ?  251 LEU A CB    1 
ATOM   2009  C  CG    . LEU A 1 251 ? 148.286 133.027 120.852 1.00 14.33 ?  251 LEU A CG    1 
ATOM   2010  C  CD1   . LEU A 1 251 ? 147.546 134.051 121.683 1.00 16.35 ?  251 LEU A CD1   1 
ATOM   2011  C  CD2   . LEU A 1 251 ? 148.473 131.742 121.626 1.00 13.33 ?  251 LEU A CD2   1 
ATOM   2012  N  N     . ASN A 1 252 ? 150.016 134.329 117.971 1.00 12.05 ?  252 ASN A N     1 
ATOM   2013  C  CA    . ASN A 1 252 ? 151.313 134.052 117.375 1.00 12.86 ?  252 ASN A CA    1 
ATOM   2014  C  C     . ASN A 1 252 ? 151.826 132.704 117.864 1.00 17.68 ?  252 ASN A C     1 
ATOM   2015  O  O     . ASN A 1 252 ? 151.645 132.337 119.027 1.00 23.42 ?  252 ASN A O     1 
ATOM   2016  C  CB    . ASN A 1 252 ? 152.304 135.162 117.720 1.00 15.86 ?  252 ASN A CB    1 
ATOM   2017  C  CG    . ASN A 1 252 ? 153.565 135.098 116.886 1.00 20.25 ?  252 ASN A CG    1 
ATOM   2018  O  OD1   . ASN A 1 252 ? 154.531 134.433 117.253 1.00 25.80 ?  252 ASN A OD1   1 
ATOM   2019  N  ND2   . ASN A 1 252 ? 153.559 135.786 115.753 1.00 15.68 ?  252 ASN A ND2   1 
ATOM   2020  N  N     . ILE A 1 253 ? 152.467 131.959 116.960 1.00 15.99 ?  253 ILE A N     1 
ATOM   2021  C  CA    . ILE A 1 253 ? 152.930 130.619 117.294 1.00 14.48 ?  253 ILE A CA    1 
ATOM   2022  C  C     . ILE A 1 253 ? 154.009 130.642 118.369 1.00 19.81 ?  253 ILE A C     1 
ATOM   2023  O  O     . ILE A 1 253 ? 154.247 129.622 119.025 1.00 23.62 ?  253 ILE A O     1 
ATOM   2024  C  CB    . ILE A 1 253 ? 153.422 129.902 116.021 1.00 17.64 ?  253 ILE A CB    1 
ATOM   2025  C  CG1   . ILE A 1 253 ? 153.488 128.391 116.246 1.00 19.79 ?  253 ILE A CG1   1 
ATOM   2026  C  CG2   . ILE A 1 253 ? 154.771 130.447 115.579 1.00 14.47 ?  253 ILE A CG2   1 
ATOM   2027  C  CD1   . ILE A 1 253 ? 152.986 127.581 115.079 1.00 16.32 ?  253 ILE A CD1   1 
ATOM   2028  N  N     . PHE A 1 254 ? 154.662 131.782 118.580 1.00 23.04 ?  254 PHE A N     1 
ATOM   2029  C  CA    . PHE A 1 254 ? 155.692 131.916 119.599 1.00 20.04 ?  254 PHE A CA    1 
ATOM   2030  C  C     . PHE A 1 254 ? 155.140 132.374 120.941 1.00 19.83 ?  254 PHE A C     1 
ATOM   2031  O  O     . PHE A 1 254 ? 155.914 132.560 121.885 1.00 29.11 ?  254 PHE A O     1 
ATOM   2032  C  CB    . PHE A 1 254 ? 156.779 132.881 119.122 1.00 23.31 ?  254 PHE A CB    1 
ATOM   2033  C  CG    . PHE A 1 254 ? 157.752 132.262 118.164 1.00 23.76 ?  254 PHE A CG    1 
ATOM   2034  C  CD1   . PHE A 1 254 ? 158.617 131.267 118.583 1.00 25.73 ?  254 PHE A CD1   1 
ATOM   2035  C  CD2   . PHE A 1 254 ? 157.792 132.662 116.840 1.00 24.41 ?  254 PHE A CD2   1 
ATOM   2036  C  CE1   . PHE A 1 254 ? 159.511 130.692 117.704 1.00 24.63 ?  254 PHE A CE1   1 
ATOM   2037  C  CE2   . PHE A 1 254 ? 158.685 132.089 115.957 1.00 28.73 ?  254 PHE A CE2   1 
ATOM   2038  C  CZ    . PHE A 1 254 ? 159.546 131.103 116.391 1.00 26.32 ?  254 PHE A CZ    1 
ATOM   2039  N  N     . HIS A 1 255 ? 153.830 132.573 121.043 1.00 22.21 ?  255 HIS A N     1 
ATOM   2040  C  CA    . HIS A 1 255 ? 153.199 132.806 122.332 1.00 22.02 ?  255 HIS A CA    1 
ATOM   2041  C  C     . HIS A 1 255 ? 153.290 131.544 123.180 1.00 23.79 ?  255 HIS A C     1 
ATOM   2042  O  O     . HIS A 1 255 ? 153.167 130.428 122.673 1.00 27.87 ?  255 HIS A O     1 
ATOM   2043  C  CB    . HIS A 1 255 ? 151.738 133.209 122.133 1.00 23.90 ?  255 HIS A CB    1 
ATOM   2044  C  CG    . HIS A 1 255 ? 151.132 133.918 123.305 1.00 19.97 ?  255 HIS A CG    1 
ATOM   2045  N  ND1   . HIS A 1 255 ? 150.749 133.264 124.454 1.00 16.34 ?  255 HIS A ND1   1 
ATOM   2046  C  CD2   . HIS A 1 255 ? 150.815 135.220 123.489 1.00 17.37 ?  255 HIS A CD2   1 
ATOM   2047  C  CE1   . HIS A 1 255 ? 150.239 134.136 125.305 1.00 17.98 ?  255 HIS A CE1   1 
ATOM   2048  N  NE2   . HIS A 1 255 ? 150.265 135.330 124.743 1.00 17.01 ?  255 HIS A NE2   1 
ATOM   2049  N  N     . ARG A 1 256 ? 153.521 131.724 124.482 1.00 23.57 ?  256 ARG A N     1 
ATOM   2050  C  CA    . ARG A 1 256 ? 153.643 130.572 125.370 1.00 26.08 ?  256 ARG A CA    1 
ATOM   2051  C  C     . ARG A 1 256 ? 152.346 129.778 125.447 1.00 25.39 ?  256 ARG A C     1 
ATOM   2052  O  O     . ARG A 1 256 ? 152.376 128.551 125.594 1.00 31.14 ?  256 ARG A O     1 
ATOM   2053  C  CB    . ARG A 1 256 ? 154.069 131.027 126.763 1.00 28.03 ?  256 ARG A CB    1 
ATOM   2054  C  CG    . ARG A 1 256 ? 154.325 129.888 127.725 1.00 29.43 ?  256 ARG A CG    1 
ATOM   2055  C  CD    . ARG A 1 256 ? 153.388 129.944 128.916 1.00 29.65 ?  256 ARG A CD    1 
ATOM   2056  N  NE    . ARG A 1 256 ? 152.130 129.254 128.669 1.00 31.35 ?  256 ARG A NE    1 
ATOM   2057  C  CZ    . ARG A 1 256 ? 151.888 127.997 129.010 1.00 34.72 ?  256 ARG A CZ    1 
ATOM   2058  N  NH1   . ARG A 1 256 ? 152.804 127.257 129.613 1.00 33.44 1  256 ARG A NH1   1 
ATOM   2059  N  NH2   . ARG A 1 256 ? 150.698 127.467 128.740 1.00 30.56 ?  256 ARG A NH2   1 
ATOM   2060  N  N     . ASP A 1 257 ? 151.204 130.451 125.342 1.00 23.03 ?  257 ASP A N     1 
ATOM   2061  C  CA    . ASP A 1 257 ? 149.900 129.811 125.435 1.00 19.77 ?  257 ASP A CA    1 
ATOM   2062  C  C     . ASP A 1 257 ? 149.473 129.128 124.146 1.00 23.50 ?  257 ASP A C     1 
ATOM   2063  O  O     . ASP A 1 257 ? 148.289 128.805 124.015 1.00 29.98 ?  257 ASP A O     1 
ATOM   2064  C  CB    . ASP A 1 257 ? 148.837 130.837 125.834 1.00 25.21 ?  257 ASP A CB    1 
ATOM   2065  C  CG    . ASP A 1 257 ? 148.926 131.236 127.287 1.00 31.90 ?  257 ASP A CG    1 
ATOM   2066  O  OD1   . ASP A 1 257 ? 149.642 130.561 128.054 1.00 32.69 ?  257 ASP A OD1   1 
ATOM   2067  O  OD2   . ASP A 1 257 ? 148.271 132.226 127.661 1.00 32.98 -1 257 ASP A OD2   1 
ATOM   2068  N  N     . ILE A 1 258 ? 150.387 128.899 123.202 1.00 24.69 ?  258 ILE A N     1 
ATOM   2069  C  CA    . ILE A 1 258 ? 149.987 128.387 121.894 1.00 21.61 ?  258 ILE A CA    1 
ATOM   2070  C  C     . ILE A 1 258 ? 149.406 126.983 122.014 1.00 20.20 ?  258 ILE A C     1 
ATOM   2071  O  O     . ILE A 1 258 ? 148.435 126.642 121.331 1.00 27.04 ?  258 ILE A O     1 
ATOM   2072  C  CB    . ILE A 1 258 ? 151.171 128.441 120.907 1.00 24.23 ?  258 ILE A CB    1 
ATOM   2073  C  CG1   . ILE A 1 258 ? 150.721 128.016 119.507 1.00 22.62 ?  258 ILE A CG1   1 
ATOM   2074  C  CG2   . ILE A 1 258 ? 152.342 127.594 121.391 1.00 17.77 ?  258 ILE A CG2   1 
ATOM   2075  C  CD1   . ILE A 1 258 ? 149.704 128.945 118.884 1.00 17.72 ?  258 ILE A CD1   1 
ATOM   2076  N  N     . ASN A 1 259 ? 149.977 126.150 122.886 1.00 31.20 ?  259 ASN A N     1 
ATOM   2077  C  CA    . ASN A 1 259 ? 149.470 124.790 123.036 1.00 25.53 ?  259 ASN A CA    1 
ATOM   2078  C  C     . ASN A 1 259 ? 148.100 124.780 123.702 1.00 29.96 ?  259 ASN A C     1 
ATOM   2079  O  O     . ASN A 1 259 ? 147.210 124.032 123.286 1.00 34.90 ?  259 ASN A O     1 
ATOM   2080  C  CB    . ASN A 1 259 ? 150.468 123.948 123.825 1.00 30.04 ?  259 ASN A CB    1 
ATOM   2081  C  CG    . ASN A 1 259 ? 151.769 123.742 123.079 1.00 34.90 ?  259 ASN A CG    1 
ATOM   2082  O  OD1   . ASN A 1 259 ? 151.804 123.084 122.041 1.00 34.38 ?  259 ASN A OD1   1 
ATOM   2083  N  ND2   . ASN A 1 259 ? 152.848 124.309 123.604 1.00 36.03 ?  259 ASN A ND2   1 
ATOM   2084  N  N     . ASP A 1 260 ? 147.910 125.603 124.737 1.00 29.27 ?  260 ASP A N     1 
ATOM   2085  C  CA    . ASP A 1 260 ? 146.585 125.739 125.331 1.00 25.18 ?  260 ASP A CA    1 
ATOM   2086  C  C     . ASP A 1 260 ? 145.614 126.414 124.373 1.00 26.78 ?  260 ASP A C     1 
ATOM   2087  O  O     . ASP A 1 260 ? 144.418 126.109 124.385 1.00 35.48 ?  260 ASP A O     1 
ATOM   2088  C  CB    . ASP A 1 260 ? 146.670 126.525 126.639 1.00 27.48 ?  260 ASP A CB    1 
ATOM   2089  C  CG    . ASP A 1 260 ? 147.798 126.050 127.532 1.00 39.93 ?  260 ASP A CG    1 
ATOM   2090  O  OD1   . ASP A 1 260 ? 147.953 124.822 127.696 1.00 37.41 ?  260 ASP A OD1   1 
ATOM   2091  O  OD2   . ASP A 1 260 ? 148.532 126.907 128.068 1.00 39.68 -1 260 ASP A OD2   1 
ATOM   2092  N  N     . PHE A 1 261 ? 146.111 127.342 123.552 1.00 31.54 ?  261 PHE A N     1 
ATOM   2093  C  CA    . PHE A 1 261 ? 145.280 127.976 122.535 1.00 22.38 ?  261 PHE A CA    1 
ATOM   2094  C  C     . PHE A 1 261 ? 144.762 126.948 121.540 1.00 21.58 ?  261 PHE A C     1 
ATOM   2095  O  O     . PHE A 1 261 ? 143.592 126.992 121.140 1.00 24.08 ?  261 PHE A O     1 
ATOM   2096  C  CB    . PHE A 1 261 ? 146.094 129.065 121.832 1.00 15.65 ?  261 PHE A CB    1 
ATOM   2097  C  CG    . PHE A 1 261 ? 145.378 129.750 120.704 1.00 22.10 ?  261 PHE A CG    1 
ATOM   2098  C  CD1   . PHE A 1 261 ? 144.520 130.805 120.954 1.00 20.48 ?  261 PHE A CD1   1 
ATOM   2099  C  CD2   . PHE A 1 261 ? 145.600 129.373 119.392 1.00 24.42 ?  261 PHE A CD2   1 
ATOM   2100  C  CE1   . PHE A 1 261 ? 143.874 131.449 119.921 1.00 14.82 ?  261 PHE A CE1   1 
ATOM   2101  C  CE2   . PHE A 1 261 ? 144.956 130.015 118.356 1.00 20.16 ?  261 PHE A CE2   1 
ATOM   2102  C  CZ    . PHE A 1 261 ? 144.095 131.055 118.623 1.00 14.38 ?  261 PHE A CZ    1 
ATOM   2103  N  N     . LEU A 1 262 ? 145.618 126.010 121.133 1.00 26.28 ?  262 LEU A N     1 
ATOM   2104  C  CA    . LEU A 1 262 ? 145.209 124.955 120.214 1.00 22.74 ?  262 LEU A CA    1 
ATOM   2105  C  C     . LEU A 1 262 ? 144.366 123.886 120.895 1.00 30.54 ?  262 LEU A C     1 
ATOM   2106  O  O     . LEU A 1 262 ? 143.518 123.267 120.244 1.00 34.37 ?  262 LEU A O     1 
ATOM   2107  C  CB    . LEU A 1 262 ? 146.438 124.312 119.573 1.00 26.69 ?  262 LEU A CB    1 
ATOM   2108  C  CG    . LEU A 1 262 ? 147.310 125.227 118.715 1.00 23.46 ?  262 LEU A CG    1 
ATOM   2109  C  CD1   . LEU A 1 262 ? 148.579 124.505 118.306 1.00 24.29 ?  262 LEU A CD1   1 
ATOM   2110  C  CD2   . LEU A 1 262 ? 146.545 125.714 117.501 1.00 22.16 ?  262 LEU A CD2   1 
ATOM   2111  N  N     . ASP A 1 263 ? 144.580 123.649 122.191 1.00 38.57 ?  263 ASP A N     1 
ATOM   2112  C  CA    . ASP A 1 263 ? 143.821 122.630 122.906 1.00 30.89 ?  263 ASP A CA    1 
ATOM   2113  C  C     . ASP A 1 263 ? 142.358 123.003 123.094 1.00 32.35 ?  263 ASP A C     1 
ATOM   2114  O  O     . ASP A 1 263 ? 141.563 122.136 123.472 1.00 41.94 ?  263 ASP A O     1 
ATOM   2115  C  CB    . ASP A 1 263 ? 144.456 122.352 124.268 1.00 33.94 ?  263 ASP A CB    1 
ATOM   2116  C  CG    . ASP A 1 263 ? 145.753 121.579 124.161 1.00 40.92 ?  263 ASP A CG    1 
ATOM   2117  O  OD1   . ASP A 1 263 ? 146.005 120.987 123.091 1.00 37.88 ?  263 ASP A OD1   1 
ATOM   2118  O  OD2   . ASP A 1 263 ? 146.519 121.564 125.146 1.00 42.51 -1 263 ASP A OD2   1 
ATOM   2119  N  N     . THR A 1 264 ? 141.983 124.260 122.852 1.00 37.53 ?  264 THR A N     1 
ATOM   2120  C  CA    . THR A 1 264 ? 140.581 124.651 122.920 1.00 36.65 ?  264 THR A CA    1 
ATOM   2121  C  C     . THR A 1 264 ? 139.755 124.071 121.780 1.00 38.27 ?  264 THR A C     1 
ATOM   2122  O  O     . THR A 1 264 ? 138.523 124.105 121.854 1.00 42.43 ?  264 THR A O     1 
ATOM   2123  C  CB    . THR A 1 264 ? 140.458 126.176 122.916 1.00 37.79 ?  264 THR A CB    1 
ATOM   2124  O  OG1   . THR A 1 264 ? 141.024 126.703 121.710 1.00 41.67 ?  264 THR A OG1   1 
ATOM   2125  C  CG2   . THR A 1 264 ? 141.182 126.773 124.111 1.00 33.19 ?  264 THR A CG2   1 
ATOM   2126  N  N     . LYS A 1 265 ? 140.397 123.544 120.739 1.00 34.74 ?  265 LYS A N     1 
ATOM   2127  C  CA    . LYS A 1 265 ? 139.701 122.978 119.594 1.00 38.69 ?  265 LYS A CA    1 
ATOM   2128  C  C     . LYS A 1 265 ? 139.773 121.460 119.537 1.00 38.10 ?  265 LYS A C     1 
ATOM   2129  O  O     . LYS A 1 265 ? 139.180 120.861 118.634 1.00 42.13 ?  265 LYS A O     1 
ATOM   2130  C  CB    . LYS A 1 265 ? 140.258 123.566 118.294 1.00 37.22 ?  265 LYS A CB    1 
ATOM   2131  C  CG    . LYS A 1 265 ? 139.733 124.947 117.971 1.00 37.99 ?  265 LYS A CG    1 
ATOM   2132  C  CD    . LYS A 1 265 ? 138.243 125.033 118.216 1.00 38.69 ?  265 LYS A CD    1 
ATOM   2133  C  CE    . LYS A 1 265 ? 137.704 126.384 117.808 1.00 36.61 ?  265 LYS A CE    1 
ATOM   2134  N  NZ    . LYS A 1 265 ? 136.317 126.591 118.300 1.00 42.06 1  265 LYS A NZ    1 
ATOM   2135  N  N     . LYS A 1 266 ? 140.481 120.824 120.463 1.00 40.85 ?  266 LYS A N     1 
ATOM   2136  C  CA    . LYS A 1 266 ? 140.528 119.370 120.493 1.00 45.78 ?  266 LYS A CA    1 
ATOM   2137  C  C     . LYS A 1 266 ? 139.159 118.802 120.844 1.00 51.25 ?  266 LYS A C     1 
ATOM   2138  O  O     . LYS A 1 266 ? 138.396 119.384 121.621 1.00 51.79 ?  266 LYS A O     1 
ATOM   2139  C  CB    . LYS A 1 266 ? 141.574 118.887 121.496 1.00 44.22 ?  266 LYS A CB    1 
ATOM   2140  C  CG    . LYS A 1 266 ? 142.994 118.909 120.962 1.00 46.23 ?  266 LYS A CG    1 
ATOM   2141  C  CD    . LYS A 1 266 ? 143.984 118.394 121.991 1.00 48.71 ?  266 LYS A CD    1 
ATOM   2142  C  CE    . LYS A 1 266 ? 145.345 118.139 121.364 1.00 49.28 ?  266 LYS A CE    1 
ATOM   2143  N  NZ    . LYS A 1 266 ? 146.419 118.005 122.387 1.00 47.87 1  266 LYS A NZ    1 
ATOM   2144  N  N     . ILE A 1 267 ? 138.845 117.651 120.249 1.00 54.28 ?  267 ILE A N     1 
ATOM   2145  C  CA    . ILE A 1 267 ? 137.559 117.008 120.503 1.00 55.14 ?  267 ILE A CA    1 
ATOM   2146  C  C     . ILE A 1 267 ? 137.457 116.565 121.957 1.00 57.07 ?  267 ILE A C     1 
ATOM   2147  O  O     . ILE A 1 267 ? 136.377 116.609 122.558 1.00 54.69 ?  267 ILE A O     1 
ATOM   2148  C  CB    . ILE A 1 267 ? 137.351 115.834 119.529 1.00 55.54 ?  267 ILE A CB    1 
ATOM   2149  C  CG1   . ILE A 1 267 ? 138.634 115.008 119.408 1.00 57.04 ?  267 ILE A CG1   1 
ATOM   2150  C  CG2   . ILE A 1 267 ? 136.906 116.343 118.169 1.00 55.23 ?  267 ILE A CG2   1 
ATOM   2151  C  CD1   . ILE A 1 267 ? 138.498 113.794 118.519 1.00 55.54 ?  267 ILE A CD1   1 
ATOM   2152  N  N     . SER A 1 268 ? 138.573 116.139 122.546 1.00 60.16 ?  268 SER A N     1 
ATOM   2153  C  CA    . SER A 1 268 ? 138.613 115.700 123.935 1.00 61.20 ?  268 SER A CA    1 
ATOM   2154  C  C     . SER A 1 268 ? 138.784 116.851 124.923 1.00 63.52 ?  268 SER A C     1 
ATOM   2155  O  O     . SER A 1 268 ? 139.165 116.607 126.075 1.00 63.03 ?  268 SER A O     1 
ATOM   2156  C  CB    . SER A 1 268 ? 139.736 114.679 124.127 1.00 63.43 ?  268 SER A CB    1 
ATOM   2157  O  OG    . SER A 1 268 ? 140.977 115.198 123.684 1.00 62.04 ?  268 SER A OG    1 
ATOM   2158  N  N     . ALA A 1 269 ? 138.517 118.087 124.510 1.00 67.34 ?  269 ALA A N     1 
ATOM   2159  C  CA    . ALA A 1 269 ? 138.685 119.224 125.404 1.00 66.38 ?  269 ALA A CA    1 
ATOM   2160  C  C     . ALA A 1 269 ? 137.547 119.289 126.415 1.00 67.63 ?  269 ALA A C     1 
ATOM   2161  O  O     . ALA A 1 269 ? 136.393 118.987 126.099 1.00 65.73 ?  269 ALA A O     1 
ATOM   2162  C  CB    . ALA A 1 269 ? 138.752 120.525 124.605 1.00 63.69 ?  269 ALA A CB    1 
ATOM   2163  N  N     . ASP A 1 270 ? 137.881 119.688 127.639 1.00 75.07 ?  270 ASP A N     1 
ATOM   2164  C  CA    . ASP A 1 270 ? 136.887 119.801 128.694 1.00 75.00 ?  270 ASP A CA    1 
ATOM   2165  C  C     . ASP A 1 270 ? 136.029 121.048 128.494 1.00 74.74 ?  270 ASP A C     1 
ATOM   2166  O  O     . ASP A 1 270 ? 136.391 121.979 127.768 1.00 75.33 ?  270 ASP A O     1 
ATOM   2167  C  CB    . ASP A 1 270 ? 137.565 119.841 130.064 1.00 75.61 ?  270 ASP A CB    1 
ATOM   2168  C  CG    . ASP A 1 270 ? 136.639 119.413 131.187 1.00 77.85 ?  270 ASP A CG    1 
ATOM   2169  O  OD1   . ASP A 1 270 ? 135.607 120.084 131.400 1.00 77.52 ?  270 ASP A OD1   1 
ATOM   2170  O  OD2   . ASP A 1 270 ? 136.942 118.403 131.857 1.00 76.02 -1 270 ASP A OD2   1 
ATOM   2171  N  N     . GLU A 1 271 ? 134.870 121.055 129.156 1.00 75.70 ?  271 GLU A N     1 
ATOM   2172  C  CA    . GLU A 1 271 ? 133.947 122.178 129.040 1.00 76.74 ?  271 GLU A CA    1 
ATOM   2173  C  C     . GLU A 1 271 ? 134.502 123.458 129.652 1.00 76.23 ?  271 GLU A C     1 
ATOM   2174  O  O     . GLU A 1 271 ? 134.039 124.548 129.300 1.00 75.27 ?  271 GLU A O     1 
ATOM   2175  C  CB    . GLU A 1 271 ? 132.610 121.826 129.692 1.00 75.14 ?  271 GLU A CB    1 
ATOM   2176  C  CG    . GLU A 1 271 ? 131.896 120.653 129.043 1.00 75.56 ?  271 GLU A CG    1 
ATOM   2177  C  CD    . GLU A 1 271 ? 131.514 120.931 127.602 1.00 76.58 ?  271 GLU A CD    1 
ATOM   2178  O  OE1   . GLU A 1 271 ? 131.087 122.067 127.307 1.00 76.79 ?  271 GLU A OE1   1 
ATOM   2179  O  OE2   . GLU A 1 271 ? 131.644 120.014 126.764 1.00 75.92 -1 271 GLU A OE2   1 
ATOM   2180  N  N     . ASP A 1 272 ? 135.476 123.355 130.555 1.00 74.59 ?  272 ASP A N     1 
ATOM   2181  C  CA    . ASP A 1 272 ? 136.091 124.530 131.157 1.00 75.23 ?  272 ASP A CA    1 
ATOM   2182  C  C     . ASP A 1 272 ? 137.216 125.109 130.309 1.00 73.89 ?  272 ASP A C     1 
ATOM   2183  O  O     . ASP A 1 272 ? 137.807 126.121 130.702 1.00 71.80 ?  272 ASP A O     1 
ATOM   2184  C  CB    . ASP A 1 272 ? 136.624 124.192 132.551 1.00 74.63 ?  272 ASP A CB    1 
ATOM   2185  C  CG    . ASP A 1 272 ? 135.548 124.247 133.618 1.00 76.48 ?  272 ASP A CG    1 
ATOM   2186  O  OD1   . ASP A 1 272 ? 134.471 124.820 133.349 1.00 76.29 ?  272 ASP A OD1   1 
ATOM   2187  O  OD2   . ASP A 1 272 ? 135.782 123.722 134.727 1.00 74.73 -1 272 ASP A OD2   1 
ATOM   2188  N  N     . VAL A 1 273 ? 137.533 124.490 129.172 1.00 64.46 ?  273 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 273 ? 138.593 124.945 128.282 1.00 63.69 ?  273 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 273 ? 138.073 125.178 126.868 1.00 61.79 ?  273 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 273 ? 138.387 126.191 126.236 1.00 62.73 ?  273 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 273 ? 139.780 123.954 128.270 1.00 64.13 ?  273 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 273 ? 140.709 124.239 127.101 1.00 60.73 ?  273 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 273 ? 140.536 124.017 129.587 1.00 62.17 ?  273 VAL A CG2   1 
ATOM   2195  N  N     . ARG A 1 274 ? 137.265 124.250 126.359 1.00 58.79 ?  274 ARG A N     1 
ATOM   2196  C  CA    . ARG A 1 274 ? 136.847 124.288 124.964 1.00 56.27 ?  274 ARG A CA    1 
ATOM   2197  C  C     . ARG A 1 274 ? 135.996 125.517 124.669 1.00 56.31 ?  274 ARG A C     1 
ATOM   2198  O  O     . ARG A 1 274 ? 135.119 125.893 125.453 1.00 59.27 ?  274 ARG A O     1 
ATOM   2199  C  CB    . ARG A 1 274 ? 136.073 123.015 124.617 1.00 58.56 ?  274 ARG A CB    1 
ATOM   2200  C  CG    . ARG A 1 274 ? 134.923 123.218 123.645 1.00 56.98 ?  274 ARG A CG    1 
ATOM   2201  C  CD    . ARG A 1 274 ? 134.377 121.888 123.140 1.00 57.29 ?  274 ARG A CD    1 
ATOM   2202  N  NE    . ARG A 1 274 ? 135.290 121.193 122.237 1.00 60.77 ?  274 ARG A NE    1 
ATOM   2203  C  CZ    . ARG A 1 274 ? 135.740 121.670 121.084 1.00 60.46 ?  274 ARG A CZ    1 
ATOM   2204  N  NH1   . ARG A 1 274 ? 135.347 122.843 120.614 1.00 59.29 1  274 ARG A NH1   1 
ATOM   2205  N  NH2   . ARG A 1 274 ? 136.596 120.942 120.372 1.00 56.10 ?  274 ARG A NH2   1 
ATOM   2206  N  N     . VAL A 1 275 ? 136.267 126.146 123.527 1.00 47.22 ?  275 VAL A N     1 
ATOM   2207  C  CA    . VAL A 1 275 ? 135.460 127.237 122.998 1.00 47.42 ?  275 VAL A CA    1 
ATOM   2208  C  C     . VAL A 1 275 ? 134.776 126.741 121.732 1.00 47.78 ?  275 VAL A C     1 
ATOM   2209  O  O     . VAL A 1 275 ? 135.384 126.030 120.925 1.00 49.68 ?  275 VAL A O     1 
ATOM   2210  C  CB    . VAL A 1 275 ? 136.304 128.496 122.716 1.00 45.57 ?  275 VAL A CB    1 
ATOM   2211  C  CG1   . VAL A 1 275 ? 136.784 129.112 124.019 1.00 42.16 ?  275 VAL A CG1   1 
ATOM   2212  C  CG2   . VAL A 1 275 ? 137.481 128.162 121.823 1.00 46.32 ?  275 VAL A CG2   1 
ATOM   2213  N  N     . LYS A 1 276 ? 133.505 127.095 121.572 1.00 47.35 ?  276 LYS A N     1 
ATOM   2214  C  CA    . LYS A 1 276 ? 132.685 126.566 120.489 1.00 48.92 ?  276 LYS A CA    1 
ATOM   2215  C  C     . LYS A 1 276 ? 132.368 127.583 119.406 1.00 45.86 ?  276 LYS A C     1 
ATOM   2216  O  O     . LYS A 1 276 ? 132.408 127.245 118.221 1.00 51.39 ?  276 LYS A O     1 
ATOM   2217  C  CB    . LYS A 1 276 ? 131.376 126.006 121.058 1.00 49.48 ?  276 LYS A CB    1 
ATOM   2218  C  CG    . LYS A 1 276 ? 131.582 124.826 121.994 1.00 50.86 ?  276 LYS A CG    1 
ATOM   2219  C  CD    . LYS A 1 276 ? 130.283 124.382 122.643 1.00 51.93 ?  276 LYS A CD    1 
ATOM   2220  C  CE    . LYS A 1 276 ? 130.517 123.201 123.574 1.00 52.38 ?  276 LYS A CE    1 
ATOM   2221  N  NZ    . LYS A 1 276 ? 129.354 122.956 124.471 1.00 54.84 1  276 LYS A NZ    1 
ATOM   2222  N  N     . THR A 1 277 ? 132.056 128.823 119.774 1.00 37.03 ?  277 THR A N     1 
ATOM   2223  C  CA    . THR A 1 277 ? 131.687 129.857 118.818 1.00 38.81 ?  277 THR A CA    1 
ATOM   2224  C  C     . THR A 1 277 ? 132.876 130.690 118.360 1.00 40.67 ?  277 THR A C     1 
ATOM   2225  O  O     . THR A 1 277 ? 132.691 131.661 117.619 1.00 39.52 ?  277 THR A O     1 
ATOM   2226  C  CB    . THR A 1 277 ? 130.618 130.772 119.417 1.00 39.99 ?  277 THR A CB    1 
ATOM   2227  O  OG1   . THR A 1 277 ? 131.249 131.842 120.133 1.00 38.24 ?  277 THR A OG1   1 
ATOM   2228  C  CG2   . THR A 1 277 ? 129.733 129.991 120.365 1.00 38.90 ?  277 THR A CG2   1 
ATOM   2229  N  N     . LEU A 1 278 ? 134.087 130.336 118.779 1.00 36.61 ?  278 LEU A N     1 
ATOM   2230  C  CA    . LEU A 1 278 ? 135.279 131.131 118.507 1.00 30.45 ?  278 LEU A CA    1 
ATOM   2231  C  C     . LEU A 1 278 ? 136.208 130.337 117.600 1.00 24.23 ?  278 LEU A C     1 
ATOM   2232  O  O     . LEU A 1 278 ? 136.795 129.340 118.029 1.00 32.43 ?  278 LEU A O     1 
ATOM   2233  C  CB    . LEU A 1 278 ? 135.984 131.514 119.808 1.00 30.01 ?  278 LEU A CB    1 
ATOM   2234  C  CG    . LEU A 1 278 ? 136.865 132.761 119.778 1.00 28.95 ?  278 LEU A CG    1 
ATOM   2235  C  CD1   . LEU A 1 278 ? 136.019 134.015 119.700 1.00 23.64 ?  278 LEU A CD1   1 
ATOM   2236  C  CD2   . LEU A 1 278 ? 137.758 132.800 121.001 1.00 26.19 ?  278 LEU A CD2   1 
ATOM   2237  N  N     . SER A 1 279 ? 136.339 130.780 116.353 1.00 24.49 ?  279 SER A N     1 
ATOM   2238  C  CA    . SER A 1 279 ? 137.365 130.245 115.474 1.00 15.83 ?  279 SER A CA    1 
ATOM   2239  C  C     . SER A 1 279 ? 138.739 130.678 115.969 1.00 17.60 ?  279 SER A C     1 
ATOM   2240  O  O     . SER A 1 279 ? 138.883 131.663 116.697 1.00 28.53 ?  279 SER A O     1 
ATOM   2241  C  CB    . SER A 1 279 ? 137.148 130.721 114.038 1.00 18.86 ?  279 SER A CB    1 
ATOM   2242  O  OG    . SER A 1 279 ? 135.858 130.373 113.571 1.00 26.41 ?  279 SER A OG    1 
ATOM   2243  N  N     . ILE A 1 280 ? 139.761 129.924 115.583 1.00 15.31 ?  280 ILE A N     1 
ATOM   2244  C  CA    . ILE A 1 280 ? 141.120 130.195 116.031 1.00 16.70 ?  280 ILE A CA    1 
ATOM   2245  C  C     . ILE A 1 280 ? 142.044 130.250 114.825 1.00 15.46 ?  280 ILE A C     1 
ATOM   2246  O  O     . ILE A 1 280 ? 141.886 129.484 113.870 1.00 20.73 ?  280 ILE A O     1 
ATOM   2247  C  CB    . ILE A 1 280 ? 141.612 129.155 117.060 1.00 17.82 ?  280 ILE A CB    1 
ATOM   2248  C  CG1   . ILE A 1 280 ? 141.633 127.746 116.469 1.00 23.63 ?  280 ILE A CG1   1 
ATOM   2249  C  CG2   . ILE A 1 280 ? 140.748 129.187 118.299 1.00 18.85 ?  280 ILE A CG2   1 
ATOM   2250  C  CD1   . ILE A 1 280 ? 142.621 126.833 117.153 1.00 18.27 ?  280 ILE A CD1   1 
ATOM   2251  N  N     . GLY A 1 281 ? 142.985 131.184 114.863 1.00 9.44  ?  281 GLY A N     1 
ATOM   2252  C  CA    . GLY A 1 281 ? 144.025 131.257 113.859 1.00 4.46  ?  281 GLY A CA    1 
ATOM   2253  C  C     . GLY A 1 281 ? 145.382 131.355 114.521 1.00 11.28 ?  281 GLY A C     1 
ATOM   2254  O  O     . GLY A 1 281 ? 145.522 131.878 115.625 1.00 21.39 ?  281 GLY A O     1 
ATOM   2255  N  N     . VAL A 1 282 ? 146.388 130.830 113.832 1.00 18.47 ?  282 VAL A N     1 
ATOM   2256  C  CA    . VAL A 1 282 ? 147.760 130.832 114.321 1.00 16.31 ?  282 VAL A CA    1 
ATOM   2257  C  C     . VAL A 1 282 ? 148.618 131.613 113.340 1.00 14.87 ?  282 VAL A C     1 
ATOM   2258  O  O     . VAL A 1 282 ? 148.609 131.333 112.137 1.00 19.62 ?  282 VAL A O     1 
ATOM   2259  C  CB    . VAL A 1 282 ? 148.303 129.404 114.512 1.00 12.54 ?  282 VAL A CB    1 
ATOM   2260  C  CG1   . VAL A 1 282 ? 149.800 129.434 114.737 1.00 19.43 ?  282 VAL A CG1   1 
ATOM   2261  C  CG2   . VAL A 1 282 ? 147.618 128.742 115.685 1.00 20.97 ?  282 VAL A CG2   1 
ATOM   2262  N  N     . VAL A 1 283 ? 149.353 132.591 113.856 1.00 12.30 ?  283 VAL A N     1 
ATOM   2263  C  CA    . VAL A 1 283 ? 150.253 133.409 113.057 1.00 8.37  ?  283 VAL A CA    1 
ATOM   2264  C  C     . VAL A 1 283 ? 151.644 132.803 113.158 1.00 13.12 ?  283 VAL A C     1 
ATOM   2265  O  O     . VAL A 1 283 ? 152.205 132.695 114.254 1.00 25.22 ?  283 VAL A O     1 
ATOM   2266  C  CB    . VAL A 1 283 ? 150.241 134.870 113.529 1.00 9.54  ?  283 VAL A CB    1 
ATOM   2267  C  CG1   . VAL A 1 283 ? 151.013 135.749 112.565 1.00 12.39 ?  283 VAL A CG1   1 
ATOM   2268  C  CG2   . VAL A 1 283 ? 148.812 135.351 113.673 1.00 9.73  ?  283 VAL A CG2   1 
ATOM   2269  N  N     . ILE A 1 284 ? 152.197 132.401 112.019 1.00 15.63 ?  284 ILE A N     1 
ATOM   2270  C  CA    . ILE A 1 284 ? 153.475 131.695 111.993 1.00 15.39 ?  284 ILE A CA    1 
ATOM   2271  C  C     . ILE A 1 284 ? 154.521 132.536 111.273 1.00 21.61 ?  284 ILE A C     1 
ATOM   2272  O  O     . ILE A 1 284 ? 154.460 132.683 110.045 1.00 21.50 ?  284 ILE A O     1 
ATOM   2273  C  CB    . ILE A 1 284 ? 153.334 130.315 111.335 1.00 15.46 ?  284 ILE A CB    1 
ATOM   2274  C  CG1   . ILE A 1 284 ? 152.173 129.544 111.963 1.00 12.76 ?  284 ILE A CG1   1 
ATOM   2275  C  CG2   . ILE A 1 284 ? 154.627 129.533 111.464 1.00 16.89 ?  284 ILE A CG2   1 
ATOM   2276  C  CD1   . ILE A 1 284 ? 152.008 128.145 111.427 1.00 16.53 ?  284 ILE A CD1   1 
ATOM   2277  N  N     . PRO A 1 285 ? 155.486 133.108 111.987 1.00 25.53 ?  285 PRO A N     1 
ATOM   2278  C  CA    . PRO A 1 285 ? 156.599 133.781 111.315 1.00 25.30 ?  285 PRO A CA    1 
ATOM   2279  C  C     . PRO A 1 285 ? 157.511 132.782 110.620 1.00 25.79 ?  285 PRO A C     1 
ATOM   2280  O  O     . PRO A 1 285 ? 157.513 131.585 110.914 1.00 25.01 ?  285 PRO A O     1 
ATOM   2281  C  CB    . PRO A 1 285 ? 157.329 134.496 112.458 1.00 26.35 ?  285 PRO A CB    1 
ATOM   2282  C  CG    . PRO A 1 285 ? 156.339 134.546 113.579 1.00 23.82 ?  285 PRO A CG    1 
ATOM   2283  C  CD    . PRO A 1 285 ? 155.528 133.302 113.443 1.00 19.89 ?  285 PRO A CD    1 
ATOM   2284  N  N     . ASP A 1 286 ? 158.295 133.300 109.671 1.00 31.22 ?  286 ASP A N     1 
ATOM   2285  C  CA    . ASP A 1 286 ? 159.266 132.469 108.967 1.00 25.97 ?  286 ASP A CA    1 
ATOM   2286  C  C     . ASP A 1 286 ? 160.267 131.829 109.919 1.00 34.55 ?  286 ASP A C     1 
ATOM   2287  O  O     . ASP A 1 286 ? 160.844 130.786 109.586 1.00 35.11 ?  286 ASP A O     1 
ATOM   2288  C  CB    . ASP A 1 286 ? 160.006 133.300 107.920 1.00 27.60 ?  286 ASP A CB    1 
ATOM   2289  C  CG    . ASP A 1 286 ? 159.472 133.086 106.520 1.00 38.61 ?  286 ASP A CG    1 
ATOM   2290  O  OD1   . ASP A 1 286 ? 158.240 132.957 106.365 1.00 42.79 ?  286 ASP A OD1   1 
ATOM   2291  O  OD2   . ASP A 1 286 ? 160.284 133.051 105.573 1.00 42.45 -1 286 ASP A OD2   1 
ATOM   2292  N  N     . LYS A 1 287 ? 160.485 132.431 111.090 1.00 32.80 ?  287 LYS A N     1 
ATOM   2293  C  CA    . LYS A 1 287 ? 161.404 131.857 112.067 1.00 27.94 ?  287 LYS A CA    1 
ATOM   2294  C  C     . LYS A 1 287 ? 160.937 130.483 112.528 1.00 27.59 ?  287 LYS A C     1 
ATOM   2295  O  O     . LYS A 1 287 ? 161.750 129.564 112.672 1.00 35.74 ?  287 LYS A O     1 
ATOM   2296  C  CB    . LYS A 1 287 ? 161.554 132.800 113.260 1.00 28.97 ?  287 LYS A CB    1 
ATOM   2297  C  CG    . LYS A 1 287 ? 162.669 132.410 114.215 1.00 27.77 ?  287 LYS A CG    1 
ATOM   2298  C  CD    . LYS A 1 287 ? 163.978 132.237 113.469 1.00 31.66 ?  287 LYS A CD    1 
ATOM   2299  C  CE    . LYS A 1 287 ? 165.113 131.897 114.413 1.00 32.61 ?  287 LYS A CE    1 
ATOM   2300  N  NZ    . LYS A 1 287 ? 166.427 131.904 113.717 1.00 33.85 1  287 LYS A NZ    1 
ATOM   2301  N  N     . PHE A 1 288 ? 159.636 130.324 112.778 1.00 27.34 ?  288 PHE A N     1 
ATOM   2302  C  CA    . PHE A 1 288 ? 159.125 129.030 113.221 1.00 22.62 ?  288 PHE A CA    1 
ATOM   2303  C  C     . PHE A 1 288 ? 159.298 127.965 112.146 1.00 25.80 ?  288 PHE A C     1 
ATOM   2304  O  O     . PHE A 1 288 ? 159.677 126.827 112.447 1.00 34.63 ?  288 PHE A O     1 
ATOM   2305  C  CB    . PHE A 1 288 ? 157.656 129.151 113.619 1.00 24.92 ?  288 PHE A CB    1 
ATOM   2306  C  CG    . PHE A 1 288 ? 157.093 127.903 114.231 1.00 27.45 ?  288 PHE A CG    1 
ATOM   2307  C  CD1   . PHE A 1 288 ? 157.252 127.646 115.581 1.00 23.19 ?  288 PHE A CD1   1 
ATOM   2308  C  CD2   . PHE A 1 288 ? 156.411 126.982 113.456 1.00 26.73 ?  288 PHE A CD2   1 
ATOM   2309  C  CE1   . PHE A 1 288 ? 156.740 126.499 116.145 1.00 27.14 ?  288 PHE A CE1   1 
ATOM   2310  C  CE2   . PHE A 1 288 ? 155.897 125.832 114.016 1.00 24.01 ?  288 PHE A CE2   1 
ATOM   2311  C  CZ    . PHE A 1 288 ? 156.061 125.592 115.360 1.00 27.79 ?  288 PHE A CZ    1 
ATOM   2312  N  N     . VAL A 1 289 ? 159.013 128.312 110.890 1.00 32.00 ?  289 VAL A N     1 
ATOM   2313  C  CA    . VAL A 1 289 ? 159.175 127.354 109.801 1.00 29.47 ?  289 VAL A CA    1 
ATOM   2314  C  C     . VAL A 1 289 ? 160.642 126.984 109.635 1.00 30.02 ?  289 VAL A C     1 
ATOM   2315  O  O     . VAL A 1 289 ? 160.978 125.825 109.369 1.00 35.14 ?  289 VAL A O     1 
ATOM   2316  C  CB    . VAL A 1 289 ? 158.580 127.923 108.499 1.00 30.34 ?  289 VAL A CB    1 
ATOM   2317  C  CG1   . VAL A 1 289 ? 158.771 126.946 107.352 1.00 30.45 ?  289 VAL A CG1   1 
ATOM   2318  C  CG2   . VAL A 1 289 ? 157.108 128.248 108.692 1.00 23.88 ?  289 VAL A CG2   1 
ATOM   2319  N  N     . GLU A 1 290 ? 161.539 127.961 109.791 1.00 37.54 ?  290 GLU A N     1 
ATOM   2320  C  CA    . GLU A 1 290 ? 162.966 127.672 109.720 1.00 34.55 ?  290 GLU A CA    1 
ATOM   2321  C  C     . GLU A 1 290 ? 163.402 126.751 110.856 1.00 35.20 ?  290 GLU A C     1 
ATOM   2322  O  O     . GLU A 1 290 ? 164.182 125.817 110.642 1.00 41.82 ?  290 GLU A O     1 
ATOM   2323  C  CB    . GLU A 1 290 ? 163.763 128.977 109.739 1.00 34.45 ?  290 GLU A CB    1 
ATOM   2324  C  CG    . GLU A 1 290 ? 165.108 128.887 110.437 1.00 39.30 ?  290 GLU A CG    1 
ATOM   2325  C  CD    . GLU A 1 290 ? 165.837 130.214 110.467 1.00 45.41 ?  290 GLU A CD    1 
ATOM   2326  O  OE1   . GLU A 1 290 ? 165.161 131.264 110.492 1.00 46.66 ?  290 GLU A OE1   1 
ATOM   2327  O  OE2   . GLU A 1 290 ? 167.085 130.210 110.468 1.00 43.61 -1 290 GLU A OE2   1 
ATOM   2328  N  N     . LEU A 1 291 ? 162.905 126.999 112.070 1.00 28.22 ?  291 LEU A N     1 
ATOM   2329  C  CA    . LEU A 1 291 ? 163.262 126.160 113.211 1.00 26.89 ?  291 LEU A CA    1 
ATOM   2330  C  C     . LEU A 1 291 ? 162.759 124.735 113.029 1.00 35.32 ?  291 LEU A C     1 
ATOM   2331  O  O     . LEU A 1 291 ? 163.467 123.774 113.350 1.00 38.89 ?  291 LEU A O     1 
ATOM   2332  C  CB    . LEU A 1 291 ? 162.705 126.761 114.501 1.00 31.08 ?  291 LEU A CB    1 
ATOM   2333  C  CG    . LEU A 1 291 ? 163.370 128.037 115.017 1.00 33.94 ?  291 LEU A CG    1 
ATOM   2334  C  CD1   . LEU A 1 291 ? 162.495 128.711 116.057 1.00 28.25 ?  291 LEU A CD1   1 
ATOM   2335  C  CD2   . LEU A 1 291 ? 164.743 127.735 115.580 1.00 31.72 ?  291 LEU A CD2   1 
ATOM   2336  N  N     . ALA A 1 292 ? 161.531 124.580 112.530 1.00 37.20 ?  292 ALA A N     1 
ATOM   2337  C  CA    . ALA A 1 292 ? 161.002 123.243 112.279 1.00 30.50 ?  292 ALA A CA    1 
ATOM   2338  C  C     . ALA A 1 292 ? 161.760 122.553 111.151 1.00 32.10 ?  292 ALA A C     1 
ATOM   2339  O  O     . ALA A 1 292 ? 161.970 121.336 111.190 1.00 35.83 ?  292 ALA A O     1 
ATOM   2340  C  CB    . ALA A 1 292 ? 159.511 123.321 111.958 1.00 26.04 ?  292 ALA A CB    1 
ATOM   2341  N  N     . ARG A 1 293 ? 162.175 123.315 110.137 1.00 32.95 ?  293 ARG A N     1 
ATOM   2342  C  CA    . ARG A 1 293 ? 162.913 122.740 109.018 1.00 33.13 ?  293 ARG A CA    1 
ATOM   2343  C  C     . ARG A 1 293 ? 164.250 122.168 109.469 1.00 39.16 ?  293 ARG A C     1 
ATOM   2344  O  O     . ARG A 1 293 ? 164.655 121.088 109.022 1.00 41.45 ?  293 ARG A O     1 
ATOM   2345  C  CB    . ARG A 1 293 ? 163.115 123.798 107.934 1.00 34.94 ?  293 ARG A CB    1 
ATOM   2346  C  CG    . ARG A 1 293 ? 163.994 123.363 106.779 1.00 35.23 ?  293 ARG A CG    1 
ATOM   2347  C  CD    . ARG A 1 293 ? 164.408 124.557 105.943 1.00 37.62 ?  293 ARG A CD    1 
ATOM   2348  N  NE    . ARG A 1 293 ? 163.277 125.432 105.661 1.00 42.26 ?  293 ARG A NE    1 
ATOM   2349  C  CZ    . ARG A 1 293 ? 163.287 126.747 105.831 1.00 40.70 ?  293 ARG A CZ    1 
ATOM   2350  N  NH1   . ARG A 1 293 ? 164.357 127.377 106.285 1.00 41.69 1  293 ARG A NH1   1 
ATOM   2351  N  NH2   . ARG A 1 293 ? 162.195 127.447 105.539 1.00 35.59 ?  293 ARG A NH2   1 
ATOM   2352  N  N     . GLU A 1 294 ? 164.948 122.874 110.354 1.00 44.74 ?  294 GLU A N     1 
ATOM   2353  C  CA    . GLU A 1 294 ? 166.238 122.422 110.859 1.00 43.18 ?  294 GLU A CA    1 
ATOM   2354  C  C     . GLU A 1 294 ? 166.109 121.437 112.011 1.00 44.44 ?  294 GLU A C     1 
ATOM   2355  O  O     . GLU A 1 294 ? 167.135 120.960 112.509 1.00 48.04 ?  294 GLU A O     1 
ATOM   2356  C  CB    . GLU A 1 294 ? 167.078 123.625 111.297 1.00 41.64 ?  294 GLU A CB    1 
ATOM   2357  C  CG    . GLU A 1 294 ? 167.191 124.715 110.243 1.00 43.84 ?  294 GLU A CG    1 
ATOM   2358  C  CD    . GLU A 1 294 ? 167.489 126.075 110.842 1.00 52.67 ?  294 GLU A CD    1 
ATOM   2359  O  OE1   . GLU A 1 294 ? 167.034 126.339 111.974 1.00 50.44 ?  294 GLU A OE1   1 
ATOM   2360  O  OE2   . GLU A 1 294 ? 168.175 126.880 110.179 1.00 51.67 -1 294 GLU A OE2   1 
ATOM   2361  N  N     . ASP A 1 295 ? 164.884 121.130 112.442 1.00 44.22 ?  295 ASP A N     1 
ATOM   2362  C  CA    . ASP A 1 295 ? 164.626 120.218 113.558 1.00 43.82 ?  295 ASP A CA    1 
ATOM   2363  C  C     . ASP A 1 295 ? 165.294 120.697 114.842 1.00 48.16 ?  295 ASP A C     1 
ATOM   2364  O  O     . ASP A 1 295 ? 165.642 119.896 115.712 1.00 51.21 ?  295 ASP A O     1 
ATOM   2365  C  CB    . ASP A 1 295 ? 165.065 118.789 113.227 1.00 46.89 ?  295 ASP A CB    1 
ATOM   2366  C  CG    . ASP A 1 295 ? 164.125 117.745 113.799 1.00 51.48 ?  295 ASP A CG    1 
ATOM   2367  O  OD1   . ASP A 1 295 ? 163.373 118.071 114.741 1.00 49.59 ?  295 ASP A OD1   1 
ATOM   2368  O  OD2   . ASP A 1 295 ? 164.137 116.597 113.305 1.00 50.75 -1 295 ASP A OD2   1 
ATOM   2369  N  N     . LYS A 1 296 ? 165.476 122.008 114.968 1.00 45.61 ?  296 LYS A N     1 
ATOM   2370  C  CA    . LYS A 1 296 ? 166.081 122.584 116.154 1.00 45.38 ?  296 LYS A CA    1 
ATOM   2371  C  C     . LYS A 1 296 ? 165.039 122.730 117.260 1.00 44.84 ?  296 LYS A C     1 
ATOM   2372  O  O     . LYS A 1 296 ? 163.843 122.514 117.059 1.00 45.52 ?  296 LYS A O     1 
ATOM   2373  C  CB    . LYS A 1 296 ? 166.716 123.934 115.825 1.00 45.77 ?  296 LYS A CB    1 
ATOM   2374  C  CG    . LYS A 1 296 ? 167.922 123.830 114.908 1.00 45.88 ?  296 LYS A CG    1 
ATOM   2375  C  CD    . LYS A 1 296 ? 168.548 125.188 114.653 1.00 46.45 ?  296 LYS A CD    1 
ATOM   2376  C  CE    . LYS A 1 296 ? 169.897 125.047 113.966 1.00 45.56 ?  296 LYS A CE    1 
ATOM   2377  N  NZ    . LYS A 1 296 ? 170.409 126.352 113.465 1.00 46.99 1  296 LYS A NZ    1 
ATOM   2378  N  N     . ALA A 1 297 ? 165.511 123.092 118.448 1.00 46.02 ?  297 ALA A N     1 
ATOM   2379  C  CA    . ALA A 1 297 ? 164.626 123.295 119.587 1.00 44.58 ?  297 ALA A CA    1 
ATOM   2380  C  C     . ALA A 1 297 ? 164.124 124.733 119.589 1.00 44.70 ?  297 ALA A C     1 
ATOM   2381  O  O     . ALA A 1 297 ? 164.905 125.669 119.784 1.00 46.57 ?  297 ALA A O     1 
ATOM   2382  C  CB    . ALA A 1 297 ? 165.350 122.974 120.891 1.00 44.33 ?  297 ALA A CB    1 
ATOM   2383  N  N     . ALA A 1 298 ? 162.826 124.906 119.369 1.00 38.12 ?  298 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 298 ? 162.219 126.226 119.384 1.00 36.96 ?  298 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 298 ? 161.783 126.588 120.800 1.00 35.89 ?  298 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 298 ? 161.704 125.744 121.692 1.00 36.72 ?  298 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 298 ? 161.032 126.283 118.425 1.00 36.58 ?  298 ALA A CB    1 
ATOM   2388  N  N     . TYR A 1 299 ? 161.499 127.872 120.999 1.00 35.49 ?  299 TYR A N     1 
ATOM   2389  C  CA    . TYR A 1 299 ? 161.073 128.381 122.293 1.00 28.47 ?  299 TYR A CA    1 
ATOM   2390  C  C     . TYR A 1 299 ? 159.842 129.253 122.113 1.00 31.38 ?  299 TYR A C     1 
ATOM   2391  O  O     . TYR A 1 299 ? 159.823 130.134 121.249 1.00 40.14 ?  299 TYR A O     1 
ATOM   2392  C  CB    . TYR A 1 299 ? 162.187 129.188 122.965 1.00 34.24 ?  299 TYR A CB    1 
ATOM   2393  C  CG    . TYR A 1 299 ? 163.221 128.343 123.667 1.00 37.70 ?  299 TYR A CG    1 
ATOM   2394  C  CD1   . TYR A 1 299 ? 163.026 127.917 124.970 1.00 35.43 ?  299 TYR A CD1   1 
ATOM   2395  C  CD2   . TYR A 1 299 ? 164.399 127.984 123.029 1.00 37.20 ?  299 TYR A CD2   1 
ATOM   2396  C  CE1   . TYR A 1 299 ? 163.968 127.151 125.618 1.00 35.26 ?  299 TYR A CE1   1 
ATOM   2397  C  CE2   . TYR A 1 299 ? 165.348 127.215 123.668 1.00 37.25 ?  299 TYR A CE2   1 
ATOM   2398  C  CZ    . TYR A 1 299 ? 165.127 126.802 124.963 1.00 40.47 ?  299 TYR A CZ    1 
ATOM   2399  O  OH    . TYR A 1 299 ? 166.068 126.035 125.610 1.00 45.23 ?  299 TYR A OH    1 
ATOM   2400  N  N     . VAL A 1 300 ? 158.822 129.005 122.916 1.00 31.06 ?  300 VAL A N     1 
ATOM   2401  C  CA    . VAL A 1 300 ? 157.702 129.927 123.045 1.00 24.27 ?  300 VAL A CA    1 
ATOM   2402  C  C     . VAL A 1 300 ? 157.997 130.846 124.219 1.00 29.18 ?  300 VAL A C     1 
ATOM   2403  O  O     . VAL A 1 300 ? 158.675 130.464 125.178 1.00 29.35 ?  300 VAL A O     1 
ATOM   2404  C  CB    . VAL A 1 300 ? 156.364 129.181 123.223 1.00 26.12 ?  300 VAL A CB    1 
ATOM   2405  C  CG1   . VAL A 1 300 ? 155.984 128.467 121.939 1.00 29.40 ?  300 VAL A CG1   1 
ATOM   2406  C  CG2   . VAL A 1 300 ? 156.447 128.203 124.380 1.00 29.28 ?  300 VAL A CG2   1 
ATOM   2407  N  N     . PHE A 1 301 ? 157.496 132.073 124.150 1.00 27.32 ?  301 PHE A N     1 
ATOM   2408  C  CA    . PHE A 1 301 ? 157.902 133.115 125.075 1.00 25.15 ?  301 PHE A CA    1 
ATOM   2409  C  C     . PHE A 1 301 ? 156.715 133.651 125.858 1.00 25.22 ?  301 PHE A C     1 
ATOM   2410  O  O     . PHE A 1 301 ? 155.570 133.607 125.399 1.00 31.04 ?  301 PHE A O     1 
ATOM   2411  C  CB    . PHE A 1 301 ? 158.592 134.263 124.336 1.00 27.97 ?  301 PHE A CB    1 
ATOM   2412  C  CG    . PHE A 1 301 ? 159.759 133.824 123.506 1.00 31.39 ?  301 PHE A CG    1 
ATOM   2413  C  CD1   . PHE A 1 301 ? 160.990 133.590 124.091 1.00 29.04 ?  301 PHE A CD1   1 
ATOM   2414  C  CD2   . PHE A 1 301 ? 159.624 133.637 122.143 1.00 26.23 ?  301 PHE A CD2   1 
ATOM   2415  C  CE1   . PHE A 1 301 ? 162.063 133.180 123.333 1.00 31.76 ?  301 PHE A CE1   1 
ATOM   2416  C  CE2   . PHE A 1 301 ? 160.695 133.229 121.382 1.00 28.48 ?  301 PHE A CE2   1 
ATOM   2417  C  CZ    . PHE A 1 301 ? 161.916 133.001 121.978 1.00 32.52 ?  301 PHE A CZ    1 
ATOM   2418  N  N     . TYR A 1 302 ? 157.009 134.150 127.056 1.00 26.97 ?  302 TYR A N     1 
ATOM   2419  C  CA    . TYR A 1 302 ? 156.019 134.828 127.878 1.00 27.45 ?  302 TYR A CA    1 
ATOM   2420  C  C     . TYR A 1 302 ? 155.971 136.284 127.442 1.00 30.56 ?  302 TYR A C     1 
ATOM   2421  O  O     . TYR A 1 302 ? 156.971 136.999 127.607 1.00 29.62 ?  302 TYR A O     1 
ATOM   2422  C  CB    . TYR A 1 302 ? 156.378 134.719 129.351 1.00 28.30 ?  302 TYR A CB    1 
ATOM   2423  C  CG    . TYR A 1 302 ? 156.197 133.335 129.934 1.00 26.25 ?  302 TYR A CG    1 
ATOM   2424  C  CD1   . TYR A 1 302 ? 157.056 132.300 129.596 1.00 27.65 ?  302 TYR A CD1   1 
ATOM   2425  C  CD2   . TYR A 1 302 ? 155.173 133.068 130.830 1.00 27.48 ?  302 TYR A CD2   1 
ATOM   2426  C  CE1   . TYR A 1 302 ? 156.896 131.038 130.125 1.00 30.31 ?  302 TYR A CE1   1 
ATOM   2427  C  CE2   . TYR A 1 302 ? 155.007 131.810 131.368 1.00 30.14 ?  302 TYR A CE2   1 
ATOM   2428  C  CZ    . TYR A 1 302 ? 155.871 130.799 131.013 1.00 33.71 ?  302 TYR A CZ    1 
ATOM   2429  O  OH    . TYR A 1 302 ? 155.708 129.542 131.546 1.00 37.78 ?  302 TYR A OH    1 
ATOM   2430  N  N     . PRO A 1 303 ? 154.860 136.762 126.879 1.00 29.03 ?  303 PRO A N     1 
ATOM   2431  C  CA    . PRO A 1 303 ? 154.849 138.119 126.307 1.00 24.96 ?  303 PRO A CA    1 
ATOM   2432  C  C     . PRO A 1 303 ? 155.133 139.219 127.311 1.00 27.56 ?  303 PRO A C     1 
ATOM   2433  O  O     . PRO A 1 303 ? 155.748 140.230 126.947 1.00 30.61 ?  303 PRO A O     1 
ATOM   2434  C  CB    . PRO A 1 303 ? 153.430 138.242 125.733 1.00 24.83 ?  303 PRO A CB    1 
ATOM   2435  C  CG    . PRO A 1 303 ? 152.953 136.850 125.585 1.00 24.18 ?  303 PRO A CG    1 
ATOM   2436  C  CD    . PRO A 1 303 ? 153.579 136.070 126.686 1.00 25.44 ?  303 PRO A CD    1 
ATOM   2437  N  N     . HIS A 1 304 ? 154.696 139.066 128.563 1.00 32.27 ?  304 HIS A N     1 
ATOM   2438  C  CA    . HIS A 1 304 ? 154.896 140.133 129.536 1.00 27.96 ?  304 HIS A CA    1 
ATOM   2439  C  C     . HIS A 1 304 ? 156.366 140.314 129.879 1.00 32.41 ?  304 HIS A C     1 
ATOM   2440  O  O     . HIS A 1 304 ? 156.808 141.443 130.103 1.00 40.50 ?  304 HIS A O     1 
ATOM   2441  C  CB    . HIS A 1 304 ? 154.092 139.866 130.805 1.00 29.89 ?  304 HIS A CB    1 
ATOM   2442  C  CG    . HIS A 1 304 ? 153.957 141.066 131.687 1.00 32.74 ?  304 HIS A CG    1 
ATOM   2443  N  ND1   . HIS A 1 304 ? 153.687 142.323 131.192 1.00 31.93 ?  304 HIS A ND1   1 
ATOM   2444  C  CD2   . HIS A 1 304 ? 154.065 141.205 133.029 1.00 35.88 ?  304 HIS A CD2   1 
ATOM   2445  C  CE1   . HIS A 1 304 ? 153.629 143.185 132.191 1.00 33.55 ?  304 HIS A CE1   1 
ATOM   2446  N  NE2   . HIS A 1 304 ? 153.854 142.532 133.316 1.00 34.35 ?  304 HIS A NE2   1 
ATOM   2447  N  N     . THR A 1 305 ? 157.134 139.225 129.927 1.00 25.74 ?  305 THR A N     1 
ATOM   2448  C  CA    . THR A 1 305 ? 158.567 139.351 130.166 1.00 29.41 ?  305 THR A CA    1 
ATOM   2449  C  C     . THR A 1 305 ? 159.247 140.118 129.038 1.00 28.69 ?  305 THR A C     1 
ATOM   2450  O  O     . THR A 1 305 ? 160.101 140.977 129.288 1.00 37.07 ?  305 THR A O     1 
ATOM   2451  C  CB    . THR A 1 305 ? 159.194 137.969 130.330 1.00 33.48 ?  305 THR A CB    1 
ATOM   2452  O  OG1   . THR A 1 305 ? 159.070 137.238 129.105 1.00 32.73 ?  305 THR A OG1   1 
ATOM   2453  C  CG2   . THR A 1 305 ? 158.495 137.207 131.440 1.00 30.50 ?  305 THR A CG2   1 
ATOM   2454  N  N     . ILE A 1 306 ? 158.870 139.832 127.791 1.00 32.69 ?  306 ILE A N     1 
ATOM   2455  C  CA    . ILE A 1 306 ? 159.435 140.556 126.658 1.00 28.02 ?  306 ILE A CA    1 
ATOM   2456  C  C     . ILE A 1 306 ? 159.045 142.026 126.714 1.00 29.49 ?  306 ILE A C     1 
ATOM   2457  O  O     . ILE A 1 306 ? 159.869 142.911 126.454 1.00 35.55 ?  306 ILE A O     1 
ATOM   2458  C  CB    . ILE A 1 306 ? 158.996 139.902 125.335 1.00 30.36 ?  306 ILE A CB    1 
ATOM   2459  C  CG1   . ILE A 1 306 ? 159.668 138.540 125.169 1.00 28.05 ?  306 ILE A CG1   1 
ATOM   2460  C  CG2   . ILE A 1 306 ? 159.324 140.798 124.153 1.00 30.85 ?  306 ILE A CG2   1 
ATOM   2461  C  CD1   . ILE A 1 306 ? 159.183 137.773 123.974 1.00 31.24 ?  306 ILE A CD1   1 
ATOM   2462  N  N     . TYR A 1 307 ? 157.786 142.314 127.047 1.00 33.59 ?  307 TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 307 ? 157.348 143.704 127.130 1.00 31.54 ?  307 TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 307 ? 158.078 144.451 128.239 1.00 35.23 ?  307 TYR A C     1 
ATOM   2465  O  O     . TYR A 1 307 ? 158.458 145.615 128.064 1.00 36.72 ?  307 TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 307 ? 155.836 143.767 127.342 1.00 29.33 ?  307 TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 307 ? 155.286 145.173 127.344 1.00 33.59 ?  307 TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 307 ? 154.995 145.824 126.155 1.00 29.32 ?  307 TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 307 ? 155.059 145.849 128.534 1.00 34.47 ?  307 TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 307 ? 154.495 147.109 126.150 1.00 33.46 ?  307 TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 307 ? 154.559 147.135 128.539 1.00 34.77 ?  307 TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 307 ? 154.279 147.759 127.343 1.00 35.97 ?  307 TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 307 ? 153.780 149.040 127.342 1.00 38.80 ?  307 TYR A OH    1 
ATOM   2474  N  N     . LYS A 1 308 ? 158.274 143.806 129.390 1.00 35.92 ?  308 LYS A N     1 
ATOM   2475  C  CA    . LYS A 1 308 ? 159.000 144.439 130.485 1.00 33.02 ?  308 LYS A CA    1 
ATOM   2476  C  C     . LYS A 1 308 ? 160.459 144.676 130.118 1.00 32.74 ?  308 LYS A C     1 
ATOM   2477  O  O     . LYS A 1 308 ? 161.024 145.727 130.439 1.00 39.07 ?  308 LYS A O     1 
ATOM   2478  C  CB    . LYS A 1 308 ? 158.898 143.579 131.745 1.00 34.34 ?  308 LYS A CB    1 
ATOM   2479  C  CG    . LYS A 1 308 ? 157.531 143.605 132.405 1.00 34.02 ?  308 LYS A CG    1 
ATOM   2480  C  CD    . LYS A 1 308 ? 157.543 142.863 133.729 1.00 34.74 ?  308 LYS A CD    1 
ATOM   2481  C  CE    . LYS A 1 308 ? 158.088 141.453 133.573 1.00 38.99 ?  308 LYS A CE    1 
ATOM   2482  N  NZ    . LYS A 1 308 ? 157.082 140.422 133.949 1.00 36.46 1  308 LYS A NZ    1 
ATOM   2483  N  N     . GLU A 1 309 ? 161.084 143.711 129.444 1.00 30.34 ?  309 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 309 ? 162.506 143.819 129.141 1.00 35.08 ?  309 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 309 ? 162.784 144.818 128.024 1.00 36.49 ?  309 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 309 ? 163.758 145.574 128.096 1.00 39.85 ?  309 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 309 ? 163.060 142.441 128.776 1.00 32.16 ?  309 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 309 ? 164.472 142.463 128.230 1.00 36.68 ?  309 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 309 ? 165.507 142.766 129.290 1.00 43.34 ?  309 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 309 ? 165.164 142.723 130.489 1.00 44.25 ?  309 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 309 ? 166.667 143.050 128.923 1.00 42.50 -1 309 GLU A OE2   1 
ATOM   2492  N  N     . TYR A 1 310 ? 161.942 144.845 126.992 1.00 34.65 ?  310 TYR A N     1 
ATOM   2493  C  CA    . TYR A 1 310 ? 162.218 145.621 125.792 1.00 35.73 ?  310 TYR A CA    1 
ATOM   2494  C  C     . TYR A 1 310 ? 161.306 146.822 125.608 1.00 33.98 ?  310 TYR A C     1 
ATOM   2495  O  O     . TYR A 1 310 ? 161.606 147.679 124.770 1.00 35.70 ?  310 TYR A O     1 
ATOM   2496  C  CB    . TYR A 1 310 ? 162.118 144.720 124.553 1.00 34.26 ?  310 TYR A CB    1 
ATOM   2497  C  CG    . TYR A 1 310 ? 163.161 143.629 124.516 1.00 34.23 ?  310 TYR A CG    1 
ATOM   2498  C  CD1   . TYR A 1 310 ? 164.421 143.865 123.988 1.00 33.53 ?  310 TYR A CD1   1 
ATOM   2499  C  CD2   . TYR A 1 310 ? 162.888 142.366 125.020 1.00 32.13 ?  310 TYR A CD2   1 
ATOM   2500  C  CE1   . TYR A 1 310 ? 165.377 142.872 123.956 1.00 36.62 ?  310 TYR A CE1   1 
ATOM   2501  C  CE2   . TYR A 1 310 ? 163.837 141.368 124.994 1.00 33.39 ?  310 TYR A CE2   1 
ATOM   2502  C  CZ    . TYR A 1 310 ? 165.080 141.627 124.460 1.00 36.69 ?  310 TYR A CZ    1 
ATOM   2503  O  OH    . TYR A 1 310 ? 166.029 140.635 124.431 1.00 35.81 ?  310 TYR A OH    1 
ATOM   2504  N  N     . GLY A 1 311 ? 160.210 146.914 126.354 1.00 31.00 ?  311 GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 311 ? 159.284 148.014 126.198 1.00 32.53 ?  311 GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 311 ? 158.327 147.882 125.036 1.00 35.66 ?  311 GLY A C     1 
ATOM   2507  O  O     . GLY A 1 311 ? 157.514 148.789 124.820 1.00 39.25 ?  311 GLY A O     1 
ATOM   2508  N  N     . GLN A 1 312 ? 158.396 146.789 124.282 1.00 36.16 ?  312 GLN A N     1 
ATOM   2509  C  CA    . GLN A 1 312 ? 157.509 146.546 123.157 1.00 32.63 ?  312 GLN A CA    1 
ATOM   2510  C  C     . GLN A 1 312 ? 156.884 145.167 123.301 1.00 33.64 ?  312 GLN A C     1 
ATOM   2511  O  O     . GLN A 1 312 ? 157.461 144.269 123.916 1.00 38.49 ?  312 GLN A O     1 
ATOM   2512  C  CB    . GLN A 1 312 ? 158.251 146.635 121.818 1.00 32.24 ?  312 GLN A CB    1 
ATOM   2513  C  CG    . GLN A 1 312 ? 158.924 147.967 121.558 1.00 35.80 ?  312 GLN A CG    1 
ATOM   2514  C  CD    . GLN A 1 312 ? 160.224 147.820 120.793 1.00 40.31 ?  312 GLN A CD    1 
ATOM   2515  O  OE1   . GLN A 1 312 ? 160.250 147.917 119.566 1.00 39.60 ?  312 GLN A OE1   1 
ATOM   2516  N  NE2   . GLN A 1 312 ? 161.312 147.581 121.516 1.00 37.60 ?  312 GLN A NE2   1 
ATOM   2517  N  N     . HIS A 1 313 ? 155.694 145.011 122.728 1.00 30.44 ?  313 HIS A N     1 
ATOM   2518  C  CA    . HIS A 1 313 ? 155.052 143.710 122.699 1.00 28.09 ?  313 HIS A CA    1 
ATOM   2519  C  C     . HIS A 1 313 ? 155.823 142.762 121.784 1.00 32.02 ?  313 HIS A C     1 
ATOM   2520  O  O     . HIS A 1 313 ? 156.530 143.181 120.864 1.00 32.61 ?  313 HIS A O     1 
ATOM   2521  C  CB    . HIS A 1 313 ? 153.604 143.836 122.229 1.00 25.78 ?  313 HIS A CB    1 
ATOM   2522  C  CG    . HIS A 1 313 ? 152.739 144.643 123.148 1.00 31.16 ?  313 HIS A CG    1 
ATOM   2523  N  ND1   . HIS A 1 313 ? 152.261 144.151 124.343 1.00 29.95 ?  313 HIS A ND1   1 
ATOM   2524  C  CD2   . HIS A 1 313 ? 152.265 145.906 123.045 1.00 30.97 ?  313 HIS A CD2   1 
ATOM   2525  C  CE1   . HIS A 1 313 ? 151.530 145.076 124.936 1.00 29.39 ?  313 HIS A CE1   1 
ATOM   2526  N  NE2   . HIS A 1 313 ? 151.516 146.151 124.170 1.00 31.94 ?  313 HIS A NE2   1 
ATOM   2527  N  N     . MET A 1 314 ? 155.689 141.463 122.061 1.00 35.83 ?  314 MET A N     1 
ATOM   2528  C  CA    . MET A 1 314 ? 156.410 140.469 121.274 1.00 29.72 ?  314 MET A CA    1 
ATOM   2529  C  C     . MET A 1 314 ? 155.962 140.478 119.818 1.00 35.52 ?  314 MET A C     1 
ATOM   2530  O  O     . MET A 1 314 ? 156.792 140.398 118.906 1.00 38.07 ?  314 MET A O     1 
ATOM   2531  C  CB    . MET A 1 314 ? 156.222 139.078 121.879 1.00 27.22 ?  314 MET A CB    1 
ATOM   2532  C  CG    . MET A 1 314 ? 156.869 137.971 121.067 1.00 32.36 ?  314 MET A CG    1 
ATOM   2533  S  SD    . MET A 1 314 ? 156.654 136.319 121.754 1.00 41.78 ?  314 MET A SD    1 
ATOM   2534  C  CE    . MET A 1 314 ? 155.288 136.586 122.874 1.00 30.24 ?  314 MET A CE    1 
ATOM   2535  N  N     . ASP A 1 315 ? 154.654 140.578 119.578 1.00 33.93 ?  315 ASP A N     1 
ATOM   2536  C  CA    . ASP A 1 315 ? 154.146 140.563 118.213 1.00 38.13 ?  315 ASP A CA    1 
ATOM   2537  C  C     . ASP A 1 315 ? 154.388 141.873 117.478 1.00 31.39 ?  315 ASP A C     1 
ATOM   2538  O  O     . ASP A 1 315 ? 154.210 141.920 116.257 1.00 39.47 ?  315 ASP A O     1 
ATOM   2539  C  CB    . ASP A 1 315 ? 152.651 140.234 118.204 1.00 31.26 ?  315 ASP A CB    1 
ATOM   2540  C  CG    . ASP A 1 315 ? 151.854 141.125 119.125 1.00 35.74 ?  315 ASP A CG    1 
ATOM   2541  O  OD1   . ASP A 1 315 ? 152.432 141.619 120.115 1.00 39.29 ?  315 ASP A OD1   1 
ATOM   2542  O  OD2   . ASP A 1 315 ? 150.652 141.332 118.861 1.00 32.58 -1 315 ASP A OD2   1 
ATOM   2543  N  N     . GLU A 1 316 ? 154.783 142.929 118.182 1.00 24.36 ?  316 GLU A N     1 
ATOM   2544  C  CA    . GLU A 1 316 ? 155.188 144.173 117.544 1.00 28.82 ?  316 GLU A CA    1 
ATOM   2545  C  C     . GLU A 1 316 ? 156.655 144.174 117.144 1.00 33.83 ?  316 GLU A C     1 
ATOM   2546  O  O     . GLU A 1 316 ? 157.124 145.159 116.564 1.00 32.98 ?  316 GLU A O     1 
ATOM   2547  C  CB    . GLU A 1 316 ? 154.907 145.358 118.472 1.00 31.77 ?  316 GLU A CB    1 
ATOM   2548  C  CG    . GLU A 1 316 ? 153.436 145.577 118.767 1.00 31.04 ?  316 GLU A CG    1 
ATOM   2549  C  CD    . GLU A 1 316 ? 152.766 146.473 117.747 1.00 38.93 ?  316 GLU A CD    1 
ATOM   2550  O  OE1   . GLU A 1 316 ? 151.615 146.893 117.987 1.00 41.23 ?  316 GLU A OE1   1 
ATOM   2551  O  OE2   . GLU A 1 316 ? 153.390 146.759 116.705 1.00 41.62 -1 316 GLU A OE2   1 
ATOM   2552  N  N     . MET A 1 317 ? 157.385 143.105 117.441 1.00 39.09 ?  317 MET A N     1 
ATOM   2553  C  CA    . MET A 1 317 ? 158.801 142.992 117.136 1.00 35.78 ?  317 MET A CA    1 
ATOM   2554  C  C     . MET A 1 317 ? 159.022 141.943 116.055 1.00 34.44 ?  317 MET A C     1 
ATOM   2555  O  O     . MET A 1 317 ? 158.186 141.067 115.826 1.00 36.95 ?  317 MET A O     1 
ATOM   2556  C  CB    . MET A 1 317 ? 159.603 142.627 118.391 1.00 34.12 ?  317 MET A CB    1 
ATOM   2557  C  CG    . MET A 1 317 ? 159.487 143.638 119.517 1.00 34.36 ?  317 MET A CG    1 
ATOM   2558  S  SD    . MET A 1 317 ? 160.321 143.106 121.021 1.00 44.92 ?  317 MET A SD    1 
ATOM   2559  C  CE    . MET A 1 317 ? 161.804 144.102 120.953 1.00 38.89 ?  317 MET A CE    1 
ATOM   2560  N  N     . ASP A 1 318 ? 160.169 142.047 115.390 1.00 41.30 ?  318 ASP A N     1 
ATOM   2561  C  CA    . ASP A 1 318 ? 160.535 141.106 114.338 1.00 38.66 ?  318 ASP A CA    1 
ATOM   2562  C  C     . ASP A 1 318 ? 161.116 139.856 114.980 1.00 37.96 ?  318 ASP A C     1 
ATOM   2563  O  O     . ASP A 1 318 ? 162.197 139.900 115.574 1.00 41.69 ?  318 ASP A O     1 
ATOM   2564  C  CB    . ASP A 1 318 ? 161.532 141.745 113.375 1.00 36.96 ?  318 ASP A CB    1 
ATOM   2565  C  CG    . ASP A 1 318 ? 161.681 140.961 112.088 1.00 46.58 ?  318 ASP A CG    1 
ATOM   2566  O  OD1   . ASP A 1 318 ? 160.726 140.252 111.706 1.00 43.51 ?  318 ASP A OD1   1 
ATOM   2567  O  OD2   . ASP A 1 318 ? 162.754 141.053 111.458 1.00 49.50 -1 318 ASP A OD2   1 
ATOM   2568  N  N     . MET A 1 319 ? 160.401 138.736 114.864 1.00 34.59 ?  319 MET A N     1 
ATOM   2569  C  CA    . MET A 1 319 ? 160.882 137.503 115.476 1.00 35.93 ?  319 MET A CA    1 
ATOM   2570  C  C     . MET A 1 319 ? 162.107 136.955 114.759 1.00 33.84 ?  319 MET A C     1 
ATOM   2571  O  O     . MET A 1 319 ? 162.988 136.379 115.402 1.00 37.29 ?  319 MET A O     1 
ATOM   2572  C  CB    . MET A 1 319 ? 159.769 136.457 115.506 1.00 33.86 ?  319 MET A CB    1 
ATOM   2573  C  CG    . MET A 1 319 ? 160.096 135.256 116.373 1.00 35.19 ?  319 MET A CG    1 
ATOM   2574  S  SD    . MET A 1 319 ? 160.420 135.695 118.091 1.00 43.77 ?  319 MET A SD    1 
ATOM   2575  C  CE    . MET A 1 319 ? 158.756 135.923 118.703 1.00 36.00 ?  319 MET A CE    1 
ATOM   2576  N  N     . ASN A 1 320 ? 162.193 137.138 113.441 1.00 39.08 ?  320 ASN A N     1 
ATOM   2577  C  CA    . ASN A 1 320 ? 163.348 136.646 112.700 1.00 40.11 ?  320 ASN A CA    1 
ATOM   2578  C  C     . ASN A 1 320 ? 164.635 137.364 113.084 1.00 41.59 ?  320 ASN A C     1 
ATOM   2579  O  O     . ASN A 1 320 ? 165.723 136.865 112.773 1.00 41.30 ?  320 ASN A O     1 
ATOM   2580  C  CB    . ASN A 1 320 ? 163.099 136.776 111.198 1.00 42.00 ?  320 ASN A CB    1 
ATOM   2581  C  CG    . ASN A 1 320 ? 162.126 135.737 110.682 1.00 43.63 ?  320 ASN A CG    1 
ATOM   2582  O  OD1   . ASN A 1 320 ? 160.921 135.978 110.613 1.00 38.11 ?  320 ASN A OD1   1 
ATOM   2583  N  ND2   . ASN A 1 320 ? 162.646 134.572 110.313 1.00 40.53 ?  320 ASN A ND2   1 
ATOM   2584  N  N     . GLU A 1 321 ? 164.542 138.518 113.746 1.00 42.57 ?  321 GLU A N     1 
ATOM   2585  C  CA    . GLU A 1 321 ? 165.717 139.241 114.205 1.00 41.38 ?  321 GLU A CA    1 
ATOM   2586  C  C     . GLU A 1 321 ? 165.840 139.314 115.720 1.00 43.34 ?  321 GLU A C     1 
ATOM   2587  O  O     . GLU A 1 321 ? 166.924 139.632 116.218 1.00 46.03 ?  321 GLU A O     1 
ATOM   2588  C  CB    . GLU A 1 321 ? 165.723 140.667 113.631 1.00 41.68 ?  321 GLU A CB    1 
ATOM   2589  C  CG    . GLU A 1 321 ? 165.177 141.727 114.573 1.00 44.45 ?  321 GLU A CG    1 
ATOM   2590  C  CD    . GLU A 1 321 ? 164.824 143.020 113.864 1.00 47.32 ?  321 GLU A CD    1 
ATOM   2591  O  OE1   . GLU A 1 321 ? 164.700 143.004 112.622 1.00 47.11 ?  321 GLU A OE1   1 
ATOM   2592  O  OE2   . GLU A 1 321 ? 164.668 144.051 114.552 1.00 43.73 -1 321 GLU A OE2   1 
ATOM   2593  N  N     . MET A 1 322 ? 164.773 139.017 116.463 1.00 40.61 ?  322 MET A N     1 
ATOM   2594  C  CA    . MET A 1 322 ? 164.788 139.113 117.916 1.00 38.13 ?  322 MET A CA    1 
ATOM   2595  C  C     . MET A 1 322 ? 164.604 137.777 118.620 1.00 35.74 ?  322 MET A C     1 
ATOM   2596  O  O     . MET A 1 322 ? 164.619 137.747 119.853 1.00 41.25 ?  322 MET A O     1 
ATOM   2597  C  CB    . MET A 1 322 ? 163.709 140.090 118.399 1.00 37.48 ?  322 MET A CB    1 
ATOM   2598  C  CG    . MET A 1 322 ? 163.838 141.497 117.850 1.00 38.97 ?  322 MET A CG    1 
ATOM   2599  S  SD    . MET A 1 322 ? 164.993 142.537 118.767 1.00 48.56 ?  322 MET A SD    1 
ATOM   2600  C  CE    . MET A 1 322 ? 164.782 141.914 120.429 1.00 39.49 ?  322 MET A CE    1 
ATOM   2601  N  N     . TYR A 1 323 ? 164.417 136.678 117.887 1.00 33.93 ?  323 TYR A N     1 
ATOM   2602  C  CA    . TYR A 1 323 ? 164.221 135.384 118.536 1.00 32.83 ?  323 TYR A CA    1 
ATOM   2603  C  C     . TYR A 1 323 ? 165.459 134.971 119.319 1.00 36.92 ?  323 TYR A C     1 
ATOM   2604  O  O     . TYR A 1 323 ? 165.364 134.515 120.465 1.00 39.12 ?  323 TYR A O     1 
ATOM   2605  C  CB    . TYR A 1 323 ? 163.862 134.322 117.496 1.00 33.05 ?  323 TYR A CB    1 
ATOM   2606  C  CG    . TYR A 1 323 ? 163.845 132.913 118.044 1.00 34.69 ?  323 TYR A CG    1 
ATOM   2607  C  CD1   . TYR A 1 323 ? 162.723 132.411 118.685 1.00 33.75 ?  323 TYR A CD1   1 
ATOM   2608  C  CD2   . TYR A 1 323 ? 164.951 132.082 117.919 1.00 32.20 ?  323 TYR A CD2   1 
ATOM   2609  C  CE1   . TYR A 1 323 ? 162.703 131.126 119.189 1.00 32.07 ?  323 TYR A CE1   1 
ATOM   2610  C  CE2   . TYR A 1 323 ? 164.940 130.800 118.420 1.00 32.37 ?  323 TYR A CE2   1 
ATOM   2611  C  CZ    . TYR A 1 323 ? 163.815 130.326 119.053 1.00 31.69 ?  323 TYR A CZ    1 
ATOM   2612  O  OH    . TYR A 1 323 ? 163.803 129.047 119.552 1.00 31.64 ?  323 TYR A OH    1 
ATOM   2613  N  N     . ASP A 1 324 ? 166.637 135.128 118.713 1.00 38.72 ?  324 ASP A N     1 
ATOM   2614  C  CA    . ASP A 1 324 ? 167.874 134.773 119.395 1.00 35.27 ?  324 ASP A CA    1 
ATOM   2615  C  C     . ASP A 1 324 ? 168.124 135.681 120.590 1.00 40.31 ?  324 ASP A C     1 
ATOM   2616  O  O     . ASP A 1 324 ? 168.635 135.231 121.621 1.00 47.00 ?  324 ASP A O     1 
ATOM   2617  C  CB    . ASP A 1 324 ? 169.045 134.831 118.416 1.00 41.26 ?  324 ASP A CB    1 
ATOM   2618  C  CG    . ASP A 1 324 ? 168.939 133.790 117.321 1.00 44.72 ?  324 ASP A CG    1 
ATOM   2619  O  OD1   . ASP A 1 324 ? 168.737 132.602 117.646 1.00 41.76 ?  324 ASP A OD1   1 
ATOM   2620  O  OD2   . ASP A 1 324 ? 169.055 134.161 116.134 1.00 44.08 -1 324 ASP A OD2   1 
ATOM   2621  N  N     . LYS A 1 325 ? 167.780 136.964 120.469 1.00 38.81 ?  325 LYS A N     1 
ATOM   2622  C  CA    . LYS A 1 325 ? 167.914 137.874 121.600 1.00 35.53 ?  325 LYS A CA    1 
ATOM   2623  C  C     . LYS A 1 325 ? 166.980 137.483 122.739 1.00 38.86 ?  325 LYS A C     1 
ATOM   2624  O  O     . LYS A 1 325 ? 167.364 137.543 123.911 1.00 43.73 ?  325 LYS A O     1 
ATOM   2625  C  CB    . LYS A 1 325 ? 167.650 139.310 121.148 1.00 37.33 ?  325 LYS A CB    1 
ATOM   2626  C  CG    . LYS A 1 325 ? 168.658 139.825 120.139 1.00 37.87 ?  325 LYS A CG    1 
ATOM   2627  C  CD    . LYS A 1 325 ? 168.317 141.231 119.683 1.00 41.16 ?  325 LYS A CD    1 
ATOM   2628  C  CE    . LYS A 1 325 ? 169.279 141.708 118.608 1.00 42.11 ?  325 LYS A CE    1 
ATOM   2629  N  NZ    . LYS A 1 325 ? 168.775 142.920 117.908 1.00 43.60 1  325 LYS A NZ    1 
ATOM   2630  N  N     . PHE A 1 326 ? 165.747 137.084 122.415 1.00 39.16 ?  326 PHE A N     1 
ATOM   2631  C  CA    . PHE A 1 326 ? 164.822 136.614 123.440 1.00 33.41 ?  326 PHE A CA    1 
ATOM   2632  C  C     . PHE A 1 326 ? 165.348 135.358 124.119 1.00 36.37 ?  326 PHE A C     1 
ATOM   2633  O  O     . PHE A 1 326 ? 165.248 135.213 125.343 1.00 40.55 ?  326 PHE A O     1 
ATOM   2634  C  CB    . PHE A 1 326 ? 163.447 136.337 122.830 1.00 32.69 ?  326 PHE A CB    1 
ATOM   2635  C  CG    . PHE A 1 326 ? 162.753 137.554 122.294 1.00 35.56 ?  326 PHE A CG    1 
ATOM   2636  C  CD1   . PHE A 1 326 ? 163.136 138.824 122.684 1.00 35.09 ?  326 PHE A CD1   1 
ATOM   2637  C  CD2   . PHE A 1 326 ? 161.708 137.421 121.396 1.00 34.20 ?  326 PHE A CD2   1 
ATOM   2638  C  CE1   . PHE A 1 326 ? 162.491 139.936 122.186 1.00 33.20 ?  326 PHE A CE1   1 
ATOM   2639  C  CE2   . PHE A 1 326 ? 161.061 138.531 120.896 1.00 37.15 ?  326 PHE A CE2   1 
ATOM   2640  C  CZ    . PHE A 1 326 ? 161.454 139.789 121.293 1.00 38.91 ?  326 PHE A CZ    1 
ATOM   2641  N  N     . VAL A 1 327 ? 165.899 134.429 123.334 1.00 39.05 ?  327 VAL A N     1 
ATOM   2642  C  CA    . VAL A 1 327 ? 166.413 133.185 123.901 1.00 38.24 ?  327 VAL A CA    1 
ATOM   2643  C  C     . VAL A 1 327 ? 167.612 133.461 124.799 1.00 40.04 ?  327 VAL A C     1 
ATOM   2644  O  O     . VAL A 1 327 ? 167.725 132.902 125.897 1.00 45.64 ?  327 VAL A O     1 
ATOM   2645  C  CB    . VAL A 1 327 ? 166.757 132.195 122.774 1.00 36.91 ?  327 VAL A CB    1 
ATOM   2646  C  CG1   . VAL A 1 327 ? 167.556 131.023 123.316 1.00 40.92 ?  327 VAL A CG1   1 
ATOM   2647  C  CG2   . VAL A 1 327 ? 165.489 131.706 122.101 1.00 33.27 ?  327 VAL A CG2   1 
ATOM   2648  N  N     . ASP A 1 328 ? 168.520 134.330 124.357 1.00 38.45 ?  328 ASP A N     1 
ATOM   2649  C  CA    . ASP A 1 328 ? 169.715 134.644 125.129 1.00 36.87 ?  328 ASP A CA    1 
ATOM   2650  C  C     . ASP A 1 328 ? 169.431 135.546 126.321 1.00 40.52 ?  328 ASP A C     1 
ATOM   2651  O  O     . ASP A 1 328 ? 170.255 135.610 127.239 1.00 45.52 ?  328 ASP A O     1 
ATOM   2652  C  CB    . ASP A 1 328 ? 170.763 135.304 124.230 1.00 38.98 ?  328 ASP A CB    1 
ATOM   2653  C  CG    . ASP A 1 328 ? 171.245 134.385 123.129 1.00 44.83 ?  328 ASP A CG    1 
ATOM   2654  O  OD1   . ASP A 1 328 ? 171.082 133.155 123.267 1.00 48.01 ?  328 ASP A OD1   1 
ATOM   2655  O  OD2   . ASP A 1 328 ? 171.787 134.893 122.125 1.00 44.15 -1 328 ASP A OD2   1 
ATOM   2656  N  N     . ASN A 1 329 ? 168.300 136.241 126.328 1.00 41.66 ?  329 ASN A N     1 
ATOM   2657  C  CA    . ASN A 1 329 ? 167.988 137.161 127.414 1.00 38.80 ?  329 ASN A CA    1 
ATOM   2658  C  C     . ASN A 1 329 ? 167.562 136.380 128.650 1.00 42.53 ?  329 ASN A C     1 
ATOM   2659  O  O     . ASN A 1 329 ? 166.578 135.635 128.588 1.00 42.49 ?  329 ASN A O     1 
ATOM   2660  C  CB    . ASN A 1 329 ? 166.887 138.124 126.994 1.00 33.89 ?  329 ASN A CB    1 
ATOM   2661  C  CG    . ASN A 1 329 ? 166.846 139.374 127.847 1.00 40.78 ?  329 ASN A CG    1 
ATOM   2662  O  OD1   . ASN A 1 329 ? 166.770 139.303 129.072 1.00 45.18 ?  329 ASN A OD1   1 
ATOM   2663  N  ND2   . ASN A 1 329 ? 166.905 140.531 127.200 1.00 41.09 ?  329 ASN A ND2   1 
ATOM   2664  N  N     . PRO A 1 330 ? 168.264 136.511 129.779 1.00 44.27 ?  330 PRO A N     1 
ATOM   2665  C  CA    . PRO A 1 330 ? 167.824 135.805 130.990 1.00 40.96 ?  330 PRO A CA    1 
ATOM   2666  C  C     . PRO A 1 330 ? 166.543 136.364 131.581 1.00 39.46 ?  330 PRO A C     1 
ATOM   2667  O  O     . PRO A 1 330 ? 165.785 135.612 132.206 1.00 40.15 ?  330 PRO A O     1 
ATOM   2668  C  CB    . PRO A 1 330 ? 169.011 135.979 131.947 1.00 39.08 ?  330 PRO A CB    1 
ATOM   2669  C  CG    . PRO A 1 330 ? 169.680 137.222 131.482 1.00 36.96 ?  330 PRO A CG    1 
ATOM   2670  C  CD    . PRO A 1 330 ? 169.522 137.246 129.991 1.00 38.41 ?  330 PRO A CD    1 
ATOM   2671  N  N     . ARG A 1 331 ? 166.275 137.658 131.404 1.00 38.41 ?  331 ARG A N     1 
ATOM   2672  C  CA    . ARG A 1 331 ? 165.083 138.273 131.971 1.00 40.80 ?  331 ARG A CA    1 
ATOM   2673  C  C     . ARG A 1 331 ? 163.822 137.962 131.178 1.00 41.59 ?  331 ARG A C     1 
ATOM   2674  O  O     . ARG A 1 331 ? 162.719 138.212 131.676 1.00 40.35 ?  331 ARG A O     1 
ATOM   2675  C  CB    . ARG A 1 331 ? 165.276 139.788 132.072 1.00 39.81 ?  331 ARG A CB    1 
ATOM   2676  C  CG    . ARG A 1 331 ? 166.224 140.207 133.184 1.00 40.33 ?  331 ARG A CG    1 
ATOM   2677  C  CD    . ARG A 1 331 ? 166.835 141.569 132.912 1.00 42.11 ?  331 ARG A CD    1 
ATOM   2678  N  NE    . ARG A 1 331 ? 167.461 141.636 131.597 1.00 41.88 ?  331 ARG A NE    1 
ATOM   2679  C  CZ    . ARG A 1 331 ? 168.641 141.108 131.300 1.00 43.13 ?  331 ARG A CZ    1 
ATOM   2680  N  NH1   . ARG A 1 331 ? 169.365 140.476 132.208 1.00 42.61 1  331 ARG A NH1   1 
ATOM   2681  N  NH2   . ARG A 1 331 ? 169.107 141.222 130.060 1.00 43.39 ?  331 ARG A NH2   1 
ATOM   2682  N  N     . VAL A 1 332 ? 163.955 137.434 129.969 1.00 37.30 ?  332 VAL A N     1 
ATOM   2683  C  CA    . VAL A 1 332 ? 162.819 136.949 129.198 1.00 32.98 ?  332 VAL A CA    1 
ATOM   2684  C  C     . VAL A 1 332 ? 162.549 135.510 129.612 1.00 37.43 ?  332 VAL A C     1 
ATOM   2685  O  O     . VAL A 1 332 ? 163.475 134.695 129.693 1.00 38.83 ?  332 VAL A O     1 
ATOM   2686  C  CB    . VAL A 1 332 ? 163.091 137.053 127.688 1.00 33.47 ?  332 VAL A CB    1 
ATOM   2687  C  CG1   . VAL A 1 332 ? 162.024 136.316 126.898 1.00 33.96 ?  332 VAL A CG1   1 
ATOM   2688  C  CG2   . VAL A 1 332 ? 163.163 138.508 127.261 1.00 34.85 ?  332 VAL A CG2   1 
ATOM   2689  N  N     . LYS A 1 333 ? 161.289 135.199 129.901 1.00 35.97 ?  333 LYS A N     1 
ATOM   2690  C  CA    . LYS A 1 333 ? 160.899 133.843 130.260 1.00 29.96 ?  333 LYS A CA    1 
ATOM   2691  C  C     . LYS A 1 333 ? 160.453 133.098 129.010 1.00 32.69 ?  333 LYS A C     1 
ATOM   2692  O  O     . LYS A 1 333 ? 159.623 133.597 128.244 1.00 35.64 ?  333 LYS A O     1 
ATOM   2693  C  CB    . LYS A 1 333 ? 159.782 133.855 131.303 1.00 28.38 ?  333 LYS A CB    1 
ATOM   2694  C  CG    . LYS A 1 333 ? 159.671 132.570 132.104 1.00 34.79 ?  333 LYS A CG    1 
ATOM   2695  C  CD    . LYS A 1 333 ? 158.471 132.601 133.033 1.00 35.04 ?  333 LYS A CD    1 
ATOM   2696  C  CE    . LYS A 1 333 ? 158.220 131.237 133.656 1.00 37.13 ?  333 LYS A CE    1 
ATOM   2697  N  NZ    . LYS A 1 333 ? 157.040 131.243 134.565 1.00 37.74 1  333 LYS A NZ    1 
ATOM   2698  N  N     . LYS A 1 334 ? 161.011 131.910 128.804 1.00 38.85 ?  334 LYS A N     1 
ATOM   2699  C  CA    . LYS A 1 334 ? 160.734 131.123 127.614 1.00 34.29 ?  334 LYS A CA    1 
ATOM   2700  C  C     . LYS A 1 334 ? 160.504 129.672 128.003 1.00 36.06 ?  334 LYS A C     1 
ATOM   2701  O  O     . LYS A 1 334 ? 161.002 129.200 129.027 1.00 39.70 ?  334 LYS A O     1 
ATOM   2702  C  CB    . LYS A 1 334 ? 161.880 131.220 126.598 1.00 32.87 ?  334 LYS A CB    1 
ATOM   2703  C  CG    . LYS A 1 334 ? 163.169 130.571 127.057 1.00 35.31 ?  334 LYS A CG    1 
ATOM   2704  C  CD    . LYS A 1 334 ? 164.375 131.427 126.729 1.00 35.92 ?  334 LYS A CD    1 
ATOM   2705  C  CE    . LYS A 1 334 ? 164.318 132.753 127.453 1.00 38.84 ?  334 LYS A CE    1 
ATOM   2706  N  NZ    . LYS A 1 334 ? 165.597 133.503 127.358 1.00 39.45 1  334 LYS A NZ    1 
ATOM   2707  N  N     . GLU A 1 335 ? 159.730 128.972 127.178 1.00 38.00 ?  335 GLU A N     1 
ATOM   2708  C  CA    . GLU A 1 335 ? 159.449 127.557 127.361 1.00 36.54 ?  335 GLU A CA    1 
ATOM   2709  C  C     . GLU A 1 335 ? 159.893 126.787 126.126 1.00 36.29 ?  335 GLU A C     1 
ATOM   2710  O  O     . GLU A 1 335 ? 159.639 127.209 124.994 1.00 40.84 ?  335 GLU A O     1 
ATOM   2711  C  CB    . GLU A 1 335 ? 157.961 127.311 127.623 1.00 36.06 ?  335 GLU A CB    1 
ATOM   2712  C  CG    . GLU A 1 335 ? 157.691 126.306 128.729 1.00 38.94 ?  335 GLU A CG    1 
ATOM   2713  C  CD    . GLU A 1 335 ? 156.412 126.596 129.485 1.00 44.57 ?  335 GLU A CD    1 
ATOM   2714  O  OE1   . GLU A 1 335 ? 156.331 126.233 130.678 1.00 44.53 ?  335 GLU A OE1   1 
ATOM   2715  O  OE2   . GLU A 1 335 ? 155.484 127.178 128.888 1.00 42.08 -1 335 GLU A OE2   1 
ATOM   2716  N  N     . LYS A 1 336 ? 160.557 125.657 126.351 1.00 37.35 ?  336 LYS A N     1 
ATOM   2717  C  CA    . LYS A 1 336 ? 161.073 124.845 125.259 1.00 32.44 ?  336 LYS A CA    1 
ATOM   2718  C  C     . LYS A 1 336 ? 159.947 124.047 124.615 1.00 37.58 ?  336 LYS A C     1 
ATOM   2719  O  O     . LYS A 1 336 ? 159.153 123.402 125.307 1.00 40.53 ?  336 LYS A O     1 
ATOM   2720  C  CB    . LYS A 1 336 ? 162.161 123.905 125.775 1.00 38.26 ?  336 LYS A CB    1 
ATOM   2721  C  CG    . LYS A 1 336 ? 163.073 123.341 124.702 1.00 43.11 ?  336 LYS A CG    1 
ATOM   2722  C  CD    . LYS A 1 336 ? 164.030 122.323 125.301 1.00 41.37 ?  336 LYS A CD    1 
ATOM   2723  C  CE    . LYS A 1 336 ? 165.234 122.090 124.405 1.00 41.46 ?  336 LYS A CE    1 
ATOM   2724  N  NZ    . LYS A 1 336 ? 165.068 120.882 123.552 1.00 42.28 1  336 LYS A NZ    1 
ATOM   2725  N  N     . ILE A 1 337 ? 159.878 124.096 123.285 1.00 34.86 ?  337 ILE A N     1 
ATOM   2726  C  CA    . ILE A 1 337 ? 158.904 123.337 122.516 1.00 30.93 ?  337 ILE A CA    1 
ATOM   2727  C  C     . ILE A 1 337 ? 159.616 122.690 121.337 1.00 34.73 ?  337 ILE A C     1 
ATOM   2728  O  O     . ILE A 1 337 ? 160.724 123.075 120.961 1.00 42.14 ?  337 ILE A O     1 
ATOM   2729  C  CB    . ILE A 1 337 ? 157.730 124.207 122.015 1.00 32.72 ?  337 ILE A CB    1 
ATOM   2730  C  CG1   . ILE A 1 337 ? 158.253 125.385 121.194 1.00 35.14 ?  337 ILE A CG1   1 
ATOM   2731  C  CG2   . ILE A 1 337 ? 156.883 124.691 123.179 1.00 36.24 ?  337 ILE A CG2   1 
ATOM   2732  C  CD1   . ILE A 1 337 ? 157.456 125.656 119.944 1.00 32.24 ?  337 ILE A CD1   1 
ATOM   2733  N  N     . ASN A 1 338 ? 158.957 121.690 120.753 1.00 36.42 ?  338 ASN A N     1 
ATOM   2734  C  CA    . ASN A 1 338 ? 159.446 121.076 119.529 1.00 31.75 ?  338 ASN A CA    1 
ATOM   2735  C  C     . ASN A 1 338 ? 158.663 121.647 118.359 1.00 33.43 ?  338 ASN A C     1 
ATOM   2736  O  O     . ASN A 1 338 ? 157.460 121.374 118.241 1.00 36.67 ?  338 ASN A O     1 
ATOM   2737  C  CB    . ASN A 1 338 ? 159.295 119.558 119.584 1.00 33.95 ?  338 ASN A CB    1 
ATOM   2738  C  CG    . ASN A 1 338 ? 160.021 118.860 118.453 1.00 36.09 ?  338 ASN A CG    1 
ATOM   2739  O  OD1   . ASN A 1 338 ? 159.400 118.372 117.510 1.00 38.24 ?  338 ASN A OD1   1 
ATOM   2740  N  ND2   . ASN A 1 338 ? 161.344 118.811 118.540 1.00 35.46 ?  338 ASN A ND2   1 
ATOM   2741  N  N     . PRO A 1 339 ? 159.281 122.450 117.489 1.00 35.15 ?  339 PRO A N     1 
ATOM   2742  C  CA    . PRO A 1 339 ? 158.519 123.068 116.392 1.00 29.42 ?  339 PRO A CA    1 
ATOM   2743  C  C     . PRO A 1 339 ? 157.890 122.066 115.442 1.00 32.59 ?  339 PRO A C     1 
ATOM   2744  O  O     . PRO A 1 339 ? 156.787 122.315 114.942 1.00 37.75 ?  339 PRO A O     1 
ATOM   2745  C  CB    . PRO A 1 339 ? 159.568 123.938 115.686 1.00 33.56 ?  339 PRO A CB    1 
ATOM   2746  C  CG    . PRO A 1 339 ? 160.877 123.338 116.058 1.00 36.27 ?  339 PRO A CG    1 
ATOM   2747  C  CD    . PRO A 1 339 ? 160.709 122.801 117.443 1.00 36.81 ?  339 PRO A CD    1 
ATOM   2748  N  N     . ARG A 1 340 ? 158.551 120.938 115.177 1.00 35.29 ?  340 ARG A N     1 
ATOM   2749  C  CA    . ARG A 1 340 ? 157.953 119.924 114.313 1.00 28.41 ?  340 ARG A CA    1 
ATOM   2750  C  C     . ARG A 1 340 ? 156.767 119.254 114.994 1.00 30.40 ?  340 ARG A C     1 
ATOM   2751  O  O     . ARG A 1 340 ? 155.771 118.930 114.340 1.00 37.55 ?  340 ARG A O     1 
ATOM   2752  C  CB    . ARG A 1 340 ? 158.999 118.891 113.905 1.00 28.21 ?  340 ARG A CB    1 
ATOM   2753  C  CG    . ARG A 1 340 ? 159.954 119.390 112.844 1.00 29.17 ?  340 ARG A CG    1 
ATOM   2754  C  CD    . ARG A 1 340 ? 160.611 118.245 112.103 1.00 33.78 ?  340 ARG A CD    1 
ATOM   2755  N  NE    . ARG A 1 340 ? 161.660 118.720 111.210 1.00 35.44 ?  340 ARG A NE    1 
ATOM   2756  C  CZ    . ARG A 1 340 ? 162.405 117.937 110.446 1.00 32.17 ?  340 ARG A CZ    1 
ATOM   2757  N  NH1   . ARG A 1 340 ? 162.245 116.624 110.438 1.00 30.86 1  340 ARG A NH1   1 
ATOM   2758  N  NH2   . ARG A 1 340 ? 163.335 118.483 109.667 1.00 33.45 ?  340 ARG A NH2   1 
ATOM   2759  N  N     . LYS A 1 341 ? 156.855 119.037 116.307 1.00 32.09 ?  341 LYS A N     1 
ATOM   2760  C  CA    . LYS A 1 341 ? 155.709 118.513 117.040 1.00 30.76 ?  341 LYS A CA    1 
ATOM   2761  C  C     . LYS A 1 341 ? 154.548 119.497 117.009 1.00 33.23 ?  341 LYS A C     1 
ATOM   2762  O  O     . LYS A 1 341 ? 153.387 119.095 116.883 1.00 36.39 ?  341 LYS A O     1 
ATOM   2763  C  CB    . LYS A 1 341 ? 156.105 118.194 118.480 1.00 35.55 ?  341 LYS A CB    1 
ATOM   2764  C  CG    . LYS A 1 341 ? 156.030 116.720 118.828 1.00 35.82 ?  341 LYS A CG    1 
ATOM   2765  C  CD    . LYS A 1 341 ? 156.806 115.881 117.827 1.00 38.75 ?  341 LYS A CD    1 
ATOM   2766  C  CE    . LYS A 1 341 ? 156.847 114.420 118.247 1.00 41.67 ?  341 LYS A CE    1 
ATOM   2767  N  NZ    . LYS A 1 341 ? 157.919 114.165 119.249 1.00 36.89 1  341 LYS A NZ    1 
ATOM   2768  N  N     . LEU A 1 342 ? 154.843 120.795 117.118 1.00 30.62 ?  342 LEU A N     1 
ATOM   2769  C  CA    . LEU A 1 342 ? 153.794 121.803 117.016 1.00 27.32 ?  342 LEU A CA    1 
ATOM   2770  C  C     . LEU A 1 342 ? 153.170 121.814 115.626 1.00 29.90 ?  342 LEU A C     1 
ATOM   2771  O  O     . LEU A 1 342 ? 151.953 121.970 115.487 1.00 33.99 ?  342 LEU A O     1 
ATOM   2772  C  CB    . LEU A 1 342 ? 154.355 123.180 117.369 1.00 31.11 ?  342 LEU A CB    1 
ATOM   2773  C  CG    . LEU A 1 342 ? 153.345 124.285 117.677 1.00 30.19 ?  342 LEU A CG    1 
ATOM   2774  C  CD1   . LEU A 1 342 ? 152.186 123.738 118.488 1.00 28.04 ?  342 LEU A CD1   1 
ATOM   2775  C  CD2   . LEU A 1 342 ? 154.019 125.429 118.413 1.00 26.81 ?  342 LEU A CD2   1 
ATOM   2776  N  N     . LEU A 1 343 ? 153.989 121.650 114.583 1.00 31.54 ?  343 LEU A N     1 
ATOM   2777  C  CA    . LEU A 1 343 ? 153.458 121.580 113.225 1.00 25.59 ?  343 LEU A CA    1 
ATOM   2778  C  C     . LEU A 1 343 ? 152.565 120.359 113.042 1.00 26.60 ?  343 LEU A C     1 
ATOM   2779  O  O     . LEU A 1 343 ? 151.501 120.443 112.416 1.00 37.59 ?  343 LEU A O     1 
ATOM   2780  C  CB    . LEU A 1 343 ? 154.606 121.558 112.218 1.00 30.44 ?  343 LEU A CB    1 
ATOM   2781  C  CG    . LEU A 1 343 ? 154.928 122.864 111.494 1.00 29.59 ?  343 LEU A CG    1 
ATOM   2782  C  CD1   . LEU A 1 343 ? 155.959 122.620 110.409 1.00 25.32 ?  343 LEU A CD1   1 
ATOM   2783  C  CD2   . LEU A 1 343 ? 153.669 123.482 110.914 1.00 33.56 ?  343 LEU A CD2   1 
ATOM   2784  N  N     . GLU A 1 344 ? 152.991 119.211 113.570 1.00 33.26 ?  344 GLU A N     1 
ATOM   2785  C  CA    . GLU A 1 344 ? 152.170 118.008 113.490 1.00 33.22 ?  344 GLU A CA    1 
ATOM   2786  C  C     . GLU A 1 344 ? 150.866 118.182 114.257 1.00 31.00 ?  344 GLU A C     1 
ATOM   2787  O  O     . GLU A 1 344 ? 149.813 117.707 113.819 1.00 34.27 ?  344 GLU A O     1 
ATOM   2788  C  CB    . GLU A 1 344 ? 152.951 116.804 114.016 1.00 30.91 ?  344 GLU A CB    1 
ATOM   2789  C  CG    . GLU A 1 344 ? 154.145 116.420 113.155 1.00 34.30 ?  344 GLU A CG    1 
ATOM   2790  C  CD    . GLU A 1 344 ? 155.224 115.697 113.937 1.00 41.97 ?  344 GLU A CD    1 
ATOM   2791  O  OE1   . GLU A 1 344 ? 154.948 115.268 115.077 1.00 44.43 ?  344 GLU A OE1   1 
ATOM   2792  O  OE2   . GLU A 1 344 ? 156.349 115.558 113.413 1.00 38.74 -1 344 GLU A OE2   1 
ATOM   2793  N  N     . LYS A 1 345 ? 150.918 118.851 115.410 1.00 29.36 ?  345 LYS A N     1 
ATOM   2794  C  CA    . LYS A 1 345 ? 149.698 119.132 116.159 1.00 28.66 ?  345 LYS A CA    1 
ATOM   2795  C  C     . LYS A 1 345 ? 148.770 120.048 115.374 1.00 31.02 ?  345 LYS A C     1 
ATOM   2796  O  O     . LYS A 1 345 ? 147.550 119.857 115.379 1.00 36.42 ?  345 LYS A O     1 
ATOM   2797  C  CB    . LYS A 1 345 ? 150.044 119.747 117.514 1.00 29.68 ?  345 LYS A CB    1 
ATOM   2798  C  CG    . LYS A 1 345 ? 148.834 120.184 118.318 1.00 30.37 ?  345 LYS A CG    1 
ATOM   2799  C  CD    . LYS A 1 345 ? 149.218 120.566 119.734 1.00 32.15 ?  345 LYS A CD    1 
ATOM   2800  C  CE    . LYS A 1 345 ? 147.999 120.969 120.542 1.00 36.64 ?  345 LYS A CE    1 
ATOM   2801  N  NZ    . LYS A 1 345 ? 148.340 121.234 121.966 1.00 33.99 1  345 LYS A NZ    1 
ATOM   2802  N  N     . LEU A 1 346 ? 149.331 121.054 114.700 1.00 30.76 ?  346 LEU A N     1 
ATOM   2803  C  CA    . LEU A 1 346 ? 148.525 121.918 113.843 1.00 25.94 ?  346 LEU A CA    1 
ATOM   2804  C  C     . LEU A 1 346 ? 147.843 121.112 112.747 1.00 28.41 ?  346 LEU A C     1 
ATOM   2805  O  O     . LEU A 1 346 ? 146.647 121.282 112.486 1.00 29.87 ?  346 LEU A O     1 
ATOM   2806  C  CB    . LEU A 1 346 ? 149.397 123.014 113.229 1.00 27.27 ?  346 LEU A CB    1 
ATOM   2807  C  CG    . LEU A 1 346 ? 149.973 124.102 114.134 1.00 29.07 ?  346 LEU A CG    1 
ATOM   2808  C  CD1   . LEU A 1 346 ? 150.947 124.965 113.355 1.00 29.73 ?  346 LEU A CD1   1 
ATOM   2809  C  CD2   . LEU A 1 346 ? 148.869 124.947 114.720 1.00 29.79 ?  346 LEU A CD2   1 
ATOM   2810  N  N     . ALA A 1 347 ? 148.595 120.224 112.095 1.00 30.42 ?  347 ALA A N     1 
ATOM   2811  C  CA    . ALA A 1 347 ? 148.021 119.408 111.029 1.00 26.76 ?  347 ALA A CA    1 
ATOM   2812  C  C     . ALA A 1 347 ? 146.921 118.496 111.558 1.00 32.78 ?  347 ALA A C     1 
ATOM   2813  O  O     . ALA A 1 347 ? 145.867 118.353 110.928 1.00 34.48 ?  347 ALA A O     1 
ATOM   2814  C  CB    . ALA A 1 347 ? 149.114 118.587 110.347 1.00 28.67 ?  347 ALA A CB    1 
ATOM   2815  N  N     . MET A 1 348 ? 147.149 117.872 112.715 1.00 35.83 ?  348 MET A N     1 
ATOM   2816  C  CA    . MET A 1 348 ? 146.140 116.997 113.303 1.00 34.31 ?  348 MET A CA    1 
ATOM   2817  C  C     . MET A 1 348 ? 144.883 117.772 113.676 1.00 34.62 ?  348 MET A C     1 
ATOM   2818  O  O     . MET A 1 348 ? 143.761 117.299 113.455 1.00 39.98 ?  348 MET A O     1 
ATOM   2819  C  CB    . MET A 1 348 ? 146.722 116.287 114.526 1.00 35.33 ?  348 MET A CB    1 
ATOM   2820  C  CG    . MET A 1 348 ? 145.705 115.530 115.358 1.00 42.25 ?  348 MET A CG    1 
ATOM   2821  S  SD    . MET A 1 348 ? 145.486 116.246 116.998 1.00 54.03 ?  348 MET A SD    1 
ATOM   2822  C  CE    . MET A 1 348 ? 147.162 116.178 117.622 1.00 37.83 ?  348 MET A CE    1 
ATOM   2823  N  N     . LEU A 1 349 ? 145.052 118.969 114.241 1.00 30.71 ?  349 LEU A N     1 
ATOM   2824  C  CA    . LEU A 1 349 ? 143.903 119.784 114.619 1.00 28.89 ?  349 LEU A CA    1 
ATOM   2825  C  C     . LEU A 1 349 ? 143.123 120.242 113.394 1.00 24.96 ?  349 LEU A C     1 
ATOM   2826  O  O     . LEU A 1 349 ? 141.890 120.302 113.428 1.00 29.91 ?  349 LEU A O     1 
ATOM   2827  C  CB    . LEU A 1 349 ? 144.365 120.982 115.445 1.00 31.98 ?  349 LEU A CB    1 
ATOM   2828  C  CG    . LEU A 1 349 ? 143.354 121.540 116.447 1.00 32.78 ?  349 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A 1 349 ? 143.112 120.548 117.571 1.00 35.13 ?  349 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A 1 349 ? 143.827 122.875 116.995 1.00 28.86 ?  349 LEU A CD2   1 
ATOM   2831  N  N     . ARG A 1 350 ? 143.819 120.584 112.308 1.00 27.26 ?  350 ARG A N     1 
ATOM   2832  C  CA    . ARG A 1 350 ? 143.115 120.959 111.085 1.00 26.52 ?  350 ARG A CA    1 
ATOM   2833  C  C     . ARG A 1 350 ? 142.409 119.766 110.457 1.00 31.57 ?  350 ARG A C     1 
ATOM   2834  O  O     . ARG A 1 350 ? 141.330 119.921 109.877 1.00 35.26 ?  350 ARG A O     1 
ATOM   2835  C  CB    . ARG A 1 350 ? 144.080 121.593 110.084 1.00 24.25 ?  350 ARG A CB    1 
ATOM   2836  C  CG    . ARG A 1 350 ? 144.794 122.827 110.600 1.00 27.97 ?  350 ARG A CG    1 
ATOM   2837  C  CD    . ARG A 1 350 ? 145.495 123.569 109.482 1.00 29.70 ?  350 ARG A CD    1 
ATOM   2838  N  NE    . ARG A 1 350 ? 144.646 124.620 108.935 1.00 36.09 ?  350 ARG A NE    1 
ATOM   2839  C  CZ    . ARG A 1 350 ? 144.518 124.888 107.644 1.00 34.03 ?  350 ARG A CZ    1 
ATOM   2840  N  NH1   . ARG A 1 350 ? 145.174 124.198 106.727 1.00 30.09 1  350 ARG A NH1   1 
ATOM   2841  N  NH2   . ARG A 1 350 ? 143.705 125.869 107.264 1.00 30.10 ?  350 ARG A NH2   1 
ATOM   2842  N  N     . SER A 1 351 ? 143.004 118.575 110.551 1.00 35.31 ?  351 SER A N     1 
ATOM   2843  C  CA    . SER A 1 351 ? 142.343 117.378 110.046 1.00 32.15 ?  351 SER A CA    1 
ATOM   2844  C  C     . SER A 1 351 ? 141.080 117.066 110.838 1.00 37.40 ?  351 SER A C     1 
ATOM   2845  O  O     . SER A 1 351 ? 140.050 116.703 110.260 1.00 43.54 ?  351 SER A O     1 
ATOM   2846  C  CB    . SER A 1 351 ? 143.305 116.192 110.087 1.00 34.90 ?  351 SER A CB    1 
ATOM   2847  O  OG    . SER A 1 351 ? 144.361 116.360 109.160 1.00 45.11 ?  351 SER A OG    1 
ATOM   2848  N  N     . GLU A 1 352 ? 141.139 117.199 112.162 1.00 34.86 ?  352 GLU A N     1 
ATOM   2849  C  CA    . GLU A 1 352 ? 140.019 116.801 113.005 1.00 32.54 ?  352 GLU A CA    1 
ATOM   2850  C  C     . GLU A 1 352 ? 138.952 117.879 113.155 1.00 37.94 ?  352 GLU A C     1 
ATOM   2851  O  O     . GLU A 1 352 ? 137.799 117.546 113.451 1.00 46.70 ?  352 GLU A O     1 
ATOM   2852  C  CB    . GLU A 1 352 ? 140.527 116.384 114.391 1.00 38.24 ?  352 GLU A CB    1 
ATOM   2853  C  CG    . GLU A 1 352 ? 140.594 117.506 115.411 1.00 41.92 ?  352 GLU A CG    1 
ATOM   2854  C  CD    . GLU A 1 352 ? 141.144 117.047 116.746 1.00 45.83 ?  352 GLU A CD    1 
ATOM   2855  O  OE1   . GLU A 1 352 ? 142.186 116.360 116.756 1.00 43.39 ?  352 GLU A OE1   1 
ATOM   2856  O  OE2   . GLU A 1 352 ? 140.534 117.371 117.786 1.00 46.21 -1 352 GLU A OE2   1 
ATOM   2857  N  N     . SER A 1 353 ? 139.293 119.154 112.962 1.00 35.27 ?  353 SER A N     1 
ATOM   2858  C  CA    . SER A 1 353 ? 138.325 120.227 113.150 1.00 36.63 ?  353 SER A CA    1 
ATOM   2859  C  C     . SER A 1 353 ? 138.370 121.319 112.092 1.00 32.80 ?  353 SER A C     1 
ATOM   2860  O  O     . SER A 1 353 ? 137.433 122.122 112.040 1.00 32.09 ?  353 SER A O     1 
ATOM   2861  C  CB    . SER A 1 353 ? 138.515 120.875 114.529 1.00 35.94 ?  353 SER A CB    1 
ATOM   2862  O  OG    . SER A 1 353 ? 139.791 121.478 114.636 1.00 33.36 ?  353 SER A OG    1 
ATOM   2863  N  N     . GLY A 1 354 ? 139.405 121.390 111.258 1.00 25.10 ?  354 GLY A N     1 
ATOM   2864  C  CA    . GLY A 1 354 ? 139.558 122.476 110.317 1.00 27.40 ?  354 GLY A CA    1 
ATOM   2865  C  C     . GLY A 1 354 ? 140.278 123.689 110.862 1.00 23.52 ?  354 GLY A C     1 
ATOM   2866  O  O     . GLY A 1 354 ? 140.577 124.610 110.093 1.00 29.14 ?  354 GLY A O     1 
ATOM   2867  N  N     . TYR A 1 355 ? 140.575 123.715 112.158 1.00 22.42 ?  355 TYR A N     1 
ATOM   2868  C  CA    . TYR A 1 355 ? 141.244 124.795 112.857 1.00 16.59 ?  355 TYR A CA    1 
ATOM   2869  C  C     . TYR A 1 355 ? 142.658 124.378 113.245 1.00 22.01 ?  355 TYR A C     1 
ATOM   2870  O  O     . TYR A 1 355 ? 142.932 123.188 113.409 1.00 27.95 ?  355 TYR A O     1 
ATOM   2871  C  CB    . TYR A 1 355 ? 140.467 125.194 114.116 1.00 23.87 ?  355 TYR A CB    1 
ATOM   2872  C  CG    . TYR A 1 355 ? 139.125 125.820 113.829 1.00 28.43 ?  355 TYR A CG    1 
ATOM   2873  C  CD1   . TYR A 1 355 ? 139.019 126.930 113.004 1.00 21.92 ?  355 TYR A CD1   1 
ATOM   2874  C  CD2   . TYR A 1 355 ? 137.963 125.299 114.380 1.00 30.32 ?  355 TYR A CD2   1 
ATOM   2875  C  CE1   . TYR A 1 355 ? 137.796 127.502 112.737 1.00 28.77 ?  355 TYR A CE1   1 
ATOM   2876  C  CE2   . TYR A 1 355 ? 136.735 125.867 114.118 1.00 26.19 ?  355 TYR A CE2   1 
ATOM   2877  C  CZ    . TYR A 1 355 ? 136.656 126.969 113.297 1.00 29.94 ?  355 TYR A CZ    1 
ATOM   2878  O  OH    . TYR A 1 355 ? 135.433 127.536 113.034 1.00 31.97 ?  355 TYR A OH    1 
ATOM   2879  N  N     . PRO A 1 356 ? 143.585 125.328 113.408 1.00 30.72 ?  356 PRO A N     1 
ATOM   2880  C  CA    . PRO A 1 356 ? 143.443 126.782 113.291 1.00 15.39 ?  356 PRO A CA    1 
ATOM   2881  C  C     . PRO A 1 356 ? 143.595 127.304 111.871 1.00 15.29 ?  356 PRO A C     1 
ATOM   2882  O  O     . PRO A 1 356 ? 144.060 126.599 110.982 1.00 24.86 ?  356 PRO A O     1 
ATOM   2883  C  CB    . PRO A 1 356 ? 144.574 127.292 114.185 1.00 17.74 ?  356 PRO A CB    1 
ATOM   2884  C  CG    . PRO A 1 356 ? 145.658 126.287 113.961 1.00 22.45 ?  356 PRO A CG    1 
ATOM   2885  C  CD    . PRO A 1 356 ? 144.955 124.957 113.804 1.00 19.53 ?  356 PRO A CD    1 
ATOM   2886  N  N     . TYR A 1 357 ? 143.185 128.546 111.634 1.00 24.77 ?  357 TYR A N     1 
ATOM   2887  C  CA    . TYR A 1 357 ? 143.625 129.253 110.443 1.00 12.22 ?  357 TYR A CA    1 
ATOM   2888  C  C     . TYR A 1 357 ? 145.127 129.475 110.532 1.00 13.71 ?  357 TYR A C     1 
ATOM   2889  O  O     . TYR A 1 357 ? 145.666 129.728 111.611 1.00 26.45 ?  357 TYR A O     1 
ATOM   2890  C  CB    . TYR A 1 357 ? 142.907 130.597 110.312 1.00 13.47 ?  357 TYR A CB    1 
ATOM   2891  C  CG    . TYR A 1 357 ? 141.402 130.539 110.439 1.00 15.80 ?  357 TYR A CG    1 
ATOM   2892  C  CD1   . TYR A 1 357 ? 140.694 129.419 110.041 1.00 17.54 ?  357 TYR A CD1   1 
ATOM   2893  C  CD2   . TYR A 1 357 ? 140.690 131.613 110.950 1.00 18.09 ?  357 TYR A CD2   1 
ATOM   2894  C  CE1   . TYR A 1 357 ? 139.321 129.364 110.148 1.00 20.23 ?  357 TYR A CE1   1 
ATOM   2895  C  CE2   . TYR A 1 357 ? 139.319 131.568 111.064 1.00 15.86 ?  357 TYR A CE2   1 
ATOM   2896  C  CZ    . TYR A 1 357 ? 138.638 130.441 110.660 1.00 19.73 ?  357 TYR A CZ    1 
ATOM   2897  O  OH    . TYR A 1 357 ? 137.269 130.390 110.769 1.00 28.22 ?  357 TYR A OH    1 
ATOM   2898  N  N     . ILE A 1 358 ? 145.810 129.372 109.400 1.00 16.22 ?  358 ILE A N     1 
ATOM   2899  C  CA    . ILE A 1 358 ? 147.258 129.526 109.350 1.00 22.30 ?  358 ILE A CA    1 
ATOM   2900  C  C     . ILE A 1 358 ? 147.571 130.818 108.613 1.00 18.25 ?  358 ILE A C     1 
ATOM   2901  O  O     . ILE A 1 358 ? 147.192 130.981 107.448 1.00 20.96 ?  358 ILE A O     1 
ATOM   2902  C  CB    . ILE A 1 358 ? 147.941 128.328 108.675 1.00 22.40 ?  358 ILE A CB    1 
ATOM   2903  C  CG1   . ILE A 1 358 ? 147.567 127.022 109.379 1.00 19.24 ?  358 ILE A CG1   1 
ATOM   2904  C  CG2   . ILE A 1 358 ? 149.448 128.517 108.660 1.00 16.40 ?  358 ILE A CG2   1 
ATOM   2905  C  CD1   . ILE A 1 358 ? 147.774 127.048 110.870 1.00 19.28 ?  358 ILE A CD1   1 
ATOM   2906  N  N     . MET A 1 359 ? 148.259 131.732 109.289 1.00 15.72 ?  359 MET A N     1 
ATOM   2907  C  CA    . MET A 1 359 ? 148.762 132.953 108.677 1.00 9.17  ?  359 MET A CA    1 
ATOM   2908  C  C     . MET A 1 359 ? 150.280 132.891 108.653 1.00 11.86 ?  359 MET A C     1 
ATOM   2909  O  O     . MET A 1 359 ? 150.916 132.779 109.705 1.00 21.73 ?  359 MET A O     1 
ATOM   2910  C  CB    . MET A 1 359 ? 148.290 134.194 109.433 1.00 11.58 ?  359 MET A CB    1 
ATOM   2911  C  CG    . MET A 1 359 ? 148.636 135.489 108.723 1.00 12.28 ?  359 MET A CG    1 
ATOM   2912  S  SD    . MET A 1 359 ? 148.285 136.959 109.694 1.00 30.94 ?  359 MET A SD    1 
ATOM   2913  C  CE    . MET A 1 359 ? 149.866 137.790 109.633 1.00 9.99  ?  359 MET A CE    1 
ATOM   2914  N  N     . PHE A 1 360 ? 150.855 132.967 107.459 1.00 12.36 ?  360 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 360 ? 152.305 133.008 107.298 1.00 10.56 ?  360 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 360 ? 152.721 134.471 107.356 1.00 14.38 ?  360 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 360 ? 152.631 135.194 106.363 1.00 20.45 ?  360 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 360 ? 152.718 132.333 105.998 1.00 14.32 ?  360 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 360 ? 152.386 130.870 105.956 1.00 19.70 ?  360 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 360 ? 152.901 130.003 106.904 1.00 19.15 ?  360 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 360 ? 151.542 130.366 104.984 1.00 14.52 ?  360 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 360 ? 152.591 128.661 106.874 1.00 19.62 ?  360 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 360 ? 151.228 129.026 104.950 1.00 15.20 ?  360 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 360 ? 151.753 128.172 105.895 1.00 17.18 ?  360 PHE A CZ    1 
ATOM   2925  N  N     . GLN A 1 361 ? 153.184 134.899 108.533 1.00 17.83 ?  361 GLN A N     1 
ATOM   2926  C  CA    . GLN A 1 361 ? 153.340 136.323 108.814 1.00 10.93 ?  361 GLN A CA    1 
ATOM   2927  C  C     . GLN A 1 361 ? 154.357 136.977 107.887 1.00 17.63 ?  361 GLN A C     1 
ATOM   2928  O  O     . GLN A 1 361 ? 154.138 138.094 107.407 1.00 22.44 ?  361 GLN A O     1 
ATOM   2929  C  CB    . GLN A 1 361 ? 153.737 136.513 110.276 1.00 19.39 ?  361 GLN A CB    1 
ATOM   2930  C  CG    . GLN A 1 361 ? 154.338 137.864 110.603 1.00 22.88 ?  361 GLN A CG    1 
ATOM   2931  C  CD    . GLN A 1 361 ? 153.708 138.487 111.830 1.00 22.79 ?  361 GLN A CD    1 
ATOM   2932  O  OE1   . GLN A 1 361 ? 153.607 137.852 112.877 1.00 24.42 ?  361 GLN A OE1   1 
ATOM   2933  N  NE2   . GLN A 1 361 ? 153.275 139.734 111.703 1.00 23.32 ?  361 GLN A NE2   1 
ATOM   2934  N  N     . ASP A 1 362 ? 155.476 136.302 107.624 1.00 25.25 ?  362 ASP A N     1 
ATOM   2935  C  CA    . ASP A 1 362 ? 156.481 136.877 106.739 1.00 18.40 ?  362 ASP A CA    1 
ATOM   2936  C  C     . ASP A 1 362 ? 156.060 136.836 105.278 1.00 17.69 ?  362 ASP A C     1 
ATOM   2937  O  O     . ASP A 1 362 ? 156.578 137.620 104.477 1.00 28.33 ?  362 ASP A O     1 
ATOM   2938  C  CB    . ASP A 1 362 ? 157.818 136.164 106.921 1.00 24.85 ?  362 ASP A CB    1 
ATOM   2939  C  CG    . ASP A 1 362 ? 158.405 136.380 108.300 1.00 31.03 ?  362 ASP A CG    1 
ATOM   2940  O  OD1   . ASP A 1 362 ? 157.760 135.988 109.293 1.00 29.17 ?  362 ASP A OD1   1 
ATOM   2941  O  OD2   . ASP A 1 362 ? 159.510 136.953 108.388 1.00 33.69 -1 362 ASP A OD2   1 
ATOM   2942  N  N     . ASN A 1 363 ? 155.144 135.938 104.911 1.00 24.62 ?  363 ASN A N     1 
ATOM   2943  C  CA    . ASN A 1 363 ? 154.576 135.978 103.568 1.00 14.12 ?  363 ASN A CA    1 
ATOM   2944  C  C     . ASN A 1 363 ? 153.672 137.188 103.398 1.00 18.06 ?  363 ASN A C     1 
ATOM   2945  O  O     . ASN A 1 363 ? 153.612 137.784 102.317 1.00 28.52 ?  363 ASN A O     1 
ATOM   2946  C  CB    . ASN A 1 363 ? 153.806 134.689 103.284 1.00 12.26 ?  363 ASN A CB    1 
ATOM   2947  C  CG    . ASN A 1 363 ? 154.701 133.569 102.807 1.00 18.23 ?  363 ASN A CG    1 
ATOM   2948  O  OD1   . ASN A 1 363 ? 155.843 133.795 102.416 1.00 21.41 ?  363 ASN A OD1   1 
ATOM   2949  N  ND2   . ASN A 1 363 ? 154.184 132.347 102.837 1.00 20.23 ?  363 ASN A ND2   1 
ATOM   2950  N  N     . VAL A 1 364 ? 152.954 137.560 104.457 1.00 14.61 ?  364 VAL A N     1 
ATOM   2951  C  CA    . VAL A 1 364 ? 152.097 138.738 104.406 1.00 9.24  ?  364 VAL A CA    1 
ATOM   2952  C  C     . VAL A 1 364 ? 152.930 140.012 104.377 1.00 16.15 ?  364 VAL A C     1 
ATOM   2953  O  O     . VAL A 1 364 ? 152.636 140.944 103.621 1.00 19.34 ?  364 VAL A O     1 
ATOM   2954  C  CB    . VAL A 1 364 ? 151.121 138.732 105.595 1.00 1.23  ?  364 VAL A CB    1 
ATOM   2955  C  CG1   . VAL A 1 364 ? 150.150 139.887 105.483 1.00 9.60  ?  364 VAL A CG1   1 
ATOM   2956  C  CG2   . VAL A 1 364 ? 150.386 137.411 105.669 1.00 6.84  ?  364 VAL A CG2   1 
ATOM   2957  N  N     . ASN A 1 365 ? 153.983 140.071 105.191 1.00 22.21 ?  365 ASN A N     1 
ATOM   2958  C  CA    . ASN A 1 365 ? 154.671 141.327 105.450 1.00 11.29 ?  365 ASN A CA    1 
ATOM   2959  C  C     . ASN A 1 365 ? 155.827 141.606 104.502 1.00 14.01 ?  365 ASN A C     1 
ATOM   2960  O  O     . ASN A 1 365 ? 156.287 142.751 104.440 1.00 23.15 ?  365 ASN A O     1 
ATOM   2961  C  CB    . ASN A 1 365 ? 155.184 141.354 106.891 1.00 17.60 ?  365 ASN A CB    1 
ATOM   2962  C  CG    . ASN A 1 365 ? 154.090 141.670 107.885 1.00 16.59 ?  365 ASN A CG    1 
ATOM   2963  O  OD1   . ASN A 1 365 ? 153.390 142.672 107.751 1.00 22.15 ?  365 ASN A OD1   1 
ATOM   2964  N  ND2   . ASN A 1 365 ? 153.932 140.817 108.884 1.00 15.77 ?  365 ASN A ND2   1 
ATOM   2965  N  N     . LYS A 1 366 ? 156.311 140.605 103.766 1.00 19.65 ?  366 LYS A N     1 
ATOM   2966  C  CA    . LYS A 1 366 ? 157.349 140.874 102.780 1.00 22.10 ?  366 LYS A CA    1 
ATOM   2967  C  C     . LYS A 1 366 ? 156.804 141.619 101.571 1.00 24.85 ?  366 LYS A C     1 
ATOM   2968  O  O     . LYS A 1 366 ? 157.572 142.272 100.858 1.00 30.20 ?  366 LYS A O     1 
ATOM   2969  C  CB    . LYS A 1 366 ? 158.019 139.570 102.342 1.00 18.14 ?  366 LYS A CB    1 
ATOM   2970  C  CG    . LYS A 1 366 ? 157.150 138.668 101.487 1.00 27.92 ?  366 LYS A CG    1 
ATOM   2971  C  CD    . LYS A 1 366 ? 157.999 137.720 100.657 1.00 29.61 ?  366 LYS A CD    1 
ATOM   2972  C  CE    . LYS A 1 366 ? 158.496 136.549 101.488 1.00 24.39 ?  366 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A 1 366 ? 159.695 135.911 100.879 1.00 31.12 1  366 LYS A NZ    1 
ATOM   2974  N  N     . VAL A 1 367 ? 155.495 141.539 101.334 1.00 24.91 ?  367 VAL A N     1 
ATOM   2975  C  CA    . VAL A 1 367 ? 154.829 142.278 100.271 1.00 13.81 ?  367 VAL A CA    1 
ATOM   2976  C  C     . VAL A 1 367 ? 153.861 143.317 100.810 1.00 21.55 ?  367 VAL A C     1 
ATOM   2977  O  O     . VAL A 1 367 ? 153.205 144.002 100.020 1.00 26.26 ?  367 VAL A O     1 
ATOM   2978  C  CB    . VAL A 1 367 ? 154.104 141.325 99.300  1.00 16.64 ?  367 VAL A CB    1 
ATOM   2979  C  CG1   . VAL A 1 367 ? 155.097 140.677 98.357  1.00 22.54 ?  367 VAL A CG1   1 
ATOM   2980  C  CG2   . VAL A 1 367 ? 153.347 140.269 100.075 1.00 13.91 ?  367 VAL A CG2   1 
ATOM   2981  N  N     . HIS A 1 368 ? 153.748 143.449 102.129 1.00 21.75 ?  368 HIS A N     1 
ATOM   2982  C  CA    . HIS A 1 368 ? 152.834 144.412 102.727 1.00 9.89  ?  368 HIS A CA    1 
ATOM   2983  C  C     . HIS A 1 368 ? 153.266 145.833 102.388 1.00 14.33 ?  368 HIS A C     1 
ATOM   2984  O  O     . HIS A 1 368 ? 154.440 146.188 102.529 1.00 24.79 ?  368 HIS A O     1 
ATOM   2985  C  CB    . HIS A 1 368 ? 152.787 144.213 104.238 1.00 8.77  ?  368 HIS A CB    1 
ATOM   2986  C  CG    . HIS A 1 368 ? 151.829 145.121 104.942 1.00 10.72 ?  368 HIS A CG    1 
ATOM   2987  N  ND1   . HIS A 1 368 ? 152.027 145.547 106.237 1.00 18.69 ?  368 HIS A ND1   1 
ATOM   2988  C  CD2   . HIS A 1 368 ? 150.666 145.680 104.535 1.00 6.90  ?  368 HIS A CD2   1 
ATOM   2989  C  CE1   . HIS A 1 368 ? 151.027 146.329 106.598 1.00 16.05 ?  368 HIS A CE1   1 
ATOM   2990  N  NE2   . HIS A 1 368 ? 150.188 146.427 105.583 1.00 10.79 ?  368 HIS A NE2   1 
ATOM   2991  N  N     . ALA A 1 369 ? 152.310 146.646 101.942 1.00 18.19 ?  369 ALA A N     1 
ATOM   2992  C  CA    . ALA A 1 369 ? 152.616 147.985 101.460 1.00 9.05  ?  369 ALA A CA    1 
ATOM   2993  C  C     . ALA A 1 369 ? 152.666 149.029 102.567 1.00 20.16 ?  369 ALA A C     1 
ATOM   2994  O  O     . ALA A 1 369 ? 153.167 150.133 102.331 1.00 24.96 ?  369 ALA A O     1 
ATOM   2995  C  CB    . ALA A 1 369 ? 151.588 148.407 100.412 1.00 14.58 ?  369 ALA A CB    1 
ATOM   2996  N  N     . ASN A 1 370 ? 152.173 148.714 103.760 1.00 19.06 ?  370 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 370 ? 152.047 149.686 104.840 1.00 9.80  ?  370 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 370 ? 152.718 149.176 106.103 1.00 8.58  ?  370 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 370 ? 152.168 149.247 107.202 1.00 18.09 ?  370 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 370 ? 150.581 150.014 105.105 1.00 10.11 ?  370 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 370 ? 149.883 150.575 103.888 1.00 12.97 ?  370 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 370 ? 150.304 151.585 103.329 1.00 28.26 ?  370 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 370 ? 148.809 149.921 103.468 1.00 13.93 ?  370 ASN A ND2   1 
ATOM   3004  N  N     . ASN A 1 371 ? 153.934 148.647 105.961 1.00 17.89 ?  371 ASN A N     1 
ATOM   3005  C  CA    . ASN A 1 371 ? 154.685 148.207 107.131 1.00 11.60 ?  371 ASN A CA    1 
ATOM   3006  C  C     . ASN A 1 371 ? 155.141 149.375 107.993 1.00 19.41 ?  371 ASN A C     1 
ATOM   3007  O  O     . ASN A 1 371 ? 155.430 149.177 109.177 1.00 22.71 ?  371 ASN A O     1 
ATOM   3008  C  CB    . ASN A 1 371 ? 155.894 147.377 106.705 1.00 6.17  ?  371 ASN A CB    1 
ATOM   3009  C  CG    . ASN A 1 371 ? 155.548 145.927 106.456 1.00 15.84 ?  371 ASN A CG    1 
ATOM   3010  O  OD1   . ASN A 1 371 ? 154.562 145.414 106.980 1.00 23.36 ?  371 ASN A OD1   1 
ATOM   3011  N  ND2   . ASN A 1 371 ? 156.359 145.257 105.650 1.00 18.12 ?  371 ASN A ND2   1 
ATOM   3012  N  N     . HIS A 1 372 ? 155.219 150.579 107.423 1.00 20.00 ?  372 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 372 ? 155.554 151.757 108.216 1.00 17.08 ?  372 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 372 ? 154.486 152.034 109.266 1.00 20.55 ?  372 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 372 ? 154.805 152.394 110.405 1.00 30.06 ?  372 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 372 ? 155.739 152.967 107.301 1.00 18.82 ?  372 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 372 ? 154.476 153.423 106.643 1.00 19.92 ?  372 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 372 ? 153.760 152.627 105.776 1.00 19.60 ?  372 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 372 ? 153.792 154.588 106.735 1.00 23.20 ?  372 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 372 ? 152.694 153.282 105.358 1.00 18.35 ?  372 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 372 ? 152.690 154.475 105.924 1.00 23.99 ?  372 HIS A NE2   1 
ATOM   3022  N  N     . ILE A 1 373 ? 153.212 151.886 108.900 1.00 14.86 ?  373 ILE A N     1 
ATOM   3023  C  CA    . ILE A 1 373 ? 152.140 152.022 109.878 1.00 16.32 ?  373 ILE A CA    1 
ATOM   3024  C  C     . ILE A 1 373 ? 152.235 150.915 110.918 1.00 19.30 ?  373 ILE A C     1 
ATOM   3025  O  O     . ILE A 1 373 ? 152.249 151.173 112.126 1.00 29.97 ?  373 ILE A O     1 
ATOM   3026  C  CB    . ILE A 1 373 ? 150.770 152.018 109.174 1.00 17.88 ?  373 ILE A CB    1 
ATOM   3027  C  CG1   . ILE A 1 373 ? 150.668 153.183 108.190 1.00 16.77 ?  373 ILE A CG1   1 
ATOM   3028  C  CG2   . ILE A 1 373 ? 149.643 152.076 110.193 1.00 17.56 ?  373 ILE A CG2   1 
ATOM   3029  C  CD1   . ILE A 1 373 ? 149.494 153.082 107.247 1.00 13.85 ?  373 ILE A CD1   1 
ATOM   3030  N  N     . SER A 1 374 ? 152.327 149.671 110.458 1.00 20.52 ?  374 SER A N     1 
ATOM   3031  C  CA    . SER A 1 374 ? 152.416 148.493 111.309 1.00 12.72 ?  374 SER A CA    1 
ATOM   3032  C  C     . SER A 1 374 ? 152.574 147.276 110.412 1.00 15.89 ?  374 SER A C     1 
ATOM   3033  O  O     . SER A 1 374 ? 152.247 147.315 109.223 1.00 16.80 ?  374 SER A O     1 
ATOM   3034  C  CB    . SER A 1 374 ? 151.182 148.332 112.197 1.00 17.29 ?  374 SER A CB    1 
ATOM   3035  O  OG    . SER A 1 374 ? 151.351 147.269 113.113 1.00 25.82 ?  374 SER A OG    1 
ATOM   3036  N  N     . LYS A 1 375 ? 153.080 146.198 110.994 1.00 22.63 ?  375 LYS A N     1 
ATOM   3037  C  CA    . LYS A 1 375 ? 153.068 144.912 110.318 1.00 15.46 ?  375 LYS A CA    1 
ATOM   3038  C  C     . LYS A 1 375 ? 151.725 144.229 110.531 1.00 14.23 ?  375 LYS A C     1 
ATOM   3039  O  O     . LYS A 1 375 ? 151.037 144.460 111.528 1.00 25.63 ?  375 LYS A O     1 
ATOM   3040  C  CB    . LYS A 1 375 ? 154.193 144.017 110.833 1.00 11.70 ?  375 LYS A CB    1 
ATOM   3041  C  CG    . LYS A 1 375 ? 155.563 144.654 110.784 1.00 19.34 ?  375 LYS A CG    1 
ATOM   3042  C  CD    . LYS A 1 375 ? 156.455 143.941 109.790 1.00 19.61 ?  375 LYS A CD    1 
ATOM   3043  C  CE    . LYS A 1 375 ? 157.752 144.691 109.566 1.00 20.30 ?  375 LYS A CE    1 
ATOM   3044  N  NZ    . LYS A 1 375 ? 158.488 144.164 108.386 1.00 25.16 1  375 LYS A NZ    1 
ATOM   3045  N  N     . VAL A 1 376 ? 151.348 143.385 109.574 1.00 11.48 ?  376 VAL A N     1 
ATOM   3046  C  CA    . VAL A 1 376 ? 150.135 142.595 109.732 1.00 17.46 ?  376 VAL A CA    1 
ATOM   3047  C  C     . VAL A 1 376 ? 150.408 141.500 110.752 1.00 14.05 ?  376 VAL A C     1 
ATOM   3048  O  O     . VAL A 1 376 ? 151.321 140.684 110.581 1.00 20.12 ?  376 VAL A O     1 
ATOM   3049  C  CB    . VAL A 1 376 ? 149.677 142.012 108.390 1.00 12.52 ?  376 VAL A CB    1 
ATOM   3050  C  CG1   . VAL A 1 376 ? 148.374 141.254 108.564 1.00 13.55 ?  376 VAL A CG1   1 
ATOM   3051  C  CG2   . VAL A 1 376 ? 149.525 143.112 107.361 1.00 3.43  ?  376 VAL A CG2   1 
ATOM   3052  N  N     . LYS A 1 377 ? 149.621 141.482 111.827 1.00 17.05 ?  377 LYS A N     1 
ATOM   3053  C  CA    . LYS A 1 377 ? 149.828 140.532 112.909 1.00 10.87 ?  377 LYS A CA    1 
ATOM   3054  C  C     . LYS A 1 377 ? 148.764 139.454 112.992 1.00 11.62 ?  377 LYS A C     1 
ATOM   3055  O  O     . LYS A 1 377 ? 148.985 138.454 113.677 1.00 27.28 ?  377 LYS A O     1 
ATOM   3056  C  CB    . LYS A 1 377 ? 149.889 141.257 114.259 1.00 13.24 ?  377 LYS A CB    1 
ATOM   3057  C  CG    . LYS A 1 377 ? 150.777 142.481 114.278 1.00 11.59 ?  377 LYS A CG    1 
ATOM   3058  C  CD    . LYS A 1 377 ? 150.312 143.445 115.347 1.00 22.02 ?  377 LYS A CD    1 
ATOM   3059  C  CE    . LYS A 1 377 ? 150.536 144.879 114.936 1.00 18.69 ?  377 LYS A CE    1 
ATOM   3060  N  NZ    . LYS A 1 377 ? 149.826 145.821 115.842 1.00 20.26 1  377 LYS A NZ    1 
ATOM   3061  N  N     . PHE A 1 378 ? 147.624 139.633 112.335 1.00 13.99 ?  378 PHE A N     1 
ATOM   3062  C  CA    . PHE A 1 378 ? 146.570 138.631 112.360 1.00 7.50  ?  378 PHE A CA    1 
ATOM   3063  C  C     . PHE A 1 378 ? 145.609 138.899 111.213 1.00 10.29 ?  378 PHE A C     1 
ATOM   3064  O  O     . PHE A 1 378 ? 145.621 139.973 110.607 1.00 18.96 ?  378 PHE A O     1 
ATOM   3065  C  CB    . PHE A 1 378 ? 145.834 138.605 113.709 1.00 6.96  ?  378 PHE A CB    1 
ATOM   3066  C  CG    . PHE A 1 378 ? 144.988 139.820 113.988 1.00 6.75  ?  378 PHE A CG    1 
ATOM   3067  C  CD1   . PHE A 1 378 ? 145.510 141.098 113.887 1.00 10.61 ?  378 PHE A CD1   1 
ATOM   3068  C  CD2   . PHE A 1 378 ? 143.672 139.674 114.386 1.00 4.93  ?  378 PHE A CD2   1 
ATOM   3069  C  CE1   . PHE A 1 378 ? 144.733 142.201 114.158 1.00 8.34  ?  378 PHE A CE1   1 
ATOM   3070  C  CE2   . PHE A 1 378 ? 142.891 140.775 114.659 1.00 10.30 ?  378 PHE A CE2   1 
ATOM   3071  C  CZ    . PHE A 1 378 ? 143.424 142.039 114.546 1.00 8.75  ?  378 PHE A CZ    1 
ATOM   3072  N  N     . SER A 1 379 ? 144.788 137.901 110.918 1.00 5.32  ?  379 SER A N     1 
ATOM   3073  C  CA    . SER A 1 379 ? 143.796 137.973 109.861 1.00 7.81  ?  379 SER A CA    1 
ATOM   3074  C  C     . SER A 1 379 ? 142.405 138.063 110.478 1.00 8.33  ?  379 SER A C     1 
ATOM   3075  O  O     . SER A 1 379 ? 142.248 138.181 111.697 1.00 16.72 ?  379 SER A O     1 
ATOM   3076  C  CB    . SER A 1 379 ? 143.933 136.773 108.923 1.00 13.39 ?  379 SER A CB    1 
ATOM   3077  O  OG    . SER A 1 379 ? 143.527 137.111 107.612 1.00 14.39 ?  379 SER A OG    1 
ATOM   3078  N  N     . ASN A 1 380 ? 141.387 138.023 109.627 1.00 8.33  ?  380 ASN A N     1 
ATOM   3079  C  CA    . ASN A 1 380 ? 140.008 138.152 110.058 1.00 7.79  ?  380 ASN A CA    1 
ATOM   3080  C  C     . ASN A 1 380 ? 139.392 136.772 110.277 1.00 16.69 ?  380 ASN A C     1 
ATOM   3081  O  O     . ASN A 1 380 ? 140.074 135.745 110.246 1.00 19.66 ?  380 ASN A O     1 
ATOM   3082  C  CB    . ASN A 1 380 ? 139.217 138.976 109.042 1.00 10.47 ?  380 ASN A CB    1 
ATOM   3083  C  CG    . ASN A 1 380 ? 139.122 138.305 107.693 1.00 7.14  ?  380 ASN A CG    1 
ATOM   3084  O  OD1   . ASN A 1 380 ? 140.091 137.734 107.201 1.00 18.25 ?  380 ASN A OD1   1 
ATOM   3085  N  ND2   . ASN A 1 380 ? 137.948 138.375 107.084 1.00 14.30 ?  380 ASN A ND2   1 
ATOM   3086  N  N     . LEU A 1 381 ? 138.079 136.750 110.513 1.00 17.42 ?  381 LEU A N     1 
ATOM   3087  C  CA    . LEU A 1 381 ? 137.377 135.487 110.706 1.00 10.98 ?  381 LEU A CA    1 
ATOM   3088  C  C     . LEU A 1 381 ? 137.372 134.646 109.436 1.00 10.10 ?  381 LEU A C     1 
ATOM   3089  O  O     . LEU A 1 381 ? 137.373 133.413 109.511 1.00 20.39 ?  381 LEU A O     1 
ATOM   3090  C  CB    . LEU A 1 381 ? 135.950 135.761 111.182 1.00 12.55 ?  381 LEU A CB    1 
ATOM   3091  C  CG    . LEU A 1 381 ? 134.960 134.600 111.268 1.00 14.65 ?  381 LEU A CG    1 
ATOM   3092  C  CD1   . LEU A 1 381 ? 135.301 133.674 112.419 1.00 16.28 ?  381 LEU A CD1   1 
ATOM   3093  C  CD2   . LEU A 1 381 ? 133.550 135.135 111.407 1.00 17.94 ?  381 LEU A CD2   1 
ATOM   3094  N  N     . CYS A 1 382 ? 137.370 135.285 108.271 1.00 18.94 ?  382 CYS A N     1 
ATOM   3095  C  CA    . CYS A 1 382 ? 137.440 134.579 107.000 1.00 13.00 ?  382 CYS A CA    1 
ATOM   3096  C  C     . CYS A 1 382 ? 138.869 134.395 106.508 1.00 7.71  ?  382 CYS A C     1 
ATOM   3097  O  O     . CYS A 1 382 ? 139.072 133.792 105.451 1.00 17.19 ?  382 CYS A O     1 
ATOM   3098  C  CB    . CYS A 1 382 ? 136.611 135.313 105.943 1.00 20.13 ?  382 CYS A CB    1 
ATOM   3099  S  SG    . CYS A 1 382 ? 134.897 135.613 106.424 1.00 26.50 ?  382 CYS A SG    1 
ATOM   3100  N  N     . SER A 1 383 ? 139.854 134.909 107.247 1.00 15.62 ?  383 SER A N     1 
ATOM   3101  C  CA    . SER A 1 383 ? 141.272 134.638 107.002 1.00 10.49 ?  383 SER A CA    1 
ATOM   3102  C  C     . SER A 1 383 ? 141.737 135.183 105.652 1.00 12.80 ?  383 SER A C     1 
ATOM   3103  O  O     . SER A 1 383 ? 142.549 134.566 104.962 1.00 26.33 ?  383 SER A O     1 
ATOM   3104  C  CB    . SER A 1 383 ? 141.570 133.141 107.116 1.00 16.56 ?  383 SER A CB    1 
ATOM   3105  O  OG    . SER A 1 383 ? 142.952 132.876 106.968 1.00 24.81 ?  383 SER A OG    1 
ATOM   3106  N  N     . GLU A 1 384 ? 141.223 136.351 105.267 1.00 14.02 ?  384 GLU A N     1 
ATOM   3107  C  CA    . GLU A 1 384 ? 141.695 136.993 104.045 1.00 5.78  ?  384 GLU A CA    1 
ATOM   3108  C  C     . GLU A 1 384 ? 141.986 138.480 104.192 1.00 14.42 ?  384 GLU A C     1 
ATOM   3109  O  O     . GLU A 1 384 ? 142.653 139.038 103.318 1.00 20.38 ?  384 GLU A O     1 
ATOM   3110  C  CB    . GLU A 1 384 ? 140.688 136.780 102.901 1.00 9.03  ?  384 GLU A CB    1 
ATOM   3111  C  CG    . GLU A 1 384 ? 139.847 137.984 102.509 1.00 10.86 ?  384 GLU A CG    1 
ATOM   3112  C  CD    . GLU A 1 384 ? 138.701 138.240 103.460 1.00 21.19 ?  384 GLU A CD    1 
ATOM   3113  O  OE1   . GLU A 1 384 ? 138.328 137.312 104.204 1.00 14.47 ?  384 GLU A OE1   1 
ATOM   3114  O  OE2   . GLU A 1 384 ? 138.157 139.361 103.445 1.00 27.61 -1 384 GLU A OE2   1 
ATOM   3115  N  N     . VAL A 1 385 ? 141.540 139.135 105.257 1.00 17.24 ?  385 VAL A N     1 
ATOM   3116  C  CA    . VAL A 1 385 ? 141.847 140.541 105.486 1.00 5.14  ?  385 VAL A CA    1 
ATOM   3117  C  C     . VAL A 1 385 ? 143.215 140.626 106.149 1.00 15.31 ?  385 VAL A C     1 
ATOM   3118  O  O     . VAL A 1 385 ? 143.425 140.071 107.231 1.00 23.18 ?  385 VAL A O     1 
ATOM   3119  C  CB    . VAL A 1 385 ? 140.774 141.215 106.351 1.00 7.09  ?  385 VAL A CB    1 
ATOM   3120  C  CG1   . VAL A 1 385 ? 141.197 142.621 106.690 1.00 8.27  ?  385 VAL A CG1   1 
ATOM   3121  C  CG2   . VAL A 1 385 ? 139.448 141.225 105.631 1.00 7.56  ?  385 VAL A CG2   1 
ATOM   3122  N  N     . LEU A 1 386 ? 144.146 141.323 105.498 1.00 16.57 ?  386 LEU A N     1 
ATOM   3123  C  CA    . LEU A 1 386 ? 145.533 141.427 105.953 1.00 2.61  ?  386 LEU A CA    1 
ATOM   3124  C  C     . LEU A 1 386 ? 145.949 142.891 105.873 1.00 5.27  ?  386 LEU A C     1 
ATOM   3125  O  O     . LEU A 1 386 ? 146.456 143.348 104.847 1.00 11.88 ?  386 LEU A O     1 
ATOM   3126  C  CB    . LEU A 1 386 ? 146.440 140.533 105.122 1.00 2.13  ?  386 LEU A CB    1 
ATOM   3127  C  CG    . LEU A 1 386 ? 146.198 139.037 105.316 1.00 6.65  ?  386 LEU A CG    1 
ATOM   3128  C  CD1   . LEU A 1 386 ? 147.069 138.243 104.384 1.00 10.46 ?  386 LEU A CD1   1 
ATOM   3129  C  CD2   . LEU A 1 386 ? 146.458 138.641 106.757 1.00 13.82 ?  386 LEU A CD2   1 
ATOM   3130  N  N     . GLN A 1 387 ? 145.740 143.620 106.966 1.00 14.61 ?  387 GLN A N     1 
ATOM   3131  C  CA    . GLN A 1 387 ? 145.997 145.048 107.021 1.00 10.55 ?  387 GLN A CA    1 
ATOM   3132  C  C     . GLN A 1 387 ? 146.769 145.388 108.288 1.00 12.82 ?  387 GLN A C     1 
ATOM   3133  O  O     . GLN A 1 387 ? 146.768 144.636 109.264 1.00 25.68 ?  387 GLN A O     1 
ATOM   3134  C  CB    . GLN A 1 387 ? 144.691 145.853 106.974 1.00 3.94  ?  387 GLN A CB    1 
ATOM   3135  C  CG    . GLN A 1 387 ? 143.806 145.518 105.793 1.00 7.66  ?  387 GLN A CG    1 
ATOM   3136  C  CD    . GLN A 1 387 ? 142.564 146.368 105.745 1.00 9.54  ?  387 GLN A CD    1 
ATOM   3137  O  OE1   . GLN A 1 387 ? 142.467 147.382 106.431 1.00 26.99 ?  387 GLN A OE1   1 
ATOM   3138  N  NE2   . GLN A 1 387 ? 141.598 145.959 104.935 1.00 13.40 ?  387 GLN A NE2   1 
ATOM   3139  N  N     . ALA A 1 388 ? 147.442 146.534 108.253 1.00 12.69 ?  388 ALA A N     1 
ATOM   3140  C  CA    . ALA A 1 388 ? 148.173 147.011 109.417 1.00 10.57 ?  388 ALA A CA    1 
ATOM   3141  C  C     . ALA A 1 388 ? 147.208 147.468 110.503 1.00 13.36 ?  388 ALA A C     1 
ATOM   3142  O  O     . ALA A 1 388 ? 146.192 148.109 110.226 1.00 25.27 ?  388 ALA A O     1 
ATOM   3143  C  CB    . ALA A 1 388 ? 149.102 148.158 109.026 1.00 11.56 ?  388 ALA A CB    1 
ATOM   3144  N  N     . SER A 1 389 ? 147.528 147.130 111.748 1.00 19.36 ?  389 SER A N     1 
ATOM   3145  C  CA    . SER A 1 389 ? 146.724 147.523 112.893 1.00 13.85 ?  389 SER A CA    1 
ATOM   3146  C  C     . SER A 1 389 ? 147.621 148.067 113.992 1.00 15.70 ?  389 SER A C     1 
ATOM   3147  O  O     . SER A 1 389 ? 148.764 147.635 114.155 1.00 23.18 ?  389 SER A O     1 
ATOM   3148  C  CB    . SER A 1 389 ? 145.898 146.351 113.440 1.00 14.60 ?  389 SER A CB    1 
ATOM   3149  O  OG    . SER A 1 389 ? 146.712 145.218 113.683 1.00 25.24 ?  389 SER A OG    1 
ATOM   3150  N  N     . GLN A 1 390 ? 147.087 149.021 114.746 1.00 17.82 ?  390 GLN A N     1 
ATOM   3151  C  CA    . GLN A 1 390 ? 147.752 149.569 115.919 1.00 14.43 ?  390 GLN A CA    1 
ATOM   3152  C  C     . GLN A 1 390 ? 146.848 149.363 117.122 1.00 14.63 ?  390 GLN A C     1 
ATOM   3153  O  O     . GLN A 1 390 ? 145.666 149.718 117.082 1.00 27.28 ?  390 GLN A O     1 
ATOM   3154  C  CB    . GLN A 1 390 ? 148.073 151.053 115.732 1.00 17.79 ?  390 GLN A CB    1 
ATOM   3155  C  CG    . GLN A 1 390 ? 149.109 151.322 114.659 1.00 17.56 ?  390 GLN A CG    1 
ATOM   3156  C  CD    . GLN A 1 390 ? 149.262 152.795 114.351 1.00 22.86 ?  390 GLN A CD    1 
ATOM   3157  O  OE1   . GLN A 1 390 ? 148.482 153.624 114.819 1.00 31.19 ?  390 GLN A OE1   1 
ATOM   3158  N  NE2   . GLN A 1 390 ? 150.274 153.132 113.562 1.00 21.59 ?  390 GLN A NE2   1 
ATOM   3159  N  N     . VAL A 1 391 ? 147.401 148.782 118.187 1.00 23.96 ?  391 VAL A N     1 
ATOM   3160  C  CA    . VAL A 1 391 ? 146.595 148.454 119.354 1.00 24.92 ?  391 VAL A CA    1 
ATOM   3161  C  C     . VAL A 1 391 ? 146.179 149.730 120.078 1.00 25.86 ?  391 VAL A C     1 
ATOM   3162  O  O     . VAL A 1 391 ? 146.902 150.735 120.097 1.00 26.45 ?  391 VAL A O     1 
ATOM   3163  C  CB    . VAL A 1 391 ? 147.357 147.494 120.289 1.00 15.46 ?  391 VAL A CB    1 
ATOM   3164  C  CG1   . VAL A 1 391 ? 148.411 148.236 121.094 1.00 21.40 ?  391 VAL A CG1   1 
ATOM   3165  C  CG2   . VAL A 1 391 ? 146.392 146.766 121.207 1.00 16.26 ?  391 VAL A CG2   1 
ATOM   3166  N  N     . SER A 1 392 ? 144.984 149.699 120.653 1.00 28.22 ?  392 SER A N     1 
ATOM   3167  C  CA    . SER A 1 392 ? 144.481 150.804 121.448 1.00 18.16 ?  392 SER A CA    1 
ATOM   3168  C  C     . SER A 1 392 ? 144.883 150.631 122.907 1.00 27.95 ?  392 SER A C     1 
ATOM   3169  O  O     . SER A 1 392 ? 145.209 149.533 123.363 1.00 36.07 ?  392 SER A O     1 
ATOM   3170  C  CB    . SER A 1 392 ? 142.960 150.909 121.332 1.00 24.73 ?  392 SER A CB    1 
ATOM   3171  O  OG    . SER A 1 392 ? 142.568 151.234 120.011 1.00 33.95 ?  392 SER A OG    1 
ATOM   3172  N  N     . SER A 1 393 ? 144.859 151.737 123.640 1.00 33.60 ?  393 SER A N     1 
ATOM   3173  C  CA    . SER A 1 393 ? 145.173 151.749 125.065 1.00 31.95 ?  393 SER A CA    1 
ATOM   3174  C  C     . SER A 1 393 ? 143.944 152.282 125.795 1.00 32.73 ?  393 SER A C     1 
ATOM   3175  O  O     . SER A 1 393 ? 143.841 153.480 126.070 1.00 34.99 ?  393 SER A O     1 
ATOM   3176  C  CB    . SER A 1 393 ? 146.412 152.590 125.352 1.00 31.84 ?  393 SER A CB    1 
ATOM   3177  O  OG    . SER A 1 393 ? 147.166 152.037 126.416 1.00 39.31 ?  393 SER A OG    1 
ATOM   3178  N  N     . TYR A 1 394 ? 143.013 151.386 126.104 1.00 34.05 ?  394 TYR A N     1 
ATOM   3179  C  CA    . TYR A 1 394 ? 141.813 151.758 126.840 1.00 31.62 ?  394 TYR A CA    1 
ATOM   3180  C  C     . TYR A 1 394 ? 142.153 151.851 128.321 1.00 35.26 ?  394 TYR A C     1 
ATOM   3181  O  O     . TYR A 1 394 ? 142.539 150.855 128.942 1.00 37.43 ?  394 TYR A O     1 
ATOM   3182  C  CB    . TYR A 1 394 ? 140.697 150.748 126.593 1.00 28.57 ?  394 TYR A CB    1 
ATOM   3183  C  CG    . TYR A 1 394 ? 140.247 150.690 125.150 1.00 30.05 ?  394 TYR A CG    1 
ATOM   3184  C  CD1   . TYR A 1 394 ? 139.515 151.729 124.591 1.00 31.16 ?  394 TYR A CD1   1 
ATOM   3185  C  CD2   . TYR A 1 394 ? 140.560 149.603 124.348 1.00 31.12 ?  394 TYR A CD2   1 
ATOM   3186  C  CE1   . TYR A 1 394 ? 139.105 151.682 123.276 1.00 33.30 ?  394 TYR A CE1   1 
ATOM   3187  C  CE2   . TYR A 1 394 ? 140.152 149.547 123.033 1.00 30.57 ?  394 TYR A CE2   1 
ATOM   3188  C  CZ    . TYR A 1 394 ? 139.426 150.589 122.501 1.00 37.78 ?  394 TYR A CZ    1 
ATOM   3189  O  OH    . TYR A 1 394 ? 139.021 150.537 121.187 1.00 39.81 ?  394 TYR A OH    1 
ATOM   3190  N  N     . THR A 1 395 ? 142.017 153.045 128.880 1.00 34.33 ?  395 THR A N     1 
ATOM   3191  C  CA    . THR A 1 395 ? 142.435 153.342 130.238 1.00 36.56 ?  395 THR A CA    1 
ATOM   3192  C  C     . THR A 1 395 ? 141.230 153.306 131.175 1.00 37.82 ?  395 THR A C     1 
ATOM   3193  O  O     . THR A 1 395 ? 140.136 152.868 130.804 1.00 34.94 ?  395 THR A O     1 
ATOM   3194  C  CB    . THR A 1 395 ? 143.146 154.695 130.269 1.00 35.93 ?  395 THR A CB    1 
ATOM   3195  O  OG1   . THR A 1 395 ? 142.264 155.709 129.771 1.00 37.71 ?  395 THR A OG1   1 
ATOM   3196  C  CG2   . THR A 1 395 ? 144.390 154.654 129.401 1.00 34.69 ?  395 THR A CG2   1 
ATOM   3197  N  N     . ASP A 1 396 ? 141.434 153.752 132.413 1.00 39.46 ?  396 ASP A N     1 
ATOM   3198  C  CA    . ASP A 1 396 ? 140.358 153.806 133.387 1.00 35.04 ?  396 ASP A CA    1 
ATOM   3199  C  C     . ASP A 1 396 ? 139.241 154.730 132.904 1.00 37.72 ?  396 ASP A C     1 
ATOM   3200  O  O     . ASP A 1 396 ? 139.379 155.468 131.927 1.00 43.75 ?  396 ASP A O     1 
ATOM   3201  C  CB    . ASP A 1 396 ? 140.885 154.272 134.743 1.00 37.84 ?  396 ASP A CB    1 
ATOM   3202  C  CG    . ASP A 1 396 ? 141.892 153.310 135.340 1.00 43.06 ?  396 ASP A CG    1 
ATOM   3203  O  OD1   . ASP A 1 396 ? 141.587 152.102 135.418 1.00 40.24 ?  396 ASP A OD1   1 
ATOM   3204  O  OD2   . ASP A 1 396 ? 142.987 153.761 135.734 1.00 44.39 -1 396 ASP A OD2   1 
ATOM   3205  N  N     . TYR A 1 397 ? 138.113 154.676 133.616 1.00 35.15 ?  397 TYR A N     1 
ATOM   3206  C  CA    . TYR A 1 397 ? 136.935 155.434 133.202 1.00 35.34 ?  397 TYR A CA    1 
ATOM   3207  C  C     . TYR A 1 397 ? 137.217 156.930 133.171 1.00 36.99 ?  397 TYR A C     1 
ATOM   3208  O  O     . TYR A 1 397 ? 136.798 157.628 132.240 1.00 41.13 ?  397 TYR A O     1 
ATOM   3209  C  CB    . TYR A 1 397 ? 135.763 155.129 134.135 1.00 30.96 ?  397 TYR A CB    1 
ATOM   3210  C  CG    . TYR A 1 397 ? 134.480 155.826 133.748 1.00 33.12 ?  397 TYR A CG    1 
ATOM   3211  C  CD1   . TYR A 1 397 ? 133.612 155.259 132.825 1.00 33.56 ?  397 TYR A CD1   1 
ATOM   3212  C  CD2   . TYR A 1 397 ? 134.140 157.054 134.301 1.00 34.28 ?  397 TYR A CD2   1 
ATOM   3213  C  CE1   . TYR A 1 397 ? 132.442 155.895 132.466 1.00 29.73 ?  397 TYR A CE1   1 
ATOM   3214  C  CE2   . TYR A 1 397 ? 132.974 157.695 133.947 1.00 33.91 ?  397 TYR A CE2   1 
ATOM   3215  C  CZ    . TYR A 1 397 ? 132.129 157.112 133.031 1.00 34.95 ?  397 TYR A CZ    1 
ATOM   3216  O  OH    . TYR A 1 397 ? 130.964 157.749 132.678 1.00 39.62 ?  397 TYR A OH    1 
ATOM   3217  N  N     . ASP A 1 398 ? 137.924 157.441 134.175 1.00 40.12 ?  398 ASP A N     1 
ATOM   3218  C  CA    . ASP A 1 398 ? 138.190 158.869 134.273 1.00 39.48 ?  398 ASP A CA    1 
ATOM   3219  C  C     . ASP A 1 398 ? 139.250 159.355 133.295 1.00 45.32 ?  398 ASP A C     1 
ATOM   3220  O  O     . ASP A 1 398 ? 139.333 160.563 133.051 1.00 46.74 ?  398 ASP A O     1 
ATOM   3221  C  CB    . ASP A 1 398 ? 138.613 159.222 135.701 1.00 43.35 ?  398 ASP A CB    1 
ATOM   3222  C  CG    . ASP A 1 398 ? 139.499 158.158 136.324 1.00 46.91 ?  398 ASP A CG    1 
ATOM   3223  O  OD1   . ASP A 1 398 ? 139.002 157.040 136.567 1.00 43.86 ?  398 ASP A OD1   1 
ATOM   3224  O  OD2   . ASP A 1 398 ? 140.690 158.440 136.569 1.00 45.84 -1 398 ASP A OD2   1 
ATOM   3225  N  N     . GLU A 1 399 ? 140.053 158.459 132.732 1.00 46.09 ?  399 GLU A N     1 
ATOM   3226  C  CA    . GLU A 1 399 ? 141.167 158.836 131.875 1.00 42.81 ?  399 GLU A CA    1 
ATOM   3227  C  C     . GLU A 1 399 ? 140.790 158.720 130.403 1.00 45.49 ?  399 GLU A C     1 
ATOM   3228  O  O     . GLU A 1 399 ? 139.876 157.985 130.022 1.00 45.00 ?  399 GLU A O     1 
ATOM   3229  C  CB    . GLU A 1 399 ? 142.390 157.965 132.167 1.00 42.35 ?  399 GLU A CB    1 
ATOM   3230  C  CG    . GLU A 1 399 ? 142.465 157.451 133.589 1.00 44.59 ?  399 GLU A CG    1 
ATOM   3231  C  CD    . GLU A 1 399 ? 143.826 156.882 133.930 1.00 50.14 ?  399 GLU A CD    1 
ATOM   3232  O  OE1   . GLU A 1 399 ? 144.123 155.749 133.493 1.00 46.87 ?  399 GLU A OE1   1 
ATOM   3233  O  OE2   . GLU A 1 399 ? 144.597 157.563 134.636 1.00 49.31 -1 399 GLU A OE2   1 
ATOM   3234  N  N     . GLU A 1 400 ? 141.515 159.468 129.576 1.00 43.20 ?  400 GLU A N     1 
ATOM   3235  C  CA    . GLU A 1 400 ? 141.317 159.410 128.136 1.00 40.44 ?  400 GLU A CA    1 
ATOM   3236  C  C     . GLU A 1 400 ? 141.961 158.155 127.558 1.00 41.95 ?  400 GLU A C     1 
ATOM   3237  O  O     . GLU A 1 400 ? 143.017 157.711 128.015 1.00 41.73 ?  400 GLU A O     1 
ATOM   3238  C  CB    . GLU A 1 400 ? 141.903 160.653 127.468 1.00 40.61 ?  400 GLU A CB    1 
ATOM   3239  C  CG    . GLU A 1 400 ? 141.050 161.900 127.617 1.00 44.10 ?  400 GLU A CG    1 
ATOM   3240  C  CD    . GLU A 1 400 ? 140.074 162.078 126.471 1.00 49.46 ?  400 GLU A CD    1 
ATOM   3241  O  OE1   . GLU A 1 400 ? 138.981 162.635 126.701 1.00 45.54 ?  400 GLU A OE1   1 
ATOM   3242  O  OE2   . GLU A 1 400 ? 140.399 161.661 125.341 1.00 49.57 -1 400 GLU A OE2   1 
ATOM   3243  N  N     . ASP A 1 401 ? 141.316 157.584 126.546 1.00 39.60 ?  401 ASP A N     1 
ATOM   3244  C  CA    . ASP A 1 401 ? 141.812 156.381 125.896 1.00 36.96 ?  401 ASP A CA    1 
ATOM   3245  C  C     . ASP A 1 401 ? 142.661 156.742 124.686 1.00 37.21 ?  401 ASP A C     1 
ATOM   3246  O  O     . ASP A 1 401 ? 142.361 157.695 123.962 1.00 39.03 ?  401 ASP A O     1 
ATOM   3247  C  CB    . ASP A 1 401 ? 140.655 155.482 125.463 1.00 35.70 ?  401 ASP A CB    1 
ATOM   3248  C  CG    . ASP A 1 401 ? 139.754 155.094 126.616 1.00 39.29 ?  401 ASP A CG    1 
ATOM   3249  O  OD1   . ASP A 1 401 ? 140.247 155.021 127.760 1.00 41.78 ?  401 ASP A OD1   1 
ATOM   3250  O  OD2   . ASP A 1 401 ? 138.552 154.857 126.377 1.00 40.69 -1 401 ASP A OD2   1 
ATOM   3251  N  N     . GLU A 1 402 ? 143.727 155.975 124.474 1.00 33.55 ?  402 GLU A N     1 
ATOM   3252  C  CA    . GLU A 1 402 ? 144.550 156.096 123.277 1.00 32.92 ?  402 GLU A CA    1 
ATOM   3253  C  C     . GLU A 1 402 ? 143.986 155.153 122.222 1.00 31.86 ?  402 GLU A C     1 
ATOM   3254  O  O     . GLU A 1 402 ? 144.158 153.934 122.313 1.00 39.81 ?  402 GLU A O     1 
ATOM   3255  C  CB    . GLU A 1 402 ? 146.010 155.771 123.583 1.00 36.93 ?  402 GLU A CB    1 
ATOM   3256  C  CG    . GLU A 1 402 ? 146.675 156.738 124.545 1.00 36.37 ?  402 GLU A CG    1 
ATOM   3257  C  CD    . GLU A 1 402 ? 147.511 156.032 125.595 1.00 43.09 ?  402 GLU A CD    1 
ATOM   3258  O  OE1   . GLU A 1 402 ? 148.696 155.749 125.321 1.00 43.53 ?  402 GLU A OE1   1 
ATOM   3259  O  OE2   . GLU A 1 402 ? 146.983 155.762 126.694 1.00 43.84 -1 402 GLU A OE2   1 
ATOM   3260  N  N     . ILE A 1 403 ? 143.310 155.713 121.228 1.00 29.35 ?  403 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 403 ? 142.623 154.926 120.211 1.00 30.38 ?  403 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 403 ? 143.614 154.547 119.120 1.00 29.83 ?  403 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 403 ? 144.293 155.412 118.555 1.00 31.37 ?  403 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 403 ? 141.431 155.705 119.632 1.00 27.23 ?  403 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 403 ? 140.389 155.970 120.722 1.00 30.31 ?  403 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 403 ? 140.817 154.950 118.468 1.00 22.57 ?  403 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 403 ? 140.033 154.749 121.541 1.00 30.63 ?  403 ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 404 ? 143.694 153.252 118.822 1.00 24.83 ?  404 GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 404 ? 144.563 152.764 117.770 1.00 15.92 ?  404 GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 404 ? 143.850 152.597 116.445 1.00 22.98 ?  404 GLY A C     1 
ATOM   3271  O  O     . GLY A 1 404 ? 142.953 153.375 116.113 1.00 33.56 ?  404 GLY A O     1 
ATOM   3272  N  N     . LEU A 1 405 ? 144.242 151.584 115.673 1.00 21.63 ?  405 LEU A N     1 
ATOM   3273  C  CA    . LEU A 1 405 ? 143.652 151.311 114.367 1.00 8.88  ?  405 LEU A CA    1 
ATOM   3274  C  C     . LEU A 1 405 ? 143.186 149.861 114.336 1.00 15.28 ?  405 LEU A C     1 
ATOM   3275  O  O     . LEU A 1 405 ? 144.010 148.942 114.346 1.00 16.33 ?  405 LEU A O     1 
ATOM   3276  C  CB    . LEU A 1 405 ? 144.651 151.579 113.241 1.00 18.00 ?  405 LEU A CB    1 
ATOM   3277  C  CG    . LEU A 1 405 ? 145.172 153.006 113.073 1.00 17.66 ?  405 LEU A CG    1 
ATOM   3278  C  CD1   . LEU A 1 405 ? 146.300 153.036 112.059 1.00 18.80 ?  405 LEU A CD1   1 
ATOM   3279  C  CD2   . LEU A 1 405 ? 144.057 153.949 112.666 1.00 16.03 ?  405 LEU A CD2   1 
ATOM   3280  N  N     . ASP A 1 406 ? 141.874 149.660 114.293 1.00 23.95 ?  406 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 406 ? 141.287 148.333 114.176 1.00 12.97 ?  406 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 406 ? 140.758 148.133 112.763 1.00 17.53 ?  406 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 406 ? 140.064 148.994 112.218 1.00 31.72 ?  406 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 406 ? 140.165 148.134 115.195 1.00 16.10 ?  406 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 406 ? 140.683 147.720 116.560 1.00 30.19 ?  406 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 406 ? 141.892 147.434 116.683 1.00 30.73 ?  406 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 406 ? 139.881 147.685 117.516 1.00 30.34 -1 406 ASP A OD2   1 
ATOM   3288  N  N     . ILE A 1 407 ? 141.068 146.984 112.186 1.00 23.30 ?  407 ILE A N     1 
ATOM   3289  C  CA    . ILE A 1 407 ? 140.866 146.766 110.760 1.00 17.70 ?  407 ILE A CA    1 
ATOM   3290  C  C     . ILE A 1 407 ? 139.397 146.492 110.465 1.00 18.01 ?  407 ILE A C     1 
ATOM   3291  O  O     . ILE A 1 407 ? 138.702 145.814 111.231 1.00 21.33 ?  407 ILE A O     1 
ATOM   3292  C  CB    . ILE A 1 407 ? 141.755 145.610 110.271 1.00 13.02 ?  407 ILE A CB    1 
ATOM   3293  C  CG1   . ILE A 1 407 ? 143.225 145.901 110.561 1.00 2.81  ?  407 ILE A CG1   1 
ATOM   3294  C  CG2   . ILE A 1 407 ? 141.551 145.369 108.802 1.00 16.48 ?  407 ILE A CG2   1 
ATOM   3295  C  CD1   . ILE A 1 407 ? 143.996 144.684 110.978 1.00 18.29 ?  407 ILE A CD1   1 
ATOM   3296  N  N     . SER A 1 408 ? 138.927 147.030 109.342 1.00 27.38 ?  408 SER A N     1 
ATOM   3297  C  CA    . SER A 1 408 ? 137.639 146.683 108.762 1.00 20.37 ?  408 SER A CA    1 
ATOM   3298  C  C     . SER A 1 408 ? 137.646 147.147 107.313 1.00 24.30 ?  408 SER A C     1 
ATOM   3299  O  O     . SER A 1 408 ? 138.083 148.263 107.020 1.00 36.21 ?  408 SER A O     1 
ATOM   3300  C  CB    . SER A 1 408 ? 136.475 147.323 109.527 1.00 21.57 ?  408 SER A CB    1 
ATOM   3301  O  OG    . SER A 1 408 ? 136.138 148.588 108.988 1.00 28.81 ?  408 SER A OG    1 
ATOM   3302  N  N     . CYS A 1 409 ? 137.176 146.290 106.412 1.00 20.11 ?  409 CYS A N     1 
ATOM   3303  C  CA    . CYS A 1 409 ? 137.096 146.638 105.002 1.00 26.27 ?  409 CYS A CA    1 
ATOM   3304  C  C     . CYS A 1 409 ? 135.764 146.178 104.430 1.00 26.33 ?  409 CYS A C     1 
ATOM   3305  O  O     . CYS A 1 409 ? 135.161 145.207 104.893 1.00 24.50 ?  409 CYS A O     1 
ATOM   3306  C  CB    . CYS A 1 409 ? 138.261 146.039 104.197 1.00 22.59 ?  409 CYS A CB    1 
ATOM   3307  S  SG    . CYS A 1 409 ? 138.177 144.261 103.912 1.00 39.49 ?  409 CYS A SG    1 
ATOM   3308  N  N     . ASN A 1 410 ? 135.307 146.902 103.413 1.00 22.83 ?  410 ASN A N     1 
ATOM   3309  C  CA    . ASN A 1 410 ? 134.075 146.574 102.718 1.00 18.43 ?  410 ASN A CA    1 
ATOM   3310  C  C     . ASN A 1 410 ? 134.384 145.595 101.598 1.00 20.75 ?  410 ASN A C     1 
ATOM   3311  O  O     . ASN A 1 410 ? 135.341 145.788 100.842 1.00 22.15 ?  410 ASN A O     1 
ATOM   3312  C  CB    . ASN A 1 410 ? 133.416 147.827 102.148 1.00 22.82 ?  410 ASN A CB    1 
ATOM   3313  C  CG    . ASN A 1 410 ? 134.085 149.092 102.614 1.00 30.14 ?  410 ASN A CG    1 
ATOM   3314  O  OD1   . ASN A 1 410 ? 134.559 149.181 103.746 1.00 31.24 ?  410 ASN A OD1   1 
ATOM   3315  N  ND2   . ASN A 1 410 ? 134.142 150.080 101.736 1.00 28.88 ?  410 ASN A ND2   1 
ATOM   3316  N  N     . LEU A 1 411 ? 133.570 144.555 101.490 1.00 17.79 ?  411 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 411 ? 133.809 143.477 100.548 1.00 12.06 ?  411 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 411 ? 132.982 143.677 99.286  1.00 13.10 ?  411 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 411 ? 131.888 144.244 99.316  1.00 19.18 ?  411 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 411 ? 133.474 142.128 101.185 1.00 21.93 ?  411 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 411 ? 134.192 141.778 102.486 1.00 14.94 ?  411 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 411 ? 134.137 140.290 102.716 1.00 20.54 ?  411 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 411 ? 135.633 142.244 102.447 1.00 19.17 ?  411 LEU A CD2   1 
ATOM   3324  N  N     . GLY A 1 412 ? 133.527 143.206 98.170  1.00 21.24 ?  412 GLY A N     1 
ATOM   3325  C  CA    . GLY A 1 412 ? 132.836 143.221 96.899  1.00 10.26 ?  412 GLY A CA    1 
ATOM   3326  C  C     . GLY A 1 412 ? 133.553 142.327 95.915  1.00 11.55 ?  412 GLY A C     1 
ATOM   3327  O  O     . GLY A 1 412 ? 134.785 142.321 95.873  1.00 25.53 ?  412 GLY A O     1 
ATOM   3328  N  N     . SER A 1 413 ? 132.811 141.566 95.120  1.00 15.23 ?  413 SER A N     1 
ATOM   3329  C  CA    . SER A 1 413 ? 133.397 140.566 94.240  1.00 9.33  ?  413 SER A CA    1 
ATOM   3330  C  C     . SER A 1 413 ? 133.094 140.891 92.788  1.00 15.97 ?  413 SER A C     1 
ATOM   3331  O  O     . SER A 1 413 ? 131.948 141.190 92.439  1.00 24.07 ?  413 SER A O     1 
ATOM   3332  C  CB    . SER A 1 413 ? 132.879 139.169 94.579  1.00 10.90 ?  413 SER A CB    1 
ATOM   3333  O  OG    . SER A 1 413 ? 133.404 138.727 95.815  1.00 29.53 ?  413 SER A OG    1 
ATOM   3334  N  N     . LEU A 1 414 ? 134.122 140.831 91.950  1.00 20.43 ?  414 LEU A N     1 
ATOM   3335  C  CA    . LEU A 1 414 ? 133.924 140.797 90.511  1.00 13.30 ?  414 LEU A CA    1 
ATOM   3336  C  C     . LEU A 1 414 ? 133.536 139.389 90.087  1.00 21.18 ?  414 LEU A C     1 
ATOM   3337  O  O     . LEU A 1 414 ? 134.067 138.403 90.603  1.00 21.96 ?  414 LEU A O     1 
ATOM   3338  C  CB    . LEU A 1 414 ? 135.194 141.221 89.776  1.00 14.83 ?  414 LEU A CB    1 
ATOM   3339  C  CG    . LEU A 1 414 ? 135.937 142.463 90.258  1.00 19.22 ?  414 LEU A CG    1 
ATOM   3340  C  CD1   . LEU A 1 414 ? 137.256 142.581 89.521  1.00 24.86 ?  414 LEU A CD1   1 
ATOM   3341  C  CD2   . LEU A 1 414 ? 135.092 143.703 90.045  1.00 24.81 ?  414 LEU A CD2   1 
ATOM   3342  N  N     . ASN A 1 415 ? 132.605 139.294 89.148  1.00 28.22 ?  415 ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 415 ? 132.277 138.020 88.522  1.00 25.19 ?  415 ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 415 ? 133.191 137.855 87.317  1.00 27.36 ?  415 ASN A C     1 
ATOM   3345  O  O     . ASN A 1 415 ? 133.008 138.525 86.297  1.00 29.83 ?  415 ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 415 ? 130.806 137.970 88.126  1.00 20.33 ?  415 ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 415 ? 130.307 136.559 87.907  1.00 23.73 ?  415 ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 415 ? 130.920 135.776 87.184  1.00 32.26 ?  415 ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 415 ? 129.186 136.227 88.530  1.00 30.02 ?  415 ASN A ND2   1 
ATOM   3350  N  N     . ILE A 1 416 ? 134.177 136.964 87.439  1.00 19.85 ?  416 ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 416 ? 135.203 136.834 86.409  1.00 22.02 ?  416 ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 416 ? 134.581 136.435 85.078  1.00 28.81 ?  416 ILE A C     1 
ATOM   3353  O  O     . ILE A 1 416 ? 134.971 136.940 84.018  1.00 26.69 ?  416 ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 416 ? 136.284 135.834 86.858  1.00 24.02 ?  416 ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 416 ? 137.047 136.388 88.062  1.00 21.73 ?  416 ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 416 ? 137.244 135.535 85.725  1.00 15.94 ?  416 ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 416 ? 137.966 135.392 88.721  1.00 19.62 ?  416 ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 417 ? 133.593 135.539 85.108  1.00 23.98 ?  417 LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 417 ? 132.956 135.097 83.871  1.00 27.03 ?  417 LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 417 ? 132.251 136.250 83.166  1.00 28.59 ?  417 LEU A C     1 
ATOM   3361  O  O     . LEU A 1 417 ? 132.442 136.467 81.964  1.00 36.05 ?  417 LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 417 ? 131.972 133.967 84.168  1.00 27.64 ?  417 LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 417 ? 131.447 133.183 82.966  1.00 25.66 ?  417 LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 417 ? 131.437 131.707 83.282  1.00 26.86 ?  417 LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 417 ? 130.057 133.654 82.585  1.00 32.99 ?  417 LEU A CD2   1 
ATOM   3366  N  N     . ASN A 1 418 ? 131.433 137.004 83.901  1.00 30.17 ?  418 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 418 ? 130.666 138.081 83.286  1.00 30.26 ?  418 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 418 ? 131.535 139.286 82.961  1.00 29.72 ?  418 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 418 ? 131.272 139.986 81.976  1.00 32.38 ?  418 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 418 ? 129.513 138.490 84.201  1.00 26.41 ?  418 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 418 ? 128.460 137.412 84.324  1.00 31.04 ?  418 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 418 ? 128.160 136.712 83.359  1.00 36.97 ?  418 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 418 ? 127.894 137.268 85.515  1.00 32.23 ?  418 ASN A ND2   1 
ATOM   3374  N  N     . VAL A 1 419 ? 132.559 139.548 83.772  1.00 29.60 ?  419 VAL A N     1 
ATOM   3375  C  CA    . VAL A 1 419 ? 133.495 140.625 83.463  1.00 28.99 ?  419 VAL A CA    1 
ATOM   3376  C  C     . VAL A 1 419 ? 134.276 140.304 82.197  1.00 31.93 ?  419 VAL A C     1 
ATOM   3377  O  O     . VAL A 1 419 ? 134.472 141.168 81.334  1.00 35.55 ?  419 VAL A O     1 
ATOM   3378  C  CB    . VAL A 1 419 ? 134.425 140.876 84.665  1.00 27.28 ?  419 VAL A CB    1 
ATOM   3379  C  CG1   . VAL A 1 419 ? 135.664 141.618 84.236  1.00 31.92 ?  419 VAL A CG1   1 
ATOM   3380  C  CG2   . VAL A 1 419 ? 133.695 141.649 85.742  1.00 27.21 ?  419 VAL A CG2   1 
ATOM   3381  N  N     . MET A 1 420 ? 134.726 139.054 82.058  1.00 37.60 ?  420 MET A N     1 
ATOM   3382  C  CA    . MET A 1 420 ? 135.479 138.656 80.874  1.00 31.13 ?  420 MET A CA    1 
ATOM   3383  C  C     . MET A 1 420 ? 134.594 138.587 79.638  1.00 29.91 ?  420 MET A C     1 
ATOM   3384  O  O     . MET A 1 420 ? 135.054 138.892 78.532  1.00 35.71 ?  420 MET A O     1 
ATOM   3385  C  CB    . MET A 1 420 ? 136.158 137.311 81.118  1.00 32.87 ?  420 MET A CB    1 
ATOM   3386  C  CG    . MET A 1 420 ? 137.427 137.404 81.944  1.00 30.68 ?  420 MET A CG    1 
ATOM   3387  S  SD    . MET A 1 420 ? 138.640 138.506 81.205  1.00 39.19 ?  420 MET A SD    1 
ATOM   3388  C  CE    . MET A 1 420 ? 139.380 137.422 79.990  1.00 30.33 ?  420 MET A CE    1 
ATOM   3389  N  N     . GLU A 1 421 ? 133.331 138.183 79.800  1.00 38.79 ?  421 GLU A N     1 
ATOM   3390  C  CA    . GLU A 1 421 ? 132.407 138.164 78.671  1.00 37.01 ?  421 GLU A CA    1 
ATOM   3391  C  C     . GLU A 1 421 ? 132.157 139.570 78.141  1.00 41.48 ?  421 GLU A C     1 
ATOM   3392  O  O     . GLU A 1 421 ? 132.101 139.782 76.924  1.00 43.64 ?  421 GLU A O     1 
ATOM   3393  C  CB    . GLU A 1 421 ? 131.091 137.508 79.084  1.00 35.64 ?  421 GLU A CB    1 
ATOM   3394  C  CG    . GLU A 1 421 ? 131.063 135.999 78.918  1.00 40.90 ?  421 GLU A CG    1 
ATOM   3395  C  CD    . GLU A 1 421 ? 129.735 135.396 79.333  1.00 46.28 ?  421 GLU A CD    1 
ATOM   3396  O  OE1   . GLU A 1 421 ? 128.943 136.104 79.989  1.00 45.01 ?  421 GLU A OE1   1 
ATOM   3397  O  OE2   . GLU A 1 421 ? 129.484 134.219 79.003  1.00 45.47 -1 421 GLU A OE2   1 
ATOM   3398  N  N     . HIS A 1 422 ? 132.005 140.541 79.039  1.00 37.78 ?  422 HIS A N     1 
ATOM   3399  C  CA    . HIS A 1 422 ? 131.742 141.920 78.653  1.00 34.71 ?  422 HIS A CA    1 
ATOM   3400  C  C     . HIS A 1 422 ? 133.005 142.689 78.295  1.00 39.06 ?  422 HIS A C     1 
ATOM   3401  O  O     . HIS A 1 422 ? 132.898 143.839 77.855  1.00 39.00 ?  422 HIS A O     1 
ATOM   3402  C  CB    . HIS A 1 422 ? 131.003 142.645 79.780  1.00 34.38 ?  422 HIS A CB    1 
ATOM   3403  C  CG    . HIS A 1 422 ? 129.633 142.109 80.048  1.00 36.59 ?  422 HIS A CG    1 
ATOM   3404  N  ND1   . HIS A 1 422 ? 129.398 141.088 80.942  1.00 36.17 ?  422 HIS A ND1   1 
ATOM   3405  C  CD2   . HIS A 1 422 ? 128.425 142.452 79.543  1.00 38.64 ?  422 HIS A CD2   1 
ATOM   3406  C  CE1   . HIS A 1 422 ? 128.105 140.822 80.976  1.00 39.68 ?  422 HIS A CE1   1 
ATOM   3407  N  NE2   . HIS A 1 422 ? 127.491 141.636 80.135  1.00 41.23 ?  422 HIS A NE2   1 
ATOM   3408  N  N     . LYS A 1 423 ? 134.182 142.086 78.466  1.00 42.93 ?  423 LYS A N     1 
ATOM   3409  C  CA    . LYS A 1 423 ? 135.461 142.748 78.214  1.00 43.56 ?  423 LYS A CA    1 
ATOM   3410  C  C     . LYS A 1 423 ? 135.540 144.076 78.962  1.00 43.41 ?  423 LYS A C     1 
ATOM   3411  O  O     . LYS A 1 423 ? 135.908 145.114 78.408  1.00 46.66 ?  423 LYS A O     1 
ATOM   3412  C  CB    . LYS A 1 423 ? 135.692 142.948 76.716  1.00 40.83 ?  423 LYS A CB    1 
ATOM   3413  C  CG    . LYS A 1 423 ? 135.472 141.700 75.882  1.00 42.34 ?  423 LYS A CG    1 
ATOM   3414  C  CD    . LYS A 1 423 ? 136.763 140.919 75.717  1.00 46.49 ?  423 LYS A CD    1 
ATOM   3415  C  CE    . LYS A 1 423 ? 136.493 139.475 75.328  1.00 46.50 ?  423 LYS A CE    1 
ATOM   3416  N  NZ    . LYS A 1 423 ? 136.320 138.598 76.518  1.00 44.64 1  423 LYS A NZ    1 
ATOM   3417  N  N     . SER A 1 424 ? 135.184 144.033 80.241  1.00 33.13 ?  424 SER A N     1 
ATOM   3418  C  CA    . SER A 1 424 ? 135.002 145.232 81.050  1.00 32.99 ?  424 SER A CA    1 
ATOM   3419  C  C     . SER A 1 424 ? 135.722 145.105 82.381  1.00 36.41 ?  424 SER A C     1 
ATOM   3420  O  O     . SER A 1 424 ? 135.158 145.366 83.443  1.00 39.49 ?  424 SER A O     1 
ATOM   3421  C  CB    . SER A 1 424 ? 133.519 145.505 81.278  1.00 35.65 ?  424 SER A CB    1 
ATOM   3422  O  OG    . SER A 1 424 ? 132.971 144.570 82.189  1.00 32.10 ?  424 SER A OG    1 
ATOM   3423  N  N     . ILE A 1 425 ? 136.991 144.693 82.349  1.00 34.09 ?  425 ILE A N     1 
ATOM   3424  C  CA    . ILE A 1 425 ? 137.769 144.635 83.583  1.00 28.18 ?  425 ILE A CA    1 
ATOM   3425  C  C     . ILE A 1 425 ? 137.957 146.035 84.154  1.00 31.11 ?  425 ILE A C     1 
ATOM   3426  O  O     . ILE A 1 425 ? 137.729 146.275 85.344  1.00 36.98 ?  425 ILE A O     1 
ATOM   3427  C  CB    . ILE A 1 425 ? 139.120 143.936 83.343  1.00 32.28 ?  425 ILE A CB    1 
ATOM   3428  C  CG1   . ILE A 1 425 ? 138.929 142.422 83.269  1.00 33.29 ?  425 ILE A CG1   1 
ATOM   3429  C  CG2   . ILE A 1 425 ? 140.108 144.286 84.443  1.00 28.28 ?  425 ILE A CG2   1 
ATOM   3430  C  CD1   . ILE A 1 425 ? 140.185 141.657 82.962  1.00 32.74 ?  425 ILE A CD1   1 
ATOM   3431  N  N     . GLU A 1 426 ? 138.346 146.986 83.304  1.00 28.74 ?  426 GLU A N     1 
ATOM   3432  C  CA    . GLU A 1 426 ? 138.643 148.336 83.775  1.00 27.28 ?  426 GLU A CA    1 
ATOM   3433  C  C     . GLU A 1 426 ? 137.411 149.005 84.370  1.00 30.36 ?  426 GLU A C     1 
ATOM   3434  O  O     . GLU A 1 426 ? 137.445 149.502 85.503  1.00 37.14 ?  426 GLU A O     1 
ATOM   3435  C  CB    . GLU A 1 426 ? 139.202 149.171 82.627  1.00 29.43 ?  426 GLU A CB    1 
ATOM   3436  C  CG    . GLU A 1 426 ? 139.178 150.665 82.878  1.00 33.41 ?  426 GLU A CG    1 
ATOM   3437  C  CD    . GLU A 1 426 ? 139.884 151.448 81.792  1.00 39.47 ?  426 GLU A CD    1 
ATOM   3438  O  OE1   . GLU A 1 426 ? 140.177 150.861 80.729  1.00 38.35 ?  426 GLU A OE1   1 
ATOM   3439  O  OE2   . GLU A 1 426 ? 140.147 152.650 82.002  1.00 38.54 -1 426 GLU A OE2   1 
ATOM   3440  N  N     . LYS A 1 427 ? 136.311 149.028 83.617  1.00 32.91 ?  427 LYS A N     1 
ATOM   3441  C  CA    . LYS A 1 427 ? 135.111 149.719 84.075  1.00 28.97 ?  427 LYS A CA    1 
ATOM   3442  C  C     . LYS A 1 427 ? 134.531 149.055 85.315  1.00 30.16 ?  427 LYS A C     1 
ATOM   3443  O  O     . LYS A 1 427 ? 134.127 149.743 86.259  1.00 36.77 ?  427 LYS A O     1 
ATOM   3444  C  CB    . LYS A 1 427 ? 134.045 149.804 82.970  1.00 34.40 ?  427 LYS A CB    1 
ATOM   3445  C  CG    . LYS A 1 427 ? 134.388 150.503 81.618  1.00 38.16 ?  427 LYS A CG    1 
ATOM   3446  C  CD    . LYS A 1 427 ? 135.704 150.157 80.910  1.00 38.84 ?  427 LYS A CD    1 
ATOM   3447  C  CE    . LYS A 1 427 ? 135.851 148.663 80.646  1.00 34.59 ?  427 LYS A CE    1 
ATOM   3448  N  NZ    . LYS A 1 427 ? 137.159 148.326 80.021  1.00 35.02 1  427 LYS A NZ    1 
ATOM   3449  N  N     . THR A 1 428 ? 134.483 147.722 85.334  1.00 29.14 ?  428 THR A N     1 
ATOM   3450  C  CA    . THR A 1 428 ? 133.961 147.026 86.504  1.00 22.10 ?  428 THR A CA    1 
ATOM   3451  C  C     . THR A 1 428 ? 134.823 147.286 87.730  1.00 28.69 ?  428 THR A C     1 
ATOM   3452  O  O     . THR A 1 428 ? 134.298 147.549 88.816  1.00 31.20 ?  428 THR A O     1 
ATOM   3453  C  CB    . THR A 1 428 ? 133.860 145.527 86.240  1.00 24.52 ?  428 THR A CB    1 
ATOM   3454  O  OG1   . THR A 1 428 ? 133.261 145.303 84.959  1.00 28.64 ?  428 THR A OG1   1 
ATOM   3455  C  CG2   . THR A 1 428 ? 133.013 144.866 87.309  1.00 25.65 ?  428 THR A CG2   1 
ATOM   3456  N  N     . VAL A 1 429 ? 136.147 147.227 87.576  1.00 28.73 ?  429 VAL A N     1 
ATOM   3457  C  CA    . VAL A 1 429 ? 137.031 147.441 88.718  1.00 22.63 ?  429 VAL A CA    1 
ATOM   3458  C  C     . VAL A 1 429 ? 136.884 148.861 89.247  1.00 23.97 ?  429 VAL A C     1 
ATOM   3459  O  O     . VAL A 1 429 ? 136.801 149.078 90.459  1.00 30.65 ?  429 VAL A O     1 
ATOM   3460  C  CB    . VAL A 1 429 ? 138.490 147.122 88.341  1.00 24.00 ?  429 VAL A CB    1 
ATOM   3461  C  CG1   . VAL A 1 429 ? 139.437 147.704 89.368  1.00 19.09 ?  429 VAL A CG1   1 
ATOM   3462  C  CG2   . VAL A 1 429 ? 138.696 145.625 88.246  1.00 23.11 ?  429 VAL A CG2   1 
ATOM   3463  N  N     . LYS A 1 430 ? 136.822 149.848 88.349  1.00 24.20 ?  430 LYS A N     1 
ATOM   3464  C  CA    . LYS A 1 430 ? 136.718 151.232 88.799  1.00 23.38 ?  430 LYS A CA    1 
ATOM   3465  C  C     . LYS A 1 430 ? 135.371 151.512 89.459  1.00 23.32 ?  430 LYS A C     1 
ATOM   3466  O  O     . LYS A 1 430 ? 135.311 152.177 90.500  1.00 31.57 ?  430 LYS A O     1 
ATOM   3467  C  CB    . LYS A 1 430 ? 136.966 152.180 87.627  1.00 24.45 ?  430 LYS A CB    1 
ATOM   3468  C  CG    . LYS A 1 430 ? 138.381 152.095 87.083  1.00 26.85 ?  430 LYS A CG    1 
ATOM   3469  C  CD    . LYS A 1 430 ? 138.751 153.316 86.270  1.00 29.76 ?  430 LYS A CD    1 
ATOM   3470  C  CE    . LYS A 1 430 ? 140.201 153.246 85.825  1.00 29.64 ?  430 LYS A CE    1 
ATOM   3471  N  NZ    . LYS A 1 430 ? 140.590 154.426 85.008  1.00 33.48 1  430 LYS A NZ    1 
ATOM   3472  N  N     . LEU A 1 431 ? 134.278 151.007 88.879  1.00 24.92 ?  431 LEU A N     1 
ATOM   3473  C  CA    . LEU A 1 431 ? 132.965 151.222 89.478  1.00 20.54 ?  431 LEU A CA    1 
ATOM   3474  C  C     . LEU A 1 431 ? 132.839 150.504 90.816  1.00 22.83 ?  431 LEU A C     1 
ATOM   3475  O  O     . LEU A 1 431 ? 132.246 151.038 91.760  1.00 28.68 ?  431 LEU A O     1 
ATOM   3476  C  CB    . LEU A 1 431 ? 131.873 150.761 88.515  1.00 27.17 ?  431 LEU A CB    1 
ATOM   3477  C  CG    . LEU A 1 431 ? 131.178 151.835 87.678  1.00 30.22 ?  431 LEU A CG    1 
ATOM   3478  C  CD1   . LEU A 1 431 ? 130.082 151.212 86.834  1.00 29.53 ?  431 LEU A CD1   1 
ATOM   3479  C  CD2   . LEU A 1 431 ? 130.617 152.931 88.564  1.00 31.29 ?  431 LEU A CD2   1 
ATOM   3480  N  N     . ALA A 1 432 ? 133.383 149.288 90.917  1.00 24.46 ?  432 ALA A N     1 
ATOM   3481  C  CA    . ALA A 1 432 ? 133.375 148.571 92.185  1.00 15.27 ?  432 ALA A CA    1 
ATOM   3482  C  C     . ALA A 1 432 ? 134.213 149.293 93.228  1.00 26.11 ?  432 ALA A C     1 
ATOM   3483  O  O     . ALA A 1 432 ? 133.849 149.332 94.407  1.00 28.99 ?  432 ALA A O     1 
ATOM   3484  C  CB    . ALA A 1 432 ? 133.886 147.146 91.981  1.00 21.06 ?  432 ALA A CB    1 
ATOM   3485  N  N     . THR A 1 433 ? 135.346 149.864 92.814  1.00 28.03 ?  433 THR A N     1 
ATOM   3486  C  CA    . THR A 1 433 ? 136.158 150.652 93.731  1.00 21.24 ?  433 THR A CA    1 
ATOM   3487  C  C     . THR A 1 433 ? 135.392 151.866 94.231  1.00 23.51 ?  433 THR A C     1 
ATOM   3488  O  O     . THR A 1 433 ? 135.443 152.194 95.420  1.00 34.90 ?  433 THR A O     1 
ATOM   3489  C  CB    . THR A 1 433 ? 137.455 151.080 93.044  1.00 27.47 ?  433 THR A CB    1 
ATOM   3490  O  OG1   . THR A 1 433 ? 138.186 149.917 92.635  1.00 29.32 ?  433 THR A OG1   1 
ATOM   3491  C  CG2   . THR A 1 433 ? 138.314 151.905 93.987  1.00 24.32 ?  433 THR A CG2   1 
ATOM   3492  N  N     . ASP A 1 434 ? 134.669 152.543 93.337  1.00 22.85 ?  434 ASP A N     1 
ATOM   3493  C  CA    . ASP A 1 434 ? 133.858 153.684 93.752  1.00 22.59 ?  434 ASP A CA    1 
ATOM   3494  C  C     . ASP A 1 434 ? 132.770 153.264 94.735  1.00 20.26 ?  434 ASP A C     1 
ATOM   3495  O  O     . ASP A 1 434 ? 132.533 153.944 95.741  1.00 24.84 ?  434 ASP A O     1 
ATOM   3496  C  CB    . ASP A 1 434 ? 133.239 154.359 92.530  1.00 24.86 ?  434 ASP A CB    1 
ATOM   3497  C  CG    . ASP A 1 434 ? 134.278 154.964 91.612  1.00 31.71 ?  434 ASP A CG    1 
ATOM   3498  O  OD1   . ASP A 1 434 ? 135.390 155.268 92.089  1.00 35.06 ?  434 ASP A OD1   1 
ATOM   3499  O  OD2   . ASP A 1 434 ? 133.981 155.140 90.411  1.00 33.12 -1 434 ASP A OD2   1 
ATOM   3500  N  N     . SER A 1 435 ? 132.093 152.147 94.458  1.00 22.09 ?  435 SER A N     1 
ATOM   3501  C  CA    . SER A 1 435 ? 131.036 151.678 95.350  1.00 20.46 ?  435 SER A CA    1 
ATOM   3502  C  C     . SER A 1 435 ? 131.590 151.296 96.717  1.00 23.29 ?  435 SER A C     1 
ATOM   3503  O  O     . SER A 1 435 ? 130.990 151.616 97.751  1.00 29.51 ?  435 SER A O     1 
ATOM   3504  C  CB    . SER A 1 435 ? 130.304 150.497 94.715  1.00 23.10 ?  435 SER A CB    1 
ATOM   3505  O  OG    . SER A 1 435 ? 131.082 149.318 94.785  1.00 20.02 ?  435 SER A OG    1 
ATOM   3506  N  N     . LEU A 1 436 ? 132.739 150.619 96.745  1.00 19.07 ?  436 LEU A N     1 
ATOM   3507  C  CA    . LEU A 1 436 ? 133.349 150.245 98.016  1.00 10.90 ?  436 LEU A CA    1 
ATOM   3508  C  C     . LEU A 1 436 ? 133.836 151.471 98.776  1.00 17.35 ?  436 LEU A C     1 
ATOM   3509  O  O     . LEU A 1 436 ? 133.750 151.519 100.007 1.00 21.46 ?  436 LEU A O     1 
ATOM   3510  C  CB    . LEU A 1 436 ? 134.492 149.262 97.772  1.00 22.54 ?  436 LEU A CB    1 
ATOM   3511  C  CG    . LEU A 1 436 ? 134.083 147.868 97.295  1.00 19.18 ?  436 LEU A CG    1 
ATOM   3512  C  CD1   . LEU A 1 436 ? 135.286 147.092 96.786  1.00 10.93 ?  436 LEU A CD1   1 
ATOM   3513  C  CD2   . LEU A 1 436 ? 133.382 147.105 98.400  1.00 20.99 ?  436 LEU A CD2   1 
ATOM   3514  N  N     . THR A 1 437 ? 134.348 152.474 98.059  1.00 23.18 ?  437 THR A N     1 
ATOM   3515  C  CA    . THR A 1 437 ? 134.722 153.731 98.697  1.00 21.46 ?  437 THR A CA    1 
ATOM   3516  C  C     . THR A 1 437 ? 133.513 154.408 99.325  1.00 24.16 ?  437 THR A C     1 
ATOM   3517  O  O     . THR A 1 437 ? 133.596 154.937 100.439 1.00 35.32 ?  437 THR A O     1 
ATOM   3518  C  CB    . THR A 1 437 ? 135.379 154.657 97.676  1.00 19.83 ?  437 THR A CB    1 
ATOM   3519  O  OG1   . THR A 1 437 ? 136.380 153.933 96.951  1.00 21.94 ?  437 THR A OG1   1 
ATOM   3520  C  CG2   . THR A 1 437 ? 136.017 155.846 98.365  1.00 22.56 ?  437 THR A CG2   1 
ATOM   3521  N  N     . HIS A 1 438 ? 132.380 154.406 98.622  1.00 21.99 ?  438 HIS A N     1 
ATOM   3522  C  CA    . HIS A 1 438 ? 131.166 154.990 99.182  1.00 23.39 ?  438 HIS A CA    1 
ATOM   3523  C  C     . HIS A 1 438 ? 130.707 154.229 100.419 1.00 23.90 ?  438 HIS A C     1 
ATOM   3524  O  O     . HIS A 1 438 ? 130.281 154.835 101.409 1.00 31.71 ?  438 HIS A O     1 
ATOM   3525  C  CB    . HIS A 1 438 ? 130.061 155.021 98.128  1.00 26.69 ?  438 HIS A CB    1 
ATOM   3526  C  CG    . HIS A 1 438 ? 128.751 155.522 98.649  1.00 27.28 ?  438 HIS A CG    1 
ATOM   3527  N  ND1   . HIS A 1 438 ? 128.466 156.864 98.776  1.00 27.32 ?  438 HIS A ND1   1 
ATOM   3528  C  CD2   . HIS A 1 438 ? 127.651 154.862 99.080  1.00 28.60 ?  438 HIS A CD2   1 
ATOM   3529  C  CE1   . HIS A 1 438 ? 127.247 157.009 99.262  1.00 31.76 ?  438 HIS A CE1   1 
ATOM   3530  N  NE2   . HIS A 1 438 ? 126.731 155.808 99.455  1.00 31.05 ?  438 HIS A NE2   1 
ATOM   3531  N  N     . VAL A 1 439 ? 130.782 152.896 100.380 1.00 25.03 ?  439 VAL A N     1 
ATOM   3532  C  CA    . VAL A 1 439 ? 130.394 152.102 101.543 1.00 20.09 ?  439 VAL A CA    1 
ATOM   3533  C  C     . VAL A 1 439 ? 131.311 152.401 102.723 1.00 27.11 ?  439 VAL A C     1 
ATOM   3534  O  O     . VAL A 1 439 ? 130.863 152.484 103.872 1.00 36.62 ?  439 VAL A O     1 
ATOM   3535  C  CB    . VAL A 1 439 ? 130.386 150.602 101.193 1.00 23.14 ?  439 VAL A CB    1 
ATOM   3536  C  CG1   . VAL A 1 439 ? 130.111 149.770 102.429 1.00 24.30 ?  439 VAL A CG1   1 
ATOM   3537  C  CG2   . VAL A 1 439 ? 129.346 150.316 100.133 1.00 25.36 ?  439 VAL A CG2   1 
ATOM   3538  N  N     . SER A 1 440 ? 132.607 152.568 102.458 1.00 25.44 ?  440 SER A N     1 
ATOM   3539  C  CA    . SER A 1 440 ? 133.541 152.940 103.517 1.00 20.24 ?  440 SER A CA    1 
ATOM   3540  C  C     . SER A 1 440 ? 133.206 154.311 104.088 1.00 26.38 ?  440 SER A C     1 
ATOM   3541  O  O     . SER A 1 440 ? 133.263 154.518 105.306 1.00 34.05 ?  440 SER A O     1 
ATOM   3542  C  CB    . SER A 1 440 ? 134.973 152.919 102.984 1.00 25.82 ?  440 SER A CB    1 
ATOM   3543  O  OG    . SER A 1 440 ? 135.915 152.921 104.043 1.00 30.51 ?  440 SER A OG    1 
ATOM   3544  N  N     . GLU A 1 441 ? 132.858 155.263 103.221 1.00 29.54 ?  441 GLU A N     1 
ATOM   3545  C  CA    . GLU A 1 441 ? 132.586 156.622 103.676 1.00 21.89 ?  441 GLU A CA    1 
ATOM   3546  C  C     . GLU A 1 441 ? 131.288 156.713 104.468 1.00 31.00 ?  441 GLU A C     1 
ATOM   3547  O  O     . GLU A 1 441 ? 131.184 157.533 105.386 1.00 40.06 ?  441 GLU A O     1 
ATOM   3548  C  CB    . GLU A 1 441 ? 132.545 157.571 102.481 1.00 22.46 ?  441 GLU A CB    1 
ATOM   3549  C  CG    . GLU A 1 441 ? 133.911 157.893 101.907 1.00 28.54 ?  441 GLU A CG    1 
ATOM   3550  C  CD    . GLU A 1 441 ? 133.830 158.728 100.648 1.00 38.58 ?  441 GLU A CD    1 
ATOM   3551  O  OE1   . GLU A 1 441 ? 133.433 158.185 99.594  1.00 38.78 ?  441 GLU A OE1   1 
ATOM   3552  O  OE2   . GLU A 1 441 ? 134.161 159.930 100.707 1.00 37.83 -1 441 GLU A OE2   1 
ATOM   3553  N  N     . THR A 1 442 ? 130.292 155.897 104.134 1.00 32.28 ?  442 THR A N     1 
ATOM   3554  C  CA    . THR A 1 442 ? 129.008 155.944 104.822 1.00 31.30 ?  442 THR A CA    1 
ATOM   3555  C  C     . THR A 1 442 ? 128.956 155.059 106.059 1.00 32.40 ?  442 THR A C     1 
ATOM   3556  O  O     . THR A 1 442 ? 127.929 155.035 106.742 1.00 38.71 ?  442 THR A O     1 
ATOM   3557  C  CB    . THR A 1 442 ? 127.873 155.551 103.869 1.00 30.83 ?  442 THR A CB    1 
ATOM   3558  O  OG1   . THR A 1 442 ? 128.054 154.197 103.435 1.00 30.72 ?  442 THR A OG1   1 
ATOM   3559  C  CG2   . THR A 1 442 ? 127.848 156.473 102.664 1.00 30.57 ?  442 THR A CG2   1 
ATOM   3560  N  N     . THR A 1 443 ? 130.027 154.333 106.363 1.00 31.71 ?  443 THR A N     1 
ATOM   3561  C  CA    . THR A 1 443 ? 130.078 153.501 107.556 1.00 34.28 ?  443 THR A CA    1 
ATOM   3562  C  C     . THR A 1 443 ? 130.602 154.319 108.728 1.00 37.40 ?  443 THR A C     1 
ATOM   3563  O  O     . THR A 1 443 ? 131.639 154.981 108.617 1.00 39.22 ?  443 THR A O     1 
ATOM   3564  C  CB    . THR A 1 443 ? 130.965 152.277 107.326 1.00 33.99 ?  443 THR A CB    1 
ATOM   3565  O  OG1   . THR A 1 443 ? 130.382 151.446 106.314 1.00 38.06 ?  443 THR A OG1   1 
ATOM   3566  C  CG2   . THR A 1 443 ? 131.107 151.476 108.607 1.00 30.56 ?  443 THR A CG2   1 
ATOM   3567  N  N     . ASP A 1 444 ? 129.880 154.277 109.847 1.00 42.90 ?  444 ASP A N     1 
ATOM   3568  C  CA    . ASP A 1 444 ? 130.274 154.998 111.058 1.00 42.22 ?  444 ASP A CA    1 
ATOM   3569  C  C     . ASP A 1 444 ? 129.907 154.135 112.260 1.00 41.14 ?  444 ASP A C     1 
ATOM   3570  O  O     . ASP A 1 444 ? 128.751 154.117 112.690 1.00 42.24 ?  444 ASP A O     1 
ATOM   3571  C  CB    . ASP A 1 444 ? 129.606 156.366 111.130 1.00 43.39 ?  444 ASP A CB    1 
ATOM   3572  C  CG    . ASP A 1 444 ? 130.495 157.413 111.767 1.00 46.17 ?  444 ASP A CG    1 
ATOM   3573  O  OD1   . ASP A 1 444 ? 130.862 157.241 112.947 1.00 45.39 ?  444 ASP A OD1   1 
ATOM   3574  O  OD2   . ASP A 1 444 ? 130.828 158.407 111.089 1.00 47.95 -1 444 ASP A OD2   1 
ATOM   3575  N  N     . ILE A 1 445 ? 130.894 153.425 112.798 1.00 38.07 ?  445 ILE A N     1 
ATOM   3576  C  CA    . ILE A 1 445 ? 130.699 152.571 113.964 1.00 40.95 ?  445 ILE A CA    1 
ATOM   3577  C  C     . ILE A 1 445 ? 130.941 153.426 115.203 1.00 44.55 ?  445 ILE A C     1 
ATOM   3578  O  O     . ILE A 1 445 ? 132.075 153.818 115.486 1.00 44.52 ?  445 ILE A O     1 
ATOM   3579  C  CB    . ILE A 1 445 ? 131.633 151.356 113.934 1.00 39.74 ?  445 ILE A CB    1 
ATOM   3580  C  CG1   . ILE A 1 445 ? 131.566 150.670 112.568 1.00 37.73 ?  445 ILE A CG1   1 
ATOM   3581  C  CG2   . ILE A 1 445 ? 131.281 150.388 115.051 1.00 39.98 ?  445 ILE A CG2   1 
ATOM   3582  C  CD1   . ILE A 1 445 ? 130.509 149.594 112.461 1.00 37.05 ?  445 ILE A CD1   1 
ATOM   3583  N  N     . ARG A 1 446 ? 129.874 153.711 115.949 1.00 47.24 ?  446 ARG A N     1 
ATOM   3584  C  CA    . ARG A 1 446 ? 129.935 154.628 117.078 1.00 50.94 ?  446 ARG A CA    1 
ATOM   3585  C  C     . ARG A 1 446 ? 130.110 153.909 118.412 1.00 49.67 ?  446 ARG A C     1 
ATOM   3586  O  O     . ARG A 1 446 ? 129.924 154.523 119.468 1.00 45.92 ?  446 ARG A O     1 
ATOM   3587  C  CB    . ARG A 1 446 ? 128.687 155.513 117.103 1.00 47.16 ?  446 ARG A CB    1 
ATOM   3588  C  CG    . ARG A 1 446 ? 127.378 154.753 116.970 1.00 46.72 ?  446 ARG A CG    1 
ATOM   3589  C  CD    . ARG A 1 446 ? 126.233 155.677 116.573 1.00 50.06 ?  446 ARG A CD    1 
ATOM   3590  N  NE    . ARG A 1 446 ? 126.476 156.340 115.295 1.00 52.22 ?  446 ARG A NE    1 
ATOM   3591  C  CZ    . ARG A 1 446 ? 126.902 157.588 115.162 1.00 52.70 ?  446 ARG A CZ    1 
ATOM   3592  N  NH1   . ARG A 1 446 ? 127.129 158.358 116.213 1.00 49.54 1  446 ARG A NH1   1 
ATOM   3593  N  NH2   . ARG A 1 446 ? 127.105 158.078 113.942 1.00 51.25 ?  446 ARG A NH2   1 
ATOM   3594  N  N     . ASN A 1 447 ? 130.464 152.625 118.385 1.00 39.92 ?  447 ASN A N     1 
ATOM   3595  C  CA    . ASN A 1 447 ? 130.782 151.890 119.599 1.00 34.85 ?  447 ASN A CA    1 
ATOM   3596  C  C     . ASN A 1 447 ? 132.100 151.138 119.507 1.00 35.19 ?  447 ASN A C     1 
ATOM   3597  O  O     . ASN A 1 447 ? 132.475 150.457 120.468 1.00 36.74 ?  447 ASN A O     1 
ATOM   3598  C  CB    . ASN A 1 447 ? 129.654 150.908 119.946 1.00 34.46 ?  447 ASN A CB    1 
ATOM   3599  C  CG    . ASN A 1 447 ? 128.890 151.321 121.185 1.00 33.05 ?  447 ASN A CG    1 
ATOM   3600  O  OD1   . ASN A 1 447 ? 129.480 151.578 122.234 1.00 37.76 ?  447 ASN A OD1   1 
ATOM   3601  N  ND2   . ASN A 1 447 ? 127.572 151.396 121.070 1.00 34.04 ?  447 ASN A ND2   1 
ATOM   3602  N  N     . ALA A 1 448 ? 132.810 151.237 118.384 1.00 38.72 ?  448 ALA A N     1 
ATOM   3603  C  CA    . ALA A 1 448 ? 134.149 150.677 118.213 1.00 33.62 ?  448 ALA A CA    1 
ATOM   3604  C  C     . ALA A 1 448 ? 135.052 151.823 117.783 1.00 33.26 ?  448 ALA A C     1 
ATOM   3605  O  O     . ALA A 1 448 ? 135.182 152.106 116.581 1.00 33.62 ?  448 ALA A O     1 
ATOM   3606  C  CB    . ALA A 1 448 ? 134.154 149.543 117.192 1.00 29.25 ?  448 ALA A CB    1 
ATOM   3607  N  N     . PRO A 1 449 ? 135.677 152.527 118.731 1.00 30.75 ?  449 PRO A N     1 
ATOM   3608  C  CA    . PRO A 1 449 ? 136.433 153.738 118.366 1.00 27.60 ?  449 PRO A CA    1 
ATOM   3609  C  C     . PRO A 1 449 ? 137.579 153.479 117.406 1.00 29.34 ?  449 PRO A C     1 
ATOM   3610  O  O     . PRO A 1 449 ? 137.812 154.283 116.495 1.00 29.06 ?  449 PRO A O     1 
ATOM   3611  C  CB    . PRO A 1 449 ? 136.940 154.256 119.720 1.00 27.90 ?  449 PRO A CB    1 
ATOM   3612  C  CG    . PRO A 1 449 ? 136.173 153.505 120.754 1.00 31.86 ?  449 PRO A CG    1 
ATOM   3613  C  CD    . PRO A 1 449 ? 135.801 152.203 120.160 1.00 30.43 ?  449 PRO A CD    1 
ATOM   3614  N  N     . ALA A 1 450 ? 138.300 152.370 117.580 1.00 31.60 ?  450 ALA A N     1 
ATOM   3615  C  CA    . ALA A 1 450 ? 139.436 152.091 116.713 1.00 23.57 ?  450 ALA A CA    1 
ATOM   3616  C  C     . ALA A 1 450 ? 138.986 151.667 115.324 1.00 25.16 ?  450 ALA A C     1 
ATOM   3617  O  O     . ALA A 1 450 ? 139.632 152.021 114.332 1.00 27.25 ?  450 ALA A O     1 
ATOM   3618  C  CB    . ALA A 1 450 ? 140.327 151.023 117.343 1.00 24.69 ?  450 ALA A CB    1 
ATOM   3619  N  N     . VAL A 1 451 ? 137.880 150.926 115.231 1.00 30.39 ?  451 VAL A N     1 
ATOM   3620  C  CA    . VAL A 1 451 ? 137.318 150.581 113.928 1.00 23.44 ?  451 VAL A CA    1 
ATOM   3621  C  C     . VAL A 1 451 ? 136.916 151.844 113.178 1.00 24.66 ?  451 VAL A C     1 
ATOM   3622  O  O     . VAL A 1 451 ? 137.212 152.003 111.989 1.00 30.89 ?  451 VAL A O     1 
ATOM   3623  C  CB    . VAL A 1 451 ? 136.128 149.619 114.097 1.00 25.62 ?  451 VAL A CB    1 
ATOM   3624  C  CG1   . VAL A 1 451 ? 135.289 149.573 112.833 1.00 26.43 ?  451 VAL A CG1   1 
ATOM   3625  C  CG2   . VAL A 1 451 ? 136.618 148.232 114.463 1.00 25.40 ?  451 VAL A CG2   1 
ATOM   3626  N  N     . ARG A 1 452 ? 136.249 152.768 113.871 1.00 24.67 ?  452 ARG A N     1 
ATOM   3627  C  CA    . ARG A 1 452 ? 135.844 154.026 113.252 1.00 25.38 ?  452 ARG A CA    1 
ATOM   3628  C  C     . ARG A 1 452 ? 137.055 154.836 112.806 1.00 26.48 ?  452 ARG A C     1 
ATOM   3629  O  O     . ARG A 1 452 ? 137.090 155.362 111.685 1.00 31.93 ?  452 ARG A O     1 
ATOM   3630  C  CB    . ARG A 1 452 ? 134.992 154.827 114.238 1.00 26.48 ?  452 ARG A CB    1 
ATOM   3631  C  CG    . ARG A 1 452 ? 133.950 155.727 113.604 1.00 29.65 ?  452 ARG A CG    1 
ATOM   3632  C  CD    . ARG A 1 452 ? 134.112 157.157 114.084 1.00 28.18 ?  452 ARG A CD    1 
ATOM   3633  N  NE    . ARG A 1 452 ? 133.703 157.323 115.472 1.00 37.09 ?  452 ARG A NE    1 
ATOM   3634  C  CZ    . ARG A 1 452 ? 132.501 157.733 115.857 1.00 39.49 ?  452 ARG A CZ    1 
ATOM   3635  N  NH1   . ARG A 1 452 ? 131.559 158.033 114.979 1.00 35.94 1  452 ARG A NH1   1 
ATOM   3636  N  NH2   . ARG A 1 452 ? 132.242 157.849 117.156 1.00 36.35 ?  452 ARG A NH2   1 
ATOM   3637  N  N     . ARG A 1 453 ? 138.066 154.942 113.672 1.00 27.41 ?  453 ARG A N     1 
ATOM   3638  C  CA    . ARG A 1 453 ? 139.246 155.734 113.336 1.00 24.98 ?  453 ARG A CA    1 
ATOM   3639  C  C     . ARG A 1 453 ? 139.991 155.139 112.150 1.00 30.87 ?  453 ARG A C     1 
ATOM   3640  O  O     . ARG A 1 453 ? 140.419 155.868 111.249 1.00 35.58 ?  453 ARG A O     1 
ATOM   3641  C  CB    . ARG A 1 453 ? 140.169 155.845 114.549 1.00 26.76 ?  453 ARG A CB    1 
ATOM   3642  C  CG    . ARG A 1 453 ? 141.286 156.858 114.376 1.00 30.43 ?  453 ARG A CG    1 
ATOM   3643  C  CD    . ARG A 1 453 ? 142.419 156.614 115.354 1.00 27.05 ?  453 ARG A CD    1 
ATOM   3644  N  NE    . ARG A 1 453 ? 143.680 157.151 114.859 1.00 29.09 ?  453 ARG A NE    1 
ATOM   3645  C  CZ    . ARG A 1 453 ? 144.871 156.635 115.126 1.00 30.96 ?  453 ARG A CZ    1 
ATOM   3646  N  NH1   . ARG A 1 453 ? 145.005 155.569 115.897 1.00 31.00 1  453 ARG A NH1   1 
ATOM   3647  N  NH2   . ARG A 1 453 ? 145.955 157.202 114.606 1.00 30.21 ?  453 ARG A NH2   1 
ATOM   3648  N  N     . ALA A 1 454 ? 140.149 153.813 112.127 1.00 26.81 ?  454 ALA A N     1 
ATOM   3649  C  CA    . ALA A 1 454 ? 140.853 153.177 111.022 1.00 20.64 ?  454 ALA A CA    1 
ATOM   3650  C  C     . ALA A 1 454 ? 140.043 153.224 109.736 1.00 19.20 ?  454 ALA A C     1 
ATOM   3651  O  O     . ALA A 1 454 ? 140.621 153.294 108.650 1.00 25.25 ?  454 ALA A O     1 
ATOM   3652  C  CB    . ALA A 1 454 ? 141.204 151.737 111.380 1.00 23.13 ?  454 ALA A CB    1 
ATOM   3653  N  N     . ASN A 1 455 ? 138.713 153.187 109.829 1.00 23.57 ?  455 ASN A N     1 
ATOM   3654  C  CA    . ASN A 1 455 ? 137.899 153.349 108.632 1.00 23.02 ?  455 ASN A CA    1 
ATOM   3655  C  C     . ASN A 1 455 ? 138.041 154.751 108.059 1.00 26.24 ?  455 ASN A C     1 
ATOM   3656  O  O     . ASN A 1 455 ? 138.091 154.926 106.836 1.00 32.44 ?  455 ASN A O     1 
ATOM   3657  C  CB    . ASN A 1 455 ? 136.437 153.038 108.945 1.00 21.33 ?  455 ASN A CB    1 
ATOM   3658  C  CG    . ASN A 1 455 ? 135.556 153.094 107.715 1.00 27.83 ?  455 ASN A CG    1 
ATOM   3659  O  OD1   . ASN A 1 455 ? 135.728 152.312 106.781 1.00 34.90 ?  455 ASN A OD1   1 
ATOM   3660  N  ND2   . ASN A 1 455 ? 134.608 154.020 107.706 1.00 26.61 ?  455 ASN A ND2   1 
ATOM   3661  N  N     . LYS A 1 456 ? 138.100 155.764 108.925 1.00 29.69 ?  456 LYS A N     1 
ATOM   3662  C  CA    . LYS A 1 456 ? 138.271 157.128 108.434 1.00 26.25 ?  456 LYS A CA    1 
ATOM   3663  C  C     . LYS A 1 456 ? 139.676 157.359 107.888 1.00 27.17 ?  456 LYS A C     1 
ATOM   3664  O  O     . LYS A 1 456 ? 139.853 158.091 106.908 1.00 31.74 ?  456 LYS A O     1 
ATOM   3665  C  CB    . LYS A 1 456 ? 137.955 158.133 109.540 1.00 26.62 ?  456 LYS A CB    1 
ATOM   3666  C  CG    . LYS A 1 456 ? 136.550 158.018 110.097 1.00 29.67 ?  456 LYS A CG    1 
ATOM   3667  C  CD    . LYS A 1 456 ? 136.189 159.229 110.937 1.00 34.00 ?  456 LYS A CD    1 
ATOM   3668  C  CE    . LYS A 1 456 ? 134.700 159.272 111.228 1.00 32.56 ?  456 LYS A CE    1 
ATOM   3669  N  NZ    . LYS A 1 456 ? 133.889 158.921 110.030 1.00 33.57 1  456 LYS A NZ    1 
ATOM   3670  N  N     . ALA A 1 457 ? 140.689 156.746 108.501 1.00 26.25 ?  457 ALA A N     1 
ATOM   3671  C  CA    . ALA A 1 457 ? 142.073 157.034 108.146 1.00 22.46 ?  457 ALA A CA    1 
ATOM   3672  C  C     . ALA A 1 457 ? 142.583 156.173 106.994 1.00 27.03 ?  457 ALA A C     1 
ATOM   3673  O  O     . ALA A 1 457 ? 143.100 156.700 106.005 1.00 31.58 ?  457 ALA A O     1 
ATOM   3674  C  CB    . ALA A 1 457 ? 142.971 156.851 109.373 1.00 22.61 ?  457 ALA A CB    1 
ATOM   3675  N  N     . MET A 1 458 ? 142.452 154.852 107.109 1.00 29.41 ?  458 MET A N     1 
ATOM   3676  C  CA    . MET A 1 458 ? 142.995 153.943 106.108 1.00 19.45 ?  458 MET A CA    1 
ATOM   3677  C  C     . MET A 1 458 ? 142.157 153.926 104.836 1.00 21.76 ?  458 MET A C     1 
ATOM   3678  O  O     . MET A 1 458 ? 142.707 153.807 103.736 1.00 29.94 ?  458 MET A O     1 
ATOM   3679  C  CB    . MET A 1 458 ? 143.097 152.532 106.687 1.00 22.04 ?  458 MET A CB    1 
ATOM   3680  C  CG    . MET A 1 458 ? 143.763 152.469 108.047 1.00 22.23 ?  458 MET A CG    1 
ATOM   3681  S  SD    . MET A 1 458 ? 145.498 152.942 107.975 1.00 33.05 ?  458 MET A SD    1 
ATOM   3682  C  CE    . MET A 1 458 ? 146.273 151.332 107.859 1.00 25.27 ?  458 MET A CE    1 
ATOM   3683  N  N     . LYS A 1 459 ? 140.834 154.034 104.968 1.00 17.12 ?  459 LYS A N     1 
ATOM   3684  C  CA    . LYS A 1 459 ? 139.916 153.959 103.829 1.00 21.91 ?  459 LYS A CA    1 
ATOM   3685  C  C     . LYS A 1 459 ? 140.118 152.667 103.041 1.00 17.93 ?  459 LYS A C     1 
ATOM   3686  O  O     . LYS A 1 459 ? 140.120 152.663 101.809 1.00 25.40 ?  459 LYS A O     1 
ATOM   3687  C  CB    . LYS A 1 459 ? 140.059 155.180 102.919 1.00 21.80 ?  459 LYS A CB    1 
ATOM   3688  C  CG    . LYS A 1 459 ? 140.020 156.506 103.652 1.00 24.86 ?  459 LYS A CG    1 
ATOM   3689  C  CD    . LYS A 1 459 ? 140.940 157.517 103.000 1.00 25.02 ?  459 LYS A CD    1 
ATOM   3690  C  CE    . LYS A 1 459 ? 140.918 158.839 103.739 1.00 28.55 ?  459 LYS A CE    1 
ATOM   3691  N  NZ    . LYS A 1 459 ? 141.940 159.780 103.207 1.00 31.75 1  459 LYS A NZ    1 
ATOM   3692  N  N     . SER A 1 460 ? 140.289 151.561 103.759 1.00 20.38 ?  460 SER A N     1 
ATOM   3693  C  CA    . SER A 1 460 ? 140.568 150.277 103.133 1.00 14.03 ?  460 SER A CA    1 
ATOM   3694  C  C     . SER A 1 460 ? 139.297 149.658 102.571 1.00 20.49 ?  460 SER A C     1 
ATOM   3695  O  O     . SER A 1 460 ? 138.228 149.728 103.183 1.00 29.78 ?  460 SER A O     1 
ATOM   3696  C  CB    . SER A 1 460 ? 141.206 149.320 104.138 1.00 8.71  ?  460 SER A CB    1 
ATOM   3697  O  OG    . SER A 1 460 ? 142.280 149.937 104.822 1.00 30.12 ?  460 SER A OG    1 
ATOM   3698  N  N     . ILE A 1 461 ? 139.423 149.046 101.396 1.00 13.07 ?  461 ILE A N     1 
ATOM   3699  C  CA    . ILE A 1 461 ? 138.335 148.318 100.763 1.00 14.90 ?  461 ILE A CA    1 
ATOM   3700  C  C     . ILE A 1 461 ? 138.856 146.947 100.363 1.00 15.17 ?  461 ILE A C     1 
ATOM   3701  O  O     . ILE A 1 461 ? 140.061 146.726 100.236 1.00 22.96 ?  461 ILE A O     1 
ATOM   3702  C  CB    . ILE A 1 461 ? 137.765 149.057 99.533  1.00 14.02 ?  461 ILE A CB    1 
ATOM   3703  C  CG1   . ILE A 1 461 ? 138.852 149.241 98.473  1.00 7.16  ?  461 ILE A CG1   1 
ATOM   3704  C  CG2   . ILE A 1 461 ? 137.178 150.398 99.940  1.00 14.31 ?  461 ILE A CG2   1 
ATOM   3705  C  CD1   . ILE A 1 461 ? 138.381 149.955 97.236  1.00 7.09  ?  461 ILE A CD1   1 
ATOM   3706  N  N     . GLY A 1 462 ? 137.929 146.013 100.186 1.00 16.88 ?  462 GLY A N     1 
ATOM   3707  C  CA    . GLY A 1 462 ? 138.298 144.717 99.657  1.00 8.05  ?  462 GLY A CA    1 
ATOM   3708  C  C     . GLY A 1 462 ? 137.526 144.367 98.406  1.00 5.76  ?  462 GLY A C     1 
ATOM   3709  O  O     . GLY A 1 462 ? 136.321 144.113 98.469  1.00 24.60 ?  462 GLY A O     1 
ATOM   3710  N  N     . LEU A 1 463 ? 138.208 144.335 97.268  1.00 13.49 ?  463 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 463 ? 137.592 143.980 95.996  1.00 11.99 ?  463 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 463 ? 138.071 142.588 95.609  1.00 15.77 ?  463 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 463 ? 139.219 142.411 95.193  1.00 27.78 ?  463 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 463 ? 137.930 145.005 94.915  1.00 18.12 ?  463 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 463 ? 137.361 144.728 93.521  1.00 17.19 ?  463 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 463 ? 135.866 144.468 93.593  1.00 7.19  ?  463 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 463 ? 137.664 145.878 92.575  1.00 15.33 ?  463 LEU A CD2   1 
ATOM   3718  N  N     . GLY A 1 464 ? 137.189 141.601 95.752  1.00 17.43 ?  464 GLY A N     1 
ATOM   3719  C  CA    . GLY A 1 464 ? 137.498 140.231 95.417  1.00 11.70 ?  464 GLY A CA    1 
ATOM   3720  C  C     . GLY A 1 464 ? 136.960 139.833 94.056  1.00 11.76 ?  464 GLY A C     1 
ATOM   3721  O  O     . GLY A 1 464 ? 136.471 140.650 93.274  1.00 18.98 ?  464 GLY A O     1 
ATOM   3722  N  N     . ALA A 1 465 ? 137.065 138.539 93.776  1.00 14.71 ?  465 ALA A N     1 
ATOM   3723  C  CA    . ALA A 1 465 ? 136.540 137.970 92.549  1.00 11.19 ?  465 ALA A CA    1 
ATOM   3724  C  C     . ALA A 1 465 ? 135.977 136.591 92.849  1.00 16.81 ?  465 ALA A C     1 
ATOM   3725  O  O     . ALA A 1 465 ? 136.351 135.947 93.832  1.00 29.03 ?  465 ALA A O     1 
ATOM   3726  C  CB    . ALA A 1 465 ? 137.615 137.890 91.459  1.00 15.71 ?  465 ALA A CB    1 
ATOM   3727  N  N     . MET A 1 466 ? 135.057 136.149 91.996  1.00 22.27 ?  466 MET A N     1 
ATOM   3728  C  CA    . MET A 1 466 ? 134.517 134.801 92.064  1.00 21.62 ?  466 MET A CA    1 
ATOM   3729  C  C     . MET A 1 466 ? 134.353 134.277 90.645  1.00 19.91 ?  466 MET A C     1 
ATOM   3730  O  O     . MET A 1 466 ? 134.663 134.966 89.667  1.00 23.91 ?  466 MET A O     1 
ATOM   3731  C  CB    . MET A 1 466 ? 133.182 134.750 92.811  1.00 26.40 ?  466 MET A CB    1 
ATOM   3732  C  CG    . MET A 1 466 ? 132.170 135.784 92.370  1.00 27.60 ?  466 MET A CG    1 
ATOM   3733  S  SD    . MET A 1 466 ? 130.635 135.617 93.294  1.00 40.18 ?  466 MET A SD    1 
ATOM   3734  C  CE    . MET A 1 466 ? 130.086 137.311 93.331  1.00 26.82 ?  466 MET A CE    1 
ATOM   3735  N  N     . ASN A 1 467 ? 133.857 133.043 90.542  1.00 20.36 ?  467 ASN A N     1 
ATOM   3736  C  CA    . ASN A 1 467 ? 133.604 132.383 89.263  1.00 20.74 ?  467 ASN A CA    1 
ATOM   3737  C  C     . ASN A 1 467 ? 134.887 132.165 88.468  1.00 21.97 ?  467 ASN A C     1 
ATOM   3738  O  O     . ASN A 1 467 ? 134.862 132.107 87.239  1.00 27.77 ?  467 ASN A O     1 
ATOM   3739  C  CB    . ASN A 1 467 ? 132.585 133.156 88.421  1.00 21.02 ?  467 ASN A CB    1 
ATOM   3740  C  CG    . ASN A 1 467 ? 131.553 132.255 87.784  1.00 26.60 ?  467 ASN A CG    1 
ATOM   3741  O  OD1   . ASN A 1 467 ? 131.507 131.058 88.057  1.00 30.58 ?  467 ASN A OD1   1 
ATOM   3742  N  ND2   . ASN A 1 467 ? 130.710 132.828 86.941  1.00 28.87 ?  467 ASN A ND2   1 
ATOM   3743  N  N     . LEU A 1 468 ? 136.024 132.049 89.158  1.00 17.20 ?  468 LEU A N     1 
ATOM   3744  C  CA    . LEU A 1 468 ? 137.263 131.713 88.466  1.00 18.24 ?  468 LEU A CA    1 
ATOM   3745  C  C     . LEU A 1 468 ? 137.203 130.299 87.906  1.00 22.11 ?  468 LEU A C     1 
ATOM   3746  O  O     . LEU A 1 468 ? 137.470 130.077 86.718  1.00 24.19 ?  468 LEU A O     1 
ATOM   3747  C  CB    . LEU A 1 468 ? 138.454 131.866 89.412  1.00 22.48 ?  468 LEU A CB    1 
ATOM   3748  C  CG    . LEU A 1 468 ? 139.775 131.298 88.885  1.00 20.24 ?  468 LEU A CG    1 
ATOM   3749  C  CD1   . LEU A 1 468 ? 140.345 132.179 87.790  1.00 17.75 ?  468 LEU A CD1   1 
ATOM   3750  C  CD2   . LEU A 1 468 ? 140.780 131.114 90.004  1.00 14.67 ?  468 LEU A CD2   1 
ATOM   3751  N  N     . HIS A 1 469 ? 136.836 129.329 88.746  1.00 25.00 ?  469 HIS A N     1 
ATOM   3752  C  CA    . HIS A 1 469 ? 136.712 127.958 88.270  1.00 15.91 ?  469 HIS A CA    1 
ATOM   3753  C  C     . HIS A 1 469 ? 135.562 127.822 87.285  1.00 25.43 ?  469 HIS A C     1 
ATOM   3754  O  O     . HIS A 1 469 ? 135.662 127.067 86.315  1.00 35.75 ?  469 HIS A O     1 
ATOM   3755  C  CB    . HIS A 1 469 ? 136.528 126.997 89.442  1.00 20.66 ?  469 HIS A CB    1 
ATOM   3756  C  CG    . HIS A 1 469 ? 136.674 125.555 89.064  1.00 24.47 ?  469 HIS A CG    1 
ATOM   3757  N  ND1   . HIS A 1 469 ? 136.399 124.525 89.935  1.00 30.41 ?  469 HIS A ND1   1 
ATOM   3758  C  CD2   . HIS A 1 469 ? 137.075 124.973 87.909  1.00 25.57 ?  469 HIS A CD2   1 
ATOM   3759  C  CE1   . HIS A 1 469 ? 136.617 123.371 89.332  1.00 26.91 ?  469 HIS A CE1   1 
ATOM   3760  N  NE2   . HIS A 1 469 ? 137.028 123.615 88.101  1.00 23.55 ?  469 HIS A NE2   1 
ATOM   3761  N  N     . GLY A 1 470 ? 134.461 128.536 87.517  1.00 23.18 ?  470 GLY A N     1 
ATOM   3762  C  CA    . GLY A 1 470 ? 133.364 128.501 86.563  1.00 18.91 ?  470 GLY A CA    1 
ATOM   3763  C  C     . GLY A 1 470 ? 133.771 129.027 85.201  1.00 13.76 ?  470 GLY A C     1 
ATOM   3764  O  O     . GLY A 1 470 ? 133.460 128.426 84.170  1.00 30.84 ?  470 GLY A O     1 
ATOM   3765  N  N     . TYR A 1 471 ? 134.489 130.152 85.184  1.00 17.80 ?  471 TYR A N     1 
ATOM   3766  C  CA    . TYR A 1 471 ? 134.956 130.716 83.924  1.00 20.66 ?  471 TYR A CA    1 
ATOM   3767  C  C     . TYR A 1 471 ? 135.935 129.781 83.227  1.00 26.74 ?  471 TYR A C     1 
ATOM   3768  O  O     . TYR A 1 471 ? 135.866 129.600 82.007  1.00 30.29 ?  471 TYR A O     1 
ATOM   3769  C  CB    . TYR A 1 471 ? 135.603 132.080 84.165  1.00 21.83 ?  471 TYR A CB    1 
ATOM   3770  C  CG    . TYR A 1 471 ? 136.220 132.685 82.927  1.00 25.96 ?  471 TYR A CG    1 
ATOM   3771  C  CD1   . TYR A 1 471 ? 135.427 133.271 81.952  1.00 25.94 ?  471 TYR A CD1   1 
ATOM   3772  C  CD2   . TYR A 1 471 ? 137.592 132.659 82.727  1.00 20.53 ?  471 TYR A CD2   1 
ATOM   3773  C  CE1   . TYR A 1 471 ? 135.983 133.821 80.817  1.00 26.67 ?  471 TYR A CE1   1 
ATOM   3774  C  CE2   . TYR A 1 471 ? 138.157 133.204 81.593  1.00 20.47 ?  471 TYR A CE2   1 
ATOM   3775  C  CZ    . TYR A 1 471 ? 137.348 133.784 80.643  1.00 28.50 ?  471 TYR A CZ    1 
ATOM   3776  O  OH    . TYR A 1 471 ? 137.908 134.330 79.513  1.00 31.36 ?  471 TYR A OH    1 
ATOM   3777  N  N     . LEU A 1 472 ? 136.858 129.182 83.983  1.00 22.56 ?  472 LEU A N     1 
ATOM   3778  C  CA    . LEU A 1 472 ? 137.842 128.294 83.370  1.00 21.54 ?  472 LEU A CA    1 
ATOM   3779  C  C     . LEU A 1 472 ? 137.194 127.021 82.838  1.00 26.87 ?  472 LEU A C     1 
ATOM   3780  O  O     . LEU A 1 472 ? 137.520 126.567 81.736  1.00 31.87 ?  472 LEU A O     1 
ATOM   3781  C  CB    . LEU A 1 472 ? 138.942 127.957 84.376  1.00 27.45 ?  472 LEU A CB    1 
ATOM   3782  C  CG    . LEU A 1 472 ? 139.821 129.121 84.838  1.00 29.85 ?  472 LEU A CG    1 
ATOM   3783  C  CD1   . LEU A 1 472 ? 140.586 128.736 86.090  1.00 22.43 ?  472 LEU A CD1   1 
ATOM   3784  C  CD2   . LEU A 1 472 ? 140.769 129.563 83.737  1.00 22.59 ?  472 LEU A CD2   1 
ATOM   3785  N  N     . ALA A 1 473 ? 136.277 126.429 83.607  1.00 28.89 ?  473 ALA A N     1 
ATOM   3786  C  CA    . ALA A 1 473 ? 135.621 125.200 83.179  1.00 25.05 ?  473 ALA A CA    1 
ATOM   3787  C  C     . ALA A 1 473 ? 134.699 125.448 81.993  1.00 32.50 ?  473 ALA A C     1 
ATOM   3788  O  O     . ALA A 1 473 ? 134.568 124.589 81.114  1.00 40.07 ?  473 ALA A O     1 
ATOM   3789  C  CB    . ALA A 1 473 ? 134.847 124.592 84.347  1.00 26.38 ?  473 ALA A CB    1 
ATOM   3790  N  N     . GLN A 1 474 ? 134.050 126.611 81.950  1.00 28.34 ?  474 GLN A N     1 
ATOM   3791  C  CA    . GLN A 1 474 ? 133.208 126.948 80.812  1.00 25.63 ?  474 GLN A CA    1 
ATOM   3792  C  C     . GLN A 1 474 ? 134.012 127.413 79.606  1.00 24.52 ?  474 GLN A C     1 
ATOM   3793  O  O     . GLN A 1 474 ? 133.425 127.645 78.544  1.00 35.27 ?  474 GLN A O     1 
ATOM   3794  C  CB    . GLN A 1 474 ? 132.192 128.021 81.208  1.00 27.87 ?  474 GLN A CB    1 
ATOM   3795  C  CG    . GLN A 1 474 ? 131.036 127.477 82.027  1.00 31.27 ?  474 GLN A CG    1 
ATOM   3796  C  CD    . GLN A 1 474 ? 130.209 128.569 82.667  1.00 30.88 ?  474 GLN A CD    1 
ATOM   3797  O  OE1   . GLN A 1 474 ? 129.521 129.324 81.982  1.00 33.25 ?  474 GLN A OE1   1 
ATOM   3798  N  NE2   . GLN A 1 474 ? 130.269 128.657 83.989  1.00 31.70 ?  474 GLN A NE2   1 
ATOM   3799  N  N     . ASN A 1 475 ? 135.328 127.561 79.744  1.00 30.94 ?  475 ASN A N     1 
ATOM   3800  C  CA    . ASN A 1 475 ? 136.206 127.901 78.634  1.00 32.64 ?  475 ASN A CA    1 
ATOM   3801  C  C     . ASN A 1 475 ? 137.167 126.772 78.289  1.00 33.12 ?  475 ASN A C     1 
ATOM   3802  O  O     . ASN A 1 475 ? 138.139 126.999 77.561  1.00 36.54 ?  475 ASN A O     1 
ATOM   3803  C  CB    . ASN A 1 475 ? 136.986 129.178 78.949  1.00 34.58 ?  475 ASN A CB    1 
ATOM   3804  C  CG    . ASN A 1 475 ? 136.134 130.423 78.836  1.00 30.33 ?  475 ASN A CG    1 
ATOM   3805  O  OD1   . ASN A 1 475 ? 136.090 131.065 77.788  1.00 35.59 ?  475 ASN A OD1   1 
ATOM   3806  N  ND2   . ASN A 1 475 ? 135.443 130.766 79.914  1.00 25.96 ?  475 ASN A ND2   1 
ATOM   3807  N  N     . GLY A 1 476 ? 136.921 125.567 78.793  1.00 29.91 ?  476 GLY A N     1 
ATOM   3808  C  CA    . GLY A 1 476 ? 137.774 124.428 78.501  1.00 30.17 ?  476 GLY A CA    1 
ATOM   3809  C  C     . GLY A 1 476 ? 139.176 124.526 79.061  1.00 34.66 ?  476 GLY A C     1 
ATOM   3810  O  O     . GLY A 1 476 ? 140.138 124.147 78.380  1.00 36.43 ?  476 GLY A O     1 
ATOM   3811  N  N     . ILE A 1 477 ? 139.320 125.026 80.285  1.00 31.37 ?  477 ILE A N     1 
ATOM   3812  C  CA    . ILE A 1 477 ? 140.615 125.149 80.942  1.00 28.71 ?  477 ILE A CA    1 
ATOM   3813  C  C     . ILE A 1 477 ? 140.542 124.440 82.285  1.00 31.58 ?  477 ILE A C     1 
ATOM   3814  O  O     . ILE A 1 477 ? 139.646 124.716 83.090  1.00 35.25 ?  477 ILE A O     1 
ATOM   3815  C  CB    . ILE A 1 477 ? 141.026 126.621 81.131  1.00 28.00 ?  477 ILE A CB    1 
ATOM   3816  C  CG1   . ILE A 1 477 ? 141.033 127.355 79.789  1.00 30.91 ?  477 ILE A CG1   1 
ATOM   3817  C  CG2   . ILE A 1 477 ? 142.389 126.709 81.788  1.00 31.37 ?  477 ILE A CG2   1 
ATOM   3818  C  CD1   . ILE A 1 477 ? 140.955 128.856 79.916  1.00 32.68 ?  477 ILE A CD1   1 
ATOM   3819  N  N     . ALA A 1 478 ? 141.478 123.525 82.523  1.00 31.56 ?  478 ALA A N     1 
ATOM   3820  C  CA    . ALA A 1 478 ? 141.548 122.847 83.809  1.00 26.59 ?  478 ALA A CA    1 
ATOM   3821  C  C     . ALA A 1 478 ? 142.074 123.795 84.876  1.00 33.48 ?  478 ALA A C     1 
ATOM   3822  O  O     . ALA A 1 478 ? 142.947 124.624 84.614  1.00 35.57 ?  478 ALA A O     1 
ATOM   3823  C  CB    . ALA A 1 478 ? 142.441 121.612 83.712  1.00 28.38 ?  478 ALA A CB    1 
ATOM   3824  N  N     . TYR A 1 479 ? 141.538 123.664 86.092  1.00 31.35 ?  479 TYR A N     1 
ATOM   3825  C  CA    . TYR A 1 479 ? 141.947 124.545 87.182  1.00 22.61 ?  479 TYR A CA    1 
ATOM   3826  C  C     . TYR A 1 479 ? 143.428 124.380 87.500  1.00 30.04 ?  479 TYR A C     1 
ATOM   3827  O  O     . TYR A 1 479 ? 144.123 125.363 87.780  1.00 39.24 ?  479 TYR A O     1 
ATOM   3828  C  CB    . TYR A 1 479 ? 141.095 124.269 88.421  1.00 21.64 ?  479 TYR A CB    1 
ATOM   3829  C  CG    . TYR A 1 479 ? 141.258 125.283 89.530  1.00 27.42 ?  479 TYR A CG    1 
ATOM   3830  C  CD1   . TYR A 1 479 ? 140.461 126.417 89.578  1.00 23.50 ?  479 TYR A CD1   1 
ATOM   3831  C  CD2   . TYR A 1 479 ? 142.201 125.101 90.533  1.00 28.82 ?  479 TYR A CD2   1 
ATOM   3832  C  CE1   . TYR A 1 479 ? 140.600 127.343 90.588  1.00 24.74 ?  479 TYR A CE1   1 
ATOM   3833  C  CE2   . TYR A 1 479 ? 142.348 126.025 91.547  1.00 26.82 ?  479 TYR A CE2   1 
ATOM   3834  C  CZ    . TYR A 1 479 ? 141.545 127.144 91.569  1.00 30.44 ?  479 TYR A CZ    1 
ATOM   3835  O  OH    . TYR A 1 479 ? 141.685 128.067 92.578  1.00 31.19 ?  479 TYR A OH    1 
ATOM   3836  N  N     . GLU A 1 480 ? 143.927 123.146 87.466  1.00 34.75 ?  480 GLU A N     1 
ATOM   3837  C  CA    . GLU A 1 480 ? 145.328 122.878 87.753  1.00 30.47 ?  480 GLU A CA    1 
ATOM   3838  C  C     . GLU A 1 480 ? 146.248 123.170 86.578  1.00 32.31 ?  480 GLU A C     1 
ATOM   3839  O  O     . GLU A 1 480 ? 147.470 123.145 86.754  1.00 38.83 ?  480 GLU A O     1 
ATOM   3840  C  CB    . GLU A 1 480 ? 145.513 121.419 88.164  1.00 35.32 ?  480 GLU A CB    1 
ATOM   3841  C  CG    . GLU A 1 480 ? 144.701 120.985 89.359  1.00 33.17 ?  480 GLU A CG    1 
ATOM   3842  C  CD    . GLU A 1 480 ? 144.405 119.503 89.325  1.00 41.41 ?  480 GLU A CD    1 
ATOM   3843  O  OE1   . GLU A 1 480 ? 143.392 119.113 88.706  1.00 41.14 ?  480 GLU A OE1   1 
ATOM   3844  O  OE2   . GLU A 1 480 ? 145.184 118.724 89.911  1.00 42.62 -1 480 GLU A OE2   1 
ATOM   3845  N  N     . SER A 1 481 ? 145.702 123.437 85.398  1.00 33.54 ?  481 SER A N     1 
ATOM   3846  C  CA    . SER A 1 481 ? 146.527 123.607 84.217  1.00 32.41 ?  481 SER A CA    1 
ATOM   3847  C  C     . SER A 1 481 ? 147.345 124.896 84.305  1.00 34.48 ?  481 SER A C     1 
ATOM   3848  O  O     . SER A 1 481 ? 146.932 125.862 84.950  1.00 37.49 ?  481 SER A O     1 
ATOM   3849  C  CB    . SER A 1 481 ? 145.661 123.627 82.962  1.00 32.23 ?  481 SER A CB    1 
ATOM   3850  O  OG    . SER A 1 481 ? 145.105 124.911 82.748  1.00 36.70 ?  481 SER A OG    1 
ATOM   3851  N  N     . PRO A 1 482 ? 148.523 124.925 83.677  1.00 39.26 ?  482 PRO A N     1 
ATOM   3852  C  CA    . PRO A 1 482 ? 149.291 126.179 83.626  1.00 35.92 ?  482 PRO A CA    1 
ATOM   3853  C  C     . PRO A 1 482 ? 148.561 127.303 82.914  1.00 35.70 ?  482 PRO A C     1 
ATOM   3854  O  O     . PRO A 1 482 ? 148.806 128.476 83.218  1.00 39.30 ?  482 PRO A O     1 
ATOM   3855  C  CB    . PRO A 1 482 ? 150.571 125.774 82.881  1.00 35.33 ?  482 PRO A CB    1 
ATOM   3856  C  CG    . PRO A 1 482 ? 150.667 124.300 83.056  1.00 36.84 ?  482 PRO A CG    1 
ATOM   3857  C  CD    . PRO A 1 482 ? 149.259 123.801 83.077  1.00 40.09 ?  482 PRO A CD    1 
ATOM   3858  N  N     . GLU A 1 483 ? 147.678 126.980 81.966  1.00 37.21 ?  483 GLU A N     1 
ATOM   3859  C  CA    . GLU A 1 483 ? 146.909 128.015 81.283  1.00 36.11 ?  483 GLU A CA    1 
ATOM   3860  C  C     . GLU A 1 483 ? 145.965 128.726 82.244  1.00 33.32 ?  483 GLU A C     1 
ATOM   3861  O  O     . GLU A 1 483 ? 145.745 129.937 82.127  1.00 36.83 ?  483 GLU A O     1 
ATOM   3862  C  CB    . GLU A 1 483 ? 146.130 127.405 80.118  1.00 38.31 ?  483 GLU A CB    1 
ATOM   3863  C  CG    . GLU A 1 483 ? 147.005 126.943 78.967  1.00 40.47 ?  483 GLU A CG    1 
ATOM   3864  C  CD    . GLU A 1 483 ? 147.441 125.500 79.115  1.00 43.75 ?  483 GLU A CD    1 
ATOM   3865  O  OE1   . GLU A 1 483 ? 147.159 124.899 80.171  1.00 41.03 ?  483 GLU A OE1   1 
ATOM   3866  O  OE2   . GLU A 1 483 ? 148.071 124.966 78.178  1.00 43.14 -1 483 GLU A OE2   1 
ATOM   3867  N  N     . ALA A 1 484 ? 145.395 127.988 83.199  1.00 27.96 ?  484 ALA A N     1 
ATOM   3868  C  CA    . ALA A 1 484 ? 144.540 128.611 84.202  1.00 28.48 ?  484 ALA A CA    1 
ATOM   3869  C  C     . ALA A 1 484 ? 145.320 129.602 85.053  1.00 29.73 ?  484 ALA A C     1 
ATOM   3870  O  O     . ALA A 1 484 ? 144.841 130.707 85.332  1.00 31.79 ?  484 ALA A O     1 
ATOM   3871  C  CB    . ALA A 1 484 ? 143.899 127.542 85.082  1.00 27.81 ?  484 ALA A CB    1 
ATOM   3872  N  N     . ARG A 1 485 ? 146.527 129.223 85.476  1.00 30.89 ?  485 ARG A N     1 
ATOM   3873  C  CA    . ARG A 1 485 ? 147.357 130.138 86.250  1.00 24.15 ?  485 ARG A CA    1 
ATOM   3874  C  C     . ARG A 1 485 ? 147.807 131.327 85.414  1.00 25.15 ?  485 ARG A C     1 
ATOM   3875  O  O     . ARG A 1 485 ? 147.928 132.435 85.939  1.00 35.58 ?  485 ARG A O     1 
ATOM   3876  C  CB    . ARG A 1 485 ? 148.563 129.397 86.824  1.00 27.04 ?  485 ARG A CB    1 
ATOM   3877  C  CG    . ARG A 1 485 ? 148.211 128.459 87.962  1.00 26.39 ?  485 ARG A CG    1 
ATOM   3878  C  CD    . ARG A 1 485 ? 149.455 127.919 88.635  1.00 28.57 ?  485 ARG A CD    1 
ATOM   3879  N  NE    . ARG A 1 485 ? 150.283 127.149 87.716  1.00 31.77 ?  485 ARG A NE    1 
ATOM   3880  C  CZ    . ARG A 1 485 ? 150.083 125.873 87.417  1.00 32.64 ?  485 ARG A CZ    1 
ATOM   3881  N  NH1   . ARG A 1 485 ? 149.083 125.187 87.947  1.00 30.58 1  485 ARG A NH1   1 
ATOM   3882  N  NH2   . ARG A 1 485 ? 150.908 125.270 86.567  1.00 29.50 ?  485 ARG A NH2   1 
ATOM   3883  N  N     . ASP A 1 486 ? 148.050 131.118 84.121  1.00 30.78 ?  486 ASP A N     1 
ATOM   3884  C  CA    . ASP A 1 486 ? 148.378 132.229 83.231  1.00 29.20 ?  486 ASP A CA    1 
ATOM   3885  C  C     . ASP A 1 486 ? 147.221 133.218 83.140  1.00 29.58 ?  486 ASP A C     1 
ATOM   3886  O  O     . ASP A 1 486 ? 147.417 134.441 83.221  1.00 36.63 ?  486 ASP A O     1 
ATOM   3887  C  CB    . ASP A 1 486 ? 148.739 131.681 81.851  1.00 33.34 ?  486 ASP A CB    1 
ATOM   3888  C  CG    . ASP A 1 486 ? 149.250 132.747 80.915  1.00 40.71 ?  486 ASP A CG    1 
ATOM   3889  O  OD1   . ASP A 1 486 ? 150.201 133.465 81.286  1.00 42.51 ?  486 ASP A OD1   1 
ATOM   3890  O  OD2   . ASP A 1 486 ? 148.702 132.861 79.800  1.00 39.27 -1 486 ASP A OD2   1 
ATOM   3891  N  N     . PHE A 1 487 ? 146.000 132.701 82.982  1.00 30.32 ?  487 PHE A N     1 
ATOM   3892  C  CA    . PHE A 1 487 ? 144.836 133.576 82.951  1.00 25.86 ?  487 PHE A CA    1 
ATOM   3893  C  C     . PHE A 1 487 ? 144.670 134.314 84.267  1.00 25.25 ?  487 PHE A C     1 
ATOM   3894  O  O     . PHE A 1 487 ? 144.365 135.507 84.278  1.00 31.24 ?  487 PHE A O     1 
ATOM   3895  C  CB    . PHE A 1 487 ? 143.561 132.800 82.641  1.00 26.95 ?  487 PHE A CB    1 
ATOM   3896  C  CG    . PHE A 1 487 ? 142.315 133.547 83.023  1.00 29.75 ?  487 PHE A CG    1 
ATOM   3897  C  CD1   . PHE A 1 487 ? 141.865 134.600 82.247  1.00 26.34 ?  487 PHE A CD1   1 
ATOM   3898  C  CD2   . PHE A 1 487 ? 141.619 133.229 84.178  1.00 26.22 ?  487 PHE A CD2   1 
ATOM   3899  C  CE1   . PHE A 1 487 ? 140.738 135.307 82.601  1.00 26.84 ?  487 PHE A CE1   1 
ATOM   3900  C  CE2   . PHE A 1 487 ? 140.491 133.935 84.536  1.00 25.28 ?  487 PHE A CE2   1 
ATOM   3901  C  CZ    . PHE A 1 487 ? 140.052 134.975 83.746  1.00 28.34 ?  487 PHE A CZ    1 
ATOM   3902  N  N     . ALA A 1 488 ? 144.827 133.609 85.389  1.00 25.81 ?  488 ALA A N     1 
ATOM   3903  C  CA    . ALA A 1 488 ? 144.688 134.257 86.687  1.00 20.51 ?  488 ALA A CA    1 
ATOM   3904  C  C     . ALA A 1 488 ? 145.731 135.351 86.861  1.00 27.80 ?  488 ALA A C     1 
ATOM   3905  O  O     . ALA A 1 488 ? 145.422 136.444 87.348  1.00 34.78 ?  488 ALA A O     1 
ATOM   3906  C  CB    . ALA A 1 488 ? 144.795 133.222 87.804  1.00 18.44 ?  488 ALA A CB    1 
ATOM   3907  N  N     . ASN A 1 489 ? 146.970 135.080 86.444  1.00 28.19 ?  489 ASN A N     1 
ATOM   3908  C  CA    . ASN A 1 489 ? 148.024 136.082 86.510  1.00 20.94 ?  489 ASN A CA    1 
ATOM   3909  C  C     . ASN A 1 489 ? 147.635 137.335 85.740  1.00 20.93 ?  489 ASN A C     1 
ATOM   3910  O  O     . ASN A 1 489 ? 147.649 138.442 86.288  1.00 30.25 ?  489 ASN A O     1 
ATOM   3911  C  CB    . ASN A 1 489 ? 149.324 135.492 85.961  1.00 22.28 ?  489 ASN A CB    1 
ATOM   3912  C  CG    . ASN A 1 489 ? 150.551 136.237 86.433  1.00 30.45 ?  489 ASN A CG    1 
ATOM   3913  O  OD1   . ASN A 1 489 ? 150.678 136.563 87.611  1.00 36.75 ?  489 ASN A OD1   1 
ATOM   3914  N  ND2   . ASN A 1 489 ? 151.471 136.498 85.514  1.00 28.71 ?  489 ASN A ND2   1 
ATOM   3915  N  N     . THR A 1 490 ? 147.252 137.174 84.470  1.00 26.43 ?  490 THR A N     1 
ATOM   3916  C  CA    . THR A 1 490 ? 146.914 138.343 83.661  1.00 24.41 ?  490 THR A CA    1 
ATOM   3917  C  C     . THR A 1 490 ? 145.688 139.066 84.206  1.00 26.18 ?  490 THR A C     1 
ATOM   3918  O  O     . THR A 1 490 ? 145.682 140.298 84.326  1.00 27.97 ?  490 THR A O     1 
ATOM   3919  C  CB    . THR A 1 490 ? 146.689 137.931 82.208  1.00 26.36 ?  490 THR A CB    1 
ATOM   3920  O  OG1   . THR A 1 490 ? 147.824 137.195 81.741  1.00 31.50 ?  490 THR A OG1   1 
ATOM   3921  C  CG2   . THR A 1 490 ? 146.494 139.159 81.332  1.00 25.93 ?  490 THR A CG2   1 
ATOM   3922  N  N     . PHE A 1 491 ? 144.644 138.313 84.558  1.00 21.58 ?  491 PHE A N     1 
ATOM   3923  C  CA    . PHE A 1 491 ? 143.394 138.908 85.009  1.00 18.72 ?  491 PHE A CA    1 
ATOM   3924  C  C     . PHE A 1 491 ? 143.593 139.702 86.291  1.00 25.92 ?  491 PHE A C     1 
ATOM   3925  O  O     . PHE A 1 491 ? 143.138 140.845 86.404  1.00 28.50 ?  491 PHE A O     1 
ATOM   3926  C  CB    . PHE A 1 491 ? 142.344 137.815 85.215  1.00 24.90 ?  491 PHE A CB    1 
ATOM   3927  C  CG    . PHE A 1 491 ? 141.040 138.319 85.758  1.00 22.44 ?  491 PHE A CG    1 
ATOM   3928  C  CD1   . PHE A 1 491 ? 140.067 138.810 84.907  1.00 18.33 ?  491 PHE A CD1   1 
ATOM   3929  C  CD2   . PHE A 1 491 ? 140.786 138.304 87.119  1.00 18.60 ?  491 PHE A CD2   1 
ATOM   3930  C  CE1   . PHE A 1 491 ? 138.870 139.278 85.400  1.00 15.30 ?  491 PHE A CE1   1 
ATOM   3931  C  CE2   . PHE A 1 491 ? 139.593 138.774 87.617  1.00 18.33 ?  491 PHE A CE2   1 
ATOM   3932  C  CZ    . PHE A 1 491 ? 138.632 139.261 86.756  1.00 19.82 ?  491 PHE A CZ    1 
ATOM   3933  N  N     . PHE A 1 492 ? 144.277 139.114 87.271  1.00 20.75 ?  492 PHE A N     1 
ATOM   3934  C  CA    . PHE A 1 492 ? 144.438 139.800 88.541  1.00 13.53 ?  492 PHE A CA    1 
ATOM   3935  C  C     . PHE A 1 492 ? 145.508 140.878 88.491  1.00 12.28 ?  492 PHE A C     1 
ATOM   3936  O  O     . PHE A 1 492 ? 145.414 141.844 89.250  1.00 22.08 ?  492 PHE A O     1 
ATOM   3937  C  CB    . PHE A 1 492 ? 144.718 138.781 89.644  1.00 20.06 ?  492 PHE A CB    1 
ATOM   3938  C  CG    . PHE A 1 492 ? 143.503 138.001 90.045  1.00 16.34 ?  492 PHE A CG    1 
ATOM   3939  C  CD1   . PHE A 1 492 ? 142.544 138.567 90.865  1.00 15.80 ?  492 PHE A CD1   1 
ATOM   3940  C  CD2   . PHE A 1 492 ? 143.297 136.720 89.567  1.00 21.73 ?  492 PHE A CD2   1 
ATOM   3941  C  CE1   . PHE A 1 492 ? 141.417 137.858 91.223  1.00 14.75 ?  492 PHE A CE1   1 
ATOM   3942  C  CE2   . PHE A 1 492 ? 142.171 136.007 89.920  1.00 16.11 ?  492 PHE A CE2   1 
ATOM   3943  C  CZ    . PHE A 1 492 ? 141.231 136.576 90.749  1.00 15.69 ?  492 PHE A CZ    1 
ATOM   3944  N  N     . MET A 1 493 ? 146.487 140.778 87.587  1.00 13.10 ?  493 MET A N     1 
ATOM   3945  C  CA    . MET A 1 493 ? 147.360 141.920 87.352  1.00 22.63 ?  493 MET A CA    1 
ATOM   3946  C  C     . MET A 1 493 ? 146.564 143.088 86.792  1.00 18.41 ?  493 MET A C     1 
ATOM   3947  O  O     . MET A 1 493 ? 146.771 144.237 87.192  1.00 28.96 ?  493 MET A O     1 
ATOM   3948  C  CB    . MET A 1 493 ? 148.506 141.532 86.414  1.00 25.38 ?  493 MET A CB    1 
ATOM   3949  C  CG    . MET A 1 493 ? 149.284 142.698 85.788  1.00 20.10 ?  493 MET A CG    1 
ATOM   3950  S  SD    . MET A 1 493 ? 148.540 143.492 84.348  1.00 34.53 ?  493 MET A SD    1 
ATOM   3951  C  CE    . MET A 1 493 ? 148.538 142.136 83.184  1.00 28.29 ?  493 MET A CE    1 
ATOM   3952  N  N     . MET A 1 494 ? 145.643 142.812 85.865  1.00 22.19 ?  494 MET A N     1 
ATOM   3953  C  CA    . MET A 1 494 ? 144.825 143.882 85.304  1.00 17.81 ?  494 MET A CA    1 
ATOM   3954  C  C     . MET A 1 494 ? 143.902 144.477 86.361  1.00 19.45 ?  494 MET A C     1 
ATOM   3955  O  O     . MET A 1 494 ? 143.707 145.699 86.414  1.00 32.12 ?  494 MET A O     1 
ATOM   3956  C  CB    . MET A 1 494 ? 144.018 143.353 84.118  1.00 24.00 ?  494 MET A CB    1 
ATOM   3957  C  CG    . MET A 1 494 ? 144.767 143.430 82.804  1.00 23.09 ?  494 MET A CG    1 
ATOM   3958  S  SD    . MET A 1 494 ? 144.011 142.536 81.439  1.00 41.86 ?  494 MET A SD    1 
ATOM   3959  C  CE    . MET A 1 494 ? 142.553 143.533 81.163  1.00 27.84 ?  494 MET A CE    1 
ATOM   3960  N  N     . VAL A 1 495 ? 143.326 143.623 87.208  1.00 22.31 ?  495 VAL A N     1 
ATOM   3961  C  CA    . VAL A 1 495 ? 142.477 144.099 88.295  1.00 13.04 ?  495 VAL A CA    1 
ATOM   3962  C  C     . VAL A 1 495 ? 143.274 144.983 89.244  1.00 19.56 ?  495 VAL A C     1 
ATOM   3963  O  O     . VAL A 1 495 ? 142.805 146.043 89.666  1.00 26.90 ?  495 VAL A O     1 
ATOM   3964  C  CB    . VAL A 1 495 ? 141.835 142.908 89.031  1.00 15.82 ?  495 VAL A CB    1 
ATOM   3965  C  CG1   . VAL A 1 495 ? 141.220 143.358 90.346  1.00 11.99 ?  495 VAL A CG1   1 
ATOM   3966  C  CG2   . VAL A 1 495 ? 140.794 142.244 88.154  1.00 18.51 ?  495 VAL A CG2   1 
ATOM   3967  N  N     . ASN A 1 496 ? 144.494 144.561 89.594  1.00 23.48 ?  496 ASN A N     1 
ATOM   3968  C  CA    . ASN A 1 496 ? 145.347 145.381 90.446  1.00 15.17 ?  496 ASN A CA    1 
ATOM   3969  C  C     . ASN A 1 496 ? 145.681 146.708 89.781  1.00 17.85 ?  496 ASN A C     1 
ATOM   3970  O  O     . ASN A 1 496 ? 145.650 147.760 90.428  1.00 23.80 ?  496 ASN A O     1 
ATOM   3971  C  CB    . ASN A 1 496 ? 146.625 144.618 90.792  1.00 19.22 ?  496 ASN A CB    1 
ATOM   3972  C  CG    . ASN A 1 496 ? 147.337 145.187 91.998  1.00 18.58 ?  496 ASN A CG    1 
ATOM   3973  O  OD1   . ASN A 1 496 ? 146.704 145.659 92.938  1.00 25.12 ?  496 ASN A OD1   1 
ATOM   3974  N  ND2   . ASN A 1 496 ? 148.661 145.145 91.977  1.00 18.92 ?  496 ASN A ND2   1 
ATOM   3975  N  N     . PHE A 1 497 ? 145.998 146.677 88.485  1.00 21.05 ?  497 PHE A N     1 
ATOM   3976  C  CA    . PHE A 1 497 ? 146.323 147.899 87.759  1.00 15.64 ?  497 PHE A CA    1 
ATOM   3977  C  C     . PHE A 1 497 ? 145.170 148.887 87.813  1.00 24.19 ?  497 PHE A C     1 
ATOM   3978  O  O     . PHE A 1 497 ? 145.356 150.064 88.140  1.00 28.93 ?  497 PHE A O     1 
ATOM   3979  C  CB    . PHE A 1 497 ? 146.668 147.564 86.307  1.00 17.27 ?  497 PHE A CB    1 
ATOM   3980  C  CG    . PHE A 1 497 ? 147.020 148.762 85.472  1.00 19.90 ?  497 PHE A CG    1 
ATOM   3981  C  CD1   . PHE A 1 497 ? 148.325 149.219 85.410  1.00 23.61 ?  497 PHE A CD1   1 
ATOM   3982  C  CD2   . PHE A 1 497 ? 146.048 149.429 84.747  1.00 21.10 ?  497 PHE A CD2   1 
ATOM   3983  C  CE1   . PHE A 1 497 ? 148.650 150.318 84.643  1.00 24.21 ?  497 PHE A CE1   1 
ATOM   3984  C  CE2   . PHE A 1 497 ? 146.370 150.529 83.981  1.00 22.95 ?  497 PHE A CE2   1 
ATOM   3985  C  CZ    . PHE A 1 497 ? 147.671 150.973 83.928  1.00 24.69 ?  497 PHE A CZ    1 
ATOM   3986  N  N     . TYR A 1 498 ? 143.960 148.419 87.514  1.00 26.98 ?  498 TYR A N     1 
ATOM   3987  C  CA    . TYR A 1 498 ? 142.830 149.334 87.459  1.00 18.45 ?  498 TYR A CA    1 
ATOM   3988  C  C     . TYR A 1 498 ? 142.352 149.746 88.844  1.00 22.85 ?  498 TYR A C     1 
ATOM   3989  O  O     . TYR A 1 498 ? 141.857 150.863 89.007  1.00 25.76 ?  498 TYR A O     1 
ATOM   3990  C  CB    . TYR A 1 498 ? 141.703 148.716 86.635  1.00 19.95 ?  498 TYR A CB    1 
ATOM   3991  C  CG    . TYR A 1 498 ? 142.043 148.683 85.165  1.00 24.72 ?  498 TYR A CG    1 
ATOM   3992  C  CD1   . TYR A 1 498 ? 142.312 149.855 84.475  1.00 24.50 ?  498 TYR A CD1   1 
ATOM   3993  C  CD2   . TYR A 1 498 ? 142.120 147.484 84.473  1.00 26.25 ?  498 TYR A CD2   1 
ATOM   3994  C  CE1   . TYR A 1 498 ? 142.636 149.837 83.137  1.00 25.80 ?  498 TYR A CE1   1 
ATOM   3995  C  CE2   . TYR A 1 498 ? 142.441 147.455 83.134  1.00 24.86 ?  498 TYR A CE2   1 
ATOM   3996  C  CZ    . TYR A 1 498 ? 142.698 148.635 82.470  1.00 30.37 ?  498 TYR A CZ    1 
ATOM   3997  O  OH    . TYR A 1 498 ? 143.019 148.618 81.134  1.00 32.57 ?  498 TYR A OH    1 
ATOM   3998  N  N     . SER A 1 499 ? 142.530 148.899 89.860  1.00 23.88 ?  499 SER A N     1 
ATOM   3999  C  CA    . SER A 1 499 ? 142.208 149.316 91.220  1.00 15.88 ?  499 SER A CA    1 
ATOM   4000  C  C     . SER A 1 499 ? 143.179 150.380 91.712  1.00 19.19 ?  499 SER A C     1 
ATOM   4001  O  O     . SER A 1 499 ? 142.768 151.350 92.358  1.00 30.15 ?  499 SER A O     1 
ATOM   4002  C  CB    . SER A 1 499 ? 142.205 148.111 92.159  1.00 15.23 ?  499 SER A CB    1 
ATOM   4003  O  OG    . SER A 1 499 ? 143.517 147.634 92.394  1.00 23.12 ?  499 SER A OG    1 
ATOM   4004  N  N     . ILE A 1 500 ? 144.471 150.226 91.407  1.00 17.80 ?  500 ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 500 ? 145.446 151.252 91.765  1.00 19.65 ?  500 ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 500 ? 145.155 152.542 91.012  1.00 18.17 ?  500 ILE A C     1 
ATOM   4007  O  O     . ILE A 1 500 ? 145.242 153.640 91.575  1.00 28.08 ?  500 ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 500 ? 146.877 150.748 91.497  1.00 22.99 ?  500 ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 500 ? 147.240 149.627 92.466  1.00 19.08 ?  500 ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 500 ? 147.876 151.875 91.632  1.00 20.01 ?  500 ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 500 ? 148.423 148.819 92.022  1.00 19.14 ?  500 ILE A CD1   1 
ATOM   4012  N  N     . GLN A 1 501 ? 144.799 152.431 89.730  1.00 24.23 ?  501 GLN A N     1 
ATOM   4013  C  CA    . GLN A 1 501 ? 144.460 153.614 88.947  1.00 22.16 ?  501 GLN A CA    1 
ATOM   4014  C  C     . GLN A 1 501 ? 143.244 154.330 89.518  1.00 28.31 ?  501 GLN A C     1 
ATOM   4015  O  O     . GLN A 1 501 ? 143.235 155.559 89.631  1.00 35.38 ?  501 GLN A O     1 
ATOM   4016  C  CB    . GLN A 1 501 ? 144.216 153.223 87.492  1.00 24.46 ?  501 GLN A CB    1 
ATOM   4017  C  CG    . GLN A 1 501 ? 144.696 154.250 86.490  1.00 25.08 ?  501 GLN A CG    1 
ATOM   4018  C  CD    . GLN A 1 501 ? 144.430 153.833 85.062  1.00 29.25 ?  501 GLN A CD    1 
ATOM   4019  O  OE1   . GLN A 1 501 ? 143.283 153.634 84.664  1.00 28.56 ?  501 GLN A OE1   1 
ATOM   4020  N  NE2   . GLN A 1 501 ? 145.492 153.693 84.279  1.00 33.56 ?  501 GLN A NE2   1 
ATOM   4021  N  N     . ARG A 1 502 ? 142.204 153.577 89.888  1.00 29.65 ?  502 ARG A N     1 
ATOM   4022  C  CA    . ARG A 1 502 ? 141.016 154.195 90.463  1.00 20.32 ?  502 ARG A CA    1 
ATOM   4023  C  C     . ARG A 1 502 ? 141.317 154.819 91.819  1.00 18.03 ?  502 ARG A C     1 
ATOM   4024  O  O     . ARG A 1 502 ? 140.805 155.896 92.134  1.00 30.49 ?  502 ARG A O     1 
ATOM   4025  C  CB    . ARG A 1 502 ? 139.892 153.167 90.581  1.00 24.31 ?  502 ARG A CB    1 
ATOM   4026  C  CG    . ARG A 1 502 ? 138.531 153.782 90.840  1.00 26.79 ?  502 ARG A CG    1 
ATOM   4027  C  CD    . ARG A 1 502 ? 138.232 154.902 89.863  1.00 27.43 ?  502 ARG A CD    1 
ATOM   4028  N  NE    . ARG A 1 502 ? 137.117 155.724 90.313  1.00 25.88 ?  502 ARG A NE    1 
ATOM   4029  C  CZ    . ARG A 1 502 ? 137.045 157.039 90.162  1.00 28.77 ?  502 ARG A CZ    1 
ATOM   4030  N  NH1   . ARG A 1 502 ? 138.010 157.718 89.565  1.00 32.34 1  502 ARG A NH1   1 
ATOM   4031  N  NH2   . ARG A 1 502 ? 135.981 157.688 90.621  1.00 30.22 ?  502 ARG A NH2   1 
ATOM   4032  N  N     . SER A 1 503 ? 142.140 154.160 92.637  1.00 18.39 ?  503 SER A N     1 
ATOM   4033  C  CA    . SER A 1 503 ? 142.510 154.733 93.927  1.00 23.96 ?  503 SER A CA    1 
ATOM   4034  C  C     . SER A 1 503 ? 143.281 156.034 93.749  1.00 24.98 ?  503 SER A C     1 
ATOM   4035  O  O     . SER A 1 503 ? 143.034 157.016 94.458  1.00 27.44 ?  503 SER A O     1 
ATOM   4036  C  CB    . SER A 1 503 ? 143.331 153.721 94.727  1.00 18.45 ?  503 SER A CB    1 
ATOM   4037  O  OG    . SER A 1 503 ? 143.261 153.987 96.114  1.00 22.93 ?  503 SER A OG    1 
ATOM   4038  N  N     . ALA A 1 504 ? 144.209 156.064 92.790  1.00 27.15 ?  504 ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 504 ? 144.962 157.284 92.520  1.00 25.35 ?  504 ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 504 ? 144.060 158.386 91.979  1.00 30.07 ?  504 ALA A C     1 
ATOM   4041  O  O     . ALA A 1 504 ? 144.219 159.558 92.338  1.00 37.59 ?  504 ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 504 ? 146.100 156.989 91.546  1.00 27.51 ?  504 ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 505 ? 143.105 158.034 91.116  1.00 28.85 ?  505 GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 505 ? 142.173 159.027 90.593  1.00 28.97 ?  505 GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 505 ? 141.275 159.580 91.693  1.00 30.69 ?  505 GLU A C     1 
ATOM   4046  O  O     . GLU A 1 505 ? 140.982 160.780 91.715  1.00 35.21 ?  505 GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 505 ? 141.334 158.417 89.471  1.00 29.45 ?  505 GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 505 ? 142.103 158.181 88.185  1.00 32.55 ?  505 GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 505 ? 141.493 157.087 87.332  1.00 35.89 ?  505 GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 505 ? 140.432 156.554 87.715  1.00 36.53 ?  505 GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 505 ? 142.075 156.762 86.277  1.00 39.44 -1 505 GLU A OE2   1 
ATOM   4052  N  N     . ILE A 1 506 ? 140.825 158.722 92.610  1.00 28.29 ?  506 ILE A N     1 
ATOM   4053  C  CA    . ILE A 1 506 ? 140.017 159.185 93.733  1.00 25.45 ?  506 ILE A CA    1 
ATOM   4054  C  C     . ILE A 1 506 ? 140.834 160.101 94.634  1.00 28.32 ?  506 ILE A C     1 
ATOM   4055  O  O     . ILE A 1 506 ? 140.339 161.129 95.107  1.00 37.79 ?  506 ILE A O     1 
ATOM   4056  C  CB    . ILE A 1 506 ? 139.445 157.985 94.508  1.00 25.65 ?  506 ILE A CB    1 
ATOM   4057  C  CG1   . ILE A 1 506 ? 138.400 157.255 93.666  1.00 28.37 ?  506 ILE A CG1   1 
ATOM   4058  C  CG2   . ILE A 1 506 ? 138.829 158.435 95.819  1.00 27.04 ?  506 ILE A CG2   1 
ATOM   4059  C  CD1   . ILE A 1 506 ? 138.039 155.889 94.198  1.00 22.37 ?  506 ILE A CD1   1 
ATOM   4060  N  N     . ALA A 1 507 ? 142.097 159.748 94.883  1.00 30.87 ?  507 ALA A N     1 
ATOM   4061  C  CA    . ALA A 1 507 ? 142.961 160.614 95.680  1.00 28.95 ?  507 ALA A CA    1 
ATOM   4062  C  C     . ALA A 1 507 ? 143.170 161.961 95.000  1.00 30.76 ?  507 ALA A C     1 
ATOM   4063  O  O     . ALA A 1 507 ? 143.183 163.004 95.663  1.00 33.56 ?  507 ALA A O     1 
ATOM   4064  C  CB    . ALA A 1 507 ? 144.301 159.924 95.936  1.00 25.37 ?  507 ALA A CB    1 
ATOM   4065  N  N     . LYS A 1 508 ? 143.346 161.958 93.678  1.00 36.54 ?  508 LYS A N     1 
ATOM   4066  C  CA    . LYS A 1 508 ? 143.507 163.209 92.942  1.00 33.53 ?  508 LYS A CA    1 
ATOM   4067  C  C     . LYS A 1 508 ? 142.242 164.059 92.999  1.00 38.04 ?  508 LYS A C     1 
ATOM   4068  O  O     . LYS A 1 508 ? 142.316 165.279 93.181  1.00 44.21 ?  508 LYS A O     1 
ATOM   4069  C  CB    . LYS A 1 508 ? 143.883 162.914 91.492  1.00 36.70 ?  508 LYS A CB    1 
ATOM   4070  C  CG    . LYS A 1 508 ? 143.864 164.131 90.585  1.00 40.47 ?  508 LYS A CG    1 
ATOM   4071  C  CD    . LYS A 1 508 ? 143.883 163.728 89.121  1.00 38.88 ?  508 LYS A CD    1 
ATOM   4072  C  CE    . LYS A 1 508 ? 144.124 164.930 88.224  1.00 39.18 ?  508 LYS A CE    1 
ATOM   4073  N  NZ    . LYS A 1 508 ? 144.961 164.582 87.046  1.00 42.23 1  508 LYS A NZ    1 
ATOM   4074  N  N     . GLU A 1 509 ? 141.076 163.432 92.844  1.00 36.02 ?  509 GLU A N     1 
ATOM   4075  C  CA    . GLU A 1 509 ? 139.822 164.179 92.837  1.00 36.32 ?  509 GLU A CA    1 
ATOM   4076  C  C     . GLU A 1 509 ? 139.514 164.751 94.215  1.00 39.00 ?  509 GLU A C     1 
ATOM   4077  O  O     . GLU A 1 509 ? 139.187 165.936 94.349  1.00 43.38 ?  509 GLU A O     1 
ATOM   4078  C  CB    . GLU A 1 509 ? 138.682 163.281 92.359  1.00 36.42 ?  509 GLU A CB    1 
ATOM   4079  C  CG    . GLU A 1 509 ? 138.692 163.003 90.866  1.00 42.34 ?  509 GLU A CG    1 
ATOM   4080  C  CD    . GLU A 1 509 ? 137.932 161.742 90.502  1.00 44.67 ?  509 GLU A CD    1 
ATOM   4081  O  OE1   . GLU A 1 509 ? 137.281 161.161 91.395  1.00 42.56 ?  509 GLU A OE1   1 
ATOM   4082  O  OE2   . GLU A 1 509 ? 137.983 161.334 89.323  1.00 42.61 -1 509 GLU A OE2   1 
ATOM   4083  N  N     . LYS A 1 510 ? 139.612 163.922 95.253  1.00 35.73 ?  510 LYS A N     1 
ATOM   4084  C  CA    . LYS A 1 510 ? 139.334 164.363 96.612  1.00 31.94 ?  510 LYS A CA    1 
ATOM   4085  C  C     . LYS A 1 510 ? 140.502 165.104 97.245  1.00 34.00 ?  510 LYS A C     1 
ATOM   4086  O  O     . LYS A 1 510 ? 140.338 165.667 98.333  1.00 39.30 ?  510 LYS A O     1 
ATOM   4087  C  CB    . LYS A 1 510 ? 138.952 163.163 97.479  1.00 30.48 ?  510 LYS A CB    1 
ATOM   4088  C  CG    . LYS A 1 510 ? 137.859 162.304 96.872  1.00 33.39 ?  510 LYS A CG    1 
ATOM   4089  C  CD    . LYS A 1 510 ? 137.243 161.367 97.892  1.00 33.07 ?  510 LYS A CD    1 
ATOM   4090  C  CE    . LYS A 1 510 ? 136.133 160.544 97.262  1.00 35.82 ?  510 LYS A CE    1 
ATOM   4091  N  NZ    . LYS A 1 510 ? 135.076 160.182 98.239  1.00 34.70 1  510 LYS A NZ    1 
ATOM   4092  N  N     . GLY A 1 511 ? 141.665 165.116 96.601  1.00 37.13 ?  511 GLY A N     1 
ATOM   4093  C  CA    . GLY A 1 511 ? 142.811 165.829 97.125  1.00 37.04 ?  511 GLY A CA    1 
ATOM   4094  C  C     . GLY A 1 511 ? 143.400 165.258 98.391  1.00 40.69 ?  511 GLY A C     1 
ATOM   4095  O  O     . GLY A 1 511 ? 144.242 165.911 99.013  1.00 42.75 ?  511 GLY A O     1 
ATOM   4096  N  N     . GLU A 1 512 ? 142.985 164.061 98.799  1.00 34.12 ?  512 GLU A N     1 
ATOM   4097  C  CA    . GLU A 1 512 ? 143.477 163.444 100.019 1.00 29.43 ?  512 GLU A CA    1 
ATOM   4098  C  C     . GLU A 1 512 ? 143.829 161.987 99.762  1.00 29.65 ?  512 GLU A C     1 
ATOM   4099  O  O     . GLU A 1 512 ? 143.196 161.308 98.951  1.00 33.10 ?  512 GLU A O     1 
ATOM   4100  C  CB    . GLU A 1 512 ? 142.445 163.540 101.152 1.00 31.02 ?  512 GLU A CB    1 
ATOM   4101  C  CG    . GLU A 1 512 ? 141.113 162.882 100.846 1.00 31.59 ?  512 GLU A CG    1 
ATOM   4102  C  CD    . GLU A 1 512 ? 140.413 162.388 102.094 1.00 35.46 ?  512 GLU A CD    1 
ATOM   4103  O  OE1   . GLU A 1 512 ? 141.113 162.040 103.067 1.00 35.24 ?  512 GLU A OE1   1 
ATOM   4104  O  OE2   . GLU A 1 512 ? 139.165 162.349 102.104 1.00 34.76 -1 512 GLU A OE2   1 
ATOM   4105  N  N     . THR A 1 513 ? 144.856 161.521 100.459 1.00 29.89 ?  513 THR A N     1 
ATOM   4106  C  CA    . THR A 1 513 ? 145.287 160.132 100.445 1.00 25.22 ?  513 THR A CA    1 
ATOM   4107  C  C     . THR A 1 513 ? 144.945 159.490 101.786 1.00 27.22 ?  513 THR A C     1 
ATOM   4108  O  O     . THR A 1 513 ? 144.448 160.145 102.705 1.00 36.88 ?  513 THR A O     1 
ATOM   4109  C  CB    . THR A 1 513 ? 146.785 160.037 100.153 1.00 24.19 ?  513 THR A CB    1 
ATOM   4110  O  OG1   . THR A 1 513 ? 147.514 160.754 101.156 1.00 28.55 ?  513 THR A OG1   1 
ATOM   4111  C  CG2   . THR A 1 513 ? 147.101 160.630 98.792  1.00 23.90 ?  513 THR A CG2   1 
ATOM   4112  N  N     . PHE A 1 514 ? 145.212 158.192 101.897 1.00 23.27 ?  514 PHE A N     1 
ATOM   4113  C  CA    . PHE A 1 514 ? 145.005 157.538 103.177 1.00 25.13 ?  514 PHE A CA    1 
ATOM   4114  C  C     . PHE A 1 514 ? 146.102 157.946 104.156 1.00 25.64 ?  514 PHE A C     1 
ATOM   4115  O  O     . PHE A 1 514 ? 147.199 158.352 103.766 1.00 28.15 ?  514 PHE A O     1 
ATOM   4116  C  CB    . PHE A 1 514 ? 144.941 156.016 103.016 1.00 18.28 ?  514 PHE A CB    1 
ATOM   4117  C  CG    . PHE A 1 514 ? 146.238 155.378 102.609 1.00 19.11 ?  514 PHE A CG    1 
ATOM   4118  C  CD1   . PHE A 1 514 ? 146.563 155.230 101.273 1.00 17.86 ?  514 PHE A CD1   1 
ATOM   4119  C  CD2   . PHE A 1 514 ? 147.118 154.892 103.562 1.00 22.51 ?  514 PHE A CD2   1 
ATOM   4120  C  CE1   . PHE A 1 514 ? 147.745 154.628 100.898 1.00 18.86 ?  514 PHE A CE1   1 
ATOM   4121  C  CE2   . PHE A 1 514 ? 148.300 154.291 103.190 1.00 17.63 ?  514 PHE A CE2   1 
ATOM   4122  C  CZ    . PHE A 1 514 ? 148.614 154.162 101.857 1.00 18.53 ?  514 PHE A CZ    1 
ATOM   4123  N  N     . ASP A 1 515 ? 145.782 157.853 105.443 1.00 29.13 ?  515 ASP A N     1 
ATOM   4124  C  CA    . ASP A 1 515 ? 146.695 158.324 106.476 1.00 27.15 ?  515 ASP A CA    1 
ATOM   4125  C  C     . ASP A 1 515 ? 148.015 157.568 106.421 1.00 29.36 ?  515 ASP A C     1 
ATOM   4126  O  O     . ASP A 1 515 ? 148.045 156.342 106.273 1.00 35.37 ?  515 ASP A O     1 
ATOM   4127  C  CB    . ASP A 1 515 ? 146.058 158.171 107.855 1.00 30.15 ?  515 ASP A CB    1 
ATOM   4128  C  CG    . ASP A 1 515 ? 145.134 159.321 108.200 1.00 38.05 ?  515 ASP A CG    1 
ATOM   4129  O  OD1   . ASP A 1 515 ? 144.645 159.993 107.268 1.00 36.62 ?  515 ASP A OD1   1 
ATOM   4130  O  OD2   . ASP A 1 515 ? 144.895 159.551 109.404 1.00 38.93 -1 515 ASP A OD2   1 
ATOM   4131  N  N     . GLN A 1 516 ? 149.112 158.317 106.546 1.00 27.50 ?  516 GLN A N     1 
ATOM   4132  C  CA    . GLN A 1 516 ? 150.467 157.772 106.458 1.00 28.05 ?  516 GLN A CA    1 
ATOM   4133  C  C     . GLN A 1 516 ? 150.710 157.096 105.111 1.00 25.00 ?  516 GLN A C     1 
ATOM   4134  O  O     . GLN A 1 516 ? 151.352 156.049 105.028 1.00 33.02 ?  516 GLN A O     1 
ATOM   4135  C  CB    . GLN A 1 516 ? 150.756 156.806 107.610 1.00 25.48 ?  516 GLN A CB    1 
ATOM   4136  C  CG    . GLN A 1 516 ? 150.573 157.406 108.991 1.00 27.14 ?  516 GLN A CG    1 
ATOM   4137  C  CD    . GLN A 1 516 ? 150.850 156.409 110.094 1.00 29.50 ?  516 GLN A CD    1 
ATOM   4138  O  OE1   . GLN A 1 516 ? 152.000 156.051 110.346 1.00 29.48 ?  516 GLN A OE1   1 
ATOM   4139  N  NE2   . GLN A 1 516 ? 149.797 155.955 110.760 1.00 28.58 ?  516 GLN A NE2   1 
ATOM   4140  N  N     . TYR A 1 517 ? 150.184 157.696 104.042 1.00 23.76 ?  517 TYR A N     1 
ATOM   4141  C  CA    . TYR A 1 517 ? 150.459 157.174 102.709 1.00 23.56 ?  517 TYR A CA    1 
ATOM   4142  C  C     . TYR A 1 517 ? 151.910 157.392 102.308 1.00 27.07 ?  517 TYR A C     1 
ATOM   4143  O  O     . TYR A 1 517 ? 152.493 156.546 101.620 1.00 34.91 ?  517 TYR A O     1 
ATOM   4144  C  CB    . TYR A 1 517 ? 149.533 157.814 101.673 1.00 24.34 ?  517 TYR A CB    1 
ATOM   4145  C  CG    . TYR A 1 517 ? 150.132 157.834 100.283 1.00 26.69 ?  517 TYR A CG    1 
ATOM   4146  C  CD1   . TYR A 1 517 ? 150.117 156.697 99.485  1.00 21.22 ?  517 TYR A CD1   1 
ATOM   4147  C  CD2   . TYR A 1 517 ? 150.728 158.981 99.777  1.00 25.97 ?  517 TYR A CD2   1 
ATOM   4148  C  CE1   . TYR A 1 517 ? 150.669 156.704 98.225  1.00 27.38 ?  517 TYR A CE1   1 
ATOM   4149  C  CE2   . TYR A 1 517 ? 151.287 158.995 98.519  1.00 25.76 ?  517 TYR A CE2   1 
ATOM   4150  C  CZ    . TYR A 1 517 ? 151.255 157.854 97.747  1.00 26.31 ?  517 TYR A CZ    1 
ATOM   4151  O  OH    . TYR A 1 517 ? 151.807 157.868 96.489  1.00 34.34 ?  517 TYR A OH    1 
ATOM   4152  N  N     . GLU A 1 518 ? 152.507 158.512 102.720 1.00 30.87 ?  518 GLU A N     1 
ATOM   4153  C  CA    . GLU A 1 518 ? 153.841 158.870 102.250 1.00 33.64 ?  518 GLU A CA    1 
ATOM   4154  C  C     . GLU A 1 518 ? 154.901 157.859 102.668 1.00 35.51 ?  518 GLU A C     1 
ATOM   4155  O  O     . GLU A 1 518 ? 155.940 157.760 102.006 1.00 38.35 ?  518 GLU A O     1 
ATOM   4156  C  CB    . GLU A 1 518 ? 154.218 160.262 102.757 1.00 34.11 ?  518 GLU A CB    1 
ATOM   4157  C  CG    . GLU A 1 518 ? 153.435 161.394 102.109 1.00 36.55 ?  518 GLU A CG    1 
ATOM   4158  C  CD    . GLU A 1 518 ? 153.708 161.530 100.620 1.00 43.50 ?  518 GLU A CD    1 
ATOM   4159  O  OE1   . GLU A 1 518 ? 154.782 161.086 100.160 1.00 39.21 ?  518 GLU A OE1   1 
ATOM   4160  O  OE2   . GLU A 1 518 ? 152.845 162.084 99.908  1.00 40.04 -1 518 GLU A OE2   1 
ATOM   4161  N  N     . GLY A 1 519 ? 154.670 157.113 103.747 1.00 24.41 ?  519 GLY A N     1 
ATOM   4162  C  CA    . GLY A 1 519 ? 155.576 156.055 104.137 1.00 20.56 ?  519 GLY A CA    1 
ATOM   4163  C  C     . GLY A 1 519 ? 155.338 154.720 103.478 1.00 21.97 ?  519 GLY A C     1 
ATOM   4164  O  O     . GLY A 1 519 ? 156.138 153.798 103.661 1.00 31.43 ?  519 GLY A O     1 
ATOM   4165  N  N     . SER A 1 520 ? 154.259 154.589 102.711 1.00 22.12 ?  520 SER A N     1 
ATOM   4166  C  CA    . SER A 1 520 ? 153.905 153.331 102.076 1.00 24.05 ?  520 SER A CA    1 
ATOM   4167  C  C     . SER A 1 520 ? 154.809 153.054 100.878 1.00 22.41 ?  520 SER A C     1 
ATOM   4168  O  O     . SER A 1 520 ? 155.530 153.926 100.389 1.00 27.98 ?  520 SER A O     1 
ATOM   4169  C  CB    . SER A 1 520 ? 152.441 153.347 101.643 1.00 20.05 ?  520 SER A CB    1 
ATOM   4170  O  OG    . SER A 1 520 ? 152.201 154.392 100.717 1.00 20.38 ?  520 SER A OG    1 
ATOM   4171  N  N     . THR A 1 521 ? 154.760 151.809 100.398 1.00 20.89 ?  521 THR A N     1 
ATOM   4172  C  CA    . THR A 1 521 ? 155.551 151.435 99.233  1.00 19.04 ?  521 THR A CA    1 
ATOM   4173  C  C     . THR A 1 521 ? 154.985 152.015 97.945  1.00 25.45 ?  521 THR A C     1 
ATOM   4174  O  O     . THR A 1 521 ? 155.711 152.101 96.949  1.00 28.88 ?  521 THR A O     1 
ATOM   4175  C  CB    . THR A 1 521 ? 155.639 149.914 99.115  1.00 28.33 ?  521 THR A CB    1 
ATOM   4176  O  OG1   . THR A 1 521 ? 154.320 149.360 99.109  1.00 29.39 ?  521 THR A OG1   1 
ATOM   4177  C  CG2   . THR A 1 521 ? 156.413 149.339 100.286 1.00 20.51 ?  521 THR A CG2   1 
ATOM   4178  N  N     . TYR A 1 522 ? 153.707 152.401 97.936  1.00 28.74 ?  522 TYR A N     1 
ATOM   4179  C  CA    . TYR A 1 522 ? 153.171 153.129 96.793  1.00 21.52 ?  522 TYR A CA    1 
ATOM   4180  C  C     . TYR A 1 522 ? 153.859 154.478 96.636  1.00 25.88 ?  522 TYR A C     1 
ATOM   4181  O  O     . TYR A 1 522 ? 154.202 154.884 95.520  1.00 29.89 ?  522 TYR A O     1 
ATOM   4182  C  CB    . TYR A 1 522 ? 151.662 153.323 96.942  1.00 18.60 ?  522 TYR A CB    1 
ATOM   4183  C  CG    . TYR A 1 522 ? 150.873 152.058 97.187  1.00 21.92 ?  522 TYR A CG    1 
ATOM   4184  C  CD1   . TYR A 1 522 ? 150.663 151.139 96.169  1.00 21.23 ?  522 TYR A CD1   1 
ATOM   4185  C  CD2   . TYR A 1 522 ? 150.312 151.800 98.429  1.00 23.68 ?  522 TYR A CD2   1 
ATOM   4186  C  CE1   . TYR A 1 522 ? 149.933 149.990 96.387  1.00 20.05 ?  522 TYR A CE1   1 
ATOM   4187  C  CE2   . TYR A 1 522 ? 149.578 150.655 98.655  1.00 22.90 ?  522 TYR A CE2   1 
ATOM   4188  C  CZ    . TYR A 1 522 ? 149.393 149.753 97.630  1.00 23.08 ?  522 TYR A CZ    1 
ATOM   4189  O  OH    . TYR A 1 522 ? 148.664 148.609 97.853  1.00 27.20 ?  522 TYR A OH    1 
ATOM   4190  N  N     . ALA A 1 523 ? 154.063 155.189 97.748  1.00 28.81 ?  523 ALA A N     1 
ATOM   4191  C  CA    . ALA A 1 523 ? 154.704 156.497 97.688  1.00 26.99 ?  523 ALA A CA    1 
ATOM   4192  C  C     . ALA A 1 523 ? 156.173 156.379 97.306  1.00 28.38 ?  523 ALA A C     1 
ATOM   4193  O  O     . ALA A 1 523 ? 156.681 157.178 96.513  1.00 32.27 ?  523 ALA A O     1 
ATOM   4194  C  CB    . ALA A 1 523 ? 154.553 157.215 99.027  1.00 23.69 ?  523 ALA A CB    1 
ATOM   4195  N  N     . THR A 1 524 ? 156.872 155.388 97.863  1.00 29.12 ?  524 THR A N     1 
ATOM   4196  C  CA    . THR A 1 524 ? 158.278 155.194 97.535  1.00 28.63 ?  524 THR A CA    1 
ATOM   4197  C  C     . THR A 1 524 ? 158.472 154.580 96.156  1.00 31.29 ?  524 THR A C     1 
ATOM   4198  O  O     . THR A 1 524 ? 159.579 154.650 95.612  1.00 36.00 ?  524 THR A O     1 
ATOM   4199  C  CB    . THR A 1 524 ? 158.950 154.314 98.589  1.00 30.58 ?  524 THR A CB    1 
ATOM   4200  O  OG1   . THR A 1 524 ? 158.493 152.964 98.450  1.00 32.71 ?  524 THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1 524 ? 158.622 154.813 99.986  1.00 27.59 ?  524 THR A CG2   1 
ATOM   4202  N  N     . GLY A 1 525 ? 157.429 153.985 95.581  1.00 25.73 ?  525 GLY A N     1 
ATOM   4203  C  CA    . GLY A 1 525 ? 157.524 153.352 94.284  1.00 27.99 ?  525 GLY A CA    1 
ATOM   4204  C  C     . GLY A 1 525 ? 158.054 151.937 94.295  1.00 32.06 ?  525 GLY A C     1 
ATOM   4205  O  O     . GLY A 1 525 ? 158.143 151.320 93.227  1.00 31.32 ?  525 GLY A O     1 
ATOM   4206  N  N     . GLU A 1 526 ? 158.412 151.403 95.464  1.00 32.87 ?  526 GLU A N     1 
ATOM   4207  C  CA    . GLU A 1 526 ? 158.907 150.035 95.548  1.00 33.19 ?  526 GLU A CA    1 
ATOM   4208  C  C     . GLU A 1 526 ? 157.817 149.013 95.250  1.00 36.82 ?  526 GLU A C     1 
ATOM   4209  O  O     . GLU A 1 526 ? 158.125 147.913 94.777  1.00 40.66 ?  526 GLU A O     1 
ATOM   4210  C  CB    . GLU A 1 526 ? 159.520 149.800 96.933  1.00 33.10 ?  526 GLU A CB    1 
ATOM   4211  C  CG    . GLU A 1 526 ? 159.567 148.354 97.396  1.00 33.56 ?  526 GLU A CG    1 
ATOM   4212  C  CD    . GLU A 1 526 ? 159.596 148.230 98.905  1.00 40.85 ?  526 GLU A CD    1 
ATOM   4213  O  OE1   . GLU A 1 526 ? 159.592 149.274 99.589  1.00 44.68 ?  526 GLU A OE1   1 
ATOM   4214  O  OE2   . GLU A 1 526 ? 159.625 147.087 99.408  1.00 39.17 -1 526 GLU A OE2   1 
ATOM   4215  N  N     . TYR A 1 527 ? 156.551 149.367 95.487  1.00 34.23 ?  527 TYR A N     1 
ATOM   4216  C  CA    . TYR A 1 527 ? 155.450 148.452 95.205  1.00 25.64 ?  527 TYR A CA    1 
ATOM   4217  C  C     . TYR A 1 527 ? 155.395 148.068 93.731  1.00 26.99 ?  527 TYR A C     1 
ATOM   4218  O  O     . TYR A 1 527 ? 155.018 146.939 93.400  1.00 29.87 ?  527 TYR A O     1 
ATOM   4219  C  CB    . TYR A 1 527 ? 154.126 149.085 95.636  1.00 22.95 ?  527 TYR A CB    1 
ATOM   4220  C  CG    . TYR A 1 527 ? 152.908 148.234 95.358  1.00 27.51 ?  527 TYR A CG    1 
ATOM   4221  C  CD1   . TYR A 1 527 ? 152.451 147.316 96.294  1.00 24.78 ?  527 TYR A CD1   1 
ATOM   4222  C  CD2   . TYR A 1 527 ? 152.211 148.352 94.163  1.00 28.27 ?  527 TYR A CD2   1 
ATOM   4223  C  CE1   . TYR A 1 527 ? 151.340 146.537 96.043  1.00 26.06 ?  527 TYR A CE1   1 
ATOM   4224  C  CE2   . TYR A 1 527 ? 151.103 147.576 93.905  1.00 24.90 ?  527 TYR A CE2   1 
ATOM   4225  C  CZ    . TYR A 1 527 ? 150.670 146.672 94.848  1.00 18.91 ?  527 TYR A CZ    1 
ATOM   4226  O  OH    . TYR A 1 527 ? 149.563 145.899 94.595  1.00 30.61 ?  527 TYR A OH    1 
ATOM   4227  N  N     . PHE A 1 528 ? 155.763 148.984 92.841  1.00 29.56 ?  528 PHE A N     1 
ATOM   4228  C  CA    . PHE A 1 528 ? 155.611 148.794 91.406  1.00 28.24 ?  528 PHE A CA    1 
ATOM   4229  C  C     . PHE A 1 528 ? 156.826 148.148 90.751  1.00 34.05 ?  528 PHE A C     1 
ATOM   4230  O  O     . PHE A 1 528 ? 156.904 148.129 89.520  1.00 41.91 ?  528 PHE A O     1 
ATOM   4231  C  CB    . PHE A 1 528 ? 155.326 150.136 90.726  1.00 29.14 ?  528 PHE A CB    1 
ATOM   4232  C  CG    . PHE A 1 528 ? 154.112 150.842 91.255  1.00 31.18 ?  528 PHE A CG    1 
ATOM   4233  C  CD1   . PHE A 1 528 ? 154.213 151.721 92.320  1.00 29.96 ?  528 PHE A CD1   1 
ATOM   4234  C  CD2   . PHE A 1 528 ? 152.871 150.636 90.681  1.00 29.03 ?  528 PHE A CD2   1 
ATOM   4235  C  CE1   . PHE A 1 528 ? 153.099 152.375 92.803  1.00 32.17 ?  528 PHE A CE1   1 
ATOM   4236  C  CE2   . PHE A 1 528 ? 151.753 151.287 91.161  1.00 29.46 ?  528 PHE A CE2   1 
ATOM   4237  C  CZ    . PHE A 1 528 ? 151.867 152.157 92.224  1.00 28.16 ?  528 PHE A CZ    1 
ATOM   4238  N  N     . ASP A 1 529 ? 157.770 147.624 91.537  1.00 34.97 ?  529 ASP A N     1 
ATOM   4239  C  CA    . ASP A 1 529 ? 159.013 147.111 90.967  1.00 32.88 ?  529 ASP A CA    1 
ATOM   4240  C  C     . ASP A 1 529 ? 158.755 145.949 90.015  1.00 34.45 ?  529 ASP A C     1 
ATOM   4241  O  O     . ASP A 1 529 ? 159.197 145.966 88.859  1.00 41.56 ?  529 ASP A O     1 
ATOM   4242  C  CB    . ASP A 1 529 ? 159.960 146.681 92.088  1.00 35.83 ?  529 ASP A CB    1 
ATOM   4243  C  CG    . ASP A 1 529 ? 160.662 147.853 92.741  1.00 42.01 ?  529 ASP A CG    1 
ATOM   4244  O  OD1   . ASP A 1 529 ? 160.574 148.976 92.204  1.00 41.20 ?  529 ASP A OD1   1 
ATOM   4245  O  OD2   . ASP A 1 529 ? 161.304 147.650 93.792  1.00 42.29 -1 529 ASP A OD2   1 
ATOM   4246  N  N     . LYS A 1 530 ? 158.029 144.931 90.482  1.00 37.67 ?  530 LYS A N     1 
ATOM   4247  C  CA    . LYS A 1 530 ? 157.748 143.774 89.641  1.00 38.51 ?  530 LYS A CA    1 
ATOM   4248  C  C     . LYS A 1 530 ? 156.805 144.113 88.498  1.00 36.82 ?  530 LYS A C     1 
ATOM   4249  O  O     . LYS A 1 530 ? 156.745 143.365 87.517  1.00 40.77 ?  530 LYS A O     1 
ATOM   4250  C  CB    . LYS A 1 530 ? 157.161 142.639 90.480  1.00 38.22 ?  530 LYS A CB    1 
ATOM   4251  C  CG    . LYS A 1 530 ? 155.645 142.629 90.545  1.00 32.22 ?  530 LYS A CG    1 
ATOM   4252  C  CD    . LYS A 1 530 ? 155.147 141.627 91.567  1.00 34.28 ?  530 LYS A CD    1 
ATOM   4253  C  CE    . LYS A 1 530 ? 153.636 141.536 91.553  1.00 34.98 ?  530 LYS A CE    1 
ATOM   4254  N  NZ    . LYS A 1 530 ? 153.083 141.624 92.928  1.00 38.69 1  530 LYS A NZ    1 
ATOM   4255  N  N     . TYR A 1 531 ? 156.073 145.215 88.599  1.00 32.53 ?  531 TYR A N     1 
ATOM   4256  C  CA    . TYR A 1 531 ? 155.159 145.617 87.543  1.00 28.43 ?  531 TYR A CA    1 
ATOM   4257  C  C     . TYR A 1 531 ? 155.842 146.438 86.462  1.00 29.37 ?  531 TYR A C     1 
ATOM   4258  O  O     . TYR A 1 531 ? 155.460 146.344 85.289  1.00 35.21 ?  531 TYR A O     1 
ATOM   4259  C  CB    . TYR A 1 531 ? 153.995 146.401 88.141  1.00 25.66 ?  531 TYR A CB    1 
ATOM   4260  C  CG    . TYR A 1 531 ? 153.015 145.532 88.886  1.00 29.92 ?  531 TYR A CG    1 
ATOM   4261  C  CD1   . TYR A 1 531 ? 152.443 144.425 88.276  1.00 29.59 ?  531 TYR A CD1   1 
ATOM   4262  C  CD2   . TYR A 1 531 ? 152.663 145.812 90.198  1.00 27.27 ?  531 TYR A CD2   1 
ATOM   4263  C  CE1   . TYR A 1 531 ? 151.546 143.625 88.948  1.00 32.41 ?  531 TYR A CE1   1 
ATOM   4264  C  CE2   . TYR A 1 531 ? 151.767 145.017 90.877  1.00 25.93 ?  531 TYR A CE2   1 
ATOM   4265  C  CZ    . TYR A 1 531 ? 151.211 143.925 90.247  1.00 28.95 ?  531 TYR A CZ    1 
ATOM   4266  O  OH    . TYR A 1 531 ? 150.317 143.128 90.920  1.00 30.57 ?  531 TYR A OH    1 
ATOM   4267  N  N     . VAL A 1 532 ? 156.846 147.238 86.827  1.00 36.10 ?  532 VAL A N     1 
ATOM   4268  C  CA    . VAL A 1 532 ? 157.636 147.959 85.835  1.00 35.37 ?  532 VAL A CA    1 
ATOM   4269  C  C     . VAL A 1 532 ? 158.777 147.119 85.284  1.00 37.91 ?  532 VAL A C     1 
ATOM   4270  O  O     . VAL A 1 532 ? 159.370 147.495 84.260  1.00 42.70 ?  532 VAL A O     1 
ATOM   4271  C  CB    . VAL A 1 532 ? 158.204 149.270 86.417  1.00 36.98 ?  532 VAL A CB    1 
ATOM   4272  C  CG1   . VAL A 1 532 ? 157.080 150.143 86.953  1.00 33.66 ?  532 VAL A CG1   1 
ATOM   4273  C  CG2   . VAL A 1 532 ? 159.229 148.977 87.500  1.00 36.45 ?  532 VAL A CG2   1 
ATOM   4274  N  N     . SER A 1 533 ? 159.106 145.995 85.920  1.00 37.93 ?  533 SER A N     1 
ATOM   4275  C  CA    . SER A 1 533 ? 160.173 145.123 85.442  1.00 36.60 ?  533 SER A CA    1 
ATOM   4276  C  C     . SER A 1 533 ? 159.661 143.897 84.700  1.00 41.39 ?  533 SER A C     1 
ATOM   4277  O  O     . SER A 1 533 ? 160.249 143.503 83.689  1.00 43.93 ?  533 SER A O     1 
ATOM   4278  C  CB    . SER A 1 533 ? 161.050 144.673 86.613  1.00 41.09 ?  533 SER A CB    1 
ATOM   4279  O  OG    . SER A 1 533 ? 160.494 143.545 87.265  1.00 42.74 ?  533 SER A OG    1 
ATOM   4280  N  N     . THR A 1 534 ? 158.580 143.284 85.172  1.00 42.79 ?  534 THR A N     1 
ATOM   4281  C  CA    . THR A 1 534 ? 158.071 142.038 84.617  1.00 38.26 ?  534 THR A CA    1 
ATOM   4282  C  C     . THR A 1 534 ? 156.776 142.289 83.856  1.00 37.89 ?  534 THR A C     1 
ATOM   4283  O  O     . THR A 1 534 ? 155.890 143.001 84.336  1.00 42.30 ?  534 THR A O     1 
ATOM   4284  C  CB    . THR A 1 534 ? 157.832 141.004 85.724  1.00 36.43 ?  534 THR A CB    1 
ATOM   4285  O  OG1   . THR A 1 534 ? 159.084 140.633 86.313  1.00 42.70 ?  534 THR A OG1   1 
ATOM   4286  C  CG2   . THR A 1 534 ? 157.152 139.760 85.171  1.00 39.87 ?  534 THR A CG2   1 
ATOM   4287  N  N     . ASP A 1 535 ? 156.678 141.706 82.664  1.00 40.76 ?  535 ASP A N     1 
ATOM   4288  C  CA    . ASP A 1 535 ? 155.460 141.761 81.869  1.00 41.03 ?  535 ASP A CA    1 
ATOM   4289  C  C     . ASP A 1 535 ? 154.546 140.609 82.264  1.00 44.13 ?  535 ASP A C     1 
ATOM   4290  O  O     . ASP A 1 535 ? 155.000 139.471 82.413  1.00 45.35 ?  535 ASP A O     1 
ATOM   4291  C  CB    . ASP A 1 535 ? 155.785 141.693 80.377  1.00 41.69 ?  535 ASP A CB    1 
ATOM   4292  C  CG    . ASP A 1 535 ? 154.589 141.296 79.537  1.00 47.77 ?  535 ASP A CG    1 
ATOM   4293  O  OD1   . ASP A 1 535 ? 153.740 142.169 79.256  1.00 48.39 ?  535 ASP A OD1   1 
ATOM   4294  O  OD2   . ASP A 1 535 ? 154.495 140.108 79.160  1.00 46.71 -1 535 ASP A OD2   1 
ATOM   4295  N  N     . PHE A 1 536 ? 153.258 140.908 82.437  1.00 33.07 ?  536 PHE A N     1 
ATOM   4296  C  CA    . PHE A 1 536 ? 152.280 139.917 82.864  1.00 31.59 ?  536 PHE A CA    1 
ATOM   4297  C  C     . PHE A 1 536 ? 151.272 139.589 81.768  1.00 38.43 ?  536 PHE A C     1 
ATOM   4298  O  O     . PHE A 1 536 ? 150.165 139.133 82.064  1.00 40.84 ?  536 PHE A O     1 
ATOM   4299  C  CB    . PHE A 1 536 ? 151.565 140.392 84.128  1.00 32.63 ?  536 PHE A CB    1 
ATOM   4300  C  CG    . PHE A 1 536 ? 152.460 140.481 85.330  1.00 33.32 ?  536 PHE A CG    1 
ATOM   4301  C  CD1   . PHE A 1 536 ? 153.191 141.628 85.582  1.00 32.41 ?  536 PHE A CD1   1 
ATOM   4302  C  CD2   . PHE A 1 536 ? 152.576 139.415 86.204  1.00 29.13 ?  536 PHE A CD2   1 
ATOM   4303  C  CE1   . PHE A 1 536 ? 154.016 141.709 86.685  1.00 33.49 ?  536 PHE A CE1   1 
ATOM   4304  C  CE2   . PHE A 1 536 ? 153.400 139.491 87.307  1.00 28.57 ?  536 PHE A CE2   1 
ATOM   4305  C  CZ    . PHE A 1 536 ? 154.119 140.640 87.548  1.00 31.83 ?  536 PHE A CZ    1 
ATOM   4306  N  N     . SER A 1 537 ? 151.635 139.823 80.510  1.00 39.75 ?  537 SER A N     1 
ATOM   4307  C  CA    . SER A 1 537 ? 150.803 139.406 79.397  1.00 37.63 ?  537 SER A CA    1 
ATOM   4308  C  C     . SER A 1 537 ? 150.725 137.879 79.352  1.00 38.56 ?  537 SER A C     1 
ATOM   4309  O  O     . SER A 1 537 ? 151.670 137.195 79.754  1.00 43.02 ?  537 SER A O     1 
ATOM   4310  C  CB    . SER A 1 537 ? 151.373 139.946 78.086  1.00 38.04 ?  537 SER A CB    1 
ATOM   4311  O  OG    . SER A 1 537 ? 150.509 139.699 76.992  1.00 45.62 ?  537 SER A OG    1 
ATOM   4312  N  N     . PRO A 1 538 ? 149.605 137.323 78.891  1.00 39.69 ?  538 PRO A N     1 
ATOM   4313  C  CA    . PRO A 1 538 ? 149.471 135.861 78.865  1.00 38.42 ?  538 PRO A CA    1 
ATOM   4314  C  C     . PRO A 1 538 ? 150.551 135.209 78.014  1.00 41.89 ?  538 PRO A C     1 
ATOM   4315  O  O     . PRO A 1 538 ? 150.904 135.697 76.939  1.00 40.90 ?  538 PRO A O     1 
ATOM   4316  C  CB    . PRO A 1 538 ? 148.077 135.642 78.266  1.00 37.81 ?  538 PRO A CB    1 
ATOM   4317  C  CG    . PRO A 1 538 ? 147.351 136.914 78.512  1.00 39.79 ?  538 PRO A CG    1 
ATOM   4318  C  CD    . PRO A 1 538 ? 148.379 137.995 78.429  1.00 37.05 ?  538 PRO A CD    1 
ATOM   4319  N  N     . LYS A 1 539 ? 151.075 134.089 78.512  1.00 42.14 ?  539 LYS A N     1 
ATOM   4320  C  CA    . LYS A 1 539 ? 152.113 133.341 77.819  1.00 41.99 ?  539 LYS A CA    1 
ATOM   4321  C  C     . LYS A 1 539 ? 151.559 132.289 76.867  1.00 44.20 ?  539 LYS A C     1 
ATOM   4322  O  O     . LYS A 1 539 ? 152.330 131.707 76.097  1.00 48.33 ?  539 LYS A O     1 
ATOM   4323  C  CB    . LYS A 1 539 ? 153.043 132.664 78.831  1.00 44.26 ?  539 LYS A CB    1 
ATOM   4324  C  CG    . LYS A 1 539 ? 153.309 133.486 80.078  1.00 46.33 ?  539 LYS A CG    1 
ATOM   4325  C  CD    . LYS A 1 539 ? 154.626 134.239 79.975  1.00 45.75 ?  539 LYS A CD    1 
ATOM   4326  C  CE    . LYS A 1 539 ? 154.701 135.358 81.002  1.00 46.33 ?  539 LYS A CE    1 
ATOM   4327  N  NZ    . LYS A 1 539 ? 153.892 136.541 80.597  1.00 44.50 1  539 LYS A NZ    1 
ATOM   4328  N  N     . TYR A 1 540 ? 150.255 132.034 76.900  1.00 43.85 ?  540 TYR A N     1 
ATOM   4329  C  CA    . TYR A 1 540 ? 149.623 131.038 76.049  1.00 43.78 ?  540 TYR A CA    1 
ATOM   4330  C  C     . TYR A 1 540 ? 148.679 131.716 75.066  1.00 46.70 ?  540 TYR A C     1 
ATOM   4331  O  O     . TYR A 1 540 ? 147.974 132.665 75.421  1.00 45.29 ?  540 TYR A O     1 
ATOM   4332  C  CB    . TYR A 1 540 ? 148.862 130.002 76.881  1.00 41.74 ?  540 TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1 540 ? 149.738 129.267 77.868  1.00 45.65 ?  540 TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1 540 ? 149.971 129.775 79.137  1.00 45.44 ?  540 TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1 540 ? 150.344 128.067 77.522  1.00 45.66 ?  540 TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1 540 ? 150.775 129.108 80.037  1.00 46.54 ?  540 TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1 540 ? 151.150 127.392 78.414  1.00 41.75 ?  540 TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1 540 ? 151.362 127.916 79.670  1.00 45.77 ?  540 TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1 540 ? 152.167 127.246 80.560  1.00 45.71 ?  540 TYR A OH    1 
ATOM   4340  N  N     . GLU A 1 541 ? 148.681 131.226 73.824  1.00 49.36 ?  541 GLU A N     1 
ATOM   4341  C  CA    . GLU A 1 541 ? 147.818 131.804 72.801  1.00 47.22 ?  541 GLU A CA    1 
ATOM   4342  C  C     . GLU A 1 541 ? 146.345 131.593 73.127  1.00 49.17 ?  541 GLU A C     1 
ATOM   4343  O  O     . GLU A 1 541 ? 145.508 132.431 72.774  1.00 47.50 ?  541 GLU A O     1 
ATOM   4344  C  CB    . GLU A 1 541 ? 148.162 131.222 71.428  1.00 48.57 ?  541 GLU A CB    1 
ATOM   4345  C  CG    . GLU A 1 541 ? 147.624 129.819 71.159  1.00 52.66 ?  541 GLU A CG    1 
ATOM   4346  C  CD    . GLU A 1 541 ? 148.331 128.747 71.971  1.00 57.43 ?  541 GLU A CD    1 
ATOM   4347  O  OE1   . GLU A 1 541 ? 149.452 129.004 72.458  1.00 55.11 ?  541 GLU A OE1   1 
ATOM   4348  O  OE2   . GLU A 1 541 ? 147.763 127.644 72.120  1.00 52.48 -1 541 GLU A OE2   1 
ATOM   4349  N  N     . LYS A 1 542 ? 146.009 130.488 73.797  1.00 47.03 ?  542 LYS A N     1 
ATOM   4350  C  CA    . LYS A 1 542 ? 144.626 130.265 74.204  1.00 44.20 ?  542 LYS A CA    1 
ATOM   4351  C  C     . LYS A 1 542 ? 144.168 131.324 75.197  1.00 43.71 ?  542 LYS A C     1 
ATOM   4352  O  O     . LYS A 1 542 ? 143.049 131.841 75.097  1.00 46.35 ?  542 LYS A O     1 
ATOM   4353  C  CB    . LYS A 1 542 ? 144.477 128.868 74.805  1.00 42.74 ?  542 LYS A CB    1 
ATOM   4354  C  CG    . LYS A 1 542 ? 143.038 128.422 74.990  1.00 44.00 ?  542 LYS A CG    1 
ATOM   4355  C  CD    . LYS A 1 542 ? 142.931 127.346 76.057  1.00 44.81 ?  542 LYS A CD    1 
ATOM   4356  C  CE    . LYS A 1 542 ? 141.607 126.607 75.965  1.00 46.45 ?  542 LYS A CE    1 
ATOM   4357  N  NZ    . LYS A 1 542 ? 140.464 127.541 75.783  1.00 47.24 1  542 LYS A NZ    1 
ATOM   4358  N  N     . ILE A 1 543 ? 145.020 131.656 76.167  1.00 40.29 ?  543 ILE A N     1 
ATOM   4359  C  CA    . ILE A 1 543 ? 144.675 132.674 77.153  1.00 38.16 ?  543 ILE A CA    1 
ATOM   4360  C  C     . ILE A 1 543 ? 144.684 134.059 76.521  1.00 39.04 ?  543 ILE A C     1 
ATOM   4361  O  O     . ILE A 1 543 ? 143.856 134.915 76.856  1.00 41.31 ?  543 ILE A O     1 
ATOM   4362  C  CB    . ILE A 1 543 ? 145.629 132.590 78.357  1.00 38.43 ?  543 ILE A CB    1 
ATOM   4363  C  CG1   . ILE A 1 543 ? 145.608 131.182 78.956  1.00 38.67 ?  543 ILE A CG1   1 
ATOM   4364  C  CG2   . ILE A 1 543 ? 145.253 133.616 79.405  1.00 39.41 ?  543 ILE A CG2   1 
ATOM   4365  C  CD1   . ILE A 1 543 ? 144.218 130.645 79.213  1.00 37.81 ?  543 ILE A CD1   1 
ATOM   4366  N  N     . ALA A 1 544 ? 145.622 134.307 75.603  1.00 41.27 ?  544 ALA A N     1 
ATOM   4367  C  CA    . ALA A 1 544 ? 145.720 135.623 74.979  1.00 43.83 ?  544 ALA A CA    1 
ATOM   4368  C  C     . ALA A 1 544 ? 144.475 135.963 74.171  1.00 43.06 ?  544 ALA A C     1 
ATOM   4369  O  O     . ALA A 1 544 ? 144.122 137.141 74.047  1.00 43.78 ?  544 ALA A O     1 
ATOM   4370  C  CB    . ALA A 1 544 ? 146.962 135.690 74.092  1.00 44.54 ?  544 ALA A CB    1 
ATOM   4371  N  N     . ASN A 1 545 ? 143.801 134.955 73.611  1.00 44.96 ?  545 ASN A N     1 
ATOM   4372  C  CA    . ASN A 1 545 ? 142.557 135.219 72.896  1.00 46.63 ?  545 ASN A CA    1 
ATOM   4373  C  C     . ASN A 1 545 ? 141.412 135.523 73.851  1.00 46.37 ?  545 ASN A C     1 
ATOM   4374  O  O     . ASN A 1 545 ? 140.451 136.197 73.467  1.00 45.67 ?  545 ASN A O     1 
ATOM   4375  C  CB    . ASN A 1 545 ? 142.199 134.037 71.995  1.00 46.98 ?  545 ASN A CB    1 
ATOM   4376  C  CG    . ASN A 1 545 ? 143.347 133.618 71.100  1.00 50.71 ?  545 ASN A CG    1 
ATOM   4377  O  OD1   . ASN A 1 545 ? 144.255 134.402 70.829  1.00 50.89 ?  545 ASN A OD1   1 
ATOM   4378  N  ND2   . ASN A 1 545 ? 143.312 132.374 70.636  1.00 49.17 ?  545 ASN A ND2   1 
ATOM   4379  N  N     . LEU A 1 546 ? 141.490 135.031 75.091  1.00 44.44 ?  546 LEU A N     1 
ATOM   4380  C  CA    . LEU A 1 546 ? 140.460 135.346 76.074  1.00 42.41 ?  546 LEU A CA    1 
ATOM   4381  C  C     . LEU A 1 546 ? 140.439 136.832 76.402  1.00 42.24 ?  546 LEU A C     1 
ATOM   4382  O  O     . LEU A 1 546 ? 139.386 137.376 76.754  1.00 45.24 ?  546 LEU A O     1 
ATOM   4383  C  CB    . LEU A 1 546 ? 140.678 134.526 77.346  1.00 40.80 ?  546 LEU A CB    1 
ATOM   4384  C  CG    . LEU A 1 546 ? 140.496 133.012 77.240  1.00 39.12 ?  546 LEU A CG    1 
ATOM   4385  C  CD1   . LEU A 1 546 ? 140.829 132.350 78.565  1.00 39.65 ?  546 LEU A CD1   1 
ATOM   4386  C  CD2   . LEU A 1 546 ? 139.081 132.666 76.810  1.00 40.10 ?  546 LEU A CD2   1 
ATOM   4387  N  N     . PHE A 1 547 ? 141.583 137.501 76.288  1.00 40.24 ?  547 PHE A N     1 
ATOM   4388  C  CA    . PHE A 1 547 ? 141.693 138.926 76.562  1.00 40.24 ?  547 PHE A CA    1 
ATOM   4389  C  C     . PHE A 1 547 ? 141.640 139.770 75.296  1.00 40.78 ?  547 PHE A C     1 
ATOM   4390  O  O     . PHE A 1 547 ? 141.893 140.977 75.358  1.00 42.05 ?  547 PHE A O     1 
ATOM   4391  C  CB    . PHE A 1 547 ? 142.985 139.214 77.329  1.00 36.73 ?  547 PHE A CB    1 
ATOM   4392  C  CG    . PHE A 1 547 ? 142.971 138.727 78.748  1.00 38.42 ?  547 PHE A CG    1 
ATOM   4393  C  CD1   . PHE A 1 547 ? 142.437 139.508 79.758  1.00 37.60 ?  547 PHE A CD1   1 
ATOM   4394  C  CD2   . PHE A 1 547 ? 143.492 137.487 79.073  1.00 37.01 ?  547 PHE A CD2   1 
ATOM   4395  C  CE1   . PHE A 1 547 ? 142.425 139.063 81.064  1.00 33.39 ?  547 PHE A CE1   1 
ATOM   4396  C  CE2   . PHE A 1 547 ? 143.481 137.036 80.378  1.00 35.07 ?  547 PHE A CE2   1 
ATOM   4397  C  CZ    . PHE A 1 547 ? 142.947 137.825 81.373  1.00 34.33 ?  547 PHE A CZ    1 
ATOM   4398  N  N     . GLU A 1 548 ? 141.325 139.164 74.154  1.00 50.24 ?  548 GLU A N     1 
ATOM   4399  C  CA    . GLU A 1 548 ? 141.237 139.908 72.905  1.00 52.22 ?  548 GLU A CA    1 
ATOM   4400  C  C     . GLU A 1 548 ? 140.108 140.927 72.976  1.00 51.05 ?  548 GLU A C     1 
ATOM   4401  O  O     . GLU A 1 548 ? 139.010 140.631 73.455  1.00 51.91 ?  548 GLU A O     1 
ATOM   4402  C  CB    . GLU A 1 548 ? 141.029 138.947 71.733  1.00 48.82 ?  548 GLU A CB    1 
ATOM   4403  C  CG    . GLU A 1 548 ? 140.392 139.562 70.491  1.00 51.53 ?  548 GLU A CG    1 
ATOM   4404  C  CD    . GLU A 1 548 ? 138.878 139.444 70.485  1.00 52.72 ?  548 GLU A CD    1 
ATOM   4405  O  OE1   . GLU A 1 548 ? 138.211 140.372 69.982  1.00 51.34 ?  548 GLU A OE1   1 
ATOM   4406  O  OE2   . GLU A 1 548 ? 138.358 138.420 70.979  1.00 53.80 -1 548 GLU A OE2   1 
ATOM   4407  N  N     . GLY A 1 549 ? 140.381 142.135 72.486  1.00 45.32 ?  549 GLY A N     1 
ATOM   4408  C  CA    . GLY A 1 549 ? 139.447 143.231 72.605  1.00 46.85 ?  549 GLY A CA    1 
ATOM   4409  C  C     . GLY A 1 549 ? 139.525 143.988 73.911  1.00 47.31 ?  549 GLY A C     1 
ATOM   4410  O  O     . GLY A 1 549 ? 138.717 144.901 74.129  1.00 46.90 ?  549 GLY A O     1 
ATOM   4411  N  N     . MET A 1 550 ? 140.466 143.641 74.785  1.00 47.64 ?  550 MET A N     1 
ATOM   4412  C  CA    . MET A 1 550 ? 140.639 144.296 76.072  1.00 44.25 ?  550 MET A CA    1 
ATOM   4413  C  C     . MET A 1 550 ? 142.119 144.579 76.271  1.00 44.66 ?  550 MET A C     1 
ATOM   4414  O  O     . MET A 1 550 ? 142.943 143.662 76.197  1.00 48.18 ?  550 MET A O     1 
ATOM   4415  C  CB    . MET A 1 550 ? 140.095 143.421 77.204  1.00 43.54 ?  550 MET A CB    1 
ATOM   4416  C  CG    . MET A 1 550 ? 139.517 144.194 78.371  1.00 48.40 ?  550 MET A CG    1 
ATOM   4417  S  SD    . MET A 1 550 ? 139.214 143.155 79.811  1.00 55.01 ?  550 MET A SD    1 
ATOM   4418  C  CE    . MET A 1 550 ? 139.219 141.521 79.081  1.00 44.39 ?  550 MET A CE    1 
ATOM   4419  N  N     . HIS A 1 551 ? 142.456 145.842 76.518  1.00 40.57 ?  551 HIS A N     1 
ATOM   4420  C  CA    . HIS A 1 551 ? 143.855 146.235 76.608  1.00 40.38 ?  551 HIS A CA    1 
ATOM   4421  C  C     . HIS A 1 551 ? 144.492 145.686 77.879  1.00 41.17 ?  551 HIS A C     1 
ATOM   4422  O  O     . HIS A 1 551 ? 143.952 145.844 78.978  1.00 42.19 ?  551 HIS A O     1 
ATOM   4423  C  CB    . HIS A 1 551 ? 143.986 147.756 76.570  1.00 39.62 ?  551 HIS A CB    1 
ATOM   4424  C  CG    . HIS A 1 551 ? 145.356 148.250 76.917  1.00 43.71 ?  551 HIS A CG    1 
ATOM   4425  N  ND1   . HIS A 1 551 ? 146.400 148.245 76.017  1.00 46.46 ?  551 HIS A ND1   1 
ATOM   4426  C  CD2   . HIS A 1 551 ? 145.855 148.762 78.068  1.00 43.40 ?  551 HIS A CD2   1 
ATOM   4427  C  CE1   . HIS A 1 551 ? 147.481 148.732 76.597  1.00 44.87 ?  551 HIS A CE1   1 
ATOM   4428  N  NE2   . HIS A 1 551 ? 147.178 149.053 77.842  1.00 43.03 ?  551 HIS A NE2   1 
ATOM   4429  N  N     . ILE A 1 552 ? 145.643 145.047 77.724  1.00 37.11 ?  552 ILE A N     1 
ATOM   4430  C  CA    . ILE A 1 552 ? 146.415 144.507 78.840  1.00 36.65 ?  552 ILE A CA    1 
ATOM   4431  C  C     . ILE A 1 552 ? 147.541 145.488 79.148  1.00 39.13 ?  552 ILE A C     1 
ATOM   4432  O  O     . ILE A 1 552 ? 148.383 145.734 78.271  1.00 41.15 ?  552 ILE A O     1 
ATOM   4433  C  CB    . ILE A 1 552 ? 146.972 143.114 78.518  1.00 36.39 ?  552 ILE A CB    1 
ATOM   4434  C  CG1   . ILE A 1 552 ? 145.832 142.146 78.202  1.00 35.61 ?  552 ILE A CG1   1 
ATOM   4435  C  CG2   . ILE A 1 552 ? 147.808 142.595 79.671  1.00 35.93 ?  552 ILE A CG2   1 
ATOM   4436  C  CD1   . ILE A 1 552 ? 146.291 140.853 77.577  1.00 39.04 ?  552 ILE A CD1   1 
ATOM   4437  N  N     . PRO A 1 553 ? 147.587 146.073 80.344  1.00 41.21 ?  553 PRO A N     1 
ATOM   4438  C  CA    . PRO A 1 553 ? 148.668 147.014 80.663  1.00 37.58 ?  553 PRO A CA    1 
ATOM   4439  C  C     . PRO A 1 553 ? 150.034 146.355 80.566  1.00 37.53 ?  553 PRO A C     1 
ATOM   4440  O  O     . PRO A 1 553 ? 150.243 145.233 81.034  1.00 35.05 ?  553 PRO A O     1 
ATOM   4441  C  CB    . PRO A 1 553 ? 148.351 147.443 82.099  1.00 34.42 ?  553 PRO A CB    1 
ATOM   4442  C  CG    . PRO A 1 553 ? 146.901 147.164 82.270  1.00 32.51 ?  553 PRO A CG    1 
ATOM   4443  C  CD    . PRO A 1 553 ? 146.610 145.964 81.436  1.00 33.93 ?  553 PRO A CD    1 
ATOM   4444  N  N     . THR A 1 554 ? 150.966 147.071 79.956  1.00 42.64 ?  554 THR A N     1 
ATOM   4445  C  CA    . THR A 1 554 ? 152.325 146.606 79.756  1.00 40.12 ?  554 THR A CA    1 
ATOM   4446  C  C     . THR A 1 554 ? 153.226 147.181 80.844  1.00 36.10 ?  554 THR A C     1 
ATOM   4447  O  O     . THR A 1 554 ? 152.758 147.756 81.831  1.00 38.78 ?  554 THR A O     1 
ATOM   4448  C  CB    . THR A 1 554 ? 152.804 146.991 78.356  1.00 38.52 ?  554 THR A CB    1 
ATOM   4449  O  OG1   . THR A 1 554 ? 152.787 148.417 78.220  1.00 43.66 ?  554 THR A OG1   1 
ATOM   4450  C  CG2   . THR A 1 554 ? 151.899 146.378 77.299  1.00 40.83 ?  554 THR A CG2   1 
ATOM   4451  N  N     . THR A 1 555 ? 154.539 147.017 80.674  1.00 38.32 ?  555 THR A N     1 
ATOM   4452  C  CA    . THR A 1 555 ? 155.476 147.639 81.601  1.00 35.88 ?  555 THR A CA    1 
ATOM   4453  C  C     . THR A 1 555 ? 155.433 149.158 81.489  1.00 38.84 ?  555 THR A C     1 
ATOM   4454  O  O     . THR A 1 555 ? 155.576 149.861 82.493  1.00 42.01 ?  555 THR A O     1 
ATOM   4455  C  CB    . THR A 1 555 ? 156.891 147.123 81.349  1.00 39.23 ?  555 THR A CB    1 
ATOM   4456  O  OG1   . THR A 1 555 ? 157.087 146.927 79.943  1.00 47.13 ?  555 THR A OG1   1 
ATOM   4457  C  CG2   . THR A 1 555 ? 157.111 145.804 82.074  1.00 38.19 ?  555 THR A CG2   1 
ATOM   4458  N  N     . GLU A 1 556 ? 155.241 149.681 80.276  1.00 39.45 ?  556 GLU A N     1 
ATOM   4459  C  CA    . GLU A 1 556 ? 155.128 151.126 80.099  1.00 41.11 ?  556 GLU A CA    1 
ATOM   4460  C  C     . GLU A 1 556 ? 153.883 151.672 80.788  1.00 41.76 ?  556 GLU A C     1 
ATOM   4461  O  O     . GLU A 1 556 ? 153.925 152.737 81.418  1.00 44.03 ?  556 GLU A O     1 
ATOM   4462  C  CB    . GLU A 1 556 ? 155.112 151.469 78.609  1.00 41.87 ?  556 GLU A CB    1 
ATOM   4463  C  CG    . GLU A 1 556 ? 156.338 151.014 77.809  1.00 45.29 ?  556 GLU A CG    1 
ATOM   4464  C  CD    . GLU A 1 556 ? 157.652 151.070 78.584  1.00 49.26 ?  556 GLU A CD    1 
ATOM   4465  O  OE1   . GLU A 1 556 ? 158.489 150.163 78.394  1.00 49.26 ?  556 GLU A OE1   1 
ATOM   4466  O  OE2   . GLU A 1 556 ? 157.881 152.044 79.333  1.00 43.00 -1 556 GLU A OE2   1 
ATOM   4467  N  N     . ASP A 1 557 ? 152.762 150.957 80.672  1.00 42.48 ?  557 ASP A N     1 
ATOM   4468  C  CA    . ASP A 1 557 ? 151.545 151.378 81.356  1.00 39.88 ?  557 ASP A CA    1 
ATOM   4469  C  C     . ASP A 1 557 ? 151.739 151.368 82.866  1.00 37.08 ?  557 ASP A C     1 
ATOM   4470  O  O     . ASP A 1 557 ? 151.266 152.269 83.567  1.00 37.78 ?  557 ASP A O     1 
ATOM   4471  C  CB    . ASP A 1 557 ? 150.381 150.473 80.959  1.00 37.18 ?  557 ASP A CB    1 
ATOM   4472  C  CG    . ASP A 1 557 ? 149.629 150.991 79.755  1.00 43.58 ?  557 ASP A CG    1 
ATOM   4473  O  OD1   . ASP A 1 557 ? 149.315 152.199 79.723  1.00 45.62 ?  557 ASP A OD1   1 
ATOM   4474  O  OD2   . ASP A 1 557 ? 149.352 150.190 78.837  1.00 43.98 -1 557 ASP A OD2   1 
ATOM   4475  N  N     . TRP A 1 558 ? 152.441 150.359 83.382  1.00 30.18 ?  558 TRP A N     1 
ATOM   4476  C  CA    . TRP A 1 558 ? 152.703 150.307 84.814  1.00 27.84 ?  558 TRP A CA    1 
ATOM   4477  C  C     . TRP A 1 558 ? 153.657 151.408 85.257  1.00 34.90 ?  558 TRP A C     1 
ATOM   4478  O  O     . TRP A 1 558 ? 153.516 151.928 86.365  1.00 35.93 ?  558 TRP A O     1 
ATOM   4479  C  CB    . TRP A 1 558 ? 153.250 148.935 85.198  1.00 30.23 ?  558 TRP A CB    1 
ATOM   4480  C  CG    . TRP A 1 558 ? 152.184 147.946 85.550  1.00 29.42 ?  558 TRP A CG    1 
ATOM   4481  C  CD1   . TRP A 1 558 ? 151.756 146.895 84.794  1.00 28.16 ?  558 TRP A CD1   1 
ATOM   4482  C  CD2   . TRP A 1 558 ? 151.405 147.918 86.752  1.00 28.54 ?  558 TRP A CD2   1 
ATOM   4483  N  NE1   . TRP A 1 558 ? 150.764 146.212 85.451  1.00 30.68 ?  558 TRP A NE1   1 
ATOM   4484  C  CE2   . TRP A 1 558 ? 150.530 146.819 86.656  1.00 29.91 ?  558 TRP A CE2   1 
ATOM   4485  C  CE3   . TRP A 1 558 ? 151.367 148.711 87.902  1.00 32.95 ?  558 TRP A CE3   1 
ATOM   4486  C  CZ2   . TRP A 1 558 ? 149.628 146.495 87.666  1.00 24.29 ?  558 TRP A CZ2   1 
ATOM   4487  C  CZ3   . TRP A 1 558 ? 150.469 148.388 88.900  1.00 27.71 ?  558 TRP A CZ3   1 
ATOM   4488  C  CH2   . TRP A 1 558 ? 149.613 147.291 88.777  1.00 19.86 ?  558 TRP A CH2   1 
ATOM   4489  N  N     . LYS A 1 559 ? 154.627 151.780 84.418  1.00 40.62 ?  559 LYS A N     1 
ATOM   4490  C  CA    . LYS A 1 559 ? 155.485 152.918 84.741  1.00 35.82 ?  559 LYS A CA    1 
ATOM   4491  C  C     . LYS A 1 559 ? 154.684 154.212 84.792  1.00 36.87 ?  559 LYS A C     1 
ATOM   4492  O  O     . LYS A 1 559 ? 154.882 155.044 85.688  1.00 40.72 ?  559 LYS A O     1 
ATOM   4493  C  CB    . LYS A 1 559 ? 156.618 153.034 83.720  1.00 38.77 ?  559 LYS A CB    1 
ATOM   4494  C  CG    . LYS A 1 559 ? 157.640 151.916 83.782  1.00 38.52 ?  559 LYS A CG    1 
ATOM   4495  C  CD    . LYS A 1 559 ? 158.502 151.896 82.532  1.00 41.10 ?  559 LYS A CD    1 
ATOM   4496  C  CE    . LYS A 1 559 ? 159.582 150.831 82.618  1.00 40.35 ?  559 LYS A CE    1 
ATOM   4497  N  NZ    . LYS A 1 559 ? 160.318 150.883 83.912  1.00 43.81 1  559 LYS A NZ    1 
ATOM   4498  N  N     . LYS A 1 560 ? 153.776 154.400 83.831  1.00 36.29 ?  560 LYS A N     1 
ATOM   4499  C  CA    . LYS A 1 560 ? 152.920 155.581 83.849  1.00 33.56 ?  560 LYS A CA    1 
ATOM   4500  C  C     . LYS A 1 560 ? 152.035 155.600 85.089  1.00 36.41 ?  560 LYS A C     1 
ATOM   4501  O  O     . LYS A 1 560 ? 151.852 156.651 85.714  1.00 42.03 ?  560 LYS A O     1 
ATOM   4502  C  CB    . LYS A 1 560 ? 152.067 155.633 82.580  1.00 34.44 ?  560 LYS A CB    1 
ATOM   4503  C  CG    . LYS A 1 560 ? 152.857 155.910 81.313  1.00 38.39 ?  560 LYS A CG    1 
ATOM   4504  C  CD    . LYS A 1 560 ? 151.948 155.966 80.099  1.00 39.77 ?  560 LYS A CD    1 
ATOM   4505  C  CE    . LYS A 1 560 ? 152.653 155.449 78.856  1.00 40.30 ?  560 LYS A CE    1 
ATOM   4506  N  NZ    . LYS A 1 560 ? 152.330 154.021 78.586  1.00 40.83 1  560 LYS A NZ    1 
ATOM   4507  N  N     . LEU A 1 561 ? 151.483 154.444 85.465  1.00 33.41 ?  561 LEU A N     1 
ATOM   4508  C  CA    . LEU A 1 561 ? 150.668 154.368 86.673  1.00 29.59 ?  561 LEU A CA    1 
ATOM   4509  C  C     . LEU A 1 561 ? 151.499 154.638 87.921  1.00 32.43 ?  561 LEU A C     1 
ATOM   4510  O  O     . LEU A 1 561 ? 151.016 155.264 88.869  1.00 36.45 ?  561 LEU A O     1 
ATOM   4511  C  CB    . LEU A 1 561 ? 149.989 153.002 86.769  1.00 31.12 ?  561 LEU A CB    1 
ATOM   4512  C  CG    . LEU A 1 561 ? 149.159 152.792 88.037  1.00 31.43 ?  561 LEU A CG    1 
ATOM   4513  C  CD1   . LEU A 1 561 ? 148.042 153.817 88.111  1.00 27.55 ?  561 LEU A CD1   1 
ATOM   4514  C  CD2   . LEU A 1 561 ? 148.601 151.387 88.105  1.00 28.89 ?  561 LEU A CD2   1 
ATOM   4515  N  N     . LYS A 1 562 ? 152.741 154.156 87.949  1.00 34.56 ?  562 LYS A N     1 
ATOM   4516  C  CA    . LYS A 1 562 ? 153.621 154.426 89.080  1.00 33.38 ?  562 LYS A CA    1 
ATOM   4517  C  C     . LYS A 1 562 ? 153.902 155.915 89.213  1.00 34.22 ?  562 LYS A C     1 
ATOM   4518  O  O     . LYS A 1 562 ? 153.878 156.462 90.321  1.00 38.77 ?  562 LYS A O     1 
ATOM   4519  C  CB    . LYS A 1 562 ? 154.924 153.641 88.922  1.00 35.62 ?  562 LYS A CB    1 
ATOM   4520  C  CG    . LYS A 1 562 ? 156.018 154.032 89.894  1.00 31.08 ?  562 LYS A CG    1 
ATOM   4521  C  CD    . LYS A 1 562 ? 157.317 153.320 89.565  1.00 28.64 ?  562 LYS A CD    1 
ATOM   4522  C  CE    . LYS A 1 562 ? 158.434 153.744 90.501  1.00 34.47 ?  562 LYS A CE    1 
ATOM   4523  N  NZ    . LYS A 1 562 ? 159.516 152.723 90.561  1.00 41.45 1  562 LYS A NZ    1 
ATOM   4524  N  N     . ALA A 1 563 ? 154.164 156.589 88.091  1.00 32.24 ?  563 ALA A N     1 
ATOM   4525  C  CA    . ALA A 1 563 ? 154.351 158.037 88.129  1.00 33.14 ?  563 ALA A CA    1 
ATOM   4526  C  C     . ALA A 1 563 ? 153.080 158.745 88.588  1.00 36.18 ?  563 ALA A C     1 
ATOM   4527  O  O     . ALA A 1 563 ? 153.137 159.690 89.386  1.00 42.44 ?  563 ALA A O     1 
ATOM   4528  C  CB    . ALA A 1 563 ? 154.785 158.545 86.755  1.00 35.79 ?  563 ALA A CB    1 
ATOM   4529  N  N     . PHE A 1 564 ? 151.924 158.294 88.098  1.00 34.18 ?  564 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 564 ? 150.651 158.886 88.496  1.00 31.53 ?  564 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 564 ? 150.417 158.738 89.995  1.00 35.60 ?  564 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 564 ? 149.952 159.674 90.654  1.00 38.50 ?  564 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 564 ? 149.517 158.236 87.703  1.00 32.91 ?  564 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 564 ? 148.219 158.985 87.759  1.00 33.21 ?  564 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 564 ? 147.932 159.969 86.829  1.00 35.68 ?  564 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 564 ? 147.279 158.694 88.731  1.00 34.31 ?  564 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 564 ? 146.735 160.655 86.875  1.00 39.13 ?  564 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 564 ? 146.082 159.376 88.783  1.00 35.63 ?  564 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 564 ? 145.807 160.357 87.853  1.00 38.90 ?  564 PHE A CZ    1 
ATOM   4540  N  N     . VAL A 1 565 ? 150.730 157.566 90.547  1.00 35.82 ?  565 VAL A N     1 
ATOM   4541  C  CA    . VAL A 1 565 ? 150.558 157.334 91.977  1.00 29.96 ?  565 VAL A CA    1 
ATOM   4542  C  C     . VAL A 1 565 ? 151.545 158.170 92.779  1.00 33.54 ?  565 VAL A C     1 
ATOM   4543  O  O     . VAL A 1 565 ? 151.194 158.741 93.818  1.00 36.12 ?  565 VAL A O     1 
ATOM   4544  C  CB    . VAL A 1 565 ? 150.698 155.832 92.286  1.00 29.53 ?  565 VAL A CB    1 
ATOM   4545  C  CG1   . VAL A 1 565 ? 150.893 155.602 93.774  1.00 28.69 ?  565 VAL A CG1   1 
ATOM   4546  C  CG2   . VAL A 1 565 ? 149.481 155.085 91.788  1.00 33.70 ?  565 VAL A CG2   1 
ATOM   4547  N  N     . ALA A 1 566 ? 152.791 158.262 92.312  1.00 36.68 ?  566 ALA A N     1 
ATOM   4548  C  CA    . ALA A 1 566 ? 153.785 159.061 93.018  1.00 36.24 ?  566 ALA A CA    1 
ATOM   4549  C  C     . ALA A 1 566 ? 153.422 160.538 93.018  1.00 38.26 ?  566 ALA A C     1 
ATOM   4550  O  O     . ALA A 1 566 ? 153.763 161.259 93.962  1.00 42.85 ?  566 ALA A O     1 
ATOM   4551  C  CB    . ALA A 1 566 ? 155.164 158.852 92.395  1.00 36.68 ?  566 ALA A CB    1 
ATOM   4552  N  N     . GLU A 1 567 ? 152.736 161.006 91.978  1.00 40.84 ?  567 GLU A N     1 
ATOM   4553  C  CA    . GLU A 1 567 ? 152.392 162.417 91.879  1.00 40.06 ?  567 GLU A CA    1 
ATOM   4554  C  C     . GLU A 1 567 ? 151.029 162.758 92.473  1.00 39.80 ?  567 GLU A C     1 
ATOM   4555  O  O     . GLU A 1 567 ? 150.800 163.923 92.817  1.00 43.67 ?  567 GLU A O     1 
ATOM   4556  C  CB    . GLU A 1 567 ? 152.458 162.858 90.411  1.00 42.38 ?  567 GLU A CB    1 
ATOM   4557  C  CG    . GLU A 1 567 ? 152.475 164.359 90.192  1.00 43.90 ?  567 GLU A CG    1 
ATOM   4558  C  CD    . GLU A 1 567 ? 151.191 164.861 89.571  1.00 47.55 ?  567 GLU A CD    1 
ATOM   4559  O  OE1   . GLU A 1 567 ? 150.544 164.076 88.847  1.00 46.07 ?  567 GLU A OE1   1 
ATOM   4560  O  OE2   . GLU A 1 567 ? 150.831 166.034 89.802  1.00 47.17 -1 567 GLU A OE2   1 
ATOM   4561  N  N     . HIS A 1 568 ? 150.127 161.783 92.615  1.00 39.70 ?  568 HIS A N     1 
ATOM   4562  C  CA    . HIS A 1 568 ? 148.809 162.023 93.188  1.00 38.76 ?  568 HIS A CA    1 
ATOM   4563  C  C     . HIS A 1 568 ? 148.500 161.227 94.447  1.00 35.94 ?  568 HIS A C     1 
ATOM   4564  O  O     . HIS A 1 568 ? 147.587 161.614 95.183  1.00 40.11 ?  568 HIS A O     1 
ATOM   4565  C  CB    . HIS A 1 568 ? 147.707 161.727 92.157  1.00 37.02 ?  568 HIS A CB    1 
ATOM   4566  C  CG    . HIS A 1 568 ? 147.631 162.726 91.047  1.00 38.46 ?  568 HIS A CG    1 
ATOM   4567  N  ND1   . HIS A 1 568 ? 146.960 162.480 89.870  1.00 42.97 ?  568 HIS A ND1   1 
ATOM   4568  C  CD2   . HIS A 1 568 ? 148.147 163.970 90.934  1.00 38.74 ?  568 HIS A CD2   1 
ATOM   4569  C  CE1   . HIS A 1 568 ? 147.071 163.531 89.076  1.00 42.21 ?  568 HIS A CE1   1 
ATOM   4570  N  NE2   . HIS A 1 568 ? 147.781 164.452 89.701  1.00 41.84 ?  568 HIS A NE2   1 
ATOM   4571  N  N     . GLY A 1 569 ? 149.213 160.140 94.718  1.00 29.47 ?  569 GLY A N     1 
ATOM   4572  C  CA    . GLY A 1 569 ? 148.942 159.350 95.901  1.00 29.61 ?  569 GLY A CA    1 
ATOM   4573  C  C     . GLY A 1 569 ? 147.843 158.327 95.691  1.00 28.19 ?  569 GLY A C     1 
ATOM   4574  O  O     . GLY A 1 569 ? 147.255 158.195 94.619  1.00 33.66 ?  569 GLY A O     1 
ATOM   4575  N  N     . MET A 1 570 ? 147.566 157.582 96.758  1.00 24.21 ?  570 MET A N     1 
ATOM   4576  C  CA    . MET A 1 570 ? 146.553 156.537 96.759  1.00 22.67 ?  570 MET A CA    1 
ATOM   4577  C  C     . MET A 1 570 ? 145.523 156.823 97.840  1.00 24.38 ?  570 MET A C     1 
ATOM   4578  O  O     . MET A 1 570 ? 145.873 157.225 98.953  1.00 31.69 ?  570 MET A O     1 
ATOM   4579  C  CB    . MET A 1 570 ? 147.178 155.158 96.990  1.00 26.83 ?  570 MET A CB    1 
ATOM   4580  C  CG    . MET A 1 570 ? 148.090 154.695 95.873  1.00 24.76 ?  570 MET A CG    1 
ATOM   4581  S  SD    . MET A 1 570 ? 147.261 153.577 94.738  1.00 38.07 ?  570 MET A SD    1 
ATOM   4582  C  CE    . MET A 1 570 ? 147.119 152.125 95.768  1.00 24.88 ?  570 MET A CE    1 
ATOM   4583  N  N     . TYR A 1 571 ? 144.250 156.610 97.509  1.00 15.53 ?  571 TYR A N     1 
ATOM   4584  C  CA    . TYR A 1 571 ? 143.183 156.884 98.463  1.00 9.58  ?  571 TYR A CA    1 
ATOM   4585  C  C     . TYR A 1 571 ? 142.970 155.734 99.439  1.00 18.52 ?  571 TYR A C     1 
ATOM   4586  O  O     . TYR A 1 571 ? 142.614 155.971 100.598 1.00 20.21 ?  571 TYR A O     1 
ATOM   4587  C  CB    . TYR A 1 571 ? 141.882 157.183 97.721  1.00 20.46 ?  571 TYR A CB    1 
ATOM   4588  C  CG    . TYR A 1 571 ? 140.807 157.772 98.600  1.00 24.83 ?  571 TYR A CG    1 
ATOM   4589  C  CD1   . TYR A 1 571 ? 140.858 159.101 98.992  1.00 23.83 ?  571 TYR A CD1   1 
ATOM   4590  C  CD2   . TYR A 1 571 ? 139.742 157.000 99.039  1.00 19.14 ?  571 TYR A CD2   1 
ATOM   4591  C  CE1   . TYR A 1 571 ? 139.881 159.643 99.794  1.00 26.06 ?  571 TYR A CE1   1 
ATOM   4592  C  CE2   . TYR A 1 571 ? 138.761 157.534 99.843  1.00 20.62 ?  571 TYR A CE2   1 
ATOM   4593  C  CZ    . TYR A 1 571 ? 138.833 158.857 100.217 1.00 28.45 ?  571 TYR A CZ    1 
ATOM   4594  O  OH    . TYR A 1 571 ? 137.855 159.395 101.017 1.00 27.40 ?  571 TYR A OH    1 
ATOM   4595  N  N     . HIS A 1 572 ? 143.171 154.497 98.998  1.00 23.11 ?  572 HIS A N     1 
ATOM   4596  C  CA    . HIS A 1 572 ? 142.942 153.319 99.821  1.00 14.41 ?  572 HIS A CA    1 
ATOM   4597  C  C     . HIS A 1 572 ? 144.273 152.686 100.192 1.00 13.07 ?  572 HIS A C     1 
ATOM   4598  O  O     . HIS A 1 572 ? 145.115 152.446 99.322  1.00 26.25 ?  572 HIS A O     1 
ATOM   4599  C  CB    . HIS A 1 572 ? 142.065 152.299 99.091  1.00 14.72 ?  572 HIS A CB    1 
ATOM   4600  C  CG    . HIS A 1 572 ? 140.893 152.903 98.385  1.00 9.11  ?  572 HIS A CG    1 
ATOM   4601  N  ND1   . HIS A 1 572 ? 140.934 153.271 97.059  1.00 18.58 ?  572 HIS A ND1   1 
ATOM   4602  C  CD2   . HIS A 1 572 ? 139.647 153.198 98.819  1.00 15.19 ?  572 HIS A CD2   1 
ATOM   4603  C  CE1   . HIS A 1 572 ? 139.764 153.771 96.707  1.00 19.44 ?  572 HIS A CE1   1 
ATOM   4604  N  NE2   . HIS A 1 572 ? 138.964 153.736 97.757  1.00 24.26 ?  572 HIS A NE2   1 
ATOM   4605  N  N     . SER A 1 573 ? 144.460 152.423 101.487 1.00 8.03  ?  573 SER A N     1 
ATOM   4606  C  CA    . SER A 1 573 ? 145.645 151.692 101.923 1.00 8.56  ?  573 SER A CA    1 
ATOM   4607  C  C     . SER A 1 573 ? 145.637 150.272 101.378 1.00 15.34 ?  573 SER A C     1 
ATOM   4608  O  O     . SER A 1 573 ? 146.679 149.748 100.969 1.00 24.43 ?  573 SER A O     1 
ATOM   4609  C  CB    . SER A 1 573 ? 145.726 151.687 103.449 1.00 12.75 ?  573 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 573 ? 144.477 151.344 104.018 1.00 21.38 ?  573 SER A OG    1 
ATOM   4611  N  N     . TYR A 1 574 ? 144.468 149.637 101.363 1.00 16.85 ?  574 TYR A N     1 
ATOM   4612  C  CA    . TYR A 1 574 ? 144.291 148.299 100.825 1.00 5.31  ?  574 TYR A CA    1 
ATOM   4613  C  C     . TYR A 1 574 ? 143.083 148.306 99.904  1.00 9.09  ?  574 TYR A C     1 
ATOM   4614  O  O     . TYR A 1 574 ? 142.098 149.001 100.169 1.00 13.59 ?  574 TYR A O     1 
ATOM   4615  C  CB    . TYR A 1 574 ? 144.110 147.275 101.948 1.00 12.98 ?  574 TYR A CB    1 
ATOM   4616  C  CG    . TYR A 1 574 ? 145.211 147.331 102.978 1.00 7.77  ?  574 TYR A CG    1 
ATOM   4617  C  CD1   . TYR A 1 574 ? 145.143 148.220 104.041 1.00 6.39  ?  574 TYR A CD1   1 
ATOM   4618  C  CD2   . TYR A 1 574 ? 146.322 146.509 102.883 1.00 10.01 ?  574 TYR A CD2   1 
ATOM   4619  C  CE1   . TYR A 1 574 ? 146.144 148.287 104.978 1.00 9.56  ?  574 TYR A CE1   1 
ATOM   4620  C  CE2   . TYR A 1 574 ? 147.328 146.568 103.820 1.00 17.92 ?  574 TYR A CE2   1 
ATOM   4621  C  CZ    . TYR A 1 574 ? 147.233 147.460 104.866 1.00 8.20  ?  574 TYR A CZ    1 
ATOM   4622  O  OH    . TYR A 1 574 ? 148.229 147.527 105.808 1.00 14.62 ?  574 TYR A OH    1 
ATOM   4623  N  N     . ARG A 1 575 ? 143.163 147.550 98.825  1.00 16.15 ?  575 ARG A N     1 
ATOM   4624  C  CA    . ARG A 1 575 ? 142.096 147.591 97.832  1.00 7.89  ?  575 ARG A CA    1 
ATOM   4625  C  C     . ARG A 1 575 ? 141.499 146.228 97.522  1.00 12.24 ?  575 ARG A C     1 
ATOM   4626  O  O     . ARG A 1 575 ? 140.285 146.125 97.342  1.00 20.45 ?  575 ARG A O     1 
ATOM   4627  C  CB    . ARG A 1 575 ? 142.611 148.223 96.534  1.00 15.51 ?  575 ARG A CB    1 
ATOM   4628  C  CG    . ARG A 1 575 ? 143.135 149.635 96.688  1.00 6.14  ?  575 ARG A CG    1 
ATOM   4629  C  CD    . ARG A 1 575 ? 144.174 149.932 95.627  1.00 12.48 ?  575 ARG A CD    1 
ATOM   4630  N  NE    . ARG A 1 575 ? 145.428 149.240 95.896  1.00 22.24 ?  575 ARG A NE    1 
ATOM   4631  C  CZ    . ARG A 1 575 ? 145.856 148.176 95.234  1.00 14.81 ?  575 ARG A CZ    1 
ATOM   4632  N  NH1   . ARG A 1 575 ? 145.155 147.650 94.245  1.00 16.91 1  575 ARG A NH1   1 
ATOM   4633  N  NH2   . ARG A 1 575 ? 147.016 147.623 95.573  1.00 10.77 ?  575 ARG A NH2   1 
ATOM   4634  N  N     . LEU A 1 576 ? 142.316 145.182 97.455  1.00 20.61 ?  576 LEU A N     1 
ATOM   4635  C  CA    . LEU A 1 576 ? 141.889 143.884 96.954  1.00 8.99  ?  576 LEU A CA    1 
ATOM   4636  C  C     . LEU A 1 576 ? 142.019 142.834 98.044  1.00 6.92  ?  576 LEU A C     1 
ATOM   4637  O  O     . LEU A 1 576 ? 143.089 142.681 98.639  1.00 16.05 ?  576 LEU A O     1 
ATOM   4638  C  CB    . LEU A 1 576 ? 142.716 143.475 95.734  1.00 4.75  ?  576 LEU A CB    1 
ATOM   4639  C  CG    . LEU A 1 576 ? 142.795 144.485 94.590  1.00 10.05 ?  576 LEU A CG    1 
ATOM   4640  C  CD1   . LEU A 1 576 ? 143.758 144.007 93.521  1.00 12.27 ?  576 LEU A CD1   1 
ATOM   4641  C  CD2   . LEU A 1 576 ? 141.422 144.732 93.999  1.00 10.86 ?  576 LEU A CD2   1 
ATOM   4642  N  N     . CYS A 1 577 ? 140.930 142.117 98.300  1.00 5.06  ?  577 CYS A N     1 
ATOM   4643  C  CA    . CYS A 1 577 ? 140.950 140.937 99.150  1.00 3.41  ?  577 CYS A CA    1 
ATOM   4644  C  C     . CYS A 1 577 ? 139.891 139.980 98.628  1.00 17.51 ?  577 CYS A C     1 
ATOM   4645  O  O     . CYS A 1 577 ? 138.774 140.399 98.320  1.00 21.24 ?  577 CYS A O     1 
ATOM   4646  C  CB    . CYS A 1 577 ? 140.703 141.292 100.624 1.00 3.50  ?  577 CYS A CB    1 
ATOM   4647  S  SG    . CYS A 1 577 ? 138.984 141.511 101.135 1.00 32.82 ?  577 CYS A SG    1 
ATOM   4648  N  N     . ILE A 1 578 ? 140.249 138.706 98.505  1.00 15.25 ?  578 ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 578 ? 139.371 137.699 97.925  1.00 10.66 ?  578 ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 578 ? 138.726 136.935 99.074  1.00 4.01  ?  578 ILE A C     1 
ATOM   4651  O  O     . ILE A 1 578 ? 139.341 136.057 99.684  1.00 14.86 ?  578 ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 578 ? 140.123 136.776 96.964  1.00 10.51 ?  578 ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 578 ? 140.758 137.600 95.845  1.00 0.00  ?  578 ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 578 ? 139.181 135.750 96.371  1.00 13.45 ?  578 ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 578 ? 141.407 136.775 94.777  1.00 6.95  ?  578 ILE A CD1   1 
ATOM   4656  N  N     . ALA A 1 579 ? 137.476 137.277 99.365  1.00 17.63 ?  579 ALA A N     1 
ATOM   4657  C  CA    . ALA A 1 579 ? 136.702 136.672 100.435 1.00 12.12 ?  579 ALA A CA    1 
ATOM   4658  C  C     . ALA A 1 579 ? 136.067 135.367 99.964  1.00 21.37 ?  579 ALA A C     1 
ATOM   4659  O  O     . ALA A 1 579 ? 136.056 135.064 98.771  1.00 27.27 ?  579 ALA A O     1 
ATOM   4660  C  CB    . ALA A 1 579 ? 135.641 137.661 100.910 1.00 9.65  ?  579 ALA A CB    1 
ATOM   4661  N  N     . PRO A 1 580 ? 135.556 134.549 100.891 1.00 26.58 ?  580 PRO A N     1 
ATOM   4662  C  CA    . PRO A 1 580 ? 134.885 133.305 100.472 1.00 22.98 ?  580 PRO A CA    1 
ATOM   4663  C  C     . PRO A 1 580 ? 133.674 133.513 99.574  1.00 25.85 ?  580 PRO A C     1 
ATOM   4664  O  O     . PRO A 1 580 ? 133.426 132.671 98.702  1.00 33.51 ?  580 PRO A O     1 
ATOM   4665  C  CB    . PRO A 1 580 ? 134.491 132.649 101.806 1.00 23.37 ?  580 PRO A CB    1 
ATOM   4666  C  CG    . PRO A 1 580 ? 134.725 133.681 102.860 1.00 24.80 ?  580 PRO A CG    1 
ATOM   4667  C  CD    . PRO A 1 580 ? 135.788 134.575 102.343 1.00 21.17 ?  580 PRO A CD    1 
ATOM   4668  N  N     . THR A 1 581 ? 132.921 134.600 99.749  1.00 22.49 ?  581 THR A N     1 
ATOM   4669  C  CA    . THR A 1 581 ? 131.718 134.889 98.959  1.00 33.36 ?  581 THR A CA    1 
ATOM   4670  C  C     . THR A 1 581 ? 130.749 133.703 98.975  1.00 31.70 ?  581 THR A C     1 
ATOM   4671  O  O     . THR A 1 581 ? 130.464 133.074 97.956  1.00 32.03 ?  581 THR A O     1 
ATOM   4672  C  CB    . THR A 1 581 ? 132.064 135.280 97.517  1.00 32.67 ?  581 THR A CB    1 
ATOM   4673  O  OG1   . THR A 1 581 ? 132.142 134.102 96.703  1.00 26.83 ?  581 THR A OG1   1 
ATOM   4674  C  CG2   . THR A 1 581 ? 133.375 136.040 97.450  1.00 30.85 ?  581 THR A CG2   1 
ATOM   4675  N  N     . GLY A 1 582 ? 130.247 133.418 100.173 1.00 35.50 ?  582 GLY A N     1 
ATOM   4676  C  CA    . GLY A 1 582 ? 129.469 132.216 100.401 1.00 32.59 ?  582 GLY A CA    1 
ATOM   4677  C  C     . GLY A 1 582 ? 128.132 132.132 99.691  1.00 35.28 ?  582 GLY A C     1 
ATOM   4678  O  O     . GLY A 1 582 ? 127.957 131.292 98.803  1.00 37.33 ?  582 GLY A O     1 
ATOM   4679  N  N     . SER A 1 583 ? 127.182 132.992 100.057 1.00 37.73 ?  583 SER A N     1 
ATOM   4680  C  CA    . SER A 1 583 ? 125.817 132.857 99.563  1.00 38.50 ?  583 SER A CA    1 
ATOM   4681  C  C     . SER A 1 583 ? 125.521 133.710 98.338  1.00 36.64 ?  583 SER A C     1 
ATOM   4682  O  O     . SER A 1 583 ? 124.580 133.399 97.601  1.00 38.67 ?  583 SER A O     1 
ATOM   4683  C  CB    . SER A 1 583 ? 124.818 133.209 100.670 1.00 42.09 ?  583 SER A CB    1 
ATOM   4684  O  OG    . SER A 1 583 ? 123.548 132.639 100.408 1.00 39.94 ?  583 SER A OG    1 
ATOM   4685  N  N     . ILE A 1 584 ? 126.290 134.775 98.101  1.00 33.14 ?  584 ILE A N     1 
ATOM   4686  C  CA    . ILE A 1 584 ? 126.068 135.587 96.911  1.00 31.28 ?  584 ILE A CA    1 
ATOM   4687  C  C     . ILE A 1 584 ? 126.513 134.864 95.648  1.00 33.16 ?  584 ILE A C     1 
ATOM   4688  O  O     . ILE A 1 584 ? 126.180 135.298 94.540  1.00 40.10 ?  584 ILE A O     1 
ATOM   4689  C  CB    . ILE A 1 584 ? 126.784 136.945 97.035  1.00 34.85 ?  584 ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1 584 ? 128.254 136.744 97.407  1.00 34.66 ?  584 ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1 584 ? 126.077 137.831 98.046  1.00 33.01 ?  584 ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1 584 ? 129.063 138.022 97.416  1.00 33.24 ?  584 ILE A CD1   1 
ATOM   4693  N  N     . SER A 1 585 ? 127.266 133.771 95.785  1.00 32.18 ?  585 SER A N     1 
ATOM   4694  C  CA    . SER A 1 585 ? 127.684 133.007 94.616  1.00 29.46 ?  585 SER A CA    1 
ATOM   4695  C  C     . SER A 1 585 ? 126.503 132.319 93.945  1.00 31.36 ?  585 SER A C     1 
ATOM   4696  O  O     . SER A 1 585 ? 126.490 132.170 92.719  1.00 33.66 ?  585 SER A O     1 
ATOM   4697  C  CB    . SER A 1 585 ? 128.747 131.985 95.011  1.00 29.82 ?  585 SER A CB    1 
ATOM   4698  O  OG    . SER A 1 585 ? 128.306 131.186 96.095  1.00 35.57 ?  585 SER A OG    1 
ATOM   4699  N  N     . TYR A 1 586 ? 125.513 131.882 94.728  1.00 31.83 ?  586 TYR A N     1 
ATOM   4700  C  CA    . TYR A 1 586 ? 124.304 131.315 94.141  1.00 33.16 ?  586 TYR A CA    1 
ATOM   4701  C  C     . TYR A 1 586 ? 123.541 132.365 93.345  1.00 32.37 ?  586 TYR A C     1 
ATOM   4702  O  O     . TYR A 1 586 ? 123.143 132.121 92.202  1.00 39.34 ?  586 TYR A O     1 
ATOM   4703  C  CB    . TYR A 1 586 ? 123.411 130.731 95.233  1.00 33.29 ?  586 TYR A CB    1 
ATOM   4704  C  CG    . TYR A 1 586 ? 124.024 129.589 96.003  1.00 34.35 ?  586 TYR A CG    1 
ATOM   4705  C  CD1   . TYR A 1 586 ? 123.977 128.293 95.513  1.00 35.32 ?  586 TYR A CD1   1 
ATOM   4706  C  CD2   . TYR A 1 586 ? 124.639 129.804 97.227  1.00 31.34 ?  586 TYR A CD2   1 
ATOM   4707  C  CE1   . TYR A 1 586 ? 124.532 127.246 96.216  1.00 36.39 ?  586 TYR A CE1   1 
ATOM   4708  C  CE2   . TYR A 1 586 ? 125.197 128.764 97.938  1.00 33.62 ?  586 TYR A CE2   1 
ATOM   4709  C  CZ    . TYR A 1 586 ? 125.141 127.486 97.427  1.00 37.41 ?  586 TYR A CZ    1 
ATOM   4710  O  OH    . TYR A 1 586 ? 125.696 126.446 98.134  1.00 40.64 ?  586 TYR A OH    1 
ATOM   4711  N  N     . VAL A 1 587 ? 123.343 133.545 93.937  1.00 29.24 ?  587 VAL A N     1 
ATOM   4712  C  CA    . VAL A 1 587 ? 122.581 134.606 93.286  1.00 27.25 ?  587 VAL A CA    1 
ATOM   4713  C  C     . VAL A 1 587 ? 123.240 135.009 91.974  1.00 30.87 ?  587 VAL A C     1 
ATOM   4714  O  O     . VAL A 1 587 ? 122.564 135.214 90.958  1.00 33.39 ?  587 VAL A O     1 
ATOM   4715  C  CB    . VAL A 1 587 ? 122.430 135.807 94.238  1.00 29.69 ?  587 VAL A CB    1 
ATOM   4716  C  CG1   . VAL A 1 587 ? 121.822 136.994 93.514  1.00 30.93 ?  587 VAL A CG1   1 
ATOM   4717  C  CG2   . VAL A 1 587 ? 121.593 135.421 95.443  1.00 31.47 ?  587 VAL A CG2   1 
ATOM   4718  N  N     . GLN A 1 588 ? 124.564 135.121 91.972  1.00 32.92 ?  588 GLN A N     1 
ATOM   4719  C  CA    . GLN A 1 588 ? 125.305 135.482 90.774  1.00 29.21 ?  588 GLN A CA    1 
ATOM   4720  C  C     . GLN A 1 588 ? 125.527 134.304 89.839  1.00 28.76 ?  588 GLN A C     1 
ATOM   4721  O  O     . GLN A 1 588 ? 126.099 134.496 88.761  1.00 31.83 ?  588 GLN A O     1 
ATOM   4722  C  CB    . GLN A 1 588 ? 126.655 136.090 91.156  1.00 26.58 ?  588 GLN A CB    1 
ATOM   4723  C  CG    . GLN A 1 588 ? 126.565 137.490 91.726  1.00 24.83 ?  588 GLN A CG    1 
ATOM   4724  C  CD    . GLN A 1 588 ? 126.788 138.554 90.675  1.00 27.77 ?  588 GLN A CD    1 
ATOM   4725  O  OE1   . GLN A 1 588 ? 127.644 138.411 89.805  1.00 29.67 ?  588 GLN A OE1   1 
ATOM   4726  N  NE2   . GLN A 1 588 ? 126.022 139.634 90.754  1.00 29.68 ?  588 GLN A NE2   1 
ATOM   4727  N  N     . SER A 1 589 ? 125.087 133.107 90.224  1.00 32.59 ?  589 SER A N     1 
ATOM   4728  C  CA    . SER A 1 589 ? 125.310 131.885 89.458  1.00 29.72 ?  589 SER A CA    1 
ATOM   4729  C  C     . SER A 1 589 ? 126.796 131.721 89.149  1.00 32.19 ?  589 SER A C     1 
ATOM   4730  O  O     . SER A 1 589 ? 127.228 131.665 87.997  1.00 30.48 ?  589 SER A O     1 
ATOM   4731  C  CB    . SER A 1 589 ? 124.465 131.872 88.182  1.00 30.42 ?  589 SER A CB    1 
ATOM   4732  O  OG    . SER A 1 589 ? 124.141 130.546 87.804  1.00 40.48 ?  589 SER A OG    1 
ATOM   4733  N  N     . SER A 1 590 ? 127.580 131.658 90.220  1.00 33.30 ?  590 SER A N     1 
ATOM   4734  C  CA    . SER A 1 590 ? 129.028 131.658 90.124  1.00 26.43 ?  590 SER A CA    1 
ATOM   4735  C  C     . SER A 1 590 ? 129.605 130.677 91.132  1.00 27.25 ?  590 SER A C     1 
ATOM   4736  O  O     . SER A 1 590 ? 128.990 130.390 92.161  1.00 31.48 ?  590 SER A O     1 
ATOM   4737  C  CB    . SER A 1 590 ? 129.599 133.059 90.370  1.00 23.21 ?  590 SER A CB    1 
ATOM   4738  O  OG    . SER A 1 590 ? 130.003 133.214 91.715  1.00 32.45 ?  590 SER A OG    1 
ATOM   4739  N  N     . THR A 1 591 ? 130.787 130.158 90.820  1.00 27.43 ?  591 THR A N     1 
ATOM   4740  C  CA    . THR A 1 591 ? 131.515 129.347 91.783  1.00 22.38 ?  591 THR A CA    1 
ATOM   4741  C  C     . THR A 1 591 ? 132.065 130.231 92.897  1.00 27.07 ?  591 THR A C     1 
ATOM   4742  O  O     . THR A 1 591 ? 132.376 131.407 92.691  1.00 25.19 ?  591 THR A O     1 
ATOM   4743  C  CB    . THR A 1 591 ? 132.648 128.580 91.101  1.00 25.20 ?  591 THR A CB    1 
ATOM   4744  O  OG1   . THR A 1 591 ? 133.660 129.497 90.671  1.00 33.06 ?  591 THR A OG1   1 
ATOM   4745  C  CG2   . THR A 1 591 ? 132.121 127.822 89.899  1.00 25.62 ?  591 THR A CG2   1 
ATOM   4746  N  N     . ALA A 1 592 ? 132.177 129.654 94.089  1.00 26.79 ?  592 ALA A N     1 
ATOM   4747  C  CA    . ALA A 1 592 ? 132.529 130.431 95.269  1.00 24.60 ?  592 ALA A CA    1 
ATOM   4748  C  C     . ALA A 1 592 ? 133.989 130.859 95.209  1.00 28.69 ?  592 ALA A C     1 
ATOM   4749  O  O     . ALA A 1 592 ? 134.891 130.014 95.179  1.00 31.31 ?  592 ALA A O     1 
ATOM   4750  C  CB    . ALA A 1 592 ? 132.261 129.620 96.533  1.00 28.80 ?  592 ALA A CB    1 
ATOM   4751  N  N     . SER A 1 593 ? 134.215 132.170 95.189  1.00 27.10 ?  593 SER A N     1 
ATOM   4752  C  CA    . SER A 1 593 ? 135.548 132.776 95.285  1.00 11.59 ?  593 SER A CA    1 
ATOM   4753  C  C     . SER A 1 593 ? 136.407 132.281 94.118  1.00 13.13 ?  593 SER A C     1 
ATOM   4754  O  O     . SER A 1 593 ? 135.885 131.907 93.059  1.00 27.44 ?  593 SER A O     1 
ATOM   4755  C  CB    . SER A 1 593 ? 136.125 132.497 96.661  1.00 28.10 ?  593 SER A CB    1 
ATOM   4756  O  OG    . SER A 1 593 ? 137.340 133.192 96.865  1.00 29.10 ?  593 SER A OG    1 
ATOM   4757  N  N     . VAL A 1 594 ? 137.729 132.285 94.295  1.00 23.32 ?  594 VAL A N     1 
ATOM   4758  C  CA    . VAL A 1 594 ? 138.650 131.748 93.302  1.00 19.82 ?  594 VAL A CA    1 
ATOM   4759  C  C     . VAL A 1 594 ? 139.029 130.306 93.592  1.00 14.86 ?  594 VAL A C     1 
ATOM   4760  O  O     . VAL A 1 594 ? 139.872 129.739 92.886  1.00 17.59 ?  594 VAL A O     1 
ATOM   4761  C  CB    . VAL A 1 594 ? 139.911 132.628 93.194  1.00 18.67 ?  594 VAL A CB    1 
ATOM   4762  C  CG1   . VAL A 1 594 ? 139.562 133.978 92.592  1.00 11.94 ?  594 VAL A CG1   1 
ATOM   4763  C  CG2   . VAL A 1 594 ? 140.554 132.805 94.557  1.00 18.42 ?  594 VAL A CG2   1 
ATOM   4764  N  N     . MET A 1 595 ? 138.431 129.698 94.613  1.00 22.05 ?  595 MET A N     1 
ATOM   4765  C  CA    . MET A 1 595 ? 138.694 128.307 94.931  1.00 20.53 ?  595 MET A CA    1 
ATOM   4766  C  C     . MET A 1 595 ? 137.968 127.385 93.955  1.00 23.58 ?  595 MET A C     1 
ATOM   4767  O  O     . MET A 1 595 ? 136.949 127.761 93.370  1.00 25.01 ?  595 MET A O     1 
ATOM   4768  C  CB    . MET A 1 595 ? 138.258 128.002 96.363  1.00 22.89 ?  595 MET A CB    1 
ATOM   4769  C  CG    . MET A 1 595 ? 139.400 127.771 97.355  1.00 21.47 ?  595 MET A CG    1 
ATOM   4770  S  SD    . MET A 1 595 ? 140.876 128.781 97.118  1.00 30.92 ?  595 MET A SD    1 
ATOM   4771  C  CE    . MET A 1 595 ? 140.226 130.439 97.288  1.00 31.89 ?  595 MET A CE    1 
ATOM   4772  N  N     . PRO A 1 596 ? 138.481 126.174 93.752  1.00 30.79 ?  596 PRO A N     1 
ATOM   4773  C  CA    . PRO A 1 596 ? 137.783 125.210 92.898  1.00 20.09 ?  596 PRO A CA    1 
ATOM   4774  C  C     . PRO A 1 596 ? 136.513 124.691 93.555  1.00 25.96 ?  596 PRO A C     1 
ATOM   4775  O  O     . PRO A 1 596 ? 136.334 124.751 94.772  1.00 30.13 ?  596 PRO A O     1 
ATOM   4776  C  CB    . PRO A 1 596 ? 138.811 124.090 92.712  1.00 23.39 ?  596 PRO A CB    1 
ATOM   4777  C  CG    . PRO A 1 596 ? 139.695 124.196 93.903  1.00 29.22 ?  596 PRO A CG    1 
ATOM   4778  C  CD    . PRO A 1 596 ? 139.768 125.651 94.242  1.00 28.42 ?  596 PRO A CD    1 
ATOM   4779  N  N     . ILE A 1 597 ? 135.620 124.172 92.710  1.00 27.79 ?  597 ILE A N     1 
ATOM   4780  C  CA    . ILE A 1 597 ? 134.334 123.682 93.185  1.00 30.69 ?  597 ILE A CA    1 
ATOM   4781  C  C     . ILE A 1 597 ? 134.524 122.420 94.016  1.00 31.57 ?  597 ILE A C     1 
ATOM   4782  O  O     . ILE A 1 597 ? 135.449 121.628 93.792  1.00 31.34 ?  597 ILE A O     1 
ATOM   4783  C  CB    . ILE A 1 597 ? 133.382 123.426 92.002  1.00 31.28 ?  597 ILE A CB    1 
ATOM   4784  C  CG1   . ILE A 1 597 ? 133.868 122.235 91.174  1.00 27.57 ?  597 ILE A CG1   1 
ATOM   4785  C  CG2   . ILE A 1 597 ? 133.269 124.660 91.139  1.00 29.49 ?  597 ILE A CG2   1 
ATOM   4786  C  CD1   . ILE A 1 597 ? 132.763 121.438 90.537  1.00 28.63 ?  597 ILE A CD1   1 
ATOM   4787  N  N     . MET A 1 598 ? 133.636 122.228 94.988  1.00 40.39 ?  598 MET A N     1 
ATOM   4788  C  CA    . MET A 1 598 ? 133.662 121.037 95.826  1.00 41.34 ?  598 MET A CA    1 
ATOM   4789  C  C     . MET A 1 598 ? 132.845 119.898 95.230  1.00 40.72 ?  598 MET A C     1 
ATOM   4790  O  O     . MET A 1 598 ? 133.297 118.749 95.228  1.00 44.88 ?  598 MET A O     1 
ATOM   4791  C  CB    . MET A 1 598 ? 133.148 121.370 97.228  1.00 42.03 ?  598 MET A CB    1 
ATOM   4792  C  CG    . MET A 1 598 ? 133.661 122.689 97.775  1.00 39.71 ?  598 MET A CG    1 
ATOM   4793  S  SD    . MET A 1 598 ? 133.515 122.817 99.567  1.00 57.19 ?  598 MET A SD    1 
ATOM   4794  C  CE    . MET A 1 598 ? 132.197 121.649 99.890  1.00 44.70 ?  598 MET A CE    1 
ATOM   4795  N  N     . GLU A 1 599 ? 131.648 120.194 94.729  1.00 41.01 ?  599 GLU A N     1 
ATOM   4796  C  CA    . GLU A 1 599 ? 130.784 119.209 94.095  1.00 39.32 ?  599 GLU A CA    1 
ATOM   4797  C  C     . GLU A 1 599 ? 130.335 119.735 92.742  1.00 38.14 ?  599 GLU A C     1 
ATOM   4798  O  O     . GLU A 1 599 ? 130.054 120.927 92.595  1.00 42.33 ?  599 GLU A O     1 
ATOM   4799  C  CB    . GLU A 1 599 ? 129.554 118.897 94.960  1.00 42.81 ?  599 GLU A CB    1 
ATOM   4800  C  CG    . GLU A 1 599 ? 129.814 118.921 96.455  1.00 44.35 ?  599 GLU A CG    1 
ATOM   4801  C  CD    . GLU A 1 599 ? 128.536 118.878 97.271  1.00 48.19 ?  599 GLU A CD    1 
ATOM   4802  O  OE1   . GLU A 1 599 ? 127.900 117.806 97.325  1.00 47.76 ?  599 GLU A OE1   1 
ATOM   4803  O  OE2   . GLU A 1 599 ? 128.171 119.916 97.860  1.00 45.85 -1 599 GLU A OE2   1 
ATOM   4804  N  N     . ARG A 1 600 ? 130.276 118.843 91.750  1.00 41.41 ?  600 ARG A N     1 
ATOM   4805  C  CA    . ARG A 1 600 ? 129.756 119.233 90.443  1.00 36.75 ?  600 ARG A CA    1 
ATOM   4806  C  C     . ARG A 1 600 ? 128.272 119.564 90.527  1.00 37.88 ?  600 ARG A C     1 
ATOM   4807  O  O     . ARG A 1 600 ? 127.826 120.603 90.028  1.00 41.00 ?  600 ARG A O     1 
ATOM   4808  C  CB    . ARG A 1 600 ? 130.002 118.122 89.425  1.00 36.61 ?  600 ARG A CB    1 
ATOM   4809  C  CG    . ARG A 1 600 ? 131.405 118.099 88.862  1.00 36.23 ?  600 ARG A CG    1 
ATOM   4810  C  CD    . ARG A 1 600 ? 131.496 117.162 87.680  1.00 36.48 ?  600 ARG A CD    1 
ATOM   4811  N  NE    . ARG A 1 600 ? 132.871 116.931 87.257  1.00 35.63 ?  600 ARG A NE    1 
ATOM   4812  C  CZ    . ARG A 1 600 ? 133.686 116.047 87.816  1.00 38.66 ?  600 ARG A CZ    1 
ATOM   4813  N  NH1   . ARG A 1 600 ? 133.302 115.307 88.841  1.00 37.64 1  600 ARG A NH1   1 
ATOM   4814  N  NH2   . ARG A 1 600 ? 134.916 115.905 87.334  1.00 39.46 ?  600 ARG A NH2   1 
ATOM   4815  N  N     . ILE A 1 601 ? 127.494 118.685 91.148  1.00 45.37 ?  601 ILE A N     1 
ATOM   4816  C  CA    . ILE A 1 601 ? 126.089 118.932 91.444  1.00 43.26 ?  601 ILE A CA    1 
ATOM   4817  C  C     . ILE A 1 601 ? 125.949 118.936 92.958  1.00 42.50 ?  601 ILE A C     1 
ATOM   4818  O  O     . ILE A 1 601 ? 126.257 117.937 93.618  1.00 46.73 ?  601 ILE A O     1 
ATOM   4819  C  CB    . ILE A 1 601 ? 125.168 117.882 90.805  1.00 42.87 ?  601 ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1 601 ? 125.521 117.698 89.328  1.00 43.32 ?  601 ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1 601 ? 123.714 118.294 90.954  1.00 42.85 ?  601 ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1 601 ? 124.688 116.657 88.625  1.00 43.38 ?  601 ILE A CD1   1 
ATOM   4823  N  N     . GLU A 1 602 ? 125.488 120.054 93.504  1.00 49.62 ?  602 GLU A N     1 
ATOM   4824  C  CA    . GLU A 1 602 ? 125.451 120.265 94.942  1.00 49.44 ?  602 GLU A CA    1 
ATOM   4825  C  C     . GLU A 1 602 ? 124.053 119.948 95.458  1.00 51.45 ?  602 GLU A C     1 
ATOM   4826  O  O     . GLU A 1 602 ? 123.073 120.570 95.036  1.00 53.93 ?  602 GLU A O     1 
ATOM   4827  C  CB    . GLU A 1 602 ? 125.850 121.700 95.281  1.00 49.41 ?  602 GLU A CB    1 
ATOM   4828  C  CG    . GLU A 1 602 ? 125.384 122.184 96.635  1.00 50.26 ?  602 GLU A CG    1 
ATOM   4829  C  CD    . GLU A 1 602 ? 125.634 123.664 96.832  1.00 54.59 ?  602 GLU A CD    1 
ATOM   4830  O  OE1   . GLU A 1 602 ? 126.627 124.178 96.275  1.00 52.32 ?  602 GLU A OE1   1 
ATOM   4831  O  OE2   . GLU A 1 602 ? 124.839 124.313 97.542  1.00 56.03 -1 602 GLU A OE2   1 
ATOM   4832  N  N     . GLU A 1 603 ? 123.966 118.978 96.363  1.00 56.98 ?  603 GLU A N     1 
ATOM   4833  C  CA    . GLU A 1 603 ? 122.701 118.536 96.931  1.00 57.36 ?  603 GLU A CA    1 
ATOM   4834  C  C     . GLU A 1 603 ? 122.510 119.172 98.301  1.00 58.62 ?  603 GLU A C     1 
ATOM   4835  O  O     . GLU A 1 603 ? 123.381 119.060 99.169  1.00 58.60 ?  603 GLU A O     1 
ATOM   4836  C  CB    . GLU A 1 603 ? 122.660 117.011 97.043  1.00 59.38 ?  603 GLU A CB    1 
ATOM   4837  C  CG    . GLU A 1 603 ? 121.365 116.461 97.613  1.00 60.68 ?  603 GLU A CG    1 
ATOM   4838  C  CD    . GLU A 1 603 ? 121.471 114.994 97.985  1.00 61.55 ?  603 GLU A CD    1 
ATOM   4839  O  OE1   . GLU A 1 603 ? 121.495 114.145 97.070  1.00 60.08 ?  603 GLU A OE1   1 
ATOM   4840  O  OE2   . GLU A 1 603 ? 121.530 114.689 99.195  1.00 59.52 -1 603 GLU A OE2   1 
ATOM   4841  N  N     . ARG A 1 604 ? 121.373 119.836 98.490  1.00 61.77 ?  604 ARG A N     1 
ATOM   4842  C  CA    . ARG A 1 604 ? 121.057 120.510 99.739  1.00 61.85 ?  604 ARG A CA    1 
ATOM   4843  C  C     . ARG A 1 604 ? 119.636 120.173 100.157 1.00 62.69 ?  604 ARG A C     1 
ATOM   4844  O  O     . ARG A 1 604 ? 118.786 119.843 99.326  1.00 64.24 ?  604 ARG A O     1 
ATOM   4845  C  CB    . ARG A 1 604 ? 121.207 122.032 99.616  1.00 59.98 ?  604 ARG A CB    1 
ATOM   4846  C  CG    . ARG A 1 604 ? 122.607 122.509 99.273  1.00 61.07 ?  604 ARG A CG    1 
ATOM   4847  C  CD    . ARG A 1 604 ? 123.558 122.317 100.441 1.00 62.30 ?  604 ARG A CD    1 
ATOM   4848  N  NE    . ARG A 1 604 ? 124.552 121.285 100.171 1.00 63.37 ?  604 ARG A NE    1 
ATOM   4849  C  CZ    . ARG A 1 604 ? 125.844 121.522 99.982  1.00 62.57 ?  604 ARG A CZ    1 
ATOM   4850  N  NH1   . ARG A 1 604 ? 126.335 122.749 100.030 1.00 61.28 1  604 ARG A NH1   1 
ATOM   4851  N  NH2   . ARG A 1 604 ? 126.661 120.503 99.737  1.00 60.05 ?  604 ARG A NH2   1 
ATOM   4852  N  N     . THR A 1 605 ? 119.384 120.259 101.461 1.00 68.82 ?  605 THR A N     1 
ATOM   4853  C  CA    . THR A 1 605 ? 118.055 120.066 102.025 1.00 70.06 ?  605 THR A CA    1 
ATOM   4854  C  C     . THR A 1 605 ? 117.642 121.346 102.735 1.00 69.42 ?  605 THR A C     1 
ATOM   4855  O  O     . THR A 1 605 ? 118.292 121.761 103.700 1.00 69.58 ?  605 THR A O     1 
ATOM   4856  C  CB    . THR A 1 605 ? 118.027 118.882 102.994 1.00 70.54 ?  605 THR A CB    1 
ATOM   4857  O  OG1   . THR A 1 605 ? 118.930 117.867 102.538 1.00 71.33 ?  605 THR A OG1   1 
ATOM   4858  C  CG2   . THR A 1 605 ? 116.627 118.300 103.079 1.00 69.20 ?  605 THR A CG2   1 
ATOM   4859  N  N     . TYR A 1 606 ? 116.568 121.968 102.258 1.00 68.76 ?  606 TYR A N     1 
ATOM   4860  C  CA    . TYR A 1 606 ? 116.029 123.189 102.849 1.00 71.10 ?  606 TYR A CA    1 
ATOM   4861  C  C     . TYR A 1 606 ? 114.685 122.846 103.478 1.00 72.93 ?  606 TYR A C     1 
ATOM   4862  O  O     . TYR A 1 606 ? 113.722 122.539 102.767 1.00 70.59 ?  606 TYR A O     1 
ATOM   4863  C  CB    . TYR A 1 606 ? 115.894 124.291 101.801 1.00 69.38 ?  606 TYR A CB    1 
ATOM   4864  C  CG    . TYR A 1 606 ? 117.221 124.776 101.264 1.00 70.30 ?  606 TYR A CG    1 
ATOM   4865  C  CD1   . TYR A 1 606 ? 117.991 125.687 101.975 1.00 68.23 ?  606 TYR A CD1   1 
ATOM   4866  C  CD2   . TYR A 1 606 ? 117.709 124.315 100.051 1.00 69.45 ?  606 TYR A CD2   1 
ATOM   4867  C  CE1   . TYR A 1 606 ? 119.207 126.127 101.488 1.00 68.83 ?  606 TYR A CE1   1 
ATOM   4868  C  CE2   . TYR A 1 606 ? 118.921 124.749 99.555  1.00 67.17 ?  606 TYR A CE2   1 
ATOM   4869  C  CZ    . TYR A 1 606 ? 119.666 125.654 100.278 1.00 70.11 ?  606 TYR A CZ    1 
ATOM   4870  O  OH    . TYR A 1 606 ? 120.875 126.087 99.786  1.00 70.97 ?  606 TYR A OH    1 
ATOM   4871  N  N     . GLY A 1 607 ? 114.621 122.906 104.802 1.00 80.04 ?  607 GLY A N     1 
ATOM   4872  C  CA    . GLY A 1 607 ? 113.431 122.446 105.496 1.00 78.48 ?  607 GLY A CA    1 
ATOM   4873  C  C     . GLY A 1 607 ? 113.244 120.960 105.268 1.00 78.34 ?  607 GLY A C     1 
ATOM   4874  O  O     . GLY A 1 607 ? 114.154 120.152 105.496 1.00 78.36 ?  607 GLY A O     1 
ATOM   4875  N  N     . ASN A 1 608 ? 112.054 120.579 104.805 1.00 79.97 ?  608 ASN A N     1 
ATOM   4876  C  CA    . ASN A 1 608 ? 111.750 119.196 104.460 1.00 81.03 ?  608 ASN A CA    1 
ATOM   4877  C  C     . ASN A 1 608 ? 111.788 118.960 102.954 1.00 80.88 ?  608 ASN A C     1 
ATOM   4878  O  O     . ASN A 1 608 ? 111.151 118.028 102.452 1.00 80.73 ?  608 ASN A O     1 
ATOM   4879  C  CB    . ASN A 1 608 ? 110.389 118.794 105.029 1.00 80.47 ?  608 ASN A CB    1 
ATOM   4880  C  CG    . ASN A 1 608 ? 110.338 118.894 106.543 1.00 81.27 ?  608 ASN A CG    1 
ATOM   4881  O  OD1   . ASN A 1 608 ? 111.371 118.983 107.208 1.00 80.58 ?  608 ASN A OD1   1 
ATOM   4882  N  ND2   . ASN A 1 608 ? 109.130 118.876 107.096 1.00 80.54 ?  608 ASN A ND2   1 
ATOM   4883  N  N     . SER A 1 609 ? 112.529 119.789 102.225 1.00 77.90 ?  609 SER A N     1 
ATOM   4884  C  CA    . SER A 1 609 ? 112.629 119.702 100.775 1.00 77.94 ?  609 SER A CA    1 
ATOM   4885  C  C     . SER A 1 609 ? 114.084 119.514 100.370 1.00 77.93 ?  609 SER A C     1 
ATOM   4886  O  O     . SER A 1 609 ? 114.977 120.183 100.899 1.00 78.15 ?  609 SER A O     1 
ATOM   4887  C  CB    . SER A 1 609 ? 112.062 120.958 100.109 1.00 76.58 ?  609 SER A CB    1 
ATOM   4888  O  OG    . SER A 1 609 ? 112.797 122.111 100.486 1.00 77.68 ?  609 SER A OG    1 
ATOM   4889  N  N     . LYS A 1 610 ? 114.315 118.607 99.427  1.00 66.97 ?  610 LYS A N     1 
ATOM   4890  C  CA    . LYS A 1 610 ? 115.648 118.315 98.917  1.00 66.32 ?  610 LYS A CA    1 
ATOM   4891  C  C     . LYS A 1 610 ? 115.768 118.846 97.496  1.00 66.53 ?  610 LYS A C     1 
ATOM   4892  O  O     . LYS A 1 610 ? 114.923 118.554 96.645  1.00 67.67 ?  610 LYS A O     1 
ATOM   4893  C  CB    . LYS A 1 610 ? 115.930 116.813 98.952  1.00 66.92 ?  610 LYS A CB    1 
ATOM   4894  C  CG    . LYS A 1 610 ? 116.951 116.343 97.930  1.00 66.39 ?  610 LYS A CG    1 
ATOM   4895  C  CD    . LYS A 1 610 ? 117.597 115.035 98.354  1.00 66.95 ?  610 LYS A CD    1 
ATOM   4896  C  CE    . LYS A 1 610 ? 118.081 115.092 99.795  1.00 66.22 ?  610 LYS A CE    1 
ATOM   4897  N  NZ    . LYS A 1 610 ? 119.059 116.193 100.006 1.00 66.39 1  610 LYS A NZ    1 
ATOM   4898  N  N     . THR A 1 611 ? 116.818 119.625 97.245  1.00 64.78 ?  611 THR A N     1 
ATOM   4899  C  CA    . THR A 1 611 ? 117.032 120.246 95.946  1.00 63.63 ?  611 THR A CA    1 
ATOM   4900  C  C     . THR A 1 611 ? 118.502 120.145 95.574  1.00 62.02 ?  611 THR A C     1 
ATOM   4901  O  O     . THR A 1 611 ? 119.374 120.076 96.442  1.00 61.18 ?  611 THR A O     1 
ATOM   4902  C  CB    . THR A 1 611 ? 116.587 121.712 95.945  1.00 64.51 ?  611 THR A CB    1 
ATOM   4903  O  OG1   . THR A 1 611 ? 117.020 122.342 94.733  1.00 68.33 ?  611 THR A OG1   1 
ATOM   4904  C  CG2   . THR A 1 611 ? 117.177 122.443 97.136  1.00 61.51 ?  611 THR A CG2   1 
ATOM   4905  N  N     . TYR A 1 612 ? 118.769 120.139 94.271  1.00 55.17 ?  612 TYR A N     1 
ATOM   4906  C  CA    . TYR A 1 612 ? 120.112 119.940 93.748  1.00 53.75 ?  612 TYR A CA    1 
ATOM   4907  C  C     . TYR A 1 612 ? 120.540 121.154 92.937  1.00 55.99 ?  612 TYR A C     1 
ATOM   4908  O  O     . TYR A 1 612 ? 119.747 121.722 92.181  1.00 55.12 ?  612 TYR A O     1 
ATOM   4909  C  CB    . TYR A 1 612 ? 120.206 118.678 92.876  1.00 56.44 ?  612 TYR A CB    1 
ATOM   4910  C  CG    . TYR A 1 612 ? 119.711 117.404 93.532  1.00 58.31 ?  612 TYR A CG    1 
ATOM   4911  C  CD1   . TYR A 1 612 ? 118.366 117.220 93.830  1.00 57.73 ?  612 TYR A CD1   1 
ATOM   4912  C  CD2   . TYR A 1 612 ? 120.598 116.396 93.879  1.00 57.67 ?  612 TYR A CD2   1 
ATOM   4913  C  CE1   . TYR A 1 612 ? 117.918 116.063 94.431  1.00 58.44 ?  612 TYR A CE1   1 
ATOM   4914  C  CE2   . TYR A 1 612 ? 120.159 115.234 94.482  1.00 58.52 ?  612 TYR A CE2   1 
ATOM   4915  C  CZ    . TYR A 1 612 ? 118.818 115.074 94.756  1.00 60.23 ?  612 TYR A CZ    1 
ATOM   4916  O  OH    . TYR A 1 612 ? 118.378 113.918 95.359  1.00 60.85 ?  612 TYR A OH    1 
ATOM   4917  N  N     . TYR A 1 613 ? 121.801 121.544 93.101  1.00 51.49 ?  613 TYR A N     1 
ATOM   4918  C  CA    . TYR A 1 613 ? 122.368 122.701 92.410  1.00 42.49 ?  613 TYR A CA    1 
ATOM   4919  C  C     . TYR A 1 613 ? 123.558 122.285 91.561  1.00 41.14 ?  613 TYR A C     1 
ATOM   4920  O  O     . TYR A 1 613 ? 124.670 122.106 92.091  1.00 44.64 ?  613 TYR A O     1 
ATOM   4921  C  CB    . TYR A 1 613 ? 122.785 123.778 93.410  1.00 41.40 ?  613 TYR A CB    1 
ATOM   4922  C  CG    . TYR A 1 613 ? 123.401 124.997 92.764  1.00 41.89 ?  613 TYR A CG    1 
ATOM   4923  C  CD1   . TYR A 1 613 ? 122.787 125.622 91.689  1.00 42.79 ?  613 TYR A CD1   1 
ATOM   4924  C  CD2   . TYR A 1 613 ? 124.597 125.523 93.230  1.00 42.04 ?  613 TYR A CD2   1 
ATOM   4925  C  CE1   . TYR A 1 613 ? 123.343 126.737 91.098  1.00 43.12 ?  613 TYR A CE1   1 
ATOM   4926  C  CE2   . TYR A 1 613 ? 125.163 126.637 92.646  1.00 43.78 ?  613 TYR A CE2   1 
ATOM   4927  C  CZ    . TYR A 1 613 ? 124.532 127.240 91.581  1.00 46.61 ?  613 TYR A CZ    1 
ATOM   4928  O  OH    . TYR A 1 613 ? 125.090 128.351 90.994  1.00 46.20 ?  613 TYR A OH    1 
ATOM   4929  N  N     . PRO A 1 614 ? 123.386 122.113 90.255  1.00 40.55 ?  614 PRO A N     1 
ATOM   4930  C  CA    . PRO A 1 614 ? 124.549 121.920 89.386  1.00 40.16 ?  614 PRO A CA    1 
ATOM   4931  C  C     . PRO A 1 614 ? 125.407 123.173 89.358  1.00 40.09 ?  614 PRO A C     1 
ATOM   4932  O  O     . PRO A 1 614 ? 124.918 124.292 89.533  1.00 43.40 ?  614 PRO A O     1 
ATOM   4933  C  CB    . PRO A 1 614 ? 123.933 121.636 88.010  1.00 37.04 ?  614 PRO A CB    1 
ATOM   4934  C  CG    . PRO A 1 614 ? 122.479 121.381 88.262  1.00 43.01 ?  614 PRO A CG    1 
ATOM   4935  C  CD    . PRO A 1 614 ? 122.127 122.135 89.498  1.00 42.07 ?  614 PRO A CD    1 
ATOM   4936  N  N     . MET A 1 615 ? 126.703 122.974 89.144  1.00 37.48 ?  615 MET A N     1 
ATOM   4937  C  CA    . MET A 1 615 ? 127.608 124.105 89.057  1.00 37.01 ?  615 MET A CA    1 
ATOM   4938  C  C     . MET A 1 615 ? 127.240 124.971 87.854  1.00 41.63 ?  615 MET A C     1 
ATOM   4939  O  O     . MET A 1 615 ? 126.750 124.463 86.842  1.00 38.54 ?  615 MET A O     1 
ATOM   4940  C  CB    . MET A 1 615 ? 129.054 123.629 88.950  1.00 33.82 ?  615 MET A CB    1 
ATOM   4941  C  CG    . MET A 1 615 ? 129.708 123.384 90.297  1.00 36.13 ?  615 MET A CG    1 
ATOM   4942  S  SD    . MET A 1 615 ? 129.256 124.627 91.522  1.00 52.76 ?  615 MET A SD    1 
ATOM   4943  C  CE    . MET A 1 615 ? 128.317 123.643 92.685  1.00 35.65 ?  615 MET A CE    1 
ATOM   4944  N  N     . PRO A 1 616 ? 127.433 126.285 87.951  1.00 40.49 ?  616 PRO A N     1 
ATOM   4945  C  CA    . PRO A 1 616 ? 127.011 127.177 86.864  1.00 35.85 ?  616 PRO A CA    1 
ATOM   4946  C  C     . PRO A 1 616 ? 127.678 126.815 85.546  1.00 36.86 ?  616 PRO A C     1 
ATOM   4947  O  O     . PRO A 1 616 ? 128.904 126.736 85.451  1.00 38.67 ?  616 PRO A O     1 
ATOM   4948  C  CB    . PRO A 1 616 ? 127.447 128.559 87.357  1.00 36.67 ?  616 PRO A CB    1 
ATOM   4949  C  CG    . PRO A 1 616 ? 127.492 128.425 88.841  1.00 38.59 ?  616 PRO A CG    1 
ATOM   4950  C  CD    . PRO A 1 616 ? 127.948 127.031 89.111  1.00 35.46 ?  616 PRO A CD    1 
ATOM   4951  N  N     . GLY A 1 617 ? 126.855 126.601 84.524  1.00 36.72 ?  617 GLY A N     1 
ATOM   4952  C  CA    . GLY A 1 617 ? 127.353 126.220 83.221  1.00 31.13 ?  617 GLY A CA    1 
ATOM   4953  C  C     . GLY A 1 617 ? 127.732 124.765 83.078  1.00 38.40 ?  617 GLY A C     1 
ATOM   4954  O  O     . GLY A 1 617 ? 128.301 124.392 82.047  1.00 40.80 ?  617 GLY A O     1 
ATOM   4955  N  N     . LEU A 1 618 ? 127.445 123.934 84.077  1.00 39.29 ?  618 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 618 ? 127.798 122.523 83.999  1.00 34.62 ?  618 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 618 ? 126.991 121.830 82.909  1.00 39.88 ?  618 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 618 ? 125.786 122.051 82.765  1.00 40.59 ?  618 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 618 ? 127.564 121.836 85.344  1.00 34.82 ?  618 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 618 ? 127.894 120.345 85.434  1.00 37.41 ?  618 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 618 ? 129.364 120.088 85.143  1.00 34.92 ?  618 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 618 ? 127.511 119.787 86.795  1.00 35.44 ?  618 LEU A CD2   1 
ATOM   4963  N  N     . ALA A 1 619 ? 127.669 120.987 82.140  1.00 43.40 ?  619 ALA A N     1 
ATOM   4964  C  CA    . ALA A 1 619 ? 127.056 120.237 81.054  1.00 43.12 ?  619 ALA A CA    1 
ATOM   4965  C  C     . ALA A 1 619 ? 127.902 118.992 80.817  1.00 44.84 ?  619 ALA A C     1 
ATOM   4966  O  O     . ALA A 1 619 ? 128.766 118.647 81.629  1.00 50.01 ?  619 ALA A O     1 
ATOM   4967  C  CB    . ALA A 1 619 ? 126.928 121.100 79.794  1.00 41.78 ?  619 ALA A CB    1 
ATOM   4968  N  N     . SER A 1 620 ? 127.651 118.311 79.700  1.00 50.05 ?  620 SER A N     1 
ATOM   4969  C  CA    . SER A 1 620 ? 128.471 117.161 79.344  1.00 50.39 ?  620 SER A CA    1 
ATOM   4970  C  C     . SER A 1 620 ? 129.719 117.572 78.574  1.00 50.52 ?  620 SER A C     1 
ATOM   4971  O  O     . SER A 1 620 ? 130.709 116.833 78.568  1.00 54.16 ?  620 SER A O     1 
ATOM   4972  C  CB    . SER A 1 620 ? 127.651 116.163 78.525  1.00 53.17 ?  620 SER A CB    1 
ATOM   4973  O  OG    . SER A 1 620 ? 126.485 115.768 79.227  1.00 55.31 ?  620 SER A OG    1 
ATOM   4974  N  N     . ASN A 1 621 ? 129.692 118.739 77.927  1.00 48.00 ?  621 ASN A N     1 
ATOM   4975  C  CA    . ASN A 1 621 ? 130.852 119.189 77.168  1.00 48.37 ?  621 ASN A CA    1 
ATOM   4976  C  C     . ASN A 1 621 ? 131.946 119.738 78.075  1.00 51.61 ?  621 ASN A C     1 
ATOM   4977  O  O     . ASN A 1 621 ? 133.104 119.839 77.653  1.00 51.96 ?  621 ASN A O     1 
ATOM   4978  C  CB    . ASN A 1 621 ? 130.430 120.243 76.143  1.00 49.02 ?  621 ASN A CB    1 
ATOM   4979  C  CG    . ASN A 1 621 ? 130.375 121.639 76.731  1.00 51.03 ?  621 ASN A CG    1 
ATOM   4980  O  OD1   . ASN A 1 621 ? 129.490 121.956 77.524  1.00 50.38 ?  621 ASN A OD1   1 
ATOM   4981  N  ND2   . ASN A 1 621 ? 131.323 122.482 76.342  1.00 47.50 ?  621 ASN A ND2   1 
ATOM   4982  N  N     . ASN A 1 622 ? 131.607 120.099 79.312  1.00 44.03 ?  622 ASN A N     1 
ATOM   4983  C  CA    . ASN A 1 622 ? 132.576 120.607 80.276  1.00 40.24 ?  622 ASN A CA    1 
ATOM   4984  C  C     . ASN A 1 622 ? 132.437 119.914 81.628  1.00 42.76 ?  622 ASN A C     1 
ATOM   4985  O  O     . ASN A 1 622 ? 132.727 120.505 82.669  1.00 48.61 ?  622 ASN A O     1 
ATOM   4986  C  CB    . ASN A 1 622 ? 132.453 122.124 80.425  1.00 42.91 ?  622 ASN A CB    1 
ATOM   4987  C  CG    . ASN A 1 622 ? 131.055 122.572 80.825  1.00 42.30 ?  622 ASN A CG    1 
ATOM   4988  O  OD1   . ASN A 1 622 ? 130.338 121.872 81.536  1.00 43.38 ?  622 ASN A OD1   1 
ATOM   4989  N  ND2   . ASN A 1 622 ? 130.668 123.757 80.368  1.00 41.97 ?  622 ASN A ND2   1 
ATOM   4990  N  N     . TRP A 1 623 ? 131.982 118.659 81.622  1.00 37.70 ?  623 TRP A N     1 
ATOM   4991  C  CA    . TRP A 1 623 ? 131.811 117.928 82.873  1.00 38.13 ?  623 TRP A CA    1 
ATOM   4992  C  C     . TRP A 1 623 ? 133.145 117.695 83.569  1.00 38.97 ?  623 TRP A C     1 
ATOM   4993  O  O     . TRP A 1 623 ? 133.255 117.867 84.789  1.00 36.89 ?  623 TRP A O     1 
ATOM   4994  C  CB    . TRP A 1 623 ? 131.108 116.598 82.605  1.00 41.13 ?  623 TRP A CB    1 
ATOM   4995  C  CG    . TRP A 1 623 ? 130.986 115.723 83.814  1.00 37.94 ?  623 TRP A CG    1 
ATOM   4996  C  CD1   . TRP A 1 623 ? 131.869 114.771 84.227  1.00 37.18 ?  623 TRP A CD1   1 
ATOM   4997  C  CD2   . TRP A 1 623 ? 129.913 115.713 84.762  1.00 36.34 ?  623 TRP A CD2   1 
ATOM   4998  N  NE1   . TRP A 1 623 ? 131.417 114.170 85.375  1.00 37.99 ?  623 TRP A NE1   1 
ATOM   4999  C  CE2   . TRP A 1 623 ? 130.217 114.730 85.723  1.00 38.89 ?  623 TRP A CE2   1 
ATOM   5000  C  CE3   . TRP A 1 623 ? 128.727 116.439 84.890  1.00 37.48 ?  623 TRP A CE3   1 
ATOM   5001  C  CZ2   . TRP A 1 623 ? 129.378 114.457 86.800  1.00 37.40 ?  623 TRP A CZ2   1 
ATOM   5002  C  CZ3   . TRP A 1 623 ? 127.895 116.166 85.960  1.00 38.40 ?  623 TRP A CZ3   1 
ATOM   5003  C  CH2   . TRP A 1 623 ? 128.226 115.184 86.900  1.00 37.73 ?  623 TRP A CH2   1 
ATOM   5004  N  N     . PHE A 1 624 ? 134.169 117.300 82.816  1.00 43.16 ?  624 PHE A N     1 
ATOM   5005  C  CA    . PHE A 1 624 ? 135.457 116.971 83.411  1.00 41.82 ?  624 PHE A CA    1 
ATOM   5006  C  C     . PHE A 1 624 ? 136.344 118.187 83.631  1.00 42.59 ?  624 PHE A C     1 
ATOM   5007  O  O     . PHE A 1 624 ? 137.337 118.086 84.360  1.00 50.03 ?  624 PHE A O     1 
ATOM   5008  C  CB    . PHE A 1 624 ? 136.183 115.940 82.546  1.00 41.56 ?  624 PHE A CB    1 
ATOM   5009  C  CG    . PHE A 1 624 ? 135.502 114.602 82.513  1.00 45.32 ?  624 PHE A CG    1 
ATOM   5010  C  CD1   . PHE A 1 624 ? 135.485 113.795 83.638  1.00 42.10 ?  624 PHE A CD1   1 
ATOM   5011  C  CD2   . PHE A 1 624 ? 134.861 114.161 81.368  1.00 44.92 ?  624 PHE A CD2   1 
ATOM   5012  C  CE1   . PHE A 1 624 ? 134.853 112.570 83.619  1.00 41.33 ?  624 PHE A CE1   1 
ATOM   5013  C  CE2   . PHE A 1 624 ? 134.226 112.936 81.344  1.00 42.77 ?  624 PHE A CE2   1 
ATOM   5014  C  CZ    . PHE A 1 624 ? 134.222 112.139 82.469  1.00 45.45 ?  624 PHE A CZ    1 
ATOM   5015  N  N     . PHE A 1 625 ? 136.013 119.328 83.027  1.00 34.98 ?  625 PHE A N     1 
ATOM   5016  C  CA    . PHE A 1 625 ? 136.682 120.570 83.389  1.00 32.84 ?  625 PHE A CA    1 
ATOM   5017  C  C     . PHE A 1 625 ? 136.194 121.105 84.725  1.00 32.46 ?  625 PHE A C     1 
ATOM   5018  O  O     . PHE A 1 625 ? 136.894 121.906 85.353  1.00 36.35 ?  625 PHE A O     1 
ATOM   5019  C  CB    . PHE A 1 625 ? 136.488 121.620 82.298  1.00 31.54 ?  625 PHE A CB    1 
ATOM   5020  C  CG    . PHE A 1 625 ? 137.260 121.339 81.045  1.00 30.72 ?  625 PHE A CG    1 
ATOM   5021  C  CD1   . PHE A 1 625 ? 138.642 121.348 81.054  1.00 33.14 ?  625 PHE A CD1   1 
ATOM   5022  C  CD2   . PHE A 1 625 ? 136.605 121.071 79.855  1.00 34.06 ?  625 PHE A CD2   1 
ATOM   5023  C  CE1   . PHE A 1 625 ? 139.358 121.094 79.904  1.00 36.70 ?  625 PHE A CE1   1 
ATOM   5024  C  CE2   . PHE A 1 625 ? 137.317 120.816 78.702  1.00 32.14 ?  625 PHE A CE2   1 
ATOM   5025  C  CZ    . PHE A 1 625 ? 138.695 120.826 78.727  1.00 36.32 ?  625 PHE A CZ    1 
ATOM   5026  N  N     . TYR A 1 626 ? 135.015 120.682 85.171  1.00 29.43 ?  626 TYR A N     1 
ATOM   5027  C  CA    . TYR A 1 626 ? 134.514 121.017 86.502  1.00 31.49 ?  626 TYR A CA    1 
ATOM   5028  C  C     . TYR A 1 626 ? 134.996 120.007 87.535  1.00 27.64 ?  626 TYR A C     1 
ATOM   5029  O  O     . TYR A 1 626 ? 134.217 119.440 88.297  1.00 30.79 ?  626 TYR A O     1 
ATOM   5030  C  CB    . TYR A 1 626 ? 132.993 121.094 86.481  1.00 32.51 ?  626 TYR A CB    1 
ATOM   5031  C  CG    . TYR A 1 626 ? 132.460 122.478 86.214  1.00 28.67 ?  626 TYR A CG    1 
ATOM   5032  C  CD1   . TYR A 1 626 ? 132.589 123.485 87.158  1.00 32.63 ?  626 TYR A CD1   1 
ATOM   5033  C  CD2   . TYR A 1 626 ? 131.829 122.779 85.015  1.00 30.61 ?  626 TYR A CD2   1 
ATOM   5034  C  CE1   . TYR A 1 626 ? 132.105 124.752 86.917  1.00 29.49 ?  626 TYR A CE1   1 
ATOM   5035  C  CE2   . TYR A 1 626 ? 131.341 124.042 84.766  1.00 28.96 ?  626 TYR A CE2   1 
ATOM   5036  C  CZ    . TYR A 1 626 ? 131.483 125.024 85.721  1.00 27.83 ?  626 TYR A CZ    1 
ATOM   5037  O  OH    . TYR A 1 626 ? 131.000 126.286 85.481  1.00 34.46 ?  626 TYR A OH    1 
ATOM   5038  N  N     . LYS A 1 627 ? 136.307 119.786 87.560  1.00 31.50 ?  627 LYS A N     1 
ATOM   5039  C  CA    . LYS A 1 627 ? 136.895 118.830 88.486  1.00 31.57 ?  627 LYS A CA    1 
ATOM   5040  C  C     . LYS A 1 627 ? 136.677 119.284 89.921  1.00 31.68 ?  627 LYS A C     1 
ATOM   5041  O  O     . LYS A 1 627 ? 136.885 120.454 90.254  1.00 35.85 ?  627 LYS A O     1 
ATOM   5042  C  CB    . LYS A 1 627 ? 138.385 118.675 88.189  1.00 34.95 ?  627 LYS A CB    1 
ATOM   5043  C  CG    . LYS A 1 627 ? 139.082 117.598 88.991  1.00 34.41 ?  627 LYS A CG    1 
ATOM   5044  C  CD    . LYS A 1 627 ? 140.486 117.366 88.467  1.00 32.48 ?  627 LYS A CD    1 
ATOM   5045  C  CE    . LYS A 1 627 ? 141.211 116.310 89.276  1.00 38.41 ?  627 LYS A CE    1 
ATOM   5046  N  NZ    . LYS A 1 627 ? 142.640 116.203 88.875  1.00 39.70 1  627 LYS A NZ    1 
ATOM   5047  N  N     . GLU A 1 628 ? 136.250 118.356 90.772  1.00 35.59 ?  628 GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 628 ? 136.001 118.690 92.166  1.00 36.22 ?  628 GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 628 ? 137.307 119.003 92.885  1.00 39.79 ?  628 GLU A C     1 
ATOM   5050  O  O     . GLU A 1 628 ? 138.372 118.481 92.546  1.00 42.87 ?  628 GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 628 ? 135.268 117.547 92.865  1.00 37.35 ?  628 GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 628 ? 133.885 117.271 92.302  1.00 39.53 ?  628 GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 628 ? 133.114 116.254 93.120  1.00 47.64 ?  628 GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 628 ? 133.557 115.931 94.242  1.00 43.85 ?  628 GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 628 ? 132.061 115.782 92.642  1.00 44.12 -1 628 GLU A OE2   1 
ATOM   5056  N  N     . ALA A 1 629 ? 137.213 119.877 93.889  1.00 38.57 ?  629 ALA A N     1 
ATOM   5057  C  CA    . ALA A 1 629 ? 138.404 120.332 94.598  1.00 34.48 ?  629 ALA A CA    1 
ATOM   5058  C  C     . ALA A 1 629 ? 139.096 119.197 95.339  1.00 37.29 ?  629 ALA A C     1 
ATOM   5059  O  O     . ALA A 1 629 ? 140.312 119.248 95.554  1.00 44.58 ?  629 ALA A O     1 
ATOM   5060  C  CB    . ALA A 1 629 ? 138.036 121.449 95.570  1.00 35.14 ?  629 ALA A CB    1 
ATOM   5061  N  N     . TYR A 1 630 ? 138.346 118.176 95.751  1.00 42.65 ?  630 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 630 ? 138.951 117.080 96.498  1.00 41.94 ?  630 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 630 ? 139.765 116.159 95.599  1.00 44.19 ?  630 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 630 ? 140.711 115.518 96.068  1.00 44.91 ?  630 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 630 ? 137.870 116.290 97.231  1.00 39.33 ?  630 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 630 ? 137.086 117.116 98.221  1.00 40.78 ?  630 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 630 ? 137.624 117.445 99.456  1.00 38.92 ?  630 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 630 ? 135.808 117.563 97.921  1.00 40.39 ?  630 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 630 ? 136.911 118.197 100.365 1.00 39.65 ?  630 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 630 ? 135.088 118.316 98.824  1.00 40.55 ?  630 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 630 ? 135.645 118.630 100.045 1.00 44.72 ?  630 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 630 ? 134.933 119.379 100.951 1.00 48.31 ?  630 TYR A OH    1 
ATOM   5073  N  N     . ASP A 1 631 ? 139.423 116.083 94.314  1.00 40.74 ?  631 ASP A N     1 
ATOM   5074  C  CA    . ASP A 1 631 ? 140.107 115.180 93.399  1.00 39.43 ?  631 ASP A CA    1 
ATOM   5075  C  C     . ASP A 1 631 ? 141.378 115.769 92.802  1.00 43.72 ?  631 ASP A C     1 
ATOM   5076  O  O     . ASP A 1 631 ? 142.117 115.042 92.132  1.00 46.48 ?  631 ASP A O     1 
ATOM   5077  C  CB    . ASP A 1 631 ? 139.164 114.768 92.264  1.00 42.42 ?  631 ASP A CB    1 
ATOM   5078  C  CG    . ASP A 1 631 ? 137.811 114.310 92.766  1.00 49.41 ?  631 ASP A CG    1 
ATOM   5079  O  OD1   . ASP A 1 631 ? 137.762 113.611 93.799  1.00 48.62 ?  631 ASP A OD1   1 
ATOM   5080  O  OD2   . ASP A 1 631 ? 136.794 114.648 92.125  1.00 51.07 -1 631 ASP A OD2   1 
ATOM   5081  N  N     . MET A 1 632 ? 141.657 117.049 93.025  1.00 39.69 ?  632 MET A N     1 
ATOM   5082  C  CA    . MET A 1 632 ? 142.808 117.694 92.415  1.00 37.62 ?  632 MET A CA    1 
ATOM   5083  C  C     . MET A 1 632 ? 143.963 117.812 93.401  1.00 36.03 ?  632 MET A C     1 
ATOM   5084  O  O     . MET A 1 632 ? 143.791 117.721 94.619  1.00 38.98 ?  632 MET A O     1 
ATOM   5085  C  CB    . MET A 1 632 ? 142.443 119.079 91.876  1.00 37.51 ?  632 MET A CB    1 
ATOM   5086  C  CG    . MET A 1 632 ? 141.483 119.872 92.723  1.00 39.98 ?  632 MET A CG    1 
ATOM   5087  S  SD    . MET A 1 632 ? 141.214 121.516 92.041  1.00 47.46 ?  632 MET A SD    1 
ATOM   5088  C  CE    . MET A 1 632 ? 140.101 121.150 90.690  1.00 33.77 ?  632 MET A CE    1 
ATOM   5089  N  N     . ASP A 1 633 ? 145.154 118.020 92.848  1.00 34.02 ?  633 ASP A N     1 
ATOM   5090  C  CA    . ASP A 1 633 ? 146.360 118.177 93.651  1.00 30.19 ?  633 ASP A CA    1 
ATOM   5091  C  C     . ASP A 1 633 ? 146.329 119.518 94.373  1.00 28.33 ?  633 ASP A C     1 
ATOM   5092  O  O     . ASP A 1 633 ? 146.178 120.569 93.740  1.00 30.74 ?  633 ASP A O     1 
ATOM   5093  C  CB    . ASP A 1 633 ? 147.594 118.076 92.759  1.00 26.25 ?  633 ASP A CB    1 
ATOM   5094  C  CG    . ASP A 1 633 ? 148.876 117.907 93.548  1.00 38.00 ?  633 ASP A CG    1 
ATOM   5095  O  OD1   . ASP A 1 633 ? 148.807 117.770 94.788  1.00 39.38 ?  633 ASP A OD1   1 
ATOM   5096  O  OD2   . ASP A 1 633 ? 149.958 117.916 92.926  1.00 36.15 -1 633 ASP A OD2   1 
ATOM   5097  N  N     . MET A 1 634 ? 146.470 119.485 95.699  1.00 26.57 ?  634 MET A N     1 
ATOM   5098  C  CA    . MET A 1 634 ? 146.511 120.723 96.466  1.00 23.16 ?  634 MET A CA    1 
ATOM   5099  C  C     . MET A 1 634 ? 147.763 121.540 96.181  1.00 25.24 ?  634 MET A C     1 
ATOM   5100  O  O     . MET A 1 634 ? 147.768 122.746 96.440  1.00 26.06 ?  634 MET A O     1 
ATOM   5101  C  CB    . MET A 1 634 ? 146.409 120.428 97.962  1.00 23.97 ?  634 MET A CB    1 
ATOM   5102  C  CG    . MET A 1 634 ? 144.984 120.280 98.460  1.00 29.04 ?  634 MET A CG    1 
ATOM   5103  S  SD    . MET A 1 634 ? 143.959 121.700 98.032  1.00 38.84 ?  634 MET A SD    1 
ATOM   5104  C  CE    . MET A 1 634 ? 142.751 120.929 96.959  1.00 28.17 ?  634 MET A CE    1 
ATOM   5105  N  N     . PHE A 1 635 ? 148.819 120.917 95.654  1.00 24.58 ?  635 PHE A N     1 
ATOM   5106  C  CA    . PHE A 1 635 ? 149.994 121.684 95.253  1.00 21.50 ?  635 PHE A CA    1 
ATOM   5107  C  C     . PHE A 1 635 ? 149.676 122.601 94.078  1.00 21.21 ?  635 PHE A C     1 
ATOM   5108  O  O     . PHE A 1 635 ? 150.119 123.754 94.046  1.00 26.87 ?  635 PHE A O     1 
ATOM   5109  C  CB    . PHE A 1 635 ? 151.146 120.740 94.910  1.00 20.93 ?  635 PHE A CB    1 
ATOM   5110  C  CG    . PHE A 1 635 ? 151.996 120.369 96.092  1.00 27.72 ?  635 PHE A CG    1 
ATOM   5111  C  CD1   . PHE A 1 635 ? 151.421 120.132 97.329  1.00 22.95 ?  635 PHE A CD1   1 
ATOM   5112  C  CD2   . PHE A 1 635 ? 153.369 120.262 95.968  1.00 23.97 ?  635 PHE A CD2   1 
ATOM   5113  C  CE1   . PHE A 1 635 ? 152.200 119.795 98.417  1.00 23.47 ?  635 PHE A CE1   1 
ATOM   5114  C  CE2   . PHE A 1 635 ? 154.152 119.924 97.053  1.00 26.52 ?  635 PHE A CE2   1 
ATOM   5115  C  CZ    . PHE A 1 635 ? 153.565 119.690 98.278  1.00 24.17 ?  635 PHE A CZ    1 
ATOM   5116  N  N     . LYS A 1 636 ? 148.891 122.117 93.115  1.00 26.05 ?  636 LYS A N     1 
ATOM   5117  C  CA    . LYS A 1 636 ? 148.516 122.957 91.983  1.00 24.89 ?  636 LYS A CA    1 
ATOM   5118  C  C     . LYS A 1 636 ? 147.523 124.040 92.391  1.00 23.61 ?  636 LYS A C     1 
ATOM   5119  O  O     . LYS A 1 636 ? 147.564 125.153 91.856  1.00 31.09 ?  636 LYS A O     1 
ATOM   5120  C  CB    . LYS A 1 636 ? 147.949 122.092 90.860  1.00 27.32 ?  636 LYS A CB    1 
ATOM   5121  C  CG    . LYS A 1 636 ? 148.939 121.063 90.335  1.00 27.16 ?  636 LYS A CG    1 
ATOM   5122  C  CD    . LYS A 1 636 ? 149.005 121.068 88.821  1.00 30.50 ?  636 LYS A CD    1 
ATOM   5123  C  CE    . LYS A 1 636 ? 148.855 119.665 88.257  1.00 32.33 ?  636 LYS A CE    1 
ATOM   5124  N  NZ    . LYS A 1 636 ? 149.016 119.646 86.778  1.00 32.76 1  636 LYS A NZ    1 
ATOM   5125  N  N     . VAL A 1 637 ? 146.638 123.744 93.345  1.00 20.12 ?  637 VAL A N     1 
ATOM   5126  C  CA    . VAL A 1 637 ? 145.751 124.775 93.874  1.00 17.76 ?  637 VAL A CA    1 
ATOM   5127  C  C     . VAL A 1 637 ? 146.555 125.831 94.623  1.00 23.34 ?  637 VAL A C     1 
ATOM   5128  O  O     . VAL A 1 637 ? 146.259 127.029 94.543  1.00 26.50 ?  637 VAL A O     1 
ATOM   5129  C  CB    . VAL A 1 637 ? 144.668 124.141 94.766  1.00 21.56 ?  637 VAL A CB    1 
ATOM   5130  C  CG1   . VAL A 1 637 ? 143.682 125.196 95.239  1.00 23.10 ?  637 VAL A CG1   1 
ATOM   5131  C  CG2   . VAL A 1 637 ? 143.947 123.036 94.014  1.00 24.87 ?  637 VAL A CG2   1 
ATOM   5132  N  N     . VAL A 1 638 ? 147.584 125.407 95.361  1.00 26.37 ?  638 VAL A N     1 
ATOM   5133  C  CA    . VAL A 1 638 ? 148.478 126.355 96.017  1.00 21.65 ?  638 VAL A CA    1 
ATOM   5134  C  C     . VAL A 1 638 ? 149.183 127.215 94.980  1.00 18.06 ?  638 VAL A C     1 
ATOM   5135  O  O     . VAL A 1 638 ? 149.339 128.427 95.160  1.00 31.86 ?  638 VAL A O     1 
ATOM   5136  C  CB    . VAL A 1 638 ? 149.488 125.612 96.913  1.00 21.89 ?  638 VAL A CB    1 
ATOM   5137  C  CG1   . VAL A 1 638 ? 150.703 126.483 97.181  1.00 15.98 ?  638 VAL A CG1   1 
ATOM   5138  C  CG2   . VAL A 1 638 ? 148.841 125.189 98.215  1.00 22.01 ?  638 VAL A CG2   1 
ATOM   5139  N  N     . ASP A 1 639 ? 149.626 126.600 93.883  1.00 13.54 ?  639 ASP A N     1 
ATOM   5140  C  CA    . ASP A 1 639 ? 150.257 127.357 92.807  1.00 16.83 ?  639 ASP A CA    1 
ATOM   5141  C  C     . ASP A 1 639 ? 149.307 128.403 92.240  1.00 24.01 ?  639 ASP A C     1 
ATOM   5142  O  O     . ASP A 1 639 ? 149.703 129.549 92.002  1.00 29.17 ?  639 ASP A O     1 
ATOM   5143  C  CB    . ASP A 1 639 ? 150.721 126.405 91.704  1.00 15.86 ?  639 ASP A CB    1 
ATOM   5144  C  CG    . ASP A 1 639 ? 151.973 125.645 92.079  1.00 29.95 ?  639 ASP A CG    1 
ATOM   5145  O  OD1   . ASP A 1 639 ? 152.858 126.236 92.732  1.00 34.26 ?  639 ASP A OD1   1 
ATOM   5146  O  OD2   . ASP A 1 639 ? 152.074 124.452 91.722  1.00 34.71 -1 639 ASP A OD2   1 
ATOM   5147  N  N     . MET A 1 640 ? 148.045 128.030 92.033  1.00 23.60 ?  640 MET A N     1 
ATOM   5148  C  CA    . MET A 1 640 ? 147.064 128.974 91.504  1.00 21.42 ?  640 MET A CA    1 
ATOM   5149  C  C     . MET A 1 640 ? 146.819 130.125 92.475  1.00 22.11 ?  640 MET A C     1 
ATOM   5150  O  O     . MET A 1 640 ? 146.796 131.297 92.078  1.00 25.58 ?  640 MET A O     1 
ATOM   5151  C  CB    . MET A 1 640 ? 145.760 128.242 91.193  1.00 24.83 ?  640 MET A CB    1 
ATOM   5152  C  CG    . MET A 1 640 ? 144.562 129.153 90.999  1.00 24.53 ?  640 MET A CG    1 
ATOM   5153  S  SD    . MET A 1 640 ? 144.627 130.061 89.447  1.00 27.79 ?  640 MET A SD    1 
ATOM   5154  C  CE    . MET A 1 640 ? 143.631 129.007 88.404  1.00 26.13 ?  640 MET A CE    1 
ATOM   5155  N  N     . ILE A 1 641 ? 146.642 129.808 93.759  1.00 21.70 ?  641 ILE A N     1 
ATOM   5156  C  CA    . ILE A 1 641 ? 146.356 130.846 94.744  1.00 16.23 ?  641 ILE A CA    1 
ATOM   5157  C  C     . ILE A 1 641 ? 147.558 131.765 94.918  1.00 18.08 ?  641 ILE A C     1 
ATOM   5158  O  O     . ILE A 1 641 ? 147.406 132.976 95.111  1.00 25.78 ?  641 ILE A O     1 
ATOM   5159  C  CB    . ILE A 1 641 ? 145.914 130.213 96.076  1.00 24.77 ?  641 ILE A CB    1 
ATOM   5160  C  CG1   . ILE A 1 641 ? 144.661 129.361 95.872  1.00 23.13 ?  641 ILE A CG1   1 
ATOM   5161  C  CG2   . ILE A 1 641 ? 145.634 131.283 97.117  1.00 16.45 ?  641 ILE A CG2   1 
ATOM   5162  C  CD1   . ILE A 1 641 ? 143.566 130.058 95.101  1.00 19.77 ?  641 ILE A CD1   1 
ATOM   5163  N  N     . ALA A 1 642 ? 148.770 131.212 94.845  1.00 13.80 ?  642 ALA A N     1 
ATOM   5164  C  CA    . ALA A 1 642 ? 149.969 132.032 94.933  1.00 14.95 ?  642 ALA A CA    1 
ATOM   5165  C  C     . ALA A 1 642 ? 150.145 132.901 93.697  1.00 15.06 ?  642 ALA A C     1 
ATOM   5166  O  O     . ALA A 1 642 ? 150.656 134.021 93.797  1.00 24.85 ?  642 ALA A O     1 
ATOM   5167  C  CB    . ALA A 1 642 ? 151.195 131.146 95.140  1.00 16.20 ?  642 ALA A CB    1 
ATOM   5168  N  N     . THR A 1 643 ? 149.742 132.401 92.528  1.00 17.82 ?  643 THR A N     1 
ATOM   5169  C  CA    . THR A 1 643 ? 149.739 133.236 91.333  1.00 20.13 ?  643 THR A CA    1 
ATOM   5170  C  C     . THR A 1 643 ? 148.769 134.400 91.486  1.00 18.40 ?  643 THR A C     1 
ATOM   5171  O  O     . THR A 1 643 ? 149.088 135.538 91.126  1.00 22.42 ?  643 THR A O     1 
ATOM   5172  C  CB    . THR A 1 643 ? 149.387 132.395 90.107  1.00 22.01 ?  643 THR A CB    1 
ATOM   5173  O  OG1   . THR A 1 643 ? 150.413 131.420 89.888  1.00 28.71 ?  643 THR A OG1   1 
ATOM   5174  C  CG2   . THR A 1 643 ? 149.263 133.272 88.877  1.00 17.65 ?  643 THR A CG2   1 
ATOM   5175  N  N     . ILE A 1 644 ? 147.578 134.134 92.026  1.00 16.05 ?  644 ILE A N     1 
ATOM   5176  C  CA    . ILE A 1 644 ? 146.624 135.211 92.260  1.00 14.62 ?  644 ILE A CA    1 
ATOM   5177  C  C     . ILE A 1 644 ? 147.108 136.125 93.381  1.00 17.27 ?  644 ILE A C     1 
ATOM   5178  O  O     . ILE A 1 644 ? 146.949 137.350 93.312  1.00 22.60 ?  644 ILE A O     1 
ATOM   5179  C  CB    . ILE A 1 644 ? 145.228 134.636 92.561  1.00 15.77 ?  644 ILE A CB    1 
ATOM   5180  C  CG1   . ILE A 1 644 ? 144.731 133.793 91.388  1.00 14.71 ?  644 ILE A CG1   1 
ATOM   5181  C  CG2   . ILE A 1 644 ? 144.247 135.752 92.851  1.00 7.74  ?  644 ILE A CG2   1 
ATOM   5182  C  CD1   . ILE A 1 644 ? 143.560 132.907 91.735  1.00 22.09 ?  644 ILE A CD1   1 
ATOM   5183  N  N     . GLN A 1 645 ? 147.711 135.547 94.425  1.00 11.57 ?  645 GLN A N     1 
ATOM   5184  C  CA    . GLN A 1 645 ? 148.073 136.322 95.609  1.00 11.89 ?  645 GLN A CA    1 
ATOM   5185  C  C     . GLN A 1 645 ? 149.102 137.403 95.300  1.00 18.71 ?  645 GLN A C     1 
ATOM   5186  O  O     . GLN A 1 645 ? 149.136 138.435 95.979  1.00 23.96 ?  645 GLN A O     1 
ATOM   5187  C  CB    . GLN A 1 645 ? 148.599 135.391 96.702  1.00 8.94  ?  645 GLN A CB    1 
ATOM   5188  C  CG    . GLN A 1 645 ? 148.931 136.079 98.016  1.00 10.21 ?  645 GLN A CG    1 
ATOM   5189  C  CD    . GLN A 1 645 ? 147.714 136.679 98.684  1.00 12.21 ?  645 GLN A CD    1 
ATOM   5190  O  OE1   . GLN A 1 645 ? 146.995 135.997 99.412  1.00 18.33 ?  645 GLN A OE1   1 
ATOM   5191  N  NE2   . GLN A 1 645 ? 147.478 137.961 98.444  1.00 4.73  ?  645 GLN A NE2   1 
ATOM   5192  N  N     . GLN A 1 646 ? 149.938 137.198 94.284  1.00 20.94 ?  646 GLN A N     1 
ATOM   5193  C  CA    . GLN A 1 646 ? 150.966 138.181 93.973  1.00 14.79 ?  646 GLN A CA    1 
ATOM   5194  C  C     . GLN A 1 646 ? 150.395 139.489 93.441  1.00 15.69 ?  646 GLN A C     1 
ATOM   5195  O  O     . GLN A 1 646 ? 151.117 140.490 93.410  1.00 20.87 ?  646 GLN A O     1 
ATOM   5196  C  CB    . GLN A 1 646 ? 151.964 137.596 92.974  1.00 20.94 ?  646 GLN A CB    1 
ATOM   5197  C  CG    . GLN A 1 646 ? 151.520 137.650 91.530  1.00 22.21 ?  646 GLN A CG    1 
ATOM   5198  C  CD    . GLN A 1 646 ? 152.473 136.920 90.607  1.00 30.10 ?  646 GLN A CD    1 
ATOM   5199  O  OE1   . GLN A 1 646 ? 152.099 135.948 89.953  1.00 25.03 ?  646 GLN A OE1   1 
ATOM   5200  N  NE2   . GLN A 1 646 ? 153.714 137.386 90.552  1.00 26.74 ?  646 GLN A NE2   1 
ATOM   5201  N  N     . HIS A 1 647 ? 149.126 139.512 93.040  1.00 21.92 ?  647 HIS A N     1 
ATOM   5202  C  CA    . HIS A 1 647 ? 148.465 140.731 92.600  1.00 14.76 ?  647 HIS A CA    1 
ATOM   5203  C  C     . HIS A 1 647 ? 147.439 141.241 93.601  1.00 15.27 ?  647 HIS A C     1 
ATOM   5204  O  O     . HIS A 1 647 ? 146.778 142.248 93.333  1.00 25.12 ?  647 HIS A O     1 
ATOM   5205  C  CB    . HIS A 1 647 ? 147.791 140.504 91.243  1.00 11.36 ?  647 HIS A CB    1 
ATOM   5206  C  CG    . HIS A 1 647 ? 148.704 139.932 90.207  1.00 16.48 ?  647 HIS A CG    1 
ATOM   5207  N  ND1   . HIS A 1 647 ? 149.838 140.584 89.775  1.00 19.03 ?  647 HIS A ND1   1 
ATOM   5208  C  CD2   . HIS A 1 647 ? 148.654 138.768 89.519  1.00 17.59 ?  647 HIS A CD2   1 
ATOM   5209  C  CE1   . HIS A 1 647 ? 150.448 139.846 88.864  1.00 20.83 ?  647 HIS A CE1   1 
ATOM   5210  N  NE2   . HIS A 1 647 ? 149.749 138.740 88.690  1.00 20.71 ?  647 HIS A NE2   1 
ATOM   5211  N  N     . ILE A 1 648 ? 147.287 140.574 94.741  1.00 13.52 ?  648 ILE A N     1 
ATOM   5212  C  CA    . ILE A 1 648 ? 146.314 140.940 95.761  1.00 12.03 ?  648 ILE A CA    1 
ATOM   5213  C  C     . ILE A 1 648 ? 147.083 141.491 96.953  1.00 12.20 ?  648 ILE A C     1 
ATOM   5214  O  O     . ILE A 1 648 ? 147.975 140.821 97.486  1.00 25.66 ?  648 ILE A O     1 
ATOM   5215  C  CB    . ILE A 1 648 ? 145.444 139.739 96.163  1.00 10.19 ?  648 ILE A CB    1 
ATOM   5216  C  CG1   . ILE A 1 648 ? 144.737 139.151 94.940  1.00 11.20 ?  648 ILE A CG1   1 
ATOM   5217  C  CG2   . ILE A 1 648 ? 144.423 140.137 97.212  1.00 5.66  ?  648 ILE A CG2   1 
ATOM   5218  C  CD1   . ILE A 1 648 ? 143.635 140.023 94.388  1.00 5.31  ?  648 ILE A CD1   1 
ATOM   5219  N  N     . ASP A 1 649 ? 146.747 142.715 97.369  1.00 7.57  ?  649 ASP A N     1 
ATOM   5220  C  CA    . ASP A 1 649 ? 147.484 143.337 98.466  1.00 8.07  ?  649 ASP A CA    1 
ATOM   5221  C  C     . ASP A 1 649 ? 147.132 142.709 99.806  1.00 9.20  ?  649 ASP A C     1 
ATOM   5222  O  O     . ASP A 1 649 ? 148.000 142.578 100.675 1.00 27.02 ?  649 ASP A O     1 
ATOM   5223  C  CB    . ASP A 1 649 ? 147.223 144.843 98.498  1.00 18.44 ?  649 ASP A CB    1 
ATOM   5224  C  CG    . ASP A 1 649 ? 145.766 145.187 98.295  1.00 19.25 ?  649 ASP A CG    1 
ATOM   5225  O  OD1   . ASP A 1 649 ? 145.312 145.184 97.136  1.00 24.05 ?  649 ASP A OD1   1 
ATOM   5226  O  OD2   . ASP A 1 649 ? 145.074 145.468 99.294  1.00 20.27 -1 649 ASP A OD2   1 
ATOM   5227  N  N     . GLN A 1 650 ? 145.875 142.336 99.997  1.00 13.71 ?  650 GLN A N     1 
ATOM   5228  C  CA    . GLN A 1 650 ? 145.448 141.592 101.171 1.00 4.37  ?  650 GLN A CA    1 
ATOM   5229  C  C     . GLN A 1 650 ? 145.518 140.098 100.848 1.00 10.77 ?  650 GLN A C     1 
ATOM   5230  O  O     . GLN A 1 650 ? 146.138 139.694 99.861  1.00 20.19 ?  650 GLN A O     1 
ATOM   5231  C  CB    . GLN A 1 650 ? 144.061 142.064 101.605 1.00 6.40  ?  650 GLN A CB    1 
ATOM   5232  C  CG    . GLN A 1 650 ? 143.994 143.550 101.904 1.00 9.80  ?  650 GLN A CG    1 
ATOM   5233  C  CD    . GLN A 1 650 ? 142.652 143.972 102.454 1.00 13.56 ?  650 GLN A CD    1 
ATOM   5234  O  OE1   . GLN A 1 650 ? 142.307 143.646 103.587 1.00 15.64 ?  650 GLN A OE1   1 
ATOM   5235  N  NE2   . GLN A 1 650 ? 141.886 144.702 101.656 1.00 3.67  ?  650 GLN A NE2   1 
ATOM   5236  N  N     . GLY A 1 651 ? 144.919 139.255 101.686 1.00 9.85  ?  651 GLY A N     1 
ATOM   5237  C  CA    . GLY A 1 651 ? 144.990 137.823 101.513 1.00 5.75  ?  651 GLY A CA    1 
ATOM   5238  C  C     . GLY A 1 651 ? 143.820 137.250 100.730 1.00 5.51  ?  651 GLY A C     1 
ATOM   5239  O  O     . GLY A 1 651 ? 142.918 137.946 100.273 1.00 10.85 ?  651 GLY A O     1 
ATOM   5240  N  N     . ILE A 1 652 ? 143.865 135.930 100.577 1.00 13.76 ?  652 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 652 ? 142.842 135.158 99.886  1.00 2.10  ?  652 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 652 ? 142.391 134.047 100.821 1.00 12.29 ?  652 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 652 ? 143.225 133.325 101.375 1.00 26.74 ?  652 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 652 ? 143.372 134.568 98.564  1.00 6.19  ?  652 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 652 ? 143.967 135.666 97.682  1.00 4.30  ?  652 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 652 ? 142.274 133.820 97.833  1.00 11.90 ?  652 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 652 ? 144.571 135.151 96.406  1.00 5.06  ?  652 ILE A CD1   1 
ATOM   5248  N  N     . SER A 1 653 ? 141.082 133.913 101.001 1.00 10.56 ?  653 SER A N     1 
ATOM   5249  C  CA    . SER A 1 653 ? 140.535 132.861 101.853 1.00 12.86 ?  653 SER A CA    1 
ATOM   5250  C  C     . SER A 1 653 ? 140.775 131.520 101.175 1.00 18.04 ?  653 SER A C     1 
ATOM   5251  O  O     . SER A 1 653 ? 140.025 131.116 100.288 1.00 20.45 ?  653 SER A O     1 
ATOM   5252  C  CB    . SER A 1 653 ? 139.052 133.093 102.106 1.00 13.46 ?  653 SER A CB    1 
ATOM   5253  O  OG    . SER A 1 653 ? 138.844 133.757 103.335 1.00 20.71 ?  653 SER A OG    1 
ATOM   5254  N  N     . PHE A 1 654 ? 141.817 130.818 101.607 1.00 22.22 ?  654 PHE A N     1 
ATOM   5255  C  CA    . PHE A 1 654 ? 142.311 129.625 100.929 1.00 10.48 ?  654 PHE A CA    1 
ATOM   5256  C  C     . PHE A 1 654 ? 141.901 128.394 101.728 1.00 13.54 ?  654 PHE A C     1 
ATOM   5257  O  O     . PHE A 1 654 ? 142.496 128.093 102.769 1.00 21.98 ?  654 PHE A O     1 
ATOM   5258  C  CB    . PHE A 1 654 ? 143.827 129.702 100.768 1.00 15.97 ?  654 PHE A CB    1 
ATOM   5259  C  CG    . PHE A 1 654 ? 144.415 128.591 99.952  1.00 16.96 ?  654 PHE A CG    1 
ATOM   5260  C  CD1   . PHE A 1 654 ? 143.621 127.812 99.130  1.00 18.84 ?  654 PHE A CD1   1 
ATOM   5261  C  CD2   . PHE A 1 654 ? 145.771 128.332 100.004 1.00 21.85 ?  654 PHE A CD2   1 
ATOM   5262  C  CE1   . PHE A 1 654 ? 144.167 126.795 98.384  1.00 18.09 ?  654 PHE A CE1   1 
ATOM   5263  C  CE2   . PHE A 1 654 ? 146.320 127.318 99.257  1.00 21.06 ?  654 PHE A CE2   1 
ATOM   5264  C  CZ    . PHE A 1 654 ? 145.518 126.548 98.445  1.00 19.78 ?  654 PHE A CZ    1 
ATOM   5265  N  N     . THR A 1 655 ? 140.900 127.676 101.230 1.00 22.24 ?  655 THR A N     1 
ATOM   5266  C  CA    . THR A 1 655 ? 140.449 126.436 101.844 1.00 23.33 ?  655 THR A CA    1 
ATOM   5267  C  C     . THR A 1 655 ? 141.233 125.263 101.271 1.00 26.54 ?  655 THR A C     1 
ATOM   5268  O  O     . THR A 1 655 ? 141.422 125.168 100.054 1.00 26.35 ?  655 THR A O     1 
ATOM   5269  C  CB    . THR A 1 655 ? 138.951 126.235 101.612 1.00 23.96 ?  655 THR A CB    1 
ATOM   5270  O  OG1   . THR A 1 655 ? 138.224 127.292 102.248 1.00 31.72 ?  655 THR A OG1   1 
ATOM   5271  C  CG2   . THR A 1 655 ? 138.496 124.904 102.183 1.00 26.42 ?  655 THR A CG2   1 
ATOM   5272  N  N     . LEU A 1 656 ? 141.695 124.377 102.149 1.00 29.51 ?  656 LEU A N     1 
ATOM   5273  C  CA    . LEU A 1 656 ? 142.370 123.156 101.734 1.00 29.05 ?  656 LEU A CA    1 
ATOM   5274  C  C     . LEU A 1 656 ? 141.365 122.016 101.675 1.00 28.32 ?  656 LEU A C     1 
ATOM   5275  O  O     . LEU A 1 656 ? 140.672 121.737 102.659 1.00 28.78 ?  656 LEU A O     1 
ATOM   5276  C  CB    . LEU A 1 656 ? 143.508 122.807 102.693 1.00 29.85 ?  656 LEU A CB    1 
ATOM   5277  C  CG    . LEU A 1 656 ? 144.698 123.763 102.702 1.00 32.35 ?  656 LEU A CG    1 
ATOM   5278  C  CD1   . LEU A 1 656 ? 145.837 123.177 103.515 1.00 29.79 ?  656 LEU A CD1   1 
ATOM   5279  C  CD2   . LEU A 1 656 ? 145.150 124.082 101.287 1.00 27.79 ?  656 LEU A CD2   1 
ATOM   5280  N  N     . PHE A 1 657 ? 141.293 121.359 100.525 1.00 27.28 ?  657 PHE A N     1 
ATOM   5281  C  CA    . PHE A 1 657 ? 140.340 120.284 100.287 1.00 27.17 ?  657 PHE A CA    1 
ATOM   5282  C  C     . PHE A 1 657 ? 141.089 118.961 100.348 1.00 34.16 ?  657 PHE A C     1 
ATOM   5283  O  O     . PHE A 1 657 ? 141.854 118.628 99.437  1.00 37.77 ?  657 PHE A O     1 
ATOM   5284  C  CB    . PHE A 1 657 ? 139.643 120.481 98.945  1.00 28.61 ?  657 PHE A CB    1 
ATOM   5285  C  CG    . PHE A 1 657 ? 139.003 121.829 98.798  1.00 33.56 ?  657 PHE A CG    1 
ATOM   5286  C  CD1   . PHE A 1 657 ? 137.714 122.050 99.247  1.00 30.41 ?  657 PHE A CD1   1 
ATOM   5287  C  CD2   . PHE A 1 657 ? 139.697 122.882 98.222  1.00 34.59 ?  657 PHE A CD2   1 
ATOM   5288  C  CE1   . PHE A 1 657 ? 137.124 123.290 99.116  1.00 33.52 ?  657 PHE A CE1   1 
ATOM   5289  C  CE2   . PHE A 1 657 ? 139.111 124.124 98.088  1.00 30.81 ?  657 PHE A CE2   1 
ATOM   5290  C  CZ    . PHE A 1 657 ? 137.823 124.327 98.538  1.00 32.22 ?  657 PHE A CZ    1 
ATOM   5291  N  N     . LEU A 1 658 ? 140.864 118.208 101.420 1.00 42.10 ?  658 LEU A N     1 
ATOM   5292  C  CA    . LEU A 1 658 ? 141.646 117.023 101.736 1.00 40.48 ?  658 LEU A CA    1 
ATOM   5293  C  C     . LEU A 1 658 ? 140.798 115.768 101.596 1.00 44.65 ?  658 LEU A C     1 
ATOM   5294  O  O     . LEU A 1 658 ? 139.614 115.763 101.942 1.00 48.50 ?  658 LEU A O     1 
ATOM   5295  C  CB    . LEU A 1 658 ? 142.201 117.109 103.159 1.00 38.92 ?  658 LEU A CB    1 
ATOM   5296  C  CG    . LEU A 1 658 ? 142.634 118.494 103.639 1.00 38.09 ?  658 LEU A CG    1 
ATOM   5297  C  CD1   . LEU A 1 658 ? 142.770 118.501 105.147 1.00 37.57 ?  658 LEU A CD1   1 
ATOM   5298  C  CD2   . LEU A 1 658 ? 143.938 118.905 102.979 1.00 39.85 ?  658 LEU A CD2   1 
ATOM   5299  N  N     . LYS A 1 659 ? 141.408 114.708 101.075 1.00 48.81 ?  659 LYS A N     1 
ATOM   5300  C  CA    . LYS A 1 659 ? 140.772 113.402 101.087 1.00 49.27 ?  659 LYS A CA    1 
ATOM   5301  C  C     . LYS A 1 659 ? 140.994 112.721 102.434 1.00 49.70 ?  659 LYS A C     1 
ATOM   5302  O  O     . LYS A 1 659 ? 141.859 113.109 103.222 1.00 53.26 ?  659 LYS A O     1 
ATOM   5303  C  CB    . LYS A 1 659 ? 141.312 112.525 99.958  1.00 50.47 ?  659 LYS A CB    1 
ATOM   5304  C  CG    . LYS A 1 659 ? 140.842 112.934 98.575  1.00 50.24 ?  659 LYS A CG    1 
ATOM   5305  C  CD    . LYS A 1 659 ? 141.233 111.900 97.534  1.00 50.40 ?  659 LYS A CD    1 
ATOM   5306  C  CE    . LYS A 1 659 ? 140.681 112.259 96.165  1.00 49.54 ?  659 LYS A CE    1 
ATOM   5307  N  NZ    . LYS A 1 659 ? 140.688 111.095 95.239  1.00 49.60 1  659 LYS A NZ    1 
ATOM   5308  N  N     . ASP A 1 660 ? 140.185 111.695 102.699 1.00 56.54 ?  660 ASP A N     1 
ATOM   5309  C  CA    . ASP A 1 660 ? 140.354 110.916 103.919 1.00 56.20 ?  660 ASP A CA    1 
ATOM   5310  C  C     . ASP A 1 660 ? 141.648 110.114 103.918 1.00 56.75 ?  660 ASP A C     1 
ATOM   5311  O  O     . ASP A 1 660 ? 142.183 109.821 104.992 1.00 56.19 ?  660 ASP A O     1 
ATOM   5312  C  CB    . ASP A 1 660 ? 139.163 109.977 104.113 1.00 57.79 ?  660 ASP A CB    1 
ATOM   5313  C  CG    . ASP A 1 660 ? 138.168 110.500 105.129 1.00 58.39 ?  660 ASP A CG    1 
ATOM   5314  O  OD1   . ASP A 1 660 ? 137.113 109.859 105.315 1.00 57.17 ?  660 ASP A OD1   1 
ATOM   5315  O  OD2   . ASP A 1 660 ? 138.443 111.549 105.746 1.00 56.44 -1 660 ASP A OD2   1 
ATOM   5316  N  N     . THR A 1 661 ? 142.161 109.758 102.738 1.00 54.72 ?  661 THR A N     1 
ATOM   5317  C  CA    . THR A 1 661 ? 143.336 108.896 102.662 1.00 54.28 ?  661 THR A CA    1 
ATOM   5318  C  C     . THR A 1 661 ? 144.602 109.600 103.136 1.00 54.79 ?  661 THR A C     1 
ATOM   5319  O  O     . THR A 1 661 ? 145.474 108.959 103.733 1.00 57.02 ?  661 THR A O     1 
ATOM   5320  C  CB    . THR A 1 661 ? 143.525 108.393 101.231 1.00 55.29 ?  661 THR A CB    1 
ATOM   5321  O  OG1   . THR A 1 661 ? 143.156 109.426 100.309 1.00 55.34 ?  661 THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1 661 ? 142.661 107.167 100.983 1.00 54.88 ?  661 THR A CG2   1 
ATOM   5323  N  N     . MET A 1 662 ? 144.729 110.899 102.884 1.00 53.00 ?  662 MET A N     1 
ATOM   5324  C  CA    . MET A 1 662 ? 145.964 111.605 103.196 1.00 52.79 ?  662 MET A CA    1 
ATOM   5325  C  C     . MET A 1 662 ? 146.113 111.800 104.700 1.00 51.88 ?  662 MET A C     1 
ATOM   5326  O  O     . MET A 1 662 ? 145.134 112.026 105.417 1.00 52.12 ?  662 MET A O     1 
ATOM   5327  C  CB    . MET A 1 662 ? 146.014 112.954 102.477 1.00 51.51 ?  662 MET A CB    1 
ATOM   5328  C  CG    . MET A 1 662 ? 144.907 113.921 102.838 1.00 52.69 ?  662 MET A CG    1 
ATOM   5329  S  SD    . MET A 1 662 ? 145.024 115.462 101.907 1.00 60.26 ?  662 MET A SD    1 
ATOM   5330  C  CE    . MET A 1 662 ? 145.902 114.925 100.443 1.00 49.12 ?  662 MET A CE    1 
ATOM   5331  N  N     . THR A 1 663 ? 147.353 111.705 105.172 1.00 44.50 ?  663 THR A N     1 
ATOM   5332  C  CA    . THR A 1 663 ? 147.660 111.749 106.592 1.00 43.95 ?  663 THR A CA    1 
ATOM   5333  C  C     . THR A 1 663 ? 147.885 113.195 107.033 1.00 45.06 ?  663 THR A C     1 
ATOM   5334  O  O     . THR A 1 663 ? 147.666 114.141 106.275 1.00 48.51 ?  663 THR A O     1 
ATOM   5335  C  CB    . THR A 1 663 ? 148.879 110.880 106.891 1.00 43.10 ?  663 THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 663 ? 150.058 111.527 106.394 1.00 41.26 ?  663 THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 663 ? 148.740 109.527 106.214 1.00 44.67 ?  663 THR A CG2   1 
ATOM   5338  N  N     . THR A 1 664 ? 148.325 113.378 108.281 1.00 39.46 ?  664 THR A N     1 
ATOM   5339  C  CA    . THR A 1 664 ? 148.692 114.715 108.734 1.00 41.82 ?  664 THR A CA    1 
ATOM   5340  C  C     . THR A 1 664 ? 149.978 115.189 108.072 1.00 40.57 ?  664 THR A C     1 
ATOM   5341  O  O     . THR A 1 664 ? 150.202 116.399 107.954 1.00 42.64 ?  664 THR A O     1 
ATOM   5342  C  CB    . THR A 1 664 ? 148.841 114.747 110.254 1.00 41.38 ?  664 THR A CB    1 
ATOM   5343  O  OG1   . THR A 1 664 ? 149.898 113.865 110.653 1.00 40.03 ?  664 THR A OG1   1 
ATOM   5344  C  CG2   . THR A 1 664 ? 147.547 114.325 110.930 1.00 39.88 ?  664 THR A CG2   1 
ATOM   5345  N  N     . ARG A 1 665 ? 150.830 114.257 107.641 1.00 39.85 ?  665 ARG A N     1 
ATOM   5346  C  CA    . ARG A 1 665 ? 152.042 114.640 106.926 1.00 38.49 ?  665 ARG A CA    1 
ATOM   5347  C  C     . ARG A 1 665 ? 151.711 115.309 105.601 1.00 41.53 ?  665 ARG A C     1 
ATOM   5348  O  O     . ARG A 1 665 ? 152.385 116.259 105.196 1.00 42.68 ?  665 ARG A O     1 
ATOM   5349  C  CB    . ARG A 1 665 ? 152.932 113.421 106.694 1.00 39.32 ?  665 ARG A CB    1 
ATOM   5350  C  CG    . ARG A 1 665 ? 154.224 113.743 105.969 1.00 37.71 ?  665 ARG A CG    1 
ATOM   5351  C  CD    . ARG A 1 665 ? 155.145 112.542 105.906 1.00 39.18 ?  665 ARG A CD    1 
ATOM   5352  N  NE    . ARG A 1 665 ? 156.224 112.731 104.946 1.00 41.76 ?  665 ARG A NE    1 
ATOM   5353  C  CZ    . ARG A 1 665 ? 156.081 112.655 103.629 1.00 45.20 ?  665 ARG A CZ    1 
ATOM   5354  N  NH1   . ARG A 1 665 ? 154.911 112.386 103.075 1.00 43.53 1  665 ARG A NH1   1 
ATOM   5355  N  NH2   . ARG A 1 665 ? 157.140 112.853 102.849 1.00 42.18 ?  665 ARG A NH2   1 
ATOM   5356  N  N     . ASP A 1 666 ? 150.682 114.823 104.905 1.00 38.83 ?  666 ASP A N     1 
ATOM   5357  C  CA    . ASP A 1 666 ? 150.286 115.450 103.648 1.00 35.10 ?  666 ASP A CA    1 
ATOM   5358  C  C     . ASP A 1 666 ? 149.749 116.857 103.875 1.00 37.66 ?  666 ASP A C     1 
ATOM   5359  O  O     . ASP A 1 666 ? 150.047 117.776 103.103 1.00 40.48 ?  666 ASP A O     1 
ATOM   5360  C  CB    . ASP A 1 666 ? 149.253 114.582 102.934 1.00 40.83 ?  666 ASP A CB    1 
ATOM   5361  C  CG    . ASP A 1 666 ? 149.811 113.235 102.524 1.00 45.35 ?  666 ASP A CG    1 
ATOM   5362  O  OD1   . ASP A 1 666 ? 150.918 113.200 101.947 1.00 45.48 ?  666 ASP A OD1   1 
ATOM   5363  O  OD2   . ASP A 1 666 ? 149.145 112.210 102.777 1.00 45.22 -1 666 ASP A OD2   1 
ATOM   5364  N  N     . LEU A 1 667 ? 148.954 117.048 104.930 1.00 36.21 ?  667 LEU A N     1 
ATOM   5365  C  CA    . LEU A 1 667 ? 148.466 118.382 105.259 1.00 31.15 ?  667 LEU A CA    1 
ATOM   5366  C  C     . LEU A 1 667 ? 149.624 119.309 105.612 1.00 29.82 ?  667 LEU A C     1 
ATOM   5367  O  O     . LEU A 1 667 ? 149.654 120.472 105.192 1.00 34.82 ?  667 LEU A O     1 
ATOM   5368  C  CB    . LEU A 1 667 ? 147.460 118.290 106.409 1.00 34.82 ?  667 LEU A CB    1 
ATOM   5369  C  CG    . LEU A 1 667 ? 146.803 119.532 107.023 1.00 36.50 ?  667 LEU A CG    1 
ATOM   5370  C  CD1   . LEU A 1 667 ? 146.594 120.638 106.000 1.00 35.38 ?  667 LEU A CD1   1 
ATOM   5371  C  CD2   . LEU A 1 667 ? 145.486 119.154 107.673 1.00 32.66 ?  667 LEU A CD2   1 
ATOM   5372  N  N     . ASN A 1 668 ? 150.596 118.803 106.373 1.00 32.07 ?  668 ASN A N     1 
ATOM   5373  C  CA    . ASN A 1 668 ? 151.769 119.604 106.711 1.00 26.94 ?  668 ASN A CA    1 
ATOM   5374  C  C     . ASN A 1 668 ? 152.579 119.949 105.468 1.00 26.92 ?  668 ASN A C     1 
ATOM   5375  O  O     . ASN A 1 668 ? 153.103 121.059 105.351 1.00 33.03 ?  668 ASN A O     1 
ATOM   5376  C  CB    . ASN A 1 668 ? 152.632 118.860 107.728 1.00 27.90 ?  668 ASN A CB    1 
ATOM   5377  C  CG    . ASN A 1 668 ? 152.324 119.262 109.154 1.00 30.77 ?  668 ASN A CG    1 
ATOM   5378  O  OD1   . ASN A 1 668 ? 151.796 120.343 109.405 1.00 31.97 ?  668 ASN A OD1   1 
ATOM   5379  N  ND2   . ASN A 1 668 ? 152.643 118.386 110.096 1.00 37.76 ?  668 ASN A ND2   1 
ATOM   5380  N  N     . ARG A 1 669 ? 152.703 119.004 104.535 1.00 30.35 ?  669 ARG A N     1 
ATOM   5381  C  CA    . ARG A 1 669 ? 153.409 119.274 103.287 1.00 31.14 ?  669 ARG A CA    1 
ATOM   5382  C  C     . ARG A 1 669 ? 152.696 120.343 102.474 1.00 27.39 ?  669 ARG A C     1 
ATOM   5383  O  O     . ARG A 1 669 ? 153.341 121.211 101.879 1.00 31.90 ?  669 ARG A O     1 
ATOM   5384  C  CB    . ARG A 1 669 ? 153.549 117.990 102.472 1.00 29.28 ?  669 ARG A CB    1 
ATOM   5385  C  CG    . ARG A 1 669 ? 154.658 117.071 102.937 1.00 31.02 ?  669 ARG A CG    1 
ATOM   5386  C  CD    . ARG A 1 669 ? 155.138 116.190 101.800 1.00 34.56 ?  669 ARG A CD    1 
ATOM   5387  N  NE    . ARG A 1 669 ? 156.047 116.896 100.906 1.00 33.91 ?  669 ARG A NE    1 
ATOM   5388  C  CZ    . ARG A 1 669 ? 155.968 116.868 99.583  1.00 33.75 ?  669 ARG A CZ    1 
ATOM   5389  N  NH1   . ARG A 1 669 ? 155.025 116.179 98.961  1.00 34.67 1  669 ARG A NH1   1 
ATOM   5390  N  NH2   . ARG A 1 669 ? 156.856 117.549 98.865  1.00 33.28 ?  669 ARG A NH2   1 
ATOM   5391  N  N     . ILE A 1 670 ? 151.363 120.291 102.429 1.00 23.06 ?  670 ILE A N     1 
ATOM   5392  C  CA    . ILE A 1 670 ? 150.609 121.327 101.728 1.00 27.95 ?  670 ILE A CA    1 
ATOM   5393  C  C     . ILE A 1 670 ? 150.828 122.682 102.388 1.00 30.84 ?  670 ILE A C     1 
ATOM   5394  O  O     . ILE A 1 670 ? 151.020 123.695 101.708 1.00 29.03 ?  670 ILE A O     1 
ATOM   5395  C  CB    . ILE A 1 670 ? 149.114 120.961 101.665 1.00 28.07 ?  670 ILE A CB    1 
ATOM   5396  C  CG1   . ILE A 1 670 ? 148.908 119.693 100.836 1.00 30.56 ?  670 ILE A CG1   1 
ATOM   5397  C  CG2   . ILE A 1 670 ? 148.310 122.102 101.068 1.00 27.64 ?  670 ILE A CG2   1 
ATOM   5398  C  CD1   . ILE A 1 670 ? 147.616 118.974 101.135 1.00 29.61 ?  670 ILE A CD1   1 
ATOM   5399  N  N     . ASP A 1 671 ? 150.810 122.721 103.724 1.00 28.70 ?  671 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 671 ? 151.039 123.977 104.435 1.00 22.91 ?  671 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 671 ? 152.437 124.524 104.167 1.00 23.48 ?  671 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 671 ? 152.613 125.730 103.956 1.00 25.79 ?  671 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 671 ? 150.823 123.778 105.935 1.00 26.10 ?  671 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 671 ? 149.410 123.344 106.271 1.00 37.56 ?  671 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 671 ? 148.483 123.689 105.509 1.00 36.26 ?  671 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 671 ? 149.226 122.656 107.298 1.00 37.09 -1 671 ASP A OD2   1 
ATOM   5407  N  N     . LEU A 1 672 ? 153.444 123.651 104.163 1.00 25.36 ?  672 LEU A N     1 
ATOM   5408  C  CA    . LEU A 1 672 ? 154.815 124.093 103.930 1.00 19.20 ?  672 LEU A CA    1 
ATOM   5409  C  C     . LEU A 1 672 ? 155.033 124.524 102.486 1.00 19.80 ?  672 LEU A C     1 
ATOM   5410  O  O     . LEU A 1 672 ? 155.815 125.444 102.229 1.00 25.70 ?  672 LEU A O     1 
ATOM   5411  C  CB    . LEU A 1 672 ? 155.793 122.984 104.309 1.00 22.76 ?  672 LEU A CB    1 
ATOM   5412  C  CG    . LEU A 1 672 ? 155.881 122.671 105.803 1.00 23.94 ?  672 LEU A CG    1 
ATOM   5413  C  CD1   . LEU A 1 672 ? 156.545 121.323 106.033 1.00 19.57 ?  672 LEU A CD1   1 
ATOM   5414  C  CD2   . LEU A 1 672 ? 156.619 123.776 106.538 1.00 21.82 ?  672 LEU A CD2   1 
ATOM   5415  N  N     . TYR A 1 673 ? 154.360 123.876 101.534 1.00 21.30 ?  673 TYR A N     1 
ATOM   5416  C  CA    . TYR A 1 673 ? 154.450 124.306 100.145 1.00 18.93 ?  673 TYR A CA    1 
ATOM   5417  C  C     . TYR A 1 673 ? 153.736 125.634 99.936  1.00 21.16 ?  673 TYR A C     1 
ATOM   5418  O  O     . TYR A 1 673 ? 154.182 126.469 99.144  1.00 24.42 ?  673 TYR A O     1 
ATOM   5419  C  CB    . TYR A 1 673 ? 153.874 123.229 99.228  1.00 14.92 ?  673 TYR A CB    1 
ATOM   5420  C  CG    . TYR A 1 673 ? 153.984 123.554 97.759  1.00 19.19 ?  673 TYR A CG    1 
ATOM   5421  C  CD1   . TYR A 1 673 ? 155.223 123.685 97.150  1.00 18.76 ?  673 TYR A CD1   1 
ATOM   5422  C  CD2   . TYR A 1 673 ? 152.850 123.724 96.979  1.00 18.36 ?  673 TYR A CD2   1 
ATOM   5423  C  CE1   . TYR A 1 673 ? 155.328 123.980 95.809  1.00 23.48 ?  673 TYR A CE1   1 
ATOM   5424  C  CE2   . TYR A 1 673 ? 152.946 124.017 95.638  1.00 21.21 ?  673 TYR A CE2   1 
ATOM   5425  C  CZ    . TYR A 1 673 ? 154.187 124.143 95.058  1.00 25.20 ?  673 TYR A CZ    1 
ATOM   5426  O  OH    . TYR A 1 673 ? 154.291 124.436 93.719  1.00 24.69 ?  673 TYR A OH    1 
ATOM   5427  N  N     . ALA A 1 674 ? 152.617 125.841 100.634 1.00 23.17 ?  674 ALA A N     1 
ATOM   5428  C  CA    . ALA A 1 674 ? 151.945 127.132 100.593 1.00 16.78 ?  674 ALA A CA    1 
ATOM   5429  C  C     . ALA A 1 674 ? 152.832 128.228 101.165 1.00 17.23 ?  674 ALA A C     1 
ATOM   5430  O  O     . ALA A 1 674 ? 152.928 129.321 100.597 1.00 25.24 ?  674 ALA A O     1 
ATOM   5431  C  CB    . ALA A 1 674 ? 150.622 127.053 101.353 1.00 12.27 ?  674 ALA A CB    1 
ATOM   5432  N  N     . HIS A 1 675 ? 153.503 127.948 102.283 1.00 15.67 ?  675 HIS A N     1 
ATOM   5433  C  CA    . HIS A 1 675 ? 154.440 128.917 102.843 1.00 19.64 ?  675 HIS A CA    1 
ATOM   5434  C  C     . HIS A 1 675 ? 155.594 129.184 101.883 1.00 19.45 ?  675 HIS A C     1 
ATOM   5435  O  O     . HIS A 1 675 ? 156.039 130.328 101.738 1.00 24.55 ?  675 HIS A O     1 
ATOM   5436  C  CB    . HIS A 1 675 ? 154.965 128.423 104.188 1.00 18.08 ?  675 HIS A CB    1 
ATOM   5437  C  CG    . HIS A 1 675 ? 156.084 129.250 104.737 1.00 20.55 ?  675 HIS A CG    1 
ATOM   5438  N  ND1   . HIS A 1 675 ? 157.406 128.886 104.617 1.00 28.37 ?  675 HIS A ND1   1 
ATOM   5439  C  CD2   . HIS A 1 675 ? 156.077 130.427 105.404 1.00 18.60 ?  675 HIS A CD2   1 
ATOM   5440  C  CE1   . HIS A 1 675 ? 158.166 129.802 105.189 1.00 23.86 ?  675 HIS A CE1   1 
ATOM   5441  N  NE2   . HIS A 1 675 ? 157.384 130.748 105.674 1.00 24.59 ?  675 HIS A NE2   1 
ATOM   5442  N  N     . HIS A 1 676 ? 156.094 128.137 101.225 1.00 22.03 ?  676 HIS A N     1 
ATOM   5443  C  CA    . HIS A 1 676 ? 157.189 128.301 100.275 1.00 19.91 ?  676 HIS A CA    1 
ATOM   5444  C  C     . HIS A 1 676 ? 156.763 129.124 99.067  1.00 25.51 ?  676 HIS A C     1 
ATOM   5445  O  O     . HIS A 1 676 ? 157.547 129.921 98.540  1.00 25.79 ?  676 HIS A O     1 
ATOM   5446  C  CB    . HIS A 1 676 ? 157.700 126.929 99.834  1.00 23.94 ?  676 HIS A CB    1 
ATOM   5447  C  CG    . HIS A 1 676 ? 158.640 126.980 98.669  1.00 24.67 ?  676 HIS A CG    1 
ATOM   5448  N  ND1   . HIS A 1 676 ? 159.948 127.396 98.786  1.00 22.61 ?  676 HIS A ND1   1 
ATOM   5449  C  CD2   . HIS A 1 676 ? 158.459 126.665 97.366  1.00 25.58 ?  676 HIS A CD2   1 
ATOM   5450  C  CE1   . HIS A 1 676 ? 160.533 127.335 97.604  1.00 29.10 ?  676 HIS A CE1   1 
ATOM   5451  N  NE2   . HIS A 1 676 ? 159.652 126.896 96.725  1.00 27.74 ?  676 HIS A NE2   1 
ATOM   5452  N  N     . ARG A 1 677 ? 155.525 128.947 98.614  1.00 23.74 ?  677 ARG A N     1 
ATOM   5453  C  CA    . ARG A 1 677 ? 155.045 129.588 97.398  1.00 19.41 ?  677 ARG A CA    1 
ATOM   5454  C  C     . ARG A 1 677 ? 154.507 130.992 97.633  1.00 20.49 ?  677 ARG A C     1 
ATOM   5455  O  O     . ARG A 1 677 ? 154.015 131.616 96.687  1.00 27.52 ?  677 ARG A O     1 
ATOM   5456  C  CB    . ARG A 1 677 ? 153.965 128.726 96.740  1.00 22.31 ?  677 ARG A CB    1 
ATOM   5457  C  CG    . ARG A 1 677 ? 154.514 127.606 95.873  1.00 22.58 ?  677 ARG A CG    1 
ATOM   5458  C  CD    . ARG A 1 677 ? 155.114 128.146 94.587  1.00 18.82 ?  677 ARG A CD    1 
ATOM   5459  N  NE    . ARG A 1 677 ? 154.108 128.325 93.547  1.00 26.67 ?  677 ARG A NE    1 
ATOM   5460  C  CZ    . ARG A 1 677 ? 153.804 129.489 92.989  1.00 31.68 ?  677 ARG A CZ    1 
ATOM   5461  N  NH1   . ARG A 1 677 ? 154.415 130.607 93.346  1.00 29.78 1  677 ARG A NH1   1 
ATOM   5462  N  NH2   . ARG A 1 677 ? 152.865 129.533 92.049  1.00 25.25 ?  677 ARG A NH2   1 
ATOM   5463  N  N     . GLY A 1 678 ? 154.588 131.505 98.856  1.00 18.80 ?  678 GLY A N     1 
ATOM   5464  C  CA    . GLY A 1 678 ? 154.134 132.850 99.140  1.00 11.84 ?  678 GLY A CA    1 
ATOM   5465  C  C     . GLY A 1 678 ? 152.685 132.976 99.539  1.00 17.48 ?  678 GLY A C     1 
ATOM   5466  O  O     . GLY A 1 678 ? 152.136 134.081 99.474  1.00 21.36 ?  678 GLY A O     1 
ATOM   5467  N  N     . ILE A 1 679 ? 152.039 131.881 99.942  1.00 18.57 ?  679 ILE A N     1 
ATOM   5468  C  CA    . ILE A 1 679 ? 150.663 131.955 100.413 1.00 11.37 ?  679 ILE A CA    1 
ATOM   5469  C  C     . ILE A 1 679 ? 150.629 132.711 101.731 1.00 13.32 ?  679 ILE A C     1 
ATOM   5470  O  O     . ILE A 1 679 ? 151.410 132.429 102.649 1.00 29.23 ?  679 ILE A O     1 
ATOM   5471  C  CB    . ILE A 1 679 ? 150.063 130.549 100.555 1.00 16.02 ?  679 ILE A CB    1 
ATOM   5472  C  CG1   . ILE A 1 679 ? 149.894 129.902 99.180  1.00 13.20 ?  679 ILE A CG1   1 
ATOM   5473  C  CG2   . ILE A 1 679 ? 148.741 130.595 101.300 1.00 14.77 ?  679 ILE A CG2   1 
ATOM   5474  C  CD1   . ILE A 1 679 ? 149.012 130.679 98.254  1.00 13.30 ?  679 ILE A CD1   1 
ATOM   5475  N  N     . LYS A 1 680 ? 149.725 133.684 101.829 1.00 9.75  ?  680 LYS A N     1 
ATOM   5476  C  CA    . LYS A 1 680 ? 149.668 134.527 103.016 1.00 6.25  ?  680 LYS A CA    1 
ATOM   5477  C  C     . LYS A 1 680 ? 148.880 133.862 104.138 1.00 5.30  ?  680 LYS A C     1 
ATOM   5478  O  O     . LYS A 1 680 ? 149.319 133.852 105.292 1.00 17.26 ?  680 LYS A O     1 
ATOM   5479  C  CB    . LYS A 1 680 ? 149.062 135.883 102.660 1.00 8.74  ?  680 LYS A CB    1 
ATOM   5480  C  CG    . LYS A 1 680 ? 149.920 136.727 101.738 1.00 0.00  ?  680 LYS A CG    1 
ATOM   5481  C  CD    . LYS A 1 680 ? 149.323 138.107 101.566 1.00 5.72  ?  680 LYS A CD    1 
ATOM   5482  C  CE    . LYS A 1 680 ? 150.052 138.897 100.505 1.00 9.99  ?  680 LYS A CE    1 
ATOM   5483  N  NZ    . LYS A 1 680 ? 149.498 140.266 100.371 1.00 15.99 1  680 LYS A NZ    1 
ATOM   5484  N  N     . THR A 1 681 ? 147.715 133.303 103.821 1.00 10.68 ?  681 THR A N     1 
ATOM   5485  C  CA    . THR A 1 681 ? 146.858 132.676 104.815 1.00 8.05  ?  681 THR A CA    1 
ATOM   5486  C  C     . THR A 1 681 ? 146.272 131.392 104.251 1.00 14.02 ?  681 THR A C     1 
ATOM   5487  O  O     . THR A 1 681 ? 146.092 131.252 103.040 1.00 25.07 ?  681 THR A O     1 
ATOM   5488  C  CB    . THR A 1 681 ? 145.712 133.606 105.257 1.00 14.36 ?  681 THR A CB    1 
ATOM   5489  O  OG1   . THR A 1 681 ? 145.076 134.171 104.104 1.00 21.48 ?  681 THR A OG1   1 
ATOM   5490  C  CG2   . THR A 1 681 ? 146.230 134.727 106.143 1.00 11.98 ?  681 THR A CG2   1 
ATOM   5491  N  N     . ILE A 1 682 ? 145.974 130.454 105.146 1.00 10.50 ?  682 ILE A N     1 
ATOM   5492  C  CA    . ILE A 1 682 ? 145.247 129.235 104.816 1.00 11.42 ?  682 ILE A CA    1 
ATOM   5493  C  C     . ILE A 1 682 ? 143.978 129.210 105.653 1.00 14.42 ?  682 ILE A C     1 
ATOM   5494  O  O     . ILE A 1 682 ? 144.041 129.291 106.885 1.00 15.39 ?  682 ILE A O     1 
ATOM   5495  C  CB    . ILE A 1 682 ? 146.092 127.973 105.064 1.00 16.27 ?  682 ILE A CB    1 
ATOM   5496  C  CG1   . ILE A 1 682 ? 147.468 128.110 104.412 1.00 17.97 ?  682 ILE A CG1   1 
ATOM   5497  C  CG2   . ILE A 1 682 ? 145.381 126.757 104.528 1.00 19.16 ?  682 ILE A CG2   1 
ATOM   5498  C  CD1   . ILE A 1 682 ? 148.340 126.890 104.571 1.00 19.40 ?  682 ILE A CD1   1 
ATOM   5499  N  N     . TYR A 1 683 ? 142.828 129.103 104.987 1.00 16.60 ?  683 TYR A N     1 
ATOM   5500  C  CA    . TYR A 1 683 ? 141.551 129.277 105.680 1.00 11.86 ?  683 TYR A CA    1 
ATOM   5501  C  C     . TYR A 1 683 ? 141.091 127.996 106.370 1.00 23.72 ?  683 TYR A C     1 
ATOM   5502  O  O     . TYR A 1 683 ? 141.038 127.922 107.600 1.00 33.70 ?  683 TYR A O     1 
ATOM   5503  C  CB    . TYR A 1 683 ? 140.491 129.765 104.687 1.00 18.22 ?  683 TYR A CB    1 
ATOM   5504  C  CG    . TYR A 1 683 ? 139.172 130.141 105.318 1.00 15.29 ?  683 TYR A CG    1 
ATOM   5505  C  CD1   . TYR A 1 683 ? 139.103 130.543 106.643 1.00 15.83 ?  683 TYR A CD1   1 
ATOM   5506  C  CD2   . TYR A 1 683 ? 137.996 130.103 104.583 1.00 13.23 ?  683 TYR A CD2   1 
ATOM   5507  C  CE1   . TYR A 1 683 ? 137.905 130.888 107.221 1.00 19.36 ?  683 TYR A CE1   1 
ATOM   5508  C  CE2   . TYR A 1 683 ? 136.789 130.450 105.153 1.00 18.00 ?  683 TYR A CE2   1 
ATOM   5509  C  CZ    . TYR A 1 683 ? 136.751 130.842 106.473 1.00 20.89 ?  683 TYR A CZ    1 
ATOM   5510  O  OH    . TYR A 1 683 ? 135.552 131.189 107.051 1.00 28.35 ?  683 TYR A OH    1 
ATOM   5511  N  N     . TYR A 1 684 ? 140.782 126.966 105.597 1.00 31.22 ?  684 TYR A N     1 
ATOM   5512  C  CA    . TYR A 1 684 ? 140.123 125.791 106.139 1.00 24.27 ?  684 TYR A CA    1 
ATOM   5513  C  C     . TYR A 1 684 ? 140.767 124.532 105.594 1.00 33.98 ?  684 TYR A C     1 
ATOM   5514  O  O     . TYR A 1 684 ? 141.273 124.506 104.470 1.00 35.72 ?  684 TYR A O     1 
ATOM   5515  C  CB    . TYR A 1 684 ? 138.626 125.784 105.809 1.00 27.98 ?  684 TYR A CB    1 
ATOM   5516  C  CG    . TYR A 1 684 ? 137.756 126.359 106.899 1.00 25.86 ?  684 TYR A CG    1 
ATOM   5517  C  CD1   . TYR A 1 684 ? 137.992 126.058 108.232 1.00 28.64 ?  684 TYR A CD1   1 
ATOM   5518  C  CD2   . TYR A 1 684 ? 136.699 127.202 106.595 1.00 27.48 ?  684 TYR A CD2   1 
ATOM   5519  C  CE1   . TYR A 1 684 ? 137.200 126.581 109.232 1.00 32.74 ?  684 TYR A CE1   1 
ATOM   5520  C  CE2   . TYR A 1 684 ? 135.902 127.732 107.586 1.00 26.81 ?  684 TYR A CE2   1 
ATOM   5521  C  CZ    . TYR A 1 684 ? 136.156 127.419 108.903 1.00 33.03 ?  684 TYR A CZ    1 
ATOM   5522  O  OH    . TYR A 1 684 ? 135.363 127.943 109.896 1.00 36.74 ?  684 TYR A OH    1 
ATOM   5523  N  N     . ALA A 1 685 ? 140.746 123.488 106.412 1.00 33.01 ?  685 ALA A N     1 
ATOM   5524  C  CA    . ALA A 1 685 ? 141.158 122.150 106.011 1.00 30.94 ?  685 ALA A CA    1 
ATOM   5525  C  C     . ALA A 1 685 ? 139.884 121.317 105.918 1.00 33.77 ?  685 ALA A C     1 
ATOM   5526  O  O     . ALA A 1 685 ? 139.502 120.630 106.865 1.00 41.20 ?  685 ALA A O     1 
ATOM   5527  C  CB    . ALA A 1 685 ? 142.157 121.563 106.996 1.00 31.56 ?  685 ALA A CB    1 
ATOM   5528  N  N     . ARG A 1 686 ? 139.225 121.390 104.766 1.00 34.12 ?  686 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 686 ? 137.987 120.662 104.533 1.00 35.47 ?  686 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 686 ? 138.304 119.256 104.047 1.00 39.33 ?  686 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 686 ? 139.052 119.080 103.081 1.00 41.11 ?  686 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 686 ? 137.113 121.389 103.511 1.00 38.70 ?  686 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 686 ? 136.334 122.556 104.080 1.00 41.76 ?  686 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 686 ? 135.076 122.806 103.273 1.00 42.10 ?  686 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 686 ? 134.319 121.578 103.064 1.00 43.83 ?  686 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 686 ? 133.017 121.455 103.284 1.00 44.76 ?  686 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 686 ? 132.290 122.474 103.712 1.00 42.57 1  686 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 686 ? 132.431 120.282 103.070 1.00 43.63 ?  686 ARG A NH2   1 
ATOM   5539  N  N     . THR A 1 687 ? 137.731 118.261 104.713 1.00 44.90 ?  687 THR A N     1 
ATOM   5540  C  CA    . THR A 1 687 ? 137.983 116.863 104.404 1.00 47.74 ?  687 THR A CA    1 
ATOM   5541  C  C     . THR A 1 687 ? 136.702 116.204 103.910 1.00 46.02 ?  687 THR A C     1 
ATOM   5542  O  O     . THR A 1 687 ? 135.621 116.439 104.459 1.00 49.65 ?  687 THR A O     1 
ATOM   5543  C  CB    . THR A 1 687 ? 138.522 116.122 105.632 1.00 47.73 ?  687 THR A CB    1 
ATOM   5544  O  OG1   . THR A 1 687 ? 139.746 116.731 106.059 1.00 47.03 ?  687 THR A OG1   1 
ATOM   5545  C  CG2   . THR A 1 687 ? 138.792 114.671 105.299 1.00 47.44 ?  687 THR A CG2   1 
ATOM   5546  N  N     . LYS A 1 688 ? 136.827 115.388 102.869 1.00 44.89 ?  688 LYS A N     1 
ATOM   5547  C  CA    . LYS A 1 688 ? 135.686 114.668 102.318 1.00 50.69 ?  688 LYS A CA    1 
ATOM   5548  C  C     . LYS A 1 688 ? 135.704 113.208 102.758 1.00 54.40 ?  688 LYS A C     1 
ATOM   5549  O  O     . LYS A 1 688 ? 136.747 112.677 103.136 1.00 56.78 ?  688 LYS A O     1 
ATOM   5550  C  CB    . LYS A 1 688 ? 135.675 114.759 100.792 1.00 49.89 ?  688 LYS A CB    1 
ATOM   5551  C  CG    . LYS A 1 688 ? 136.571 113.743 100.104 1.00 49.17 ?  688 LYS A CG    1 
ATOM   5552  C  CD    . LYS A 1 688 ? 136.121 113.473 98.678  1.00 51.52 ?  688 LYS A CD    1 
ATOM   5553  C  CE    . LYS A 1 688 ? 134.606 113.410 98.566  1.00 51.01 ?  688 LYS A CE    1 
ATOM   5554  N  NZ    . LYS A 1 688 ? 134.172 113.079 97.181  1.00 50.48 ?  688 LYS A NZ    1 
ATOM   5555  N  N     . VAL B 1 6   ? 153.832 115.888 163.730 1.00 58.06 ?  6   VAL B N     1 
ATOM   5556  C  CA    . VAL B 1 6   ? 152.735 116.631 164.340 1.00 60.47 ?  6   VAL B CA    1 
ATOM   5557  C  C     . VAL B 1 6   ? 153.279 117.699 165.282 1.00 60.85 ?  6   VAL B C     1 
ATOM   5558  O  O     . VAL B 1 6   ? 154.028 117.393 166.209 1.00 56.42 ?  6   VAL B O     1 
ATOM   5559  C  CB    . VAL B 1 6   ? 151.770 115.690 165.080 1.00 59.34 ?  6   VAL B CB    1 
ATOM   5560  C  CG1   . VAL B 1 6   ? 150.573 116.465 165.602 1.00 55.45 ?  6   VAL B CG1   1 
ATOM   5561  C  CG2   . VAL B 1 6   ? 151.321 114.564 164.164 1.00 59.30 ?  6   VAL B CG2   1 
ATOM   5562  N  N     . PRO B 1 7   ? 152.908 118.954 165.033 1.00 59.15 ?  7   PRO B N     1 
ATOM   5563  C  CA    . PRO B 1 7   ? 153.392 120.049 165.882 1.00 53.13 ?  7   PRO B CA    1 
ATOM   5564  C  C     . PRO B 1 7   ? 152.922 119.900 167.321 1.00 55.56 ?  7   PRO B C     1 
ATOM   5565  O  O     . PRO B 1 7   ? 151.873 119.316 167.600 1.00 60.63 ?  7   PRO B O     1 
ATOM   5566  C  CB    . PRO B 1 7   ? 152.794 121.300 165.233 1.00 52.80 ?  7   PRO B CB    1 
ATOM   5567  C  CG    . PRO B 1 7   ? 152.429 120.912 163.854 1.00 56.23 ?  7   PRO B CG    1 
ATOM   5568  C  CD    . PRO B 1 7   ? 152.252 119.430 163.803 1.00 56.88 ?  7   PRO B CD    1 
ATOM   5569  N  N     . LYS B 1 8   ? 153.729 120.432 168.242 1.00 55.11 ?  8   LYS B N     1 
ATOM   5570  C  CA    . LYS B 1 8   ? 153.400 120.343 169.661 1.00 54.87 ?  8   LYS B CA    1 
ATOM   5571  C  C     . LYS B 1 8   ? 152.098 121.066 169.977 1.00 57.26 ?  8   LYS B C     1 
ATOM   5572  O  O     . LYS B 1 8   ? 151.265 120.558 170.739 1.00 59.71 ?  8   LYS B O     1 
ATOM   5573  C  CB    . LYS B 1 8   ? 154.544 120.910 170.501 1.00 55.07 ?  8   LYS B CB    1 
ATOM   5574  C  CG    . LYS B 1 8   ? 154.521 120.468 171.954 1.00 55.73 ?  8   LYS B CG    1 
ATOM   5575  C  CD    . LYS B 1 8   ? 155.039 121.563 172.872 1.00 56.79 ?  8   LYS B CD    1 
ATOM   5576  C  CE    . LYS B 1 8   ? 154.368 121.502 174.235 1.00 58.05 ?  8   LYS B CE    1 
ATOM   5577  N  NZ    . LYS B 1 8   ? 155.205 122.126 175.295 1.00 56.65 1  8   LYS B NZ    1 
ATOM   5578  N  N     . TRP B 1 9   ? 151.903 122.255 169.403 1.00 58.22 ?  9   TRP B N     1 
ATOM   5579  C  CA    . TRP B 1 9   ? 150.658 122.979 169.630 1.00 51.60 ?  9   TRP B CA    1 
ATOM   5580  C  C     . TRP B 1 9   ? 149.469 122.254 169.018 1.00 51.94 ?  9   TRP B C     1 
ATOM   5581  O  O     . TRP B 1 9   ? 148.365 122.312 169.566 1.00 58.14 ?  9   TRP B O     1 
ATOM   5582  C  CB    . TRP B 1 9   ? 150.755 124.399 169.073 1.00 50.43 ?  9   TRP B CB    1 
ATOM   5583  C  CG    . TRP B 1 9   ? 151.136 124.475 167.628 1.00 48.99 ?  9   TRP B CG    1 
ATOM   5584  C  CD1   . TRP B 1 9   ? 150.290 124.493 166.561 1.00 48.05 ?  9   TRP B CD1   1 
ATOM   5585  C  CD2   . TRP B 1 9   ? 152.460 124.572 167.093 1.00 48.63 ?  9   TRP B CD2   1 
ATOM   5586  N  NE1   . TRP B 1 9   ? 151.004 124.583 165.392 1.00 47.61 ?  9   TRP B NE1   1 
ATOM   5587  C  CE2   . TRP B 1 9   ? 152.339 124.635 165.692 1.00 50.20 ?  9   TRP B CE2   1 
ATOM   5588  C  CE3   . TRP B 1 9   ? 153.736 124.606 167.662 1.00 45.96 ?  9   TRP B CE3   1 
ATOM   5589  C  CZ2   . TRP B 1 9   ? 153.445 124.728 164.851 1.00 49.91 ?  9   TRP B CZ2   1 
ATOM   5590  C  CZ3   . TRP B 1 9   ? 154.831 124.700 166.826 1.00 51.15 ?  9   TRP B CZ3   1 
ATOM   5591  C  CH2   . TRP B 1 9   ? 154.679 124.759 165.437 1.00 51.69 ?  9   TRP B CH2   1 
ATOM   5592  N  N     . ILE B 1 10  ? 149.670 121.573 167.890 1.00 52.13 ?  10  ILE B N     1 
ATOM   5593  C  CA    . ILE B 1 10  ? 148.584 120.802 167.294 1.00 53.51 ?  10  ILE B CA    1 
ATOM   5594  C  C     . ILE B 1 10  ? 148.216 119.625 168.190 1.00 54.08 ?  10  ILE B C     1 
ATOM   5595  O  O     . ILE B 1 10  ? 147.033 119.307 168.366 1.00 56.39 ?  10  ILE B O     1 
ATOM   5596  C  CB    . ILE B 1 10  ? 148.968 120.347 165.875 1.00 54.76 ?  10  ILE B CB    1 
ATOM   5597  C  CG1   . ILE B 1 10  ? 148.841 121.511 164.890 1.00 53.72 ?  10  ILE B CG1   1 
ATOM   5598  C  CG2   . ILE B 1 10  ? 148.094 119.191 165.426 1.00 55.30 ?  10  ILE B CG2   1 
ATOM   5599  C  CD1   . ILE B 1 10  ? 147.647 122.406 165.140 1.00 54.18 ?  10  ILE B CD1   1 
ATOM   5600  N  N     . GLN B 1 11  ? 149.217 118.965 168.776 1.00 57.56 ?  11  GLN B N     1 
ATOM   5601  C  CA    . GLN B 1 11  ? 148.935 117.894 169.725 1.00 57.04 ?  11  GLN B CA    1 
ATOM   5602  C  C     . GLN B 1 11  ? 148.187 118.420 170.942 1.00 59.28 ?  11  GLN B C     1 
ATOM   5603  O  O     . GLN B 1 11  ? 147.202 117.816 171.380 1.00 60.20 ?  11  GLN B O     1 
ATOM   5604  C  CB    . GLN B 1 11  ? 150.233 117.212 170.158 1.00 56.99 ?  11  GLN B CB    1 
ATOM   5605  C  CG    . GLN B 1 11  ? 150.698 116.100 169.238 1.00 60.82 ?  11  GLN B CG    1 
ATOM   5606  C  CD    . GLN B 1 11  ? 152.206 115.950 169.231 1.00 62.31 ?  11  GLN B CD    1 
ATOM   5607  O  OE1   . GLN B 1 11  ? 152.815 115.732 168.185 1.00 61.39 ?  11  GLN B OE1   1 
ATOM   5608  N  NE2   . GLN B 1 11  ? 152.817 116.070 170.403 1.00 60.14 ?  11  GLN B NE2   1 
ATOM   5609  N  N     . LEU B 1 12  ? 148.634 119.551 171.494 1.00 58.79 ?  12  LEU B N     1 
ATOM   5610  C  CA    . LEU B 1 12  ? 147.976 120.113 172.670 1.00 54.13 ?  12  LEU B CA    1 
ATOM   5611  C  C     . LEU B 1 12  ? 146.540 120.517 172.362 1.00 57.99 ?  12  LEU B C     1 
ATOM   5612  O  O     . LEU B 1 12  ? 145.638 120.315 173.183 1.00 60.10 ?  12  LEU B O     1 
ATOM   5613  C  CB    . LEU B 1 12  ? 148.767 121.311 173.193 1.00 55.26 ?  12  LEU B CB    1 
ATOM   5614  C  CG    . LEU B 1 12  ? 149.863 121.004 174.212 1.00 58.07 ?  12  LEU B CG    1 
ATOM   5615  C  CD1   . LEU B 1 12  ? 150.743 122.222 174.424 1.00 58.53 ?  12  LEU B CD1   1 
ATOM   5616  C  CD2   . LEU B 1 12  ? 149.258 120.540 175.523 1.00 56.30 ?  12  LEU B CD2   1 
ATOM   5617  N  N     . ASN B 1 13  ? 146.310 121.099 171.184 1.00 53.89 ?  13  ASN B N     1 
ATOM   5618  C  CA    . ASN B 1 13  ? 144.957 121.467 170.787 1.00 52.68 ?  13  ASN B CA    1 
ATOM   5619  C  C     . ASN B 1 13  ? 144.090 120.231 170.583 1.00 56.13 ?  13  ASN B C     1 
ATOM   5620  O  O     . ASN B 1 13  ? 142.872 120.279 170.785 1.00 62.41 ?  13  ASN B O     1 
ATOM   5621  C  CB    . ASN B 1 13  ? 145.005 122.317 169.517 1.00 53.91 ?  13  ASN B CB    1 
ATOM   5622  C  CG    . ASN B 1 13  ? 143.638 122.534 168.906 1.00 53.99 ?  13  ASN B CG    1 
ATOM   5623  O  OD1   . ASN B 1 13  ? 143.224 121.800 168.010 1.00 55.79 ?  13  ASN B OD1   1 
ATOM   5624  N  ND2   . ASN B 1 13  ? 142.928 123.545 169.388 1.00 54.99 ?  13  ASN B ND2   1 
ATOM   5625  N  N     . ASN B 1 14  ? 144.701 119.114 170.185 1.00 59.08 ?  14  ASN B N     1 
ATOM   5626  C  CA    . ASN B 1 14  ? 143.947 117.884 169.983 1.00 55.76 ?  14  ASN B CA    1 
ATOM   5627  C  C     . ASN B 1 14  ? 143.579 117.201 171.294 1.00 58.53 ?  14  ASN B C     1 
ATOM   5628  O  O     . ASN B 1 14  ? 142.706 116.329 171.296 1.00 63.28 ?  14  ASN B O     1 
ATOM   5629  C  CB    . ASN B 1 14  ? 144.740 116.922 169.101 1.00 59.59 ?  14  ASN B CB    1 
ATOM   5630  C  CG    . ASN B 1 14  ? 144.651 117.273 167.630 1.00 59.07 ?  14  ASN B CG    1 
ATOM   5631  O  OD1   . ASN B 1 14  ? 144.382 118.417 167.269 1.00 59.30 ?  14  ASN B OD1   1 
ATOM   5632  N  ND2   . ASN B 1 14  ? 144.878 116.286 166.772 1.00 58.70 ?  14  ASN B ND2   1 
ATOM   5633  N  N     . GLU B 1 15  ? 144.216 117.576 172.405 1.00 59.48 ?  15  GLU B N     1 
ATOM   5634  C  CA    . GLU B 1 15  ? 143.884 116.988 173.697 1.00 59.95 ?  15  GLU B CA    1 
ATOM   5635  C  C     . GLU B 1 15  ? 142.601 117.548 174.292 1.00 61.82 ?  15  GLU B C     1 
ATOM   5636  O  O     . GLU B 1 15  ? 142.175 117.078 175.352 1.00 64.87 ?  15  GLU B O     1 
ATOM   5637  C  CB    . GLU B 1 15  ? 145.030 117.186 174.693 1.00 60.50 ?  15  GLU B CB    1 
ATOM   5638  C  CG    . GLU B 1 15  ? 146.396 116.802 174.165 1.00 62.55 ?  15  GLU B CG    1 
ATOM   5639  C  CD    . GLU B 1 15  ? 147.457 116.793 175.247 1.00 66.42 ?  15  GLU B CD    1 
ATOM   5640  O  OE1   . GLU B 1 15  ? 147.090 116.734 176.438 1.00 64.42 ?  15  GLU B OE1   1 
ATOM   5641  O  OE2   . GLU B 1 15  ? 148.657 116.846 174.905 1.00 66.45 -1 15  GLU B OE2   1 
ATOM   5642  N  N     . ILE B 1 16  ? 141.987 118.546 173.653 1.00 60.94 ?  16  ILE B N     1 
ATOM   5643  C  CA    . ILE B 1 16  ? 140.695 119.038 174.118 1.00 60.27 ?  16  ILE B CA    1 
ATOM   5644  C  C     . ILE B 1 16  ? 139.643 117.941 174.015 1.00 60.83 ?  16  ILE B C     1 
ATOM   5645  O  O     . ILE B 1 16  ? 138.840 117.742 174.934 1.00 61.27 ?  16  ILE B O     1 
ATOM   5646  C  CB    . ILE B 1 16  ? 140.285 120.294 173.328 1.00 61.94 ?  16  ILE B CB    1 
ATOM   5647  C  CG1   . ILE B 1 16  ? 141.395 121.345 173.387 1.00 60.80 ?  16  ILE B CG1   1 
ATOM   5648  C  CG2   . ILE B 1 16  ? 138.978 120.858 173.863 1.00 60.34 ?  16  ILE B CG2   1 
ATOM   5649  C  CD1   . ILE B 1 16  ? 140.942 122.735 173.015 1.00 58.23 ?  16  ILE B CD1   1 
ATOM   5650  N  N     . MET B 1 17  ? 139.637 117.210 172.898 1.00 62.13 ?  17  MET B N     1 
ATOM   5651  C  CA    . MET B 1 17  ? 138.659 116.146 172.710 1.00 63.00 ?  17  MET B CA    1 
ATOM   5652  C  C     . MET B 1 17  ? 138.925 114.942 173.603 1.00 63.88 ?  17  MET B C     1 
ATOM   5653  O  O     . MET B 1 17  ? 138.000 114.163 173.856 1.00 65.86 ?  17  MET B O     1 
ATOM   5654  C  CB    . MET B 1 17  ? 138.633 115.704 171.247 1.00 63.13 ?  17  MET B CB    1 
ATOM   5655  C  CG    . MET B 1 17  ? 138.459 116.808 170.196 1.00 63.32 ?  17  MET B CG    1 
ATOM   5656  S  SD    . MET B 1 17  ? 136.894 117.723 170.090 1.00 70.70 ?  17  MET B SD    1 
ATOM   5657  C  CE    . MET B 1 17  ? 136.888 118.736 171.565 1.00 62.37 ?  17  MET B CE    1 
ATOM   5658  N  N     . ILE B 1 18  ? 140.156 114.765 174.076 1.00 63.36 ?  18  ILE B N     1 
ATOM   5659  C  CA    . ILE B 1 18  ? 140.444 113.691 175.020 1.00 63.14 ?  18  ILE B CA    1 
ATOM   5660  C  C     . ILE B 1 18  ? 139.738 114.038 176.327 1.00 63.69 ?  18  ILE B C     1 
ATOM   5661  O  O     . ILE B 1 18  ? 140.113 114.991 177.016 1.00 64.62 ?  18  ILE B O     1 
ATOM   5662  C  CB    . ILE B 1 18  ? 141.952 113.496 175.225 1.00 63.13 ?  18  ILE B CB    1 
ATOM   5663  C  CG1   . ILE B 1 18  ? 142.557 112.681 174.078 1.00 62.85 ?  18  ILE B CG1   1 
ATOM   5664  C  CG2   . ILE B 1 18  ? 142.227 112.775 176.535 1.00 63.54 ?  18  ILE B CG2   1 
ATOM   5665  C  CD1   . ILE B 1 18  ? 142.734 113.442 172.781 1.00 62.27 ?  18  ILE B CD1   1 
ATOM   5666  N  N     . GLN B 1 19  ? 138.695 113.282 176.656 1.00 68.67 ?  19  GLN B N     1 
ATOM   5667  C  CA    . GLN B 1 19  ? 137.853 113.598 177.800 1.00 69.55 ?  19  GLN B CA    1 
ATOM   5668  C  C     . GLN B 1 19  ? 138.504 113.081 179.075 1.00 70.48 ?  19  GLN B C     1 
ATOM   5669  O  O     . GLN B 1 19  ? 138.701 111.872 179.236 1.00 71.79 ?  19  GLN B O     1 
ATOM   5670  C  CB    . GLN B 1 19  ? 136.462 112.995 177.616 1.00 70.06 ?  19  GLN B CB    1 
ATOM   5671  C  CG    . GLN B 1 19  ? 135.528 113.854 176.779 1.00 69.09 ?  19  GLN B CG    1 
ATOM   5672  C  CD    . GLN B 1 19  ? 134.114 113.875 177.320 1.00 72.31 ?  19  GLN B CD    1 
ATOM   5673  O  OE1   . GLN B 1 19  ? 133.859 113.440 178.442 1.00 72.66 ?  19  GLN B OE1   1 
ATOM   5674  N  NE2   . GLN B 1 19  ? 133.184 114.385 176.520 1.00 69.92 ?  19  GLN B NE2   1 
ATOM   5675  N  N     . LYS B 1 20  ? 138.841 113.997 179.978 1.00 74.71 ?  20  LYS B N     1 
ATOM   5676  C  CA    . LYS B 1 20  ? 139.420 113.663 181.272 1.00 74.45 ?  20  LYS B CA    1 
ATOM   5677  C  C     . LYS B 1 20  ? 138.387 113.953 182.351 1.00 77.20 ?  20  LYS B C     1 
ATOM   5678  O  O     . LYS B 1 20  ? 137.864 115.070 182.428 1.00 74.44 ?  20  LYS B O     1 
ATOM   5679  C  CB    . LYS B 1 20  ? 140.703 114.456 181.519 1.00 71.73 ?  20  LYS B CB    1 
ATOM   5680  C  CG    . LYS B 1 20  ? 141.375 114.151 182.846 1.00 74.91 ?  20  LYS B CG    1 
ATOM   5681  C  CD    . LYS B 1 20  ? 142.192 115.335 183.342 1.00 75.30 ?  20  LYS B CD    1 
ATOM   5682  C  CE    . LYS B 1 20  ? 141.325 116.567 183.534 1.00 76.62 ?  20  LYS B CE    1 
ATOM   5683  N  NZ    . LYS B 1 20  ? 140.051 116.251 184.236 1.00 78.76 1  20  LYS B NZ    1 
ATOM   5684  N  N     . ASP B 1 21  ? 138.094 112.945 183.176 1.00 82.99 ?  21  ASP B N     1 
ATOM   5685  C  CA    . ASP B 1 21  ? 137.104 113.054 184.249 1.00 82.58 ?  21  ASP B CA    1 
ATOM   5686  C  C     . ASP B 1 21  ? 135.731 113.439 183.701 1.00 82.92 ?  21  ASP B C     1 
ATOM   5687  O  O     . ASP B 1 21  ? 134.981 114.197 184.322 1.00 82.22 ?  21  ASP B O     1 
ATOM   5688  C  CB    . ASP B 1 21  ? 137.563 114.043 185.326 1.00 82.38 ?  21  ASP B CB    1 
ATOM   5689  C  CG    . ASP B 1 21  ? 136.818 113.866 186.636 1.00 84.51 ?  21  ASP B CG    1 
ATOM   5690  O  OD1   . ASP B 1 21  ? 136.560 112.707 187.024 1.00 82.89 ?  21  ASP B OD1   1 
ATOM   5691  O  OD2   . ASP B 1 21  ? 136.491 114.888 187.277 1.00 84.64 -1 21  ASP B OD2   1 
ATOM   5692  N  N     . GLY B 1 22  ? 135.398 112.915 182.523 1.00 75.34 ?  22  GLY B N     1 
ATOM   5693  C  CA    . GLY B 1 22  ? 134.097 113.150 181.931 1.00 74.48 ?  22  GLY B CA    1 
ATOM   5694  C  C     . GLY B 1 22  ? 133.891 114.526 181.341 1.00 76.15 ?  22  GLY B C     1 
ATOM   5695  O  O     . GLY B 1 22  ? 132.752 114.870 181.005 1.00 75.95 ?  22  GLY B O     1 
ATOM   5696  N  N     . LYS B 1 23  ? 134.947 115.324 181.205 1.00 72.59 ?  23  LYS B N     1 
ATOM   5697  C  CA    . LYS B 1 23  ? 134.843 116.673 180.673 1.00 69.37 ?  23  LYS B CA    1 
ATOM   5698  C  C     . LYS B 1 23  ? 135.950 116.916 179.659 1.00 70.04 ?  23  LYS B C     1 
ATOM   5699  O  O     . LYS B 1 23  ? 137.040 116.344 179.755 1.00 69.80 ?  23  LYS B O     1 
ATOM   5700  C  CB    . LYS B 1 23  ? 134.930 117.727 181.784 1.00 68.27 ?  23  LYS B CB    1 
ATOM   5701  C  CG    . LYS B 1 23  ? 133.784 117.692 182.777 1.00 68.38 ?  23  LYS B CG    1 
ATOM   5702  C  CD    . LYS B 1 23  ? 133.922 118.808 183.796 1.00 68.60 ?  23  LYS B CD    1 
ATOM   5703  C  CE    . LYS B 1 23  ? 132.865 118.712 184.879 1.00 69.97 ?  23  LYS B CE    1 
ATOM   5704  N  NZ    . LYS B 1 23  ? 133.089 119.719 185.951 1.00 68.39 1  23  LYS B NZ    1 
ATOM   5705  N  N     . PHE B 1 24  ? 135.658 117.771 178.682 1.00 65.61 ?  24  PHE B N     1 
ATOM   5706  C  CA    . PHE B 1 24  ? 136.680 118.190 177.735 1.00 62.62 ?  24  PHE B CA    1 
ATOM   5707  C  C     . PHE B 1 24  ? 137.757 118.996 178.449 1.00 61.66 ?  24  PHE B C     1 
ATOM   5708  O  O     . PHE B 1 24  ? 137.487 119.728 179.405 1.00 61.85 ?  24  PHE B O     1 
ATOM   5709  C  CB    . PHE B 1 24  ? 136.069 119.028 176.611 1.00 61.12 ?  24  PHE B CB    1 
ATOM   5710  C  CG    . PHE B 1 24  ? 135.097 118.278 175.750 1.00 61.30 ?  24  PHE B CG    1 
ATOM   5711  C  CD1   . PHE B 1 24  ? 135.528 117.615 174.615 1.00 64.24 ?  24  PHE B CD1   1 
ATOM   5712  C  CD2   . PHE B 1 24  ? 133.749 118.254 176.062 1.00 61.65 ?  24  PHE B CD2   1 
ATOM   5713  C  CE1   . PHE B 1 24  ? 134.634 116.930 173.816 1.00 64.73 ?  24  PHE B CE1   1 
ATOM   5714  C  CE2   . PHE B 1 24  ? 132.851 117.571 175.266 1.00 62.37 ?  24  PHE B CE2   1 
ATOM   5715  C  CZ    . PHE B 1 24  ? 133.295 116.908 174.141 1.00 61.31 ?  24  PHE B CZ    1 
ATOM   5716  N  N     . GLN B 1 25  ? 138.995 118.856 177.979 1.00 62.73 ?  25  GLN B N     1 
ATOM   5717  C  CA    . GLN B 1 25  ? 140.121 119.602 178.543 1.00 63.64 ?  25  GLN B CA    1 
ATOM   5718  C  C     . GLN B 1 25  ? 140.209 120.944 177.824 1.00 64.69 ?  25  GLN B C     1 
ATOM   5719  O  O     . GLN B 1 25  ? 141.033 121.165 176.934 1.00 64.40 ?  25  GLN B O     1 
ATOM   5720  C  CB    . GLN B 1 25  ? 141.411 118.801 178.426 1.00 64.71 ?  25  GLN B CB    1 
ATOM   5721  C  CG    . GLN B 1 25  ? 141.448 117.563 179.307 1.00 62.14 ?  25  GLN B CG    1 
ATOM   5722  C  CD    . GLN B 1 25  ? 142.631 116.670 179.003 1.00 63.89 ?  25  GLN B CD    1 
ATOM   5723  O  OE1   . GLN B 1 25  ? 143.712 116.840 179.563 1.00 63.37 ?  25  GLN B OE1   1 
ATOM   5724  N  NE2   . GLN B 1 25  ? 142.431 115.710 178.108 1.00 64.37 ?  25  GLN B NE2   1 
ATOM   5725  N  N     . PHE B 1 26  ? 139.323 121.858 178.230 1.00 59.58 ?  26  PHE B N     1 
ATOM   5726  C  CA    . PHE B 1 26  ? 139.275 123.175 177.605 1.00 56.88 ?  26  PHE B CA    1 
ATOM   5727  C  C     . PHE B 1 26  ? 140.524 123.991 177.907 1.00 59.74 ?  26  PHE B C     1 
ATOM   5728  O  O     . PHE B 1 26  ? 140.899 124.861 177.114 1.00 60.98 ?  26  PHE B O     1 
ATOM   5729  C  CB    . PHE B 1 26  ? 138.026 123.926 178.065 1.00 52.78 ?  26  PHE B CB    1 
ATOM   5730  C  CG    . PHE B 1 26  ? 136.751 123.393 177.482 1.00 55.55 ?  26  PHE B CG    1 
ATOM   5731  C  CD1   . PHE B 1 26  ? 136.618 123.221 176.115 1.00 55.27 ?  26  PHE B CD1   1 
ATOM   5732  C  CD2   . PHE B 1 26  ? 135.685 123.060 178.301 1.00 54.50 ?  26  PHE B CD2   1 
ATOM   5733  C  CE1   . PHE B 1 26  ? 135.447 122.729 175.576 1.00 56.32 ?  26  PHE B CE1   1 
ATOM   5734  C  CE2   . PHE B 1 26  ? 134.512 122.568 177.766 1.00 52.70 ?  26  PHE B CE2   1 
ATOM   5735  C  CZ    . PHE B 1 26  ? 134.392 122.402 176.402 1.00 52.96 ?  26  PHE B CZ    1 
ATOM   5736  N  N     . ASP B 1 27  ? 141.176 123.727 179.042 1.00 63.05 ?  27  ASP B N     1 
ATOM   5737  C  CA    . ASP B 1 27  ? 142.386 124.451 179.411 1.00 58.55 ?  27  ASP B CA    1 
ATOM   5738  C  C     . ASP B 1 27  ? 143.576 124.104 178.528 1.00 60.78 ?  27  ASP B C     1 
ATOM   5739  O  O     . ASP B 1 27  ? 144.593 124.803 178.592 1.00 62.31 ?  27  ASP B O     1 
ATOM   5740  C  CB    . ASP B 1 27  ? 142.732 124.172 180.874 1.00 60.43 ?  27  ASP B CB    1 
ATOM   5741  C  CG    . ASP B 1 27  ? 141.523 124.257 181.784 1.00 65.03 ?  27  ASP B CG    1 
ATOM   5742  O  OD1   . ASP B 1 27  ? 140.475 123.673 181.435 1.00 65.00 ?  27  ASP B OD1   1 
ATOM   5743  O  OD2   . ASP B 1 27  ? 141.619 124.906 182.846 1.00 65.17 -1 27  ASP B OD2   1 
ATOM   5744  N  N     . LYS B 1 28  ? 143.481 123.050 177.715 1.00 60.48 ?  28  LYS B N     1 
ATOM   5745  C  CA    . LYS B 1 28  ? 144.580 122.692 176.827 1.00 61.30 ?  28  LYS B CA    1 
ATOM   5746  C  C     . LYS B 1 28  ? 144.768 123.697 175.701 1.00 61.69 ?  28  LYS B C     1 
ATOM   5747  O  O     . LYS B 1 28  ? 145.857 123.761 175.121 1.00 62.22 ?  28  LYS B O     1 
ATOM   5748  C  CB    . LYS B 1 28  ? 144.351 121.298 176.242 1.00 61.12 ?  28  LYS B CB    1 
ATOM   5749  C  CG    . LYS B 1 28  ? 144.602 120.167 177.221 1.00 61.20 ?  28  LYS B CG    1 
ATOM   5750  C  CD    . LYS B 1 28  ? 146.087 119.947 177.434 1.00 61.63 ?  28  LYS B CD    1 
ATOM   5751  C  CE    . LYS B 1 28  ? 146.347 119.077 178.649 1.00 61.66 ?  28  LYS B CE    1 
ATOM   5752  N  NZ    . LYS B 1 28  ? 147.783 118.710 178.765 1.00 59.46 1  28  LYS B NZ    1 
ATOM   5753  N  N     . ASP B 1 29  ? 143.738 124.483 175.379 1.00 58.24 ?  29  ASP B N     1 
ATOM   5754  C  CA    . ASP B 1 29  ? 143.866 125.450 174.295 1.00 55.40 ?  29  ASP B CA    1 
ATOM   5755  C  C     . ASP B 1 29  ? 144.754 126.623 174.692 1.00 55.16 ?  29  ASP B C     1 
ATOM   5756  O  O     . ASP B 1 29  ? 145.429 127.202 173.833 1.00 57.74 ?  29  ASP B O     1 
ATOM   5757  C  CB    . ASP B 1 29  ? 142.486 125.937 173.862 1.00 55.23 ?  29  ASP B CB    1 
ATOM   5758  C  CG    . ASP B 1 29  ? 142.321 125.948 172.356 1.00 58.52 ?  29  ASP B CG    1 
ATOM   5759  O  OD1   . ASP B 1 29  ? 141.484 126.723 171.852 1.00 55.50 ?  29  ASP B OD1   1 
ATOM   5760  O  OD2   . ASP B 1 29  ? 143.031 125.179 171.674 1.00 58.35 -1 29  ASP B OD2   1 
ATOM   5761  N  N     . LYS B 1 30  ? 144.762 126.993 175.974 1.00 55.30 ?  30  LYS B N     1 
ATOM   5762  C  CA    . LYS B 1 30  ? 145.734 127.973 176.448 1.00 56.62 ?  30  LYS B CA    1 
ATOM   5763  C  C     . LYS B 1 30  ? 147.152 127.429 176.332 1.00 56.50 ?  30  LYS B C     1 
ATOM   5764  O  O     . LYS B 1 30  ? 148.065 128.139 175.891 1.00 57.10 ?  30  LYS B O     1 
ATOM   5765  C  CB    . LYS B 1 30  ? 145.428 128.366 177.892 1.00 54.70 ?  30  LYS B CB    1 
ATOM   5766  C  CG    . LYS B 1 30  ? 144.120 129.114 178.070 1.00 56.61 ?  30  LYS B CG    1 
ATOM   5767  C  CD    . LYS B 1 30  ? 144.357 130.552 178.505 1.00 58.11 ?  30  LYS B CD    1 
ATOM   5768  C  CE    . LYS B 1 30  ? 145.422 130.637 179.589 1.00 58.82 ?  30  LYS B CE    1 
ATOM   5769  N  NZ    . LYS B 1 30  ? 145.450 131.974 180.243 1.00 58.06 1  30  LYS B NZ    1 
ATOM   5770  N  N     . GLU B 1 31  ? 147.352 126.167 176.715 1.00 57.78 ?  31  GLU B N     1 
ATOM   5771  C  CA    . GLU B 1 31  ? 148.640 125.526 176.490 1.00 54.53 ?  31  GLU B CA    1 
ATOM   5772  C  C     . GLU B 1 31  ? 148.938 125.420 175.001 1.00 55.31 ?  31  GLU B C     1 
ATOM   5773  O  O     . GLU B 1 31  ? 150.082 125.602 174.576 1.00 57.92 ?  31  GLU B O     1 
ATOM   5774  C  CB    . GLU B 1 31  ? 148.664 124.146 177.145 1.00 55.06 ?  31  GLU B CB    1 
ATOM   5775  C  CG    . GLU B 1 31  ? 148.637 124.178 178.663 1.00 56.40 ?  31  GLU B CG    1 
ATOM   5776  C  CD    . GLU B 1 31  ? 148.717 122.793 179.274 1.00 63.70 ?  31  GLU B CD    1 
ATOM   5777  O  OE1   . GLU B 1 31  ? 148.702 121.804 178.512 1.00 65.30 ?  31  GLU B OE1   1 
ATOM   5778  O  OE2   . GLU B 1 31  ? 148.795 122.693 180.516 1.00 60.64 -1 31  GLU B OE2   1 
ATOM   5779  N  N     . ALA B 1 32  ? 147.915 125.130 174.195 1.00 52.44 ?  32  ALA B N     1 
ATOM   5780  C  CA    . ALA B 1 32  ? 148.118 125.021 172.755 1.00 49.90 ?  32  ALA B CA    1 
ATOM   5781  C  C     . ALA B 1 32  ? 148.575 126.344 172.154 1.00 51.55 ?  32  ALA B C     1 
ATOM   5782  O  O     . ALA B 1 32  ? 149.519 126.374 171.361 1.00 52.12 ?  32  ALA B O     1 
ATOM   5783  C  CB    . ALA B 1 32  ? 146.835 124.541 172.076 1.00 49.16 ?  32  ALA B CB    1 
ATOM   5784  N  N     . VAL B 1 33  ? 147.928 127.452 172.527 1.00 54.60 ?  33  VAL B N     1 
ATOM   5785  C  CA    . VAL B 1 33  ? 148.312 128.744 171.965 1.00 50.88 ?  33  VAL B CA    1 
ATOM   5786  C  C     . VAL B 1 33  ? 149.671 129.183 172.502 1.00 53.80 ?  33  VAL B C     1 
ATOM   5787  O  O     . VAL B 1 33  ? 150.477 129.775 171.772 1.00 55.05 ?  33  VAL B O     1 
ATOM   5788  C  CB    . VAL B 1 33  ? 147.219 129.801 172.218 1.00 45.90 ?  33  VAL B CB    1 
ATOM   5789  C  CG1   . VAL B 1 33  ? 147.056 130.099 173.696 1.00 47.37 ?  33  VAL B CG1   1 
ATOM   5790  C  CG2   . VAL B 1 33  ? 147.525 131.074 171.444 1.00 49.25 ?  33  VAL B CG2   1 
ATOM   5791  N  N     . HIS B 1 34  ? 149.952 128.903 173.779 1.00 51.44 ?  34  HIS B N     1 
ATOM   5792  C  CA    . HIS B 1 34  ? 151.262 129.239 174.329 1.00 47.49 ?  34  HIS B CA    1 
ATOM   5793  C  C     . HIS B 1 34  ? 152.369 128.490 173.601 1.00 48.88 ?  34  HIS B C     1 
ATOM   5794  O  O     . HIS B 1 34  ? 153.402 129.071 173.249 1.00 52.29 ?  34  HIS B O     1 
ATOM   5795  C  CB    . HIS B 1 34  ? 151.298 128.930 175.825 1.00 52.36 ?  34  HIS B CB    1 
ATOM   5796  C  CG    . HIS B 1 34  ? 152.604 129.262 176.476 1.00 53.70 ?  34  HIS B CG    1 
ATOM   5797  N  ND1   . HIS B 1 34  ? 153.631 128.350 176.593 1.00 52.99 ?  34  HIS B ND1   1 
ATOM   5798  C  CD2   . HIS B 1 34  ? 153.051 130.406 177.045 1.00 53.10 ?  34  HIS B CD2   1 
ATOM   5799  C  CE1   . HIS B 1 34  ? 154.654 128.917 177.206 1.00 51.59 ?  34  HIS B CE1   1 
ATOM   5800  N  NE2   . HIS B 1 34  ? 154.327 130.165 177.493 1.00 53.65 ?  34  HIS B NE2   1 
ATOM   5801  N  N     . SER B 1 35  ? 152.168 127.191 173.366 1.00 54.75 ?  35  SER B N     1 
ATOM   5802  C  CA    . SER B 1 35  ? 153.150 126.408 172.627 1.00 52.29 ?  35  SER B CA    1 
ATOM   5803  C  C     . SER B 1 35  ? 153.274 126.900 171.193 1.00 52.81 ?  35  SER B C     1 
ATOM   5804  O  O     . SER B 1 35  ? 154.386 127.021 170.669 1.00 55.62 ?  35  SER B O     1 
ATOM   5805  C  CB    . SER B 1 35  ? 152.772 124.928 172.657 1.00 52.45 ?  35  SER B CB    1 
ATOM   5806  O  OG    . SER B 1 35  ? 153.691 124.156 171.905 1.00 56.52 ?  35  SER B OG    1 
ATOM   5807  N  N     . TYR B 1 36  ? 152.143 127.196 170.548 1.00 49.85 ?  36  TYR B N     1 
ATOM   5808  C  CA    . TYR B 1 36  ? 152.170 127.723 169.188 1.00 50.26 ?  36  TYR B CA    1 
ATOM   5809  C  C     . TYR B 1 36  ? 153.036 128.966 169.108 1.00 47.90 ?  36  TYR B C     1 
ATOM   5810  O  O     . TYR B 1 36  ? 153.962 129.040 168.293 1.00 49.13 ?  36  TYR B O     1 
ATOM   5811  C  CB    . TYR B 1 36  ? 150.748 128.033 168.722 1.00 45.19 ?  36  TYR B CB    1 
ATOM   5812  C  CG    . TYR B 1 36  ? 150.669 128.638 167.339 1.00 43.48 ?  36  TYR B CG    1 
ATOM   5813  C  CD1   . TYR B 1 36  ? 151.339 128.064 166.269 1.00 44.00 ?  36  TYR B CD1   1 
ATOM   5814  C  CD2   . TYR B 1 36  ? 149.926 129.787 167.106 1.00 45.84 ?  36  TYR B CD2   1 
ATOM   5815  C  CE1   . TYR B 1 36  ? 151.267 128.610 165.006 1.00 46.30 ?  36  TYR B CE1   1 
ATOM   5816  C  CE2   . TYR B 1 36  ? 149.849 130.343 165.845 1.00 44.51 ?  36  TYR B CE2   1 
ATOM   5817  C  CZ    . TYR B 1 36  ? 150.523 129.751 164.800 1.00 46.87 ?  36  TYR B CZ    1 
ATOM   5818  O  OH    . TYR B 1 36  ? 150.451 130.300 163.541 1.00 47.50 ?  36  TYR B OH    1 
ATOM   5819  N  N     . PHE B 1 37  ? 152.775 129.941 169.980 1.00 51.88 ?  37  PHE B N     1 
ATOM   5820  C  CA    . PHE B 1 37  ? 153.592 131.147 169.998 1.00 50.44 ?  37  PHE B CA    1 
ATOM   5821  C  C     . PHE B 1 37  ? 155.055 130.807 170.241 1.00 51.90 ?  37  PHE B C     1 
ATOM   5822  O  O     . PHE B 1 37  ? 155.890 130.978 169.347 1.00 55.87 ?  37  PHE B O     1 
ATOM   5823  C  CB    . PHE B 1 37  ? 153.073 132.123 171.051 1.00 52.29 ?  37  PHE B CB    1 
ATOM   5824  C  CG    . PHE B 1 37  ? 152.198 133.196 170.483 1.00 53.14 ?  37  PHE B CG    1 
ATOM   5825  C  CD1   . PHE B 1 37  ? 152.752 134.355 169.971 1.00 51.94 ?  37  PHE B CD1   1 
ATOM   5826  C  CD2   . PHE B 1 37  ? 150.826 133.040 170.438 1.00 52.91 ?  37  PHE B CD2   1 
ATOM   5827  C  CE1   . PHE B 1 37  ? 151.954 135.341 169.439 1.00 53.84 ?  37  PHE B CE1   1 
ATOM   5828  C  CE2   . PHE B 1 37  ? 150.025 134.023 169.908 1.00 51.40 ?  37  PHE B CE2   1 
ATOM   5829  C  CZ    . PHE B 1 37  ? 150.589 135.174 169.407 1.00 51.87 ?  37  PHE B CZ    1 
ATOM   5830  N  N     . VAL B 1 38  ? 155.357 130.231 171.409 1.00 55.94 ?  38  VAL B N     1 
ATOM   5831  C  CA    . VAL B 1 38  ? 156.734 130.066 171.863 1.00 56.74 ?  38  VAL B CA    1 
ATOM   5832  C  C     . VAL B 1 38  ? 157.556 129.219 170.895 1.00 55.35 ?  38  VAL B C     1 
ATOM   5833  O  O     . VAL B 1 38  ? 158.774 129.403 170.784 1.00 57.62 ?  38  VAL B O     1 
ATOM   5834  C  CB    . VAL B 1 38  ? 156.724 129.479 173.293 1.00 54.50 ?  38  VAL B CB    1 
ATOM   5835  C  CG1   . VAL B 1 38  ? 157.973 128.662 173.579 1.00 56.35 ?  38  VAL B CG1   1 
ATOM   5836  C  CG2   . VAL B 1 38  ? 156.568 130.593 174.315 1.00 52.68 ?  38  VAL B CG2   1 
ATOM   5837  N  N     . ASP B 1 39  ? 156.918 128.315 170.150 1.00 53.36 ?  39  ASP B N     1 
ATOM   5838  C  CA    . ASP B 1 39  ? 157.653 127.412 169.277 1.00 52.42 ?  39  ASP B CA    1 
ATOM   5839  C  C     . ASP B 1 39  ? 157.669 127.835 167.815 1.00 57.74 ?  39  ASP B C     1 
ATOM   5840  O  O     . ASP B 1 39  ? 158.609 127.478 167.099 1.00 61.98 ?  39  ASP B O     1 
ATOM   5841  C  CB    . ASP B 1 39  ? 157.074 125.996 169.375 1.00 55.14 ?  39  ASP B CB    1 
ATOM   5842  C  CG    . ASP B 1 39  ? 157.199 125.412 170.765 1.00 60.48 ?  39  ASP B CG    1 
ATOM   5843  O  OD1   . ASP B 1 39  ? 157.788 126.078 171.641 1.00 59.89 ?  39  ASP B OD1   1 
ATOM   5844  O  OD2   . ASP B 1 39  ? 156.709 124.285 170.986 1.00 62.77 -1 39  ASP B OD2   1 
ATOM   5845  N  N     . TYR B 1 40  ? 156.669 128.576 167.339 1.00 58.16 ?  40  TYR B N     1 
ATOM   5846  C  CA    . TYR B 1 40  ? 156.604 128.938 165.930 1.00 55.81 ?  40  TYR B CA    1 
ATOM   5847  C  C     . TYR B 1 40  ? 156.618 130.440 165.704 1.00 59.41 ?  40  TYR B C     1 
ATOM   5848  O  O     . TYR B 1 40  ? 157.375 130.926 164.855 1.00 62.58 ?  40  TYR B O     1 
ATOM   5849  C  CB    . TYR B 1 40  ? 155.343 128.324 165.299 1.00 52.29 ?  40  TYR B CB    1 
ATOM   5850  C  CG    . TYR B 1 40  ? 155.273 128.454 163.797 1.00 56.35 ?  40  TYR B CG    1 
ATOM   5851  C  CD1   . TYR B 1 40  ? 156.013 127.619 162.973 1.00 56.20 ?  40  TYR B CD1   1 
ATOM   5852  C  CD2   . TYR B 1 40  ? 154.460 129.409 163.202 1.00 58.17 ?  40  TYR B CD2   1 
ATOM   5853  C  CE1   . TYR B 1 40  ? 155.950 127.734 161.599 1.00 57.45 ?  40  TYR B CE1   1 
ATOM   5854  C  CE2   . TYR B 1 40  ? 154.389 129.532 161.830 1.00 57.38 ?  40  TYR B CE2   1 
ATOM   5855  C  CZ    . TYR B 1 40  ? 155.136 128.692 161.032 1.00 59.93 ?  40  TYR B CZ    1 
ATOM   5856  O  OH    . TYR B 1 40  ? 155.069 128.811 159.663 1.00 61.60 ?  40  TYR B OH    1 
ATOM   5857  N  N     . ILE B 1 41  ? 155.801 131.195 166.440 1.00 54.61 ?  41  ILE B N     1 
ATOM   5858  C  CA    . ILE B 1 41  ? 155.615 132.606 166.121 1.00 54.22 ?  41  ILE B CA    1 
ATOM   5859  C  C     . ILE B 1 41  ? 156.846 133.407 166.521 1.00 53.52 ?  41  ILE B C     1 
ATOM   5860  O  O     . ILE B 1 41  ? 157.373 134.199 165.733 1.00 56.05 ?  41  ILE B O     1 
ATOM   5861  C  CB    . ILE B 1 41  ? 154.342 133.148 166.793 1.00 52.78 ?  41  ILE B CB    1 
ATOM   5862  C  CG1   . ILE B 1 41  ? 153.109 132.399 166.286 1.00 50.99 ?  41  ILE B CG1   1 
ATOM   5863  C  CG2   . ILE B 1 41  ? 154.198 134.638 166.537 1.00 51.98 ?  41  ILE B CG2   1 
ATOM   5864  C  CD1   . ILE B 1 41  ? 152.987 132.376 164.782 1.00 49.66 ?  41  ILE B CD1   1 
ATOM   5865  N  N     . ASN B 1 42  ? 157.328 133.205 167.749 1.00 52.27 ?  42  ASN B N     1 
ATOM   5866  C  CA    . ASN B 1 42  ? 158.516 133.922 168.197 1.00 54.55 ?  42  ASN B CA    1 
ATOM   5867  C  C     . ASN B 1 42  ? 159.747 133.521 167.395 1.00 56.60 ?  42  ASN B C     1 
ATOM   5868  O  O     . ASN B 1 42  ? 160.690 134.310 167.275 1.00 58.07 ?  42  ASN B O     1 
ATOM   5869  C  CB    . ASN B 1 42  ? 158.746 133.678 169.688 1.00 55.05 ?  42  ASN B CB    1 
ATOM   5870  C  CG    . ASN B 1 42  ? 157.603 134.191 170.543 1.00 56.64 ?  42  ASN B CG    1 
ATOM   5871  O  OD1   . ASN B 1 42  ? 156.608 134.697 170.026 1.00 59.11 ?  42  ASN B OD1   1 
ATOM   5872  N  ND2   . ASN B 1 42  ? 157.746 134.070 171.856 1.00 58.92 ?  42  ASN B ND2   1 
ATOM   5873  N  N     . GLN B 1 43  ? 159.757 132.307 166.842 1.00 59.89 ?  43  GLN B N     1 
ATOM   5874  C  CA    . GLN B 1 43  ? 160.860 131.887 165.985 1.00 57.85 ?  43  GLN B CA    1 
ATOM   5875  C  C     . GLN B 1 43  ? 160.773 132.525 164.604 1.00 58.98 ?  43  GLN B C     1 
ATOM   5876  O  O     . GLN B 1 43  ? 161.798 132.895 164.023 1.00 61.60 ?  43  GLN B O     1 
ATOM   5877  C  CB    . GLN B 1 43  ? 160.880 130.363 165.864 1.00 57.38 ?  43  GLN B CB    1 
ATOM   5878  C  CG    . GLN B 1 43  ? 161.747 129.662 166.898 1.00 60.30 ?  43  GLN B CG    1 
ATOM   5879  C  CD    . GLN B 1 43  ? 161.231 129.842 168.311 1.00 62.50 ?  43  GLN B CD    1 
ATOM   5880  O  OE1   . GLN B 1 43  ? 160.062 130.163 168.519 1.00 62.16 ?  43  GLN B OE1   1 
ATOM   5881  N  NE2   . GLN B 1 43  ? 162.101 129.639 169.292 1.00 60.18 ?  43  GLN B NE2   1 
ATOM   5882  N  N     . ASN B 1 44  ? 159.562 132.662 164.065 1.00 54.48 ?  44  ASN B N     1 
ATOM   5883  C  CA    . ASN B 1 44  ? 159.361 133.148 162.708 1.00 56.91 ?  44  ASN B CA    1 
ATOM   5884  C  C     . ASN B 1 44  ? 159.001 134.627 162.652 1.00 57.23 ?  44  ASN B C     1 
ATOM   5885  O  O     . ASN B 1 44  ? 158.659 135.129 161.577 1.00 55.75 ?  44  ASN B O     1 
ATOM   5886  C  CB    . ASN B 1 44  ? 158.281 132.321 162.006 1.00 54.58 ?  44  ASN B CB    1 
ATOM   5887  C  CG    . ASN B 1 44  ? 158.698 130.880 161.786 1.00 58.80 ?  44  ASN B CG    1 
ATOM   5888  O  OD1   . ASN B 1 44  ? 158.831 130.428 160.648 1.00 62.13 ?  44  ASN B OD1   1 
ATOM   5889  N  ND2   . ASN B 1 44  ? 158.895 130.143 162.874 1.00 57.89 ?  44  ASN B ND2   1 
ATOM   5890  N  N     . THR B 1 45  ? 159.069 135.334 163.776 1.00 57.35 ?  45  THR B N     1 
ATOM   5891  C  CA    . THR B 1 45  ? 158.805 136.766 163.805 1.00 58.16 ?  45  THR B CA    1 
ATOM   5892  C  C     . THR B 1 45  ? 160.113 137.521 163.607 1.00 57.10 ?  45  THR B C     1 
ATOM   5893  O  O     . THR B 1 45  ? 161.036 137.393 164.417 1.00 58.92 ?  45  THR B O     1 
ATOM   5894  C  CB    . THR B 1 45  ? 158.151 137.178 165.124 1.00 56.69 ?  45  THR B CB    1 
ATOM   5895  O  OG1   . THR B 1 45  ? 156.858 136.572 165.230 1.00 60.69 ?  45  THR B OG1   1 
ATOM   5896  C  CG2   . THR B 1 45  ? 158.006 138.690 165.197 1.00 54.98 ?  45  THR B CG2   1 
ATOM   5897  N  N     . VAL B 1 46  ? 160.192 138.300 162.528 1.00 56.57 ?  46  VAL B N     1 
ATOM   5898  C  CA    . VAL B 1 46  ? 161.360 139.142 162.305 1.00 56.20 ?  46  VAL B CA    1 
ATOM   5899  C  C     . VAL B 1 46  ? 161.418 140.202 163.394 1.00 57.03 ?  46  VAL B C     1 
ATOM   5900  O  O     . VAL B 1 46  ? 160.447 140.932 163.626 1.00 58.62 ?  46  VAL B O     1 
ATOM   5901  C  CB    . VAL B 1 46  ? 161.311 139.784 160.912 1.00 54.12 ?  46  VAL B CB    1 
ATOM   5902  C  CG1   . VAL B 1 46  ? 162.556 140.622 160.673 1.00 54.46 ?  46  VAL B CG1   1 
ATOM   5903  C  CG2   . VAL B 1 46  ? 161.174 138.722 159.846 1.00 54.07 ?  46  VAL B CG2   1 
ATOM   5904  N  N     . PHE B 1 47  ? 162.557 140.290 164.070 1.00 61.45 ?  47  PHE B N     1 
ATOM   5905  C  CA    . PHE B 1 47  ? 162.753 141.253 165.139 1.00 63.31 ?  47  PHE B CA    1 
ATOM   5906  C  C     . PHE B 1 47  ? 163.784 142.287 164.718 1.00 64.07 ?  47  PHE B C     1 
ATOM   5907  O  O     . PHE B 1 47  ? 164.764 141.965 164.039 1.00 63.48 ?  47  PHE B O     1 
ATOM   5908  C  CB    . PHE B 1 47  ? 163.197 140.568 166.432 1.00 62.59 ?  47  PHE B CB    1 
ATOM   5909  C  CG    . PHE B 1 47  ? 163.122 141.455 167.641 1.00 64.31 ?  47  PHE B CG    1 
ATOM   5910  C  CD1   . PHE B 1 47  ? 161.902 141.758 168.217 1.00 62.63 ?  47  PHE B CD1   1 
ATOM   5911  C  CD2   . PHE B 1 47  ? 164.272 141.989 168.197 1.00 63.97 ?  47  PHE B CD2   1 
ATOM   5912  C  CE1   . PHE B 1 47  ? 161.827 142.577 169.328 1.00 64.84 ?  47  PHE B CE1   1 
ATOM   5913  C  CE2   . PHE B 1 47  ? 164.206 142.807 169.308 1.00 63.35 ?  47  PHE B CE2   1 
ATOM   5914  C  CZ    . PHE B 1 47  ? 162.982 143.102 169.875 1.00 64.46 ?  47  PHE B CZ    1 
ATOM   5915  N  N     . PHE B 1 48  ? 163.553 143.531 165.124 1.00 61.83 ?  48  PHE B N     1 
ATOM   5916  C  CA    . PHE B 1 48  ? 164.433 144.644 164.821 1.00 57.75 ?  48  PHE B CA    1 
ATOM   5917  C  C     . PHE B 1 48  ? 164.905 145.268 166.126 1.00 60.79 ?  48  PHE B C     1 
ATOM   5918  O  O     . PHE B 1 48  ? 164.231 145.170 167.156 1.00 61.58 ?  48  PHE B O     1 
ATOM   5919  C  CB    . PHE B 1 48  ? 163.731 145.698 163.955 1.00 58.73 ?  48  PHE B CB    1 
ATOM   5920  C  CG    . PHE B 1 48  ? 163.202 145.166 162.651 1.00 57.73 ?  48  PHE B CG    1 
ATOM   5921  C  CD1   . PHE B 1 48  ? 162.043 144.408 162.609 1.00 57.85 ?  48  PHE B CD1   1 
ATOM   5922  C  CD2   . PHE B 1 48  ? 163.859 145.435 161.463 1.00 60.31 ?  48  PHE B CD2   1 
ATOM   5923  C  CE1   . PHE B 1 48  ? 161.555 143.927 161.411 1.00 59.31 ?  48  PHE B CE1   1 
ATOM   5924  C  CE2   . PHE B 1 48  ? 163.374 144.956 160.263 1.00 60.19 ?  48  PHE B CE2   1 
ATOM   5925  C  CZ    . PHE B 1 48  ? 162.221 144.201 160.238 1.00 57.88 ?  48  PHE B CZ    1 
ATOM   5926  N  N     . HIS B 1 49  ? 166.078 145.902 166.077 1.00 65.61 ?  49  HIS B N     1 
ATOM   5927  C  CA    . HIS B 1 49  ? 166.653 146.481 167.286 1.00 65.59 ?  49  HIS B CA    1 
ATOM   5928  C  C     . HIS B 1 49  ? 165.751 147.565 167.863 1.00 67.22 ?  49  HIS B C     1 
ATOM   5929  O  O     . HIS B 1 49  ? 165.595 147.670 169.085 1.00 67.83 ?  49  HIS B O     1 
ATOM   5930  C  CB    . HIS B 1 49  ? 168.045 147.039 166.991 1.00 66.47 ?  49  HIS B CB    1 
ATOM   5931  C  CG    . HIS B 1 49  ? 168.909 147.179 168.205 1.00 70.11 ?  49  HIS B CG    1 
ATOM   5932  N  ND1   . HIS B 1 49  ? 168.643 148.087 169.208 1.00 69.32 ?  49  HIS B ND1   1 
ATOM   5933  C  CD2   . HIS B 1 49  ? 170.033 146.524 168.580 1.00 69.08 ?  49  HIS B CD2   1 
ATOM   5934  C  CE1   . HIS B 1 49  ? 169.567 147.986 170.147 1.00 68.02 ?  49  HIS B CE1   1 
ATOM   5935  N  NE2   . HIS B 1 49  ? 170.422 147.045 169.790 1.00 68.93 ?  49  HIS B NE2   1 
ATOM   5936  N  N     . ASN B 1 50  ? 165.148 148.378 167.001 1.00 65.61 ?  50  ASN B N     1 
ATOM   5937  C  CA    . ASN B 1 50  ? 164.241 149.430 167.430 1.00 63.02 ?  50  ASN B CA    1 
ATOM   5938  C  C     . ASN B 1 50  ? 163.054 149.480 166.481 1.00 61.96 ?  50  ASN B C     1 
ATOM   5939  O  O     . ASN B 1 50  ? 163.085 148.917 165.385 1.00 61.45 ?  50  ASN B O     1 
ATOM   5940  C  CB    . ASN B 1 50  ? 164.942 150.793 167.484 1.00 61.90 ?  50  ASN B CB    1 
ATOM   5941  C  CG    . ASN B 1 50  ? 165.765 151.073 166.245 1.00 63.89 ?  50  ASN B CG    1 
ATOM   5942  O  OD1   . ASN B 1 50  ? 165.224 151.354 165.177 1.00 64.93 ?  50  ASN B OD1   1 
ATOM   5943  N  ND2   . ASN B 1 50  ? 167.083 150.995 166.380 1.00 64.38 ?  50  ASN B ND2   1 
ATOM   5944  N  N     . LEU B 1 51  ? 161.994 150.159 166.926 1.00 58.68 ?  51  LEU B N     1 
ATOM   5945  C  CA    . LEU B 1 51  ? 160.816 150.325 166.082 1.00 58.75 ?  51  LEU B CA    1 
ATOM   5946  C  C     . LEU B 1 51  ? 161.127 151.158 164.845 1.00 60.56 ?  51  LEU B C     1 
ATOM   5947  O  O     . LEU B 1 51  ? 160.513 150.954 163.792 1.00 62.00 ?  51  LEU B O     1 
ATOM   5948  C  CB    . LEU B 1 51  ? 159.682 150.963 166.884 1.00 58.13 ?  51  LEU B CB    1 
ATOM   5949  C  CG    . LEU B 1 51  ? 158.396 151.309 166.133 1.00 57.06 ?  51  LEU B CG    1 
ATOM   5950  C  CD1   . LEU B 1 51  ? 157.794 150.073 165.484 1.00 54.72 ?  51  LEU B CD1   1 
ATOM   5951  C  CD2   . LEU B 1 51  ? 157.399 151.970 167.064 1.00 57.42 ?  51  LEU B CD2   1 
ATOM   5952  N  N     . LYS B 1 52  ? 162.071 152.097 164.953 1.00 59.05 ?  52  LYS B N     1 
ATOM   5953  C  CA    . LYS B 1 52  ? 162.442 152.912 163.800 1.00 57.11 ?  52  LYS B CA    1 
ATOM   5954  C  C     . LYS B 1 52  ? 163.007 152.054 162.676 1.00 60.44 ?  52  LYS B C     1 
ATOM   5955  O  O     . LYS B 1 52  ? 162.662 152.248 161.504 1.00 61.28 ?  52  LYS B O     1 
ATOM   5956  C  CB    . LYS B 1 52  ? 163.454 153.977 164.219 1.00 56.54 ?  52  LYS B CB    1 
ATOM   5957  C  CG    . LYS B 1 52  ? 163.407 155.245 163.389 1.00 60.79 ?  52  LYS B CG    1 
ATOM   5958  C  CD    . LYS B 1 52  ? 164.550 156.179 163.754 1.00 63.71 ?  52  LYS B CD    1 
ATOM   5959  C  CE    . LYS B 1 52  ? 164.239 156.969 165.014 1.00 60.86 ?  52  LYS B CE    1 
ATOM   5960  N  NZ    . LYS B 1 52  ? 165.385 156.980 165.964 1.00 61.13 1  52  LYS B NZ    1 
ATOM   5961  N  N     . GLU B 1 53  ? 163.877 151.099 163.015 1.00 62.10 ?  53  GLU B N     1 
ATOM   5962  C  CA    . GLU B 1 53  ? 164.441 150.218 161.998 1.00 60.79 ?  53  GLU B CA    1 
ATOM   5963  C  C     . GLU B 1 53  ? 163.360 149.369 161.343 1.00 61.00 ?  53  GLU B C     1 
ATOM   5964  O  O     . GLU B 1 53  ? 163.363 149.181 160.121 1.00 61.80 ?  53  GLU B O     1 
ATOM   5965  C  CB    . GLU B 1 53  ? 165.521 149.331 162.615 1.00 60.31 ?  53  GLU B CB    1 
ATOM   5966  C  CG    . GLU B 1 53  ? 166.478 148.725 161.602 1.00 62.43 ?  53  GLU B CG    1 
ATOM   5967  C  CD    . GLU B 1 53  ? 166.766 147.263 161.873 1.00 65.53 ?  53  GLU B CD    1 
ATOM   5968  O  OE1   . GLU B 1 53  ? 166.918 146.895 163.057 1.00 66.13 ?  53  GLU B OE1   1 
ATOM   5969  O  OE2   . GLU B 1 53  ? 166.841 146.481 160.903 1.00 64.07 -1 53  GLU B OE2   1 
ATOM   5970  N  N     . LYS B 1 54  ? 162.423 148.851 162.141 1.00 58.53 ?  54  LYS B N     1 
ATOM   5971  C  CA    . LYS B 1 54  ? 161.334 148.050 161.591 1.00 58.25 ?  54  LYS B CA    1 
ATOM   5972  C  C     . LYS B 1 54  ? 160.474 148.876 160.645 1.00 54.87 ?  54  LYS B C     1 
ATOM   5973  O  O     . LYS B 1 54  ? 160.127 148.426 159.546 1.00 56.61 ?  54  LYS B O     1 
ATOM   5974  C  CB    . LYS B 1 54  ? 160.485 147.476 162.723 1.00 56.86 ?  54  LYS B CB    1 
ATOM   5975  C  CG    . LYS B 1 54  ? 159.177 146.861 162.258 1.00 56.41 ?  54  LYS B CG    1 
ATOM   5976  C  CD    . LYS B 1 54  ? 158.497 146.096 163.376 1.00 57.38 ?  54  LYS B CD    1 
ATOM   5977  C  CE    . LYS B 1 54  ? 157.194 145.479 162.902 1.00 59.39 ?  54  LYS B CE    1 
ATOM   5978  N  NZ    . LYS B 1 54  ? 156.771 144.347 163.770 1.00 59.58 1  54  LYS B NZ    1 
ATOM   5979  N  N     . LEU B 1 55  ? 160.124 150.095 161.056 1.00 55.55 ?  55  LEU B N     1 
ATOM   5980  C  CA    . LEU B 1 55  ? 159.296 150.949 160.214 1.00 56.17 ?  55  LEU B CA    1 
ATOM   5981  C  C     . LEU B 1 55  ? 160.013 151.312 158.923 1.00 59.21 ?  55  LEU B C     1 
ATOM   5982  O  O     . LEU B 1 55  ? 159.404 151.310 157.848 1.00 63.12 ?  55  LEU B O     1 
ATOM   5983  C  CB    . LEU B 1 55  ? 158.894 152.209 160.979 1.00 57.73 ?  55  LEU B CB    1 
ATOM   5984  C  CG    . LEU B 1 55  ? 157.837 152.013 162.066 1.00 57.81 ?  55  LEU B CG    1 
ATOM   5985  C  CD1   . LEU B 1 55  ? 157.648 153.295 162.852 1.00 58.16 ?  55  LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B 1 55  ? 156.521 151.551 161.459 1.00 57.18 ?  55  LEU B CD2   1 
ATOM   5987  N  N     . ASP B 1 56  ? 161.310 151.628 159.010 1.00 60.82 ?  56  ASP B N     1 
ATOM   5988  C  CA    . ASP B 1 56  ? 162.080 151.955 157.815 1.00 60.69 ?  56  ASP B CA    1 
ATOM   5989  C  C     . ASP B 1 56  ? 162.161 150.765 156.870 1.00 59.63 ?  56  ASP B C     1 
ATOM   5990  O  O     . ASP B 1 56  ? 162.003 150.917 155.651 1.00 62.40 ?  56  ASP B O     1 
ATOM   5991  C  CB    . ASP B 1 56  ? 163.479 152.427 158.207 1.00 62.18 ?  56  ASP B CB    1 
ATOM   5992  C  CG    . ASP B 1 56  ? 163.551 153.925 158.415 1.00 64.79 ?  56  ASP B CG    1 
ATOM   5993  O  OD1   . ASP B 1 56  ? 164.485 154.386 159.104 1.00 65.13 ?  56  ASP B OD1   1 
ATOM   5994  O  OD2   . ASP B 1 56  ? 162.674 154.642 157.889 1.00 63.28 -1 56  ASP B OD2   1 
ATOM   5995  N  N     . TYR B 1 57  ? 162.398 149.568 157.414 1.00 55.20 ?  57  TYR B N     1 
ATOM   5996  C  CA    . TYR B 1 57  ? 162.425 148.367 156.587 1.00 56.47 ?  57  TYR B CA    1 
ATOM   5997  C  C     . TYR B 1 57  ? 161.082 148.140 155.908 1.00 57.12 ?  57  TYR B C     1 
ATOM   5998  O  O     . TYR B 1 57  ? 161.029 147.757 154.736 1.00 58.36 ?  57  TYR B O     1 
ATOM   5999  C  CB    . TYR B 1 57  ? 162.807 147.154 157.437 1.00 57.82 ?  57  TYR B CB    1 
ATOM   6000  C  CG    . TYR B 1 57  ? 162.688 145.828 156.716 1.00 57.26 ?  57  TYR B CG    1 
ATOM   6001  C  CD1   . TYR B 1 57  ? 163.724 145.349 155.927 1.00 57.59 ?  57  TYR B CD1   1 
ATOM   6002  C  CD2   . TYR B 1 57  ? 161.542 145.051 156.834 1.00 58.80 ?  57  TYR B CD2   1 
ATOM   6003  C  CE1   . TYR B 1 57  ? 163.619 144.139 155.269 1.00 57.28 ?  57  TYR B CE1   1 
ATOM   6004  C  CE2   . TYR B 1 57  ? 161.429 143.843 156.181 1.00 59.93 ?  57  TYR B CE2   1 
ATOM   6005  C  CZ    . TYR B 1 57  ? 162.470 143.390 155.400 1.00 60.41 ?  57  TYR B CZ    1 
ATOM   6006  O  OH    . TYR B 1 57  ? 162.359 142.184 154.748 1.00 60.67 ?  57  TYR B OH    1 
ATOM   6007  N  N     . LEU B 1 58  ? 159.986 148.372 156.630 1.00 55.53 ?  58  LEU B N     1 
ATOM   6008  C  CA    . LEU B 1 58  ? 158.671 148.101 156.062 1.00 55.09 ?  58  LEU B CA    1 
ATOM   6009  C  C     . LEU B 1 58  ? 158.304 149.115 154.984 1.00 52.51 ?  58  LEU B C     1 
ATOM   6010  O  O     . LEU B 1 58  ? 157.727 148.745 153.956 1.00 54.87 ?  58  LEU B O     1 
ATOM   6011  C  CB    . LEU B 1 58  ? 157.621 148.065 157.172 1.00 53.67 ?  58  LEU B CB    1 
ATOM   6012  C  CG    . LEU B 1 58  ? 157.750 146.833 158.074 1.00 53.10 ?  58  LEU B CG    1 
ATOM   6013  C  CD1   . LEU B 1 58  ? 156.923 146.973 159.338 1.00 53.31 ?  58  LEU B CD1   1 
ATOM   6014  C  CD2   . LEU B 1 58  ? 157.368 145.573 157.318 1.00 51.72 ?  58  LEU B CD2   1 
ATOM   6015  N  N     . VAL B 1 59  ? 158.623 150.396 155.188 1.00 55.94 ?  59  VAL B N     1 
ATOM   6016  C  CA    . VAL B 1 59  ? 158.272 151.381 154.166 1.00 59.41 ?  59  VAL B CA    1 
ATOM   6017  C  C     . VAL B 1 59  ? 159.174 151.233 152.945 1.00 61.68 ?  59  VAL B C     1 
ATOM   6018  O  O     . VAL B 1 59  ? 158.708 151.311 151.803 1.00 58.99 ?  59  VAL B O     1 
ATOM   6019  C  CB    . VAL B 1 59  ? 158.317 152.819 154.721 1.00 58.77 ?  59  VAL B CB    1 
ATOM   6020  C  CG1   . VAL B 1 59  ? 157.083 153.108 155.570 1.00 57.57 ?  59  VAL B CG1   1 
ATOM   6021  C  CG2   . VAL B 1 59  ? 159.612 153.106 155.458 1.00 59.07 ?  59  VAL B CG2   1 
ATOM   6022  N  N     . GLU B 1 60  ? 160.476 151.016 153.161 1.00 62.25 ?  60  GLU B N     1 
ATOM   6023  C  CA    . GLU B 1 60  ? 161.412 150.994 152.042 1.00 60.57 ?  60  GLU B CA    1 
ATOM   6024  C  C     . GLU B 1 60  ? 161.325 149.706 151.232 1.00 61.73 ?  60  GLU B C     1 
ATOM   6025  O  O     . GLU B 1 60  ? 161.657 149.709 150.042 1.00 64.04 ?  60  GLU B O     1 
ATOM   6026  C  CB    . GLU B 1 60  ? 162.840 151.219 152.547 1.00 60.61 ?  60  GLU B CB    1 
ATOM   6027  C  CG    . GLU B 1 60  ? 163.578 149.964 152.973 1.00 61.74 ?  60  GLU B CG    1 
ATOM   6028  C  CD    . GLU B 1 60  ? 164.799 150.266 153.821 1.00 64.83 ?  60  GLU B CD    1 
ATOM   6029  O  OE1   . GLU B 1 60  ? 165.077 151.461 154.060 1.00 64.26 ?  60  GLU B OE1   1 
ATOM   6030  O  OE2   . GLU B 1 60  ? 165.478 149.311 154.250 1.00 61.61 -1 60  GLU B OE2   1 
ATOM   6031  N  N     . ASN B 1 61  ? 160.886 148.604 151.841 1.00 57.46 ?  61  ASN B N     1 
ATOM   6032  C  CA    . ASN B 1 61  ? 160.733 147.339 151.137 1.00 57.98 ?  61  ASN B CA    1 
ATOM   6033  C  C     . ASN B 1 61  ? 159.334 147.150 150.564 1.00 57.86 ?  61  ASN B C     1 
ATOM   6034  O  O     . ASN B 1 61  ? 158.931 146.010 150.305 1.00 59.49 ?  61  ASN B O     1 
ATOM   6035  C  CB    . ASN B 1 61  ? 161.084 146.168 152.058 1.00 59.20 ?  61  ASN B CB    1 
ATOM   6036  C  CG    . ASN B 1 61  ? 162.577 145.954 152.181 1.00 61.20 ?  61  ASN B CG    1 
ATOM   6037  O  OD1   . ASN B 1 61  ? 163.156 145.120 151.486 1.00 60.39 ?  61  ASN B OD1   1 
ATOM   6038  N  ND2   . ASN B 1 61  ? 163.210 146.708 153.070 1.00 60.53 ?  61  ASN B ND2   1 
ATOM   6039  N  N     . GLN B 1 62  ? 158.590 148.240 150.372 1.00 56.47 ?  62  GLN B N     1 
ATOM   6040  C  CA    . GLN B 1 62  ? 157.275 148.210 149.728 1.00 58.76 ?  62  GLN B CA    1 
ATOM   6041  C  C     . GLN B 1 62  ? 156.281 147.347 150.501 1.00 57.86 ?  62  GLN B C     1 
ATOM   6042  O  O     . GLN B 1 62  ? 155.510 146.583 149.918 1.00 59.50 ?  62  GLN B O     1 
ATOM   6043  C  CB    . GLN B 1 62  ? 157.384 147.744 148.273 1.00 58.26 ?  62  GLN B CB    1 
ATOM   6044  C  CG    . GLN B 1 62  ? 158.342 148.567 147.427 1.00 58.23 ?  62  GLN B CG    1 
ATOM   6045  C  CD    . GLN B 1 62  ? 157.993 150.041 147.419 1.00 61.67 ?  62  GLN B CD    1 
ATOM   6046  O  OE1   . GLN B 1 62  ? 158.562 150.832 148.169 1.00 60.56 ?  62  GLN B OE1   1 
ATOM   6047  N  NE2   . GLN B 1 62  ? 157.048 150.419 146.566 1.00 59.67 ?  62  GLN B NE2   1 
ATOM   6048  N  N     . TYR B 1 63  ? 156.296 147.469 151.827 1.00 56.30 ?  63  TYR B N     1 
ATOM   6049  C  CA    . TYR B 1 63  ? 155.317 146.804 152.677 1.00 55.71 ?  63  TYR B CA    1 
ATOM   6050  C  C     . TYR B 1 63  ? 154.259 147.758 153.210 1.00 54.98 ?  63  TYR B C     1 
ATOM   6051  O  O     . TYR B 1 63  ? 153.079 147.399 153.262 1.00 55.89 ?  63  TYR B O     1 
ATOM   6052  C  CB    . TYR B 1 63  ? 156.010 146.112 153.856 1.00 52.99 ?  63  TYR B CB    1 
ATOM   6053  C  CG    . TYR B 1 63  ? 156.746 144.848 153.484 1.00 55.76 ?  63  TYR B CG    1 
ATOM   6054  C  CD1   . TYR B 1 63  ? 156.087 143.795 152.864 1.00 53.23 ?  63  TYR B CD1   1 
ATOM   6055  C  CD2   . TYR B 1 63  ? 158.099 144.704 153.755 1.00 55.99 ?  63  TYR B CD2   1 
ATOM   6056  C  CE1   . TYR B 1 63  ? 156.755 142.638 152.525 1.00 54.08 ?  63  TYR B CE1   1 
ATOM   6057  C  CE2   . TYR B 1 63  ? 158.775 143.551 153.420 1.00 55.25 ?  63  TYR B CE2   1 
ATOM   6058  C  CZ    . TYR B 1 63  ? 158.099 142.521 152.805 1.00 58.33 ?  63  TYR B CZ    1 
ATOM   6059  O  OH    . TYR B 1 63  ? 158.772 141.370 152.469 1.00 61.61 ?  63  TYR B OH    1 
ATOM   6060  N  N     . TYR B 1 64  ? 154.654 148.962 153.603 1.00 51.12 ?  64  TYR B N     1 
ATOM   6061  C  CA    . TYR B 1 64  ? 153.747 149.973 154.124 1.00 49.36 ?  64  TYR B CA    1 
ATOM   6062  C  C     . TYR B 1 64  ? 153.630 151.131 153.144 1.00 51.84 ?  64  TYR B C     1 
ATOM   6063  O  O     . TYR B 1 64  ? 154.316 151.189 152.119 1.00 56.22 ?  64  TYR B O     1 
ATOM   6064  C  CB    . TYR B 1 64  ? 154.229 150.491 155.483 1.00 51.22 ?  64  TYR B CB    1 
ATOM   6065  C  CG    . TYR B 1 64  ? 153.955 149.564 156.638 1.00 49.14 ?  64  TYR B CG    1 
ATOM   6066  C  CD1   . TYR B 1 64  ? 153.221 148.400 156.463 1.00 47.95 ?  64  TYR B CD1   1 
ATOM   6067  C  CD2   . TYR B 1 64  ? 154.429 149.855 157.907 1.00 50.77 ?  64  TYR B CD2   1 
ATOM   6068  C  CE1   . TYR B 1 64  ? 152.970 147.550 157.519 1.00 45.37 ?  64  TYR B CE1   1 
ATOM   6069  C  CE2   . TYR B 1 64  ? 154.183 149.015 158.967 1.00 50.87 ?  64  TYR B CE2   1 
ATOM   6070  C  CZ    . TYR B 1 64  ? 153.454 147.863 158.769 1.00 50.19 ?  64  TYR B CZ    1 
ATOM   6071  O  OH    . TYR B 1 64  ? 153.212 147.026 159.830 1.00 55.95 ?  64  TYR B OH    1 
ATOM   6072  N  N     . GLU B 1 65  ? 152.747 152.064 153.478 1.00 56.36 ?  65  GLU B N     1 
ATOM   6073  C  CA    . GLU B 1 65  ? 152.598 153.307 152.738 1.00 57.07 ?  65  GLU B CA    1 
ATOM   6074  C  C     . GLU B 1 65  ? 153.250 154.435 153.528 1.00 58.36 ?  65  GLU B C     1 
ATOM   6075  O  O     . GLU B 1 65  ? 152.943 154.630 154.708 1.00 59.05 ?  65  GLU B O     1 
ATOM   6076  C  CB    . GLU B 1 65  ? 151.123 153.624 152.483 1.00 54.02 ?  65  GLU B CB    1 
ATOM   6077  C  CG    . GLU B 1 65  ? 150.421 152.637 151.568 1.00 52.75 ?  65  GLU B CG    1 
ATOM   6078  C  CD    . GLU B 1 65  ? 148.921 152.856 151.521 1.00 59.36 ?  65  GLU B CD    1 
ATOM   6079  O  OE1   . GLU B 1 65  ? 148.304 152.995 152.597 1.00 59.54 ?  65  GLU B OE1   1 
ATOM   6080  O  OE2   . GLU B 1 65  ? 148.358 152.890 150.406 1.00 56.85 -1 65  GLU B OE2   1 
ATOM   6081  N  N     . GLU B 1 66  ? 154.154 155.167 152.877 1.00 58.13 ?  66  GLU B N     1 
ATOM   6082  C  CA    . GLU B 1 66  ? 154.823 156.274 153.546 1.00 59.42 ?  66  GLU B CA    1 
ATOM   6083  C  C     . GLU B 1 66  ? 153.894 157.460 153.769 1.00 60.55 ?  66  GLU B C     1 
ATOM   6084  O  O     . GLU B 1 66  ? 154.180 158.302 154.627 1.00 58.82 ?  66  GLU B O     1 
ATOM   6085  C  CB    . GLU B 1 66  ? 156.048 156.710 152.736 1.00 61.14 ?  66  GLU B CB    1 
ATOM   6086  C  CG    . GLU B 1 66  ? 157.043 157.608 153.476 1.00 61.57 ?  66  GLU B CG    1 
ATOM   6087  C  CD    . GLU B 1 66  ? 157.367 157.128 154.882 1.00 65.09 ?  66  GLU B CD    1 
ATOM   6088  O  OE1   . GLU B 1 66  ? 156.595 157.424 155.818 1.00 63.13 ?  66  GLU B OE1   1 
ATOM   6089  O  OE2   . GLU B 1 66  ? 158.404 156.452 155.052 1.00 62.81 -1 66  GLU B OE2   1 
ATOM   6090  N  N     . GLU B 1 67  ? 152.788 157.541 153.026 1.00 58.11 ?  67  GLU B N     1 
ATOM   6091  C  CA    . GLU B 1 67  ? 151.916 158.707 153.110 1.00 55.39 ?  67  GLU B CA    1 
ATOM   6092  C  C     . GLU B 1 67  ? 151.267 158.826 154.484 1.00 59.38 ?  67  GLU B C     1 
ATOM   6093  O  O     . GLU B 1 67  ? 151.308 159.894 155.108 1.00 60.34 ?  67  GLU B O     1 
ATOM   6094  C  CB    . GLU B 1 67  ? 150.848 158.640 152.018 1.00 57.45 ?  67  GLU B CB    1 
ATOM   6095  C  CG    . GLU B 1 67  ? 151.407 158.584 150.607 1.00 58.19 ?  67  GLU B CG    1 
ATOM   6096  C  CD    . GLU B 1 67  ? 151.484 157.170 150.068 1.00 61.21 ?  67  GLU B CD    1 
ATOM   6097  O  OE1   . GLU B 1 67  ? 150.420 156.584 149.779 1.00 62.20 ?  67  GLU B OE1   1 
ATOM   6098  O  OE2   . GLU B 1 67  ? 152.609 156.646 149.931 1.00 62.48 -1 67  GLU B OE2   1 
ATOM   6099  N  N     . PHE B 1 68  ? 150.662 157.744 154.974 1.00 53.85 ?  68  PHE B N     1 
ATOM   6100  C  CA    . PHE B 1 68  ? 149.957 157.816 156.248 1.00 49.12 ?  68  PHE B CA    1 
ATOM   6101  C  C     . PHE B 1 68  ? 150.912 157.836 157.434 1.00 50.48 ?  68  PHE B C     1 
ATOM   6102  O  O     . PHE B 1 68  ? 150.594 158.434 158.467 1.00 54.75 ?  68  PHE B O     1 
ATOM   6103  C  CB    . PHE B 1 68  ? 148.959 156.657 156.370 1.00 49.06 ?  68  PHE B CB    1 
ATOM   6104  C  CG    . PHE B 1 68  ? 149.539 155.398 156.954 1.00 45.75 ?  68  PHE B CG    1 
ATOM   6105  C  CD1   . PHE B 1 68  ? 150.194 154.485 156.149 1.00 48.64 ?  68  PHE B CD1   1 
ATOM   6106  C  CD2   . PHE B 1 68  ? 149.399 155.112 158.304 1.00 45.10 ?  68  PHE B CD2   1 
ATOM   6107  C  CE1   . PHE B 1 68  ? 150.722 153.325 156.679 1.00 48.69 ?  68  PHE B CE1   1 
ATOM   6108  C  CE2   . PHE B 1 68  ? 149.925 153.952 158.838 1.00 47.79 ?  68  PHE B CE2   1 
ATOM   6109  C  CZ    . PHE B 1 68  ? 150.583 153.057 158.024 1.00 48.99 ?  68  PHE B CZ    1 
ATOM   6110  N  N     . LEU B 1 69  ? 152.078 157.198 157.312 1.00 48.84 ?  69  LEU B N     1 
ATOM   6111  C  CA    . LEU B 1 69  ? 153.043 157.217 158.405 1.00 50.00 ?  69  LEU B CA    1 
ATOM   6112  C  C     . LEU B 1 69  ? 153.752 158.559 158.518 1.00 53.07 ?  69  LEU B C     1 
ATOM   6113  O  O     . LEU B 1 69  ? 154.184 158.935 159.614 1.00 50.57 ?  69  LEU B O     1 
ATOM   6114  C  CB    . LEU B 1 69  ? 154.067 156.096 158.227 1.00 50.19 ?  69  LEU B CB    1 
ATOM   6115  C  CG    . LEU B 1 69  ? 153.618 154.716 158.708 1.00 49.96 ?  69  LEU B CG    1 
ATOM   6116  C  CD1   . LEU B 1 69  ? 154.624 153.650 158.312 1.00 50.10 ?  69  LEU B CD1   1 
ATOM   6117  C  CD2   . LEU B 1 69  ? 153.397 154.721 160.211 1.00 50.65 ?  69  LEU B CD2   1 
ATOM   6118  N  N     . SER B 1 70  ? 153.879 159.293 157.411 1.00 57.68 ?  70  SER B N     1 
ATOM   6119  C  CA    . SER B 1 70  ? 154.511 160.607 157.453 1.00 54.92 ?  70  SER B CA    1 
ATOM   6120  C  C     . SER B 1 70  ? 153.664 161.631 158.193 1.00 51.98 ?  70  SER B C     1 
ATOM   6121  O  O     . SER B 1 70  ? 154.174 162.701 158.542 1.00 53.93 ?  70  SER B O     1 
ATOM   6122  C  CB    . SER B 1 70  ? 154.798 161.103 156.037 1.00 53.34 ?  70  SER B CB    1 
ATOM   6123  O  OG    . SER B 1 70  ? 153.631 161.054 155.237 1.00 54.26 ?  70  SER B OG    1 
ATOM   6124  N  N     . LEU B 1 71  ? 152.387 161.333 158.433 1.00 46.56 ?  71  LEU B N     1 
ATOM   6125  C  CA    . LEU B 1 71  ? 151.507 162.257 159.136 1.00 46.13 ?  71  LEU B CA    1 
ATOM   6126  C  C     . LEU B 1 71  ? 151.841 162.380 160.614 1.00 47.72 ?  71  LEU B C     1 
ATOM   6127  O  O     . LEU B 1 71  ? 151.322 163.286 161.275 1.00 50.28 ?  71  LEU B O     1 
ATOM   6128  C  CB    . LEU B 1 71  ? 150.053 161.815 158.970 1.00 46.23 ?  71  LEU B CB    1 
ATOM   6129  C  CG    . LEU B 1 71  ? 149.427 162.076 157.600 1.00 50.87 ?  71  LEU B CG    1 
ATOM   6130  C  CD1   . LEU B 1 71  ? 147.915 162.041 157.689 1.00 48.61 ?  71  LEU B CD1   1 
ATOM   6131  C  CD2   . LEU B 1 71  ? 149.900 163.406 157.036 1.00 49.17 ?  71  LEU B CD2   1 
ATOM   6132  N  N     . TYR B 1 72  ? 152.688 161.502 161.145 1.00 45.28 ?  72  TYR B N     1 
ATOM   6133  C  CA    . TYR B 1 72  ? 153.078 161.524 162.546 1.00 44.42 ?  72  TYR B CA    1 
ATOM   6134  C  C     . TYR B 1 72  ? 154.588 161.664 162.658 1.00 48.54 ?  72  TYR B C     1 
ATOM   6135  O  O     . TYR B 1 72  ? 155.333 161.135 161.827 1.00 50.77 ?  72  TYR B O     1 
ATOM   6136  C  CB    . TYR B 1 72  ? 152.648 160.245 163.275 1.00 46.60 ?  72  TYR B CB    1 
ATOM   6137  C  CG    . TYR B 1 72  ? 151.220 159.818 163.040 1.00 44.13 ?  72  TYR B CG    1 
ATOM   6138  C  CD1   . TYR B 1 72  ? 150.881 159.032 161.949 1.00 40.51 ?  72  TYR B CD1   1 
ATOM   6139  C  CD2   . TYR B 1 72  ? 150.213 160.180 163.924 1.00 45.33 ?  72  TYR B CD2   1 
ATOM   6140  C  CE1   . TYR B 1 72  ? 149.583 158.636 161.732 1.00 40.64 ?  72  TYR B CE1   1 
ATOM   6141  C  CE2   . TYR B 1 72  ? 148.910 159.784 163.717 1.00 41.64 ?  72  TYR B CE2   1 
ATOM   6142  C  CZ    . TYR B 1 72  ? 148.600 159.012 162.619 1.00 42.12 ?  72  TYR B CZ    1 
ATOM   6143  O  OH    . TYR B 1 72  ? 147.304 158.615 162.407 1.00 47.11 ?  72  TYR B OH    1 
ATOM   6144  N  N     . SER B 1 73  ? 155.034 162.377 163.685 1.00 54.10 ?  73  SER B N     1 
ATOM   6145  C  CA    . SER B 1 73  ? 156.421 162.265 164.100 1.00 54.69 ?  73  SER B CA    1 
ATOM   6146  C  C     . SER B 1 73  ? 156.669 160.863 164.641 1.00 54.99 ?  73  SER B C     1 
ATOM   6147  O  O     . SER B 1 73  ? 155.755 160.201 165.142 1.00 58.63 ?  73  SER B O     1 
ATOM   6148  C  CB    . SER B 1 73  ? 156.755 163.312 165.160 1.00 53.07 ?  73  SER B CB    1 
ATOM   6149  O  OG    . SER B 1 73  ? 156.120 163.011 166.389 1.00 51.89 ?  73  SER B OG    1 
ATOM   6150  N  N     . PHE B 1 74  ? 157.914 160.398 164.525 1.00 56.10 ?  74  PHE B N     1 
ATOM   6151  C  CA    . PHE B 1 74  ? 158.210 159.036 164.957 1.00 55.84 ?  74  PHE B CA    1 
ATOM   6152  C  C     . PHE B 1 74  ? 157.940 158.840 166.443 1.00 55.08 ?  74  PHE B C     1 
ATOM   6153  O  O     . PHE B 1 74  ? 157.660 157.719 166.877 1.00 60.39 ?  74  PHE B O     1 
ATOM   6154  C  CB    . PHE B 1 74  ? 159.656 158.660 164.643 1.00 56.32 ?  74  PHE B CB    1 
ATOM   6155  C  CG    . PHE B 1 74  ? 160.056 157.329 165.210 1.00 57.06 ?  74  PHE B CG    1 
ATOM   6156  C  CD1   . PHE B 1 74  ? 159.525 156.160 164.692 1.00 56.22 ?  74  PHE B CD1   1 
ATOM   6157  C  CD2   . PHE B 1 74  ? 160.929 157.247 166.280 1.00 57.99 ?  74  PHE B CD2   1 
ATOM   6158  C  CE1   . PHE B 1 74  ? 159.875 154.935 165.216 1.00 58.61 ?  74  PHE B CE1   1 
ATOM   6159  C  CE2   . PHE B 1 74  ? 161.283 156.024 166.808 1.00 57.74 ?  74  PHE B CE2   1 
ATOM   6160  C  CZ    . PHE B 1 74  ? 160.754 154.866 166.277 1.00 59.91 ?  74  PHE B CZ    1 
ATOM   6161  N  N     . GLU B 1 75  ? 158.016 159.910 167.237 1.00 54.53 ?  75  GLU B N     1 
ATOM   6162  C  CA    . GLU B 1 75  ? 157.688 159.792 168.653 1.00 58.15 ?  75  GLU B CA    1 
ATOM   6163  C  C     . GLU B 1 75  ? 156.228 159.399 168.845 1.00 60.11 ?  75  GLU B C     1 
ATOM   6164  O  O     . GLU B 1 75  ? 155.907 158.567 169.700 1.00 60.42 ?  75  GLU B O     1 
ATOM   6165  C  CB    . GLU B 1 75  ? 157.993 161.104 169.375 1.00 56.36 ?  75  GLU B CB    1 
ATOM   6166  C  CG    . GLU B 1 75  ? 159.473 161.432 169.451 1.00 56.59 ?  75  GLU B CG    1 
ATOM   6167  C  CD    . GLU B 1 75  ? 160.301 160.272 169.969 1.00 63.42 ?  75  GLU B CD    1 
ATOM   6168  O  OE1   . GLU B 1 75  ? 160.059 159.831 171.113 1.00 63.49 ?  75  GLU B OE1   1 
ATOM   6169  O  OE2   . GLU B 1 75  ? 161.191 159.798 169.233 1.00 62.13 -1 75  GLU B OE2   1 
ATOM   6170  N  N     . ASP B 1 76  ? 155.330 159.985 168.052 1.00 55.72 ?  76  ASP B N     1 
ATOM   6171  C  CA    . ASP B 1 76  ? 153.914 159.646 168.155 1.00 54.37 ?  76  ASP B CA    1 
ATOM   6172  C  C     . ASP B 1 76  ? 153.661 158.196 167.762 1.00 55.43 ?  76  ASP B C     1 
ATOM   6173  O  O     . ASP B 1 76  ? 152.879 157.495 168.415 1.00 58.92 ?  76  ASP B O     1 
ATOM   6174  C  CB    . ASP B 1 76  ? 153.089 160.592 167.285 1.00 55.73 ?  76  ASP B CB    1 
ATOM   6175  C  CG    . ASP B 1 76  ? 153.175 162.030 167.748 1.00 58.99 ?  76  ASP B CG    1 
ATOM   6176  O  OD1   . ASP B 1 76  ? 153.185 162.261 168.975 1.00 59.14 ?  76  ASP B OD1   1 
ATOM   6177  O  OD2   . ASP B 1 76  ? 153.226 162.932 166.887 1.00 58.03 -1 76  ASP B OD2   1 
ATOM   6178  N  N     . ILE B 1 77  ? 154.311 157.728 166.694 1.00 48.13 ?  77  ILE B N     1 
ATOM   6179  C  CA    . ILE B 1 77  ? 154.160 156.334 166.281 1.00 49.21 ?  77  ILE B CA    1 
ATOM   6180  C  C     . ILE B 1 77  ? 154.706 155.403 167.355 1.00 50.79 ?  77  ILE B C     1 
ATOM   6181  O  O     . ILE B 1 77  ? 154.129 154.345 167.638 1.00 54.21 ?  77  ILE B O     1 
ATOM   6182  C  CB    . ILE B 1 77  ? 154.849 156.104 164.925 1.00 49.26 ?  77  ILE B CB    1 
ATOM   6183  C  CG1   . ILE B 1 77  ? 154.219 156.991 163.852 1.00 49.08 ?  77  ILE B CG1   1 
ATOM   6184  C  CG2   . ILE B 1 77  ? 154.754 154.643 164.521 1.00 49.31 ?  77  ILE B CG2   1 
ATOM   6185  C  CD1   . ILE B 1 77  ? 155.033 157.081 162.588 1.00 50.74 ?  77  ILE B CD1   1 
ATOM   6186  N  N     . LYS B 1 78  ? 155.833 155.778 167.961 1.00 52.56 ?  78  LYS B N     1 
ATOM   6187  C  CA    . LYS B 1 78  ? 156.403 154.974 169.035 1.00 51.80 ?  78  LYS B CA    1 
ATOM   6188  C  C     . LYS B 1 78  ? 155.458 154.899 170.225 1.00 52.98 ?  78  LYS B C     1 
ATOM   6189  O  O     . LYS B 1 78  ? 155.299 153.836 170.831 1.00 56.49 ?  78  LYS B O     1 
ATOM   6190  C  CB    . LYS B 1 78  ? 157.756 155.547 169.454 1.00 55.18 ?  78  LYS B CB    1 
ATOM   6191  C  CG    . LYS B 1 78  ? 158.480 154.727 170.505 1.00 54.95 ?  78  LYS B CG    1 
ATOM   6192  C  CD    . LYS B 1 78  ? 159.913 154.448 170.089 1.00 55.76 ?  78  LYS B CD    1 
ATOM   6193  C  CE    . LYS B 1 78  ? 160.898 154.939 171.135 1.00 57.25 ?  78  LYS B CE    1 
ATOM   6194  N  NZ    . LYS B 1 78  ? 162.308 154.771 170.692 1.00 55.90 1  78  LYS B NZ    1 
ATOM   6195  N  N     . GLU B 1 79  ? 154.815 156.016 170.571 1.00 53.27 ?  79  GLU B N     1 
ATOM   6196  C  CA    . GLU B 1 79  ? 153.856 155.993 171.672 1.00 52.11 ?  79  GLU B CA    1 
ATOM   6197  C  C     . GLU B 1 79  ? 152.615 155.180 171.325 1.00 51.11 ?  79  GLU B C     1 
ATOM   6198  O  O     . GLU B 1 79  ? 152.042 154.525 172.202 1.00 52.30 ?  79  GLU B O     1 
ATOM   6199  C  CB    . GLU B 1 79  ? 153.470 157.419 172.070 1.00 52.64 ?  79  GLU B CB    1 
ATOM   6200  C  CG    . GLU B 1 79  ? 154.625 158.286 172.575 1.00 56.29 ?  79  GLU B CG    1 
ATOM   6201  C  CD    . GLU B 1 79  ? 155.677 157.519 173.369 1.00 58.47 ?  79  GLU B CD    1 
ATOM   6202  O  OE1   . GLU B 1 79  ? 156.880 157.803 173.179 1.00 56.16 ?  79  GLU B OE1   1 
ATOM   6203  O  OE2   . GLU B 1 79  ? 155.315 156.674 174.216 1.00 57.13 -1 79  GLU B OE2   1 
ATOM   6204  N  N     . VAL B 1 80  ? 152.188 155.203 170.062 1.00 48.64 ?  80  VAL B N     1 
ATOM   6205  C  CA    . VAL B 1 80  ? 151.063 154.370 169.644 1.00 45.07 ?  80  VAL B CA    1 
ATOM   6206  C  C     . VAL B 1 80  ? 151.413 152.891 169.783 1.00 48.97 ?  80  VAL B C     1 
ATOM   6207  O  O     . VAL B 1 80  ? 150.622 152.092 170.306 1.00 51.77 ?  80  VAL B O     1 
ATOM   6208  C  CB    . VAL B 1 80  ? 150.649 154.730 168.204 1.00 44.98 ?  80  VAL B CB    1 
ATOM   6209  C  CG1   . VAL B 1 80  ? 149.748 153.665 167.617 1.00 46.55 ?  80  VAL B CG1   1 
ATOM   6210  C  CG2   . VAL B 1 80  ? 149.955 156.082 168.181 1.00 45.90 ?  80  VAL B CG2   1 
ATOM   6211  N  N     . PHE B 1 81  ? 152.610 152.508 169.334 1.00 47.44 ?  81  PHE B N     1 
ATOM   6212  C  CA    . PHE B 1 81  ? 153.054 151.126 169.494 1.00 44.10 ?  81  PHE B CA    1 
ATOM   6213  C  C     . PHE B 1 81  ? 153.205 150.764 170.968 1.00 45.61 ?  81  PHE B C     1 
ATOM   6214  O  O     . PHE B 1 81  ? 152.930 149.626 171.366 1.00 51.04 ?  81  PHE B O     1 
ATOM   6215  C  CB    . PHE B 1 81  ? 154.367 150.905 168.746 1.00 43.36 ?  81  PHE B CB    1 
ATOM   6216  C  CG    . PHE B 1 81  ? 154.187 150.506 167.310 1.00 43.48 ?  81  PHE B CG    1 
ATOM   6217  C  CD1   . PHE B 1 81  ? 153.876 151.450 166.346 1.00 44.24 ?  81  PHE B CD1   1 
ATOM   6218  C  CD2   . PHE B 1 81  ? 154.332 149.186 166.923 1.00 43.71 ?  81  PHE B CD2   1 
ATOM   6219  C  CE1   . PHE B 1 81  ? 153.711 151.083 165.025 1.00 44.16 ?  81  PHE B CE1   1 
ATOM   6220  C  CE2   . PHE B 1 81  ? 154.168 148.814 165.604 1.00 45.21 ?  81  PHE B CE2   1 
ATOM   6221  C  CZ    . PHE B 1 81  ? 153.857 149.765 164.654 1.00 43.39 ?  81  PHE B CZ    1 
ATOM   6222  N  N     . LYS B 1 82  ? 153.646 151.716 171.789 1.00 47.11 ?  82  LYS B N     1 
ATOM   6223  C  CA    . LYS B 1 82  ? 153.708 151.499 173.231 1.00 51.39 ?  82  LYS B CA    1 
ATOM   6224  C  C     . LYS B 1 82  ? 152.325 151.208 173.794 1.00 51.71 ?  82  LYS B C     1 
ATOM   6225  O  O     . LYS B 1 82  ? 152.152 150.308 174.622 1.00 51.17 ?  82  LYS B O     1 
ATOM   6226  C  CB    . LYS B 1 82  ? 154.308 152.726 173.917 1.00 53.58 ?  82  LYS B CB    1 
ATOM   6227  C  CG    . LYS B 1 82  ? 155.634 152.497 174.617 1.00 53.04 ?  82  LYS B CG    1 
ATOM   6228  C  CD    . LYS B 1 82  ? 156.787 152.433 173.637 1.00 54.24 ?  82  LYS B CD    1 
ATOM   6229  C  CE    . LYS B 1 82  ? 158.113 152.567 174.367 1.00 55.14 ?  82  LYS B CE    1 
ATOM   6230  N  NZ    . LYS B 1 82  ? 159.159 151.666 173.817 1.00 56.03 1  82  LYS B NZ    1 
ATOM   6231  N  N     . THR B 1 83  ? 151.326 151.974 173.353 1.00 47.16 ?  83  THR B N     1 
ATOM   6232  C  CA    . THR B 1 83  ? 149.958 151.754 173.807 1.00 45.62 ?  83  THR B CA    1 
ATOM   6233  C  C     . THR B 1 83  ? 149.457 150.377 173.391 1.00 47.50 ?  83  THR B C     1 
ATOM   6234  O  O     . THR B 1 83  ? 148.761 149.703 174.160 1.00 51.83 ?  83  THR B O     1 
ATOM   6235  C  CB    . THR B 1 83  ? 149.042 152.847 173.260 1.00 45.08 ?  83  THR B CB    1 
ATOM   6236  O  OG1   . THR B 1 83  ? 149.600 154.131 173.566 1.00 51.98 ?  83  THR B OG1   1 
ATOM   6237  C  CG2   . THR B 1 83  ? 147.663 152.748 173.882 1.00 47.96 ?  83  THR B CG2   1 
ATOM   6238  N  N     . ALA B 1 84  ? 149.796 149.944 172.174 1.00 41.73 ?  84  ALA B N     1 
ATOM   6239  C  CA    . ALA B 1 84  ? 149.385 148.612 171.739 1.00 38.19 ?  84  ALA B CA    1 
ATOM   6240  C  C     . ALA B 1 84  ? 150.031 147.521 172.585 1.00 41.93 ?  84  ALA B C     1 
ATOM   6241  O  O     . ALA B 1 84  ? 149.364 146.553 172.971 1.00 50.02 ?  84  ALA B O     1 
ATOM   6242  C  CB    . ALA B 1 84  ? 149.723 148.412 170.266 1.00 41.37 ?  84  ALA B CB    1 
ATOM   6243  N  N     . TYR B 1 85  ? 151.324 147.653 172.880 1.00 48.73 ?  85  TYR B N     1 
ATOM   6244  C  CA    . TYR B 1 85  ? 152.021 146.639 173.660 1.00 44.08 ?  85  TYR B CA    1 
ATOM   6245  C  C     . TYR B 1 85  ? 151.821 146.802 175.159 1.00 45.71 ?  85  TYR B C     1 
ATOM   6246  O  O     . TYR B 1 85  ? 152.152 145.883 175.916 1.00 48.79 ?  85  TYR B O     1 
ATOM   6247  C  CB    . TYR B 1 85  ? 153.517 146.656 173.333 1.00 45.03 ?  85  TYR B CB    1 
ATOM   6248  C  CG    . TYR B 1 85  ? 153.862 146.024 172.004 1.00 45.73 ?  85  TYR B CG    1 
ATOM   6249  C  CD1   . TYR B 1 85  ? 153.838 146.767 170.833 1.00 45.47 ?  85  TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B 1 85  ? 154.213 144.685 171.923 1.00 45.37 ?  85  TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B 1 85  ? 154.153 146.194 169.619 1.00 45.26 ?  85  TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B 1 85  ? 154.529 144.104 170.713 1.00 45.88 ?  85  TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B 1 85  ? 154.497 144.862 169.565 1.00 47.44 ?  85  TYR B CZ    1 
ATOM   6254  O  OH    . TYR B 1 85  ? 154.812 144.287 168.358 1.00 49.52 ?  85  TYR B OH    1 
ATOM   6255  N  N     . ALA B 1 86  ? 151.293 147.942 175.608 1.00 48.77 ?  86  ALA B N     1 
ATOM   6256  C  CA    . ALA B 1 86  ? 151.032 148.124 177.031 1.00 49.11 ?  86  ALA B CA    1 
ATOM   6257  C  C     . ALA B 1 86  ? 149.921 147.214 177.534 1.00 51.18 ?  86  ALA B C     1 
ATOM   6258  O  O     . ALA B 1 86  ? 149.880 146.911 178.731 1.00 50.07 ?  86  ALA B O     1 
ATOM   6259  C  CB    . ALA B 1 86  ? 150.675 149.581 177.327 1.00 45.01 ?  86  ALA B CB    1 
ATOM   6260  N  N     . LYS B 1 87  ? 149.022 146.777 176.653 1.00 43.59 ?  87  LYS B N     1 
ATOM   6261  C  CA    . LYS B 1 87  ? 147.932 145.901 177.058 1.00 43.37 ?  87  LYS B CA    1 
ATOM   6262  C  C     . LYS B 1 87  ? 148.389 144.473 177.319 1.00 46.64 ?  87  LYS B C     1 
ATOM   6263  O  O     . LYS B 1 87  ? 147.697 143.741 178.034 1.00 46.53 ?  87  LYS B O     1 
ATOM   6264  C  CB    . LYS B 1 87  ? 146.834 145.898 175.993 1.00 46.41 ?  87  LYS B CB    1 
ATOM   6265  C  CG    . LYS B 1 87  ? 145.439 145.668 176.543 1.00 47.31 ?  87  LYS B CG    1 
ATOM   6266  C  CD    . LYS B 1 87  ? 144.760 144.499 175.851 1.00 43.91 ?  87  LYS B CD    1 
ATOM   6267  C  CE    . LYS B 1 87  ? 143.495 144.085 176.582 1.00 43.53 ?  87  LYS B CE    1 
ATOM   6268  N  NZ    . LYS B 1 87  ? 142.784 142.980 175.883 1.00 41.20 1  87  LYS B NZ    1 
ATOM   6269  N  N     . LYS B 1 88  ? 149.534 144.069 176.766 1.00 51.97 ?  88  LYS B N     1 
ATOM   6270  C  CA    . LYS B 1 88  ? 150.033 142.698 176.876 1.00 47.74 ?  88  LYS B CA    1 
ATOM   6271  C  C     . LYS B 1 88  ? 148.965 141.700 176.437 1.00 46.69 ?  88  LYS B C     1 
ATOM   6272  O  O     . LYS B 1 88  ? 148.649 140.737 177.139 1.00 49.88 ?  88  LYS B O     1 
ATOM   6273  C  CB    . LYS B 1 88  ? 150.519 142.399 178.295 1.00 48.98 ?  88  LYS B CB    1 
ATOM   6274  C  CG    . LYS B 1 88  ? 151.367 143.502 178.908 1.00 47.10 ?  88  LYS B CG    1 
ATOM   6275  C  CD    . LYS B 1 88  ? 152.694 142.964 179.412 1.00 50.61 ?  88  LYS B CD    1 
ATOM   6276  C  CE    . LYS B 1 88  ? 152.508 142.124 180.664 1.00 52.66 ?  88  LYS B CE    1 
ATOM   6277  N  NZ    . LYS B 1 88  ? 153.693 141.262 180.936 1.00 51.45 1  88  LYS B NZ    1 
ATOM   6278  N  N     . PHE B 1 89  ? 148.396 141.950 175.260 1.00 45.43 ?  89  PHE B N     1 
ATOM   6279  C  CA    . PHE B 1 89  ? 147.293 141.134 174.772 1.00 40.04 ?  89  PHE B CA    1 
ATOM   6280  C  C     . PHE B 1 89  ? 147.749 139.703 174.527 1.00 42.32 ?  89  PHE B C     1 
ATOM   6281  O  O     . PHE B 1 89  ? 148.801 139.464 173.928 1.00 43.62 ?  89  PHE B O     1 
ATOM   6282  C  CB    . PHE B 1 89  ? 146.720 141.728 173.485 1.00 39.99 ?  89  PHE B CB    1 
ATOM   6283  C  CG    . PHE B 1 89  ? 145.697 140.853 172.823 1.00 38.98 ?  89  PHE B CG    1 
ATOM   6284  C  CD1   . PHE B 1 89  ? 144.391 140.833 173.277 1.00 37.21 ?  89  PHE B CD1   1 
ATOM   6285  C  CD2   . PHE B 1 89  ? 146.041 140.043 171.756 1.00 39.03 ?  89  PHE B CD2   1 
ATOM   6286  C  CE1   . PHE B 1 89  ? 143.449 140.028 172.678 1.00 39.04 ?  89  PHE B CE1   1 
ATOM   6287  C  CE2   . PHE B 1 89  ? 145.101 139.235 171.152 1.00 35.00 ?  89  PHE B CE2   1 
ATOM   6288  C  CZ    . PHE B 1 89  ? 143.804 139.227 171.613 1.00 38.35 ?  89  PHE B CZ    1 
ATOM   6289  N  N     . ARG B 1 90  ? 146.946 138.751 174.988 1.00 43.49 ?  90  ARG B N     1 
ATOM   6290  C  CA    . ARG B 1 90  ? 147.207 137.334 174.794 1.00 43.41 ?  90  ARG B CA    1 
ATOM   6291  C  C     . ARG B 1 90  ? 146.030 136.707 174.064 1.00 43.90 ?  90  ARG B C     1 
ATOM   6292  O  O     . ARG B 1 90  ? 144.876 136.917 174.449 1.00 47.64 ?  90  ARG B O     1 
ATOM   6293  C  CB    . ARG B 1 90  ? 147.438 136.625 176.131 1.00 46.45 ?  90  ARG B CB    1 
ATOM   6294  C  CG    . ARG B 1 90  ? 148.609 137.169 176.924 1.00 46.45 ?  90  ARG B CG    1 
ATOM   6295  C  CD    . ARG B 1 90  ? 149.904 136.488 176.525 1.00 48.43 ?  90  ARG B CD    1 
ATOM   6296  N  NE    . ARG B 1 90  ? 150.718 137.337 175.665 1.00 51.01 ?  90  ARG B NE    1 
ATOM   6297  C  CZ    . ARG B 1 90  ? 151.464 138.345 176.094 1.00 49.77 ?  90  ARG B CZ    1 
ATOM   6298  N  NH1   . ARG B 1 90  ? 151.542 138.650 177.379 1.00 47.15 1  90  ARG B NH1   1 
ATOM   6299  N  NH2   . ARG B 1 90  ? 152.152 139.064 175.213 1.00 51.52 ?  90  ARG B NH2   1 
ATOM   6300  N  N     . PHE B 1 91  ? 146.323 135.955 173.016 1.00 36.62 ?  91  PHE B N     1 
ATOM   6301  C  CA    . PHE B 1 91  ? 145.283 135.199 172.338 1.00 39.12 ?  91  PHE B CA    1 
ATOM   6302  C  C     . PHE B 1 91  ? 144.788 134.092 173.262 1.00 44.74 ?  91  PHE B C     1 
ATOM   6303  O  O     . PHE B 1 91  ? 145.594 133.290 173.746 1.00 45.97 ?  91  PHE B O     1 
ATOM   6304  C  CB    . PHE B 1 91  ? 145.812 134.609 171.035 1.00 39.16 ?  91  PHE B CB    1 
ATOM   6305  C  CG    . PHE B 1 91  ? 145.953 135.613 169.927 1.00 40.47 ?  91  PHE B CG    1 
ATOM   6306  C  CD1   . PHE B 1 91  ? 144.838 136.092 169.261 1.00 43.58 ?  91  PHE B CD1   1 
ATOM   6307  C  CD2   . PHE B 1 91  ? 147.200 136.076 169.551 1.00 42.01 ?  91  PHE B CD2   1 
ATOM   6308  C  CE1   . PHE B 1 91  ? 144.966 137.011 168.241 1.00 40.28 ?  91  PHE B CE1   1 
ATOM   6309  C  CE2   . PHE B 1 91  ? 147.333 136.995 168.532 1.00 40.89 ?  91  PHE B CE2   1 
ATOM   6310  C  CZ    . PHE B 1 91  ? 146.215 137.463 167.876 1.00 36.90 ?  91  PHE B CZ    1 
ATOM   6311  N  N     . PRO B 1 92  ? 143.484 134.016 173.538 1.00 44.11 ?  92  PRO B N     1 
ATOM   6312  C  CA    . PRO B 1 92  ? 143.008 133.010 174.498 1.00 40.42 ?  92  PRO B CA    1 
ATOM   6313  C  C     . PRO B 1 92  ? 143.044 131.595 173.953 1.00 39.94 ?  92  PRO B C     1 
ATOM   6314  O  O     . PRO B 1 92  ? 143.207 130.647 174.731 1.00 43.37 ?  92  PRO B O     1 
ATOM   6315  C  CB    . PRO B 1 92  ? 141.575 133.467 174.793 1.00 40.58 ?  92  PRO B CB    1 
ATOM   6316  C  CG    . PRO B 1 92  ? 141.152 134.153 173.543 1.00 40.82 ?  92  PRO B CG    1 
ATOM   6317  C  CD    . PRO B 1 92  ? 142.381 134.815 172.979 1.00 42.53 ?  92  PRO B CD    1 
ATOM   6318  N  N     . SER B 1 93  ? 142.903 131.423 172.644 1.00 38.53 ?  93  SER B N     1 
ATOM   6319  C  CA    . SER B 1 93  ? 142.830 130.109 172.030 1.00 40.38 ?  93  SER B CA    1 
ATOM   6320  C  C     . SER B 1 93  ? 143.863 130.014 170.919 1.00 42.60 ?  93  SER B C     1 
ATOM   6321  O  O     . SER B 1 93  ? 144.338 131.024 170.395 1.00 47.55 ?  93  SER B O     1 
ATOM   6322  C  CB    . SER B 1 93  ? 141.427 129.834 171.474 1.00 44.04 ?  93  SER B CB    1 
ATOM   6323  O  OG    . SER B 1 93  ? 141.373 130.085 170.082 1.00 50.00 ?  93  SER B OG    1 
ATOM   6324  N  N     . PHE B 1 94  ? 144.221 128.776 170.572 1.00 41.90 ?  94  PHE B N     1 
ATOM   6325  C  CA    . PHE B 1 94  ? 145.175 128.570 169.489 1.00 40.14 ?  94  PHE B CA    1 
ATOM   6326  C  C     . PHE B 1 94  ? 144.612 129.039 168.155 1.00 42.76 ?  94  PHE B C     1 
ATOM   6327  O  O     . PHE B 1 94  ? 145.349 129.568 167.318 1.00 47.43 ?  94  PHE B O     1 
ATOM   6328  C  CB    . PHE B 1 94  ? 145.581 127.100 169.404 1.00 40.16 ?  94  PHE B CB    1 
ATOM   6329  C  CG    . PHE B 1 94  ? 146.180 126.723 168.082 1.00 41.76 ?  94  PHE B CG    1 
ATOM   6330  C  CD1   . PHE B 1 94  ? 147.431 127.186 167.721 1.00 42.32 ?  94  PHE B CD1   1 
ATOM   6331  C  CD2   . PHE B 1 94  ? 145.485 125.925 167.191 1.00 43.73 ?  94  PHE B CD2   1 
ATOM   6332  C  CE1   . PHE B 1 94  ? 147.980 126.854 166.502 1.00 42.88 ?  94  PHE B CE1   1 
ATOM   6333  C  CE2   . PHE B 1 94  ? 146.034 125.591 165.971 1.00 41.04 ?  94  PHE B CE2   1 
ATOM   6334  C  CZ    . PHE B 1 94  ? 147.281 126.055 165.627 1.00 40.39 ?  94  PHE B CZ    1 
ATOM   6335  N  N     . MET B 1 95  ? 143.310 128.844 167.935 1.00 38.81 ?  95  MET B N     1 
ATOM   6336  C  CA    . MET B 1 95  ? 142.724 129.188 166.645 1.00 34.84 ?  95  MET B CA    1 
ATOM   6337  C  C     . MET B 1 95  ? 142.734 130.689 166.392 1.00 41.06 ?  95  MET B C     1 
ATOM   6338  O  O     . MET B 1 95  ? 142.889 131.112 165.245 1.00 43.38 ?  95  MET B O     1 
ATOM   6339  C  CB    . MET B 1 95  ? 141.302 128.639 166.544 1.00 41.10 ?  95  MET B CB    1 
ATOM   6340  C  CG    . MET B 1 95  ? 140.619 128.830 165.185 1.00 45.93 ?  95  MET B CG    1 
ATOM   6341  S  SD    . MET B 1 95  ? 141.367 128.166 163.671 1.00 55.90 ?  95  MET B SD    1 
ATOM   6342  C  CE    . MET B 1 95  ? 142.401 126.825 164.252 1.00 43.07 ?  95  MET B CE    1 
ATOM   6343  N  N     . SER B 1 96  ? 142.585 131.506 167.436 1.00 36.73 ?  96  SER B N     1 
ATOM   6344  C  CA    . SER B 1 96  ? 142.657 132.953 167.254 1.00 33.30 ?  96  SER B CA    1 
ATOM   6345  C  C     . SER B 1 96  ? 144.010 133.370 166.691 1.00 36.80 ?  96  SER B C     1 
ATOM   6346  O  O     . SER B 1 96  ? 144.091 134.052 165.658 1.00 32.79 ?  96  SER B O     1 
ATOM   6347  C  CB    . SER B 1 96  ? 142.395 133.655 168.585 1.00 36.01 ?  96  SER B CB    1 
ATOM   6348  O  OG    . SER B 1 96  ? 141.388 132.989 169.322 1.00 42.95 ?  96  SER B OG    1 
ATOM   6349  N  N     . ALA B 1 97  ? 145.088 132.949 167.356 1.00 36.06 ?  97  ALA B N     1 
ATOM   6350  C  CA    . ALA B 1 97  ? 146.432 133.292 166.907 1.00 32.56 ?  97  ALA B CA    1 
ATOM   6351  C  C     . ALA B 1 97  ? 146.736 132.677 165.550 1.00 34.38 ?  97  ALA B C     1 
ATOM   6352  O  O     . ALA B 1 97  ? 147.360 133.319 164.700 1.00 40.22 ?  97  ALA B O     1 
ATOM   6353  C  CB    . ALA B 1 97  ? 147.457 132.837 167.941 1.00 38.51 ?  97  ALA B CB    1 
ATOM   6354  N  N     . PHE B 1 98  ? 146.315 131.431 165.335 1.00 37.04 ?  98  PHE B N     1 
ATOM   6355  C  CA    . PHE B 1 98  ? 146.558 130.776 164.055 1.00 34.05 ?  98  PHE B CA    1 
ATOM   6356  C  C     . PHE B 1 98  ? 145.875 131.526 162.921 1.00 36.17 ?  98  PHE B C     1 
ATOM   6357  O  O     . PHE B 1 98  ? 146.485 131.789 161.880 1.00 48.45 ?  98  PHE B O     1 
ATOM   6358  C  CB    . PHE B 1 98  ? 146.078 129.326 164.108 1.00 39.75 ?  98  PHE B CB    1 
ATOM   6359  C  CG    . PHE B 1 98  ? 146.188 128.605 162.797 1.00 39.93 ?  98  PHE B CG    1 
ATOM   6360  C  CD1   . PHE B 1 98  ? 147.394 128.060 162.391 1.00 39.71 ?  98  PHE B CD1   1 
ATOM   6361  C  CD2   . PHE B 1 98  ? 145.086 128.471 161.969 1.00 41.60 ?  98  PHE B CD2   1 
ATOM   6362  C  CE1   . PHE B 1 98  ? 147.498 127.398 161.186 1.00 39.50 ?  98  PHE B CE1   1 
ATOM   6363  C  CE2   . PHE B 1 98  ? 145.187 127.812 160.762 1.00 44.69 ?  98  PHE B CE2   1 
ATOM   6364  C  CZ    . PHE B 1 98  ? 146.393 127.274 160.371 1.00 43.40 ?  98  PHE B CZ    1 
ATOM   6365  N  N     . LYS B 1 99  ? 144.607 131.894 163.111 1.00 41.42 ?  99  LYS B N     1 
ATOM   6366  C  CA    . LYS B 1 99  ? 143.880 132.614 162.077 1.00 39.05 ?  99  LYS B CA    1 
ATOM   6367  C  C     . LYS B 1 99  ? 144.505 133.974 161.812 1.00 37.72 ?  99  LYS B C     1 
ATOM   6368  O  O     . LYS B 1 99  ? 144.660 134.375 160.654 1.00 42.56 ?  99  LYS B O     1 
ATOM   6369  C  CB    . LYS B 1 99  ? 142.412 132.762 162.472 1.00 37.97 ?  99  LYS B CB    1 
ATOM   6370  C  CG    . LYS B 1 99  ? 141.575 131.523 162.213 1.00 42.93 ?  99  LYS B CG    1 
ATOM   6371  C  CD    . LYS B 1 99  ? 141.696 131.061 160.774 1.00 42.94 ?  99  LYS B CD    1 
ATOM   6372  C  CE    . LYS B 1 99  ? 140.454 130.311 160.332 1.00 42.46 ?  99  LYS B CE    1 
ATOM   6373  N  NZ    . LYS B 1 99  ? 139.998 130.747 158.985 1.00 47.99 1  99  LYS B NZ    1 
ATOM   6374  N  N     . PHE B 1 100 ? 144.896 134.694 162.868 1.00 36.96 ?  100 PHE B N     1 
ATOM   6375  C  CA    . PHE B 1 100 ? 145.514 135.996 162.645 1.00 34.43 ?  100 PHE B CA    1 
ATOM   6376  C  C     . PHE B 1 100 ? 146.831 135.859 161.892 1.00 37.14 ?  100 PHE B C     1 
ATOM   6377  O  O     . PHE B 1 100 ? 147.047 136.524 160.874 1.00 41.84 ?  100 PHE B O     1 
ATOM   6378  C  CB    . PHE B 1 100 ? 145.744 136.736 163.960 1.00 34.19 ?  100 PHE B CB    1 
ATOM   6379  C  CG    . PHE B 1 100 ? 146.475 138.032 163.775 1.00 37.70 ?  100 PHE B CG    1 
ATOM   6380  C  CD1   . PHE B 1 100 ? 145.840 139.120 163.201 1.00 37.53 ?  100 PHE B CD1   1 
ATOM   6381  C  CD2   . PHE B 1 100 ? 147.807 138.148 164.123 1.00 34.09 ?  100 PHE B CD2   1 
ATOM   6382  C  CE1   . PHE B 1 100 ? 146.513 140.307 163.007 1.00 37.84 ?  100 PHE B CE1   1 
ATOM   6383  C  CE2   . PHE B 1 100 ? 148.484 139.331 163.928 1.00 35.09 ?  100 PHE B CE2   1 
ATOM   6384  C  CZ    . PHE B 1 100 ? 147.837 140.412 163.372 1.00 37.50 ?  100 PHE B CZ    1 
ATOM   6385  N  N     . TYR B 1 101 ? 147.718 134.989 162.365 1.00 40.14 ?  101 TYR B N     1 
ATOM   6386  C  CA    . TYR B 1 101 ? 149.040 134.873 161.769 1.00 36.34 ?  101 TYR B CA    1 
ATOM   6387  C  C     . TYR B 1 101 ? 149.037 134.094 160.462 1.00 35.53 ?  101 TYR B C     1 
ATOM   6388  O  O     . TYR B 1 101 ? 150.085 133.999 159.818 1.00 44.77 ?  101 TYR B O     1 
ATOM   6389  C  CB    . TYR B 1 101 ? 150.006 134.237 162.770 1.00 35.64 ?  101 TYR B CB    1 
ATOM   6390  C  CG    . TYR B 1 101 ? 150.413 135.195 163.863 1.00 33.35 ?  101 TYR B CG    1 
ATOM   6391  C  CD1   . TYR B 1 101 ? 151.276 136.249 163.602 1.00 34.17 ?  101 TYR B CD1   1 
ATOM   6392  C  CD2   . TYR B 1 101 ? 149.913 135.062 165.149 1.00 37.40 ?  101 TYR B CD2   1 
ATOM   6393  C  CE1   . TYR B 1 101 ? 151.640 137.134 164.594 1.00 36.52 ?  101 TYR B CE1   1 
ATOM   6394  C  CE2   . TYR B 1 101 ? 150.270 135.942 166.146 1.00 39.90 ?  101 TYR B CE2   1 
ATOM   6395  C  CZ    . TYR B 1 101 ? 151.134 136.976 165.864 1.00 40.02 ?  101 TYR B CZ    1 
ATOM   6396  O  OH    . TYR B 1 101 ? 151.490 137.853 166.860 1.00 39.82 ?  101 TYR B OH    1 
ATOM   6397  N  N     . ASN B 1 102 ? 147.897 133.535 160.056 1.00 38.82 ?  102 ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 102 ? 147.791 132.912 158.747 1.00 41.96 ?  102 ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 102 ? 147.000 133.740 157.742 1.00 43.72 ?  102 ASN B C     1 
ATOM   6400  O  O     . ASN B 1 102 ? 147.140 133.510 156.536 1.00 48.13 ?  102 ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 102 ? 147.141 131.528 158.869 1.00 40.56 ?  102 ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 102 ? 148.155 130.430 159.125 1.00 44.81 ?  102 ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 102 ? 149.009 130.548 160.004 1.00 48.40 ?  102 ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 102 ? 148.066 129.354 158.353 1.00 43.12 ?  102 ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 103 ? 146.181 134.688 158.194 1.00 42.99 ?  103 ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 103 ? 145.347 135.455 157.276 1.00 42.91 ?  103 ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 103 ? 145.652 136.943 157.258 1.00 42.58 ?  103 ASP B C     1 
ATOM   6408  O  O     . ASP B 1 103 ? 145.575 137.564 156.196 1.00 46.97 ?  103 ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 103 ? 143.863 135.255 157.626 1.00 45.28 ?  103 ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 103 ? 143.401 133.825 157.424 1.00 50.09 ?  103 ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 103 ? 144.199 132.999 156.938 1.00 50.18 ?  103 ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 103 ? 142.235 133.526 157.758 1.00 53.52 -1 103 ASP B OD2   1 
ATOM   6413  N  N     . TYR B 1 104 ? 145.997 137.538 158.397 1.00 36.66 ?  104 TYR B N     1 
ATOM   6414  C  CA    . TYR B 1 104 ? 146.097 138.986 158.513 1.00 41.43 ?  104 TYR B CA    1 
ATOM   6415  C  C     . TYR B 1 104 ? 147.490 139.494 158.848 1.00 39.97 ?  104 TYR B C     1 
ATOM   6416  O  O     . TYR B 1 104 ? 147.798 140.643 158.528 1.00 45.56 ?  104 TYR B O     1 
ATOM   6417  C  CB    . TYR B 1 104 ? 145.119 139.501 159.580 1.00 37.76 ?  104 TYR B CB    1 
ATOM   6418  C  CG    . TYR B 1 104 ? 143.693 139.068 159.342 1.00 41.00 ?  104 TYR B CG    1 
ATOM   6419  C  CD1   . TYR B 1 104 ? 142.860 139.795 158.505 1.00 40.31 ?  104 TYR B CD1   1 
ATOM   6420  C  CD2   . TYR B 1 104 ? 143.184 137.927 159.945 1.00 35.66 ?  104 TYR B CD2   1 
ATOM   6421  C  CE1   . TYR B 1 104 ? 141.559 139.402 158.280 1.00 39.93 ?  104 TYR B CE1   1 
ATOM   6422  C  CE2   . TYR B 1 104 ? 141.884 137.525 159.724 1.00 36.77 ?  104 TYR B CE2   1 
ATOM   6423  C  CZ    . TYR B 1 104 ? 141.076 138.268 158.891 1.00 41.95 ?  104 TYR B CZ    1 
ATOM   6424  O  OH    . TYR B 1 104 ? 139.779 137.874 158.667 1.00 41.50 ?  104 TYR B OH    1 
ATOM   6425  N  N     . ALA B 1 105 ? 148.331 138.685 159.487 1.00 42.71 ?  105 ALA B N     1 
ATOM   6426  C  CA    . ALA B 1 105 ? 149.670 139.137 159.835 1.00 42.57 ?  105 ALA B CA    1 
ATOM   6427  C  C     . ALA B 1 105 ? 150.507 139.348 158.582 1.00 45.88 ?  105 ALA B C     1 
ATOM   6428  O  O     . ALA B 1 105 ? 150.469 138.544 157.646 1.00 44.64 ?  105 ALA B O     1 
ATOM   6429  C  CB    . ALA B 1 105 ? 150.352 138.127 160.755 1.00 38.01 ?  105 ALA B CB    1 
ATOM   6430  N  N     . LEU B 1 106 ? 151.263 140.442 158.565 1.00 47.08 ?  106 LEU B N     1 
ATOM   6431  C  CA    . LEU B 1 106 ? 152.109 140.747 157.421 1.00 44.38 ?  106 LEU B CA    1 
ATOM   6432  C  C     . LEU B 1 106 ? 153.286 139.782 157.368 1.00 47.36 ?  106 LEU B C     1 
ATOM   6433  O  O     . LEU B 1 106 ? 153.990 139.586 158.362 1.00 47.74 ?  106 LEU B O     1 
ATOM   6434  C  CB    . LEU B 1 106 ? 152.607 142.189 157.496 1.00 48.24 ?  106 LEU B CB    1 
ATOM   6435  C  CG    . LEU B 1 106 ? 153.397 142.706 156.293 1.00 44.94 ?  106 LEU B CG    1 
ATOM   6436  C  CD1   . LEU B 1 106 ? 152.504 142.807 155.069 1.00 44.16 ?  106 LEU B CD1   1 
ATOM   6437  C  CD2   . LEU B 1 106 ? 154.029 144.050 156.607 1.00 44.60 ?  106 LEU B CD2   1 
ATOM   6438  N  N     . LYS B 1 107 ? 153.497 139.184 156.202 1.00 55.35 ?  107 LYS B N     1 
ATOM   6439  C  CA    . LYS B 1 107 ? 154.579 138.242 155.980 1.00 55.18 ?  107 LYS B CA    1 
ATOM   6440  C  C     . LYS B 1 107 ? 155.529 138.790 154.926 1.00 56.71 ?  107 LYS B C     1 
ATOM   6441  O  O     . LYS B 1 107 ? 155.208 139.734 154.198 1.00 55.21 ?  107 LYS B O     1 
ATOM   6442  C  CB    . LYS B 1 107 ? 154.048 136.873 155.542 1.00 54.68 ?  107 LYS B CB    1 
ATOM   6443  C  CG    . LYS B 1 107 ? 153.591 135.991 156.685 1.00 52.82 ?  107 LYS B CG    1 
ATOM   6444  C  CD    . LYS B 1 107 ? 152.762 134.827 156.178 1.00 55.63 ?  107 LYS B CD    1 
ATOM   6445  C  CE    . LYS B 1 107 ? 151.982 134.184 157.306 1.00 57.28 ?  107 LYS B CE    1 
ATOM   6446  N  NZ    . LYS B 1 107 ? 151.568 135.186 158.328 1.00 56.18 1  107 LYS B NZ    1 
ATOM   6447  N  N     . THR B 1 108 ? 156.713 138.187 154.855 1.00 60.92 ?  108 THR B N     1 
ATOM   6448  C  CA    . THR B 1 108 ? 157.688 138.566 153.849 1.00 60.71 ?  108 THR B CA    1 
ATOM   6449  C  C     . THR B 1 108 ? 157.144 138.269 152.451 1.00 62.10 ?  108 THR B C     1 
ATOM   6450  O  O     . THR B 1 108 ? 156.151 137.560 152.276 1.00 62.89 ?  108 THR B O     1 
ATOM   6451  C  CB    . THR B 1 108 ? 159.006 137.826 154.072 1.00 59.88 ?  108 THR B CB    1 
ATOM   6452  O  OG1   . THR B 1 108 ? 158.746 136.427 154.238 1.00 62.05 ?  108 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 1 108 ? 159.713 138.349 155.309 1.00 57.02 ?  108 THR B CG2   1 
ATOM   6454  N  N     . ASN B 1 109 ? 157.817 138.831 151.442 1.00 63.27 ?  109 ASN B N     1 
ATOM   6455  C  CA    . ASN B 1 109 ? 157.367 138.648 150.065 1.00 63.09 ?  109 ASN B CA    1 
ATOM   6456  C  C     . ASN B 1 109 ? 157.376 137.182 149.653 1.00 66.07 ?  109 ASN B C     1 
ATOM   6457  O  O     . ASN B 1 109 ? 156.605 136.782 148.773 1.00 65.99 ?  109 ASN B O     1 
ATOM   6458  C  CB    . ASN B 1 109 ? 158.233 139.473 149.113 1.00 61.80 ?  109 ASN B CB    1 
ATOM   6459  C  CG    . ASN B 1 109 ? 158.244 140.946 149.467 1.00 64.04 ?  109 ASN B CG    1 
ATOM   6460  O  OD1   . ASN B 1 109 ? 157.218 141.622 149.384 1.00 66.19 ?  109 ASN B OD1   1 
ATOM   6461  N  ND2   . ASN B 1 109 ? 159.405 141.451 149.862 1.00 63.88 ?  109 ASN B ND2   1 
ATOM   6462  N  N     . ASP B 1 110 ? 158.231 136.368 150.268 1.00 66.04 ?  110 ASP B N     1 
ATOM   6463  C  CA    . ASP B 1 110 ? 158.236 134.932 150.033 1.00 67.63 ?  110 ASP B CA    1 
ATOM   6464  C  C     . ASP B 1 110 ? 157.356 134.176 151.021 1.00 66.77 ?  110 ASP B C     1 
ATOM   6465  O  O     . ASP B 1 110 ? 157.340 132.940 150.997 1.00 67.18 ?  110 ASP B O     1 
ATOM   6466  C  CB    . ASP B 1 110 ? 159.668 134.387 150.080 1.00 68.15 ?  110 ASP B CB    1 
ATOM   6467  C  CG    . ASP B 1 110 ? 160.319 134.566 151.435 1.00 69.90 ?  110 ASP B CG    1 
ATOM   6468  O  OD1   . ASP B 1 110 ? 159.924 135.492 152.168 1.00 69.54 ?  110 ASP B OD1   1 
ATOM   6469  O  OD2   . ASP B 1 110 ? 161.231 133.779 151.766 1.00 69.81 -1 110 ASP B OD2   1 
ATOM   6470  N  N     . LYS B 1 111 ? 156.624 134.892 151.880 1.00 64.62 ?  111 LYS B N     1 
ATOM   6471  C  CA    . LYS B 1 111 ? 155.703 134.292 152.848 1.00 64.06 ?  111 LYS B CA    1 
ATOM   6472  C  C     . LYS B 1 111 ? 156.413 133.279 153.742 1.00 66.24 ?  111 LYS B C     1 
ATOM   6473  O  O     . LYS B 1 111 ? 155.885 132.205 154.036 1.00 67.00 ?  111 LYS B O     1 
ATOM   6474  C  CB    . LYS B 1 111 ? 154.502 133.651 152.148 1.00 64.89 ?  111 LYS B CB    1 
ATOM   6475  C  CG    . LYS B 1 111 ? 153.873 134.508 151.059 1.00 64.51 ?  111 LYS B CG    1 
ATOM   6476  C  CD    . LYS B 1 111 ? 153.501 135.893 151.573 1.00 66.11 ?  111 LYS B CD    1 
ATOM   6477  C  CE    . LYS B 1 111 ? 152.294 135.839 152.494 1.00 67.79 ?  111 LYS B CE    1 
ATOM   6478  N  NZ    . LYS B 1 111 ? 151.087 135.304 151.807 1.00 68.04 1  111 LYS B NZ    1 
ATOM   6479  N  N     . LYS B 1 112 ? 157.620 133.626 154.181 1.00 65.24 ?  112 LYS B N     1 
ATOM   6480  C  CA    . LYS B 1 112 ? 158.433 132.757 155.024 1.00 64.41 ?  112 LYS B CA    1 
ATOM   6481  C  C     . LYS B 1 112 ? 158.495 133.211 156.473 1.00 64.17 ?  112 LYS B C     1 
ATOM   6482  O  O     . LYS B 1 112 ? 158.381 132.381 157.379 1.00 65.83 ?  112 LYS B O     1 
ATOM   6483  C  CB    . LYS B 1 112 ? 159.855 132.660 154.458 1.00 63.97 ?  112 LYS B CB    1 
ATOM   6484  C  CG    . LYS B 1 112 ? 160.930 132.310 155.477 1.00 67.04 ?  112 LYS B CG    1 
ATOM   6485  C  CD    . LYS B 1 112 ? 160.910 130.828 155.821 1.00 65.11 ?  112 LYS B CD    1 
ATOM   6486  C  CE    . LYS B 1 112 ? 161.464 130.580 157.215 1.00 65.22 ?  112 LYS B CE    1 
ATOM   6487  N  NZ    . LYS B 1 112 ? 160.593 131.166 158.271 1.00 64.88 1  112 LYS B NZ    1 
ATOM   6488  N  N     . LYS B 1 113 ? 158.662 134.503 156.717 1.00 60.20 ?  113 LYS B N     1 
ATOM   6489  C  CA    . LYS B 1 113 ? 158.776 135.057 158.059 1.00 59.08 ?  113 LYS B CA    1 
ATOM   6490  C  C     . LYS B 1 113 ? 157.589 135.974 158.342 1.00 59.43 ?  113 LYS B C     1 
ATOM   6491  O  O     . LYS B 1 113 ? 156.753 136.233 157.474 1.00 57.53 ?  113 LYS B O     1 
ATOM   6492  C  CB    . LYS B 1 113 ? 160.104 135.801 158.221 1.00 57.33 ?  113 LYS B CB    1 
ATOM   6493  C  CG    . LYS B 1 113 ? 161.305 134.896 158.435 1.00 57.95 ?  113 LYS B CG    1 
ATOM   6494  C  CD    . LYS B 1 113 ? 161.328 134.332 159.843 1.00 59.48 ?  113 LYS B CD    1 
ATOM   6495  C  CE    . LYS B 1 113 ? 162.726 133.894 160.241 1.00 57.00 ?  113 LYS B CE    1 
ATOM   6496  N  NZ    . LYS B 1 113 ? 162.822 132.415 160.375 1.00 58.77 1  113 LYS B NZ    1 
ATOM   6497  N  N     . ILE B 1 114 ? 157.526 136.470 159.574 1.00 52.83 ?  114 ILE B N     1 
ATOM   6498  C  CA    . ILE B 1 114 ? 156.420 137.298 160.045 1.00 49.84 ?  114 ILE B CA    1 
ATOM   6499  C  C     . ILE B 1 114 ? 156.969 138.669 160.412 1.00 51.40 ?  114 ILE B C     1 
ATOM   6500  O  O     . ILE B 1 114 ? 157.875 138.777 161.247 1.00 54.24 ?  114 ILE B O     1 
ATOM   6501  C  CB    . ILE B 1 114 ? 155.704 136.657 161.246 1.00 51.19 ?  114 ILE B CB    1 
ATOM   6502  C  CG1   . ILE B 1 114 ? 154.865 135.460 160.797 1.00 49.80 ?  114 ILE B CG1   1 
ATOM   6503  C  CG2   . ILE B 1 114 ? 154.835 137.675 161.960 1.00 51.04 ?  114 ILE B CG2   1 
ATOM   6504  C  CD1   . ILE B 1 114 ? 154.440 134.560 161.932 1.00 46.81 ?  114 ILE B CD1   1 
ATOM   6505  N  N     . LEU B 1 115 ? 156.422 139.714 159.790 1.00 48.43 ?  115 LEU B N     1 
ATOM   6506  C  CA    . LEU B 1 115 ? 156.812 141.081 160.118 1.00 47.70 ?  115 LEU B CA    1 
ATOM   6507  C  C     . LEU B 1 115 ? 155.932 141.697 161.195 1.00 50.04 ?  115 LEU B C     1 
ATOM   6508  O  O     . LEU B 1 115 ? 156.424 142.457 162.036 1.00 51.35 ?  115 LEU B O     1 
ATOM   6509  C  CB    . LEU B 1 115 ? 156.768 141.969 158.872 1.00 49.26 ?  115 LEU B CB    1 
ATOM   6510  C  CG    . LEU B 1 115 ? 157.880 141.860 157.829 1.00 47.40 ?  115 LEU B CG    1 
ATOM   6511  C  CD1   . LEU B 1 115 ? 159.238 141.686 158.490 1.00 49.77 ?  115 LEU B CD1   1 
ATOM   6512  C  CD2   . LEU B 1 115 ? 157.594 140.735 156.863 1.00 48.91 ?  115 LEU B CD2   1 
ATOM   6513  N  N     . GLU B 1 116 ? 154.639 141.388 161.189 1.00 46.96 ?  116 GLU B N     1 
ATOM   6514  C  CA    . GLU B 1 116 ? 153.665 142.056 162.039 1.00 46.21 ?  116 GLU B CA    1 
ATOM   6515  C  C     . GLU B 1 116 ? 153.144 141.106 163.105 1.00 44.69 ?  116 GLU B C     1 
ATOM   6516  O  O     . GLU B 1 116 ? 152.711 139.991 162.795 1.00 49.18 ?  116 GLU B O     1 
ATOM   6517  C  CB    . GLU B 1 116 ? 152.494 142.588 161.211 1.00 43.45 ?  116 GLU B CB    1 
ATOM   6518  C  CG    . GLU B 1 116 ? 152.585 144.060 160.875 1.00 44.40 ?  116 GLU B CG    1 
ATOM   6519  C  CD    . GLU B 1 116 ? 151.439 144.524 160.002 1.00 47.71 ?  116 GLU B CD    1 
ATOM   6520  O  OE1   . GLU B 1 116 ? 150.632 143.670 159.579 1.00 49.39 ?  116 GLU B OE1   1 
ATOM   6521  O  OE2   . GLU B 1 116 ? 151.343 145.739 159.739 1.00 50.22 -1 116 GLU B OE2   1 
ATOM   6522  N  N     . ARG B 1 117 ? 153.180 141.553 164.355 1.00 39.36 ?  117 ARG B N     1 
ATOM   6523  C  CA    . ARG B 1 117 ? 152.439 140.904 165.419 1.00 41.72 ?  117 ARG B CA    1 
ATOM   6524  C  C     . ARG B 1 117 ? 151.018 141.461 165.435 1.00 41.09 ?  117 ARG B C     1 
ATOM   6525  O  O     . ARG B 1 117 ? 150.645 142.299 164.610 1.00 39.45 ?  117 ARG B O     1 
ATOM   6526  C  CB    . ARG B 1 117 ? 153.134 141.111 166.763 1.00 42.00 ?  117 ARG B CB    1 
ATOM   6527  C  CG    . ARG B 1 117 ? 154.537 140.539 166.835 1.00 40.80 ?  117 ARG B CG    1 
ATOM   6528  C  CD    . ARG B 1 117 ? 154.569 139.081 166.401 1.00 46.77 ?  117 ARG B CD    1 
ATOM   6529  N  NE    . ARG B 1 117 ? 154.363 138.167 167.518 1.00 44.38 ?  117 ARG B NE    1 
ATOM   6530  C  CZ    . ARG B 1 117 ? 155.240 137.949 168.488 1.00 45.70 ?  117 ARG B CZ    1 
ATOM   6531  N  NH1   . ARG B 1 117 ? 156.419 138.550 168.505 1.00 43.54 1  117 ARG B NH1   1 
ATOM   6532  N  NH2   . ARG B 1 117 ? 154.930 137.102 169.465 1.00 47.75 ?  117 ARG B NH2   1 
ATOM   6533  N  N     . TYR B 1 118 ? 150.205 140.988 166.377 1.00 41.03 ?  118 TYR B N     1 
ATOM   6534  C  CA    . TYR B 1 118 ? 148.866 141.546 166.524 1.00 35.12 ?  118 TYR B CA    1 
ATOM   6535  C  C     . TYR B 1 118 ? 148.933 143.020 166.902 1.00 38.01 ?  118 TYR B C     1 
ATOM   6536  O  O     . TYR B 1 118 ? 148.186 143.846 166.363 1.00 40.88 ?  118 TYR B O     1 
ATOM   6537  C  CB    . TYR B 1 118 ? 148.077 140.753 167.564 1.00 36.39 ?  118 TYR B CB    1 
ATOM   6538  C  CG    . TYR B 1 118 ? 146.594 141.034 167.551 1.00 38.14 ?  118 TYR B CG    1 
ATOM   6539  C  CD1   . TYR B 1 118 ? 145.853 140.896 166.386 1.00 33.51 ?  118 TYR B CD1   1 
ATOM   6540  C  CD2   . TYR B 1 118 ? 145.936 141.440 168.701 1.00 36.95 ?  118 TYR B CD2   1 
ATOM   6541  C  CE1   . TYR B 1 118 ? 144.500 141.152 166.369 1.00 33.42 ?  118 TYR B CE1   1 
ATOM   6542  C  CE2   . TYR B 1 118 ? 144.581 141.694 168.695 1.00 33.77 ?  118 TYR B CE2   1 
ATOM   6543  C  CZ    . TYR B 1 118 ? 143.868 141.549 167.525 1.00 35.25 ?  118 TYR B CZ    1 
ATOM   6544  O  OH    . TYR B 1 118 ? 142.519 141.806 167.512 1.00 45.00 ?  118 TYR B OH    1 
ATOM   6545  N  N     . GLU B 1 119 ? 149.841 143.366 167.815 1.00 44.44 ?  119 GLU B N     1 
ATOM   6546  C  CA    . GLU B 1 119 ? 149.983 144.755 168.235 1.00 38.64 ?  119 GLU B CA    1 
ATOM   6547  C  C     . GLU B 1 119 ? 150.464 145.639 167.091 1.00 38.45 ?  119 GLU B C     1 
ATOM   6548  O  O     . GLU B 1 119 ? 150.010 146.776 166.955 1.00 49.14 ?  119 GLU B O     1 
ATOM   6549  C  CB    . GLU B 1 119 ? 150.934 144.844 169.426 1.00 38.99 ?  119 GLU B CB    1 
ATOM   6550  C  CG    . GLU B 1 119 ? 150.396 144.199 170.691 1.00 39.79 ?  119 GLU B CG    1 
ATOM   6551  C  CD    . GLU B 1 119 ? 150.853 142.764 170.855 1.00 45.71 ?  119 GLU B CD    1 
ATOM   6552  O  OE1   . GLU B 1 119 ? 151.107 142.097 169.830 1.00 45.33 ?  119 GLU B OE1   1 
ATOM   6553  O  OE2   . GLU B 1 119 ? 150.957 142.299 172.010 1.00 46.42 -1 119 GLU B OE2   1 
ATOM   6554  N  N     . ASP B 1 120 ? 151.386 145.143 166.262 1.00 40.96 ?  120 ASP B N     1 
ATOM   6555  C  CA    . ASP B 1 120 ? 151.864 145.943 165.136 1.00 39.84 ?  120 ASP B CA    1 
ATOM   6556  C  C     . ASP B 1 120 ? 150.752 146.197 164.127 1.00 39.51 ?  120 ASP B C     1 
ATOM   6557  O  O     . ASP B 1 120 ? 150.590 147.319 163.635 1.00 44.82 ?  120 ASP B O     1 
ATOM   6558  C  CB    . ASP B 1 120 ? 153.052 145.257 164.461 1.00 45.29 ?  120 ASP B CB    1 
ATOM   6559  C  CG    . ASP B 1 120 ? 154.054 144.716 165.453 1.00 47.85 ?  120 ASP B CG    1 
ATOM   6560  O  OD1   . ASP B 1 120 ? 154.483 143.557 165.288 1.00 51.60 ?  120 ASP B OD1   1 
ATOM   6561  O  OD2   . ASP B 1 120 ? 154.407 145.447 166.401 1.00 46.55 -1 120 ASP B OD2   1 
ATOM   6562  N  N     . ARG B 1 121 ? 149.980 145.158 163.801 1.00 34.52 ?  121 ARG B N     1 
ATOM   6563  C  CA    . ARG B 1 121 ? 148.860 145.322 162.881 1.00 31.09 ?  121 ARG B CA    1 
ATOM   6564  C  C     . ARG B 1 121 ? 147.838 146.305 163.433 1.00 35.79 ?  121 ARG B C     1 
ATOM   6565  O  O     . ARG B 1 121 ? 147.343 147.176 162.705 1.00 45.87 ?  121 ARG B O     1 
ATOM   6566  C  CB    . ARG B 1 121 ? 148.215 143.964 162.604 1.00 35.38 ?  121 ARG B CB    1 
ATOM   6567  C  CG    . ARG B 1 121 ? 146.967 144.014 161.742 1.00 32.93 ?  121 ARG B CG    1 
ATOM   6568  C  CD    . ARG B 1 121 ? 147.305 143.941 160.268 1.00 32.41 ?  121 ARG B CD    1 
ATOM   6569  N  NE    . ARG B 1 121 ? 147.108 145.226 159.612 1.00 43.28 ?  121 ARG B NE    1 
ATOM   6570  C  CZ    . ARG B 1 121 ? 147.899 145.714 158.668 1.00 39.89 ?  121 ARG B CZ    1 
ATOM   6571  N  NH1   . ARG B 1 121 ? 148.956 145.046 158.239 1.00 42.44 1  121 ARG B NH1   1 
ATOM   6572  N  NH2   . ARG B 1 121 ? 147.623 146.903 158.143 1.00 32.92 ?  121 ARG B NH2   1 
ATOM   6573  N  N     . ILE B 1 122 ? 147.522 146.195 164.724 1.00 35.39 ?  122 ILE B N     1 
ATOM   6574  C  CA    . ILE B 1 122 ? 146.547 147.095 165.327 1.00 29.58 ?  122 ILE B CA    1 
ATOM   6575  C  C     . ILE B 1 122 ? 147.073 148.526 165.351 1.00 30.42 ?  122 ILE B C     1 
ATOM   6576  O  O     . ILE B 1 122 ? 146.330 149.476 165.086 1.00 37.63 ?  122 ILE B O     1 
ATOM   6577  C  CB    . ILE B 1 122 ? 146.160 146.592 166.729 1.00 35.40 ?  122 ILE B CB    1 
ATOM   6578  C  CG1   . ILE B 1 122 ? 145.115 145.484 166.601 1.00 32.27 ?  122 ILE B CG1   1 
ATOM   6579  C  CG2   . ILE B 1 122 ? 145.637 147.726 167.597 1.00 31.89 ?  122 ILE B CG2   1 
ATOM   6580  C  CD1   . ILE B 1 122 ? 144.490 145.085 167.898 1.00 32.92 ?  122 ILE B CD1   1 
ATOM   6581  N  N     . SER B 1 123 ? 148.361 148.705 165.655 1.00 33.76 ?  123 SER B N     1 
ATOM   6582  C  CA    . SER B 1 123 ? 148.944 150.042 165.658 1.00 32.60 ?  123 SER B CA    1 
ATOM   6583  C  C     . SER B 1 123 ? 148.915 150.664 164.271 1.00 36.18 ?  123 SER B C     1 
ATOM   6584  O  O     . SER B 1 123 ? 148.605 151.850 164.122 1.00 36.84 ?  123 SER B O     1 
ATOM   6585  C  CB    . SER B 1 123 ? 150.379 149.991 166.177 1.00 32.05 ?  123 SER B CB    1 
ATOM   6586  O  OG    . SER B 1 123 ? 150.438 149.398 167.455 1.00 37.98 ?  123 SER B OG    1 
ATOM   6587  N  N     . ILE B 1 124 ? 149.241 149.881 163.242 1.00 36.71 ?  124 ILE B N     1 
ATOM   6588  C  CA    . ILE B 1 124 ? 149.225 150.412 161.883 1.00 34.76 ?  124 ILE B CA    1 
ATOM   6589  C  C     . ILE B 1 124 ? 147.805 150.774 161.467 1.00 39.62 ?  124 ILE B C     1 
ATOM   6590  O  O     . ILE B 1 124 ? 147.571 151.830 160.864 1.00 39.84 ?  124 ILE B O     1 
ATOM   6591  C  CB    . ILE B 1 124 ? 149.873 149.408 160.914 1.00 39.41 ?  124 ILE B CB    1 
ATOM   6592  C  CG1   . ILE B 1 124 ? 151.393 149.446 161.072 1.00 41.25 ?  124 ILE B CG1   1 
ATOM   6593  C  CG2   . ILE B 1 124 ? 149.478 149.710 159.479 1.00 36.46 ?  124 ILE B CG2   1 
ATOM   6594  C  CD1   . ILE B 1 124 ? 151.981 150.839 160.976 1.00 36.63 ?  124 ILE B CD1   1 
ATOM   6595  N  N     . VAL B 1 125 ? 146.833 149.920 161.797 1.00 32.40 ?  125 VAL B N     1 
ATOM   6596  C  CA    . VAL B 1 125 ? 145.443 150.212 161.458 1.00 30.50 ?  125 VAL B CA    1 
ATOM   6597  C  C     . VAL B 1 125 ? 144.970 151.471 162.176 1.00 25.65 ?  125 VAL B C     1 
ATOM   6598  O  O     . VAL B 1 125 ? 144.282 152.315 161.591 1.00 35.98 ?  125 VAL B O     1 
ATOM   6599  C  CB    . VAL B 1 125 ? 144.550 148.998 161.775 1.00 37.24 ?  125 VAL B CB    1 
ATOM   6600  C  CG1   . VAL B 1 125 ? 143.086 149.375 161.700 1.00 32.65 ?  125 VAL B CG1   1 
ATOM   6601  C  CG2   . VAL B 1 125 ? 144.847 147.862 160.812 1.00 27.59 ?  125 VAL B CG2   1 
ATOM   6602  N  N     . ALA B 1 126 ? 145.343 151.626 163.448 1.00 24.10 ?  126 ALA B N     1 
ATOM   6603  C  CA    . ALA B 1 126 ? 144.942 152.807 164.206 1.00 26.21 ?  126 ALA B CA    1 
ATOM   6604  C  C     . ALA B 1 126 ? 145.594 154.073 163.666 1.00 31.08 ?  126 ALA B C     1 
ATOM   6605  O  O     . ALA B 1 126 ? 144.951 155.127 163.594 1.00 34.62 ?  126 ALA B O     1 
ATOM   6606  C  CB    . ALA B 1 126 ? 145.291 152.621 165.679 1.00 29.96 ?  126 ALA B CB    1 
ATOM   6607  N  N     . LEU B 1 127 ? 146.874 153.995 163.298 1.00 36.91 ?  127 LEU B N     1 
ATOM   6608  C  CA    . LEU B 1 127 ? 147.559 155.156 162.743 1.00 26.42 ?  127 LEU B CA    1 
ATOM   6609  C  C     . LEU B 1 127 ? 146.972 155.544 161.395 1.00 26.74 ?  127 LEU B C     1 
ATOM   6610  O  O     . LEU B 1 127 ? 146.921 156.729 161.050 1.00 33.01 ?  127 LEU B O     1 
ATOM   6611  C  CB    . LEU B 1 127 ? 149.057 154.875 162.618 1.00 28.93 ?  127 LEU B CB    1 
ATOM   6612  C  CG    . LEU B 1 127 ? 149.868 154.849 163.913 1.00 32.83 ?  127 LEU B CG    1 
ATOM   6613  C  CD1   . LEU B 1 127 ? 151.184 154.124 163.703 1.00 38.52 ?  127 LEU B CD1   1 
ATOM   6614  C  CD2   . LEU B 1 127 ? 150.112 156.254 164.428 1.00 33.35 ?  127 LEU B CD2   1 
ATOM   6615  N  N     . PHE B 1 128 ? 146.532 154.556 160.614 1.00 32.50 ?  128 PHE B N     1 
ATOM   6616  C  CA    . PHE B 1 128 ? 145.847 154.860 159.362 1.00 33.27 ?  128 PHE B CA    1 
ATOM   6617  C  C     . PHE B 1 128 ? 144.477 155.480 159.625 1.00 30.13 ?  128 PHE B C     1 
ATOM   6618  O  O     . PHE B 1 128 ? 144.057 156.394 158.907 1.00 40.74 ?  128 PHE B O     1 
ATOM   6619  C  CB    . PHE B 1 128 ? 145.739 153.590 158.513 1.00 29.67 ?  128 PHE B CB    1 
ATOM   6620  C  CG    . PHE B 1 128 ? 144.759 153.687 157.376 1.00 35.44 ?  128 PHE B CG    1 
ATOM   6621  C  CD1   . PHE B 1 128 ? 143.416 153.396 157.560 1.00 33.75 ?  128 PHE B CD1   1 
ATOM   6622  C  CD2   . PHE B 1 128 ? 145.186 154.076 156.119 1.00 37.02 ?  128 PHE B CD2   1 
ATOM   6623  C  CE1   . PHE B 1 128 ? 142.525 153.492 156.514 1.00 34.62 ?  128 PHE B CE1   1 
ATOM   6624  C  CE2   . PHE B 1 128 ? 144.298 154.171 155.070 1.00 36.99 ?  128 PHE B CE2   1 
ATOM   6625  C  CZ    . PHE B 1 128 ? 142.967 153.880 155.268 1.00 34.68 ?  128 PHE B CZ    1 
ATOM   6626  N  N     . PHE B 1 129 ? 143.766 154.988 160.642 1.00 27.70 ?  129 PHE B N     1 
ATOM   6627  C  CA    . PHE B 1 129 ? 142.450 155.527 160.969 1.00 21.42 ?  129 PHE B CA    1 
ATOM   6628  C  C     . PHE B 1 129 ? 142.534 156.976 161.430 1.00 30.37 ?  129 PHE B C     1 
ATOM   6629  O  O     . PHE B 1 129 ? 141.714 157.809 161.027 1.00 33.81 ?  129 PHE B O     1 
ATOM   6630  C  CB    . PHE B 1 129 ? 141.787 154.682 162.055 1.00 24.55 ?  129 PHE B CB    1 
ATOM   6631  C  CG    . PHE B 1 129 ? 141.152 153.425 161.550 1.00 26.58 ?  129 PHE B CG    1 
ATOM   6632  C  CD1   . PHE B 1 129 ? 140.920 153.238 160.200 1.00 26.21 ?  129 PHE B CD1   1 
ATOM   6633  C  CD2   . PHE B 1 129 ? 140.775 152.429 162.434 1.00 28.07 ?  129 PHE B CD2   1 
ATOM   6634  C  CE1   . PHE B 1 129 ? 140.332 152.079 159.743 1.00 25.06 ?  129 PHE B CE1   1 
ATOM   6635  C  CE2   . PHE B 1 129 ? 140.184 151.269 161.982 1.00 30.63 ?  129 PHE B CE2   1 
ATOM   6636  C  CZ    . PHE B 1 129 ? 139.964 151.093 160.635 1.00 30.17 ?  129 PHE B CZ    1 
ATOM   6637  N  N     . ALA B 1 130 ? 143.509 157.292 162.284 1.00 35.74 ?  130 ALA B N     1 
ATOM   6638  C  CA    . ALA B 1 130 ? 143.549 158.613 162.903 1.00 35.44 ?  130 ALA B CA    1 
ATOM   6639  C  C     . ALA B 1 130 ? 143.904 159.706 161.903 1.00 42.14 ?  130 ALA B C     1 
ATOM   6640  O  O     . ALA B 1 130 ? 143.459 160.849 162.060 1.00 47.31 ?  130 ALA B O     1 
ATOM   6641  C  CB    . ALA B 1 130 ? 144.538 158.616 164.062 1.00 33.44 ?  130 ALA B CB    1 
ATOM   6642  N  N     . ASN B 1 131 ? 144.704 159.381 160.886 1.00 41.73 ?  131 ASN B N     1 
ATOM   6643  C  CA    . ASN B 1 131 ? 145.055 160.318 159.819 1.00 41.38 ?  131 ASN B CA    1 
ATOM   6644  C  C     . ASN B 1 131 ? 145.754 161.563 160.370 1.00 42.82 ?  131 ASN B C     1 
ATOM   6645  O  O     . ASN B 1 131 ? 145.440 162.696 160.002 1.00 46.71 ?  131 ASN B O     1 
ATOM   6646  C  CB    . ASN B 1 131 ? 143.817 160.700 159.001 1.00 40.39 ?  131 ASN B CB    1 
ATOM   6647  C  CG    . ASN B 1 131 ? 144.160 161.150 157.597 1.00 46.02 ?  131 ASN B CG    1 
ATOM   6648  O  OD1   . ASN B 1 131 ? 145.023 160.569 156.939 1.00 45.99 ?  131 ASN B OD1   1 
ATOM   6649  N  ND2   . ASN B 1 131 ? 143.482 162.189 157.128 1.00 44.13 ?  131 ASN B ND2   1 
ATOM   6650  N  N     . GLY B 1 132 ? 146.716 161.342 161.264 1.00 42.48 ?  132 GLY B N     1 
ATOM   6651  C  CA    . GLY B 1 132 ? 147.554 162.408 161.779 1.00 39.49 ?  132 GLY B CA    1 
ATOM   6652  C  C     . GLY B 1 132 ? 147.310 162.789 163.222 1.00 44.84 ?  132 GLY B C     1 
ATOM   6653  O  O     . GLY B 1 132 ? 148.068 163.607 163.759 1.00 50.55 ?  132 GLY B O     1 
ATOM   6654  N  N     . ASP B 1 133 ? 146.292 162.236 163.873 1.00 46.99 ?  133 ASP B N     1 
ATOM   6655  C  CA    . ASP B 1 133 ? 145.975 162.563 165.257 1.00 47.34 ?  133 ASP B CA    1 
ATOM   6656  C  C     . ASP B 1 133 ? 146.546 161.484 166.170 1.00 48.68 ?  133 ASP B C     1 
ATOM   6657  O  O     . ASP B 1 133 ? 146.184 160.310 166.053 1.00 48.93 ?  133 ASP B O     1 
ATOM   6658  C  CB    . ASP B 1 133 ? 144.464 162.692 165.450 1.00 47.18 ?  133 ASP B CB    1 
ATOM   6659  C  CG    . ASP B 1 133 ? 144.095 163.401 166.740 1.00 52.90 ?  133 ASP B CG    1 
ATOM   6660  O  OD1   . ASP B 1 133 ? 144.983 163.591 167.597 1.00 54.28 ?  133 ASP B OD1   1 
ATOM   6661  O  OD2   . ASP B 1 133 ? 142.911 163.762 166.899 1.00 50.36 -1 133 ASP B OD2   1 
ATOM   6662  N  N     . THR B 1 134 ? 147.436 161.883 167.080 1.00 49.26 ?  134 THR B N     1 
ATOM   6663  C  CA    . THR B 1 134 ? 148.081 160.907 167.953 1.00 45.20 ?  134 THR B CA    1 
ATOM   6664  C  C     . THR B 1 134 ? 147.127 160.404 169.030 1.00 47.30 ?  134 THR B C     1 
ATOM   6665  O  O     . THR B 1 134 ? 147.091 159.203 169.322 1.00 50.75 ?  134 THR B O     1 
ATOM   6666  C  CB    . THR B 1 134 ? 149.328 161.518 168.586 1.00 53.73 ?  134 THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 134 ? 150.193 162.000 167.552 1.00 55.93 ?  134 THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 134 ? 150.067 160.480 169.414 1.00 50.56 ?  134 THR B CG2   1 
ATOM   6669  N  N     . GLU B 1 135 ? 146.350 161.305 169.635 1.00 46.01 ?  135 GLU B N     1 
ATOM   6670  C  CA    . GLU B 1 135 ? 145.384 160.884 170.643 1.00 45.42 ?  135 GLU B CA    1 
ATOM   6671  C  C     . GLU B 1 135 ? 144.301 160.005 170.033 1.00 50.14 ?  135 GLU B C     1 
ATOM   6672  O  O     . GLU B 1 135 ? 143.881 159.015 170.641 1.00 51.83 ?  135 GLU B O     1 
ATOM   6673  C  CB    . GLU B 1 135 ? 144.769 162.105 171.324 1.00 47.74 ?  135 GLU B CB    1 
ATOM   6674  C  CG    . GLU B 1 135 ? 145.792 163.058 171.917 1.00 48.68 ?  135 GLU B CG    1 
ATOM   6675  C  CD    . GLU B 1 135 ? 146.905 162.336 172.649 1.00 55.32 ?  135 GLU B CD    1 
ATOM   6676  O  OE1   . GLU B 1 135 ? 146.612 161.636 173.641 1.00 54.01 ?  135 GLU B OE1   1 
ATOM   6677  O  OE2   . GLU B 1 135 ? 148.074 162.467 172.230 1.00 55.95 -1 135 GLU B OE2   1 
ATOM   6678  N  N     . LYS B 1 136 ? 143.838 160.353 168.831 1.00 40.63 ?  136 LYS B N     1 
ATOM   6679  C  CA    . LYS B 1 136 ? 142.865 159.514 168.140 1.00 38.65 ?  136 LYS B CA    1 
ATOM   6680  C  C     . LYS B 1 136 ? 143.453 158.147 167.812 1.00 39.71 ?  136 LYS B C     1 
ATOM   6681  O  O     . LYS B 1 136 ? 142.768 157.124 167.926 1.00 46.00 ?  136 LYS B O     1 
ATOM   6682  C  CB    . LYS B 1 136 ? 142.382 160.214 166.871 1.00 46.29 ?  136 LYS B CB    1 
ATOM   6683  C  CG    . LYS B 1 136 ? 141.105 159.653 166.283 1.00 41.83 ?  136 LYS B CG    1 
ATOM   6684  C  CD    . LYS B 1 136 ? 139.881 160.214 166.979 1.00 43.62 ?  136 LYS B CD    1 
ATOM   6685  C  CE    . LYS B 1 136 ? 138.616 159.901 166.200 1.00 46.52 ?  136 LYS B CE    1 
ATOM   6686  N  NZ    . LYS B 1 136 ? 137.450 160.671 166.712 1.00 49.13 1  136 LYS B NZ    1 
ATOM   6687  N  N     . ALA B 1 137 ? 144.721 158.109 167.395 1.00 34.81 ?  137 ALA B N     1 
ATOM   6688  C  CA    . ALA B 1 137 ? 145.372 156.833 167.118 1.00 31.55 ?  137 ALA B CA    1 
ATOM   6689  C  C     . ALA B 1 137 ? 145.477 155.984 168.377 1.00 35.22 ?  137 ALA B C     1 
ATOM   6690  O  O     . ALA B 1 137 ? 145.267 154.767 168.333 1.00 38.48 ?  137 ALA B O     1 
ATOM   6691  C  CB    . ALA B 1 137 ? 146.755 157.064 166.510 1.00 31.27 ?  137 ALA B CB    1 
ATOM   6692  N  N     . LYS B 1 138 ? 145.806 156.607 169.510 1.00 39.95 ?  138 LYS B N     1 
ATOM   6693  C  CA    . LYS B 1 138 ? 145.861 155.871 170.769 1.00 38.43 ?  138 LYS B CA    1 
ATOM   6694  C  C     . LYS B 1 138 ? 144.481 155.367 171.171 1.00 38.29 ?  138 LYS B C     1 
ATOM   6695  O  O     . LYS B 1 138 ? 144.348 154.265 171.715 1.00 41.57 ?  138 LYS B O     1 
ATOM   6696  C  CB    . LYS B 1 138 ? 146.456 156.753 171.866 1.00 46.55 ?  138 LYS B CB    1 
ATOM   6697  C  CG    . LYS B 1 138 ? 147.927 156.490 172.134 1.00 45.57 ?  138 LYS B CG    1 
ATOM   6698  C  CD    . LYS B 1 138 ? 148.726 157.779 172.179 1.00 42.75 ?  138 LYS B CD    1 
ATOM   6699  C  CE    . LYS B 1 138 ? 148.191 158.727 173.236 1.00 41.41 ?  138 LYS B CE    1 
ATOM   6700  N  NZ    . LYS B 1 138 ? 149.045 159.939 173.370 1.00 45.27 1  138 LYS B NZ    1 
ATOM   6701  N  N     . GLU B 1 139 ? 143.440 156.164 170.921 1.00 42.21 ?  139 GLU B N     1 
ATOM   6702  C  CA    . GLU B 1 139 ? 142.079 155.717 171.201 1.00 37.82 ?  139 GLU B CA    1 
ATOM   6703  C  C     . GLU B 1 139 ? 141.707 154.513 170.345 1.00 34.72 ?  139 GLU B C     1 
ATOM   6704  O  O     . GLU B 1 139 ? 141.094 153.559 170.837 1.00 43.86 ?  139 GLU B O     1 
ATOM   6705  C  CB    . GLU B 1 139 ? 141.094 156.862 170.978 1.00 36.39 ?  139 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 1 139 ? 140.617 157.520 172.256 1.00 41.29 ?  139 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 1 139 ? 140.419 159.014 172.106 1.00 49.30 ?  139 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 1 139 ? 139.895 159.443 171.056 1.00 46.90 ?  139 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 1 139 ? 140.785 159.759 173.037 1.00 47.07 -1 139 GLU B OE2   1 
ATOM   6710  N  N     . TYR B 1 140 ? 142.066 154.541 169.061 1.00 27.13 ?  140 TYR B N     1 
ATOM   6711  C  CA    . TYR B 1 140 ? 141.810 153.392 168.195 1.00 28.57 ?  140 TYR B CA    1 
ATOM   6712  C  C     . TYR B 1 140 ? 142.598 152.171 168.656 1.00 32.48 ?  140 TYR B C     1 
ATOM   6713  O  O     . TYR B 1 140 ? 142.095 151.041 168.605 1.00 35.20 ?  140 TYR B O     1 
ATOM   6714  C  CB    . TYR B 1 140 ? 142.159 153.728 166.748 1.00 31.21 ?  140 TYR B CB    1 
ATOM   6715  C  CG    . TYR B 1 140 ? 141.170 154.619 166.038 1.00 33.68 ?  140 TYR B CG    1 
ATOM   6716  C  CD1   . TYR B 1 140 ? 139.828 154.277 165.952 1.00 36.18 ?  140 TYR B CD1   1 
ATOM   6717  C  CD2   . TYR B 1 140 ? 141.586 155.794 165.433 1.00 34.26 ?  140 TYR B CD2   1 
ATOM   6718  C  CE1   . TYR B 1 140 ? 138.929 155.089 165.293 1.00 34.00 ?  140 TYR B CE1   1 
ATOM   6719  C  CE2   . TYR B 1 140 ? 140.697 156.609 164.776 1.00 32.61 ?  140 TYR B CE2   1 
ATOM   6720  C  CZ    . TYR B 1 140 ? 139.371 156.256 164.709 1.00 30.34 ?  140 TYR B CZ    1 
ATOM   6721  O  OH    . TYR B 1 140 ? 138.492 157.079 164.049 1.00 37.65 ?  140 TYR B OH    1 
ATOM   6722  N  N     . VAL B 1 141 ? 143.842 152.379 169.091 1.00 36.80 ?  141 VAL B N     1 
ATOM   6723  C  CA    . VAL B 1 141 ? 144.652 151.281 169.611 1.00 34.60 ?  141 VAL B CA    1 
ATOM   6724  C  C     . VAL B 1 141 ? 143.988 150.663 170.832 1.00 31.82 ?  141 VAL B C     1 
ATOM   6725  O  O     . VAL B 1 141 ? 143.913 149.439 170.961 1.00 38.24 ?  141 VAL B O     1 
ATOM   6726  C  CB    . VAL B 1 141 ? 146.076 151.767 169.936 1.00 36.80 ?  141 VAL B CB    1 
ATOM   6727  C  CG1   . VAL B 1 141 ? 146.736 150.833 170.921 1.00 35.04 ?  141 VAL B CG1   1 
ATOM   6728  C  CG2   . VAL B 1 141 ? 146.903 151.836 168.681 1.00 35.06 ?  141 VAL B CG2   1 
ATOM   6729  N  N     . ASN B 1 142 ? 143.503 151.498 171.749 1.00 33.90 ?  142 ASN B N     1 
ATOM   6730  C  CA    . ASN B 1 142 ? 142.825 150.974 172.930 1.00 33.04 ?  142 ASN B CA    1 
ATOM   6731  C  C     . ASN B 1 142 ? 141.541 150.252 172.547 1.00 34.96 ?  142 ASN B C     1 
ATOM   6732  O  O     . ASN B 1 142 ? 141.200 149.225 173.143 1.00 41.23 ?  142 ASN B O     1 
ATOM   6733  C  CB    . ASN B 1 142 ? 142.536 152.105 173.914 1.00 30.82 ?  142 ASN B CB    1 
ATOM   6734  C  CG    . ASN B 1 142 ? 143.768 152.531 174.684 1.00 36.66 ?  142 ASN B CG    1 
ATOM   6735  O  OD1   . ASN B 1 142 ? 144.501 151.697 175.213 1.00 37.28 ?  142 ASN B OD1   1 
ATOM   6736  N  ND2   . ASN B 1 142 ? 144.005 153.835 174.746 1.00 38.79 ?  142 ASN B ND2   1 
ATOM   6737  N  N     . LEU B 1 143 ? 140.817 150.774 171.557 1.00 34.18 ?  143 LEU B N     1 
ATOM   6738  C  CA    . LEU B 1 143 ? 139.572 150.146 171.132 1.00 28.75 ?  143 LEU B CA    1 
ATOM   6739  C  C     . LEU B 1 143 ? 139.814 148.773 170.518 1.00 32.78 ?  143 LEU B C     1 
ATOM   6740  O  O     . LEU B 1 143 ? 139.052 147.834 170.767 1.00 36.15 ?  143 LEU B O     1 
ATOM   6741  C  CB    . LEU B 1 143 ? 138.844 151.054 170.144 1.00 28.80 ?  143 LEU B CB    1 
ATOM   6742  C  CG    . LEU B 1 143 ? 137.335 150.852 170.049 1.00 34.07 ?  143 LEU B CG    1 
ATOM   6743  C  CD1   . LEU B 1 143 ? 136.665 151.381 171.302 1.00 32.88 ?  143 LEU B CD1   1 
ATOM   6744  C  CD2   . LEU B 1 143 ? 136.793 151.539 168.814 1.00 33.46 ?  143 LEU B CD2   1 
ATOM   6745  N  N     . MET B 1 144 ? 140.864 148.636 169.709 1.00 34.58 ?  144 MET B N     1 
ATOM   6746  C  CA    . MET B 1 144 ? 141.104 147.386 168.998 1.00 24.95 ?  144 MET B CA    1 
ATOM   6747  C  C     . MET B 1 144 ? 141.901 146.370 169.806 1.00 25.64 ?  144 MET B C     1 
ATOM   6748  O  O     . MET B 1 144 ? 141.652 145.166 169.682 1.00 34.30 ?  144 MET B O     1 
ATOM   6749  C  CB    . MET B 1 144 ? 141.814 147.665 167.672 1.00 27.95 ?  144 MET B CB    1 
ATOM   6750  C  CG    . MET B 1 144 ? 140.970 148.454 166.686 1.00 28.00 ?  144 MET B CG    1 
ATOM   6751  S  SD    . MET B 1 144 ? 141.694 148.520 165.041 1.00 45.60 ?  144 MET B SD    1 
ATOM   6752  C  CE    . MET B 1 144 ? 143.116 149.555 165.355 1.00 26.96 ?  144 MET B CE    1 
ATOM   6753  N  N     . ILE B 1 145 ? 142.860 146.815 170.622 1.00 28.38 ?  145 ILE B N     1 
ATOM   6754  C  CA    . ILE B 1 145 ? 143.608 145.882 171.458 1.00 29.34 ?  145 ILE B CA    1 
ATOM   6755  C  C     . ILE B 1 145 ? 142.728 145.349 172.580 1.00 35.80 ?  145 ILE B C     1 
ATOM   6756  O  O     . ILE B 1 145 ? 142.901 144.207 173.023 1.00 39.90 ?  145 ILE B O     1 
ATOM   6757  C  CB    . ILE B 1 145 ? 144.898 146.543 171.986 1.00 31.03 ?  145 ILE B CB    1 
ATOM   6758  C  CG1   . ILE B 1 145 ? 145.995 145.494 172.183 1.00 32.44 ?  145 ILE B CG1   1 
ATOM   6759  C  CG2   . ILE B 1 145 ? 144.653 147.303 173.282 1.00 33.30 ?  145 ILE B CG2   1 
ATOM   6760  C  CD1   . ILE B 1 145 ? 146.520 144.907 170.896 1.00 35.50 ?  145 ILE B CD1   1 
ATOM   6761  N  N     . ASN B 1 146 ? 141.771 146.150 173.056 1.00 33.84 ?  146 ASN B N     1 
ATOM   6762  C  CA    . ASN B 1 146 ? 140.733 145.633 173.935 1.00 27.26 ?  146 ASN B CA    1 
ATOM   6763  C  C     . ASN B 1 146 ? 139.729 144.780 173.179 1.00 29.59 ?  146 ASN B C     1 
ATOM   6764  O  O     . ASN B 1 146 ? 138.882 144.142 173.813 1.00 38.22 ?  146 ASN B O     1 
ATOM   6765  C  CB    . ASN B 1 146 ? 140.008 146.778 174.640 1.00 27.33 ?  146 ASN B CB    1 
ATOM   6766  C  CG    . ASN B 1 146 ? 140.874 147.467 175.672 1.00 33.18 ?  146 ASN B CG    1 
ATOM   6767  O  OD1   . ASN B 1 146 ? 141.874 146.916 176.127 1.00 41.26 ?  146 ASN B OD1   1 
ATOM   6768  N  ND2   . ASN B 1 146 ? 140.493 148.682 176.045 1.00 34.54 ?  146 ASN B ND2   1 
ATOM   6769  N  N     . GLN B 1 147 ? 139.809 144.768 171.849 1.00 33.55 ?  147 GLN B N     1 
ATOM   6770  C  CA    . GLN B 1 147 ? 138.955 143.948 170.996 1.00 24.10 ?  147 GLN B CA    1 
ATOM   6771  C  C     . GLN B 1 147 ? 137.484 144.298 171.184 1.00 23.97 ?  147 GLN B C     1 
ATOM   6772  O  O     . GLN B 1 147 ? 136.615 143.429 171.166 1.00 38.00 ?  147 GLN B O     1 
ATOM   6773  C  CB    . GLN B 1 147 ? 139.205 142.459 171.238 1.00 23.94 ?  147 GLN B CB    1 
ATOM   6774  C  CG    . GLN B 1 147 ? 140.570 141.995 170.769 1.00 24.48 ?  147 GLN B CG    1 
ATOM   6775  C  CD    . GLN B 1 147 ? 140.655 140.497 170.619 1.00 31.06 ?  147 GLN B CD    1 
ATOM   6776  O  OE1   . GLN B 1 147 ? 140.189 139.748 171.477 1.00 41.78 ?  147 GLN B OE1   1 
ATOM   6777  N  NE2   . GLN B 1 147 ? 141.254 140.046 169.525 1.00 31.16 ?  147 GLN B NE2   1 
ATOM   6778  N  N     . GLU B 1 148 ? 137.206 145.587 171.382 1.00 25.67 ?  148 GLU B N     1 
ATOM   6779  C  CA    . GLU B 1 148 ? 135.826 146.056 171.402 1.00 23.25 ?  148 GLU B CA    1 
ATOM   6780  C  C     . GLU B 1 148 ? 135.290 146.288 169.999 1.00 29.08 ?  148 GLU B C     1 
ATOM   6781  O  O     . GLU B 1 148 ? 134.096 146.087 169.754 1.00 35.96 ?  148 GLU B O     1 
ATOM   6782  C  CB    . GLU B 1 148 ? 135.716 147.346 172.212 1.00 18.14 ?  148 GLU B CB    1 
ATOM   6783  C  CG    . GLU B 1 148 ? 136.082 147.206 173.672 1.00 21.97 ?  148 GLU B CG    1 
ATOM   6784  C  CD    . GLU B 1 148 ? 136.445 148.534 174.300 1.00 35.44 ?  148 GLU B CD    1 
ATOM   6785  O  OE1   . GLU B 1 148 ? 137.576 149.009 174.077 1.00 35.25 ?  148 GLU B OE1   1 
ATOM   6786  O  OE2   . GLU B 1 148 ? 135.596 149.108 175.014 1.00 42.82 -1 148 GLU B OE2   1 
ATOM   6787  N  N     . TYR B 1 149 ? 136.149 146.709 169.076 1.00 26.98 ?  149 TYR B N     1 
ATOM   6788  C  CA    . TYR B 1 149 ? 135.769 146.957 167.694 1.00 19.69 ?  149 TYR B CA    1 
ATOM   6789  C  C     . TYR B 1 149 ? 136.754 146.254 166.777 1.00 24.35 ?  149 TYR B C     1 
ATOM   6790  O  O     . TYR B 1 149 ? 137.969 146.365 166.963 1.00 32.74 ?  149 TYR B O     1 
ATOM   6791  C  CB    . TYR B 1 149 ? 135.741 148.454 167.383 1.00 22.94 ?  149 TYR B CB    1 
ATOM   6792  C  CG    . TYR B 1 149 ? 135.620 148.766 165.911 1.00 24.46 ?  149 TYR B CG    1 
ATOM   6793  C  CD1   . TYR B 1 149 ? 134.496 148.386 165.193 1.00 19.89 ?  149 TYR B CD1   1 
ATOM   6794  C  CD2   . TYR B 1 149 ? 136.633 149.435 165.239 1.00 17.39 ?  149 TYR B CD2   1 
ATOM   6795  C  CE1   . TYR B 1 149 ? 134.383 148.667 163.848 1.00 19.99 ?  149 TYR B CE1   1 
ATOM   6796  C  CE2   . TYR B 1 149 ? 136.528 149.719 163.896 1.00 24.90 ?  149 TYR B CE2   1 
ATOM   6797  C  CZ    . TYR B 1 149 ? 135.400 149.335 163.205 1.00 20.08 ?  149 TYR B CZ    1 
ATOM   6798  O  OH    . TYR B 1 149 ? 135.290 149.615 161.864 1.00 16.11 ?  149 TYR B OH    1 
ATOM   6799  N  N     . GLN B 1 150 ? 136.228 145.535 165.796 1.00 19.57 ?  150 GLN B N     1 
ATOM   6800  C  CA    . GLN B 1 150 ? 137.049 144.853 164.798 1.00 12.37 ?  150 GLN B CA    1 
ATOM   6801  C  C     . GLN B 1 150 ? 136.743 145.416 163.421 1.00 20.86 ?  150 GLN B C     1 
ATOM   6802  O  O     . GLN B 1 150 ? 135.618 145.234 162.919 1.00 32.26 ?  150 GLN B O     1 
ATOM   6803  C  CB    . GLN B 1 150 ? 136.796 143.346 164.829 1.00 19.69 ?  150 GLN B CB    1 
ATOM   6804  C  CG    . GLN B 1 150 ? 137.468 142.559 163.716 1.00 20.88 ?  150 GLN B CG    1 
ATOM   6805  C  CD    . GLN B 1 150 ? 138.966 142.765 163.672 1.00 20.38 ?  150 GLN B CD    1 
ATOM   6806  O  OE1   . GLN B 1 150 ? 139.686 142.369 164.585 1.00 27.08 ?  150 GLN B OE1   1 
ATOM   6807  N  NE2   . GLN B 1 150 ? 139.445 143.382 162.600 1.00 15.99 ?  150 GLN B NE2   1 
ATOM   6808  N  N     . PRO B 1 151 ? 137.680 146.108 162.779 1.00 27.09 ?  151 PRO B N     1 
ATOM   6809  C  CA    . PRO B 1 151 ? 137.481 146.482 161.377 1.00 14.54 ?  151 PRO B CA    1 
ATOM   6810  C  C     . PRO B 1 151 ? 137.350 145.239 160.514 1.00 20.56 ?  151 PRO B C     1 
ATOM   6811  O  O     . PRO B 1 151 ? 137.878 144.172 160.839 1.00 29.40 ?  151 PRO B O     1 
ATOM   6812  C  CB    . PRO B 1 151 ? 138.744 147.278 161.033 1.00 18.53 ?  151 PRO B CB    1 
ATOM   6813  C  CG    . PRO B 1 151 ? 139.309 147.696 162.348 1.00 20.87 ?  151 PRO B CG    1 
ATOM   6814  C  CD    . PRO B 1 151 ? 138.951 146.619 163.316 1.00 17.91 ?  151 PRO B CD    1 
ATOM   6815  N  N     . SER B 1 152 ? 136.622 145.379 159.411 1.00 24.85 ?  152 SER B N     1 
ATOM   6816  C  CA    . SER B 1 152 ? 136.359 144.243 158.543 1.00 18.45 ?  152 SER B CA    1 
ATOM   6817  C  C     . SER B 1 152 ? 137.661 143.658 158.003 1.00 24.70 ?  152 SER B C     1 
ATOM   6818  O  O     . SER B 1 152 ? 138.727 144.274 158.067 1.00 25.54 ?  152 SER B O     1 
ATOM   6819  C  CB    . SER B 1 152 ? 135.453 144.653 157.385 1.00 21.43 ?  152 SER B CB    1 
ATOM   6820  O  OG    . SER B 1 152 ? 136.102 145.578 156.534 1.00 26.76 ?  152 SER B OG    1 
ATOM   6821  N  N     . THR B 1 153 ? 137.558 142.440 157.475 1.00 32.55 ?  153 THR B N     1 
ATOM   6822  C  CA    . THR B 1 153 ? 138.720 141.772 156.895 1.00 20.41 ?  153 THR B CA    1 
ATOM   6823  C  C     . THR B 1 153 ? 139.450 142.622 155.859 1.00 31.50 ?  153 THR B C     1 
ATOM   6824  O  O     . THR B 1 153 ? 140.688 142.694 155.933 1.00 34.82 ?  153 THR B O     1 
ATOM   6825  C  CB    . THR B 1 153 ? 138.291 140.424 156.294 1.00 27.31 ?  153 THR B CB    1 
ATOM   6826  O  OG1   . THR B 1 153 ? 137.991 139.502 157.348 1.00 33.85 ?  153 THR B OG1   1 
ATOM   6827  C  CG2   . THR B 1 153 ? 139.392 139.845 155.423 1.00 30.48 ?  153 THR B CG2   1 
ATOM   6828  N  N     . PRO B 1 154 ? 138.786 143.288 154.905 1.00 33.93 ?  154 PRO B N     1 
ATOM   6829  C  CA    . PRO B 1 154 ? 139.543 144.174 154.001 1.00 21.38 ?  154 PRO B CA    1 
ATOM   6830  C  C     . PRO B 1 154 ? 140.265 145.294 154.727 1.00 22.56 ?  154 PRO B C     1 
ATOM   6831  O  O     . PRO B 1 154 ? 141.459 145.515 154.490 1.00 31.19 ?  154 PRO B O     1 
ATOM   6832  C  CB    . PRO B 1 154 ? 138.458 144.709 153.056 1.00 24.01 ?  154 PRO B CB    1 
ATOM   6833  C  CG    . PRO B 1 154 ? 137.370 143.724 153.135 1.00 22.70 ?  154 PRO B CG    1 
ATOM   6834  C  CD    . PRO B 1 154 ? 137.362 143.233 154.531 1.00 25.54 ?  154 PRO B CD    1 
ATOM   6835  N  N     . THR B 1 155 ? 139.572 146.007 155.616 1.00 25.99 ?  155 THR B N     1 
ATOM   6836  C  CA    . THR B 1 155 ? 140.197 147.118 156.326 1.00 22.14 ?  155 THR B CA    1 
ATOM   6837  C  C     . THR B 1 155 ? 141.321 146.633 157.231 1.00 25.99 ?  155 THR B C     1 
ATOM   6838  O  O     . THR B 1 155 ? 142.434 147.166 157.198 1.00 25.30 ?  155 THR B O     1 
ATOM   6839  C  CB    . THR B 1 155 ? 139.148 147.877 157.139 1.00 23.99 ?  155 THR B CB    1 
ATOM   6840  O  OG1   . THR B 1 155 ? 138.034 148.202 156.300 1.00 26.39 ?  155 THR B OG1   1 
ATOM   6841  C  CG2   . THR B 1 155 ? 139.740 149.153 157.699 1.00 20.80 ?  155 THR B CG2   1 
ATOM   6842  N  N     . PHE B 1 156 ? 141.050 145.612 158.047 1.00 30.04 ?  156 PHE B N     1 
ATOM   6843  C  CA    . PHE B 1 156 ? 142.058 145.122 158.981 1.00 21.34 ?  156 PHE B CA    1 
ATOM   6844  C  C     . PHE B 1 156 ? 143.271 144.565 158.247 1.00 29.13 ?  156 PHE B C     1 
ATOM   6845  O  O     . PHE B 1 156 ? 144.413 144.781 158.666 1.00 32.96 ?  156 PHE B O     1 
ATOM   6846  C  CB    . PHE B 1 156 ? 141.450 144.062 159.898 1.00 26.41 ?  156 PHE B CB    1 
ATOM   6847  C  CG    . PHE B 1 156 ? 142.233 143.826 161.155 1.00 30.29 ?  156 PHE B CG    1 
ATOM   6848  C  CD1   . PHE B 1 156 ? 142.504 144.870 162.022 1.00 28.22 ?  156 PHE B CD1   1 
ATOM   6849  C  CD2   . PHE B 1 156 ? 142.698 142.561 161.471 1.00 23.06 ?  156 PHE B CD2   1 
ATOM   6850  C  CE1   . PHE B 1 156 ? 143.226 144.658 163.177 1.00 30.39 ?  156 PHE B CE1   1 
ATOM   6851  C  CE2   . PHE B 1 156 ? 143.418 142.344 162.626 1.00 25.10 ?  156 PHE B CE2   1 
ATOM   6852  C  CZ    . PHE B 1 156 ? 143.682 143.394 163.480 1.00 30.21 ?  156 PHE B CZ    1 
ATOM   6853  N  N     . LEU B 1 157 ? 143.043 143.844 157.151 1.00 32.80 ?  157 LEU B N     1 
ATOM   6854  C  CA    . LEU B 1 157 ? 144.140 143.211 156.431 1.00 27.12 ?  157 LEU B CA    1 
ATOM   6855  C  C     . LEU B 1 157 ? 144.957 144.224 155.637 1.00 33.90 ?  157 LEU B C     1 
ATOM   6856  O  O     . LEU B 1 157 ? 146.188 144.127 155.583 1.00 41.74 ?  157 LEU B O     1 
ATOM   6857  C  CB    . LEU B 1 157 ? 143.589 142.126 155.508 1.00 32.38 ?  157 LEU B CB    1 
ATOM   6858  C  CG    . LEU B 1 157 ? 144.551 141.508 154.496 1.00 33.14 ?  157 LEU B CG    1 
ATOM   6859  C  CD1   . LEU B 1 157 ? 145.586 140.656 155.200 1.00 33.58 ?  157 LEU B CD1   1 
ATOM   6860  C  CD2   . LEU B 1 157 ? 143.788 140.691 153.470 1.00 30.09 ?  157 LEU B CD2   1 
ATOM   6861  N  N     . ASN B 1 158 ? 144.299 145.205 155.019 1.00 35.49 ?  158 ASN B N     1 
ATOM   6862  C  CA    . ASN B 1 158 ? 144.947 146.015 153.998 1.00 28.83 ?  158 ASN B CA    1 
ATOM   6863  C  C     . ASN B 1 158 ? 145.336 147.414 154.454 1.00 32.73 ?  158 ASN B C     1 
ATOM   6864  O  O     . ASN B 1 158 ? 146.144 148.055 153.775 1.00 39.64 ?  158 ASN B O     1 
ATOM   6865  C  CB    . ASN B 1 158 ? 144.036 146.132 152.770 1.00 33.04 ?  158 ASN B CB    1 
ATOM   6866  C  CG    . ASN B 1 158 ? 143.858 144.813 152.051 1.00 38.50 ?  158 ASN B CG    1 
ATOM   6867  O  OD1   . ASN B 1 158 ? 144.817 144.070 151.848 1.00 39.97 ?  158 ASN B OD1   1 
ATOM   6868  N  ND2   . ASN B 1 158 ? 142.626 144.512 151.663 1.00 36.86 ?  158 ASN B ND2   1 
ATOM   6869  N  N     . ALA B 1 159 ? 144.798 147.907 155.568 1.00 32.24 ?  159 ALA B N     1 
ATOM   6870  C  CA    . ALA B 1 159 ? 145.069 149.282 155.971 1.00 32.52 ?  159 ALA B CA    1 
ATOM   6871  C  C     . ALA B 1 159 ? 146.558 149.493 156.211 1.00 38.45 ?  159 ALA B C     1 
ATOM   6872  O  O     . ALA B 1 159 ? 147.198 148.731 156.941 1.00 44.26 ?  159 ALA B O     1 
ATOM   6873  C  CB    . ALA B 1 159 ? 144.280 149.636 157.230 1.00 33.14 ?  159 ALA B CB    1 
ATOM   6874  N  N     . GLY B 1 160 ? 147.106 150.536 155.594 1.00 43.15 ?  160 GLY B N     1 
ATOM   6875  C  CA    . GLY B 1 160 ? 148.511 150.844 155.745 1.00 38.96 ?  160 GLY B CA    1 
ATOM   6876  C  C     . GLY B 1 160 ? 149.462 149.940 154.998 1.00 41.97 ?  160 GLY B C     1 
ATOM   6877  O  O     . GLY B 1 160 ? 150.633 149.850 155.375 1.00 50.62 ?  160 GLY B O     1 
ATOM   6878  N  N     . ARG B 1 161 ? 149.001 149.263 153.951 1.00 44.25 ?  161 ARG B N     1 
ATOM   6879  C  CA    . ARG B 1 161 ? 149.837 148.374 153.160 1.00 44.56 ?  161 ARG B CA    1 
ATOM   6880  C  C     . ARG B 1 161 ? 149.983 148.915 151.744 1.00 48.02 ?  161 ARG B C     1 
ATOM   6881  O  O     . ARG B 1 161 ? 149.004 149.351 151.132 1.00 49.36 ?  161 ARG B O     1 
ATOM   6882  C  CB    . ARG B 1 161 ? 149.254 146.959 153.118 1.00 41.42 ?  161 ARG B CB    1 
ATOM   6883  C  CG    . ARG B 1 161 ? 149.335 146.219 154.440 1.00 41.80 ?  161 ARG B CG    1 
ATOM   6884  C  CD    . ARG B 1 161 ? 149.301 144.718 154.227 1.00 42.34 ?  161 ARG B CD    1 
ATOM   6885  N  NE    . ARG B 1 161 ? 149.254 143.992 155.489 1.00 44.00 ?  161 ARG B NE    1 
ATOM   6886  C  CZ    . ARG B 1 161 ? 148.927 142.713 155.606 1.00 46.38 ?  161 ARG B CZ    1 
ATOM   6887  N  NH1   . ARG B 1 161 ? 148.623 141.978 154.549 1.00 49.01 1  161 ARG B NH1   1 
ATOM   6888  N  NH2   . ARG B 1 161 ? 148.904 142.157 156.814 1.00 45.53 ?  161 ARG B NH2   1 
ATOM   6889  N  N     . LYS B 1 162 ? 151.216 148.889 151.232 1.00 57.73 ?  162 LYS B N     1 
ATOM   6890  C  CA    . LYS B 1 162 ? 151.475 149.397 149.889 1.00 57.20 ?  162 LYS B CA    1 
ATOM   6891  C  C     . LYS B 1 162 ? 150.839 148.505 148.830 1.00 58.40 ?  162 LYS B C     1 
ATOM   6892  O  O     . LYS B 1 162 ? 150.149 148.991 147.926 1.00 60.39 ?  162 LYS B O     1 
ATOM   6893  C  CB    . LYS B 1 162 ? 152.981 149.518 149.659 1.00 57.41 ?  162 LYS B CB    1 
ATOM   6894  C  CG    . LYS B 1 162 ? 153.376 149.767 148.216 1.00 59.42 ?  162 LYS B CG    1 
ATOM   6895  C  CD    . LYS B 1 162 ? 153.306 151.244 147.875 1.00 58.54 ?  162 LYS B CD    1 
ATOM   6896  C  CE    . LYS B 1 162 ? 154.351 152.035 148.644 1.00 57.34 ?  162 LYS B CE    1 
ATOM   6897  N  NZ    . LYS B 1 162 ? 154.020 153.486 148.698 1.00 58.40 1  162 LYS B NZ    1 
ATOM   6898  N  N     . ARG B 1 163 ? 151.058 147.195 148.925 1.00 57.99 ?  163 ARG B N     1 
ATOM   6899  C  CA    . ARG B 1 163 ? 150.478 146.240 147.981 1.00 60.65 ?  163 ARG B CA    1 
ATOM   6900  C  C     . ARG B 1 163 ? 149.179 145.664 148.547 1.00 62.84 ?  163 ARG B C     1 
ATOM   6901  O  O     . ARG B 1 163 ? 149.069 144.484 148.877 1.00 61.14 ?  163 ARG B O     1 
ATOM   6902  C  CB    . ARG B 1 163 ? 151.480 145.139 147.655 1.00 61.32 ?  163 ARG B CB    1 
ATOM   6903  C  CG    . ARG B 1 163 ? 152.563 145.556 146.675 1.00 62.25 ?  163 ARG B CG    1 
ATOM   6904  C  CD    . ARG B 1 163 ? 153.730 144.589 146.708 1.00 61.92 ?  163 ARG B CD    1 
ATOM   6905  N  NE    . ARG B 1 163 ? 154.604 144.827 147.850 1.00 64.82 ?  163 ARG B NE    1 
ATOM   6906  C  CZ    . ARG B 1 163 ? 155.360 143.899 148.420 1.00 66.36 ?  163 ARG B CZ    1 
ATOM   6907  N  NH1   . ARG B 1 163 ? 155.373 142.652 147.979 1.00 63.10 1  163 ARG B NH1   1 
ATOM   6908  N  NH2   . ARG B 1 163 ? 156.122 144.231 149.458 1.00 62.68 ?  163 ARG B NH2   1 
ATOM   6909  N  N     . ARG B 1 164 ? 148.184 146.537 148.651 1.00 56.69 ?  164 ARG B N     1 
ATOM   6910  C  CA    . ARG B 1 164 ? 146.915 146.213 149.278 1.00 53.92 ?  164 ARG B CA    1 
ATOM   6911  C  C     . ARG B 1 164 ? 145.789 146.231 148.256 1.00 53.28 ?  164 ARG B C     1 
ATOM   6912  O  O     . ARG B 1 164 ? 145.864 146.914 147.230 1.00 52.80 ?  164 ARG B O     1 
ATOM   6913  C  CB    . ARG B 1 164 ? 146.592 147.201 150.404 1.00 52.22 ?  164 ARG B CB    1 
ATOM   6914  C  CG    . ARG B 1 164 ? 146.103 148.559 149.914 1.00 51.00 ?  164 ARG B CG    1 
ATOM   6915  C  CD    . ARG B 1 164 ? 145.583 149.412 151.058 1.00 53.16 ?  164 ARG B CD    1 
ATOM   6916  N  NE    . ARG B 1 164 ? 145.315 150.788 150.658 1.00 53.94 ?  164 ARG B NE    1 
ATOM   6917  C  CZ    . ARG B 1 164 ? 144.237 151.178 149.988 1.00 56.41 ?  164 ARG B CZ    1 
ATOM   6918  N  NH1   . ARG B 1 164 ? 143.301 150.318 149.622 1.00 51.21 1  164 ARG B NH1   1 
ATOM   6919  N  NH2   . ARG B 1 164 ? 144.097 152.463 149.680 1.00 56.21 ?  164 ARG B NH2   1 
ATOM   6920  N  N     . GLY B 1 165 ? 144.747 145.454 148.540 1.00 50.68 ?  165 GLY B N     1 
ATOM   6921  C  CA    . GLY B 1 165 ? 143.492 145.594 147.841 1.00 47.35 ?  165 GLY B CA    1 
ATOM   6922  C  C     . GLY B 1 165 ? 142.685 146.741 148.409 1.00 51.38 ?  165 GLY B C     1 
ATOM   6923  O  O     . GLY B 1 165 ? 143.122 147.481 149.289 1.00 52.32 ?  165 GLY B O     1 
ATOM   6924  N  N     . GLU B 1 166 ? 141.474 146.892 147.887 1.00 48.09 ?  166 GLU B N     1 
ATOM   6925  C  CA    . GLU B 1 166 ? 140.589 147.931 148.388 1.00 42.72 ?  166 GLU B CA    1 
ATOM   6926  C  C     . GLU B 1 166 ? 140.137 147.606 149.807 1.00 42.86 ?  166 GLU B C     1 
ATOM   6927  O  O     . GLU B 1 166 ? 140.071 146.443 150.213 1.00 39.32 ?  166 GLU B O     1 
ATOM   6928  C  CB    . GLU B 1 166 ? 139.378 148.092 147.469 1.00 41.35 ?  166 GLU B CB    1 
ATOM   6929  C  CG    . GLU B 1 166 ? 138.975 149.538 147.224 1.00 45.08 ?  166 GLU B CG    1 
ATOM   6930  C  CD    . GLU B 1 166 ? 140.042 150.332 146.491 1.00 49.94 ?  166 GLU B CD    1 
ATOM   6931  O  OE1   . GLU B 1 166 ? 140.848 149.720 145.759 1.00 49.58 ?  166 GLU B OE1   1 
ATOM   6932  O  OE2   . GLU B 1 166 ? 140.075 151.570 146.648 1.00 48.28 -1 166 GLU B OE2   1 
ATOM   6933  N  N     . LEU B 1 167 ? 139.832 148.655 150.570 1.00 38.04 ?  167 LEU B N     1 
ATOM   6934  C  CA    . LEU B 1 167 ? 139.318 148.481 151.921 1.00 32.21 ?  167 LEU B CA    1 
ATOM   6935  C  C     . LEU B 1 167 ? 137.836 148.136 151.943 1.00 35.31 ?  167 LEU B C     1 
ATOM   6936  O  O     . LEU B 1 167 ? 137.306 147.815 153.011 1.00 38.65 ?  167 LEU B O     1 
ATOM   6937  C  CB    . LEU B 1 167 ? 139.568 149.748 152.745 1.00 33.90 ?  167 LEU B CB    1 
ATOM   6938  C  CG    . LEU B 1 167 ? 140.802 149.769 153.651 1.00 34.71 ?  167 LEU B CG    1 
ATOM   6939  C  CD1   . LEU B 1 167 ? 142.014 149.180 152.952 1.00 31.87 ?  167 LEU B CD1   1 
ATOM   6940  C  CD2   . LEU B 1 167 ? 141.090 151.184 154.108 1.00 32.27 ?  167 LEU B CD2   1 
ATOM   6941  N  N     . VAL B 1 168 ? 137.166 148.195 150.797 1.00 36.93 ?  168 VAL B N     1 
ATOM   6942  C  CA    . VAL B 1 168 ? 135.767 147.810 150.660 1.00 28.61 ?  168 VAL B CA    1 
ATOM   6943  C  C     . VAL B 1 168 ? 135.711 146.534 149.833 1.00 33.31 ?  168 VAL B C     1 
ATOM   6944  O  O     . VAL B 1 168 ? 136.431 146.399 148.838 1.00 39.76 ?  168 VAL B O     1 
ATOM   6945  C  CB    . VAL B 1 168 ? 134.937 148.931 150.003 1.00 27.73 ?  168 VAL B CB    1 
ATOM   6946  C  CG1   . VAL B 1 168 ? 133.470 148.541 149.925 1.00 34.50 ?  168 VAL B CG1   1 
ATOM   6947  C  CG2   . VAL B 1 168 ? 135.106 150.231 150.765 1.00 31.65 ?  168 VAL B CG2   1 
ATOM   6948  N  N     . SER B 1 169 ? 134.866 145.592 150.252 1.00 29.47 ?  169 SER B N     1 
ATOM   6949  C  CA    . SER B 1 169 ? 134.723 144.335 149.536 1.00 29.73 ?  169 SER B CA    1 
ATOM   6950  C  C     . SER B 1 169 ? 133.293 144.003 149.137 1.00 31.28 ?  169 SER B C     1 
ATOM   6951  O  O     . SER B 1 169 ? 133.076 142.967 148.504 1.00 40.22 ?  169 SER B O     1 
ATOM   6952  C  CB    . SER B 1 169 ? 135.291 143.173 150.363 1.00 36.48 ?  169 SER B CB    1 
ATOM   6953  O  OG    . SER B 1 169 ? 136.682 143.025 150.138 1.00 43.76 ?  169 SER B OG    1 
ATOM   6954  N  N     . CYS B 1 170 ? 132.317 144.833 149.488 1.00 25.02 ?  170 CYS B N     1 
ATOM   6955  C  CA    . CYS B 1 170 ? 130.936 144.624 149.076 1.00 23.57 ?  170 CYS B CA    1 
ATOM   6956  C  C     . CYS B 1 170 ? 130.526 145.759 148.153 1.00 23.82 ?  170 CYS B C     1 
ATOM   6957  O  O     . CYS B 1 170 ? 130.612 146.933 148.528 1.00 31.72 ?  170 CYS B O     1 
ATOM   6958  C  CB    . CYS B 1 170 ? 129.998 144.527 150.284 1.00 34.88 ?  170 CYS B CB    1 
ATOM   6959  S  SG    . CYS B 1 170 ? 130.062 145.907 151.445 1.00 46.19 ?  170 CYS B SG    1 
ATOM   6960  N  N     . PHE B 1 171 ? 130.094 145.409 146.946 1.00 25.86 ?  171 PHE B N     1 
ATOM   6961  C  CA    . PHE B 1 171 ? 129.633 146.371 145.958 1.00 11.61 ?  171 PHE B CA    1 
ATOM   6962  C  C     . PHE B 1 171 ? 128.309 145.897 145.386 1.00 16.26 ?  171 PHE B C     1 
ATOM   6963  O  O     . PHE B 1 171 ? 128.087 144.694 145.226 1.00 24.49 ?  171 PHE B O     1 
ATOM   6964  C  CB    . PHE B 1 171 ? 130.659 146.558 144.836 1.00 17.72 ?  171 PHE B CB    1 
ATOM   6965  C  CG    . PHE B 1 171 ? 132.037 146.873 145.329 1.00 17.83 ?  171 PHE B CG    1 
ATOM   6966  C  CD1   . PHE B 1 171 ? 132.376 148.161 145.692 1.00 19.98 ?  171 PHE B CD1   1 
ATOM   6967  C  CD2   . PHE B 1 171 ? 132.994 145.880 145.429 1.00 19.73 ?  171 PHE B CD2   1 
ATOM   6968  C  CE1   . PHE B 1 171 ? 133.640 148.454 146.151 1.00 13.29 ?  171 PHE B CE1   1 
ATOM   6969  C  CE2   . PHE B 1 171 ? 134.259 146.168 145.887 1.00 17.80 ?  171 PHE B CE2   1 
ATOM   6970  C  CZ    . PHE B 1 171 ? 134.583 147.458 146.247 1.00 10.83 ?  171 PHE B CZ    1 
ATOM   6971  N  N     . LEU B 1 172 ? 127.430 146.848 145.086 1.00 14.93 ?  172 LEU B N     1 
ATOM   6972  C  CA    . LEU B 1 172 ? 126.109 146.560 144.544 1.00 7.54  ?  172 LEU B CA    1 
ATOM   6973  C  C     . LEU B 1 172 ? 125.917 147.398 143.293 1.00 13.54 ?  172 LEU B C     1 
ATOM   6974  O  O     . LEU B 1 172 ? 125.895 148.630 143.369 1.00 21.70 ?  172 LEU B O     1 
ATOM   6975  C  CB    . LEU B 1 172 ? 125.008 146.861 145.564 1.00 8.45  ?  172 LEU B CB    1 
ATOM   6976  C  CG    . LEU B 1 172 ? 124.901 145.998 146.820 1.00 2.85  ?  172 LEU B CG    1 
ATOM   6977  C  CD1   . LEU B 1 172 ? 125.926 146.410 147.861 1.00 11.18 ?  172 LEU B CD1   1 
ATOM   6978  C  CD2   . LEU B 1 172 ? 123.505 146.106 147.383 1.00 16.09 ?  172 LEU B CD2   1 
ATOM   6979  N  N     . LEU B 1 173 ? 125.765 146.735 142.153 1.00 20.16 ?  173 LEU B N     1 
ATOM   6980  C  CA    . LEU B 1 173 ? 125.651 147.402 140.865 1.00 8.80  ?  173 LEU B CA    1 
ATOM   6981  C  C     . LEU B 1 173 ? 124.249 147.235 140.299 1.00 18.02 ?  173 LEU B C     1 
ATOM   6982  O  O     . LEU B 1 173 ? 123.679 146.141 140.335 1.00 29.94 ?  173 LEU B O     1 
ATOM   6983  C  CB    . LEU B 1 173 ? 126.668 146.848 139.867 1.00 13.72 ?  173 LEU B CB    1 
ATOM   6984  C  CG    . LEU B 1 173 ? 128.124 146.731 140.310 1.00 19.57 ?  173 LEU B CG    1 
ATOM   6985  C  CD1   . LEU B 1 173 ? 128.966 146.263 139.140 1.00 22.40 ?  173 LEU B CD1   1 
ATOM   6986  C  CD2   . LEU B 1 173 ? 128.636 148.053 140.848 1.00 25.38 ?  173 LEU B CD2   1 
ATOM   6987  N  N     . GLU B 1 174 ? 123.699 148.327 139.784 1.00 26.42 ?  174 GLU B N     1 
ATOM   6988  C  CA    . GLU B 1 174 ? 122.489 148.278 138.979 1.00 22.09 ?  174 GLU B CA    1 
ATOM   6989  C  C     . GLU B 1 174 ? 122.871 148.091 137.519 1.00 20.40 ?  174 GLU B C     1 
ATOM   6990  O  O     . GLU B 1 174 ? 123.786 148.749 137.017 1.00 31.33 ?  174 GLU B O     1 
ATOM   6991  C  CB    . GLU B 1 174 ? 121.674 149.561 139.143 1.00 26.22 ?  174 GLU B CB    1 
ATOM   6992  C  CG    . GLU B 1 174 ? 121.086 149.773 140.520 1.00 22.93 ?  174 GLU B CG    1 
ATOM   6993  C  CD    . GLU B 1 174 ? 119.596 149.516 140.555 1.00 27.60 ?  174 GLU B CD    1 
ATOM   6994  O  OE1   . GLU B 1 174 ? 119.048 149.060 139.531 1.00 31.09 ?  174 GLU B OE1   1 
ATOM   6995  O  OE2   . GLU B 1 174 ? 118.972 149.777 141.603 1.00 26.84 -1 174 GLU B OE2   1 
ATOM   6996  N  N     . VAL B 1 175 ? 122.167 147.193 136.838 1.00 17.81 ?  175 VAL B N     1 
ATOM   6997  C  CA    . VAL B 1 175 ? 122.405 146.913 135.428 1.00 17.01 ?  175 VAL B CA    1 
ATOM   6998  C  C     . VAL B 1 175 ? 121.192 147.390 134.644 1.00 21.62 ?  175 VAL B C     1 
ATOM   6999  O  O     . VAL B 1 175 ? 120.066 146.943 134.895 1.00 24.85 ?  175 VAL B O     1 
ATOM   7000  C  CB    . VAL B 1 175 ? 122.675 145.420 135.180 1.00 18.44 ?  175 VAL B CB    1 
ATOM   7001  C  CG1   . VAL B 1 175 ? 123.195 145.203 133.770 1.00 7.81  ?  175 VAL B CG1   1 
ATOM   7002  C  CG2   . VAL B 1 175 ? 123.656 144.881 136.209 1.00 18.22 ?  175 VAL B CG2   1 
ATOM   7003  N  N     . ASN B 1 176 ? 121.418 148.295 133.701 1.00 17.07 ?  176 ASN B N     1 
ATOM   7004  C  CA    . ASN B 1 176 ? 120.352 148.817 132.862 1.00 18.01 ?  176 ASN B CA    1 
ATOM   7005  C  C     . ASN B 1 176 ? 120.111 147.898 131.669 1.00 22.69 ?  176 ASN B C     1 
ATOM   7006  O  O     . ASN B 1 176 ? 120.971 147.108 131.275 1.00 27.73 ?  176 ASN B O     1 
ATOM   7007  C  CB    . ASN B 1 176 ? 120.684 150.228 132.384 1.00 19.42 ?  176 ASN B CB    1 
ATOM   7008  C  CG    . ASN B 1 176 ? 119.477 151.134 132.352 1.00 17.10 ?  176 ASN B CG    1 
ATOM   7009  O  OD1   . ASN B 1 176 ? 118.340 150.670 132.309 1.00 26.13 ?  176 ASN B OD1   1 
ATOM   7010  N  ND2   . ASN B 1 176 ? 119.717 152.437 132.377 1.00 18.44 ?  176 ASN B ND2   1 
ATOM   7011  N  N     . ASP B 1 177 ? 118.917 148.017 131.090 1.00 27.31 ?  177 ASP B N     1 
ATOM   7012  C  CA    . ASP B 1 177 ? 118.479 147.137 130.008 1.00 23.71 ?  177 ASP B CA    1 
ATOM   7013  C  C     . ASP B 1 177 ? 119.038 147.653 128.684 1.00 24.80 ?  177 ASP B C     1 
ATOM   7014  O  O     . ASP B 1 177 ? 118.352 148.291 127.882 1.00 31.45 ?  177 ASP B O     1 
ATOM   7015  C  CB    . ASP B 1 177 ? 116.961 147.045 129.985 1.00 20.34 ?  177 ASP B CB    1 
ATOM   7016  C  CG    . ASP B 1 177 ? 116.460 145.916 129.121 1.00 26.79 ?  177 ASP B CG    1 
ATOM   7017  O  OD1   . ASP B 1 177 ? 117.127 144.861 129.075 1.00 34.35 ?  177 ASP B OD1   1 
ATOM   7018  O  OD2   . ASP B 1 177 ? 115.395 146.079 128.493 1.00 33.24 -1 177 ASP B OD2   1 
ATOM   7019  N  N     . SER B 1 178 ? 120.314 147.355 128.455 1.00 19.77 ?  178 SER B N     1 
ATOM   7020  C  CA    . SER B 1 178 ? 121.001 147.748 127.232 1.00 17.17 ?  178 SER B CA    1 
ATOM   7021  C  C     . SER B 1 178 ? 122.308 146.978 127.147 1.00 21.75 ?  178 SER B C     1 
ATOM   7022  O  O     . SER B 1 178 ? 122.873 146.571 128.165 1.00 34.49 ?  178 SER B O     1 
ATOM   7023  C  CB    . SER B 1 178 ? 121.260 149.258 127.188 1.00 14.65 ?  178 SER B CB    1 
ATOM   7024  O  OG    . SER B 1 178 ? 122.496 149.582 127.791 1.00 27.93 ?  178 SER B OG    1 
ATOM   7025  N  N     . LEU B 1 179 ? 122.779 146.774 125.914 1.00 32.35 ?  179 LEU B N     1 
ATOM   7026  C  CA    . LEU B 1 179 ? 124.046 146.077 125.716 1.00 19.98 ?  179 LEU B CA    1 
ATOM   7027  C  C     . LEU B 1 179 ? 125.216 146.905 126.229 1.00 17.04 ?  179 LEU B C     1 
ATOM   7028  O  O     . LEU B 1 179 ? 126.178 146.356 126.777 1.00 26.29 ?  179 LEU B O     1 
ATOM   7029  C  CB    . LEU B 1 179 ? 124.239 145.736 124.239 1.00 23.05 ?  179 LEU B CB    1 
ATOM   7030  C  CG    . LEU B 1 179 ? 125.452 144.859 123.919 1.00 23.10 ?  179 LEU B CG    1 
ATOM   7031  C  CD1   . LEU B 1 179 ? 125.254 143.455 124.466 1.00 20.90 ?  179 LEU B CD1   1 
ATOM   7032  C  CD2   . LEU B 1 179 ? 125.713 144.823 122.425 1.00 21.71 ?  179 LEU B CD2   1 
ATOM   7033  N  N     . ASN B 1 180 ? 125.155 148.227 126.054 1.00 19.32 ?  180 ASN B N     1 
ATOM   7034  C  CA    . ASN B 1 180 ? 126.190 149.099 126.599 1.00 14.81 ?  180 ASN B CA    1 
ATOM   7035  C  C     . ASN B 1 180 ? 126.280 148.953 128.110 1.00 22.05 ?  180 ASN B C     1 
ATOM   7036  O  O     . ASN B 1 180 ? 127.371 148.796 128.674 1.00 30.45 ?  180 ASN B O     1 
ATOM   7037  C  CB    . ASN B 1 180 ? 125.899 150.552 126.221 1.00 23.77 ?  180 ASN B CB    1 
ATOM   7038  C  CG    . ASN B 1 180 ? 126.367 150.901 124.825 1.00 29.53 ?  180 ASN B CG    1 
ATOM   7039  O  OD1   . ASN B 1 180 ? 127.213 150.218 124.253 1.00 34.41 ?  180 ASN B OD1   1 
ATOM   7040  N  ND2   . ASN B 1 180 ? 125.817 151.972 124.270 1.00 27.63 ?  180 ASN B ND2   1 
ATOM   7041  N  N     . ASP B 1 181 ? 125.129 148.977 128.783 1.00 24.53 ?  181 ASP B N     1 
ATOM   7042  C  CA    . ASP B 1 181 ? 125.108 148.868 130.235 1.00 15.71 ?  181 ASP B CA    1 
ATOM   7043  C  C     . ASP B 1 181 ? 125.501 147.474 130.703 1.00 20.15 ?  181 ASP B C     1 
ATOM   7044  O  O     . ASP B 1 181 ? 126.149 147.338 131.742 1.00 30.36 ?  181 ASP B O     1 
ATOM   7045  C  CB    . ASP B 1 181 ? 123.727 149.245 130.760 1.00 27.99 ?  181 ASP B CB    1 
ATOM   7046  C  CG    . ASP B 1 181 ? 123.422 150.720 130.579 1.00 31.71 ?  181 ASP B CG    1 
ATOM   7047  O  OD1   . ASP B 1 181 ? 124.019 151.545 131.300 1.00 32.18 ?  181 ASP B OD1   1 
ATOM   7048  O  OD2   . ASP B 1 181 ? 122.583 151.056 129.717 1.00 26.06 -1 181 ASP B OD2   1 
ATOM   7049  N  N     . ILE B 1 182 ? 125.136 146.431 129.956 1.00 21.62 ?  182 ILE B N     1 
ATOM   7050  C  CA    . ILE B 1 182 ? 125.530 145.076 130.330 1.00 21.44 ?  182 ILE B CA    1 
ATOM   7051  C  C     . ILE B 1 182 ? 127.039 144.896 130.195 1.00 19.32 ?  182 ILE B C     1 
ATOM   7052  O  O     . ILE B 1 182 ? 127.690 144.304 131.066 1.00 22.73 ?  182 ILE B O     1 
ATOM   7053  C  CB    . ILE B 1 182 ? 124.749 144.048 129.491 1.00 19.85 ?  182 ILE B CB    1 
ATOM   7054  C  CG1   . ILE B 1 182 ? 123.321 143.919 130.019 1.00 20.49 ?  182 ILE B CG1   1 
ATOM   7055  C  CG2   . ILE B 1 182 ? 125.443 142.698 129.502 1.00 22.79 ?  182 ILE B CG2   1 
ATOM   7056  C  CD1   . ILE B 1 182 ? 122.382 143.235 129.067 1.00 23.22 ?  182 ILE B CD1   1 
ATOM   7057  N  N     . SER B 1 183 ? 127.619 145.403 129.106 1.00 26.18 ?  183 SER B N     1 
ATOM   7058  C  CA    . SER B 1 183 ? 129.067 145.330 128.940 1.00 16.94 ?  183 SER B CA    1 
ATOM   7059  C  C     . SER B 1 183 ? 129.783 146.129 130.019 1.00 19.44 ?  183 SER B C     1 
ATOM   7060  O  O     . SER B 1 183 ? 130.805 145.684 130.559 1.00 27.79 ?  183 SER B O     1 
ATOM   7061  C  CB    . SER B 1 183 ? 129.460 145.829 127.553 1.00 17.25 ?  183 SER B CB    1 
ATOM   7062  O  OG    . SER B 1 183 ? 128.927 147.115 127.306 1.00 33.98 ?  183 SER B OG    1 
ATOM   7063  N  N     . ARG B 1 184 ? 129.262 147.313 130.352 1.00 25.39 ?  184 ARG B N     1 
ATOM   7064  C  CA    . ARG B 1 184 ? 129.859 148.098 131.424 1.00 17.87 ?  184 ARG B CA    1 
ATOM   7065  C  C     . ARG B 1 184 ? 129.734 147.386 132.765 1.00 26.39 ?  184 ARG B C     1 
ATOM   7066  O  O     . ARG B 1 184 ? 130.641 147.460 133.598 1.00 31.50 ?  184 ARG B O     1 
ATOM   7067  C  CB    . ARG B 1 184 ? 129.213 149.479 131.487 1.00 16.95 ?  184 ARG B CB    1 
ATOM   7068  C  CG    . ARG B 1 184 ? 129.893 150.423 132.460 1.00 27.61 ?  184 ARG B CG    1 
ATOM   7069  C  CD    . ARG B 1 184 ? 131.393 150.442 132.261 1.00 26.09 ?  184 ARG B CD    1 
ATOM   7070  N  NE    . ARG B 1 184 ? 131.791 151.432 131.270 1.00 34.37 ?  184 ARG B NE    1 
ATOM   7071  C  CZ    . ARG B 1 184 ? 132.966 151.448 130.656 1.00 34.93 ?  184 ARG B CZ    1 
ATOM   7072  N  NH1   . ARG B 1 184 ? 133.888 150.532 130.905 1.00 25.59 1  184 ARG B NH1   1 
ATOM   7073  N  NH2   . ARG B 1 184 ? 133.223 152.408 129.772 1.00 32.42 ?  184 ARG B NH2   1 
ATOM   7074  N  N     . ALA B 1 185 ? 128.613 146.701 132.998 1.00 31.15 ?  185 ALA B N     1 
ATOM   7075  C  CA    . ALA B 1 185 ? 128.447 145.938 134.228 1.00 8.29  ?  185 ALA B CA    1 
ATOM   7076  C  C     . ALA B 1 185 ? 129.459 144.809 134.312 1.00 12.71 ?  185 ALA B C     1 
ATOM   7077  O  O     . ALA B 1 185 ? 130.032 144.561 135.377 1.00 22.32 ?  185 ALA B O     1 
ATOM   7078  C  CB    . ALA B 1 185 ? 127.024 145.389 134.318 1.00 9.14  ?  185 ALA B CB    1 
ATOM   7079  N  N     . ILE B 1 186 ? 129.695 144.112 133.199 1.00 22.82 ?  186 ILE B N     1 
ATOM   7080  C  CA    . ILE B 1 186 ? 130.707 143.056 133.186 1.00 23.20 ?  186 ILE B CA    1 
ATOM   7081  C  C     . ILE B 1 186 ? 132.085 143.641 133.470 1.00 17.77 ?  186 ILE B C     1 
ATOM   7082  O  O     . ILE B 1 186 ? 132.862 143.092 134.265 1.00 26.42 ?  186 ILE B O     1 
ATOM   7083  C  CB    . ILE B 1 186 ? 130.674 142.302 131.842 1.00 27.87 ?  186 ILE B CB    1 
ATOM   7084  C  CG1   . ILE B 1 186 ? 129.503 141.322 131.811 1.00 21.95 ?  186 ILE B CG1   1 
ATOM   7085  C  CG2   . ILE B 1 186 ? 131.983 141.567 131.598 1.00 23.79 ?  186 ILE B CG2   1 
ATOM   7086  C  CD1   . ILE B 1 186 ? 128.861 141.195 130.453 1.00 27.46 ?  186 ILE B CD1   1 
ATOM   7087  N  N     . ASP B 1 187 ? 132.403 144.772 132.837 1.00 23.35 ?  187 ASP B N     1 
ATOM   7088  C  CA    . ASP B 1 187 ? 133.694 145.415 133.056 1.00 18.17 ?  187 ASP B CA    1 
ATOM   7089  C  C     . ASP B 1 187 ? 133.872 145.820 134.515 1.00 28.09 ?  187 ASP B C     1 
ATOM   7090  O  O     . ASP B 1 187 ? 134.913 145.551 135.122 1.00 34.35 ?  187 ASP B O     1 
ATOM   7091  C  CB    . ASP B 1 187 ? 133.829 146.632 132.141 1.00 17.20 ?  187 ASP B CB    1 
ATOM   7092  C  CG    . ASP B 1 187 ? 134.892 147.603 132.614 1.00 35.28 ?  187 ASP B CG    1 
ATOM   7093  O  OD1   . ASP B 1 187 ? 136.051 147.180 132.797 1.00 34.32 ?  187 ASP B OD1   1 
ATOM   7094  O  OD2   . ASP B 1 187 ? 134.565 148.793 132.808 1.00 41.83 -1 187 ASP B OD2   1 
ATOM   7095  N  N     . ILE B 1 188 ? 132.860 146.467 135.093 1.00 23.60 ?  188 ILE B N     1 
ATOM   7096  C  CA    . ILE B 1 188 ? 132.958 146.940 136.469 1.00 22.56 ?  188 ILE B CA    1 
ATOM   7097  C  C     . ILE B 1 188 ? 133.010 145.767 137.438 1.00 25.27 ?  188 ILE B C     1 
ATOM   7098  O  O     . ILE B 1 188 ? 133.716 145.813 138.450 1.00 27.77 ?  188 ILE B O     1 
ATOM   7099  C  CB    . ILE B 1 188 ? 131.794 147.896 136.790 1.00 26.73 ?  188 ILE B CB    1 
ATOM   7100  C  CG1   . ILE B 1 188 ? 131.895 149.163 135.945 1.00 25.52 ?  188 ILE B CG1   1 
ATOM   7101  C  CG2   . ILE B 1 188 ? 131.801 148.278 138.252 1.00 26.77 ?  188 ILE B CG2   1 
ATOM   7102  C  CD1   . ILE B 1 188 ? 130.708 150.080 136.101 1.00 21.59 ?  188 ILE B CD1   1 
ATOM   7103  N  N     . SER B 1 189 ? 132.265 144.699 137.149 1.00 19.85 ?  189 SER B N     1 
ATOM   7104  C  CA    . SER B 1 189 ? 132.327 143.507 137.984 1.00 13.40 ?  189 SER B CA    1 
ATOM   7105  C  C     . SER B 1 189 ? 133.724 142.908 137.976 1.00 20.94 ?  189 SER B C     1 
ATOM   7106  O  O     . SER B 1 189 ? 134.247 142.528 139.029 1.00 25.83 ?  189 SER B O     1 
ATOM   7107  C  CB    . SER B 1 189 ? 131.300 142.481 137.509 1.00 20.14 ?  189 SER B CB    1 
ATOM   7108  O  OG    . SER B 1 189 ? 129.999 143.035 137.502 1.00 29.91 ?  189 SER B OG    1 
ATOM   7109  N  N     . MET B 1 190 ? 134.352 142.823 136.800 1.00 30.19 ?  190 MET B N     1 
ATOM   7110  C  CA    . MET B 1 190 ? 135.715 142.305 136.742 1.00 22.37 ?  190 MET B CA    1 
ATOM   7111  C  C     . MET B 1 190 ? 136.694 143.232 137.453 1.00 16.93 ?  190 MET B C     1 
ATOM   7112  O  O     . MET B 1 190 ? 137.615 142.764 138.128 1.00 21.26 ?  190 MET B O     1 
ATOM   7113  C  CB    . MET B 1 190 ? 136.140 142.080 135.292 1.00 21.58 ?  190 MET B CB    1 
ATOM   7114  C  CG    . MET B 1 190 ? 135.361 140.984 134.596 1.00 27.32 ?  190 MET B CG    1 
ATOM   7115  S  SD    . MET B 1 190 ? 136.230 140.259 133.197 1.00 35.79 ?  190 MET B SD    1 
ATOM   7116  C  CE    . MET B 1 190 ? 136.214 141.631 132.051 1.00 25.79 ?  190 MET B CE    1 
ATOM   7117  N  N     . GLN B 1 191 ? 136.509 144.546 137.320 1.00 21.42 ?  191 GLN B N     1 
ATOM   7118  C  CA    . GLN B 1 191 ? 137.408 145.487 137.984 1.00 23.07 ?  191 GLN B CA    1 
ATOM   7119  C  C     . GLN B 1 191 ? 137.285 145.405 139.501 1.00 25.57 ?  191 GLN B C     1 
ATOM   7120  O  O     . GLN B 1 191 ? 138.291 145.493 140.214 1.00 32.40 ?  191 GLN B O     1 
ATOM   7121  C  CB    . GLN B 1 191 ? 137.136 146.913 137.503 1.00 24.32 ?  191 GLN B CB    1 
ATOM   7122  C  CG    . GLN B 1 191 ? 137.390 147.135 136.024 1.00 23.68 ?  191 GLN B CG    1 
ATOM   7123  C  CD    . GLN B 1 191 ? 138.863 147.171 135.674 1.00 27.63 ?  191 GLN B CD    1 
ATOM   7124  O  OE1   . GLN B 1 191 ? 139.726 147.163 136.550 1.00 30.80 ?  191 GLN B OE1   1 
ATOM   7125  N  NE2   . GLN B 1 191 ? 139.158 147.208 134.382 1.00 28.81 ?  191 GLN B NE2   1 
ATOM   7126  N  N     . LEU B 1 192 ? 136.064 145.249 140.013 1.00 24.98 ?  192 LEU B N     1 
ATOM   7127  C  CA    . LEU B 1 192 ? 135.867 145.183 141.456 1.00 16.38 ?  192 LEU B CA    1 
ATOM   7128  C  C     . LEU B 1 192 ? 136.281 143.830 142.019 1.00 23.84 ?  192 LEU B C     1 
ATOM   7129  O  O     . LEU B 1 192 ? 136.827 143.759 143.124 1.00 36.16 ?  192 LEU B O     1 
ATOM   7130  C  CB    . LEU B 1 192 ? 134.411 145.488 141.802 1.00 18.21 ?  192 LEU B CB    1 
ATOM   7131  C  CG    . LEU B 1 192 ? 133.938 146.911 141.498 1.00 19.83 ?  192 LEU B CG    1 
ATOM   7132  C  CD1   . LEU B 1 192 ? 132.430 147.008 141.618 1.00 19.10 ?  192 LEU B CD1   1 
ATOM   7133  C  CD2   . LEU B 1 192 ? 134.619 147.914 142.413 1.00 17.33 ?  192 LEU B CD2   1 
ATOM   7134  N  N     . SER B 1 193 ? 136.027 142.747 141.281 1.00 27.70 ?  193 SER B N     1 
ATOM   7135  C  CA    . SER B 1 193 ? 136.518 141.439 141.694 1.00 20.19 ?  193 SER B CA    1 
ATOM   7136  C  C     . SER B 1 193 ? 138.037 141.388 141.661 1.00 28.24 ?  193 SER B C     1 
ATOM   7137  O  O     . SER B 1 193 ? 138.652 140.683 142.466 1.00 36.87 ?  193 SER B O     1 
ATOM   7138  C  CB    . SER B 1 193 ? 135.924 140.353 140.799 1.00 25.64 ?  193 SER B CB    1 
ATOM   7139  O  OG    . SER B 1 193 ? 136.237 139.062 141.287 1.00 42.27 ?  193 SER B OG    1 
ATOM   7140  N  N     . LYS B 1 194 ? 138.655 142.128 140.739 1.00 34.56 ?  194 LYS B N     1 
ATOM   7141  C  CA    . LYS B 1 194 ? 140.108 142.247 140.724 1.00 32.01 ?  194 LYS B CA    1 
ATOM   7142  C  C     . LYS B 1 194 ? 140.619 142.868 142.017 1.00 35.73 ?  194 LYS B C     1 
ATOM   7143  O  O     . LYS B 1 194 ? 141.636 142.432 142.567 1.00 43.69 ?  194 LYS B O     1 
ATOM   7144  C  CB    . LYS B 1 194 ? 140.540 143.074 139.512 1.00 27.19 ?  194 LYS B CB    1 
ATOM   7145  C  CG    . LYS B 1 194 ? 141.939 143.641 139.599 1.00 36.44 ?  194 LYS B CG    1 
ATOM   7146  C  CD    . LYS B 1 194 ? 142.171 144.692 138.529 1.00 38.23 ?  194 LYS B CD    1 
ATOM   7147  C  CE    . LYS B 1 194 ? 143.655 144.948 138.321 1.00 36.81 ?  194 LYS B CE    1 
ATOM   7148  N  NZ    . LYS B 1 194 ? 143.895 145.982 137.277 1.00 37.91 1  194 LYS B NZ    1 
ATOM   7149  N  N     . LEU B 1 195 ? 139.915 143.881 142.525 1.00 34.15 ?  195 LEU B N     1 
ATOM   7150  C  CA    . LEU B 1 195 ? 140.261 144.490 143.803 1.00 35.73 ?  195 LEU B CA    1 
ATOM   7151  C  C     . LEU B 1 195 ? 139.991 143.571 144.986 1.00 35.64 ?  195 LEU B C     1 
ATOM   7152  O  O     . LEU B 1 195 ? 140.401 143.896 146.105 1.00 42.62 ?  195 LEU B O     1 
ATOM   7153  C  CB    . LEU B 1 195 ? 139.490 145.798 143.985 1.00 38.37 ?  195 LEU B CB    1 
ATOM   7154  C  CG    . LEU B 1 195 ? 139.725 146.866 142.919 1.00 37.71 ?  195 LEU B CG    1 
ATOM   7155  C  CD1   . LEU B 1 195 ? 138.915 148.117 143.226 1.00 32.38 ?  195 LEU B CD1   1 
ATOM   7156  C  CD2   . LEU B 1 195 ? 141.203 147.189 142.801 1.00 34.65 ?  195 LEU B CD2   1 
ATOM   7157  N  N     . GLY B 1 196 ? 139.314 142.448 144.772 1.00 31.06 ?  196 GLY B N     1 
ATOM   7158  C  CA    . GLY B 1 196 ? 139.020 141.511 145.832 1.00 30.00 ?  196 GLY B CA    1 
ATOM   7159  C  C     . GLY B 1 196 ? 137.654 141.646 146.458 1.00 36.77 ?  196 GLY B C     1 
ATOM   7160  O  O     . GLY B 1 196 ? 137.398 141.005 147.483 1.00 39.00 ?  196 GLY B O     1 
ATOM   7161  N  N     . GLY B 1 197 ? 136.768 142.449 145.879 1.00 30.42 ?  197 GLY B N     1 
ATOM   7162  C  CA    . GLY B 1 197 ? 135.463 142.709 146.458 1.00 25.49 ?  197 GLY B CA    1 
ATOM   7163  C  C     . GLY B 1 197 ? 134.370 141.861 145.828 1.00 27.37 ?  197 GLY B C     1 
ATOM   7164  O  O     . GLY B 1 197 ? 134.386 141.600 144.625 1.00 31.59 ?  197 GLY B O     1 
ATOM   7165  N  N     . GLY B 1 198 ? 133.425 141.436 146.661 1.00 25.08 ?  198 GLY B N     1 
ATOM   7166  C  CA    . GLY B 1 198 ? 132.244 140.767 146.149 1.00 14.95 ?  198 GLY B CA    1 
ATOM   7167  C  C     . GLY B 1 198 ? 131.298 141.764 145.505 1.00 14.13 ?  198 GLY B C     1 
ATOM   7168  O  O     . GLY B 1 198 ? 131.074 142.860 146.015 1.00 24.21 ?  198 GLY B O     1 
ATOM   7169  N  N     . VAL B 1 199 ? 130.742 141.375 144.362 1.00 22.61 ?  199 VAL B N     1 
ATOM   7170  C  CA    . VAL B 1 199 ? 129.929 142.261 143.538 1.00 17.88 ?  199 VAL B CA    1 
ATOM   7171  C  C     . VAL B 1 199 ? 128.529 141.678 143.429 1.00 8.99  ?  199 VAL B C     1 
ATOM   7172  O  O     . VAL B 1 199 ? 128.365 140.503 143.083 1.00 18.81 ?  199 VAL B O     1 
ATOM   7173  C  CB    . VAL B 1 199 ? 130.546 142.461 142.143 1.00 12.95 ?  199 VAL B CB    1 
ATOM   7174  C  CG1   . VAL B 1 199 ? 129.790 143.530 141.378 1.00 18.72 ?  199 VAL B CG1   1 
ATOM   7175  C  CG2   . VAL B 1 199 ? 132.015 142.818 142.261 1.00 17.15 ?  199 VAL B CG2   1 
ATOM   7176  N  N     . SER B 1 200 ? 127.527 142.496 143.728 1.00 18.60 ?  200 SER B N     1 
ATOM   7177  C  CA    . SER B 1 200 ? 126.129 142.123 143.584 1.00 7.07  ?  200 SER B CA    1 
ATOM   7178  C  C     . SER B 1 200 ? 125.521 142.928 142.448 1.00 13.22 ?  200 SER B C     1 
ATOM   7179  O  O     . SER B 1 200 ? 125.715 144.145 142.370 1.00 22.94 ?  200 SER B O     1 
ATOM   7180  C  CB    . SER B 1 200 ? 125.358 142.363 144.881 1.00 13.11 ?  200 SER B CB    1 
ATOM   7181  O  OG    . SER B 1 200 ? 124.179 141.582 144.919 1.00 22.00 ?  200 SER B OG    1 
ATOM   7182  N  N     . LEU B 1 201 ? 124.793 142.250 141.567 1.00 20.67 ?  201 LEU B N     1 
ATOM   7183  C  CA    . LEU B 1 201 ? 124.218 142.871 140.383 1.00 7.80  ?  201 LEU B CA    1 
ATOM   7184  C  C     . LEU B 1 201 ? 122.707 142.712 140.404 1.00 10.12 ?  201 LEU B C     1 
ATOM   7185  O  O     . LEU B 1 201 ? 122.196 141.619 140.668 1.00 14.11 ?  201 LEU B O     1 
ATOM   7186  C  CB    . LEU B 1 201 ? 124.804 142.258 139.110 1.00 20.30 ?  201 LEU B CB    1 
ATOM   7187  C  CG    . LEU B 1 201 ? 126.319 142.415 138.975 1.00 18.96 ?  201 LEU B CG    1 
ATOM   7188  C  CD1   . LEU B 1 201 ? 127.020 141.085 139.196 1.00 22.23 ?  201 LEU B CD1   1 
ATOM   7189  C  CD2   . LEU B 1 201 ? 126.677 142.999 137.623 1.00 16.03 ?  201 LEU B CD2   1 
ATOM   7190  N  N     . ASN B 1 202 ? 121.999 143.806 140.138 1.00 15.66 ?  202 ASN B N     1 
ATOM   7191  C  CA    . ASN B 1 202 ? 120.548 143.790 140.014 1.00 7.09  ?  202 ASN B CA    1 
ATOM   7192  C  C     . ASN B 1 202 ? 120.197 143.528 138.555 1.00 22.09 ?  202 ASN B C     1 
ATOM   7193  O  O     . ASN B 1 202 ? 120.490 144.351 137.681 1.00 34.99 ?  202 ASN B O     1 
ATOM   7194  C  CB    . ASN B 1 202 ? 119.951 145.108 140.496 1.00 9.23  ?  202 ASN B CB    1 
ATOM   7195  C  CG    . ASN B 1 202 ? 118.472 145.004 140.791 1.00 13.69 ?  202 ASN B CG    1 
ATOM   7196  O  OD1   . ASN B 1 202 ? 117.952 143.920 141.048 1.00 23.02 ?  202 ASN B OD1   1 
ATOM   7197  N  ND2   . ASN B 1 202 ? 117.783 146.137 140.758 1.00 13.77 ?  202 ASN B ND2   1 
ATOM   7198  N  N     . LEU B 1 203 ? 119.572 142.385 138.289 1.00 13.13 ?  203 LEU B N     1 
ATOM   7199  C  CA    . LEU B 1 203 ? 119.209 141.989 136.937 1.00 10.38 ?  203 LEU B CA    1 
ATOM   7200  C  C     . LEU B 1 203 ? 117.731 142.202 136.639 1.00 11.78 ?  203 LEU B C     1 
ATOM   7201  O  O     . LEU B 1 203 ? 117.245 141.732 135.608 1.00 20.55 ?  203 LEU B O     1 
ATOM   7202  C  CB    . LEU B 1 203 ? 119.586 140.524 136.703 1.00 19.25 ?  203 LEU B CB    1 
ATOM   7203  C  CG    . LEU B 1 203 ? 121.058 140.150 136.882 1.00 19.16 ?  203 LEU B CG    1 
ATOM   7204  C  CD1   . LEU B 1 203 ? 121.348 138.812 136.228 1.00 15.97 ?  203 LEU B CD1   1 
ATOM   7205  C  CD2   . LEU B 1 203 ? 121.972 141.227 136.321 1.00 18.43 ?  203 LEU B CD2   1 
ATOM   7206  N  N     . SER B 1 204 ? 117.008 142.903 137.516 1.00 16.09 ?  204 SER B N     1 
ATOM   7207  C  CA    . SER B 1 204 ? 115.565 143.031 137.351 1.00 17.71 ?  204 SER B CA    1 
ATOM   7208  C  C     . SER B 1 204 ? 115.199 143.969 136.208 1.00 20.50 ?  204 SER B C     1 
ATOM   7209  O  O     . SER B 1 204 ? 114.125 143.826 135.615 1.00 27.93 ?  204 SER B O     1 
ATOM   7210  C  CB    . SER B 1 204 ? 114.933 143.514 138.654 1.00 12.46 ?  204 SER B CB    1 
ATOM   7211  O  OG    . SER B 1 204 ? 115.139 142.574 139.689 1.00 24.39 ?  204 SER B OG    1 
ATOM   7212  N  N     . LYS B 1 205 ? 116.062 144.932 135.890 1.00 17.96 ?  205 LYS B N     1 
ATOM   7213  C  CA    . LYS B 1 205 ? 115.785 145.844 134.790 1.00 16.97 ?  205 LYS B CA    1 
ATOM   7214  C  C     . LYS B 1 205 ? 115.994 145.201 133.427 1.00 21.08 ?  205 LYS B C     1 
ATOM   7215  O  O     . LYS B 1 205 ? 115.388 145.650 132.450 1.00 30.01 ?  205 LYS B O     1 
ATOM   7216  C  CB    . LYS B 1 205 ? 116.653 147.095 134.905 1.00 17.17 ?  205 LYS B CB    1 
ATOM   7217  C  CG    . LYS B 1 205 ? 116.276 147.986 136.064 1.00 13.29 ?  205 LYS B CG    1 
ATOM   7218  C  CD    . LYS B 1 205 ? 117.112 149.244 136.078 1.00 19.85 ?  205 LYS B CD    1 
ATOM   7219  C  CE    . LYS B 1 205 ? 116.579 150.239 137.086 1.00 24.37 ?  205 LYS B CE    1 
ATOM   7220  N  NZ    . LYS B 1 205 ? 116.720 149.753 138.482 1.00 17.22 1  205 LYS B NZ    1 
ATOM   7221  N  N     . LEU B 1 206 ? 116.833 144.172 133.342 1.00 17.26 ?  206 LEU B N     1 
ATOM   7222  C  CA    . LEU B 1 206 ? 117.046 143.481 132.080 1.00 11.29 ?  206 LEU B CA    1 
ATOM   7223  C  C     . LEU B 1 206 ? 115.756 142.820 131.616 1.00 19.76 ?  206 LEU B C     1 
ATOM   7224  O  O     . LEU B 1 206 ? 115.070 142.154 132.395 1.00 25.80 ?  206 LEU B O     1 
ATOM   7225  C  CB    . LEU B 1 206 ? 118.146 142.434 132.232 1.00 19.80 ?  206 LEU B CB    1 
ATOM   7226  C  CG    . LEU B 1 206 ? 119.474 142.935 132.793 1.00 22.20 ?  206 LEU B CG    1 
ATOM   7227  C  CD1   . LEU B 1 206 ? 120.426 141.775 132.990 1.00 17.52 ?  206 LEU B CD1   1 
ATOM   7228  C  CD2   . LEU B 1 206 ? 120.074 143.979 131.876 1.00 26.19 ?  206 LEU B CD2   1 
ATOM   7229  N  N     . ARG B 1 207 ? 115.430 143.002 130.340 1.00 26.99 ?  207 ARG B N     1 
ATOM   7230  C  CA    . ARG B 1 207 ? 114.211 142.421 129.803 1.00 22.95 ?  207 ARG B CA    1 
ATOM   7231  C  C     . ARG B 1 207 ? 114.340 140.906 129.699 1.00 26.41 ?  207 ARG B C     1 
ATOM   7232  O  O     . ARG B 1 207 ? 115.433 140.357 129.536 1.00 30.49 ?  207 ARG B O     1 
ATOM   7233  C  CB    . ARG B 1 207 ? 113.876 143.030 128.441 1.00 23.26 ?  207 ARG B CB    1 
ATOM   7234  C  CG    . ARG B 1 207 ? 114.893 142.786 127.348 1.00 24.90 ?  207 ARG B CG    1 
ATOM   7235  C  CD    . ARG B 1 207 ? 114.570 143.633 126.130 1.00 22.50 ?  207 ARG B CD    1 
ATOM   7236  N  NE    . ARG B 1 207 ? 114.934 145.029 126.333 1.00 27.64 ?  207 ARG B NE    1 
ATOM   7237  C  CZ    . ARG B 1 207 ? 115.141 145.902 125.356 1.00 21.97 ?  207 ARG B CZ    1 
ATOM   7238  N  NH1   . ARG B 1 207 ? 114.994 145.566 124.086 1.00 28.60 1  207 ARG B NH1   1 
ATOM   7239  N  NH2   . ARG B 1 207 ? 115.509 147.142 125.663 1.00 18.36 ?  207 ARG B NH2   1 
ATOM   7240  N  N     . ALA B 1 208 ? 113.199 140.231 129.804 1.00 30.71 ?  208 ALA B N     1 
ATOM   7241  C  CA    . ALA B 1 208 ? 113.173 138.785 129.916 1.00 29.17 ?  208 ALA B CA    1 
ATOM   7242  C  C     . ALA B 1 208 ? 113.530 138.120 128.588 1.00 33.52 ?  208 ALA B C     1 
ATOM   7243  O  O     . ALA B 1 208 ? 113.733 138.771 127.559 1.00 35.30 ?  208 ALA B O     1 
ATOM   7244  C  CB    . ALA B 1 208 ? 111.799 138.316 130.382 1.00 26.41 ?  208 ALA B CB    1 
ATOM   7245  N  N     . LYS B 1 209 ? 113.612 136.793 128.632 1.00 26.37 ?  209 LYS B N     1 
ATOM   7246  C  CA    . LYS B 1 209 ? 113.869 136.009 127.436 1.00 22.11 ?  209 LYS B CA    1 
ATOM   7247  C  C     . LYS B 1 209 ? 112.676 136.075 126.491 1.00 33.53 ?  209 LYS B C     1 
ATOM   7248  O  O     . LYS B 1 209 ? 111.520 136.031 126.919 1.00 35.56 ?  209 LYS B O     1 
ATOM   7249  C  CB    . LYS B 1 209 ? 114.166 134.558 127.811 1.00 27.44 ?  209 LYS B CB    1 
ATOM   7250  C  CG    . LYS B 1 209 ? 114.987 133.798 126.784 1.00 33.01 ?  209 LYS B CG    1 
ATOM   7251  C  CD    . LYS B 1 209 ? 114.447 132.392 126.573 1.00 31.98 ?  209 LYS B CD    1 
ATOM   7252  C  CE    . LYS B 1 209 ? 113.897 131.806 127.862 1.00 36.48 ?  209 LYS B CE    1 
ATOM   7253  N  NZ    . LYS B 1 209 ? 113.209 130.505 127.636 1.00 35.63 1  209 LYS B NZ    1 
ATOM   7254  N  N     . GLY B 1 210 ? 112.964 136.173 125.196 1.00 36.34 ?  210 GLY B N     1 
ATOM   7255  C  CA    . GLY B 1 210 ? 111.908 136.296 124.214 1.00 32.08 ?  210 GLY B CA    1 
ATOM   7256  C  C     . GLY B 1 210 ? 111.293 137.672 124.117 1.00 36.40 ?  210 GLY B C     1 
ATOM   7257  O  O     . GLY B 1 210 ? 110.097 137.788 123.831 1.00 38.93 ?  210 GLY B O     1 
ATOM   7258  N  N     . GLU B 1 211 ? 112.069 138.720 124.360 1.00 39.33 ?  211 GLU B N     1 
ATOM   7259  C  CA    . GLU B 1 211 ? 111.614 140.092 124.203 1.00 33.16 ?  211 GLU B CA    1 
ATOM   7260  C  C     . GLU B 1 211 ? 112.224 140.700 122.947 1.00 36.67 ?  211 GLU B C     1 
ATOM   7261  O  O     . GLU B 1 211 ? 113.205 140.200 122.392 1.00 39.90 ?  211 GLU B O     1 
ATOM   7262  C  CB    . GLU B 1 211 ? 111.966 140.931 125.435 1.00 34.62 ?  211 GLU B CB    1 
ATOM   7263  C  CG    . GLU B 1 211 ? 111.113 140.617 126.648 1.00 35.76 ?  211 GLU B CG    1 
ATOM   7264  C  CD    . GLU B 1 211 ? 110.524 141.858 127.283 1.00 41.33 ?  211 GLU B CD    1 
ATOM   7265  O  OE1   . GLU B 1 211 ? 109.745 142.559 126.606 1.00 43.31 ?  211 GLU B OE1   1 
ATOM   7266  O  OE2   . GLU B 1 211 ? 110.829 142.129 128.462 1.00 41.92 -1 211 GLU B OE2   1 
ATOM   7267  N  N     . ALA B 1 212 ? 111.623 141.796 122.499 1.00 37.07 ?  212 ALA B N     1 
ATOM   7268  C  CA    . ALA B 1 212 ? 112.019 142.441 121.257 1.00 33.37 ?  212 ALA B CA    1 
ATOM   7269  C  C     . ALA B 1 212 ? 113.227 143.343 121.472 1.00 38.75 ?  212 ALA B C     1 
ATOM   7270  O  O     . ALA B 1 212 ? 113.339 144.021 122.496 1.00 40.21 ?  212 ALA B O     1 
ATOM   7271  C  CB    . ALA B 1 212 ? 110.860 143.254 120.680 1.00 37.58 ?  212 ALA B CB    1 
ATOM   7272  N  N     . ILE B 1 213 ? 114.131 143.342 120.496 1.00 35.60 ?  213 ILE B N     1 
ATOM   7273  C  CA    . ILE B 1 213 ? 115.269 144.254 120.462 1.00 35.47 ?  213 ILE B CA    1 
ATOM   7274  C  C     . ILE B 1 213 ? 115.090 145.124 119.226 1.00 35.53 ?  213 ILE B C     1 
ATOM   7275  O  O     . ILE B 1 213 ? 115.377 144.687 118.106 1.00 42.01 ?  213 ILE B O     1 
ATOM   7276  C  CB    . ILE B 1 213 ? 116.612 143.516 120.438 1.00 37.16 ?  213 ILE B CB    1 
ATOM   7277  C  CG1   . ILE B 1 213 ? 116.709 142.533 121.604 1.00 36.22 ?  213 ILE B CG1   1 
ATOM   7278  C  CG2   . ILE B 1 213 ? 117.763 144.507 120.486 1.00 33.09 ?  213 ILE B CG2   1 
ATOM   7279  C  CD1   . ILE B 1 213 ? 117.893 141.600 121.515 1.00 31.45 ?  213 ILE B CD1   1 
ATOM   7280  N  N     . LYS B 1 214 ? 114.609 146.355 119.429 1.00 40.21 ?  214 LYS B N     1 
ATOM   7281  C  CA    . LYS B 1 214 ? 114.369 147.352 118.384 1.00 39.89 ?  214 LYS B CA    1 
ATOM   7282  C  C     . LYS B 1 214 ? 113.702 146.750 117.150 1.00 45.59 ?  214 LYS B C     1 
ATOM   7283  O  O     . LYS B 1 214 ? 114.309 146.683 116.075 1.00 45.66 ?  214 LYS B O     1 
ATOM   7284  C  CB    . LYS B 1 214 ? 115.657 148.109 118.006 1.00 39.26 ?  214 LYS B CB    1 
ATOM   7285  C  CG    . LYS B 1 214 ? 116.900 147.294 117.681 1.00 41.69 ?  214 LYS B CG    1 
ATOM   7286  C  CD    . LYS B 1 214 ? 117.934 148.150 116.974 1.00 40.17 ?  214 LYS B CD    1 
ATOM   7287  C  CE    . LYS B 1 214 ? 119.281 147.457 116.912 1.00 42.26 ?  214 LYS B CE    1 
ATOM   7288  N  NZ    . LYS B 1 214 ? 120.401 148.435 116.979 1.00 44.06 1  214 LYS B NZ    1 
ATOM   7289  N  N     . ASP B 1 215 ? 112.460 146.293 117.313 1.00 52.33 ?  215 ASP B N     1 
ATOM   7290  C  CA    . ASP B 1 215 ? 111.544 145.767 116.306 1.00 53.60 ?  215 ASP B CA    1 
ATOM   7291  C  C     . ASP B 1 215 ? 111.841 144.318 115.931 1.00 54.25 ?  215 ASP B C     1 
ATOM   7292  O  O     . ASP B 1 215 ? 111.123 143.758 115.102 1.00 56.29 ?  215 ASP B O     1 
ATOM   7293  C  CB    . ASP B 1 215 ? 111.505 146.610 115.015 1.00 52.06 ?  215 ASP B CB    1 
ATOM   7294  C  CG    . ASP B 1 215 ? 110.818 147.944 115.212 1.00 59.18 ?  215 ASP B CG    1 
ATOM   7295  O  OD1   . ASP B 1 215 ? 109.584 147.956 115.408 1.00 56.38 ?  215 ASP B OD1   1 
ATOM   7296  O  OD2   . ASP B 1 215 ? 111.512 148.982 115.168 1.00 56.99 -1 215 ASP B OD2   1 
ATOM   7297  N  N     . VAL B 1 216 ? 112.862 143.687 116.502 1.00 48.01 ?  216 VAL B N     1 
ATOM   7298  C  CA    . VAL B 1 216 ? 113.101 142.267 116.271 1.00 43.71 ?  216 VAL B CA    1 
ATOM   7299  C  C     . VAL B 1 216 ? 112.601 141.498 117.488 1.00 48.49 ?  216 VAL B C     1 
ATOM   7300  O  O     . VAL B 1 216 ? 113.293 141.409 118.506 1.00 51.75 ?  216 VAL B O     1 
ATOM   7301  C  CB    . VAL B 1 216 ? 114.587 141.989 116.006 1.00 45.75 ?  216 VAL B CB    1 
ATOM   7302  C  CG1   . VAL B 1 216 ? 114.828 140.498 115.837 1.00 45.61 ?  216 VAL B CG1   1 
ATOM   7303  C  CG2   . VAL B 1 216 ? 115.053 142.752 114.780 1.00 43.69 ?  216 VAL B CG2   1 
ATOM   7304  N  N     . GLU B 1 217 ? 111.400 140.940 117.381 1.00 49.70 ?  217 GLU B N     1 
ATOM   7305  C  CA    . GLU B 1 217 ? 110.741 140.281 118.498 1.00 50.06 ?  217 GLU B CA    1 
ATOM   7306  C  C     . GLU B 1 217 ? 111.426 138.966 118.838 1.00 45.18 ?  217 GLU B C     1 
ATOM   7307  O  O     . GLU B 1 217 ? 112.081 138.345 118.001 1.00 45.39 ?  217 GLU B O     1 
ATOM   7308  C  CB    . GLU B 1 217 ? 109.267 140.029 118.178 1.00 46.34 ?  217 GLU B CB    1 
ATOM   7309  C  CG    . GLU B 1 217 ? 108.662 141.033 117.218 1.00 49.31 ?  217 GLU B CG    1 
ATOM   7310  C  CD    . GLU B 1 217 ? 108.296 142.335 117.900 1.00 52.31 ?  217 GLU B CD    1 
ATOM   7311  O  OE1   . GLU B 1 217 ? 107.687 142.285 118.988 1.00 50.98 ?  217 GLU B OE1   1 
ATOM   7312  O  OE2   . GLU B 1 217 ? 108.619 143.407 117.347 1.00 54.93 -1 217 GLU B OE2   1 
ATOM   7313  N  N     . ASN B 1 218 ? 111.265 138.549 120.096 1.00 42.09 ?  218 ASN B N     1 
ATOM   7314  C  CA    . ASN B 1 218 ? 111.752 137.255 120.578 1.00 43.42 ?  218 ASN B CA    1 
ATOM   7315  C  C     . ASN B 1 218 ? 113.251 137.089 120.336 1.00 46.69 ?  218 ASN B C     1 
ATOM   7316  O  O     . ASN B 1 218 ? 113.720 136.031 119.911 1.00 48.20 ?  218 ASN B O     1 
ATOM   7317  C  CB    . ASN B 1 218 ? 110.965 136.109 119.937 1.00 42.39 ?  218 ASN B CB    1 
ATOM   7318  C  CG    . ASN B 1 218 ? 110.916 134.877 120.812 1.00 46.35 ?  218 ASN B CG    1 
ATOM   7319  O  OD1   . ASN B 1 218 ? 110.033 134.738 121.658 1.00 49.47 ?  218 ASN B OD1   1 
ATOM   7320  N  ND2   . ASN B 1 218 ? 111.866 133.972 120.613 1.00 47.74 ?  218 ASN B ND2   1 
ATOM   7321  N  N     . ALA B 1 219 ? 114.017 138.145 120.618 1.00 35.88 ?  219 ALA B N     1 
ATOM   7322  C  CA    . ALA B 1 219 ? 115.445 138.155 120.337 1.00 33.97 ?  219 ALA B CA    1 
ATOM   7323  C  C     . ALA B 1 219 ? 116.328 138.191 121.576 1.00 37.71 ?  219 ALA B C     1 
ATOM   7324  O  O     . ALA B 1 219 ? 117.539 137.988 121.452 1.00 37.78 ?  219 ALA B O     1 
ATOM   7325  C  CB    . ALA B 1 219 ? 115.804 139.353 119.446 1.00 34.85 ?  219 ALA B CB    1 
ATOM   7326  N  N     . THR B 1 220 ? 115.764 138.442 122.752 1.00 34.96 ?  220 THR B N     1 
ATOM   7327  C  CA    . THR B 1 220 ? 116.549 138.599 123.969 1.00 33.11 ?  220 THR B CA    1 
ATOM   7328  C  C     . THR B 1 220 ? 116.731 137.252 124.655 1.00 35.08 ?  220 THR B C     1 
ATOM   7329  O  O     . THR B 1 220 ? 115.774 136.486 124.800 1.00 33.67 ?  220 THR B O     1 
ATOM   7330  C  CB    . THR B 1 220 ? 115.872 139.592 124.915 1.00 28.35 ?  220 THR B CB    1 
ATOM   7331  O  OG1   . THR B 1 220 ? 115.699 140.847 124.248 1.00 34.03 ?  220 THR B OG1   1 
ATOM   7332  C  CG2   . THR B 1 220 ? 116.713 139.806 126.160 1.00 33.35 ?  220 THR B CG2   1 
ATOM   7333  N  N     . LYS B 1 221 ? 117.967 136.963 125.069 1.00 35.88 ?  221 LYS B N     1 
ATOM   7334  C  CA    . LYS B 1 221 ? 118.257 135.750 125.822 1.00 32.46 ?  221 LYS B CA    1 
ATOM   7335  C  C     . LYS B 1 221 ? 117.816 135.837 127.274 1.00 36.33 ?  221 LYS B C     1 
ATOM   7336  O  O     . LYS B 1 221 ? 117.853 134.821 127.977 1.00 40.45 ?  221 LYS B O     1 
ATOM   7337  C  CB    . LYS B 1 221 ? 119.753 135.434 125.773 1.00 33.12 ?  221 LYS B CB    1 
ATOM   7338  C  CG    . LYS B 1 221 ? 120.475 136.002 124.573 1.00 31.06 ?  221 LYS B CG    1 
ATOM   7339  C  CD    . LYS B 1 221 ? 121.822 135.330 124.392 1.00 36.10 ?  221 LYS B CD    1 
ATOM   7340  C  CE    . LYS B 1 221 ? 121.668 133.907 123.894 1.00 37.98 ?  221 LYS B CE    1 
ATOM   7341  N  NZ    . LYS B 1 221 ? 120.943 133.857 122.600 1.00 37.38 1  221 LYS B NZ    1 
ATOM   7342  N  N     . GLY B 1 222 ? 117.414 137.010 127.739 1.00 34.14 ?  222 GLY B N     1 
ATOM   7343  C  CA    . GLY B 1 222 ? 116.947 137.166 129.096 1.00 32.70 ?  222 GLY B CA    1 
ATOM   7344  C  C     . GLY B 1 222 ? 118.076 137.417 130.075 1.00 31.75 ?  222 GLY B C     1 
ATOM   7345  O  O     . GLY B 1 222 ? 119.206 137.754 129.714 1.00 34.90 ?  222 GLY B O     1 
ATOM   7346  N  N     . VAL B 1 223 ? 117.746 137.247 131.358 1.00 26.93 ?  223 VAL B N     1 
ATOM   7347  C  CA    . VAL B 1 223 ? 118.731 137.462 132.414 1.00 30.96 ?  223 VAL B CA    1 
ATOM   7348  C  C     . VAL B 1 223 ? 119.727 136.322 132.528 1.00 22.59 ?  223 VAL B C     1 
ATOM   7349  O  O     . VAL B 1 223 ? 120.772 136.496 133.160 1.00 25.89 ?  223 VAL B O     1 
ATOM   7350  C  CB    . VAL B 1 223 ? 118.053 137.678 133.780 1.00 27.74 ?  223 VAL B CB    1 
ATOM   7351  C  CG1   . VAL B 1 223 ? 116.952 138.715 133.665 1.00 21.69 ?  223 VAL B CG1   1 
ATOM   7352  C  CG2   . VAL B 1 223 ? 117.510 136.368 134.328 1.00 26.44 ?  223 VAL B CG2   1 
ATOM   7353  N  N     . VAL B 1 224 ? 119.447 135.166 131.923 1.00 26.79 ?  224 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 224 ? 120.347 134.026 132.070 1.00 26.01 ?  224 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 224 ? 121.580 134.169 131.180 1.00 31.64 ?  224 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 224 ? 122.670 133.722 131.552 1.00 37.19 ?  224 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 224 ? 119.593 132.717 131.791 1.00 32.12 ?  224 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 224 ? 120.486 131.521 132.066 1.00 28.23 ?  224 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 224 ? 118.341 132.648 132.641 1.00 32.42 ?  224 VAL B CG2   1 
ATOM   7360  N  N     . GLY B 1 225 ? 121.449 134.787 130.005 1.00 20.31 ?  225 GLY B N     1 
ATOM   7361  C  CA    . GLY B 1 225 ? 122.631 135.079 129.210 1.00 17.94 ?  225 GLY B CA    1 
ATOM   7362  C  C     . GLY B 1 225 ? 123.568 136.043 129.911 1.00 20.10 ?  225 GLY B C     1 
ATOM   7363  O  O     . GLY B 1 225 ? 124.788 135.845 129.930 1.00 30.82 ?  225 GLY B O     1 
ATOM   7364  N  N     . VAL B 1 226 ? 123.007 137.095 130.511 1.00 18.63 ?  226 VAL B N     1 
ATOM   7365  C  CA    . VAL B 1 226 ? 123.804 138.010 131.319 1.00 21.71 ?  226 VAL B CA    1 
ATOM   7366  C  C     . VAL B 1 226 ? 124.378 137.289 132.528 1.00 18.90 ?  226 VAL B C     1 
ATOM   7367  O  O     . VAL B 1 226 ? 125.492 137.586 132.965 1.00 23.94 ?  226 VAL B O     1 
ATOM   7368  C  CB    . VAL B 1 226 ? 122.957 139.230 131.733 1.00 21.28 ?  226 VAL B CB    1 
ATOM   7369  C  CG1   . VAL B 1 226 ? 123.803 140.234 132.496 1.00 29.21 ?  226 VAL B CG1   1 
ATOM   7370  C  CG2   . VAL B 1 226 ? 122.336 139.874 130.509 1.00 23.54 ?  226 VAL B CG2   1 
ATOM   7371  N  N     . MET B 1 227 ? 123.631 136.336 133.086 1.00 22.86 ?  227 MET B N     1 
ATOM   7372  C  CA    . MET B 1 227 ? 124.135 135.545 134.204 1.00 23.74 ?  227 MET B CA    1 
ATOM   7373  C  C     . MET B 1 227 ? 125.361 134.738 133.804 1.00 25.47 ?  227 MET B C     1 
ATOM   7374  O  O     . MET B 1 227 ? 126.336 134.668 134.555 1.00 28.53 ?  227 MET B O     1 
ATOM   7375  C  CB    . MET B 1 227 ? 123.034 134.621 134.717 1.00 17.04 ?  227 MET B CB    1 
ATOM   7376  C  CG    . MET B 1 227 ? 122.097 135.256 135.719 1.00 18.35 ?  227 MET B CG    1 
ATOM   7377  S  SD    . MET B 1 227 ? 121.036 134.020 136.473 1.00 33.72 ?  227 MET B SD    1 
ATOM   7378  C  CE    . MET B 1 227 ? 122.092 133.468 137.798 1.00 30.40 ?  227 MET B CE    1 
ATOM   7379  N  N     . LYS B 1 228 ? 125.324 134.112 132.627 1.00 23.81 ?  228 LYS B N     1 
ATOM   7380  C  CA    . LYS B 1 228 ? 126.485 133.375 132.134 1.00 19.93 ?  228 LYS B CA    1 
ATOM   7381  C  C     . LYS B 1 228 ? 127.663 134.306 131.883 1.00 20.40 ?  228 LYS B C     1 
ATOM   7382  O  O     . LYS B 1 228 ? 128.811 133.978 132.216 1.00 26.34 ?  228 LYS B O     1 
ATOM   7383  C  CB    . LYS B 1 228 ? 126.128 132.622 130.855 1.00 22.60 ?  228 LYS B CB    1 
ATOM   7384  C  CG    . LYS B 1 228 ? 125.009 131.619 131.009 1.00 24.65 ?  228 LYS B CG    1 
ATOM   7385  C  CD    . LYS B 1 228 ? 125.011 130.635 129.857 1.00 33.66 ?  228 LYS B CD    1 
ATOM   7386  C  CE    . LYS B 1 228 ? 124.077 131.081 128.743 1.00 38.31 ?  228 LYS B CE    1 
ATOM   7387  N  NZ    . LYS B 1 228 ? 122.655 130.764 129.051 1.00 36.29 1  228 LYS B NZ    1 
ATOM   7388  N  N     . LEU B 1 229 ? 127.397 135.471 131.287 1.00 22.70 ?  229 LEU B N     1 
ATOM   7389  C  CA    . LEU B 1 229 ? 128.458 136.447 131.063 1.00 20.74 ?  229 LEU B CA    1 
ATOM   7390  C  C     . LEU B 1 229 ? 129.105 136.861 132.376 1.00 24.12 ?  229 LEU B C     1 
ATOM   7391  O  O     . LEU B 1 229 ? 130.334 136.923 132.486 1.00 29.02 ?  229 LEU B O     1 
ATOM   7392  C  CB    . LEU B 1 229 ? 127.903 137.674 130.342 1.00 23.24 ?  229 LEU B CB    1 
ATOM   7393  C  CG    . LEU B 1 229 ? 127.667 137.613 128.837 1.00 19.83 ?  229 LEU B CG    1 
ATOM   7394  C  CD1   . LEU B 1 229 ? 126.775 138.765 128.425 1.00 24.18 ?  229 LEU B CD1   1 
ATOM   7395  C  CD2   . LEU B 1 229 ? 128.983 137.659 128.089 1.00 19.50 ?  229 LEU B CD2   1 
ATOM   7396  N  N     . LEU B 1 230 ? 128.286 137.139 133.392 1.00 27.00 ?  230 LEU B N     1 
ATOM   7397  C  CA    . LEU B 1 230 ? 128.807 137.566 134.685 1.00 18.28 ?  230 LEU B CA    1 
ATOM   7398  C  C     . LEU B 1 230 ? 129.542 136.435 135.389 1.00 13.47 ?  230 LEU B C     1 
ATOM   7399  O  O     . LEU B 1 230 ? 130.549 136.670 136.060 1.00 32.34 ?  230 LEU B O     1 
ATOM   7400  C  CB    . LEU B 1 230 ? 127.670 138.092 135.559 1.00 19.19 ?  230 LEU B CB    1 
ATOM   7401  C  CG    . LEU B 1 230 ? 127.028 139.402 135.106 1.00 23.66 ?  230 LEU B CG    1 
ATOM   7402  C  CD1   . LEU B 1 230 ? 125.790 139.697 135.935 1.00 28.79 ?  230 LEU B CD1   1 
ATOM   7403  C  CD2   . LEU B 1 230 ? 128.024 140.547 135.188 1.00 24.41 ?  230 LEU B CD2   1 
ATOM   7404  N  N     . ASP B 1 231 ? 129.049 135.203 135.259 1.00 22.77 ?  231 ASP B N     1 
ATOM   7405  C  CA    . ASP B 1 231 ? 129.731 134.068 135.870 1.00 25.27 ?  231 ASP B CA    1 
ATOM   7406  C  C     . ASP B 1 231 ? 131.117 133.880 135.273 1.00 29.78 ?  231 ASP B C     1 
ATOM   7407  O  O     . ASP B 1 231 ? 132.094 133.674 136.003 1.00 33.95 ?  231 ASP B O     1 
ATOM   7408  C  CB    . ASP B 1 231 ? 128.894 132.802 135.700 1.00 24.32 ?  231 ASP B CB    1 
ATOM   7409  C  CG    . ASP B 1 231 ? 129.445 131.630 136.482 1.00 40.21 ?  231 ASP B CG    1 
ATOM   7410  O  OD1   . ASP B 1 231 ? 129.269 131.604 137.718 1.00 44.23 ?  231 ASP B OD1   1 
ATOM   7411  O  OD2   . ASP B 1 231 ? 130.055 130.732 135.865 1.00 39.45 -1 231 ASP B OD2   1 
ATOM   7412  N  N     . ASN B 1 232 ? 131.231 133.972 133.947 1.00 30.21 ?  232 ASN B N     1 
ATOM   7413  C  CA    . ASN B 1 232 ? 132.546 133.872 133.323 1.00 28.77 ?  232 ASN B CA    1 
ATOM   7414  C  C     . ASN B 1 232 ? 133.421 135.077 133.654 1.00 23.15 ?  232 ASN B C     1 
ATOM   7415  O  O     . ASN B 1 232 ? 134.641 134.941 133.796 1.00 31.63 ?  232 ASN B O     1 
ATOM   7416  C  CB    . ASN B 1 232 ? 132.398 133.691 131.817 1.00 26.34 ?  232 ASN B CB    1 
ATOM   7417  C  CG    . ASN B 1 232 ? 132.366 132.234 131.420 1.00 31.22 ?  232 ASN B CG    1 
ATOM   7418  O  OD1   . ASN B 1 232 ? 133.167 131.434 131.901 1.00 36.86 ?  232 ASN B OD1   1 
ATOM   7419  N  ND2   . ASN B 1 232 ? 131.414 131.871 130.585 1.00 35.04 ?  232 ASN B ND2   1 
ATOM   7420  N  N     . ALA B 1 233 ? 132.820 136.260 133.783 1.00 18.47 ?  233 ALA B N     1 
ATOM   7421  C  CA    . ALA B 1 233 ? 133.588 137.439 134.166 1.00 15.26 ?  233 ALA B CA    1 
ATOM   7422  C  C     . ALA B 1 233 ? 134.167 137.289 135.568 1.00 26.94 ?  233 ALA B C     1 
ATOM   7423  O  O     . ALA B 1 233 ? 135.314 137.675 135.819 1.00 30.67 ?  233 ALA B O     1 
ATOM   7424  C  CB    . ALA B 1 233 ? 132.706 138.683 134.076 1.00 20.26 ?  233 ALA B CB    1 
ATOM   7425  N  N     . PHE B 1 234 ? 133.383 136.737 136.496 1.00 30.52 ?  234 PHE B N     1 
ATOM   7426  C  CA    . PHE B 1 234 ? 133.870 136.522 137.854 1.00 24.01 ?  234 PHE B CA    1 
ATOM   7427  C  C     . PHE B 1 234 ? 134.877 135.383 137.913 1.00 24.34 ?  234 PHE B C     1 
ATOM   7428  O  O     . PHE B 1 234 ? 135.808 135.424 138.725 1.00 29.06 ?  234 PHE B O     1 
ATOM   7429  C  CB    . PHE B 1 234 ? 132.700 136.247 138.797 1.00 21.79 ?  234 PHE B CB    1 
ATOM   7430  C  CG    . PHE B 1 234 ? 131.948 137.480 139.197 1.00 21.25 ?  234 PHE B CG    1 
ATOM   7431  C  CD1   . PHE B 1 234 ? 132.595 138.530 139.820 1.00 24.86 ?  234 PHE B CD1   1 
ATOM   7432  C  CD2   . PHE B 1 234 ? 130.593 137.589 138.950 1.00 23.68 ?  234 PHE B CD2   1 
ATOM   7433  C  CE1   . PHE B 1 234 ? 131.903 139.665 140.184 1.00 24.28 ?  234 PHE B CE1   1 
ATOM   7434  C  CE2   . PHE B 1 234 ? 129.899 138.722 139.309 1.00 23.92 ?  234 PHE B CE2   1 
ATOM   7435  C  CZ    . PHE B 1 234 ? 130.554 139.759 139.929 1.00 24.77 ?  234 PHE B CZ    1 
ATOM   7436  N  N     . ARG B 1 235 ? 134.705 134.357 137.076 1.00 31.14 ?  235 ARG B N     1 
ATOM   7437  C  CA    . ARG B 1 235 ? 135.697 133.290 137.003 1.00 25.16 ?  235 ARG B CA    1 
ATOM   7438  C  C     . ARG B 1 235 ? 137.027 133.808 136.469 1.00 31.81 ?  235 ARG B C     1 
ATOM   7439  O  O     . ARG B 1 235 ? 138.092 133.387 136.933 1.00 40.91 ?  235 ARG B O     1 
ATOM   7440  C  CB    . ARG B 1 235 ? 135.177 132.143 136.138 1.00 28.01 ?  235 ARG B CB    1 
ATOM   7441  C  CG    . ARG B 1 235 ? 134.441 131.078 136.928 1.00 38.67 ?  235 ARG B CG    1 
ATOM   7442  C  CD    . ARG B 1 235 ? 134.194 129.821 136.112 1.00 33.71 ?  235 ARG B CD    1 
ATOM   7443  N  NE    . ARG B 1 235 ? 132.846 129.787 135.561 1.00 37.92 ?  235 ARG B NE    1 
ATOM   7444  C  CZ    . ARG B 1 235 ? 132.568 129.725 134.265 1.00 40.90 ?  235 ARG B CZ    1 
ATOM   7445  N  NH1   . ARG B 1 235 ? 133.528 129.671 133.357 1.00 42.51 1  235 ARG B NH1   1 
ATOM   7446  N  NH2   . ARG B 1 235 ? 131.299 129.718 133.874 1.00 36.14 ?  235 ARG B NH2   1 
ATOM   7447  N  N     . TYR B 1 236 ? 136.988 134.708 135.486 1.00 22.81 ?  236 TYR B N     1 
ATOM   7448  C  CA    . TYR B 1 236 ? 138.228 135.257 134.950 1.00 24.99 ?  236 TYR B CA    1 
ATOM   7449  C  C     . TYR B 1 236 ? 138.898 136.184 135.955 1.00 24.34 ?  236 TYR B C     1 
ATOM   7450  O  O     . TYR B 1 236 ? 140.104 136.079 136.205 1.00 26.55 ?  236 TYR B O     1 
ATOM   7451  C  CB    . TYR B 1 236 ? 137.958 135.998 133.642 1.00 24.45 ?  236 TYR B CB    1 
ATOM   7452  C  CG    . TYR B 1 236 ? 139.211 136.536 133.002 1.00 22.08 ?  236 TYR B CG    1 
ATOM   7453  C  CD1   . TYR B 1 236 ? 140.109 135.681 132.382 1.00 18.62 ?  236 TYR B CD1   1 
ATOM   7454  C  CD2   . TYR B 1 236 ? 139.507 137.891 133.029 1.00 18.79 ?  236 TYR B CD2   1 
ATOM   7455  C  CE1   . TYR B 1 236 ? 141.255 136.156 131.800 1.00 23.08 ?  236 TYR B CE1   1 
ATOM   7456  C  CE2   . TYR B 1 236 ? 140.655 138.376 132.447 1.00 13.61 ?  236 TYR B CE2   1 
ATOM   7457  C  CZ    . TYR B 1 236 ? 141.525 137.503 131.835 1.00 20.82 ?  236 TYR B CZ    1 
ATOM   7458  O  OH    . TYR B 1 236 ? 142.673 137.968 131.248 1.00 30.55 ?  236 TYR B OH    1 
ATOM   7459  N  N     . ALA B 1 237 ? 138.132 137.104 136.542 1.00 29.80 ?  237 ALA B N     1 
ATOM   7460  C  CA    . ALA B 1 237 ? 138.659 138.045 137.530 1.00 29.51 ?  237 ALA B CA    1 
ATOM   7461  C  C     . ALA B 1 237 ? 138.692 137.358 138.895 1.00 36.56 ?  237 ALA B C     1 
ATOM   7462  O  O     . ALA B 1 237 ? 137.917 137.650 139.807 1.00 36.35 ?  237 ALA B O     1 
ATOM   7463  C  CB    . ALA B 1 237 ? 137.828 139.320 137.556 1.00 30.47 ?  237 ALA B CB    1 
ATOM   7464  N  N     . ASP B 1 238 ? 139.630 136.419 139.020 1.00 51.59 ?  238 ASP B N     1 
ATOM   7465  C  CA    . ASP B 1 238 ? 139.728 135.555 140.188 1.00 51.32 ?  238 ASP B CA    1 
ATOM   7466  C  C     . ASP B 1 238 ? 140.720 136.072 141.220 1.00 55.56 ?  238 ASP B C     1 
ATOM   7467  O  O     . ASP B 1 238 ? 141.357 135.267 141.916 1.00 57.66 ?  238 ASP B O     1 
ATOM   7468  C  CB    . ASP B 1 238 ? 140.100 134.135 139.757 1.00 49.85 ?  238 ASP B CB    1 
ATOM   7469  C  CG    . ASP B 1 238 ? 138.959 133.158 139.935 1.00 54.08 ?  238 ASP B CG    1 
ATOM   7470  O  OD1   . ASP B 1 238 ? 138.967 132.106 139.263 1.00 53.16 ?  238 ASP B OD1   1 
ATOM   7471  O  OD2   . ASP B 1 238 ? 138.043 133.452 140.728 1.00 53.25 -1 238 ASP B OD2   1 
ATOM   7472  N  N     . GLN B 1 239 ? 140.880 137.393 141.324 1.00 64.45 ?  239 GLN B N     1 
ATOM   7473  C  CA    . GLN B 1 239 ? 141.757 138.017 142.316 1.00 65.28 ?  239 GLN B CA    1 
ATOM   7474  C  C     . GLN B 1 239 ? 143.194 137.511 142.184 1.00 67.16 ?  239 GLN B C     1 
ATOM   7475  O  O     . GLN B 1 239 ? 143.804 137.045 143.149 1.00 64.76 ?  239 GLN B O     1 
ATOM   7476  C  CB    . GLN B 1 239 ? 141.226 137.793 143.735 1.00 64.30 ?  239 GLN B CB    1 
ATOM   7477  C  CG    . GLN B 1 239 ? 139.773 138.185 143.918 1.00 63.46 ?  239 GLN B CG    1 
ATOM   7478  C  CD    . GLN B 1 239 ? 139.224 137.771 145.266 1.00 66.62 ?  239 GLN B CD    1 
ATOM   7479  O  OE1   . GLN B 1 239 ? 138.034 137.492 145.405 1.00 64.72 ?  239 GLN B OE1   1 
ATOM   7480  N  NE2   . GLN B 1 239 ? 140.091 137.731 146.270 1.00 66.44 ?  239 GLN B NE2   1 
ATOM   7481  N  N     . MET B 1 240 ? 143.728 137.601 140.964 1.00 68.36 ?  240 MET B N     1 
ATOM   7482  C  CA    . MET B 1 240 ? 145.096 137.180 140.658 1.00 67.11 ?  240 MET B CA    1 
ATOM   7483  C  C     . MET B 1 240 ? 145.341 135.719 141.026 1.00 67.96 ?  240 MET B C     1 
ATOM   7484  O  O     . MET B 1 240 ? 146.435 135.352 141.461 1.00 68.29 ?  240 MET B O     1 
ATOM   7485  C  CB    . MET B 1 240 ? 146.124 138.080 141.350 1.00 67.19 ?  240 MET B CB    1 
ATOM   7486  C  CG    . MET B 1 240 ? 146.185 139.498 140.809 1.00 68.64 ?  240 MET B CG    1 
ATOM   7487  S  SD    . MET B 1 240 ? 144.572 140.189 140.402 1.00 76.69 ?  240 MET B SD    1 
ATOM   7488  C  CE    . MET B 1 240 ? 144.995 141.923 140.271 1.00 66.55 ?  240 MET B CE    1 
ATOM   7489  N  N     . GLY B 1 241 ? 144.325 134.875 140.861 1.00 70.46 ?  241 GLY B N     1 
ATOM   7490  C  CA    . GLY B 1 241 ? 144.464 133.470 141.184 1.00 69.56 ?  241 GLY B CA    1 
ATOM   7491  C  C     . GLY B 1 241 ? 144.617 133.159 142.654 1.00 72.28 ?  241 GLY B C     1 
ATOM   7492  O  O     . GLY B 1 241 ? 145.064 132.060 142.996 1.00 72.91 ?  241 GLY B O     1 
ATOM   7493  N  N     . GLN B 1 242 ? 144.264 134.092 143.538 1.00 73.68 ?  242 GLN B N     1 
ATOM   7494  C  CA    . GLN B 1 242 ? 144.405 133.884 144.976 1.00 73.00 ?  242 GLN B CA    1 
ATOM   7495  C  C     . GLN B 1 242 ? 143.123 133.327 145.588 1.00 73.64 ?  242 GLN B C     1 
ATOM   7496  O  O     . GLN B 1 242 ? 143.126 132.244 146.182 1.00 71.98 ?  242 GLN B O     1 
ATOM   7497  C  CB    . GLN B 1 242 ? 144.798 135.199 145.660 1.00 71.35 ?  242 GLN B CB    1 
ATOM   7498  C  CG    . GLN B 1 242 ? 146.174 135.718 145.276 1.00 73.43 ?  242 GLN B CG    1 
ATOM   7499  C  CD    . GLN B 1 242 ? 146.710 136.738 146.265 1.00 75.32 ?  242 GLN B CD    1 
ATOM   7500  O  OE1   . GLN B 1 242 ? 146.137 136.943 147.335 1.00 75.18 ?  242 GLN B OE1   1 
ATOM   7501  N  NE2   . GLN B 1 242 ? 147.817 137.381 145.911 1.00 72.12 ?  242 GLN B NE2   1 
ATOM   7502  N  N     . ARG B 1 243 ? 142.020 134.057 145.444 1.00 68.25 ?  243 ARG B N     1 
ATOM   7503  C  CA    . ARG B 1 243 ? 140.728 133.662 145.982 1.00 66.93 ?  243 ARG B CA    1 
ATOM   7504  C  C     . ARG B 1 243 ? 139.691 133.724 144.872 1.00 66.24 ?  243 ARG B C     1 
ATOM   7505  O  O     . ARG B 1 243 ? 139.693 134.657 144.064 1.00 65.42 ?  243 ARG B O     1 
ATOM   7506  C  CB    . ARG B 1 243 ? 140.322 134.566 147.155 1.00 66.32 ?  243 ARG B CB    1 
ATOM   7507  C  CG    . ARG B 1 243 ? 138.962 134.262 147.759 1.00 66.93 ?  243 ARG B CG    1 
ATOM   7508  C  CD    . ARG B 1 243 ? 138.456 135.447 148.569 1.00 67.50 ?  243 ARG B CD    1 
ATOM   7509  N  NE    . ARG B 1 243 ? 137.732 136.410 147.749 1.00 69.40 ?  243 ARG B NE    1 
ATOM   7510  C  CZ    . ARG B 1 243 ? 136.559 136.939 148.072 1.00 69.52 ?  243 ARG B CZ    1 
ATOM   7511  N  NH1   . ARG B 1 243 ? 135.947 136.624 149.201 1.00 66.61 1  243 ARG B NH1   1 
ATOM   7512  N  NH2   . ARG B 1 243 ? 135.988 137.808 147.243 1.00 64.05 ?  243 ARG B NH2   1 
ATOM   7513  N  N     . GLN B 1 244 ? 138.813 132.724 144.835 1.00 64.22 ?  244 GLN B N     1 
ATOM   7514  C  CA    . GLN B 1 244 ? 137.845 132.611 143.752 1.00 63.23 ?  244 GLN B CA    1 
ATOM   7515  C  C     . GLN B 1 244 ? 136.926 133.825 143.712 1.00 63.95 ?  244 GLN B C     1 
ATOM   7516  O  O     . GLN B 1 244 ? 136.421 134.274 144.745 1.00 61.87 ?  244 GLN B O     1 
ATOM   7517  C  CB    . GLN B 1 244 ? 137.026 131.331 143.911 1.00 61.27 ?  244 GLN B CB    1 
ATOM   7518  C  CG    . GLN B 1 244 ? 137.858 130.058 143.879 1.00 62.33 ?  244 GLN B CG    1 
ATOM   7519  C  CD    . GLN B 1 244 ? 137.005 128.804 143.864 1.00 62.46 ?  244 GLN B CD    1 
ATOM   7520  O  OE1   . GLN B 1 244 ? 135.982 128.727 144.544 1.00 60.44 ?  244 GLN B OE1   1 
ATOM   7521  N  NE2   . GLN B 1 244 ? 137.424 127.813 143.087 1.00 60.00 ?  244 GLN B NE2   1 
ATOM   7522  N  N     . GLY B 1 245 ? 136.717 134.358 142.508 1.00 49.21 ?  245 GLY B N     1 
ATOM   7523  C  CA    . GLY B 1 245 ? 135.850 135.505 142.317 1.00 44.50 ?  245 GLY B CA    1 
ATOM   7524  C  C     . GLY B 1 245 ? 134.406 135.211 142.660 1.00 44.34 ?  245 GLY B C     1 
ATOM   7525  O  O     . GLY B 1 245 ? 133.798 134.299 142.092 1.00 41.39 ?  245 GLY B O     1 
ATOM   7526  N  N     . SER B 1 246 ? 133.843 135.981 143.585 1.00 39.46 ?  246 SER B N     1 
ATOM   7527  C  CA    . SER B 1 246 ? 132.496 135.756 144.086 1.00 33.42 ?  246 SER B CA    1 
ATOM   7528  C  C     . SER B 1 246 ? 131.597 136.912 143.675 1.00 30.07 ?  246 SER B C     1 
ATOM   7529  O  O     . SER B 1 246 ? 131.935 138.079 143.893 1.00 23.53 ?  246 SER B O     1 
ATOM   7530  C  CB    . SER B 1 246 ? 132.498 135.602 145.609 1.00 31.88 ?  246 SER B CB    1 
ATOM   7531  O  OG    . SER B 1 246 ? 133.150 136.695 146.231 1.00 38.37 ?  246 SER B OG    1 
ATOM   7532  N  N     . GLY B 1 247 ? 130.453 136.580 143.082 1.00 26.03 ?  247 GLY B N     1 
ATOM   7533  C  CA    . GLY B 1 247 ? 129.488 137.582 142.695 1.00 10.12 ?  247 GLY B CA    1 
ATOM   7534  C  C     . GLY B 1 247 ? 128.082 137.092 142.969 1.00 12.49 ?  247 GLY B C     1 
ATOM   7535  O  O     . GLY B 1 247 ? 127.837 135.896 143.137 1.00 22.70 ?  247 GLY B O     1 
ATOM   7536  N  N     . ALA B 1 248 ? 127.156 138.043 143.015 1.00 17.14 ?  248 ALA B N     1 
ATOM   7537  C  CA    . ALA B 1 248 ? 125.758 137.750 143.274 1.00 17.75 ?  248 ALA B CA    1 
ATOM   7538  C  C     . ALA B 1 248 ? 124.891 138.440 142.234 1.00 16.83 ?  248 ALA B C     1 
ATOM   7539  O  O     . ALA B 1 248 ? 125.212 139.529 141.755 1.00 23.25 ?  248 ALA B O     1 
ATOM   7540  C  CB    . ALA B 1 248 ? 125.335 138.191 144.681 1.00 4.65  ?  248 ALA B CB    1 
ATOM   7541  N  N     . ALA B 1 249 ? 123.789 137.785 141.884 1.00 16.18 ?  249 ALA B N     1 
ATOM   7542  C  CA    . ALA B 1 249 ? 122.799 138.334 140.971 1.00 14.30 ?  249 ALA B CA    1 
ATOM   7543  C  C     . ALA B 1 249 ? 121.449 138.342 141.668 1.00 16.37 ?  249 ALA B C     1 
ATOM   7544  O  O     . ALA B 1 249 ? 121.067 137.353 142.298 1.00 24.63 ?  249 ALA B O     1 
ATOM   7545  C  CB    . ALA B 1 249 ? 122.730 137.526 139.675 1.00 11.62 ?  249 ALA B CB    1 
ATOM   7546  N  N     . TYR B 1 250 ? 120.735 139.454 141.562 1.00 17.18 ?  250 TYR B N     1 
ATOM   7547  C  CA    . TYR B 1 250 ? 119.433 139.601 142.189 1.00 5.89  ?  250 TYR B CA    1 
ATOM   7548  C  C     . TYR B 1 250 ? 118.373 139.820 141.124 1.00 7.44  ?  250 TYR B C     1 
ATOM   7549  O  O     . TYR B 1 250 ? 118.577 140.583 140.176 1.00 21.34 ?  250 TYR B O     1 
ATOM   7550  C  CB    . TYR B 1 250 ? 119.424 140.762 143.186 1.00 12.37 ?  250 TYR B CB    1 
ATOM   7551  C  CG    . TYR B 1 250 ? 119.908 140.381 144.563 1.00 15.54 ?  250 TYR B CG    1 
ATOM   7552  C  CD1   . TYR B 1 250 ? 121.254 140.154 144.808 1.00 8.40  ?  250 TYR B CD1   1 
ATOM   7553  C  CD2   . TYR B 1 250 ? 119.017 140.234 145.617 1.00 12.52 ?  250 TYR B CD2   1 
ATOM   7554  C  CE1   . TYR B 1 250 ? 121.701 139.800 146.061 1.00 1.20  ?  250 TYR B CE1   1 
ATOM   7555  C  CE2   . TYR B 1 250 ? 119.456 139.879 146.876 1.00 7.97  ?  250 TYR B CE2   1 
ATOM   7556  C  CZ    . TYR B 1 250 ? 120.800 139.665 147.091 1.00 11.67 ?  250 TYR B CZ    1 
ATOM   7557  O  OH    . TYR B 1 250 ? 121.244 139.315 148.343 1.00 21.15 ?  250 TYR B OH    1 
ATOM   7558  N  N     . LEU B 1 251 ? 117.244 139.139 141.284 1.00 14.84 ?  251 LEU B N     1 
ATOM   7559  C  CA    . LEU B 1 251 ? 116.116 139.286 140.381 1.00 15.67 ?  251 LEU B CA    1 
ATOM   7560  C  C     . LEU B 1 251 ? 114.838 139.399 141.192 1.00 10.15 ?  251 LEU B C     1 
ATOM   7561  O  O     . LEU B 1 251 ? 114.663 138.691 142.187 1.00 19.07 ?  251 LEU B O     1 
ATOM   7562  C  CB    . LEU B 1 251 ? 116.013 138.105 139.410 1.00 14.63 ?  251 LEU B CB    1 
ATOM   7563  C  CG    . LEU B 1 251 ? 115.183 138.355 138.154 1.00 14.48 ?  251 LEU B CG    1 
ATOM   7564  C  CD1   . LEU B 1 251 ? 115.900 139.301 137.216 1.00 6.94  ?  251 LEU B CD1   1 
ATOM   7565  C  CD2   . LEU B 1 251 ? 114.860 137.049 137.459 1.00 10.11 ?  251 LEU B CD2   1 
ATOM   7566  N  N     . ASN B 1 252 ? 113.952 140.293 140.766 1.00 12.31 ?  252 ASN B N     1 
ATOM   7567  C  CA    . ASN B 1 252 ? 112.642 140.397 141.390 1.00 10.56 ?  252 ASN B CA    1 
ATOM   7568  C  C     . ASN B 1 252 ? 111.827 139.142 141.110 1.00 17.18 ?  252 ASN B C     1 
ATOM   7569  O  O     . ASN B 1 252 ? 111.915 138.550 140.032 1.00 27.97 ?  252 ASN B O     1 
ATOM   7570  C  CB    . ASN B 1 252 ? 111.906 141.631 140.876 1.00 13.51 ?  252 ASN B CB    1 
ATOM   7571  C  CG    . ASN B 1 252 ? 110.920 142.181 141.885 1.00 20.90 ?  252 ASN B CG    1 
ATOM   7572  O  OD1   . ASN B 1 252 ? 109.867 141.591 142.124 1.00 31.96 ?  252 ASN B OD1   1 
ATOM   7573  N  ND2   . ASN B 1 252 ? 111.259 143.313 142.485 1.00 16.81 ?  252 ASN B ND2   1 
ATOM   7574  N  N     . ILE B 1 253 ? 111.028 138.730 142.097 1.00 12.04 ?  253 ILE B N     1 
ATOM   7575  C  CA    . ILE B 1 253 ? 110.209 137.536 141.930 1.00 17.59 ?  253 ILE B CA    1 
ATOM   7576  C  C     . ILE B 1 253 ? 109.123 137.737 140.879 1.00 23.32 ?  253 ILE B C     1 
ATOM   7577  O  O     . ILE B 1 253 ? 108.609 136.756 140.331 1.00 24.82 ?  253 ILE B O     1 
ATOM   7578  C  CB    . ILE B 1 253 ? 109.604 137.111 143.282 1.00 20.99 ?  253 ILE B CB    1 
ATOM   7579  C  CG1   . ILE B 1 253 ? 109.218 135.632 143.250 1.00 16.36 ?  253 ILE B CG1   1 
ATOM   7580  C  CG2   . ILE B 1 253 ? 108.417 137.988 143.645 1.00 14.57 ?  253 ILE B CG2   1 
ATOM   7581  C  CD1   . ILE B 1 253 ? 109.356 134.938 144.576 1.00 18.96 ?  253 ILE B CD1   1 
ATOM   7582  N  N     . PHE B 1 254 ? 108.764 138.981 140.573 1.00 30.33 ?  254 PHE B N     1 
ATOM   7583  C  CA    . PHE B 1 254 ? 107.785 139.274 139.537 1.00 18.12 ?  254 PHE B CA    1 
ATOM   7584  C  C     . PHE B 1 254 ? 108.417 139.429 138.161 1.00 20.80 ?  254 PHE B C     1 
ATOM   7585  O  O     . PHE B 1 254 ? 107.701 139.680 137.188 1.00 27.34 ?  254 PHE B O     1 
ATOM   7586  C  CB    . PHE B 1 254 ? 106.995 140.534 139.899 1.00 21.69 ?  254 PHE B CB    1 
ATOM   7587  C  CG    . PHE B 1 254 ? 105.918 140.297 140.919 1.00 26.47 ?  254 PHE B CG    1 
ATOM   7588  C  CD1   . PHE B 1 254 ? 104.832 139.494 140.619 1.00 25.87 ?  254 PHE B CD1   1 
ATOM   7589  C  CD2   . PHE B 1 254 ? 105.995 140.866 142.176 1.00 25.47 ?  254 PHE B CD2   1 
ATOM   7590  C  CE1   . PHE B 1 254 ? 103.841 139.271 141.551 1.00 29.44 ?  254 PHE B CE1   1 
ATOM   7591  C  CE2   . PHE B 1 254 ? 105.005 140.645 143.113 1.00 26.38 ?  254 PHE B CE2   1 
ATOM   7592  C  CZ    . PHE B 1 254 ? 103.928 139.846 142.799 1.00 25.35 ?  254 PHE B CZ    1 
ATOM   7593  N  N     . HIS B 1 255 ? 109.735 139.293 138.064 1.00 27.15 ?  255 HIS B N     1 
ATOM   7594  C  CA    . HIS B 1 255 ? 110.394 139.243 136.769 1.00 20.76 ?  255 HIS B CA    1 
ATOM   7595  C  C     . HIS B 1 255 ? 109.995 137.973 136.033 1.00 23.58 ?  255 HIS B C     1 
ATOM   7596  O  O     . HIS B 1 255 ? 109.823 136.911 136.638 1.00 30.47 ?  255 HIS B O     1 
ATOM   7597  C  CB    . HIS B 1 255 ? 111.910 139.302 136.943 1.00 17.98 ?  255 HIS B CB    1 
ATOM   7598  C  CG    . HIS B 1 255 ? 112.653 139.686 135.701 1.00 22.26 ?  255 HIS B CG    1 
ATOM   7599  N  ND1   . HIS B 1 255 ? 112.855 138.813 134.654 1.00 14.82 ?  255 HIS B ND1   1 
ATOM   7600  C  CD2   . HIS B 1 255 ? 113.256 140.845 135.346 1.00 20.06 ?  255 HIS B CD2   1 
ATOM   7601  C  CE1   . HIS B 1 255 ? 113.544 139.421 133.704 1.00 12.90 ?  255 HIS B CE1   1 
ATOM   7602  N  NE2   . HIS B 1 255 ? 113.802 140.653 134.100 1.00 12.09 ?  255 HIS B NE2   1 
ATOM   7603  N  N     . ARG B 1 256 ? 109.847 138.092 134.715 1.00 26.39 ?  256 ARG B N     1 
ATOM   7604  C  CA    . ARG B 1 256 ? 109.401 136.962 133.911 1.00 22.29 ?  256 ARG B CA    1 
ATOM   7605  C  C     . ARG B 1 256 ? 110.398 135.812 133.958 1.00 24.96 ?  256 ARG B C     1 
ATOM   7606  O  O     . ARG B 1 256 ? 110.008 134.640 133.958 1.00 32.64 ?  256 ARG B O     1 
ATOM   7607  C  CB    . ARG B 1 256 ? 109.169 137.421 132.475 1.00 26.13 ?  256 ARG B CB    1 
ATOM   7608  C  CG    . ARG B 1 256 ? 108.001 136.764 131.799 1.00 35.87 ?  256 ARG B CG    1 
ATOM   7609  C  CD    . ARG B 1 256 ? 108.366 135.398 131.272 1.00 31.95 ?  256 ARG B CD    1 
ATOM   7610  N  NE    . ARG B 1 256 ? 109.746 135.312 130.815 1.00 30.96 ?  256 ARG B NE    1 
ATOM   7611  C  CZ    . ARG B 1 256 ? 110.303 134.204 130.347 1.00 33.29 ?  256 ARG B CZ    1 
ATOM   7612  N  NH1   . ARG B 1 256 ? 109.626 133.069 130.272 1.00 30.55 1  256 ARG B NH1   1 
ATOM   7613  N  NH2   . ARG B 1 256 ? 111.570 134.233 129.949 1.00 34.33 ?  256 ARG B NH2   1 
ATOM   7614  N  N     . ASP B 1 257 ? 111.689 136.127 134.006 1.00 26.22 ?  257 ASP B N     1 
ATOM   7615  C  CA    . ASP B 1 257 ? 112.744 135.124 134.005 1.00 21.49 ?  257 ASP B CA    1 
ATOM   7616  C  C     . ASP B 1 257 ? 113.020 134.537 135.380 1.00 22.72 ?  257 ASP B C     1 
ATOM   7617  O  O     . ASP B 1 257 ? 114.098 133.968 135.575 1.00 27.09 ?  257 ASP B O     1 
ATOM   7618  C  CB    . ASP B 1 257 ? 114.032 135.721 133.440 1.00 25.70 ?  257 ASP B CB    1 
ATOM   7619  C  CG    . ASP B 1 257 ? 114.046 135.753 131.932 1.00 32.76 ?  257 ASP B CG    1 
ATOM   7620  O  OD1   . ASP B 1 257 ? 113.166 135.122 131.312 1.00 31.80 ?  257 ASP B OD1   1 
ATOM   7621  O  OD2   . ASP B 1 257 ? 114.937 136.413 131.366 1.00 36.44 -1 257 ASP B OD2   1 
ATOM   7622  N  N     . ILE B 1 258 ? 112.090 134.655 136.330 1.00 26.47 ?  258 ILE B N     1 
ATOM   7623  C  CA    . ILE B 1 258 ? 112.368 134.210 137.693 1.00 23.00 ?  258 ILE B CA    1 
ATOM   7624  C  C     . ILE B 1 258 ? 112.577 132.701 137.739 1.00 22.75 ?  258 ILE B C     1 
ATOM   7625  O  O     . ILE B 1 258 ? 113.441 132.207 138.470 1.00 34.15 ?  258 ILE B O     1 
ATOM   7626  C  CB    . ILE B 1 258 ? 111.250 134.671 138.647 1.00 27.55 ?  258 ILE B CB    1 
ATOM   7627  C  CG1   . ILE B 1 258 ? 111.591 134.298 140.093 1.00 24.90 ?  258 ILE B CG1   1 
ATOM   7628  C  CG2   . ILE B 1 258 ? 109.898 134.109 138.231 1.00 19.92 ?  258 ILE B CG2   1 
ATOM   7629  C  CD1   . ILE B 1 258 ? 112.887 134.902 140.584 1.00 17.22 ?  258 ILE B CD1   1 
ATOM   7630  N  N     . ASN B 1 259 ? 111.810 131.944 136.952 1.00 31.64 ?  259 ASN B N     1 
ATOM   7631  C  CA    . ASN B 1 259 ? 111.970 130.493 136.955 1.00 28.34 ?  259 ASN B CA    1 
ATOM   7632  C  C     . ASN B 1 259 ? 113.277 130.081 136.290 1.00 28.53 ?  259 ASN B C     1 
ATOM   7633  O  O     . ASN B 1 259 ? 113.971 129.183 136.778 1.00 30.84 ?  259 ASN B O     1 
ATOM   7634  C  CB    . ASN B 1 259 ? 110.776 129.829 136.271 1.00 29.00 ?  259 ASN B CB    1 
ATOM   7635  C  CG    . ASN B 1 259 ? 109.566 129.741 137.177 1.00 33.29 ?  259 ASN B CG    1 
ATOM   7636  O  OD1   . ASN B 1 259 ? 109.625 129.144 138.252 1.00 34.36 ?  259 ASN B OD1   1 
ATOM   7637  N  ND2   . ASN B 1 259 ? 108.461 130.336 136.749 1.00 34.97 ?  259 ASN B ND2   1 
ATOM   7638  N  N     . ASP B 1 260 ? 113.632 130.729 135.179 1.00 31.47 ?  260 ASP B N     1 
ATOM   7639  C  CA    . ASP B 1 260 ? 114.944 130.508 134.580 1.00 24.64 ?  260 ASP B CA    1 
ATOM   7640  C  C     . ASP B 1 260 ? 116.054 130.936 135.529 1.00 28.75 ?  260 ASP B C     1 
ATOM   7641  O  O     . ASP B 1 260 ? 117.101 130.282 135.612 1.00 33.75 ?  260 ASP B O     1 
ATOM   7642  C  CB    . ASP B 1 260 ? 115.049 131.264 133.257 1.00 27.87 ?  260 ASP B CB    1 
ATOM   7643  C  CG    . ASP B 1 260 ? 113.979 130.860 132.267 1.00 40.56 ?  260 ASP B CG    1 
ATOM   7644  O  OD1   . ASP B 1 260 ? 113.881 131.504 131.202 1.00 37.76 ?  260 ASP B OD1   1 
ATOM   7645  O  OD2   . ASP B 1 260 ? 113.235 129.899 132.554 1.00 42.90 -1 260 ASP B OD2   1 
ATOM   7646  N  N     . PHE B 1 261 ? 115.843 132.044 136.243 1.00 33.42 ?  261 PHE B N     1 
ATOM   7647  C  CA    . PHE B 1 261 ? 116.810 132.514 137.230 1.00 20.73 ?  261 PHE B CA    1 
ATOM   7648  C  C     . PHE B 1 261 ? 117.055 131.462 138.305 1.00 23.47 ?  261 PHE B C     1 
ATOM   7649  O  O     . PHE B 1 261 ? 118.199 131.230 138.710 1.00 26.79 ?  261 PHE B O     1 
ATOM   7650  C  CB    . PHE B 1 261 ? 116.295 133.813 137.847 1.00 14.21 ?  261 PHE B CB    1 
ATOM   7651  C  CG    . PHE B 1 261 ? 117.259 134.486 138.776 1.00 27.64 ?  261 PHE B CG    1 
ATOM   7652  C  CD1   . PHE B 1 261 ? 118.334 135.199 138.280 1.00 22.13 ?  261 PHE B CD1   1 
ATOM   7653  C  CD2   . PHE B 1 261 ? 117.068 134.439 140.145 1.00 21.15 ?  261 PHE B CD2   1 
ATOM   7654  C  CE1   . PHE B 1 261 ? 119.212 135.829 139.130 1.00 14.29 ?  261 PHE B CE1   1 
ATOM   7655  C  CE2   . PHE B 1 261 ? 117.945 135.069 140.999 1.00 12.58 ?  261 PHE B CE2   1 
ATOM   7656  C  CZ    . PHE B 1 261 ? 119.017 135.765 140.490 1.00 17.93 ?  261 PHE B CZ    1 
ATOM   7657  N  N     . LEU B 1 262 ? 115.988 130.815 138.778 1.00 31.41 ?  262 LEU B N     1 
ATOM   7658  C  CA    . LEU B 1 262 ? 116.128 129.803 139.817 1.00 25.47 ?  262 LEU B CA    1 
ATOM   7659  C  C     . LEU B 1 262 ? 116.692 128.497 139.274 1.00 30.04 ?  262 LEU B C     1 
ATOM   7660  O  O     . LEU B 1 262 ? 117.391 127.781 139.999 1.00 32.42 ?  262 LEU B O     1 
ATOM   7661  C  CB    . LEU B 1 262 ? 114.779 129.556 140.486 1.00 32.20 ?  262 LEU B CB    1 
ATOM   7662  C  CG    . LEU B 1 262 ? 114.127 130.772 141.137 1.00 22.35 ?  262 LEU B CG    1 
ATOM   7663  C  CD1   . LEU B 1 262 ? 112.754 130.416 141.671 1.00 29.16 ?  262 LEU B CD1   1 
ATOM   7664  C  CD2   . LEU B 1 262 ? 115.018 131.315 142.233 1.00 22.81 ?  262 LEU B CD2   1 
ATOM   7665  N  N     . ASP B 1 263 ? 116.405 128.168 138.013 1.00 42.45 ?  263 ASP B N     1 
ATOM   7666  C  CA    . ASP B 1 263 ? 116.880 126.916 137.435 1.00 31.66 ?  263 ASP B CA    1 
ATOM   7667  C  C     . ASP B 1 263 ? 118.391 126.875 137.265 1.00 34.41 ?  263 ASP B C     1 
ATOM   7668  O  O     . ASP B 1 263 ? 118.940 125.793 137.035 1.00 47.73 ?  263 ASP B O     1 
ATOM   7669  C  CB    . ASP B 1 263 ? 116.209 126.669 136.084 1.00 37.05 ?  263 ASP B CB    1 
ATOM   7670  C  CG    . ASP B 1 263 ? 114.733 126.363 136.214 1.00 46.24 ?  263 ASP B CG    1 
ATOM   7671  O  OD1   . ASP B 1 263 ? 114.273 126.115 137.346 1.00 42.48 ?  263 ASP B OD1   1 
ATOM   7672  O  OD2   . ASP B 1 263 ? 114.030 126.372 135.181 1.00 47.80 -1 263 ASP B OD2   1 
ATOM   7673  N  N     . THR B 1 264 ? 119.075 128.016 137.365 1.00 38.94 ?  264 THR B N     1 
ATOM   7674  C  CA    . THR B 1 264 ? 120.528 128.033 137.273 1.00 37.20 ?  264 THR B CA    1 
ATOM   7675  C  C     . THR B 1 264 ? 121.203 127.393 138.477 1.00 40.49 ?  264 THR B C     1 
ATOM   7676  O  O     . THR B 1 264 ? 122.405 127.115 138.415 1.00 41.51 ?  264 THR B O     1 
ATOM   7677  C  CB    . THR B 1 264 ? 121.029 129.470 137.108 1.00 34.86 ?  264 THR B CB    1 
ATOM   7678  O  OG1   . THR B 1 264 ? 120.628 130.253 138.240 1.00 37.84 ?  264 THR B OG1   1 
ATOM   7679  C  CG2   . THR B 1 264 ? 120.460 130.091 135.847 1.00 35.27 ?  264 THR B CG2   1 
ATOM   7680  N  N     . LYS B 1 265 ? 120.469 127.149 139.562 1.00 34.45 ?  265 LYS B N     1 
ATOM   7681  C  CA    . LYS B 1 265 ? 121.031 126.570 140.773 1.00 36.43 ?  265 LYS B CA    1 
ATOM   7682  C  C     . LYS B 1 265 ? 120.602 125.130 141.012 1.00 41.95 ?  265 LYS B C     1 
ATOM   7683  O  O     . LYS B 1 265 ? 120.994 124.545 142.027 1.00 44.94 ?  265 LYS B O     1 
ATOM   7684  C  CB    . LYS B 1 265 ? 120.655 127.426 141.987 1.00 35.53 ?  265 LYS B CB    1 
ATOM   7685  C  CG    . LYS B 1 265 ? 121.453 128.704 142.101 1.00 38.41 ?  265 LYS B CG    1 
ATOM   7686  C  CD    . LYS B 1 265 ? 122.935 128.422 141.992 1.00 42.43 ?  265 LYS B CD    1 
ATOM   7687  C  CE    . LYS B 1 265 ? 123.733 129.703 141.979 1.00 39.18 ?  265 LYS B CE    1 
ATOM   7688  N  NZ    . LYS B 1 265 ? 125.161 129.454 141.657 1.00 43.31 1  265 LYS B NZ    1 
ATOM   7689  N  N     . LYS B 1 266 ? 119.812 124.545 140.119 1.00 46.48 ?  266 LYS B N     1 
ATOM   7690  C  CA    . LYS B 1 266 ? 119.430 123.150 140.272 1.00 48.96 ?  266 LYS B CA    1 
ATOM   7691  C  C     . LYS B 1 266 ? 120.627 122.239 140.032 1.00 55.08 ?  266 LYS B C     1 
ATOM   7692  O  O     . LYS B 1 266 ? 121.518 122.542 139.234 1.00 56.31 ?  266 LYS B O     1 
ATOM   7693  C  CB    . LYS B 1 266 ? 118.297 122.795 139.310 1.00 48.89 ?  266 LYS B CB    1 
ATOM   7694  C  CG    . LYS B 1 266 ? 116.934 123.298 139.748 1.00 50.80 ?  266 LYS B CG    1 
ATOM   7695  C  CD    . LYS B 1 266 ? 115.874 122.989 138.706 1.00 51.90 ?  266 LYS B CD    1 
ATOM   7696  C  CE    . LYS B 1 266 ? 114.482 123.324 139.217 1.00 50.94 ?  266 LYS B CE    1 
ATOM   7697  N  NZ    . LYS B 1 266 ? 113.462 123.250 138.134 1.00 50.51 1  266 LYS B NZ    1 
ATOM   7698  N  N     . ILE B 1 267 ? 120.649 121.112 140.747 1.00 58.24 ?  267 ILE B N     1 
ATOM   7699  C  CA    . ILE B 1 267 ? 121.743 120.160 140.591 1.00 60.88 ?  267 ILE B CA    1 
ATOM   7700  C  C     . ILE B 1 267 ? 121.713 119.527 139.206 1.00 62.41 ?  267 ILE B C     1 
ATOM   7701  O  O     . ILE B 1 267 ? 122.758 119.139 138.669 1.00 61.60 ?  267 ILE B O     1 
ATOM   7702  C  CB    . ILE B 1 267 ? 121.695 119.089 141.697 1.00 62.07 ?  267 ILE B CB    1 
ATOM   7703  C  CG1   . ILE B 1 267 ? 121.938 119.716 143.072 1.00 61.89 ?  267 ILE B CG1   1 
ATOM   7704  C  CG2   . ILE B 1 267 ? 122.716 117.997 141.427 1.00 58.67 ?  267 ILE B CG2   1 
ATOM   7705  C  CD1   . ILE B 1 267 ? 120.673 119.959 143.872 1.00 60.76 ?  267 ILE B CD1   1 
ATOM   7706  N  N     . SER B 1 268 ? 120.531 119.412 138.607 1.00 63.05 ?  268 SER B N     1 
ATOM   7707  C  CA    . SER B 1 268 ? 120.366 118.839 137.280 1.00 64.65 ?  268 SER B CA    1 
ATOM   7708  C  C     . SER B 1 268 ? 120.445 119.880 136.171 1.00 65.97 ?  268 SER B C     1 
ATOM   7709  O  O     . SER B 1 268 ? 120.088 119.578 135.029 1.00 65.58 ?  268 SER B O     1 
ATOM   7710  C  CB    . SER B 1 268 ? 119.030 118.095 137.193 1.00 66.48 ?  268 SER B CB    1 
ATOM   7711  O  OG    . SER B 1 268 ? 117.958 118.941 137.569 1.00 61.93 ?  268 SER B OG    1 
ATOM   7712  N  N     . ALA B 1 269 ? 120.892 121.095 136.483 1.00 70.03 ?  269 ALA B N     1 
ATOM   7713  C  CA    . ALA B 1 269 ? 120.899 122.167 135.497 1.00 70.26 ?  269 ALA B CA    1 
ATOM   7714  C  C     . ALA B 1 269 ? 121.866 121.860 134.360 1.00 71.13 ?  269 ALA B C     1 
ATOM   7715  O  O     . ALA B 1 269 ? 122.958 121.324 134.574 1.00 68.97 ?  269 ALA B O     1 
ATOM   7716  C  CB    . ALA B 1 269 ? 121.272 123.493 136.159 1.00 66.54 ?  269 ALA B CB    1 
ATOM   7717  N  N     . ASP B 1 270 ? 121.453 122.202 133.143 1.00 74.02 ?  270 ASP B N     1 
ATOM   7718  C  CA    . ASP B 1 270 ? 122.306 122.034 131.977 1.00 74.33 ?  270 ASP B CA    1 
ATOM   7719  C  C     . ASP B 1 270 ? 123.508 122.969 132.058 1.00 73.93 ?  270 ASP B C     1 
ATOM   7720  O  O     . ASP B 1 270 ? 123.445 124.050 132.652 1.00 75.43 ?  270 ASP B O     1 
ATOM   7721  C  CB    . ASP B 1 270 ? 121.514 122.302 130.697 1.00 73.65 ?  270 ASP B CB    1 
ATOM   7722  C  CG    . ASP B 1 270 ? 122.135 121.651 129.477 1.00 76.84 ?  270 ASP B CG    1 
ATOM   7723  O  OD1   . ASP B 1 270 ? 123.319 121.924 129.188 1.00 75.94 ?  270 ASP B OD1   1 
ATOM   7724  O  OD2   . ASP B 1 270 ? 121.437 120.865 128.802 1.00 75.61 -1 270 ASP B OD2   1 
ATOM   7725  N  N     . GLU B 1 271 ? 124.618 122.539 131.453 1.00 74.27 ?  271 GLU B N     1 
ATOM   7726  C  CA    . GLU B 1 271 ? 125.847 123.322 131.510 1.00 75.67 ?  271 GLU B CA    1 
ATOM   7727  C  C     . GLU B 1 271 ? 125.733 124.649 130.771 1.00 73.53 ?  271 GLU B C     1 
ATOM   7728  O  O     . GLU B 1 271 ? 126.523 125.560 131.039 1.00 73.03 ?  271 GLU B O     1 
ATOM   7729  C  CB    . GLU B 1 271 ? 127.014 122.511 130.947 1.00 73.87 ?  271 GLU B CB    1 
ATOM   7730  C  CG    . GLU B 1 271 ? 127.439 121.349 131.830 1.00 73.21 ?  271 GLU B CG    1 
ATOM   7731  C  CD    . GLU B 1 271 ? 127.961 121.801 133.179 1.00 75.05 ?  271 GLU B CD    1 
ATOM   7732  O  OE1   . GLU B 1 271 ? 128.648 122.843 133.236 1.00 75.43 ?  271 GLU B OE1   1 
ATOM   7733  O  OE2   . GLU B 1 271 ? 127.682 121.117 134.186 1.00 74.89 -1 271 GLU B OE2   1 
ATOM   7734  N  N     . ASP B 1 272 ? 124.779 124.783 129.852 1.00 69.75 ?  272 ASP B N     1 
ATOM   7735  C  CA    . ASP B 1 272 ? 124.523 126.058 129.196 1.00 71.73 ?  272 ASP B CA    1 
ATOM   7736  C  C     . ASP B 1 272 ? 123.554 126.933 129.979 1.00 70.44 ?  272 ASP B C     1 
ATOM   7737  O  O     . ASP B 1 272 ? 123.243 128.042 129.535 1.00 66.88 ?  272 ASP B O     1 
ATOM   7738  C  CB    . ASP B 1 272 ? 123.995 125.830 127.772 1.00 70.85 ?  272 ASP B CB    1 
ATOM   7739  C  CG    . ASP B 1 272 ? 122.547 125.375 127.746 1.00 73.30 ?  272 ASP B CG    1 
ATOM   7740  O  OD1   . ASP B 1 272 ? 122.106 124.706 128.703 1.00 72.91 ?  272 ASP B OD1   1 
ATOM   7741  O  OD2   . ASP B 1 272 ? 121.846 125.688 126.759 1.00 70.51 -1 272 ASP B OD2   1 
ATOM   7742  N  N     . VAL B 1 273 ? 123.058 126.451 131.120 1.00 66.23 ?  273 VAL B N     1 
ATOM   7743  C  CA    . VAL B 1 273 ? 122.197 127.225 132.002 1.00 66.52 ?  273 VAL B CA    1 
ATOM   7744  C  C     . VAL B 1 273 ? 122.829 127.427 133.373 1.00 64.95 ?  273 VAL B C     1 
ATOM   7745  O  O     . VAL B 1 273 ? 122.723 128.511 133.958 1.00 66.14 ?  273 VAL B O     1 
ATOM   7746  C  CB    . VAL B 1 273 ? 120.808 126.563 132.139 1.00 68.18 ?  273 VAL B CB    1 
ATOM   7747  C  CG1   . VAL B 1 273 ? 119.922 127.360 133.088 1.00 62.76 ?  273 VAL B CG1   1 
ATOM   7748  C  CG2   . VAL B 1 273 ? 120.150 126.423 130.777 1.00 65.62 ?  273 VAL B CG2   1 
ATOM   7749  N  N     . ARG B 1 274 ? 123.499 126.402 133.896 1.00 62.96 ?  274 ARG B N     1 
ATOM   7750  C  CA    . ARG B 1 274 ? 124.040 126.452 135.247 1.00 61.76 ?  274 ARG B CA    1 
ATOM   7751  C  C     . ARG B 1 274 ? 125.129 127.512 135.370 1.00 62.60 ?  274 ARG B C     1 
ATOM   7752  O  O     . ARG B 1 274 ? 125.967 127.677 134.480 1.00 62.96 ?  274 ARG B O     1 
ATOM   7753  C  CB    . ARG B 1 274 ? 124.597 125.079 135.633 1.00 65.11 ?  274 ARG B CB    1 
ATOM   7754  C  CG    . ARG B 1 274 ? 125.737 125.113 136.639 1.00 62.82 ?  274 ARG B CG    1 
ATOM   7755  C  CD    . ARG B 1 274 ? 125.773 123.853 137.486 1.00 63.74 ?  274 ARG B CD    1 
ATOM   7756  N  NE    . ARG B 1 274 ? 126.199 122.690 136.716 1.00 66.77 ?  274 ARG B NE    1 
ATOM   7757  C  CZ    . ARG B 1 274 ? 125.435 121.635 136.466 1.00 68.61 ?  274 ARG B CZ    1 
ATOM   7758  N  NH1   . ARG B 1 274 ? 124.194 121.558 136.916 1.00 67.06 1  274 ARG B NH1   1 
ATOM   7759  N  NH2   . ARG B 1 274 ? 125.930 120.633 135.745 1.00 66.55 ?  274 ARG B NH2   1 
ATOM   7760  N  N     . VAL B 1 275 ? 125.106 128.236 136.488 1.00 49.50 ?  275 VAL B N     1 
ATOM   7761  C  CA    . VAL B 1 275 ? 126.157 129.176 136.861 1.00 46.65 ?  275 VAL B CA    1 
ATOM   7762  C  C     . VAL B 1 275 ? 126.792 128.677 138.152 1.00 49.29 ?  275 VAL B C     1 
ATOM   7763  O  O     . VAL B 1 275 ? 126.093 128.197 139.053 1.00 54.55 ?  275 VAL B O     1 
ATOM   7764  C  CB    . VAL B 1 275 ? 125.617 130.611 137.022 1.00 45.30 ?  275 VAL B CB    1 
ATOM   7765  C  CG1   . VAL B 1 275 ? 125.230 131.186 135.670 1.00 41.64 ?  275 VAL B CG1   1 
ATOM   7766  C  CG2   . VAL B 1 275 ? 124.429 130.636 137.966 1.00 48.00 ?  275 VAL B CG2   1 
ATOM   7767  N  N     . LYS B 1 276 ? 128.117 128.771 138.234 1.00 43.13 ?  276 LYS B N     1 
ATOM   7768  C  CA    . LYS B 1 276 ? 128.873 128.167 139.326 1.00 44.19 ?  276 LYS B CA    1 
ATOM   7769  C  C     . LYS B 1 276 ? 129.302 129.175 140.385 1.00 42.13 ?  276 LYS B C     1 
ATOM   7770  O  O     . LYS B 1 276 ? 129.117 128.931 141.581 1.00 48.13 ?  276 LYS B O     1 
ATOM   7771  C  CB    . LYS B 1 276 ? 130.114 127.430 138.791 1.00 45.94 ?  276 LYS B CB    1 
ATOM   7772  C  CG    . LYS B 1 276 ? 129.853 126.117 138.034 1.00 47.42 ?  276 LYS B CG    1 
ATOM   7773  C  CD    . LYS B 1 276 ? 129.208 126.273 136.655 1.00 48.40 ?  276 LYS B CD    1 
ATOM   7774  C  CE    . LYS B 1 276 ? 129.720 127.492 135.900 1.00 45.33 ?  276 LYS B CE    1 
ATOM   7775  N  NZ    . LYS B 1 276 ? 129.408 127.407 134.446 1.00 49.22 1  276 LYS B NZ    1 
ATOM   7776  N  N     . THR B 1 277 ? 129.878 130.301 139.975 1.00 38.02 ?  277 THR B N     1 
ATOM   7777  C  CA    . THR B 1 277 ? 130.436 131.275 140.902 1.00 39.22 ?  277 THR B CA    1 
ATOM   7778  C  C     . THR B 1 277 ? 129.520 132.467 141.134 1.00 38.73 ?  277 THR B C     1 
ATOM   7779  O  O     . THR B 1 277 ? 129.961 133.471 141.703 1.00 39.15 ?  277 THR B O     1 
ATOM   7780  C  CB    . THR B 1 277 ? 131.797 131.760 140.401 1.00 41.69 ?  277 THR B CB    1 
ATOM   7781  O  OG1   . THR B 1 277 ? 131.611 132.654 139.295 1.00 33.70 ?  277 THR B OG1   1 
ATOM   7782  C  CG2   . THR B 1 277 ? 132.648 130.581 139.963 1.00 39.64 ?  277 THR B CG2   1 
ATOM   7783  N  N     . LEU B 1 278 ? 128.263 132.384 140.710 1.00 34.18 ?  278 LEU B N     1 
ATOM   7784  C  CA    . LEU B 1 278 ? 127.319 133.491 140.811 1.00 28.24 ?  278 LEU B CA    1 
ATOM   7785  C  C     . LEU B 1 278 ? 126.207 133.102 141.775 1.00 24.52 ?  278 LEU B C     1 
ATOM   7786  O  O     . LEU B 1 278 ? 125.327 132.311 141.424 1.00 36.61 ?  278 LEU B O     1 
ATOM   7787  C  CB    . LEU B 1 278 ? 126.753 133.849 139.438 1.00 30.67 ?  278 LEU B CB    1 
ATOM   7788  C  CG    . LEU B 1 278 ? 126.207 135.265 139.260 1.00 28.70 ?  278 LEU B CG    1 
ATOM   7789  C  CD1   . LEU B 1 278 ? 127.339 136.254 139.081 1.00 24.89 ?  278 LEU B CD1   1 
ATOM   7790  C  CD2   . LEU B 1 278 ? 125.260 135.321 138.079 1.00 27.96 ?  278 LEU B CD2   1 
ATOM   7791  N  N     . SER B 1 279 ? 126.249 133.654 142.983 1.00 24.89 ?  279 SER B N     1 
ATOM   7792  C  CA    . SER B 1 279 ? 125.147 133.492 143.919 1.00 17.98 ?  279 SER B CA    1 
ATOM   7793  C  C     . SER B 1 279 ? 123.918 134.226 143.402 1.00 21.42 ?  279 SER B C     1 
ATOM   7794  O  O     . SER B 1 279 ? 124.018 135.187 142.638 1.00 30.82 ?  279 SER B O     1 
ATOM   7795  C  CB    . SER B 1 279 ? 125.532 134.025 145.297 1.00 18.46 ?  279 SER B CB    1 
ATOM   7796  O  OG    . SER B 1 279 ? 126.723 133.420 145.764 1.00 31.78 ?  279 SER B OG    1 
ATOM   7797  N  N     . ILE B 1 280 ? 122.744 133.759 143.814 1.00 19.86 ?  280 ILE B N     1 
ATOM   7798  C  CA    . ILE B 1 280 ? 121.488 134.336 143.359 1.00 20.27 ?  280 ILE B CA    1 
ATOM   7799  C  C     . ILE B 1 280 ? 120.666 134.759 144.564 1.00 12.37 ?  280 ILE B C     1 
ATOM   7800  O  O     . ILE B 1 280 ? 120.649 134.077 145.593 1.00 25.03 ?  280 ILE B O     1 
ATOM   7801  C  CB    . ILE B 1 280 ? 120.693 133.364 142.462 1.00 15.42 ?  280 ILE B CB    1 
ATOM   7802  C  CG1   . ILE B 1 280 ? 120.338 132.076 143.203 1.00 21.88 ?  280 ILE B CG1   1 
ATOM   7803  C  CG2   . ILE B 1 280 ? 121.477 133.042 141.216 1.00 16.03 ?  280 ILE B CG2   1 
ATOM   7804  C  CD1   . ILE B 1 280 ? 119.125 131.380 142.631 1.00 15.40 ?  280 ILE B CD1   1 
ATOM   7805  N  N     . GLY B 1 281 ? 120.017 135.902 144.443 1.00 6.93  ?  281 GLY B N     1 
ATOM   7806  C  CA    . GLY B 1 281 ? 119.073 136.355 145.450 1.00 6.77  ?  281 GLY B CA    1 
ATOM   7807  C  C     . GLY B 1 281 ? 117.777 136.775 144.796 1.00 4.21  ?  281 GLY B C     1 
ATOM   7808  O  O     . GLY B 1 281 ? 117.777 137.374 143.725 1.00 20.89 ?  281 GLY B O     1 
ATOM   7809  N  N     . VAL B 1 282 ? 116.670 136.445 145.451 1.00 13.07 ?  282 VAL B N     1 
ATOM   7810  C  CA    . VAL B 1 282 ? 115.338 136.759 144.951 1.00 16.12 ?  282 VAL B CA    1 
ATOM   7811  C  C     . VAL B 1 282 ? 114.750 137.869 145.809 1.00 12.86 ?  282 VAL B C     1 
ATOM   7812  O  O     . VAL B 1 282 ? 114.775 137.791 147.043 1.00 21.68 ?  282 VAL B O     1 
ATOM   7813  C  CB    . VAL B 1 282 ? 114.429 135.518 144.942 1.00 16.31 ?  282 VAL B CB    1 
ATOM   7814  C  CG1   . VAL B 1 282 ? 112.987 135.916 144.702 1.00 20.40 ?  282 VAL B CG1   1 
ATOM   7815  C  CG2   . VAL B 1 282 ? 114.883 134.558 143.868 1.00 22.87 ?  282 VAL B CG2   1 
ATOM   7816  N  N     . VAL B 1 283 ? 114.234 138.902 145.155 1.00 2.61  ?  283 VAL B N     1 
ATOM   7817  C  CA    . VAL B 1 283 ? 113.567 140.011 145.822 1.00 9.73  ?  283 VAL B CA    1 
ATOM   7818  C  C     . VAL B 1 283 ? 112.068 139.760 145.777 1.00 12.01 ?  283 VAL B C     1 
ATOM   7819  O  O     . VAL B 1 283 ? 111.494 139.572 144.699 1.00 22.77 ?  283 VAL B O     1 
ATOM   7820  C  CB    . VAL B 1 283 ? 113.926 141.352 145.161 1.00 8.36  ?  283 VAL B CB    1 
ATOM   7821  C  CG1   . VAL B 1 283 ? 113.459 142.501 146.023 1.00 10.05 ?  283 VAL B CG1   1 
ATOM   7822  C  CG2   . VAL B 1 283 ? 115.422 141.430 144.922 1.00 9.21  ?  283 VAL B CG2   1 
ATOM   7823  N  N     . ILE B 1 284 ? 111.436 139.748 146.946 1.00 16.01 ?  284 ILE B N     1 
ATOM   7824  C  CA    . ILE B 1 284 ? 110.021 139.408 147.050 1.00 17.63 ?  284 ILE B CA    1 
ATOM   7825  C  C     . ILE B 1 284 ? 109.245 140.579 147.640 1.00 21.20 ?  284 ILE B C     1 
ATOM   7826  O  O     . ILE B 1 284 ? 109.393 140.882 148.833 1.00 24.03 ?  284 ILE B O     1 
ATOM   7827  C  CB    . ILE B 1 284 ? 109.815 138.140 147.893 1.00 14.12 ?  284 ILE B CB    1 
ATOM   7828  C  CG1   . ILE B 1 284 ? 110.680 136.999 147.359 1.00 17.29 ?  284 ILE B CG1   1 
ATOM   7829  C  CG2   . ILE B 1 284 ? 108.350 137.743 147.905 1.00 15.92 ?  284 ILE B CG2   1 
ATOM   7830  C  CD1   . ILE B 1 284 ? 110.466 135.691 148.073 1.00 20.09 ?  284 ILE B CD1   1 
ATOM   7831  N  N     . PRO B 1 285 ? 108.421 141.264 146.854 1.00 20.06 ?  285 PRO B N     1 
ATOM   7832  C  CA    . PRO B 1 285 ? 107.525 142.273 147.426 1.00 29.69 ?  285 PRO B CA    1 
ATOM   7833  C  C     . PRO B 1 285 ? 106.401 141.626 148.217 1.00 28.16 ?  285 PRO B C     1 
ATOM   7834  O  O     . PRO B 1 285 ? 106.145 140.423 148.125 1.00 23.12 ?  285 PRO B O     1 
ATOM   7835  C  CB    . PRO B 1 285 ? 106.983 143.011 146.197 1.00 22.68 ?  285 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 1 285 ? 107.914 142.660 145.084 1.00 20.66 ?  285 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 1 285 ? 108.407 141.286 145.384 1.00 14.72 ?  285 PRO B CD    1 
ATOM   7838  N  N     . ASP B 1 286 ? 105.722 142.452 149.015 1.00 31.68 ?  286 ASP B N     1 
ATOM   7839  C  CA    . ASP B 1 286 ? 104.579 141.968 149.783 1.00 25.85 ?  286 ASP B CA    1 
ATOM   7840  C  C     . ASP B 1 286 ? 103.451 141.482 148.886 1.00 32.58 ?  286 ASP B C     1 
ATOM   7841  O  O     . ASP B 1 286 ? 102.629 140.673 149.328 1.00 36.13 ?  286 ASP B O     1 
ATOM   7842  C  CB    . ASP B 1 286 ? 104.058 143.064 150.712 1.00 27.89 ?  286 ASP B CB    1 
ATOM   7843  C  CG    . ASP B 1 286 ? 104.630 142.967 152.109 1.00 42.45 ?  286 ASP B CG    1 
ATOM   7844  O  OD1   . ASP B 1 286 ? 105.548 142.149 152.325 1.00 38.68 ?  286 ASP B OD1   1 
ATOM   7845  O  OD2   . ASP B 1 286 ? 104.166 143.716 152.994 1.00 45.98 -1 286 ASP B OD2   1 
ATOM   7846  N  N     . LYS B 1 287 ? 103.391 141.964 147.642 1.00 35.56 ?  287 LYS B N     1 
ATOM   7847  C  CA    . LYS B 1 287 ? 102.342 141.533 146.725 1.00 29.84 ?  287 LYS B CA    1 
ATOM   7848  C  C     . LYS B 1 287 ? 102.437 140.041 146.435 1.00 31.94 ?  287 LYS B C     1 
ATOM   7849  O  O     . LYS B 1 287 ? 101.416 139.348 146.373 1.00 37.47 ?  287 LYS B O     1 
ATOM   7850  C  CB    . LYS B 1 287 ? 102.418 142.336 145.427 1.00 29.52 ?  287 LYS B CB    1 
ATOM   7851  C  CG    . LYS B 1 287 ? 101.187 142.205 144.549 1.00 27.75 ?  287 LYS B CG    1 
ATOM   7852  C  CD    . LYS B 1 287 ? 99.936  142.582 145.320 1.00 34.61 ?  287 LYS B CD    1 
ATOM   7853  C  CE    . LYS B 1 287 ? 98.715  142.600 144.422 1.00 35.33 ?  287 LYS B CE    1 
ATOM   7854  N  NZ    . LYS B 1 287 ? 97.540  143.204 145.105 1.00 36.98 1  287 LYS B NZ    1 
ATOM   7855  N  N     . PHE B 1 288 ? 103.655 139.528 146.247 1.00 31.64 ?  288 PHE B N     1 
ATOM   7856  C  CA    . PHE B 1 288 ? 103.821 138.102 145.982 1.00 25.08 ?  288 PHE B CA    1 
ATOM   7857  C  C     . PHE B 1 288 ? 103.385 137.262 147.175 1.00 26.26 ?  288 PHE B C     1 
ATOM   7858  O  O     . PHE B 1 288 ? 102.729 136.227 147.006 1.00 36.76 ?  288 PHE B O     1 
ATOM   7859  C  CB    . PHE B 1 288 ? 105.273 137.802 145.618 1.00 26.32 ?  288 PHE B CB    1 
ATOM   7860  C  CG    . PHE B 1 288 ? 105.494 136.403 145.127 1.00 26.81 ?  288 PHE B CG    1 
ATOM   7861  C  CD1   . PHE B 1 288 ? 105.792 135.384 146.014 1.00 23.51 ?  288 PHE B CD1   1 
ATOM   7862  C  CD2   . PHE B 1 288 ? 105.402 136.107 143.780 1.00 24.59 ?  288 PHE B CD2   1 
ATOM   7863  C  CE1   . PHE B 1 288 ? 105.993 134.098 145.566 1.00 23.18 ?  288 PHE B CE1   1 
ATOM   7864  C  CE2   . PHE B 1 288 ? 105.605 134.823 143.326 1.00 30.28 ?  288 PHE B CE2   1 
ATOM   7865  C  CZ    . PHE B 1 288 ? 105.901 133.817 144.222 1.00 29.49 ?  288 PHE B CZ    1 
ATOM   7866  N  N     . VAL B 1 289 ? 103.747 137.684 148.386 1.00 33.44 ?  289 VAL B N     1 
ATOM   7867  C  CA    . VAL B 1 289 ? 103.351 136.943 149.577 1.00 30.03 ?  289 VAL B CA    1 
ATOM   7868  C  C     . VAL B 1 289 ? 101.841 136.997 149.758 1.00 32.62 ?  289 VAL B C     1 
ATOM   7869  O  O     . VAL B 1 289 ? 101.219 136.025 150.197 1.00 35.56 ?  289 VAL B O     1 
ATOM   7870  C  CB    . VAL B 1 289 ? 104.097 137.481 150.811 1.00 32.52 ?  289 VAL B CB    1 
ATOM   7871  C  CG1   . VAL B 1 289 ? 103.695 136.710 152.057 1.00 31.58 ?  289 VAL B CG1   1 
ATOM   7872  C  CG2   . VAL B 1 289 ? 105.598 137.402 150.594 1.00 25.79 ?  289 VAL B CG2   1 
ATOM   7873  N  N     . GLU B 1 290 ? 101.225 138.132 149.422 1.00 36.62 ?  290 GLU B N     1 
ATOM   7874  C  CA    . GLU B 1 290 ? 99.773  138.237 149.499 1.00 33.24 ?  290 GLU B CA    1 
ATOM   7875  C  C     . GLU B 1 290 ? 99.094  137.325 148.484 1.00 37.81 ?  290 GLU B C     1 
ATOM   7876  O  O     . GLU B 1 290 ? 98.075  136.696 148.790 1.00 45.39 ?  290 GLU B O     1 
ATOM   7877  C  CB    . GLU B 1 290 ? 99.345  139.690 149.292 1.00 36.09 ?  290 GLU B CB    1 
ATOM   7878  C  CG    . GLU B 1 290 ? 97.844  139.909 149.313 1.00 39.32 ?  290 GLU B CG    1 
ATOM   7879  C  CD    . GLU B 1 290 ? 97.471  141.378 149.280 1.00 48.27 ?  290 GLU B CD    1 
ATOM   7880  O  OE1   . GLU B 1 290 ? 97.909  142.082 148.345 1.00 46.35 ?  290 GLU B OE1   1 
ATOM   7881  O  OE2   . GLU B 1 290 ? 96.738  141.828 150.185 1.00 49.09 -1 290 GLU B OE2   1 
ATOM   7882  N  N     . LEU B 1 291 ? 99.640  137.246 147.268 1.00 30.84 ?  291 LEU B N     1 
ATOM   7883  C  CA    . LEU B 1 291 ? 99.067  136.367 146.252 1.00 27.61 ?  291 LEU B CA    1 
ATOM   7884  C  C     . LEU B 1 291 ? 99.216  134.903 146.637 1.00 34.77 ?  291 LEU B C     1 
ATOM   7885  O  O     . LEU B 1 291 ? 98.293  134.106 146.439 1.00 38.54 ?  291 LEU B O     1 
ATOM   7886  C  CB    . LEU B 1 291 ? 99.721  136.631 144.896 1.00 32.42 ?  291 LEU B CB    1 
ATOM   7887  C  CG    . LEU B 1 291 ? 99.457  137.995 144.259 1.00 33.84 ?  291 LEU B CG    1 
ATOM   7888  C  CD1   . LEU B 1 291 ? 100.455 138.258 143.148 1.00 26.96 ?  291 LEU B CD1   1 
ATOM   7889  C  CD2   . LEU B 1 291 ? 98.034  138.082 143.740 1.00 31.97 ?  291 LEU B CD2   1 
ATOM   7890  N  N     . ALA B 1 292 ? 100.375 134.525 147.181 1.00 41.06 ?  292 ALA B N     1 
ATOM   7891  C  CA    . ALA B 1 292 ? 100.576 133.147 147.616 1.00 31.29 ?  292 ALA B CA    1 
ATOM   7892  C  C     . ALA B 1 292 ? 99.718  132.809 148.827 1.00 31.33 ?  292 ALA B C     1 
ATOM   7893  O  O     . ALA B 1 292 ? 99.259  131.670 148.962 1.00 38.52 ?  292 ALA B O     1 
ATOM   7894  C  CB    . ALA B 1 292 ? 102.052 132.903 147.927 1.00 27.35 ?  292 ALA B CB    1 
ATOM   7895  N  N     . ARG B 1 293 ? 99.496  133.779 149.715 1.00 36.05 ?  293 ARG B N     1 
ATOM   7896  C  CA    . ARG B 1 293 ? 98.685  133.540 150.903 1.00 36.19 ?  293 ARG B CA    1 
ATOM   7897  C  C     . ARG B 1 293 ? 97.251  133.187 150.532 1.00 41.29 ?  293 ARG B C     1 
ATOM   7898  O  O     . ARG B 1 293 ? 96.655  132.277 151.119 1.00 47.95 ?  293 ARG B O     1 
ATOM   7899  C  CB    . ARG B 1 293 ? 98.723  134.774 151.804 1.00 37.33 ?  293 ARG B CB    1 
ATOM   7900  C  CG    . ARG B 1 293 ? 97.752  134.756 152.965 1.00 37.72 ?  293 ARG B CG    1 
ATOM   7901  C  CD    . ARG B 1 293 ? 97.707  136.120 153.627 1.00 38.99 ?  293 ARG B CD    1 
ATOM   7902  N  NE    . ARG B 1 293 ? 99.048  136.657 153.826 1.00 45.33 ?  293 ARG B NE    1 
ATOM   7903  C  CZ    . ARG B 1 293 ? 99.423  137.883 153.485 1.00 43.13 ?  293 ARG B CZ    1 
ATOM   7904  N  NH1   . ARG B 1 293 ? 98.578  138.737 152.933 1.00 42.09 1  293 ARG B NH1   1 
ATOM   7905  N  NH2   . ARG B 1 293 ? 100.680 138.259 153.703 1.00 40.00 ?  293 ARG B NH2   1 
ATOM   7906  N  N     . GLU B 1 294 ? 96.685  133.890 149.558 1.00 48.58 ?  294 GLU B N     1 
ATOM   7907  C  CA    . GLU B 1 294 ? 95.320  133.653 149.113 1.00 47.69 ?  294 GLU B CA    1 
ATOM   7908  C  C     . GLU B 1 294 ? 95.235  132.644 147.976 1.00 45.66 ?  294 GLU B C     1 
ATOM   7909  O  O     . GLU B 1 294 ? 94.138  132.403 147.464 1.00 48.04 ?  294 GLU B O     1 
ATOM   7910  C  CB    . GLU B 1 294 ? 94.673  134.972 148.685 1.00 44.43 ?  294 GLU B CB    1 
ATOM   7911  C  CG    . GLU B 1 294 ? 94.558  135.992 149.803 1.00 48.49 ?  294 GLU B CG    1 
ATOM   7912  C  CD    . GLU B 1 294 ? 94.622  137.417 149.294 1.00 55.04 ?  294 GLU B CD    1 
ATOM   7913  O  OE1   . GLU B 1 294 ? 94.789  137.602 148.071 1.00 56.38 ?  294 GLU B OE1   1 
ATOM   7914  O  OE2   . GLU B 1 294 ? 94.509  138.350 150.117 1.00 54.30 -1 294 GLU B OE2   1 
ATOM   7915  N  N     . ASP B 1 295 ? 96.365  132.065 147.568 1.00 44.07 ?  295 ASP B N     1 
ATOM   7916  C  CA    . ASP B 1 295 ? 96.439  131.041 146.527 1.00 43.93 ?  295 ASP B CA    1 
ATOM   7917  C  C     . ASP B 1 295 ? 95.944  131.539 145.173 1.00 49.15 ?  295 ASP B C     1 
ATOM   7918  O  O     . ASP B 1 295 ? 95.648  130.734 144.285 1.00 47.46 ?  295 ASP B O     1 
ATOM   7919  C  CB    . ASP B 1 295 ? 95.675  129.773 146.930 1.00 45.64 ?  295 ASP B CB    1 
ATOM   7920  C  CG    . ASP B 1 295 ? 96.415  128.502 146.558 1.00 52.77 ?  295 ASP B CG    1 
ATOM   7921  O  OD1   . ASP B 1 295 ? 97.333  128.573 145.715 1.00 54.24 ?  295 ASP B OD1   1 
ATOM   7922  O  OD2   . ASP B 1 295 ? 96.076  127.432 147.103 1.00 50.23 -1 295 ASP B OD2   1 
ATOM   7923  N  N     . LYS B 1 296 ? 95.843  132.854 144.993 1.00 49.66 ?  296 LYS B N     1 
ATOM   7924  C  CA    . LYS B 1 296 ? 95.505  133.398 143.686 1.00 47.19 ?  296 LYS B CA    1 
ATOM   7925  C  C     . LYS B 1 296 ? 96.662  133.187 142.721 1.00 45.50 ?  296 LYS B C     1 
ATOM   7926  O  O     . LYS B 1 296 ? 97.830  133.336 143.088 1.00 51.87 ?  296 LYS B O     1 
ATOM   7927  C  CB    . LYS B 1 296 ? 95.180  134.887 143.790 1.00 46.04 ?  296 LYS B CB    1 
ATOM   7928  C  CG    . LYS B 1 296 ? 94.627  135.314 145.135 1.00 47.76 ?  296 LYS B CG    1 
ATOM   7929  C  CD    . LYS B 1 296 ? 93.625  136.445 144.990 1.00 49.04 ?  296 LYS B CD    1 
ATOM   7930  C  CE    . LYS B 1 296 ? 92.246  135.918 144.632 1.00 51.74 ?  296 LYS B CE    1 
ATOM   7931  N  NZ    . LYS B 1 296 ? 91.696  135.030 145.693 1.00 50.32 1  296 LYS B NZ    1 
ATOM   7932  N  N     . ALA B 1 297 ? 96.337  132.836 141.481 1.00 45.38 ?  297 ALA B N     1 
ATOM   7933  C  CA    . ALA B 1 297 ? 97.368  132.650 140.471 1.00 46.15 ?  297 ALA B CA    1 
ATOM   7934  C  C     . ALA B 1 297 ? 98.002  133.991 140.125 1.00 45.62 ?  297 ALA B C     1 
ATOM   7935  O  O     . ALA B 1 297 ? 97.302  134.965 139.830 1.00 53.38 ?  297 ALA B O     1 
ATOM   7936  C  CB    . ALA B 1 297 ? 96.779  131.996 139.225 1.00 44.20 ?  297 ALA B CB    1 
ATOM   7937  N  N     . ALA B 1 298 ? 99.329  134.041 140.164 1.00 38.81 ?  298 ALA B N     1 
ATOM   7938  C  CA    . ALA B 1 298 ? 100.072 135.280 140.000 1.00 39.74 ?  298 ALA B CA    1 
ATOM   7939  C  C     . ALA B 1 298 ? 100.607 135.410 138.580 1.00 37.91 ?  298 ALA B C     1 
ATOM   7940  O  O     . ALA B 1 298 ? 100.580 134.470 137.783 1.00 41.21 ?  298 ALA B O     1 
ATOM   7941  C  CB    . ALA B 1 298 ? 101.219 135.354 141.011 1.00 42.58 ?  298 ALA B CB    1 
ATOM   7942  N  N     . TYR B 1 299 ? 101.107 136.603 138.273 1.00 38.47 ?  299 TYR B N     1 
ATOM   7943  C  CA    . TYR B 1 299 ? 101.646 136.929 136.962 1.00 31.67 ?  299 TYR B CA    1 
ATOM   7944  C  C     . TYR B 1 299 ? 103.067 137.448 137.109 1.00 33.77 ?  299 TYR B C     1 
ATOM   7945  O  O     . TYR B 1 299 ? 103.334 138.306 137.955 1.00 41.45 ?  299 TYR B O     1 
ATOM   7946  C  CB    . TYR B 1 299 ? 100.784 137.980 136.260 1.00 32.93 ?  299 TYR B CB    1 
ATOM   7947  C  CG    . TYR B 1 299 ? 99.518  137.438 135.642 1.00 35.07 ?  299 TYR B CG    1 
ATOM   7948  C  CD1   . TYR B 1 299 ? 99.565  136.633 134.514 1.00 37.58 ?  299 TYR B CD1   1 
ATOM   7949  C  CD2   . TYR B 1 299 ? 98.277  137.737 136.184 1.00 36.23 ?  299 TYR B CD2   1 
ATOM   7950  C  CE1   . TYR B 1 299 ? 98.411  136.139 133.945 1.00 41.02 ?  299 TYR B CE1   1 
ATOM   7951  C  CE2   . TYR B 1 299 ? 97.118  137.247 135.622 1.00 39.48 ?  299 TYR B CE2   1 
ATOM   7952  C  CZ    . TYR B 1 299 ? 97.190  136.449 134.503 1.00 44.62 ?  299 TYR B CZ    1 
ATOM   7953  O  OH    . TYR B 1 299 ? 96.035  135.959 133.938 1.00 45.44 ?  299 TYR B OH    1 
ATOM   7954  N  N     . VAL B 1 300 ? 103.973 136.925 136.291 1.00 32.57 ?  300 VAL B N     1 
ATOM   7955  C  CA    . VAL B 1 300 ? 105.302 137.499 136.121 1.00 28.85 ?  300 VAL B CA    1 
ATOM   7956  C  C     . VAL B 1 300 ? 105.297 138.290 134.825 1.00 27.75 ?  300 VAL B C     1 
ATOM   7957  O  O     . VAL B 1 300 ? 104.671 137.883 133.840 1.00 32.37 ?  300 VAL B O     1 
ATOM   7958  C  CB    . VAL B 1 300 ? 106.397 136.415 136.117 1.00 24.24 ?  300 VAL B CB    1 
ATOM   7959  C  CG1   . VAL B 1 300 ? 106.646 135.916 137.528 1.00 26.78 ?  300 VAL B CG1   1 
ATOM   7960  C  CG2   . VAL B 1 300 ? 106.012 135.269 135.199 1.00 31.98 ?  300 VAL B CG2   1 
ATOM   7961  N  N     . PHE B 1 301 ? 105.983 139.425 134.819 1.00 30.11 ?  301 PHE B N     1 
ATOM   7962  C  CA    . PHE B 1 301 ? 105.847 140.400 133.750 1.00 23.39 ?  301 PHE B CA    1 
ATOM   7963  C  C     . PHE B 1 301 ? 107.143 140.538 132.969 1.00 31.95 ?  301 PHE B C     1 
ATOM   7964  O  O     . PHE B 1 301 ? 108.239 140.377 133.514 1.00 33.95 ?  301 PHE B O     1 
ATOM   7965  C  CB    . PHE B 1 301 ? 105.434 141.763 134.307 1.00 24.46 ?  301 PHE B CB    1 
ATOM   7966  C  CG    . PHE B 1 301 ? 104.251 141.703 135.224 1.00 31.13 ?  301 PHE B CG    1 
ATOM   7967  C  CD1   . PHE B 1 301 ? 102.965 141.720 134.717 1.00 28.85 ?  301 PHE B CD1   1 
ATOM   7968  C  CD2   . PHE B 1 301 ? 104.426 141.617 136.593 1.00 27.61 ?  301 PHE B CD2   1 
ATOM   7969  C  CE1   . PHE B 1 301 ? 101.876 141.658 135.557 1.00 30.97 ?  301 PHE B CE1   1 
ATOM   7970  C  CE2   . PHE B 1 301 ? 103.339 141.555 137.437 1.00 28.61 ?  301 PHE B CE2   1 
ATOM   7971  C  CZ    . PHE B 1 301 ? 102.063 141.577 136.918 1.00 33.66 ?  301 PHE B CZ    1 
ATOM   7972  N  N     . TYR B 1 302 ? 107.002 140.833 131.682 1.00 31.27 ?  302 TYR B N     1 
ATOM   7973  C  CA    . TYR B 1 302 ? 108.149 141.172 130.856 1.00 28.12 ?  302 TYR B CA    1 
ATOM   7974  C  C     . TYR B 1 302 ? 108.531 142.623 131.121 1.00 29.09 ?  302 TYR B C     1 
ATOM   7975  O  O     . TYR B 1 302 ? 107.725 143.520 130.854 1.00 32.21 ?  302 TYR B O     1 
ATOM   7976  C  CB    . TYR B 1 302 ? 107.830 140.967 129.381 1.00 29.30 ?  302 TYR B CB    1 
ATOM   7977  C  CG    . TYR B 1 302 ? 107.646 139.520 128.976 1.00 31.34 ?  302 TYR B CG    1 
ATOM   7978  C  CD1   . TYR B 1 302 ? 106.486 138.830 129.298 1.00 30.03 ?  302 TYR B CD1   1 
ATOM   7979  C  CD2   . TYR B 1 302 ? 108.632 138.846 128.269 1.00 29.42 ?  302 TYR B CD2   1 
ATOM   7980  C  CE1   . TYR B 1 302 ? 106.313 137.513 128.927 1.00 30.43 ?  302 TYR B CE1   1 
ATOM   7981  C  CE2   . TYR B 1 302 ? 108.468 137.528 127.897 1.00 31.36 ?  302 TYR B CE2   1 
ATOM   7982  C  CZ    . TYR B 1 302 ? 107.307 136.867 128.229 1.00 34.48 ?  302 TYR B CZ    1 
ATOM   7983  O  OH    . TYR B 1 302 ? 107.137 135.552 127.860 1.00 34.45 ?  302 TYR B OH    1 
ATOM   7984  N  N     . PRO B 1 303 ? 109.724 142.894 131.655 1.00 26.70 ?  303 PRO B N     1 
ATOM   7985  C  CA    . PRO B 1 303 ? 110.041 144.267 132.079 1.00 30.11 ?  303 PRO B CA    1 
ATOM   7986  C  C     . PRO B 1 303 ? 110.031 145.290 130.957 1.00 28.10 ?  303 PRO B C     1 
ATOM   7987  O  O     . PRO B 1 303 ? 109.677 146.451 131.201 1.00 33.19 ?  303 PRO B O     1 
ATOM   7988  C  CB    . PRO B 1 303 ? 111.441 144.122 132.690 1.00 29.93 ?  303 PRO B CB    1 
ATOM   7989  C  CG    . PRO B 1 303 ? 111.523 142.701 133.095 1.00 27.96 ?  303 PRO B CG    1 
ATOM   7990  C  CD    . PRO B 1 303 ? 110.770 141.940 132.052 1.00 23.22 ?  303 PRO B CD    1 
ATOM   7991  N  N     . HIS B 1 304 ? 110.415 144.908 129.738 1.00 29.44 ?  304 HIS B N     1 
ATOM   7992  C  CA    . HIS B 1 304 ? 110.493 145.896 128.668 1.00 27.98 ?  304 HIS B CA    1 
ATOM   7993  C  C     . HIS B 1 304 ? 109.114 146.377 128.242 1.00 34.11 ?  304 HIS B C     1 
ATOM   7994  O  O     . HIS B 1 304 ? 108.959 147.541 127.866 1.00 41.97 ?  304 HIS B O     1 
ATOM   7995  C  CB    . HIS B 1 304 ? 111.252 145.335 127.468 1.00 29.58 ?  304 HIS B CB    1 
ATOM   7996  C  CG    . HIS B 1 304 ? 111.627 146.377 126.461 1.00 33.21 ?  304 HIS B CG    1 
ATOM   7997  N  ND1   . HIS B 1 304 ? 112.231 147.565 126.812 1.00 33.55 ?  304 HIS B ND1   1 
ATOM   7998  C  CD2   . HIS B 1 304 ? 111.473 146.416 125.118 1.00 34.93 ?  304 HIS B CD2   1 
ATOM   7999  C  CE1   . HIS B 1 304 ? 112.440 148.288 125.727 1.00 32.26 ?  304 HIS B CE1   1 
ATOM   8000  N  NE2   . HIS B 1 304 ? 111.988 147.614 124.685 1.00 34.44 ?  304 HIS B NE2   1 
ATOM   8001  N  N     . THR B 1 305 ? 108.103 145.507 128.295 1.00 33.07 ?  305 THR B N     1 
ATOM   8002  C  CA    . THR B 1 305 ? 106.743 145.950 128.009 1.00 32.53 ?  305 THR B CA    1 
ATOM   8003  C  C     . THR B 1 305 ? 106.282 146.989 129.023 1.00 29.67 ?  305 THR B C     1 
ATOM   8004  O  O     . THR B 1 305 ? 105.660 147.993 128.657 1.00 35.87 ?  305 THR B O     1 
ATOM   8005  C  CB    . THR B 1 305 ? 105.793 144.755 127.993 1.00 31.15 ?  305 THR B CB    1 
ATOM   8006  O  OG1   . THR B 1 305 ? 105.653 144.236 129.320 1.00 29.56 ?  305 THR B OG1   1 
ATOM   8007  C  CG2   . THR B 1 305 ? 106.334 143.667 127.084 1.00 31.52 ?  305 THR B CG2   1 
ATOM   8008  N  N     . ILE B 1 306 ? 106.592 146.769 130.302 1.00 35.97 ?  306 ILE B N     1 
ATOM   8009  C  CA    . ILE B 1 306 ? 106.237 147.735 131.335 1.00 29.61 ?  306 ILE B CA    1 
ATOM   8010  C  C     . ILE B 1 306 ? 106.981 149.047 131.120 1.00 28.38 ?  306 ILE B C     1 
ATOM   8011  O  O     . ILE B 1 306 ? 106.406 150.134 131.260 1.00 35.85 ?  306 ILE B O     1 
ATOM   8012  C  CB    . ILE B 1 306 ? 106.514 147.143 132.728 1.00 27.13 ?  306 ILE B CB    1 
ATOM   8013  C  CG1   . ILE B 1 306 ? 105.449 146.105 133.078 1.00 27.32 ?  306 ILE B CG1   1 
ATOM   8014  C  CG2   . ILE B 1 306 ? 106.568 148.237 133.783 1.00 30.70 ?  306 ILE B CG2   1 
ATOM   8015  C  CD1   . ILE B 1 306 ? 105.721 145.363 134.351 1.00 29.91 ?  306 ILE B CD1   1 
ATOM   8016  N  N     . TYR B 1 307 ? 108.267 148.968 130.775 1.00 30.49 ?  307 TYR B N     1 
ATOM   8017  C  CA    . TYR B 1 307 ? 109.043 150.178 130.526 1.00 31.96 ?  307 TYR B CA    1 
ATOM   8018  C  C     . TYR B 1 307 ? 108.492 150.956 129.338 1.00 35.66 ?  307 TYR B C     1 
ATOM   8019  O  O     . TYR B 1 307 ? 108.439 152.190 129.363 1.00 39.51 ?  307 TYR B O     1 
ATOM   8020  C  CB    . TYR B 1 307 ? 110.512 149.823 130.301 1.00 26.23 ?  307 TYR B CB    1 
ATOM   8021  C  CG    . TYR B 1 307 ? 111.399 151.026 130.108 1.00 35.96 ?  307 TYR B CG    1 
ATOM   8022  C  CD1   . TYR B 1 307 ? 111.816 151.784 131.193 1.00 31.13 ?  307 TYR B CD1   1 
ATOM   8023  C  CD2   . TYR B 1 307 ? 111.815 151.410 128.842 1.00 37.14 ?  307 TYR B CD2   1 
ATOM   8024  C  CE1   . TYR B 1 307 ? 112.626 152.886 131.022 1.00 31.45 ?  307 TYR B CE1   1 
ATOM   8025  C  CE2   . TYR B 1 307 ? 112.624 152.511 128.661 1.00 36.70 ?  307 TYR B CE2   1 
ATOM   8026  C  CZ    . TYR B 1 307 ? 113.026 153.246 129.754 1.00 37.64 ?  307 TYR B CZ    1 
ATOM   8027  O  OH    . TYR B 1 307 ? 113.834 154.344 129.577 1.00 40.14 ?  307 TYR B OH    1 
ATOM   8028  N  N     . LYS B 1 308 ? 108.090 150.250 128.280 1.00 39.05 ?  308 LYS B N     1 
ATOM   8029  C  CA    . LYS B 1 308 ? 107.523 150.916 127.113 1.00 32.40 ?  308 LYS B CA    1 
ATOM   8030  C  C     . LYS B 1 308 ? 106.167 151.534 127.430 1.00 28.74 ?  308 LYS B C     1 
ATOM   8031  O  O     . LYS B 1 308 ? 105.844 152.621 126.938 1.00 37.26 ?  308 LYS B O     1 
ATOM   8032  C  CB    . LYS B 1 308 ? 107.400 149.925 125.958 1.00 32.55 ?  308 LYS B CB    1 
ATOM   8033  C  CG    . LYS B 1 308 ? 108.629 149.850 125.069 1.00 33.55 ?  308 LYS B CG    1 
ATOM   8034  C  CD    . LYS B 1 308 ? 108.729 148.507 124.356 1.00 37.52 ?  308 LYS B CD    1 
ATOM   8035  C  CE    . LYS B 1 308 ? 107.365 147.864 124.156 1.00 38.18 ?  308 LYS B CE    1 
ATOM   8036  N  NZ    . LYS B 1 308 ? 107.454 146.383 124.043 1.00 39.44 1  308 LYS B NZ    1 
ATOM   8037  N  N     . GLU B 1 309 ? 105.361 150.857 128.248 1.00 30.88 ?  309 GLU B N     1 
ATOM   8038  C  CA    . GLU B 1 309 ? 104.019 151.351 128.532 1.00 35.01 ?  309 GLU B CA    1 
ATOM   8039  C  C     . GLU B 1 309 ? 104.041 152.539 129.486 1.00 39.29 ?  309 GLU B C     1 
ATOM   8040  O  O     . GLU B 1 309 ? 103.280 153.496 129.309 1.00 42.53 ?  309 GLU B O     1 
ATOM   8041  C  CB    . GLU B 1 309 ? 103.160 150.222 129.100 1.00 31.66 ?  309 GLU B CB    1 
ATOM   8042  C  CG    . GLU B 1 309 ? 101.766 150.649 129.525 1.00 37.92 ?  309 GLU B CG    1 
ATOM   8043  C  CD    . GLU B 1 309 ? 100.899 151.078 128.359 1.00 44.26 ?  309 GLU B CD    1 
ATOM   8044  O  OE1   . GLU B 1 309 ? 101.263 150.789 127.200 1.00 44.90 ?  309 GLU B OE1   1 
ATOM   8045  O  OE2   . GLU B 1 309 ? 99.850  151.711 128.603 1.00 42.88 -1 309 GLU B OE2   1 
ATOM   8046  N  N     . TYR B 1 310 ? 104.901 152.501 130.503 1.00 38.41 ?  310 TYR B N     1 
ATOM   8047  C  CA    . TYR B 1 310 ? 104.868 153.493 131.568 1.00 32.71 ?  310 TYR B CA    1 
ATOM   8048  C  C     . TYR B 1 310 ? 106.082 154.409 131.601 1.00 31.48 ?  310 TYR B C     1 
ATOM   8049  O  O     . TYR B 1 310 ? 106.072 155.384 132.359 1.00 37.24 ?  310 TYR B O     1 
ATOM   8050  C  CB    . TYR B 1 310 ? 104.727 152.797 132.929 1.00 34.92 ?  310 TYR B CB    1 
ATOM   8051  C  CG    . TYR B 1 310 ? 103.490 151.938 133.040 1.00 35.19 ?  310 TYR B CG    1 
ATOM   8052  C  CD1   . TYR B 1 310 ? 102.260 152.499 133.357 1.00 31.87 ?  310 TYR B CD1   1 
ATOM   8053  C  CD2   . TYR B 1 310 ? 103.547 150.571 132.811 1.00 30.33 ?  310 TYR B CD2   1 
ATOM   8054  C  CE1   . TYR B 1 310 ? 101.127 151.721 133.452 1.00 34.98 ?  310 TYR B CE1   1 
ATOM   8055  C  CE2   . TYR B 1 310 ? 102.417 149.787 132.903 1.00 31.20 ?  310 TYR B CE2   1 
ATOM   8056  C  CZ    . TYR B 1 310 ? 101.211 150.365 133.225 1.00 35.71 ?  310 TYR B CZ    1 
ATOM   8057  O  OH    . TYR B 1 310 ? 100.083 149.586 133.319 1.00 36.16 ?  310 TYR B OH    1 
ATOM   8058  N  N     . GLY B 1 311 ? 107.117 154.131 130.815 1.00 27.99 ?  311 GLY B N     1 
ATOM   8059  C  CA    . GLY B 1 311 ? 108.323 154.927 130.869 1.00 30.48 ?  311 GLY B CA    1 
ATOM   8060  C  C     . GLY B 1 311 ? 109.174 154.704 132.096 1.00 31.62 ?  311 GLY B C     1 
ATOM   8061  O  O     . GLY B 1 311 ? 110.187 155.394 132.260 1.00 40.98 ?  311 GLY B O     1 
ATOM   8062  N  N     . GLN B 1 312 ? 108.798 153.769 132.963 1.00 31.69 ?  312 GLN B N     1 
ATOM   8063  C  CA    . GLN B 1 312 ? 109.546 153.454 134.167 1.00 30.03 ?  312 GLN B CA    1 
ATOM   8064  C  C     . GLN B 1 312 ? 109.810 151.959 134.211 1.00 31.15 ?  312 GLN B C     1 
ATOM   8065  O  O     . GLN B 1 312 ? 109.016 151.159 133.710 1.00 39.00 ?  312 GLN B O     1 
ATOM   8066  C  CB    . GLN B 1 312 ? 108.790 153.880 135.430 1.00 34.29 ?  312 GLN B CB    1 
ATOM   8067  C  CG    . GLN B 1 312 ? 108.384 155.339 135.454 1.00 37.13 ?  312 GLN B CG    1 
ATOM   8068  C  CD    . GLN B 1 312 ? 107.308 155.621 136.480 1.00 39.55 ?  312 GLN B CD    1 
ATOM   8069  O  OE1   . GLN B 1 312 ? 106.131 155.746 136.143 1.00 38.28 ?  312 GLN B OE1   1 
ATOM   8070  N  NE2   . GLN B 1 312 ? 107.706 155.722 137.741 1.00 37.71 ?  312 GLN B NE2   1 
ATOM   8071  N  N     . HIS B 1 313 ? 110.936 151.589 134.812 1.00 28.09 ?  313 HIS B N     1 
ATOM   8072  C  CA    . HIS B 1 313 ? 111.262 150.182 134.976 1.00 28.27 ?  313 HIS B CA    1 
ATOM   8073  C  C     . HIS B 1 313 ? 110.289 149.520 135.944 1.00 32.03 ?  313 HIS B C     1 
ATOM   8074  O  O     . HIS B 1 313 ? 109.747 150.158 136.849 1.00 34.17 ?  313 HIS B O     1 
ATOM   8075  C  CB    . HIS B 1 313 ? 112.695 150.021 135.477 1.00 26.18 ?  313 HIS B CB    1 
ATOM   8076  C  CG    . HIS B 1 313 ? 113.732 150.420 134.476 1.00 27.23 ?  313 HIS B CG    1 
ATOM   8077  N  ND1   . HIS B 1 313 ? 114.013 149.667 133.356 1.00 30.43 ?  313 HIS B ND1   1 
ATOM   8078  C  CD2   . HIS B 1 313 ? 114.559 151.491 134.425 1.00 28.25 ?  313 HIS B CD2   1 
ATOM   8079  C  CE1   . HIS B 1 313 ? 114.967 150.258 132.659 1.00 27.83 ?  313 HIS B CE1   1 
ATOM   8080  N  NE2   . HIS B 1 313 ? 115.316 151.366 133.287 1.00 32.42 ?  313 HIS B NE2   1 
ATOM   8081  N  N     . MET B 1 314 ? 110.068 148.222 135.738 1.00 34.99 ?  314 MET B N     1 
ATOM   8082  C  CA    . MET B 1 314 ? 109.128 147.490 136.581 1.00 29.03 ?  314 MET B CA    1 
ATOM   8083  C  C     . MET B 1 314 ? 109.598 147.461 138.030 1.00 34.23 ?  314 MET B C     1 
ATOM   8084  O  O     . MET B 1 314 ? 108.785 147.577 138.956 1.00 38.94 ?  314 MET B O     1 
ATOM   8085  C  CB    . MET B 1 314 ? 108.934 146.074 136.038 1.00 26.60 ?  314 MET B CB    1 
ATOM   8086  C  CG    . MET B 1 314 ? 108.356 145.085 137.031 1.00 27.15 ?  314 MET B CG    1 
ATOM   8087  S  SD    . MET B 1 314 ? 108.711 143.378 136.580 1.00 43.44 ?  314 MET B SD    1 
ATOM   8088  C  CE    . MET B 1 314 ? 110.353 143.180 137.267 1.00 34.29 ?  314 MET B CE    1 
ATOM   8089  N  N     . ASP B 1 315 ? 110.904 147.316 138.250 1.00 34.31 ?  315 ASP B N     1 
ATOM   8090  C  CA    . ASP B 1 315 ? 111.441 147.323 139.604 1.00 34.44 ?  315 ASP B CA    1 
ATOM   8091  C  C     . ASP B 1 315 ? 111.572 148.723 140.194 1.00 28.83 ?  315 ASP B C     1 
ATOM   8092  O  O     . ASP B 1 315 ? 111.864 148.850 141.387 1.00 38.87 ?  315 ASP B O     1 
ATOM   8093  C  CB    . ASP B 1 315 ? 112.779 146.558 139.639 1.00 29.64 ?  315 ASP B CB    1 
ATOM   8094  C  CG    . ASP B 1 315 ? 113.984 147.390 139.187 1.00 33.54 ?  315 ASP B CG    1 
ATOM   8095  O  OD1   . ASP B 1 315 ? 113.853 148.565 138.789 1.00 40.00 ?  315 ASP B OD1   1 
ATOM   8096  O  OD2   . ASP B 1 315 ? 115.104 146.840 139.242 1.00 35.00 -1 315 ASP B OD2   1 
ATOM   8097  N  N     . GLU B 1 316 ? 111.361 149.767 139.394 1.00 24.99 ?  316 GLU B N     1 
ATOM   8098  C  CA    . GLU B 1 316 ? 111.320 151.133 139.895 1.00 27.13 ?  316 GLU B CA    1 
ATOM   8099  C  C     . GLU B 1 316 ? 109.947 151.532 140.415 1.00 35.65 ?  316 GLU B C     1 
ATOM   8100  O  O     . GLU B 1 316 ? 109.808 152.626 140.972 1.00 35.99 ?  316 GLU B O     1 
ATOM   8101  C  CB    . GLU B 1 316 ? 111.746 152.109 138.797 1.00 31.43 ?  316 GLU B CB    1 
ATOM   8102  C  CG    . GLU B 1 316 ? 112.682 153.203 139.265 1.00 34.63 ?  316 GLU B CG    1 
ATOM   8103  C  CD    . GLU B 1 316 ? 114.059 152.684 139.600 1.00 39.24 ?  316 GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 1 316 ? 114.505 151.723 138.942 1.00 40.91 ?  316 GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 1 316 ? 114.697 153.238 140.519 1.00 38.33 -1 316 GLU B OE2   1 
ATOM   8106  N  N     . MET B 1 317 ? 108.940 150.681 140.251 1.00 38.87 ?  317 MET B N     1 
ATOM   8107  C  CA    . MET B 1 317 ? 107.570 150.994 140.619 1.00 34.88 ?  317 MET B CA    1 
ATOM   8108  C  C     . MET B 1 317 ? 107.110 150.111 141.772 1.00 38.69 ?  317 MET B C     1 
ATOM   8109  O  O     . MET B 1 317 ? 107.645 149.025 142.009 1.00 39.26 ?  317 MET B O     1 
ATOM   8110  C  CB    . MET B 1 317 ? 106.632 150.822 139.420 1.00 35.43 ?  317 MET B CB    1 
ATOM   8111  C  CG    . MET B 1 317 ? 107.121 151.515 138.160 1.00 37.07 ?  317 MET B CG    1 
ATOM   8112  S  SD    . MET B 1 317 ? 106.498 150.753 136.654 1.00 48.33 ?  317 MET B SD    1 
ATOM   8113  C  CE    . MET B 1 317 ? 105.024 151.729 136.384 1.00 39.01 ?  317 MET B CE    1 
ATOM   8114  N  N     . ASP B 1 318 ? 106.100 150.598 142.489 1.00 40.07 ?  318 ASP B N     1 
ATOM   8115  C  CA    . ASP B 1 318 ? 105.549 149.885 143.635 1.00 37.58 ?  318 ASP B CA    1 
ATOM   8116  C  C     . ASP B 1 318 ? 104.608 148.798 143.132 1.00 42.08 ?  318 ASP B C     1 
ATOM   8117  O  O     . ASP B 1 318 ? 103.533 149.095 142.603 1.00 44.38 ?  318 ASP B O     1 
ATOM   8118  C  CB    . ASP B 1 318 ? 104.824 150.855 144.564 1.00 39.27 ?  318 ASP B CB    1 
ATOM   8119  C  CG    . ASP B 1 318 ? 104.382 150.203 145.857 1.00 49.10 ?  318 ASP B CG    1 
ATOM   8120  O  OD1   . ASP B 1 318 ? 105.090 149.295 146.342 1.00 46.36 ?  318 ASP B OD1   1 
ATOM   8121  O  OD2   . ASP B 1 318 ? 103.325 150.600 146.390 1.00 50.01 -1 318 ASP B OD2   1 
ATOM   8122  N  N     . MET B 1 319 ? 105.010 147.537 143.300 1.00 40.62 ?  319 MET B N     1 
ATOM   8123  C  CA    . MET B 1 319 ? 104.197 146.432 142.803 1.00 35.55 ?  319 MET B CA    1 
ATOM   8124  C  C     . MET B 1 319 ? 102.862 146.333 143.529 1.00 36.85 ?  319 MET B C     1 
ATOM   8125  O  O     . MET B 1 319 ? 101.890 145.829 142.958 1.00 42.15 ?  319 MET B O     1 
ATOM   8126  C  CB    . MET B 1 319 ? 104.961 145.116 142.928 1.00 35.05 ?  319 MET B CB    1 
ATOM   8127  C  CG    . MET B 1 319 ? 104.430 144.013 142.029 1.00 37.88 ?  319 MET B CG    1 
ATOM   8128  S  SD    . MET B 1 319 ? 104.567 144.401 140.275 1.00 47.61 ?  319 MET B SD    1 
ATOM   8129  C  CE    . MET B 1 319 ? 106.345 144.443 140.083 1.00 41.96 ?  319 MET B CE    1 
ATOM   8130  N  N     . ASN B 1 320 ? 102.788 146.819 144.768 1.00 39.09 ?  320 ASN B N     1 
ATOM   8131  C  CA    . ASN B 1 320 ? 101.538 146.737 145.516 1.00 39.65 ?  320 ASN B CA    1 
ATOM   8132  C  C     . ASN B 1 320 ? 100.434 147.541 144.841 1.00 46.07 ?  320 ASN B C     1 
ATOM   8133  O  O     . ASN B 1 320 ? 99.277  147.104 144.795 1.00 46.18 ?  320 ASN B O     1 
ATOM   8134  C  CB    . ASN B 1 320 ? 101.757 147.213 146.952 1.00 40.73 ?  320 ASN B CB    1 
ATOM   8135  C  CG    . ASN B 1 320 ? 102.799 146.389 147.682 1.00 43.14 ?  320 ASN B CG    1 
ATOM   8136  O  OD1   . ASN B 1 320 ? 102.591 145.208 147.954 1.00 42.76 ?  320 ASN B OD1   1 
ATOM   8137  N  ND2   . ASN B 1 320 ? 103.927 147.011 148.001 1.00 43.71 ?  320 ASN B ND2   1 
ATOM   8138  N  N     . GLU B 1 321 ? 100.767 148.716 144.310 1.00 46.25 ?  321 GLU B N     1 
ATOM   8139  C  CA    . GLU B 1 321 ? 99.788  149.523 143.595 1.00 44.91 ?  321 GLU B CA    1 
ATOM   8140  C  C     . GLU B 1 321 ? 99.788  149.265 142.095 1.00 43.62 ?  321 GLU B C     1 
ATOM   8141  O  O     . GLU B 1 321 ? 98.759  149.462 141.440 1.00 45.23 ?  321 GLU B O     1 
ATOM   8142  C  CB    . GLU B 1 321 ? 100.039 151.012 143.850 1.00 43.47 ?  321 GLU B CB    1 
ATOM   8143  C  CG    . GLU B 1 321 ? 101.396 151.504 143.377 1.00 47.11 ?  321 GLU B CG    1 
ATOM   8144  C  CD    . GLU B 1 321 ? 101.340 152.901 142.791 1.00 51.86 ?  321 GLU B CD    1 
ATOM   8145  O  OE1   . GLU B 1 321 ? 100.222 153.411 142.570 1.00 49.66 ?  321 GLU B OE1   1 
ATOM   8146  O  OE2   . GLU B 1 321 ? 102.415 153.490 142.550 1.00 51.96 -1 321 GLU B OE2   1 
ATOM   8147  N  N     . MET B 1 322 ? 100.914 148.827 141.537 1.00 40.70 ?  322 MET B N     1 
ATOM   8148  C  CA    . MET B 1 322 ? 101.048 148.686 140.095 1.00 35.62 ?  322 MET B CA    1 
ATOM   8149  C  C     . MET B 1 322 ? 100.729 147.289 139.580 1.00 37.11 ?  322 MET B C     1 
ATOM   8150  O  O     . MET B 1 322 ? 100.659 147.109 138.363 1.00 47.12 ?  322 MET B O     1 
ATOM   8151  C  CB    . MET B 1 322 ? 102.468 149.061 139.655 1.00 35.35 ?  322 MET B CB    1 
ATOM   8152  C  CG    . MET B 1 322 ? 102.731 150.554 139.579 1.00 39.64 ?  322 MET B CG    1 
ATOM   8153  S  SD    . MET B 1 322 ? 101.275 151.498 139.105 1.00 50.65 ?  322 MET B SD    1 
ATOM   8154  C  CE    . MET B 1 322 ? 101.375 151.396 137.321 1.00 39.32 ?  322 MET B CE    1 
ATOM   8155  N  N     . TYR B 1 323 ? 100.538 146.301 140.457 1.00 37.53 ?  323 TYR B N     1 
ATOM   8156  C  CA    . TYR B 1 323 ? 100.349 144.931 139.987 1.00 33.11 ?  323 TYR B CA    1 
ATOM   8157  C  C     . TYR B 1 323 ? 99.032  144.781 139.237 1.00 40.15 ?  323 TYR B C     1 
ATOM   8158  O  O     . TYR B 1 323 ? 98.983  144.170 138.162 1.00 43.00 ?  323 TYR B O     1 
ATOM   8159  C  CB    . TYR B 1 323 ? 100.414 143.959 141.165 1.00 34.53 ?  323 TYR B CB    1 
ATOM   8160  C  CG    . TYR B 1 323 ? 100.122 142.522 140.793 1.00 37.76 ?  323 TYR B CG    1 
ATOM   8161  C  CD1   . TYR B 1 323 ? 101.115 141.706 140.268 1.00 31.61 ?  323 TYR B CD1   1 
ATOM   8162  C  CD2   . TYR B 1 323 ? 98.855  141.980 140.969 1.00 37.36 ?  323 TYR B CD2   1 
ATOM   8163  C  CE1   . TYR B 1 323 ? 100.852 140.395 139.929 1.00 28.11 ?  323 TYR B CE1   1 
ATOM   8164  C  CE2   . TYR B 1 323 ? 98.586  140.671 140.632 1.00 33.00 ?  323 TYR B CE2   1 
ATOM   8165  C  CZ    . TYR B 1 323 ? 99.588  139.885 140.113 1.00 32.57 ?  323 TYR B CZ    1 
ATOM   8166  O  OH    . TYR B 1 323 ? 99.323  138.580 139.776 1.00 38.21 ?  323 TYR B OH    1 
ATOM   8167  N  N     . ASP B 1 324 ? 97.950  145.330 139.791 1.00 43.32 ?  324 ASP B N     1 
ATOM   8168  C  CA    . ASP B 1 324 ? 96.656  145.245 139.123 1.00 38.89 ?  324 ASP B CA    1 
ATOM   8169  C  C     . ASP B 1 324 ? 96.668  146.005 137.805 1.00 41.91 ?  324 ASP B C     1 
ATOM   8170  O  O     . ASP B 1 324 ? 96.083  145.555 136.814 1.00 47.99 ?  324 ASP B O     1 
ATOM   8171  C  CB    . ASP B 1 324 ? 95.555  145.771 140.041 1.00 42.11 ?  324 ASP B CB    1 
ATOM   8172  C  CG    . ASP B 1 324 ? 95.343  144.892 141.256 1.00 45.33 ?  324 ASP B CG    1 
ATOM   8173  O  OD1   . ASP B 1 324 ? 95.458  143.657 141.123 1.00 45.34 ?  324 ASP B OD1   1 
ATOM   8174  O  OD2   . ASP B 1 324 ? 95.061  145.436 142.343 1.00 46.45 -1 324 ASP B OD2   1 
ATOM   8175  N  N     . LYS B 1 325 ? 97.328  147.165 137.775 1.00 42.05 ?  325 LYS B N     1 
ATOM   8176  C  CA    . LYS B 1 325 ? 97.433  147.926 136.535 1.00 41.84 ?  325 LYS B CA    1 
ATOM   8177  C  C     . LYS B 1 325 ? 98.237  147.168 135.488 1.00 41.15 ?  325 LYS B C     1 
ATOM   8178  O  O     . LYS B 1 325 ? 97.891  147.184 134.301 1.00 46.54 ?  325 LYS B O     1 
ATOM   8179  C  CB    . LYS B 1 325 ? 98.054  149.294 136.812 1.00 39.41 ?  325 LYS B CB    1 
ATOM   8180  C  CG    . LYS B 1 325 ? 97.293  150.109 137.842 1.00 38.15 ?  325 LYS B CG    1 
ATOM   8181  C  CD    . LYS B 1 325 ? 97.226  151.575 137.451 1.00 43.84 ?  325 LYS B CD    1 
ATOM   8182  C  CE    . LYS B 1 325 ? 97.867  152.460 138.505 1.00 44.36 ?  325 LYS B CE    1 
ATOM   8183  N  NZ    . LYS B 1 325 ? 97.099  152.448 139.781 1.00 46.04 1  325 LYS B NZ    1 
ATOM   8184  N  N     . PHE B 1 326 ? 99.318  146.506 135.904 1.00 39.33 ?  326 PHE B N     1 
ATOM   8185  C  CA    . PHE B 1 326 ? 100.097 145.694 134.976 1.00 36.16 ?  326 PHE B CA    1 
ATOM   8186  C  C     . PHE B 1 326 ? 99.265  144.546 134.424 1.00 36.41 ?  326 PHE B C     1 
ATOM   8187  O  O     . PHE B 1 326 ? 99.297  144.270 133.220 1.00 44.28 ?  326 PHE B O     1 
ATOM   8188  C  CB    . PHE B 1 326 ? 101.344 145.144 135.672 1.00 34.73 ?  326 PHE B CB    1 
ATOM   8189  C  CG    . PHE B 1 326 ? 102.354 146.190 136.045 1.00 32.72 ?  326 PHE B CG    1 
ATOM   8190  C  CD1   . PHE B 1 326 ? 102.303 147.459 135.500 1.00 34.49 ?  326 PHE B CD1   1 
ATOM   8191  C  CD2   . PHE B 1 326 ? 103.362 145.895 136.947 1.00 36.10 ?  326 PHE B CD2   1 
ATOM   8192  C  CE1   . PHE B 1 326 ? 103.236 148.413 135.850 1.00 33.27 ?  326 PHE B CE1   1 
ATOM   8193  C  CE2   . PHE B 1 326 ? 104.297 146.844 137.297 1.00 39.21 ?  326 PHE B CE2   1 
ATOM   8194  C  CZ    . PHE B 1 326 ? 104.233 148.105 136.746 1.00 39.45 ?  326 PHE B CZ    1 
ATOM   8195  N  N     . VAL B 1 327 ? 98.515  143.865 135.294 1.00 40.83 ?  327 VAL B N     1 
ATOM   8196  C  CA    . VAL B 1 327 ? 97.726  142.716 134.860 1.00 43.25 ?  327 VAL B CA    1 
ATOM   8197  C  C     . VAL B 1 327 ? 96.612  143.154 133.917 1.00 43.55 ?  327 VAL B C     1 
ATOM   8198  O  O     . VAL B 1 327 ? 96.356  142.507 132.894 1.00 45.72 ?  327 VAL B O     1 
ATOM   8199  C  CB    . VAL B 1 327 ? 97.176  141.956 136.081 1.00 37.68 ?  327 VAL B CB    1 
ATOM   8200  C  CG1   . VAL B 1 327 ? 96.183  140.895 135.646 1.00 40.71 ?  327 VAL B CG1   1 
ATOM   8201  C  CG2   . VAL B 1 327 ? 98.312  141.325 136.865 1.00 31.33 ?  327 VAL B CG2   1 
ATOM   8202  N  N     . ASP B 1 328 ? 95.941  144.260 134.232 1.00 44.04 ?  328 ASP B N     1 
ATOM   8203  C  CA    . ASP B 1 328 ? 94.839  144.741 133.411 1.00 45.35 ?  328 ASP B CA    1 
ATOM   8204  C  C     . ASP B 1 328 ? 95.300  145.465 132.154 1.00 45.87 ?  328 ASP B C     1 
ATOM   8205  O  O     . ASP B 1 328 ? 94.466  145.752 131.288 1.00 49.89 ?  328 ASP B O     1 
ATOM   8206  C  CB    . ASP B 1 328 ? 93.938  145.668 134.229 1.00 45.98 ?  328 ASP B CB    1 
ATOM   8207  C  CG    . ASP B 1 328 ? 93.096  144.916 135.238 1.00 52.99 ?  328 ASP B CG    1 
ATOM   8208  O  OD1   . ASP B 1 328 ? 92.986  143.679 135.117 1.00 52.45 ?  328 ASP B OD1   1 
ATOM   8209  O  OD2   . ASP B 1 328 ? 92.544  145.563 136.153 1.00 51.64 -1 328 ASP B OD2   1 
ATOM   8210  N  N     . ASN B 1 329 ? 96.585  145.769 132.032 1.00 40.44 ?  329 ASN B N     1 
ATOM   8211  C  CA    . ASN B 1 329 ? 97.083  146.449 130.844 1.00 39.47 ?  329 ASN B CA    1 
ATOM   8212  C  C     . ASN B 1 329 ? 97.309  145.437 129.728 1.00 47.37 ?  329 ASN B C     1 
ATOM   8213  O  O     . ASN B 1 329 ? 98.144  144.538 129.883 1.00 44.71 ?  329 ASN B O     1 
ATOM   8214  C  CB    . ASN B 1 329 ? 98.379  147.186 131.152 1.00 36.96 ?  329 ASN B CB    1 
ATOM   8215  C  CG    . ASN B 1 329 ? 98.644  148.324 130.189 1.00 42.80 ?  329 ASN B CG    1 
ATOM   8216  O  OD1   . ASN B 1 329 ? 99.025  148.104 129.042 1.00 47.29 ?  329 ASN B OD1   1 
ATOM   8217  N  ND2   . ASN B 1 329 ? 98.443  149.551 130.654 1.00 40.27 ?  329 ASN B ND2   1 
ATOM   8218  N  N     . PRO B 1 330 ? 96.593  145.535 128.605 1.00 49.24 ?  330 PRO B N     1 
ATOM   8219  C  CA    . PRO B 1 330 ? 96.835  144.596 127.499 1.00 43.76 ?  330 PRO B CA    1 
ATOM   8220  C  C     . PRO B 1 330 ? 98.195  144.760 126.849 1.00 41.32 ?  330 PRO B C     1 
ATOM   8221  O  O     . PRO B 1 330 ? 98.699  143.796 126.260 1.00 44.94 ?  330 PRO B O     1 
ATOM   8222  C  CB    . PRO B 1 330 ? 95.704  144.915 126.514 1.00 46.22 ?  330 PRO B CB    1 
ATOM   8223  C  CG    . PRO B 1 330 ? 95.340  146.327 126.813 1.00 43.83 ?  330 PRO B CG    1 
ATOM   8224  C  CD    . PRO B 1 330 ? 95.525  146.498 128.290 1.00 42.32 ?  330 PRO B CD    1 
ATOM   8225  N  N     . ARG B 1 331 ? 98.803  145.941 126.934 1.00 39.59 ?  331 ARG B N     1 
ATOM   8226  C  CA    . ARG B 1 331 ? 100.103 146.185 126.327 1.00 42.99 ?  331 ARG B CA    1 
ATOM   8227  C  C     . ARG B 1 331 ? 101.260 145.709 127.196 1.00 42.42 ?  331 ARG B C     1 
ATOM   8228  O  O     . ARG B 1 331 ? 102.412 145.771 126.755 1.00 41.85 ?  331 ARG B O     1 
ATOM   8229  C  CB    . ARG B 1 331 ? 100.260 147.675 126.014 1.00 40.58 ?  331 ARG B CB    1 
ATOM   8230  C  CG    . ARG B 1 331 ? 99.140  148.234 125.153 1.00 41.00 ?  331 ARG B CG    1 
ATOM   8231  C  CD    . ARG B 1 331 ? 99.187  149.756 125.092 1.00 41.46 ?  331 ARG B CD    1 
ATOM   8232  N  NE    . ARG B 1 331 ? 98.448  150.428 126.160 1.00 41.04 ?  331 ARG B NE    1 
ATOM   8233  C  CZ    . ARG B 1 331 ? 97.196  150.175 126.525 1.00 45.31 ?  331 ARG B CZ    1 
ATOM   8234  N  NH1   . ARG B 1 331 ? 96.433  149.321 125.862 1.00 45.36 1  331 ARG B NH1   1 
ATOM   8235  N  NH2   . ARG B 1 331 ? 96.684  150.822 127.568 1.00 42.03 ?  331 ARG B NH2   1 
ATOM   8236  N  N     . VAL B 1 332 ? 100.984 145.248 128.411 1.00 37.76 ?  332 VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? 101.990 144.655 129.283 1.00 34.85 ?  332 VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? 101.902 143.144 129.131 1.00 38.85 ?  332 VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? 100.834 142.553 129.331 1.00 40.26 ?  332 VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? 101.788 145.081 130.746 1.00 35.51 ?  332 VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? 102.595 144.191 131.674 1.00 37.32 ?  332 VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? 102.178 146.538 130.933 1.00 34.26 ?  332 VAL B CG2   1 
ATOM   8243  N  N     . LYS B 1 333 ? 103.016 142.517 128.767 1.00 34.79 ?  333 LYS B N     1 
ATOM   8244  C  CA    . LYS B 1 333 ? 103.053 141.078 128.547 1.00 31.33 ?  333 LYS B CA    1 
ATOM   8245  C  C     . LYS B 1 333 ? 103.367 140.350 129.847 1.00 34.52 ?  333 LYS B C     1 
ATOM   8246  O  O     . LYS B 1 333 ? 104.210 140.789 130.634 1.00 35.76 ?  333 LYS B O     1 
ATOM   8247  C  CB    . LYS B 1 333 ? 104.087 140.726 127.476 1.00 30.40 ?  333 LYS B CB    1 
ATOM   8248  C  CG    . LYS B 1 333 ? 103.926 139.334 126.895 1.00 37.96 ?  333 LYS B CG    1 
ATOM   8249  C  CD    . LYS B 1 333 ? 105.075 138.985 125.965 1.00 38.66 ?  333 LYS B CD    1 
ATOM   8250  C  CE    . LYS B 1 333 ? 104.976 137.550 125.482 1.00 38.80 ?  333 LYS B CE    1 
ATOM   8251  N  NZ    . LYS B 1 333 ? 106.084 137.200 124.553 1.00 40.45 1  333 LYS B NZ    1 
ATOM   8252  N  N     . LYS B 1 334 ? 102.678 139.231 130.067 1.00 37.10 ?  334 LYS B N     1 
ATOM   8253  C  CA    . LYS B 1 334 ? 102.820 138.472 131.300 1.00 32.47 ?  334 LYS B CA    1 
ATOM   8254  C  C     . LYS B 1 334 ? 102.477 137.015 131.032 1.00 35.58 ?  334 LYS B C     1 
ATOM   8255  O  O     . LYS B 1 334 ? 101.839 136.683 130.030 1.00 43.50 ?  334 LYS B O     1 
ATOM   8256  C  CB    . LYS B 1 334 ? 101.915 139.030 132.401 1.00 33.98 ?  334 LYS B CB    1 
ATOM   8257  C  CG    . LYS B 1 334 ? 100.452 139.090 132.001 1.00 35.77 ?  334 LYS B CG    1 
ATOM   8258  C  CD    . LYS B 1 334 ? 99.689  140.138 132.783 1.00 33.80 ?  334 LYS B CD    1 
ATOM   8259  C  CE    . LYS B 1 334 ? 99.572  141.424 131.992 1.00 37.85 ?  334 LYS B CE    1 
ATOM   8260  N  NZ    . LYS B 1 334 ? 98.598  141.317 130.872 1.00 37.62 1  334 LYS B NZ    1 
ATOM   8261  N  N     . GLU B 1 335 ? 102.915 136.140 131.938 1.00 38.13 ?  335 GLU B N     1 
ATOM   8262  C  CA    . GLU B 1 335 ? 102.458 134.758 131.964 1.00 43.58 ?  335 GLU B CA    1 
ATOM   8263  C  C     . GLU B 1 335 ? 102.010 134.394 133.371 1.00 41.91 ?  335 GLU B C     1 
ATOM   8264  O  O     . GLU B 1 335 ? 102.587 134.860 134.357 1.00 44.95 ?  335 GLU B O     1 
ATOM   8265  C  CB    . GLU B 1 335 ? 103.527 133.756 131.520 1.00 39.57 ?  335 GLU B CB    1 
ATOM   8266  C  CG    . GLU B 1 335 ? 104.955 134.159 131.763 1.00 40.04 ?  335 GLU B CG    1 
ATOM   8267  C  CD    . GLU B 1 335 ? 105.919 133.269 131.009 1.00 47.14 ?  335 GLU B CD    1 
ATOM   8268  O  OE1   . GLU B 1 335 ? 106.845 132.723 131.645 1.00 44.33 ?  335 GLU B OE1   1 
ATOM   8269  O  OE2   . GLU B 1 335 ? 105.750 133.110 129.781 1.00 46.65 -1 335 GLU B OE2   1 
ATOM   8270  N  N     . LYS B 1 336 ? 100.984 133.553 133.450 1.00 38.84 ?  336 LYS B N     1 
ATOM   8271  C  CA    . LYS B 1 336 ? 100.484 133.090 134.735 1.00 30.35 ?  336 LYS B CA    1 
ATOM   8272  C  C     . LYS B 1 336 ? 101.514 132.204 135.423 1.00 37.36 ?  336 LYS B C     1 
ATOM   8273  O  O     . LYS B 1 336 ? 102.192 131.396 134.782 1.00 40.56 ?  336 LYS B O     1 
ATOM   8274  C  CB    . LYS B 1 336 ? 99.181  132.316 134.545 1.00 40.33 ?  336 LYS B CB    1 
ATOM   8275  C  CG    . LYS B 1 336 ? 98.360  132.152 135.808 1.00 43.04 ?  336 LYS B CG    1 
ATOM   8276  C  CD    . LYS B 1 336 ? 97.443  133.342 136.005 1.00 44.70 ?  336 LYS B CD    1 
ATOM   8277  C  CE    . LYS B 1 336 ? 96.087  133.096 135.368 1.00 41.52 ?  336 LYS B CE    1 
ATOM   8278  N  NZ    . LYS B 1 336 ? 95.191  132.309 136.257 1.00 41.81 1  336 LYS B NZ    1 
ATOM   8279  N  N     . ILE B 1 337 ? 101.636 132.365 136.740 1.00 38.68 ?  337 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 337 ? 102.433 131.481 137.578 1.00 36.88 ?  337 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 337 ? 101.613 131.133 138.811 1.00 39.62 ?  337 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 337 ? 100.607 131.771 139.120 1.00 45.76 ?  337 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 337 ? 103.784 132.100 137.990 1.00 35.97 ?  337 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 337 ? 103.562 133.429 138.714 1.00 37.24 ?  337 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 337 ? 104.694 132.270 136.785 1.00 37.46 ?  337 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 337 ? 104.561 133.703 139.810 1.00 33.60 ?  337 ILE B CD1   1 
ATOM   8287  N  N     . ASN B 1 338 ? 102.058 130.098 139.518 1.00 38.80 ?  338 ASN B N     1 
ATOM   8288  C  CA    . ASN B 1 338 ? 101.485 129.771 140.814 1.00 34.32 ?  338 ASN B CA    1 
ATOM   8289  C  C     . ASN B 1 338 ? 102.426 130.284 141.890 1.00 35.85 ?  338 ASN B C     1 
ATOM   8290  O  O     . ASN B 1 338 ? 103.524 129.732 142.051 1.00 42.95 ?  338 ASN B O     1 
ATOM   8291  C  CB    . ASN B 1 338 ? 101.277 128.266 140.955 1.00 35.42 ?  338 ASN B CB    1 
ATOM   8292  C  CG    . ASN B 1 338 ? 100.269 127.917 142.029 1.00 39.78 ?  338 ASN B CG    1 
ATOM   8293  O  OD1   . ASN B 1 338 ? 99.802  128.786 142.765 1.00 41.66 ?  338 ASN B OD1   1 
ATOM   8294  N  ND2   . ASN B 1 338 ? 99.923  126.639 142.124 1.00 39.95 ?  338 ASN B ND2   1 
ATOM   8295  N  N     . PRO B 1 339 ? 102.063 131.335 142.630 1.00 36.61 ?  339 PRO B N     1 
ATOM   8296  C  CA    . PRO B 1 339 ? 102.985 131.864 143.647 1.00 34.86 ?  339 PRO B CA    1 
ATOM   8297  C  C     . PRO B 1 339 ? 103.326 130.865 144.736 1.00 32.01 ?  339 PRO B C     1 
ATOM   8298  O  O     . PRO B 1 339 ? 104.455 130.880 145.242 1.00 36.23 ?  339 PRO B O     1 
ATOM   8299  C  CB    . PRO B 1 339 ? 102.231 133.078 144.204 1.00 33.12 ?  339 PRO B CB    1 
ATOM   8300  C  CG    . PRO B 1 339 ? 100.806 132.803 143.909 1.00 36.79 ?  339 PRO B CG    1 
ATOM   8301  C  CD    . PRO B 1 339 ? 100.788 132.068 142.607 1.00 36.01 ?  339 PRO B CD    1 
ATOM   8302  N  N     . ARG B 1 340 ? 102.388 129.997 145.118 1.00 33.55 ?  340 ARG B N     1 
ATOM   8303  C  CA    . ARG B 1 340 ? 102.699 128.974 146.108 1.00 32.24 ?  340 ARG B CA    1 
ATOM   8304  C  C     . ARG B 1 340 ? 103.678 127.952 145.550 1.00 33.47 ?  340 ARG B C     1 
ATOM   8305  O  O     . ARG B 1 340 ? 104.581 127.497 146.261 1.00 39.77 ?  340 ARG B O     1 
ATOM   8306  C  CB    . ARG B 1 340 ? 101.419 128.292 146.585 1.00 31.38 ?  340 ARG B CB    1 
ATOM   8307  C  CG    . ARG B 1 340 ? 100.586 129.151 147.509 1.00 29.58 ?  340 ARG B CG    1 
ATOM   8308  C  CD    . ARG B 1 340 ? 99.669  128.315 148.379 1.00 31.39 ?  340 ARG B CD    1 
ATOM   8309  N  NE    . ARG B 1 340 ? 98.739  129.151 149.127 1.00 33.49 ?  340 ARG B NE    1 
ATOM   8310  C  CZ    . ARG B 1 340 ? 97.829  128.690 149.972 1.00 35.94 ?  340 ARG B CZ    1 
ATOM   8311  N  NH1   . ARG B 1 340 ? 97.697  127.395 150.207 1.00 35.30 1  340 ARG B NH1   1 
ATOM   8312  N  NH2   . ARG B 1 340 ? 97.028  129.549 150.595 1.00 36.79 ?  340 ARG B NH2   1 
ATOM   8313  N  N     . LYS B 1 341 ? 103.516 127.579 144.280 1.00 34.62 ?  341 LYS B N     1 
ATOM   8314  C  CA    . LYS B 1 341 ? 104.480 126.682 143.654 1.00 33.59 ?  341 LYS B CA    1 
ATOM   8315  C  C     . LYS B 1 341 ? 105.849 127.338 143.547 1.00 30.60 ?  341 LYS B C     1 
ATOM   8316  O  O     . LYS B 1 341 ? 106.875 126.673 143.720 1.00 32.98 ?  341 LYS B O     1 
ATOM   8317  C  CB    . LYS B 1 341 ? 103.980 126.247 142.277 1.00 37.60 ?  341 LYS B CB    1 
ATOM   8318  C  CG    . LYS B 1 341 ? 102.905 125.169 142.312 1.00 38.96 ?  341 LYS B CG    1 
ATOM   8319  C  CD    . LYS B 1 341 ? 103.019 124.297 143.554 1.00 40.97 ?  341 LYS B CD    1 
ATOM   8320  C  CE    . LYS B 1 341 ? 102.031 123.145 143.515 1.00 41.70 ?  341 LYS B CE    1 
ATOM   8321  N  NZ    . LYS B 1 341 ? 102.699 121.842 143.782 1.00 40.34 1  341 LYS B NZ    1 
ATOM   8322  N  N     . LEU B 1 342 ? 105.888 128.642 143.268 1.00 32.33 ?  342 LEU B N     1 
ATOM   8323  C  CA    . LEU B 1 342 ? 107.163 129.351 143.241 1.00 29.16 ?  342 LEU B CA    1 
ATOM   8324  C  C     . LEU B 1 342 ? 107.805 129.387 144.623 1.00 29.99 ?  342 LEU B C     1 
ATOM   8325  O  O     . LEU B 1 342 ? 109.025 129.237 144.749 1.00 38.62 ?  342 LEU B O     1 
ATOM   8326  C  CB    . LEU B 1 342 ? 106.967 130.766 142.697 1.00 28.81 ?  342 LEU B CB    1 
ATOM   8327  C  CG    . LEU B 1 342 ? 108.226 131.470 142.188 1.00 29.11 ?  342 LEU B CG    1 
ATOM   8328  C  CD1   . LEU B 1 342 ? 109.071 130.521 141.356 1.00 28.49 ?  342 LEU B CD1   1 
ATOM   8329  C  CD2   . LEU B 1 342 ? 107.865 132.706 141.386 1.00 28.15 ?  342 LEU B CD2   1 
ATOM   8330  N  N     . LEU B 1 343 ? 107.002 129.582 145.672 1.00 27.61 ?  343 LEU B N     1 
ATOM   8331  C  CA    . LEU B 1 343 ? 107.532 129.544 147.033 1.00 29.13 ?  343 LEU B CA    1 
ATOM   8332  C  C     . LEU B 1 343 ? 108.080 128.166 147.375 1.00 28.50 ?  343 LEU B C     1 
ATOM   8333  O  O     . LEU B 1 343 ? 109.141 128.045 148.002 1.00 32.52 ?  343 LEU B O     1 
ATOM   8334  C  CB    . LEU B 1 343 ? 106.444 129.945 148.027 1.00 31.73 ?  343 LEU B CB    1 
ATOM   8335  C  CG    . LEU B 1 343 ? 106.386 131.411 148.450 1.00 32.63 ?  343 LEU B CG    1 
ATOM   8336  C  CD1   . LEU B 1 343 ? 105.228 131.634 149.403 1.00 27.04 ?  343 LEU B CD1   1 
ATOM   8337  C  CD2   . LEU B 1 343 ? 107.697 131.837 149.087 1.00 33.94 ?  343 LEU B CD2   1 
ATOM   8338  N  N     . GLU B 1 344 ? 107.361 127.112 146.987 1.00 34.65 ?  344 GLU B N     1 
ATOM   8339  C  CA    . GLU B 1 344 ? 107.841 125.758 147.238 1.00 32.82 ?  344 GLU B CA    1 
ATOM   8340  C  C     . GLU B 1 344 ? 109.118 125.475 146.456 1.00 29.44 ?  344 GLU B C     1 
ATOM   8341  O  O     . GLU B 1 344 ? 110.015 124.787 146.951 1.00 34.99 ?  344 GLU B O     1 
ATOM   8342  C  CB    . GLU B 1 344 ? 106.755 124.743 146.891 1.00 35.28 ?  344 GLU B CB    1 
ATOM   8343  C  CG    . GLU B 1 344 ? 105.501 124.870 147.739 1.00 36.66 ?  344 GLU B CG    1 
ATOM   8344  C  CD    . GLU B 1 344 ? 104.381 123.973 147.257 1.00 45.78 ?  344 GLU B CD    1 
ATOM   8345  O  OE1   . GLU B 1 344 ? 104.678 122.908 146.677 1.00 44.97 ?  344 GLU B OE1   1 
ATOM   8346  O  OE2   . GLU B 1 344 ? 103.202 124.334 147.458 1.00 43.83 -1 344 GLU B OE2   1 
ATOM   8347  N  N     . LYS B 1 345 ? 109.215 125.999 145.233 1.00 29.73 ?  345 LYS B N     1 
ATOM   8348  C  CA    . LYS B 1 345 ? 110.444 125.865 144.460 1.00 28.05 ?  345 LYS B CA    1 
ATOM   8349  C  C     . LYS B 1 345 ? 111.598 126.595 145.132 1.00 33.02 ?  345 LYS B C     1 
ATOM   8350  O  O     . LYS B 1 345 ? 112.728 126.095 145.154 1.00 36.04 ?  345 LYS B O     1 
ATOM   8351  C  CB    . LYS B 1 345 ? 110.224 126.388 143.041 1.00 29.85 ?  345 LYS B CB    1 
ATOM   8352  C  CG    . LYS B 1 345 ? 111.426 126.246 142.132 1.00 30.65 ?  345 LYS B CG    1 
ATOM   8353  C  CD    . LYS B 1 345 ? 111.126 126.770 140.741 1.00 29.51 ?  345 LYS B CD    1 
ATOM   8354  C  CE    . LYS B 1 345 ? 112.358 126.718 139.861 1.00 34.19 ?  345 LYS B CE    1 
ATOM   8355  N  NZ    . LYS B 1 345 ? 112.106 127.305 138.520 1.00 34.65 1  345 LYS B NZ    1 
ATOM   8356  N  N     . LEU B 1 346 ? 111.330 127.779 145.686 1.00 33.81 ?  346 LEU B N     1 
ATOM   8357  C  CA    . LEU B 1 346 ? 112.353 128.504 146.433 1.00 27.40 ?  346 LEU B CA    1 
ATOM   8358  C  C     . LEU B 1 346 ? 112.834 127.690 147.625 1.00 25.79 ?  346 LEU B C     1 
ATOM   8359  O  O     . LEU B 1 346 ? 114.039 127.572 147.865 1.00 28.42 ?  346 LEU B O     1 
ATOM   8360  C  CB    . LEU B 1 346 ? 111.808 129.853 146.902 1.00 27.66 ?  346 LEU B CB    1 
ATOM   8361  C  CG    . LEU B 1 346 ? 111.542 130.946 145.870 1.00 26.18 ?  346 LEU B CG    1 
ATOM   8362  C  CD1   . LEU B 1 346 ? 110.908 132.151 146.539 1.00 30.49 ?  346 LEU B CD1   1 
ATOM   8363  C  CD2   . LEU B 1 346 ? 112.822 131.337 145.172 1.00 27.88 ?  346 LEU B CD2   1 
ATOM   8364  N  N     . ALA B 1 347 ? 111.897 127.116 148.382 1.00 26.69 ?  347 ALA B N     1 
ATOM   8365  C  CA    . ALA B 1 347 ? 112.274 126.327 149.551 1.00 20.04 ?  347 ALA B CA    1 
ATOM   8366  C  C     . ALA B 1 347 ? 113.054 125.080 149.152 1.00 27.48 ?  347 ALA B C     1 
ATOM   8367  O  O     . ALA B 1 347 ? 114.026 124.707 149.819 1.00 35.93 ?  347 ALA B O     1 
ATOM   8368  C  CB    . ALA B 1 347 ? 111.032 125.950 150.353 1.00 19.98 ?  347 ALA B CB    1 
ATOM   8369  N  N     . MET B 1 348 ? 112.639 124.418 148.070 1.00 33.95 ?  348 MET B N     1 
ATOM   8370  C  CA    . MET B 1 348 ? 113.363 123.247 147.588 1.00 31.21 ?  348 MET B CA    1 
ATOM   8371  C  C     . MET B 1 348 ? 114.778 123.612 147.163 1.00 31.70 ?  348 MET B C     1 
ATOM   8372  O  O     . MET B 1 348 ? 115.735 122.890 147.470 1.00 40.09 ?  348 MET B O     1 
ATOM   8373  C  CB    . MET B 1 348 ? 112.594 122.606 146.431 1.00 33.42 ?  348 MET B CB    1 
ATOM   8374  C  CG    . MET B 1 348 ? 113.347 121.514 145.691 1.00 40.99 ?  348 MET B CG    1 
ATOM   8375  S  SD    . MET B 1 348 ? 114.114 122.088 144.162 1.00 60.89 ?  348 MET B SD    1 
ATOM   8376  C  CE    . MET B 1 348 ? 112.780 123.038 143.439 1.00 38.33 ?  348 MET B CE    1 
ATOM   8377  N  N     . LEU B 1 349 ? 114.931 124.737 146.462 1.00 26.74 ?  349 LEU B N     1 
ATOM   8378  C  CA    . LEU B 1 349 ? 116.255 125.171 146.037 1.00 27.33 ?  349 LEU B CA    1 
ATOM   8379  C  C     . LEU B 1 349 ? 117.132 125.522 147.230 1.00 28.95 ?  349 LEU B C     1 
ATOM   8380  O  O     . LEU B 1 349 ? 118.333 125.230 147.232 1.00 32.49 ?  349 LEU B O     1 
ATOM   8381  C  CB    . LEU B 1 349 ? 116.129 126.363 145.094 1.00 27.93 ?  349 LEU B CB    1 
ATOM   8382  C  CG    . LEU B 1 349 ? 116.096 126.013 143.609 1.00 33.81 ?  349 LEU B CG    1 
ATOM   8383  C  CD1   . LEU B 1 349 ? 115.298 127.052 142.861 1.00 34.75 ?  349 LEU B CD1   1 
ATOM   8384  C  CD2   . LEU B 1 349 ? 117.504 125.912 143.054 1.00 33.96 ?  349 LEU B CD2   1 
ATOM   8385  N  N     . ARG B 1 350 ? 116.558 126.166 148.249 1.00 26.35 ?  350 ARG B N     1 
ATOM   8386  C  CA    . ARG B 1 350 ? 117.337 126.493 149.440 1.00 22.58 ?  350 ARG B CA    1 
ATOM   8387  C  C     . ARG B 1 350 ? 117.729 125.243 150.214 1.00 30.68 ?  350 ARG B C     1 
ATOM   8388  O  O     . ARG B 1 350 ? 118.830 125.184 150.774 1.00 41.06 ?  350 ARG B O     1 
ATOM   8389  C  CB    . ARG B 1 350 ? 116.561 127.456 150.336 1.00 25.27 ?  350 ARG B CB    1 
ATOM   8390  C  CG    . ARG B 1 350 ? 116.169 128.755 149.658 1.00 24.47 ?  350 ARG B CG    1 
ATOM   8391  C  CD    . ARG B 1 350 ? 115.778 129.810 150.667 1.00 26.29 ?  350 ARG B CD    1 
ATOM   8392  N  NE    . ARG B 1 350 ? 116.873 130.738 150.919 1.00 33.09 ?  350 ARG B NE    1 
ATOM   8393  C  CZ    . ARG B 1 350 ? 117.252 131.134 152.124 1.00 28.82 ?  350 ARG B CZ    1 
ATOM   8394  N  NH1   . ARG B 1 350 ? 116.663 130.681 153.217 1.00 26.87 1  350 ARG B NH1   1 
ATOM   8395  N  NH2   . ARG B 1 350 ? 118.252 132.003 152.235 1.00 32.13 ?  350 ARG B NH2   1 
ATOM   8396  N  N     . SER B 1 351 ? 116.849 124.244 150.270 1.00 33.84 ?  351 SER B N     1 
ATOM   8397  C  CA    . SER B 1 351 ? 117.216 122.977 150.892 1.00 33.14 ?  351 SER B CA    1 
ATOM   8398  C  C     . SER B 1 351 ? 118.345 122.298 150.128 1.00 34.19 ?  351 SER B C     1 
ATOM   8399  O  O     . SER B 1 351 ? 119.283 121.766 150.733 1.00 42.75 ?  351 SER B O     1 
ATOM   8400  C  CB    . SER B 1 351 ? 115.999 122.056 150.970 1.00 34.41 ?  351 SER B CB    1 
ATOM   8401  O  OG    . SER B 1 351 ? 115.018 122.575 151.849 1.00 44.10 ?  351 SER B OG    1 
ATOM   8402  N  N     . GLU B 1 352 ? 118.273 122.307 148.796 1.00 34.56 ?  352 GLU B N     1 
ATOM   8403  C  CA    . GLU B 1 352 ? 119.259 121.584 148.000 1.00 35.03 ?  352 GLU B CA    1 
ATOM   8404  C  C     . GLU B 1 352 ? 120.614 122.283 147.996 1.00 35.91 ?  352 GLU B C     1 
ATOM   8405  O  O     . GLU B 1 352 ? 121.652 121.632 148.156 1.00 44.61 ?  352 GLU B O     1 
ATOM   8406  C  CB    . GLU B 1 352 ? 118.744 121.402 146.575 1.00 36.46 ?  352 GLU B CB    1 
ATOM   8407  C  CG    . GLU B 1 352 ? 117.653 120.355 146.448 1.00 39.07 ?  352 GLU B CG    1 
ATOM   8408  C  CD    . GLU B 1 352 ? 116.936 120.421 145.116 1.00 47.81 ?  352 GLU B CD    1 
ATOM   8409  O  OE1   . GLU B 1 352 ? 117.223 121.351 144.334 1.00 44.81 ?  352 GLU B OE1   1 
ATOM   8410  O  OE2   . GLU B 1 352 ? 116.091 119.542 144.850 1.00 45.72 -1 352 GLU B OE2   1 
ATOM   8411  N  N     . SER B 1 353 ? 120.631 123.606 147.817 1.00 36.06 ?  353 SER B N     1 
ATOM   8412  C  CA    . SER B 1 353 ? 121.876 124.331 147.601 1.00 36.19 ?  353 SER B CA    1 
ATOM   8413  C  C     . SER B 1 353 ? 122.064 125.560 148.477 1.00 30.27 ?  353 SER B C     1 
ATOM   8414  O  O     . SER B 1 353 ? 123.125 126.187 148.394 1.00 32.66 ?  353 SER B O     1 
ATOM   8415  C  CB    . SER B 1 353 ? 121.991 124.765 146.132 1.00 37.72 ?  353 SER B CB    1 
ATOM   8416  O  OG    . SER B 1 353 ? 121.047 125.776 145.826 1.00 35.84 ?  353 SER B OG    1 
ATOM   8417  N  N     . GLY B 1 354 ? 121.086 125.931 149.301 1.00 25.89 ?  354 GLY B N     1 
ATOM   8418  C  CA    . GLY B 1 354 ? 121.185 127.129 150.106 1.00 27.51 ?  354 GLY B CA    1 
ATOM   8419  C  C     . GLY B 1 354 ? 120.801 128.407 149.400 1.00 23.43 ?  354 GLY B C     1 
ATOM   8420  O  O     . GLY B 1 354 ? 120.794 129.469 150.036 1.00 27.53 ?  354 GLY B O     1 
ATOM   8421  N  N     . TYR B 1 355 ? 120.478 128.346 148.117 1.00 26.70 ?  355 TYR B N     1 
ATOM   8422  C  CA    . TYR B 1 355 ? 120.110 129.488 147.302 1.00 16.72 ?  355 TYR B CA    1 
ATOM   8423  C  C     . TYR B 1 355 ? 118.633 129.424 146.938 1.00 24.56 ?  355 TYR B C     1 
ATOM   8424  O  O     . TYR B 1 355 ? 118.037 128.343 146.917 1.00 29.05 ?  355 TYR B O     1 
ATOM   8425  C  CB    . TYR B 1 355 ? 120.955 129.526 146.021 1.00 19.98 ?  355 TYR B CB    1 
ATOM   8426  C  CG    . TYR B 1 355 ? 122.401 129.876 146.258 1.00 28.27 ?  355 TYR B CG    1 
ATOM   8427  C  CD1   . TYR B 1 355 ? 122.754 131.033 146.935 1.00 25.74 ?  355 TYR B CD1   1 
ATOM   8428  C  CD2   . TYR B 1 355 ? 123.417 129.047 145.806 1.00 30.44 ?  355 TYR B CD2   1 
ATOM   8429  C  CE1   . TYR B 1 355 ? 124.075 131.354 147.154 1.00 27.80 ?  355 TYR B CE1   1 
ATOM   8430  C  CE2   . TYR B 1 355 ? 124.742 129.360 146.021 1.00 29.65 ?  355 TYR B CE2   1 
ATOM   8431  C  CZ    . TYR B 1 355 ? 125.065 130.517 146.695 1.00 30.27 ?  355 TYR B CZ    1 
ATOM   8432  O  OH    . TYR B 1 355 ? 126.383 130.838 146.914 1.00 34.28 ?  355 TYR B OH    1 
ATOM   8433  N  N     . PRO B 1 356 ? 118.004 130.564 146.637 1.00 27.49 ?  356 PRO B N     1 
ATOM   8434  C  CA    . PRO B 1 356 ? 118.534 131.933 146.606 1.00 15.66 ?  356 PRO B CA    1 
ATOM   8435  C  C     . PRO B 1 356 ? 118.484 132.646 147.947 1.00 16.09 ?  356 PRO B C     1 
ATOM   8436  O  O     . PRO B 1 356 ? 117.855 132.183 148.891 1.00 24.60 ?  356 PRO B O     1 
ATOM   8437  C  CB    . PRO B 1 356 ? 117.611 132.615 145.596 1.00 18.31 ?  356 PRO B CB    1 
ATOM   8438  C  CG    . PRO B 1 356 ? 116.292 131.963 145.856 1.00 22.80 ?  356 PRO B CG    1 
ATOM   8439  C  CD    . PRO B 1 356 ? 116.617 130.518 146.139 1.00 13.71 ?  356 PRO B CD    1 
ATOM   8440  N  N     . TYR B 1 357 ? 119.155 133.788 148.055 1.00 21.55 ?  357 TYR B N     1 
ATOM   8441  C  CA    . TYR B 1 357 ? 118.868 134.707 149.143 1.00 13.99 ?  357 TYR B CA    1 
ATOM   8442  C  C     . TYR B 1 357 ? 117.465 135.267 148.957 1.00 17.78 ?  357 TYR B C     1 
ATOM   8443  O  O     . TYR B 1 357 ? 117.021 135.503 147.832 1.00 26.50 ?  357 TYR B O     1 
ATOM   8444  C  CB    . TYR B 1 357 ? 119.882 135.853 149.184 1.00 12.95 ?  357 TYR B CB    1 
ATOM   8445  C  CG    . TYR B 1 357 ? 121.331 135.464 148.986 1.00 16.72 ?  357 TYR B CG    1 
ATOM   8446  C  CD1   . TYR B 1 357 ? 121.819 134.248 149.438 1.00 17.56 ?  357 TYR B CD1   1 
ATOM   8447  C  CD2   . TYR B 1 357 ? 122.217 136.325 148.354 1.00 19.44 ?  357 TYR B CD2   1 
ATOM   8448  C  CE1   . TYR B 1 357 ? 123.137 133.898 149.266 1.00 19.94 ?  357 TYR B CE1   1 
ATOM   8449  C  CE2   . TYR B 1 357 ? 123.540 135.983 148.176 1.00 15.34 ?  357 TYR B CE2   1 
ATOM   8450  C  CZ    . TYR B 1 357 ? 123.994 134.768 148.634 1.00 24.11 ?  357 TYR B CZ    1 
ATOM   8451  O  OH    . TYR B 1 357 ? 125.313 134.418 148.462 1.00 31.95 ?  357 TYR B OH    1 
ATOM   8452  N  N     . ILE B 1 358 ? 116.760 135.472 150.061 1.00 25.86 ?  358 ILE B N     1 
ATOM   8453  C  CA    . ILE B 1 358 ? 115.419 136.038 150.035 1.00 18.22 ?  358 ILE B CA    1 
ATOM   8454  C  C     . ILE B 1 358 ? 115.496 137.446 150.602 1.00 19.32 ?  358 ILE B C     1 
ATOM   8455  O  O     . ILE B 1 358 ? 115.906 137.636 151.752 1.00 24.72 ?  358 ILE B O     1 
ATOM   8456  C  CB    . ILE B 1 358 ? 114.417 135.182 150.825 1.00 18.88 ?  358 ILE B CB    1 
ATOM   8457  C  CG1   . ILE B 1 358 ? 114.415 133.740 150.315 1.00 15.46 ?  358 ILE B CG1   1 
ATOM   8458  C  CG2   . ILE B 1 358 ? 113.029 135.790 150.742 1.00 17.41 ?  358 ILE B CG2   1 
ATOM   8459  C  CD1   . ILE B 1 358 ? 113.980 133.598 148.877 1.00 21.51 ?  358 ILE B CD1   1 
ATOM   8460  N  N     . MET B 1 359 ? 115.107 138.430 149.799 1.00 13.23 ?  359 MET B N     1 
ATOM   8461  C  CA    . MET B 1 359 ? 115.007 139.814 150.238 1.00 2.07  ?  359 MET B CA    1 
ATOM   8462  C  C     . MET B 1 359 ? 113.544 140.226 150.182 1.00 7.01  ?  359 MET B C     1 
ATOM   8463  O  O     . MET B 1 359 ? 112.947 140.261 149.102 1.00 20.50 ?  359 MET B O     1 
ATOM   8464  C  CB    . MET B 1 359 ? 115.869 140.732 149.373 1.00 10.80 ?  359 MET B CB    1 
ATOM   8465  C  CG    . MET B 1 359 ? 115.836 142.191 149.794 1.00 9.94  ?  359 MET B CG    1 
ATOM   8466  S  SD    . MET B 1 359 ? 115.897 143.333 148.408 1.00 38.89 ?  359 MET B SD    1 
ATOM   8467  C  CE    . MET B 1 359 ? 114.994 144.724 149.068 1.00 16.35 ?  359 MET B CE    1 
ATOM   8468  N  N     . PHE B 1 360 ? 112.968 140.519 151.343 1.00 13.11 ?  360 PHE B N     1 
ATOM   8469  C  CA    . PHE B 1 360 ? 111.574 140.947 151.423 1.00 5.13  ?  360 PHE B CA    1 
ATOM   8470  C  C     . PHE B 1 360 ? 111.534 142.442 151.142 1.00 13.75 ?  360 PHE B C     1 
ATOM   8471  O  O     . PHE B 1 360 ? 111.861 143.258 152.005 1.00 21.20 ?  360 PHE B O     1 
ATOM   8472  C  CB    . PHE B 1 360 ? 110.987 140.599 152.784 1.00 11.94 ?  360 PHE B CB    1 
ATOM   8473  C  CG    . PHE B 1 360 ? 110.929 139.123 153.052 1.00 16.25 ?  360 PHE B CG    1 
ATOM   8474  C  CD1   . PHE B 1 360 ? 110.133 138.294 152.277 1.00 19.55 ?  360 PHE B CD1   1 
ATOM   8475  C  CD2   . PHE B 1 360 ? 111.687 138.558 154.061 1.00 13.35 ?  360 PHE B CD2   1 
ATOM   8476  C  CE1   . PHE B 1 360 ? 110.086 136.936 152.515 1.00 18.52 ?  360 PHE B CE1   1 
ATOM   8477  C  CE2   . PHE B 1 360 ? 111.644 137.202 154.303 1.00 18.20 ?  360 PHE B CE2   1 
ATOM   8478  C  CZ    . PHE B 1 360 ? 110.842 136.390 153.530 1.00 15.01 ?  360 PHE B CZ    1 
ATOM   8479  N  N     . GLN B 1 361 ? 111.117 142.796 149.923 1.00 18.99 ?  361 GLN B N     1 
ATOM   8480  C  CA    . GLN B 1 361 ? 111.261 144.165 149.436 1.00 9.60  ?  361 GLN B CA    1 
ATOM   8481  C  C     . GLN B 1 361 ? 110.517 145.164 150.312 1.00 9.13  ?  361 GLN B C     1 
ATOM   8482  O  O     . GLN B 1 361 ? 111.046 146.234 150.631 1.00 14.03 ?  361 GLN B O     1 
ATOM   8483  C  CB    . GLN B 1 361 ? 110.765 144.249 147.992 1.00 19.01 ?  361 GLN B CB    1 
ATOM   8484  C  CG    . GLN B 1 361 ? 110.648 145.658 147.445 1.00 20.19 ?  361 GLN B CG    1 
ATOM   8485  C  CD    . GLN B 1 361 ? 111.642 145.939 146.342 1.00 20.87 ?  361 GLN B CD    1 
ATOM   8486  O  OE1   . GLN B 1 361 ? 111.782 145.158 145.404 1.00 30.14 ?  361 GLN B OE1   1 
ATOM   8487  N  NE2   . GLN B 1 361 ? 112.344 147.060 146.449 1.00 20.20 ?  361 GLN B NE2   1 
ATOM   8488  N  N     . ASP B 1 362 ? 109.288 144.839 150.710 1.00 23.19 ?  362 ASP B N     1 
ATOM   8489  C  CA    . ASP B 1 362 ? 108.489 145.782 151.479 1.00 13.79 ?  362 ASP B CA    1 
ATOM   8490  C  C     . ASP B 1 362 ? 108.881 145.831 152.949 1.00 13.78 ?  362 ASP B C     1 
ATOM   8491  O  O     . ASP B 1 362 ? 108.618 146.840 153.610 1.00 23.01 ?  362 ASP B O     1 
ATOM   8492  C  CB    . ASP B 1 362 ? 107.004 145.452 151.338 1.00 16.01 ?  362 ASP B CB    1 
ATOM   8493  C  CG    . ASP B 1 362 ? 106.523 145.551 149.902 1.00 27.61 ?  362 ASP B CG    1 
ATOM   8494  O  OD1   . ASP B 1 362 ? 107.364 145.461 148.984 1.00 24.96 ?  362 ASP B OD1   1 
ATOM   8495  O  OD2   . ASP B 1 362 ? 105.309 145.737 149.688 1.00 37.15 -1 362 ASP B OD2   1 
ATOM   8496  N  N     . ASN B 1 363 ? 109.497 144.772 153.478 1.00 28.56 ?  363 ASN B N     1 
ATOM   8497  C  CA    . ASN B 1 363 ? 110.066 144.852 154.818 1.00 13.54 ?  363 ASN B CA    1 
ATOM   8498  C  C     . ASN B 1 363 ? 111.232 145.832 154.853 1.00 19.84 ?  363 ASN B C     1 
ATOM   8499  O  O     . ASN B 1 363 ? 111.396 146.577 155.826 1.00 25.82 ?  363 ASN B O     1 
ATOM   8500  C  CB    . ASN B 1 363 ? 110.516 143.469 155.288 1.00 10.51 ?  363 ASN B CB    1 
ATOM   8501  C  CG    . ASN B 1 363 ? 109.368 142.625 155.794 1.00 17.88 ?  363 ASN B CG    1 
ATOM   8502  O  OD1   . ASN B 1 363 ? 108.252 143.111 155.961 1.00 22.12 ?  363 ASN B OD1   1 
ATOM   8503  N  ND2   . ASN B 1 363 ? 109.637 141.351 156.045 1.00 20.62 ?  363 ASN B ND2   1 
ATOM   8504  N  N     . VAL B 1 364 ? 112.053 145.838 153.803 1.00 17.04 ?  364 VAL B N     1 
ATOM   8505  C  CA    . VAL B 1 364 ? 113.173 146.767 153.733 1.00 10.09 ?  364 VAL B CA    1 
ATOM   8506  C  C     . VAL B 1 364 ? 112.674 148.199 153.591 1.00 19.58 ?  364 VAL B C     1 
ATOM   8507  O  O     . VAL B 1 364 ? 113.128 149.106 154.296 1.00 25.50 ?  364 VAL B O     1 
ATOM   8508  C  CB    . VAL B 1 364 ? 114.111 146.387 152.573 1.00 0.06  ?  364 VAL B CB    1 
ATOM   8509  C  CG1   . VAL B 1 364 ? 115.334 147.273 152.577 1.00 7.05  ?  364 VAL B CG1   1 
ATOM   8510  C  CG2   . VAL B 1 364 ? 114.503 144.928 152.661 1.00 3.59  ?  364 VAL B CG2   1 
ATOM   8511  N  N     . ASN B 1 365 ? 111.729 148.421 152.679 1.00 14.89 ?  365 ASN B N     1 
ATOM   8512  C  CA    . ASN B 1 365 ? 111.361 149.772 152.280 1.00 4.58  ?  365 ASN B CA    1 
ATOM   8513  C  C     . ASN B 1 365 ? 110.323 150.417 153.185 1.00 12.69 ?  365 ASN B C     1 
ATOM   8514  O  O     . ASN B 1 365 ? 110.126 151.633 153.097 1.00 24.10 ?  365 ASN B O     1 
ATOM   8515  C  CB    . ASN B 1 365 ? 110.853 149.764 150.840 1.00 18.94 ?  365 ASN B CB    1 
ATOM   8516  C  CG    . ASN B 1 365 ? 111.938 149.411 149.847 1.00 16.80 ?  365 ASN B CG    1 
ATOM   8517  O  OD1   . ASN B 1 365 ? 112.989 150.046 149.812 1.00 14.28 ?  365 ASN B OD1   1 
ATOM   8518  N  ND2   . ASN B 1 365 ? 111.692 148.392 149.039 1.00 18.87 ?  365 ASN B ND2   1 
ATOM   8519  N  N     . LYS B 1 366 ? 109.656 149.650 154.050 1.00 16.21 ?  366 LYS B N     1 
ATOM   8520  C  CA    . LYS B 1 366 ? 108.718 150.257 154.985 1.00 19.85 ?  366 LYS B CA    1 
ATOM   8521  C  C     . LYS B 1 366 ? 109.432 150.986 156.112 1.00 20.14 ?  366 LYS B C     1 
ATOM   8522  O  O     . LYS B 1 366 ? 108.835 151.863 156.745 1.00 30.80 ?  366 LYS B O     1 
ATOM   8523  C  CB    . LYS B 1 366 ? 107.773 149.197 155.552 1.00 16.52 ?  366 LYS B CB    1 
ATOM   8524  C  CG    . LYS B 1 366 ? 108.365 148.346 156.658 1.00 25.80 ?  366 LYS B CG    1 
ATOM   8525  C  CD    . LYS B 1 366 ? 107.276 147.613 157.418 1.00 28.53 ?  366 LYS B CD    1 
ATOM   8526  C  CE    . LYS B 1 366 ? 106.386 146.820 156.476 1.00 23.89 ?  366 LYS B CE    1 
ATOM   8527  N  NZ    . LYS B 1 366 ? 105.449 145.936 157.220 1.00 28.97 1  366 LYS B NZ    1 
ATOM   8528  N  N     . VAL B 1 367 ? 110.695 150.649 156.369 1.00 26.19 ?  367 VAL B N     1 
ATOM   8529  C  CA    . VAL B 1 367 ? 111.516 151.315 157.365 1.00 18.01 ?  367 VAL B CA    1 
ATOM   8530  C  C     . VAL B 1 367 ? 112.728 151.990 156.739 1.00 17.99 ?  367 VAL B C     1 
ATOM   8531  O  O     . VAL B 1 367 ? 113.593 152.493 157.454 1.00 23.59 ?  367 VAL B O     1 
ATOM   8532  C  CB    . VAL B 1 367 ? 111.951 150.334 158.472 1.00 14.88 ?  367 VAL B CB    1 
ATOM   8533  C  CG1   . VAL B 1 367 ? 110.750 149.902 159.292 1.00 17.71 ?  367 VAL B CG1   1 
ATOM   8534  C  CG2   . VAL B 1 367 ? 112.638 149.135 157.862 1.00 8.15  ?  367 VAL B CG2   1 
ATOM   8535  N  N     . HIS B 1 368 ? 112.810 152.000 155.411 1.00 17.51 ?  368 HIS B N     1 
ATOM   8536  C  CA    . HIS B 1 368 ? 113.925 152.636 154.726 1.00 3.61  ?  368 HIS B CA    1 
ATOM   8537  C  C     . HIS B 1 368 ? 113.853 154.146 154.904 1.00 17.40 ?  368 HIS B C     1 
ATOM   8538  O  O     . HIS B 1 368 ? 112.793 154.754 154.729 1.00 30.35 ?  368 HIS B O     1 
ATOM   8539  C  CB    . HIS B 1 368 ? 113.905 152.270 153.244 1.00 10.78 ?  368 HIS B CB    1 
ATOM   8540  C  CG    . HIS B 1 368 ? 115.099 152.754 152.483 1.00 6.15  ?  368 HIS B CG    1 
ATOM   8541  N  ND1   . HIS B 1 368 ? 115.027 153.160 151.170 1.00 18.67 ?  368 HIS B ND1   1 
ATOM   8542  C  CD2   . HIS B 1 368 ? 116.393 152.896 152.850 1.00 7.27  ?  368 HIS B CD2   1 
ATOM   8543  C  CE1   . HIS B 1 368 ? 116.226 153.530 150.758 1.00 17.56 ?  368 HIS B CE1   1 
ATOM   8544  N  NE2   . HIS B 1 368 ? 117.072 153.381 151.760 1.00 16.59 ?  368 HIS B NE2   1 
ATOM   8545  N  N     . ALA B 1 369 ? 114.983 154.750 155.255 1.00 20.81 ?  369 ALA B N     1 
ATOM   8546  C  CA    . ALA B 1 369 ? 115.037 156.175 155.544 1.00 13.95 ?  369 ALA B CA    1 
ATOM   8547  C  C     . ALA B 1 369 ? 115.318 157.029 154.318 1.00 25.08 ?  369 ALA B C     1 
ATOM   8548  O  O     . ALA B 1 369 ? 115.263 158.258 154.417 1.00 32.91 ?  369 ALA B O     1 
ATOM   8549  C  CB    . ALA B 1 369 ? 116.098 156.454 156.611 1.00 11.15 ?  369 ALA B CB    1 
ATOM   8550  N  N     . ASN B 1 370 ? 115.606 156.421 153.172 1.00 18.57 ?  370 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 370 ? 115.997 157.149 151.974 1.00 12.01 ?  370 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 370 ? 115.172 156.707 150.777 1.00 13.34 ?  370 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 370 ? 115.690 156.541 149.671 1.00 24.87 ?  370 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 370 ? 117.487 156.975 151.695 1.00 12.83 ?  370 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 370 ? 118.357 157.545 152.795 1.00 12.83 ?  370 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 370 ? 118.329 158.744 153.064 1.00 29.53 ?  370 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 370 ? 119.136 156.686 153.437 1.00 12.13 ?  370 ASN B ND2   1 
ATOM   8558  N  N     . ASN B 1 371 ? 113.867 156.512 150.979 1.00 19.78 ?  371 ASN B N     1 
ATOM   8559  C  CA    . ASN B 1 371 ? 112.990 156.142 149.874 1.00 11.60 ?  371 ASN B CA    1 
ATOM   8560  C  C     . ASN B 1 371 ? 112.852 157.259 148.849 1.00 16.37 ?  371 ASN B C     1 
ATOM   8561  O  O     . ASN B 1 371 ? 112.516 156.983 147.694 1.00 26.99 ?  371 ASN B O     1 
ATOM   8562  C  CB    . ASN B 1 371 ? 111.609 155.749 150.398 1.00 9.05  ?  371 ASN B CB    1 
ATOM   8563  C  CG    . ASN B 1 371 ? 111.553 154.316 150.874 1.00 17.59 ?  371 ASN B CG    1 
ATOM   8564  O  OD1   . ASN B 1 371 ? 112.388 153.495 150.503 1.00 23.47 ?  371 ASN B OD1   1 
ATOM   8565  N  ND2   . ASN B 1 371 ? 110.566 154.007 151.703 1.00 24.49 ?  371 ASN B ND2   1 
ATOM   8566  N  N     . HIS B 1 372 ? 113.093 158.509 149.250 1.00 19.85 ?  372 HIS B N     1 
ATOM   8567  C  CA    . HIS B 1 372 ? 113.069 159.614 148.299 1.00 19.82 ?  372 HIS B CA    1 
ATOM   8568  C  C     . HIS B 1 372 ? 114.177 159.471 147.264 1.00 22.75 ?  372 HIS B C     1 
ATOM   8569  O  O     . HIS B 1 372 ? 113.970 159.749 146.077 1.00 28.09 ?  372 HIS B O     1 
ATOM   8570  C  CB    . HIS B 1 372 ? 113.192 160.945 149.039 1.00 23.38 ?  372 HIS B CB    1 
ATOM   8571  C  CG    . HIS B 1 372 ? 114.515 161.140 149.710 1.00 22.20 ?  372 HIS B CG    1 
ATOM   8572  N  ND1   . HIS B 1 372 ? 114.949 160.341 150.745 1.00 21.74 ?  372 HIS B ND1   1 
ATOM   8573  C  CD2   . HIS B 1 372 ? 115.503 162.038 149.489 1.00 24.73 ?  372 HIS B CD2   1 
ATOM   8574  C  CE1   . HIS B 1 372 ? 116.147 160.736 151.132 1.00 20.00 ?  372 HIS B CE1   1 
ATOM   8575  N  NE2   . HIS B 1 372 ? 116.505 161.767 150.389 1.00 23.90 ?  372 HIS B NE2   1 
ATOM   8576  N  N     . ILE B 1 373 ? 115.367 159.053 147.699 1.00 16.66 ?  373 ILE B N     1 
ATOM   8577  C  CA    . ILE B 1 373 ? 116.460 158.812 146.761 1.00 19.92 ?  373 ILE B CA    1 
ATOM   8578  C  C     . ILE B 1 373 ? 116.105 157.664 145.831 1.00 21.25 ?  373 ILE B C     1 
ATOM   8579  O  O     . ILE B 1 373 ? 116.199 157.778 144.603 1.00 37.31 ?  373 ILE B O     1 
ATOM   8580  C  CB    . ILE B 1 373 ? 117.767 158.532 147.525 1.00 24.82 ?  373 ILE B CB    1 
ATOM   8581  C  CG1   . ILE B 1 373 ? 118.183 159.755 148.339 1.00 21.51 ?  373 ILE B CG1   1 
ATOM   8582  C  CG2   . ILE B 1 373 ? 118.871 158.122 146.565 1.00 21.97 ?  373 ILE B CG2   1 
ATOM   8583  C  CD1   . ILE B 1 373 ? 119.199 159.452 149.408 1.00 18.19 ?  373 ILE B CD1   1 
ATOM   8584  N  N     . SER B 1 374 ? 115.672 156.546 146.406 1.00 15.22 ?  374 SER B N     1 
ATOM   8585  C  CA    . SER B 1 374 ? 115.258 155.353 145.685 1.00 10.77 ?  374 SER B CA    1 
ATOM   8586  C  C     . SER B 1 374 ? 114.783 154.338 146.710 1.00 20.36 ?  374 SER B C     1 
ATOM   8587  O  O     . SER B 1 374 ? 115.128 154.420 147.892 1.00 23.07 ?  374 SER B O     1 
ATOM   8588  C  CB    . SER B 1 374 ? 116.394 154.762 144.847 1.00 21.86 ?  374 SER B CB    1 
ATOM   8589  O  OG    . SER B 1 374 ? 115.917 153.748 143.985 1.00 35.99 ?  374 SER B OG    1 
ATOM   8590  N  N     . LYS B 1 375 ? 113.983 153.385 146.248 1.00 26.47 ?  375 LYS B N     1 
ATOM   8591  C  CA    . LYS B 1 375 ? 113.689 152.222 147.064 1.00 12.12 ?  375 LYS B CA    1 
ATOM   8592  C  C     . LYS B 1 375 ? 114.872 151.261 147.033 1.00 15.13 ?  375 LYS B C     1 
ATOM   8593  O  O     . LYS B 1 375 ? 115.682 151.262 146.102 1.00 28.03 ?  375 LYS B O     1 
ATOM   8594  C  CB    . LYS B 1 375 ? 112.426 151.519 146.566 1.00 14.41 ?  375 LYS B CB    1 
ATOM   8595  C  CG    . LYS B 1 375 ? 111.178 152.381 146.584 1.00 18.59 ?  375 LYS B CG    1 
ATOM   8596  C  CD    . LYS B 1 375 ? 110.588 152.462 147.975 1.00 21.94 ?  375 LYS B CD    1 
ATOM   8597  C  CE    . LYS B 1 375 ? 109.074 152.514 147.928 1.00 23.73 ?  375 LYS B CE    1 
ATOM   8598  N  NZ    . LYS B 1 375 ? 108.579 153.916 147.875 1.00 26.61 1  375 LYS B NZ    1 
ATOM   8599  N  N     . VAL B 1 376 ? 114.979 150.442 148.072 1.00 12.10 ?  376 VAL B N     1 
ATOM   8600  C  CA    . VAL B 1 376 ? 115.975 149.377 148.087 1.00 13.01 ?  376 VAL B CA    1 
ATOM   8601  C  C     . VAL B 1 376 ? 115.452 148.239 147.221 1.00 15.90 ?  376 VAL B C     1 
ATOM   8602  O  O     . VAL B 1 376 ? 114.411 147.645 147.519 1.00 25.73 ?  376 VAL B O     1 
ATOM   8603  C  CB    . VAL B 1 376 ? 116.266 148.902 149.517 1.00 9.66  ?  376 VAL B CB    1 
ATOM   8604  C  CG1   . VAL B 1 376 ? 117.322 147.806 149.508 1.00 5.98  ?  376 VAL B CG1   1 
ATOM   8605  C  CG2   . VAL B 1 376 ? 116.703 150.065 150.385 1.00 6.35  ?  376 VAL B CG2   1 
ATOM   8606  N  N     . LYS B 1 377 ? 116.171 147.935 146.142 1.00 14.65 ?  377 LYS B N     1 
ATOM   8607  C  CA    . LYS B 1 377 ? 115.718 146.942 145.181 1.00 13.59 ?  377 LYS B CA    1 
ATOM   8608  C  C     . LYS B 1 377 ? 116.423 145.604 145.313 1.00 8.55  ?  377 LYS B C     1 
ATOM   8609  O  O     . LYS B 1 377 ? 115.882 144.594 144.854 1.00 25.31 ?  377 LYS B O     1 
ATOM   8610  C  CB    . LYS B 1 377 ? 115.909 147.460 143.752 1.00 16.40 ?  377 LYS B CB    1 
ATOM   8611  C  CG    . LYS B 1 377 ? 115.133 148.719 143.440 1.00 9.68  ?  377 LYS B CG    1 
ATOM   8612  C  CD    . LYS B 1 377 ? 115.794 149.475 142.310 1.00 20.92 ?  377 LYS B CD    1 
ATOM   8613  C  CE    . LYS B 1 377 ? 115.706 150.968 142.525 1.00 25.14 ?  377 LYS B CE    1 
ATOM   8614  N  NZ    . LYS B 1 377 ? 116.666 151.710 141.664 1.00 23.03 1  377 LYS B NZ    1 
ATOM   8615  N  N     . PHE B 1 378 ? 117.605 145.570 145.919 1.00 6.05  ?  378 PHE B N     1 
ATOM   8616  C  CA    . PHE B 1 378 ? 118.369 144.336 146.034 1.00 5.14  ?  378 PHE B CA    1 
ATOM   8617  C  C     . PHE B 1 378 ? 119.415 144.514 147.123 1.00 10.46 ?  378 PHE B C     1 
ATOM   8618  O  O     . PHE B 1 378 ? 119.595 145.604 147.669 1.00 14.98 ?  378 PHE B O     1 
ATOM   8619  C  CB    . PHE B 1 378 ? 119.009 143.941 144.697 1.00 2.96  ?  378 PHE B CB    1 
ATOM   8620  C  CG    . PHE B 1 378 ? 120.139 144.834 144.261 1.00 7.80  ?  378 PHE B CG    1 
ATOM   8621  C  CD1   . PHE B 1 378 ? 119.950 146.197 144.099 1.00 14.95 ?  378 PHE B CD1   1 
ATOM   8622  C  CD2   . PHE B 1 378 ? 121.386 144.303 143.984 1.00 4.48  ?  378 PHE B CD2   1 
ATOM   8623  C  CE1   . PHE B 1 378 ? 120.982 147.009 143.690 1.00 6.75  ?  378 PHE B CE1   1 
ATOM   8624  C  CE2   . PHE B 1 378 ? 122.421 145.114 143.571 1.00 7.80  ?  378 PHE B CE2   1 
ATOM   8625  C  CZ    . PHE B 1 378 ? 122.218 146.468 143.424 1.00 9.48  ?  378 PHE B CZ    1 
ATOM   8626  N  N     . SER B 1 379 ? 120.100 143.422 147.434 1.00 2.51  ?  379 SER B N     1 
ATOM   8627  C  CA    . SER B 1 379 ? 121.085 143.374 148.502 1.00 7.97  ?  379 SER B CA    1 
ATOM   8628  C  C     . SER B 1 379 ? 122.438 142.964 147.931 1.00 8.40  ?  379 SER B C     1 
ATOM   8629  O  O     . SER B 1 379 ? 122.606 142.803 146.722 1.00 19.01 ?  379 SER B O     1 
ATOM   8630  C  CB    . SER B 1 379 ? 120.641 142.412 149.605 1.00 6.80  ?  379 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 379 ? 121.122 142.833 150.866 1.00 10.43 ?  379 SER B OG    1 
ATOM   8632  N  N     . ASN B 1 380 ? 123.409 142.798 148.822 1.00 10.17 ?  380 ASN B N     1 
ATOM   8633  C  CA    . ASN B 1 380 ? 124.771 142.478 148.431 1.00 7.85  ?  380 ASN B CA    1 
ATOM   8634  C  C     . ASN B 1 380 ? 124.958 140.962 148.392 1.00 13.89 ?  380 ASN B C     1 
ATOM   8635  O  O     . ASN B 1 380 ? 124.000 140.188 148.456 1.00 20.08 ?  380 ASN B O     1 
ATOM   8636  C  CB    . ASN B 1 380 ? 125.768 143.150 149.372 1.00 8.11  ?  380 ASN B CB    1 
ATOM   8637  C  CG    . ASN B 1 380 ? 125.673 142.634 150.788 1.00 8.77  ?  380 ASN B CG    1 
ATOM   8638  O  OD1   . ASN B 1 380 ? 124.582 142.427 151.312 1.00 22.19 ?  380 ASN B OD1   1 
ATOM   8639  N  ND2   . ASN B 1 380 ? 126.820 142.442 151.423 1.00 17.17 ?  380 ASN B ND2   1 
ATOM   8640  N  N     . LEU B 1 381 ? 126.213 140.527 148.271 1.00 19.78 ?  381 LEU B N     1 
ATOM   8641  C  CA    . LEU B 1 381 ? 126.523 139.105 148.240 1.00 8.77  ?  381 LEU B CA    1 
ATOM   8642  C  C     . LEU B 1 381 ? 126.285 138.434 149.587 1.00 6.62  ?  381 LEU B C     1 
ATOM   8643  O  O     . LEU B 1 381 ? 126.092 137.214 149.632 1.00 22.70 ?  381 LEU B O     1 
ATOM   8644  C  CB    . LEU B 1 381 ? 127.973 138.916 147.789 1.00 17.60 ?  381 LEU B CB    1 
ATOM   8645  C  CG    . LEU B 1 381 ? 128.615 137.529 147.767 1.00 20.47 ?  381 LEU B CG    1 
ATOM   8646  C  CD1   . LEU B 1 381 ? 127.891 136.598 146.814 1.00 22.72 ?  381 LEU B CD1   1 
ATOM   8647  C  CD2   . LEU B 1 381 ? 130.077 137.645 147.394 1.00 15.48 ?  381 LEU B CD2   1 
ATOM   8648  N  N     . CYS B 1 382 ? 126.279 139.198 150.676 1.00 21.44 ?  382 CYS B N     1 
ATOM   8649  C  CA    . CYS B 1 382 ? 126.064 138.655 152.010 1.00 3.70  ?  382 CYS B CA    1 
ATOM   8650  C  C     . CYS B 1 382 ? 124.692 138.992 152.575 1.00 12.64 ?  382 CYS B C     1 
ATOM   8651  O  O     . CYS B 1 382 ? 124.405 138.627 153.719 1.00 23.34 ?  382 CYS B O     1 
ATOM   8652  C  CB    . CYS B 1 382 ? 127.159 139.149 152.961 1.00 20.70 ?  382 CYS B CB    1 
ATOM   8653  S  SG    . CYS B 1 382 ? 128.847 138.830 152.393 1.00 37.09 ?  382 CYS B SG    1 
ATOM   8654  N  N     . SER B 1 383 ? 123.848 139.695 151.814 1.00 15.80 ?  383 SER B N     1 
ATOM   8655  C  CA    . SER B 1 383 ? 122.432 139.888 152.126 1.00 11.02 ?  383 SER B CA    1 
ATOM   8656  C  C     . SER B 1 383 ? 122.204 140.769 153.353 1.00 18.31 ?  383 SER B C     1 
ATOM   8657  O  O     . SER B 1 383 ? 121.208 140.603 154.060 1.00 27.77 ?  383 SER B O     1 
ATOM   8658  C  CB    . SER B 1 383 ? 121.714 138.547 152.306 1.00 8.16  ?  383 SER B CB    1 
ATOM   8659  O  OG    . SER B 1 383 ? 121.768 137.782 151.118 1.00 36.35 ?  383 SER B OG    1 
ATOM   8660  N  N     . GLU B 1 384 ? 123.100 141.711 153.629 1.00 11.76 ?  384 GLU B N     1 
ATOM   8661  C  CA    . GLU B 1 384 ? 122.888 142.644 154.726 1.00 9.89  ?  384 GLU B CA    1 
ATOM   8662  C  C     . GLU B 1 384 ? 122.924 144.105 154.307 1.00 16.66 ?  384 GLU B C     1 
ATOM   8663  O  O     . GLU B 1 384 ? 122.460 144.958 155.071 1.00 26.21 ?  384 GLU B O     1 
ATOM   8664  C  CB    . GLU B 1 384 ? 123.920 142.413 155.843 1.00 9.21  ?  384 GLU B CB    1 
ATOM   8665  C  CG    . GLU B 1 384 ? 125.122 143.336 155.808 1.00 11.23 ?  384 GLU B CG    1 
ATOM   8666  C  CD    . GLU B 1 384 ? 126.185 142.868 154.846 1.00 22.17 ?  384 GLU B CD    1 
ATOM   8667  O  OE1   . GLU B 1 384 ? 126.086 141.720 154.375 1.00 23.44 ?  384 GLU B OE1   1 
ATOM   8668  O  OE2   . GLU B 1 384 ? 127.121 143.642 154.568 1.00 29.48 -1 384 GLU B OE2   1 
ATOM   8669  N  N     . VAL B 1 385 ? 123.442 144.421 153.128 1.00 11.10 ?  385 VAL B N     1 
ATOM   8670  C  CA    . VAL B 1 385 ? 123.506 145.796 152.652 1.00 2.81  ?  385 VAL B CA    1 
ATOM   8671  C  C     . VAL B 1 385 ? 122.203 146.116 151.936 1.00 17.93 ?  385 VAL B C     1 
ATOM   8672  O  O     . VAL B 1 385 ? 121.871 145.493 150.922 1.00 25.12 ?  385 VAL B O     1 
ATOM   8673  C  CB    . VAL B 1 385 ? 124.710 146.010 151.726 1.00 5.27  ?  385 VAL B CB    1 
ATOM   8674  C  CG1   . VAL B 1 385 ? 124.670 147.398 151.143 1.00 8.53  ?  385 VAL B CG1   1 
ATOM   8675  C  CG2   . VAL B 1 385 ? 125.996 145.800 152.490 1.00 8.98  ?  385 VAL B CG2   1 
ATOM   8676  N  N     . LEU B 1 386 ? 121.460 147.088 152.466 1.00 19.30 ?  386 LEU B N     1 
ATOM   8677  C  CA    . LEU B 1 386 ? 120.149 147.471 151.942 1.00 2.15  ?  386 LEU B CA    1 
ATOM   8678  C  C     . LEU B 1 386 ? 120.119 148.990 151.825 1.00 5.61  ?  386 LEU B C     1 
ATOM   8679  O  O     . LEU B 1 386 ? 119.755 149.688 152.775 1.00 12.33 ?  386 LEU B O     1 
ATOM   8680  C  CB    . LEU B 1 386 ? 119.036 146.945 152.836 1.00 5.81  ?  386 LEU B CB    1 
ATOM   8681  C  CG    . LEU B 1 386 ? 118.949 145.421 152.891 1.00 0.77  ?  386 LEU B CG    1 
ATOM   8682  C  CD1   . LEU B 1 386 ? 117.915 144.990 153.893 1.00 7.88  ?  386 LEU B CD1   1 
ATOM   8683  C  CD2   . LEU B 1 386 ? 118.631 144.863 151.516 1.00 6.73  ?  386 LEU B CD2   1 
ATOM   8684  N  N     . GLN B 1 387 ? 120.502 149.499 150.658 1.00 13.17 ?  387 GLN B N     1 
ATOM   8685  C  CA    . GLN B 1 387 ? 120.618 150.929 150.429 1.00 3.15  ?  387 GLN B CA    1 
ATOM   8686  C  C     . GLN B 1 387 ? 119.952 151.303 149.113 1.00 8.38  ?  387 GLN B C     1 
ATOM   8687  O  O     . GLN B 1 387 ? 119.752 150.466 148.232 1.00 22.69 ?  387 GLN B O     1 
ATOM   8688  C  CB    . GLN B 1 387 ? 122.087 151.372 150.418 1.00 0.56  ?  387 GLN B CB    1 
ATOM   8689  C  CG    . GLN B 1 387 ? 122.856 150.947 151.649 1.00 4.37  ?  387 GLN B CG    1 
ATOM   8690  C  CD    . GLN B 1 387 ? 124.270 151.464 151.656 1.00 10.53 ?  387 GLN B CD    1 
ATOM   8691  O  OE1   . GLN B 1 387 ? 124.622 152.354 150.886 1.00 20.68 ?  387 GLN B OE1   1 
ATOM   8692  N  NE2   . GLN B 1 387 ? 125.095 150.906 152.527 1.00 9.52  ?  387 GLN B NE2   1 
ATOM   8693  N  N     . ALA B 1 388 ? 119.599 152.579 149.001 1.00 9.62  ?  388 ALA B N     1 
ATOM   8694  C  CA    . ALA B 1 388 ? 119.021 153.095 147.768 1.00 7.64  ?  388 ALA B CA    1 
ATOM   8695  C  C     . ALA B 1 388 ? 120.063 153.122 146.659 1.00 14.26 ?  388 ALA B C     1 
ATOM   8696  O  O     . ALA B 1 388 ? 121.223 153.483 146.881 1.00 25.40 ?  388 ALA B O     1 
ATOM   8697  C  CB    . ALA B 1 388 ? 118.459 154.497 147.992 1.00 11.59 ?  388 ALA B CB    1 
ATOM   8698  N  N     . SER B 1 389 ? 119.645 152.740 145.458 1.00 19.81 ?  389 SER B N     1 
ATOM   8699  C  CA    . SER B 1 389 ? 120.516 152.732 144.295 1.00 8.84  ?  389 SER B CA    1 
ATOM   8700  C  C     . SER B 1 389 ? 119.808 153.391 143.122 1.00 12.83 ?  389 SER B C     1 
ATOM   8701  O  O     . SER B 1 389 ? 118.580 153.367 143.021 1.00 23.31 ?  389 SER B O     1 
ATOM   8702  C  CB    . SER B 1 389 ? 120.933 151.308 143.912 1.00 17.11 ?  389 SER B CB    1 
ATOM   8703  O  OG    . SER B 1 389 ? 119.811 150.445 143.852 1.00 23.86 ?  389 SER B OG    1 
ATOM   8704  N  N     . GLN B 1 390 ? 120.600 153.982 142.234 1.00 22.95 ?  390 GLN B N     1 
ATOM   8705  C  CA    . GLN B 1 390 ? 120.099 154.562 140.998 1.00 12.92 ?  390 GLN B CA    1 
ATOM   8706  C  C     . GLN B 1 390 ? 120.876 153.957 139.843 1.00 14.09 ?  390 GLN B C     1 
ATOM   8707  O  O     . GLN B 1 390 ? 122.110 153.915 139.876 1.00 25.00 ?  390 GLN B O     1 
ATOM   8708  C  CB    . GLN B 1 390 ? 120.235 156.086 141.002 1.00 10.67 ?  390 GLN B CB    1 
ATOM   8709  C  CG    . GLN B 1 390 ? 119.271 156.776 141.946 1.00 11.92 ?  390 GLN B CG    1 
ATOM   8710  C  CD    . GLN B 1 390 ? 119.473 158.273 141.996 1.00 26.59 ?  390 GLN B CD    1 
ATOM   8711  O  OE1   . GLN B 1 390 ? 120.421 158.803 141.419 1.00 33.24 ?  390 GLN B OE1   1 
ATOM   8712  N  NE2   . GLN B 1 390 ? 118.580 158.965 142.692 1.00 18.02 ?  390 GLN B NE2   1 
ATOM   8713  N  N     . VAL B 1 391 ? 120.157 153.480 138.829 1.00 26.31 ?  391 VAL B N     1 
ATOM   8714  C  CA    . VAL B 1 391 ? 120.807 152.817 137.709 1.00 20.02 ?  391 VAL B CA    1 
ATOM   8715  C  C     . VAL B 1 391 ? 121.524 153.848 136.848 1.00 25.64 ?  391 VAL B C     1 
ATOM   8716  O  O     . VAL B 1 391 ? 121.054 154.980 136.669 1.00 22.59 ?  391 VAL B O     1 
ATOM   8717  C  CB    . VAL B 1 391 ? 119.784 152.003 136.896 1.00 15.69 ?  391 VAL B CB    1 
ATOM   8718  C  CG1   . VAL B 1 391 ? 118.839 152.915 136.128 1.00 16.52 ?  391 VAL B CG1   1 
ATOM   8719  C  CG2   . VAL B 1 391 ? 120.495 151.035 135.963 1.00 17.13 ?  391 VAL B CG2   1 
ATOM   8720  N  N     . SER B 1 392 ? 122.689 153.468 136.337 1.00 32.86 ?  392 SER B N     1 
ATOM   8721  C  CA    . SER B 1 392 ? 123.462 154.329 135.459 1.00 21.49 ?  392 SER B CA    1 
ATOM   8722  C  C     . SER B 1 392 ? 123.093 154.067 134.007 1.00 28.88 ?  392 SER B C     1 
ATOM   8723  O  O     . SER B 1 392 ? 122.775 152.940 133.618 1.00 31.81 ?  392 SER B O     1 
ATOM   8724  C  CB    . SER B 1 392 ? 124.961 154.109 135.662 1.00 25.83 ?  392 SER B CB    1 
ATOM   8725  O  OG    . SER B 1 392 ? 125.323 154.276 137.020 1.00 36.93 ?  392 SER B OG    1 
ATOM   8726  N  N     . SER B 1 393 ? 123.138 155.123 133.207 1.00 35.47 ?  393 SER B N     1 
ATOM   8727  C  CA    . SER B 1 393 ? 122.865 155.047 131.776 1.00 28.19 ?  393 SER B CA    1 
ATOM   8728  C  C     . SER B 1 393 ? 124.202 155.177 131.053 1.00 32.27 ?  393 SER B C     1 
ATOM   8729  O  O     . SER B 1 393 ? 124.635 156.278 130.708 1.00 35.82 ?  393 SER B O     1 
ATOM   8730  C  CB    . SER B 1 393 ? 121.882 156.127 131.345 1.00 31.94 ?  393 SER B CB    1 
ATOM   8731  O  OG    . SER B 1 393 ? 120.788 156.203 132.242 1.00 43.25 ?  393 SER B OG    1 
ATOM   8732  N  N     . TYR B 1 394 ? 124.857 154.042 130.830 1.00 32.45 ?  394 TYR B N     1 
ATOM   8733  C  CA    . TYR B 1 394 ? 126.115 154.017 130.095 1.00 29.04 ?  394 TYR B CA    1 
ATOM   8734  C  C     . TYR B 1 394 ? 125.802 154.044 128.606 1.00 30.77 ?  394 TYR B C     1 
ATOM   8735  O  O     . TYR B 1 394 ? 125.253 153.082 128.060 1.00 34.55 ?  394 TYR B O     1 
ATOM   8736  C  CB    . TYR B 1 394 ? 126.933 152.787 130.472 1.00 28.80 ?  394 TYR B CB    1 
ATOM   8737  C  CG    . TYR B 1 394 ? 127.340 152.753 131.926 1.00 28.49 ?  394 TYR B CG    1 
ATOM   8738  C  CD1   . TYR B 1 394 ? 128.321 153.606 132.414 1.00 29.28 ?  394 TYR B CD1   1 
ATOM   8739  C  CD2   . TYR B 1 394 ? 126.738 151.873 132.814 1.00 25.63 ?  394 TYR B CD2   1 
ATOM   8740  C  CE1   . TYR B 1 394 ? 128.693 153.579 133.742 1.00 29.53 ?  394 TYR B CE1   1 
ATOM   8741  C  CE2   . TYR B 1 394 ? 127.104 151.838 134.142 1.00 26.56 ?  394 TYR B CE2   1 
ATOM   8742  C  CZ    . TYR B 1 394 ? 128.080 152.692 134.601 1.00 36.49 ?  394 TYR B CZ    1 
ATOM   8743  O  OH    . TYR B 1 394 ? 128.445 152.659 135.928 1.00 40.21 ?  394 TYR B OH    1 
ATOM   8744  N  N     . THR B 1 395 ? 126.143 155.147 127.954 1.00 38.04 ?  395 THR B N     1 
ATOM   8745  C  CA    . THR B 1 395 ? 125.801 155.376 126.561 1.00 33.83 ?  395 THR B CA    1 
ATOM   8746  C  C     . THR B 1 395 ? 126.924 154.864 125.661 1.00 37.74 ?  395 THR B C     1 
ATOM   8747  O  O     . THR B 1 395 ? 127.823 154.141 126.098 1.00 34.98 ?  395 THR B O     1 
ATOM   8748  C  CB    . THR B 1 395 ? 125.519 156.857 126.336 1.00 36.13 ?  395 THR B CB    1 
ATOM   8749  O  OG1   . THR B 1 395 ? 126.698 157.615 126.629 1.00 37.24 ?  395 THR B OG1   1 
ATOM   8750  C  CG2   . THR B 1 395 ? 124.393 157.323 127.243 1.00 35.65 ?  395 THR B CG2   1 
ATOM   8751  N  N     . ASP B 1 396 ? 126.877 155.236 124.384 1.00 40.82 ?  396 ASP B N     1 
ATOM   8752  C  CA    . ASP B 1 396 ? 127.924 154.851 123.452 1.00 34.89 ?  396 ASP B CA    1 
ATOM   8753  C  C     . ASP B 1 396 ? 129.251 155.497 123.847 1.00 39.22 ?  396 ASP B C     1 
ATOM   8754  O  O     . ASP B 1 396 ? 129.320 156.366 124.719 1.00 46.61 ?  396 ASP B O     1 
ATOM   8755  C  CB    . ASP B 1 396 ? 127.541 155.240 122.025 1.00 39.86 ?  396 ASP B CB    1 
ATOM   8756  C  CG    . ASP B 1 396 ? 126.324 154.490 121.523 1.00 45.72 ?  396 ASP B CG    1 
ATOM   8757  O  OD1   . ASP B 1 396 ? 126.266 153.256 121.707 1.00 42.96 ?  396 ASP B OD1   1 
ATOM   8758  O  OD2   . ASP B 1 396 ? 125.427 155.131 120.939 1.00 46.25 -1 396 ASP B OD2   1 
ATOM   8759  N  N     . TYR B 1 397 ? 130.319 155.053 123.182 1.00 32.24 ?  397 TYR B N     1 
ATOM   8760  C  CA    . TYR B 1 397 ? 131.661 155.492 123.554 1.00 34.09 ?  397 TYR B CA    1 
ATOM   8761  C  C     . TYR B 1 397 ? 131.822 156.999 123.385 1.00 34.30 ?  397 TYR B C     1 
ATOM   8762  O  O     . TYR B 1 397 ? 132.441 157.661 124.225 1.00 41.35 ?  397 TYR B O     1 
ATOM   8763  C  CB    . TYR B 1 397 ? 132.703 154.738 122.727 1.00 32.22 ?  397 TYR B CB    1 
ATOM   8764  C  CG    . TYR B 1 397 ? 134.128 155.180 122.970 1.00 31.70 ?  397 TYR B CG    1 
ATOM   8765  C  CD1   . TYR B 1 397 ? 134.686 156.225 122.244 1.00 32.38 ?  397 TYR B CD1   1 
ATOM   8766  C  CD2   . TYR B 1 397 ? 134.917 154.550 123.922 1.00 28.43 ?  397 TYR B CD2   1 
ATOM   8767  C  CE1   . TYR B 1 397 ? 135.983 156.631 122.463 1.00 33.34 ?  397 TYR B CE1   1 
ATOM   8768  C  CE2   . TYR B 1 397 ? 136.216 154.950 124.146 1.00 30.86 ?  397 TYR B CE2   1 
ATOM   8769  C  CZ    . TYR B 1 397 ? 136.744 155.991 123.414 1.00 36.04 ?  397 TYR B CZ    1 
ATOM   8770  O  OH    . TYR B 1 397 ? 138.039 156.395 123.632 1.00 39.42 ?  397 TYR B OH    1 
ATOM   8771  N  N     . ASP B 1 398 ? 131.280 157.556 122.303 1.00 43.33 ?  398 ASP B N     1 
ATOM   8772  C  CA    . ASP B 1 398 ? 131.451 158.982 122.043 1.00 43.51 ?  398 ASP B CA    1 
ATOM   8773  C  C     . ASP B 1 398 ? 130.591 159.839 122.962 1.00 47.22 ?  398 ASP B C     1 
ATOM   8774  O  O     . ASP B 1 398 ? 130.943 160.990 123.240 1.00 49.56 ?  398 ASP B O     1 
ATOM   8775  C  CB    . ASP B 1 398 ? 131.132 159.290 120.581 1.00 45.31 ?  398 ASP B CB    1 
ATOM   8776  C  CG    . ASP B 1 398 ? 129.897 158.559 120.088 1.00 49.08 ?  398 ASP B CG    1 
ATOM   8777  O  OD1   . ASP B 1 398 ? 129.846 157.319 120.226 1.00 47.02 ?  398 ASP B OD1   1 
ATOM   8778  O  OD2   . ASP B 1 398 ? 128.981 159.222 119.561 1.00 51.13 -1 398 ASP B OD2   1 
ATOM   8779  N  N     . GLU B 1 399 ? 129.472 159.305 123.439 1.00 46.85 ?  399 GLU B N     1 
ATOM   8780  C  CA    . GLU B 1 399 ? 128.526 160.070 124.235 1.00 42.12 ?  399 GLU B CA    1 
ATOM   8781  C  C     . GLU B 1 399 ? 128.944 160.103 125.704 1.00 48.56 ?  399 GLU B C     1 
ATOM   8782  O  O     . GLU B 1 399 ? 129.855 159.397 126.140 1.00 48.89 ?  399 GLU B O     1 
ATOM   8783  C  CB    . GLU B 1 399 ? 127.122 159.486 124.095 1.00 44.22 ?  399 GLU B CB    1 
ATOM   8784  C  CG    . GLU B 1 399 ? 126.475 159.750 122.751 1.00 48.53 ?  399 GLU B CG    1 
ATOM   8785  C  CD    . GLU B 1 399 ? 125.447 158.701 122.387 1.00 52.02 ?  399 GLU B CD    1 
ATOM   8786  O  OE1   . GLU B 1 399 ? 124.844 158.115 123.310 1.00 50.37 ?  399 GLU B OE1   1 
ATOM   8787  O  OE2   . GLU B 1 399 ? 125.240 158.465 121.179 1.00 53.71 -1 399 GLU B OE2   1 
ATOM   8788  N  N     . GLU B 1 400 ? 128.257 160.947 126.469 1.00 47.89 ?  400 GLU B N     1 
ATOM   8789  C  CA    . GLU B 1 400 ? 128.506 161.093 127.896 1.00 41.02 ?  400 GLU B CA    1 
ATOM   8790  C  C     . GLU B 1 400 ? 127.566 160.187 128.680 1.00 44.36 ?  400 GLU B C     1 
ATOM   8791  O  O     . GLU B 1 400 ? 126.354 160.186 128.445 1.00 43.18 ?  400 GLU B O     1 
ATOM   8792  C  CB    . GLU B 1 400 ? 128.319 162.546 128.331 1.00 41.65 ?  400 GLU B CB    1 
ATOM   8793  C  CG    . GLU B 1 400 ? 129.534 163.431 128.110 1.00 47.55 ?  400 GLU B CG    1 
ATOM   8794  C  CD    . GLU B 1 400 ? 130.754 162.954 128.875 1.00 52.56 ?  400 GLU B CD    1 
ATOM   8795  O  OE1   . GLU B 1 400 ? 130.594 162.488 130.023 1.00 52.78 ?  400 GLU B OE1   1 
ATOM   8796  O  OE2   . GLU B 1 400 ? 131.873 163.050 128.330 1.00 49.93 -1 400 GLU B OE2   1 
ATOM   8797  N  N     . ASP B 1 401 ? 128.128 159.421 129.610 1.00 42.88 ?  401 ASP B N     1 
ATOM   8798  C  CA    . ASP B 1 401 ? 127.336 158.512 130.422 1.00 37.73 ?  401 ASP B CA    1 
ATOM   8799  C  C     . ASP B 1 401 ? 126.584 159.268 131.510 1.00 39.48 ?  401 ASP B C     1 
ATOM   8800  O  O     . ASP B 1 401 ? 127.028 160.313 131.993 1.00 43.20 ?  401 ASP B O     1 
ATOM   8801  C  CB    . ASP B 1 401 ? 128.224 157.446 131.062 1.00 37.41 ?  401 ASP B CB    1 
ATOM   8802  C  CG    . ASP B 1 401 ? 128.913 156.570 130.041 1.00 40.11 ?  401 ASP B CG    1 
ATOM   8803  O  OD1   . ASP B 1 401 ? 128.300 156.277 128.994 1.00 44.10 ?  401 ASP B OD1   1 
ATOM   8804  O  OD2   . ASP B 1 401 ? 130.070 156.174 130.285 1.00 40.53 -1 401 ASP B OD2   1 
ATOM   8805  N  N     . GLU B 1 402 ? 125.433 158.724 131.894 1.00 38.02 ?  402 GLU B N     1 
ATOM   8806  C  CA    . GLU B 1 402 ? 124.635 159.251 132.997 1.00 32.62 ?  402 GLU B CA    1 
ATOM   8807  C  C     . GLU B 1 402 ? 124.908 158.376 134.214 1.00 34.97 ?  402 GLU B C     1 
ATOM   8808  O  O     . GLU B 1 402 ? 124.339 157.292 134.355 1.00 39.72 ?  402 GLU B O     1 
ATOM   8809  C  CB    . GLU B 1 402 ? 123.152 159.272 132.641 1.00 37.87 ?  402 GLU B CB    1 
ATOM   8810  C  CG    . GLU B 1 402 ? 122.495 160.661 132.540 1.00 41.50 ?  402 GLU B CG    1 
ATOM   8811  C  CD    . GLU B 1 402 ? 122.578 161.528 133.801 1.00 48.02 ?  402 GLU B CD    1 
ATOM   8812  O  OE1   . GLU B 1 402 ? 121.803 162.505 133.876 1.00 46.69 ?  402 GLU B OE1   1 
ATOM   8813  O  OE2   . GLU B 1 402 ? 123.374 161.250 134.723 1.00 49.75 -1 402 GLU B OE2   1 
ATOM   8814  N  N     . ILE B 1 403 ? 125.778 158.855 135.095 1.00 32.50 ?  403 ILE B N     1 
ATOM   8815  C  CA    . ILE B 1 403 ? 126.232 158.064 136.232 1.00 28.63 ?  403 ILE B CA    1 
ATOM   8816  C  C     . ILE B 1 403 ? 125.192 158.125 137.342 1.00 31.15 ?  403 ILE B C     1 
ATOM   8817  O  O     . ILE B 1 403 ? 124.751 159.210 137.740 1.00 32.16 ?  403 ILE B O     1 
ATOM   8818  C  CB    . ILE B 1 403 ? 127.599 158.562 136.722 1.00 23.85 ?  403 ILE B CB    1 
ATOM   8819  C  CG1   . ILE B 1 403 ? 128.664 158.336 135.646 1.00 26.86 ?  403 ILE B CG1   1 
ATOM   8820  C  CG2   . ILE B 1 403 ? 127.978 157.876 138.015 1.00 23.30 ?  403 ILE B CG2   1 
ATOM   8821  C  CD1   . ILE B 1 403 ? 128.711 156.925 135.121 1.00 31.86 ?  403 ILE B CD1   1 
ATOM   8822  N  N     . GLY B 1 404 ? 124.798 156.962 137.841 1.00 26.12 ?  404 GLY B N     1 
ATOM   8823  C  CA    . GLY B 1 404 ? 123.872 156.832 138.946 1.00 14.51 ?  404 GLY B CA    1 
ATOM   8824  C  C     . GLY B 1 404 ? 124.579 156.580 140.261 1.00 21.90 ?  404 GLY B C     1 
ATOM   8825  O  O     . GLY B 1 404 ? 125.709 157.028 140.483 1.00 34.25 ?  404 GLY B O     1 
ATOM   8826  N  N     . LEU B 1 405 ? 123.906 155.853 141.148 1.00 25.58 ?  405 LEU B N     1 
ATOM   8827  C  CA    . LEU B 1 405 ? 124.442 155.516 142.461 1.00 9.14  ?  405 LEU B CA    1 
ATOM   8828  C  C     . LEU B 1 405 ? 124.491 154.003 142.604 1.00 12.56 ?  405 LEU B C     1 
ATOM   8829  O  O     . LEU B 1 405 ? 123.452 153.339 142.555 1.00 20.84 ?  405 LEU B O     1 
ATOM   8830  C  CB    . LEU B 1 405 ? 123.593 156.129 143.576 1.00 19.52 ?  405 LEU B CB    1 
ATOM   8831  C  CG    . LEU B 1 405 ? 123.443 157.650 143.579 1.00 17.62 ?  405 LEU B CG    1 
ATOM   8832  C  CD1   . LEU B 1 405 ? 122.466 158.083 144.654 1.00 25.45 ?  405 LEU B CD1   1 
ATOM   8833  C  CD2   . LEU B 1 405 ? 124.788 158.323 143.774 1.00 19.08 ?  405 LEU B CD2   1 
ATOM   8834  N  N     . ASP B 1 406 ? 125.692 153.465 142.792 1.00 24.10 ?  406 ASP B N     1 
ATOM   8835  C  CA    . ASP B 1 406 ? 125.891 152.049 143.060 1.00 12.26 ?  406 ASP B CA    1 
ATOM   8836  C  C     . ASP B 1 406 ? 126.411 151.875 144.480 1.00 23.28 ?  406 ASP B C     1 
ATOM   8837  O  O     . ASP B 1 406 ? 127.327 152.581 144.908 1.00 34.31 ?  406 ASP B O     1 
ATOM   8838  C  CB    . ASP B 1 406 ? 126.866 151.424 142.062 1.00 18.39 ?  406 ASP B CB    1 
ATOM   8839  C  CG    . ASP B 1 406 ? 126.227 151.146 140.717 1.00 35.02 ?  406 ASP B CG    1 
ATOM   8840  O  OD1   . ASP B 1 406 ? 124.999 151.326 140.585 1.00 37.66 ?  406 ASP B OD1   1 
ATOM   8841  O  OD2   . ASP B 1 406 ? 126.958 150.744 139.787 1.00 32.49 -1 406 ASP B OD2   1 
ATOM   8842  N  N     . ILE B 1 407 ? 125.837 150.921 145.196 1.00 30.17 ?  407 ILE B N     1 
ATOM   8843  C  CA    . ILE B 1 407 ? 126.034 150.817 146.636 1.00 17.45 ?  407 ILE B CA    1 
ATOM   8844  C  C     . ILE B 1 407 ? 127.388 150.194 146.946 1.00 16.83 ?  407 ILE B C     1 
ATOM   8845  O  O     . ILE B 1 407 ? 127.818 149.233 146.297 1.00 24.89 ?  407 ILE B O     1 
ATOM   8846  C  CB    . ILE B 1 407 ? 124.891 150.007 147.271 1.00 10.96 ?  407 ILE B CB    1 
ATOM   8847  C  CG1   . ILE B 1 407 ? 123.540 150.635 146.937 1.00 4.34  ?  407 ILE B CG1   1 
ATOM   8848  C  CG2   . ILE B 1 407 ? 125.070 149.922 148.758 1.00 16.64 ?  407 ILE B CG2   1 
ATOM   8849  C  CD1   . ILE B 1 407 ? 122.473 149.621 146.647 1.00 18.14 ?  407 ILE B CD1   1 
ATOM   8850  N  N     . SER B 1 408 ? 128.063 150.753 147.947 1.00 28.19 ?  408 SER B N     1 
ATOM   8851  C  CA    . SER B 1 408 ? 129.288 150.174 148.493 1.00 25.83 ?  408 SER B CA    1 
ATOM   8852  C  C     . SER B 1 408 ? 129.499 150.768 149.875 1.00 27.97 ?  408 SER B C     1 
ATOM   8853  O  O     . SER B 1 408 ? 129.748 151.972 149.993 1.00 38.52 ?  408 SER B O     1 
ATOM   8854  C  CB    . SER B 1 408 ? 130.485 150.460 147.590 1.00 30.99 ?  408 SER B CB    1 
ATOM   8855  O  OG    . SER B 1 408 ? 131.161 151.637 147.998 1.00 34.38 ?  408 SER B OG    1 
ATOM   8856  N  N     . CYS B 1 409 ? 129.400 149.944 150.913 1.00 21.98 ?  409 CYS B N     1 
ATOM   8857  C  CA    . CYS B 1 409 ? 129.523 150.423 152.280 1.00 31.49 ?  409 CYS B CA    1 
ATOM   8858  C  C     . CYS B 1 409 ? 130.692 149.740 152.978 1.00 26.72 ?  409 CYS B C     1 
ATOM   8859  O  O     . CYS B 1 409 ? 131.107 148.636 152.618 1.00 25.56 ?  409 CYS B O     1 
ATOM   8860  C  CB    . CYS B 1 409 ? 128.223 150.206 153.071 1.00 27.84 ?  409 CYS B CB    1 
ATOM   8861  S  SG    . CYS B 1 409 ? 128.103 148.660 153.985 1.00 38.82 ?  409 CYS B SG    1 
ATOM   8862  N  N     . ASN B 1 410 ? 131.222 150.425 153.985 1.00 22.62 ?  410 ASN B N     1 
ATOM   8863  C  CA    . ASN B 1 410 ? 132.402 149.986 154.715 1.00 22.90 ?  410 ASN B CA    1 
ATOM   8864  C  C     . ASN B 1 410 ? 131.966 149.267 155.982 1.00 24.05 ?  410 ASN B C     1 
ATOM   8865  O  O     . ASN B 1 410 ? 131.078 149.742 156.695 1.00 31.21 ?  410 ASN B O     1 
ATOM   8866  C  CB    . ASN B 1 410 ? 133.293 151.181 155.050 1.00 28.30 ?  410 ASN B CB    1 
ATOM   8867  C  CG    . ASN B 1 410 ? 133.238 152.255 153.983 1.00 37.57 ?  410 ASN B CG    1 
ATOM   8868  O  OD1   . ASN B 1 410 ? 134.201 152.460 153.248 1.00 42.49 ?  410 ASN B OD1   1 
ATOM   8869  N  ND2   . ASN B 1 410 ? 132.119 152.963 153.911 1.00 31.73 ?  410 ASN B ND2   1 
ATOM   8870  N  N     . LEU B 1 411 ? 132.596 148.132 156.263 1.00 16.74 ?  411 LEU B N     1 
ATOM   8871  C  CA    . LEU B 1 411 ? 132.141 147.224 157.305 1.00 9.81  ?  411 LEU B CA    1 
ATOM   8872  C  C     . LEU B 1 411 ? 133.007 147.329 158.553 1.00 13.17 ?  411 LEU B C     1 
ATOM   8873  O  O     . LEU B 1 411 ? 134.228 147.482 158.469 1.00 24.64 ?  411 LEU B O     1 
ATOM   8874  C  CB    . LEU B 1 411 ? 132.148 145.781 156.800 1.00 20.83 ?  411 LEU B CB    1 
ATOM   8875  C  CG    . LEU B 1 411 ? 131.319 145.457 155.561 1.00 19.90 ?  411 LEU B CG    1 
ATOM   8876  C  CD1   . LEU B 1 411 ? 131.054 143.973 155.495 1.00 25.47 ?  411 LEU B CD1   1 
ATOM   8877  C  CD2   . LEU B 1 411 ? 130.012 146.212 155.604 1.00 18.66 ?  411 LEU B CD2   1 
ATOM   8878  N  N     . GLY B 1 412 ? 132.353 147.256 159.707 1.00 18.40 ?  412 GLY B N     1 
ATOM   8879  C  CA    . GLY B 1 412 ? 133.037 147.133 160.979 1.00 4.64  ?  412 GLY B CA    1 
ATOM   8880  C  C     . GLY B 1 412 ? 132.114 146.443 161.956 1.00 11.43 ?  412 GLY B C     1 
ATOM   8881  O  O     . GLY B 1 412 ? 130.888 146.501 161.824 1.00 29.68 ?  412 GLY B O     1 
ATOM   8882  N  N     . SER B 1 413 ? 132.710 145.781 162.943 1.00 13.53 ?  413 SER B N     1 
ATOM   8883  C  CA    . SER B 1 413 ? 131.944 144.980 163.888 1.00 14.25 ?  413 SER B CA    1 
ATOM   8884  C  C     . SER B 1 413 ? 132.320 145.329 165.318 1.00 15.86 ?  413 SER B C     1 
ATOM   8885  O  O     . SER B 1 413 ? 133.499 145.302 165.679 1.00 23.31 ?  413 SER B O     1 
ATOM   8886  C  CB    . SER B 1 413 ? 132.161 143.485 163.649 1.00 10.59 ?  413 SER B CB    1 
ATOM   8887  O  OG    . SER B 1 413 ? 131.467 143.060 162.494 1.00 30.53 ?  413 SER B OG    1 
ATOM   8888  N  N     . LEU B 1 414 ? 131.314 145.653 166.122 1.00 17.46 ?  414 LEU B N     1 
ATOM   8889  C  CA    . LEU B 1 414 ? 131.503 145.722 167.562 1.00 9.58  ?  414 LEU B CA    1 
ATOM   8890  C  C     . LEU B 1 414 ? 131.537 144.318 168.143 1.00 20.99 ?  414 LEU B C     1 
ATOM   8891  O  O     . LEU B 1 414 ? 130.761 143.446 167.746 1.00 27.41 ?  414 LEU B O     1 
ATOM   8892  C  CB    . LEU B 1 414 ? 130.376 146.517 168.217 1.00 19.06 ?  414 LEU B CB    1 
ATOM   8893  C  CG    . LEU B 1 414 ? 129.967 147.852 167.601 1.00 20.59 ?  414 LEU B CG    1 
ATOM   8894  C  CD1   . LEU B 1 414 ? 128.705 148.353 168.269 1.00 23.38 ?  414 LEU B CD1   1 
ATOM   8895  C  CD2   . LEU B 1 414 ? 131.082 148.866 167.738 1.00 25.08 ?  414 LEU B CD2   1 
ATOM   8896  N  N     . ASN B 1 415 ? 132.445 144.098 169.084 1.00 30.18 ?  415 ASN B N     1 
ATOM   8897  C  CA    . ASN B 1 415 ? 132.446 142.875 169.876 1.00 26.52 ?  415 ASN B CA    1 
ATOM   8898  C  C     . ASN B 1 415 ? 131.511 143.101 171.058 1.00 24.97 ?  415 ASN B C     1 
ATOM   8899  O  O     . ASN B 1 415 ? 131.839 143.852 171.980 1.00 29.48 ?  415 ASN B O     1 
ATOM   8900  C  CB    . ASN B 1 415 ? 133.857 142.527 170.333 1.00 21.57 ?  415 ASN B CB    1 
ATOM   8901  C  CG    . ASN B 1 415 ? 133.985 141.095 170.801 1.00 21.47 ?  415 ASN B CG    1 
ATOM   8902  O  OD1   . ASN B 1 415 ? 133.212 140.630 171.636 1.00 37.85 ?  415 ASN B OD1   1 
ATOM   8903  N  ND2   . ASN B 1 415 ? 134.969 140.385 170.266 1.00 29.64 ?  415 ASN B ND2   1 
ATOM   8904  N  N     . ILE B 1 416 ? 130.342 142.458 171.020 1.00 17.78 ?  416 ILE B N     1 
ATOM   8905  C  CA    . ILE B 1 416 ? 129.313 142.716 172.024 1.00 21.17 ?  416 ILE B CA    1 
ATOM   8906  C  C     . ILE B 1 416 ? 129.812 142.341 173.414 1.00 28.90 ?  416 ILE B C     1 
ATOM   8907  O  O     . ILE B 1 416 ? 129.545 143.045 174.393 1.00 27.87 ?  416 ILE B O     1 
ATOM   8908  C  CB    . ILE B 1 416 ? 128.015 141.972 171.658 1.00 27.96 ?  416 ILE B CB    1 
ATOM   8909  C  CG1   . ILE B 1 416 ? 127.385 142.595 170.412 1.00 20.31 ?  416 ILE B CG1   1 
ATOM   8910  C  CG2   . ILE B 1 416 ? 127.027 142.001 172.808 1.00 9.74  ?  416 ILE B CG2   1 
ATOM   8911  C  CD1   . ILE B 1 416 ? 126.192 141.840 169.883 1.00 15.27 ?  416 ILE B CD1   1 
ATOM   8912  N  N     . LEU B 1 417 ? 130.558 141.240 173.521 1.00 21.36 ?  417 LEU B N     1 
ATOM   8913  C  CA    . LEU B 1 417 ? 131.079 140.824 174.819 1.00 26.32 ?  417 LEU B CA    1 
ATOM   8914  C  C     . LEU B 1 417 ? 132.062 141.848 175.377 1.00 30.42 ?  417 LEU B C     1 
ATOM   8915  O  O     . LEU B 1 417 ? 131.963 142.251 176.542 1.00 38.35 ?  417 LEU B O     1 
ATOM   8916  C  CB    . LEU B 1 417 ? 131.742 139.453 174.701 1.00 29.69 ?  417 LEU B CB    1 
ATOM   8917  C  CG    . LEU B 1 417 ? 132.536 138.961 175.912 1.00 30.91 ?  417 LEU B CG    1 
ATOM   8918  C  CD1   . LEU B 1 417 ? 131.620 138.311 176.930 1.00 28.98 ?  417 LEU B CD1   1 
ATOM   8919  C  CD2   . LEU B 1 417 ? 133.625 137.998 175.479 1.00 35.30 ?  417 LEU B CD2   1 
ATOM   8920  N  N     . ASN B 1 418 ? 133.015 142.291 174.555 1.00 30.35 ?  418 ASN B N     1 
ATOM   8921  C  CA    . ASN B 1 418 ? 134.029 143.227 175.023 1.00 27.79 ?  418 ASN B CA    1 
ATOM   8922  C  C     . ASN B 1 418 ? 133.476 144.633 175.208 1.00 29.87 ?  418 ASN B C     1 
ATOM   8923  O  O     . ASN B 1 418 ? 133.897 145.343 176.128 1.00 34.48 ?  418 ASN B O     1 
ATOM   8924  C  CB    . ASN B 1 418 ? 135.209 143.249 174.053 1.00 25.73 ?  418 ASN B CB    1 
ATOM   8925  C  CG    . ASN B 1 418 ? 136.021 141.974 174.102 1.00 26.42 ?  418 ASN B CG    1 
ATOM   8926  O  OD1   . ASN B 1 418 ? 136.175 141.366 175.160 1.00 34.90 ?  418 ASN B OD1   1 
ATOM   8927  N  ND2   . ASN B 1 418 ? 136.540 141.556 172.957 1.00 30.58 ?  418 ASN B ND2   1 
ATOM   8928  N  N     . VAL B 1 419 ? 132.547 145.053 174.349 1.00 32.67 ?  419 VAL B N     1 
ATOM   8929  C  CA    . VAL B 1 419 ? 131.901 146.347 174.527 1.00 31.64 ?  419 VAL B CA    1 
ATOM   8930  C  C     . VAL B 1 419 ? 131.050 146.345 175.789 1.00 30.72 ?  419 VAL B C     1 
ATOM   8931  O  O     . VAL B 1 419 ? 130.992 147.340 176.522 1.00 33.42 ?  419 VAL B O     1 
ATOM   8932  C  CB    . VAL B 1 419 ? 131.071 146.695 173.276 1.00 28.04 ?  419 VAL B CB    1 
ATOM   8933  C  CG1   . VAL B 1 419 ? 130.070 147.787 173.577 1.00 33.19 ?  419 VAL B CG1   1 
ATOM   8934  C  CG2   . VAL B 1 419 ? 131.984 147.109 172.139 1.00 24.47 ?  419 VAL B CG2   1 
ATOM   8935  N  N     . MET B 1 420 ? 130.395 145.221 176.076 1.00 36.25 ?  420 MET B N     1 
ATOM   8936  C  CA    . MET B 1 420 ? 129.523 145.136 177.239 1.00 33.76 ?  420 MET B CA    1 
ATOM   8937  C  C     . MET B 1 420 ? 130.329 145.060 178.529 1.00 31.81 ?  420 MET B C     1 
ATOM   8938  O  O     . MET B 1 420 ? 129.951 145.660 179.541 1.00 34.69 ?  420 MET B O     1 
ATOM   8939  C  CB    . MET B 1 420 ? 128.605 143.922 177.101 1.00 33.22 ?  420 MET B CB    1 
ATOM   8940  C  CG    . MET B 1 420 ? 127.229 144.234 176.535 1.00 24.56 ?  420 MET B CG    1 
ATOM   8941  S  SD    . MET B 1 420 ? 126.648 145.890 176.923 1.00 41.26 ?  420 MET B SD    1 
ATOM   8942  C  CE    . MET B 1 420 ? 125.872 145.593 178.503 1.00 33.19 ?  420 MET B CE    1 
ATOM   8943  N  N     . GLU B 1 421 ? 131.448 144.327 178.513 1.00 39.01 ?  421 GLU B N     1 
ATOM   8944  C  CA    . GLU B 1 421 ? 132.277 144.219 179.708 1.00 38.31 ?  421 GLU B CA    1 
ATOM   8945  C  C     . GLU B 1 421 ? 133.011 145.521 180.008 1.00 36.84 ?  421 GLU B C     1 
ATOM   8946  O  O     . GLU B 1 421 ? 133.299 145.812 181.174 1.00 39.33 ?  421 GLU B O     1 
ATOM   8947  C  CB    . GLU B 1 421 ? 133.265 143.058 179.560 1.00 33.75 ?  421 GLU B CB    1 
ATOM   8948  C  CG    . GLU B 1 421 ? 134.552 143.407 178.830 1.00 38.99 ?  421 GLU B CG    1 
ATOM   8949  C  CD    . GLU B 1 421 ? 135.601 142.317 178.927 1.00 46.20 ?  421 GLU B CD    1 
ATOM   8950  O  OE1   . GLU B 1 421 ? 136.366 142.310 179.914 1.00 43.21 ?  421 GLU B OE1   1 
ATOM   8951  O  OE2   . GLU B 1 421 ? 135.661 141.468 178.014 1.00 43.32 -1 421 GLU B OE2   1 
ATOM   8952  N  N     . HIS B 1 422 ? 133.322 146.312 178.982 1.00 36.68 ?  422 HIS B N     1 
ATOM   8953  C  CA    . HIS B 1 422 ? 133.970 147.601 179.172 1.00 37.50 ?  422 HIS B CA    1 
ATOM   8954  C  C     . HIS B 1 422 ? 132.983 148.730 179.426 1.00 41.79 ?  422 HIS B C     1 
ATOM   8955  O  O     . HIS B 1 422 ? 133.414 149.846 179.736 1.00 45.27 ?  422 HIS B O     1 
ATOM   8956  C  CB    . HIS B 1 422 ? 134.831 147.953 177.954 1.00 35.17 ?  422 HIS B CB    1 
ATOM   8957  C  CG    . HIS B 1 422 ? 136.184 147.313 177.959 1.00 38.00 ?  422 HIS B CG    1 
ATOM   8958  N  ND1   . HIS B 1 422 ? 136.364 145.953 177.838 1.00 39.87 ?  422 HIS B ND1   1 
ATOM   8959  C  CD2   . HIS B 1 422 ? 137.422 147.848 178.067 1.00 40.59 ?  422 HIS B CD2   1 
ATOM   8960  C  CE1   . HIS B 1 422 ? 137.655 145.676 177.873 1.00 41.07 ?  422 HIS B CE1   1 
ATOM   8961  N  NE2   . HIS B 1 422 ? 138.319 146.809 178.012 1.00 42.75 ?  422 HIS B NE2   1 
ATOM   8962  N  N     . LYS B 1 423 ? 131.679 148.466 179.306 1.00 43.51 ?  423 LYS B N     1 
ATOM   8963  C  CA    . LYS B 1 423 ? 130.642 149.480 179.491 1.00 44.04 ?  423 LYS B CA    1 
ATOM   8964  C  C     . LYS B 1 423 ? 130.881 150.680 178.579 1.00 47.14 ?  423 LYS B C     1 
ATOM   8965  O  O     . LYS B 1 423 ? 130.722 151.835 178.978 1.00 48.45 ?  423 LYS B O     1 
ATOM   8966  C  CB    . LYS B 1 423 ? 130.552 149.915 180.955 1.00 43.16 ?  423 LYS B CB    1 
ATOM   8967  C  CG    . LYS B 1 423 ? 129.923 148.884 181.873 1.00 44.78 ?  423 LYS B CG    1 
ATOM   8968  C  CD    . LYS B 1 423 ? 130.906 148.431 182.940 1.00 48.99 ?  423 LYS B CD    1 
ATOM   8969  C  CE    . LYS B 1 423 ? 130.390 147.211 183.687 1.00 47.55 ?  423 LYS B CE    1 
ATOM   8970  N  NZ    . LYS B 1 423 ? 130.857 145.938 183.071 1.00 42.92 1  423 LYS B NZ    1 
ATOM   8971  N  N     . SER B 1 424 ? 131.260 150.399 177.337 1.00 32.45 ?  424 SER B N     1 
ATOM   8972  C  CA    . SER B 1 424 ? 131.690 151.420 176.389 1.00 32.35 ?  424 SER B CA    1 
ATOM   8973  C  C     . SER B 1 424 ? 130.927 151.297 175.078 1.00 36.47 ?  424 SER B C     1 
ATOM   8974  O  O     . SER B 1 424 ? 131.513 151.270 173.995 1.00 38.35 ?  424 SER B O     1 
ATOM   8975  C  CB    . SER B 1 424 ? 133.192 151.327 176.142 1.00 36.99 ?  424 SER B CB    1 
ATOM   8976  O  OG    . SER B 1 424 ? 133.519 150.149 175.427 1.00 34.67 ?  424 SER B OG    1 
ATOM   8977  N  N     . ILE B 1 425 ? 129.599 151.211 175.154 1.00 35.88 ?  425 ILE B N     1 
ATOM   8978  C  CA    . ILE B 1 425 ? 128.800 151.195 173.931 1.00 28.36 ?  425 ILE B CA    1 
ATOM   8979  C  C     . ILE B 1 425 ? 128.953 152.513 173.184 1.00 34.18 ?  425 ILE B C     1 
ATOM   8980  O  O     . ILE B 1 425 ? 129.219 152.536 171.978 1.00 39.14 ?  425 ILE B O     1 
ATOM   8981  C  CB    . ILE B 1 425 ? 127.323 150.900 174.249 1.00 33.41 ?  425 ILE B CB    1 
ATOM   8982  C  CG1   . ILE B 1 425 ? 127.151 149.460 174.729 1.00 33.95 ?  425 ILE B CG1   1 
ATOM   8983  C  CG2   . ILE B 1 425 ? 126.458 151.153 173.025 1.00 29.70 ?  425 ILE B CG2   1 
ATOM   8984  C  CD1   . ILE B 1 425 ? 125.717 149.082 175.005 1.00 34.91 ?  425 ILE B CD1   1 
ATOM   8985  N  N     . GLU B 1 426 ? 128.816 153.630 173.900 1.00 32.69 ?  426 GLU B N     1 
ATOM   8986  C  CA    . GLU B 1 426 ? 128.869 154.940 173.257 1.00 31.07 ?  426 GLU B CA    1 
ATOM   8987  C  C     . GLU B 1 426 ? 130.234 155.200 172.632 1.00 31.81 ?  426 GLU B C     1 
ATOM   8988  O  O     . GLU B 1 426 ? 130.332 155.558 171.453 1.00 42.23 ?  426 GLU B O     1 
ATOM   8989  C  CB    . GLU B 1 426 ? 128.526 156.027 174.274 1.00 32.52 ?  426 GLU B CB    1 
ATOM   8990  C  CG    . GLU B 1 426 ? 128.924 157.426 173.850 1.00 33.06 ?  426 GLU B CG    1 
ATOM   8991  C  CD    . GLU B 1 426 ? 128.731 158.440 174.956 1.00 42.02 ?  426 GLU B CD    1 
ATOM   8992  O  OE1   . GLU B 1 426 ? 128.392 158.030 176.085 1.00 42.80 ?  426 GLU B OE1   1 
ATOM   8993  O  OE2   . GLU B 1 426 ? 128.922 159.647 174.701 1.00 46.74 -1 426 GLU B OE2   1 
ATOM   8994  N  N     . LYS B 1 427 ? 131.302 155.021 173.413 1.00 33.13 ?  427 LYS B N     1 
ATOM   8995  C  CA    . LYS B 1 427 ? 132.640 155.338 172.926 1.00 31.12 ?  427 LYS B CA    1 
ATOM   8996  C  C     . LYS B 1 427 ? 133.044 154.420 171.781 1.00 32.71 ?  427 LYS B C     1 
ATOM   8997  O  O     . LYS B 1 427 ? 133.585 154.885 170.770 1.00 37.83 ?  427 LYS B O     1 
ATOM   8998  C  CB    . LYS B 1 427 ? 133.676 155.261 174.059 1.00 34.87 ?  427 LYS B CB    1 
ATOM   8999  C  CG    . LYS B 1 427 ? 133.645 156.383 175.123 1.00 41.24 ?  427 LYS B CG    1 
ATOM   9000  C  CD    . LYS B 1 427 ? 132.377 156.500 175.986 1.00 40.26 ?  427 LYS B CD    1 
ATOM   9001  C  CE    . LYS B 1 427 ? 131.777 155.148 176.364 1.00 36.14 ?  427 LYS B CE    1 
ATOM   9002  N  NZ    . LYS B 1 427 ? 130.655 155.276 177.332 1.00 40.00 1  427 LYS B NZ    1 
ATOM   9003  N  N     . THR B 1 428 ? 132.794 153.117 171.919 1.00 28.98 ?  428 THR B N     1 
ATOM   9004  C  CA    . THR B 1 428 ? 133.136 152.190 170.847 1.00 24.30 ?  428 THR B CA    1 
ATOM   9005  C  C     . THR B 1 428 ? 132.334 152.481 169.588 1.00 26.69 ?  428 THR B C     1 
ATOM   9006  O  O     . THR B 1 428 ? 132.883 152.461 168.482 1.00 34.84 ?  428 THR B O     1 
ATOM   9007  C  CB    . THR B 1 428 ? 132.916 150.744 171.291 1.00 21.44 ?  428 THR B CB    1 
ATOM   9008  O  OG1   . THR B 1 428 ? 133.552 150.527 172.556 1.00 25.87 ?  428 THR B OG1   1 
ATOM   9009  C  CG2   . THR B 1 428 ? 133.496 149.787 170.269 1.00 27.34 ?  428 THR B CG2   1 
ATOM   9010  N  N     . VAL B 1 429 ? 131.037 152.760 169.733 1.00 26.34 ?  429 VAL B N     1 
ATOM   9011  C  CA    . VAL B 1 429 ? 130.209 153.043 168.564 1.00 23.04 ?  429 VAL B CA    1 
ATOM   9012  C  C     . VAL B 1 429 ? 130.698 154.298 167.857 1.00 24.84 ?  429 VAL B C     1 
ATOM   9013  O  O     . VAL B 1 429 ? 130.816 154.327 166.626 1.00 30.08 ?  429 VAL B O     1 
ATOM   9014  C  CB    . VAL B 1 429 ? 128.726 153.159 168.968 1.00 24.85 ?  429 VAL B CB    1 
ATOM   9015  C  CG1   . VAL B 1 429 ? 127.954 153.935 167.924 1.00 23.31 ?  429 VAL B CG1   1 
ATOM   9016  C  CG2   . VAL B 1 429 ? 128.115 151.786 169.139 1.00 26.10 ?  429 VAL B CG2   1 
ATOM   9017  N  N     . LYS B 1 430 ? 131.010 155.349 168.617 1.00 29.56 ?  430 LYS B N     1 
ATOM   9018  C  CA    . LYS B 1 430 ? 131.428 156.600 167.994 1.00 24.43 ?  430 LYS B CA    1 
ATOM   9019  C  C     . LYS B 1 430 ? 132.800 156.473 167.340 1.00 23.08 ?  430 LYS B C     1 
ATOM   9020  O  O     . LYS B 1 430 ? 133.014 156.986 166.235 1.00 31.25 ?  430 LYS B O     1 
ATOM   9021  C  CB    . LYS B 1 430 ? 131.409 157.725 169.026 1.00 26.41 ?  430 LYS B CB    1 
ATOM   9022  C  CG    . LYS B 1 430 ? 130.003 158.080 169.481 1.00 23.26 ?  430 LYS B CG    1 
ATOM   9023  C  CD    . LYS B 1 430 ? 129.963 159.382 170.250 1.00 31.44 ?  430 LYS B CD    1 
ATOM   9024  C  CE    . LYS B 1 430 ? 128.534 159.773 170.573 1.00 34.84 ?  430 LYS B CE    1 
ATOM   9025  N  NZ    . LYS B 1 430 ? 128.467 161.005 171.400 1.00 36.10 1  430 LYS B NZ    1 
ATOM   9026  N  N     . LEU B 1 431 ? 133.741 155.785 167.992 1.00 30.77 ?  431 LEU B N     1 
ATOM   9027  C  CA    . LEU B 1 431 ? 135.055 155.592 167.385 1.00 22.41 ?  431 LEU B CA    1 
ATOM   9028  C  C     . LEU B 1 431 ? 134.970 154.705 166.148 1.00 23.25 ?  431 LEU B C     1 
ATOM   9029  O  O     . LEU B 1 431 ? 135.666 154.948 165.155 1.00 32.08 ?  431 LEU B O     1 
ATOM   9030  C  CB    . LEU B 1 431 ? 136.023 155.003 168.409 1.00 30.91 ?  431 LEU B CB    1 
ATOM   9031  C  CG    . LEU B 1 431 ? 136.879 156.000 169.188 1.00 32.90 ?  431 LEU B CG    1 
ATOM   9032  C  CD1   . LEU B 1 431 ? 137.648 155.292 170.288 1.00 28.93 ?  431 LEU B CD1   1 
ATOM   9033  C  CD2   . LEU B 1 431 ? 137.827 156.735 168.258 1.00 34.52 ?  431 LEU B CD2   1 
ATOM   9034  N  N     . ALA B 1 432 ? 134.131 153.666 166.190 1.00 25.20 ?  432 ALA B N     1 
ATOM   9035  C  CA    . ALA B 1 432 ? 133.928 152.827 165.018 1.00 20.02 ?  432 ALA B CA    1 
ATOM   9036  C  C     . ALA B 1 432 ? 133.300 153.617 163.881 1.00 25.84 ?  432 ALA B C     1 
ATOM   9037  O  O     . ALA B 1 432 ? 133.659 153.430 162.714 1.00 29.63 ?  432 ALA B O     1 
ATOM   9038  C  CB    . ALA B 1 432 ? 133.061 151.623 165.382 1.00 24.13 ?  432 ALA B CB    1 
ATOM   9039  N  N     . THR B 1 433 ? 132.354 154.503 164.202 1.00 27.18 ?  433 THR B N     1 
ATOM   9040  C  CA    . THR B 1 433 ? 131.769 155.370 163.187 1.00 17.25 ?  433 THR B CA    1 
ATOM   9041  C  C     . THR B 1 433 ? 132.824 156.277 162.570 1.00 25.04 ?  433 THR B C     1 
ATOM   9042  O  O     . THR B 1 433 ? 132.848 156.470 161.350 1.00 33.17 ?  433 THR B O     1 
ATOM   9043  C  CB    . THR B 1 433 ? 130.637 156.198 163.799 1.00 24.03 ?  433 THR B CB    1 
ATOM   9044  O  OG1   . THR B 1 433 ? 129.658 155.322 164.367 1.00 32.99 ?  433 THR B OG1   1 
ATOM   9045  C  CG2   . THR B 1 433 ? 129.975 157.069 162.744 1.00 24.11 ?  433 THR B CG2   1 
ATOM   9046  N  N     . ASP B 1 434 ? 133.709 156.837 163.396 1.00 24.94 ?  434 ASP B N     1 
ATOM   9047  C  CA    . ASP B 1 434 ? 134.781 157.681 162.873 1.00 18.95 ?  434 ASP B CA    1 
ATOM   9048  C  C     . ASP B 1 434 ? 135.710 156.894 161.956 1.00 19.23 ?  434 ASP B C     1 
ATOM   9049  O  O     . ASP B 1 434 ? 136.099 157.381 160.886 1.00 26.71 ?  434 ASP B O     1 
ATOM   9050  C  CB    . ASP B 1 434 ? 135.568 158.303 164.025 1.00 25.35 ?  434 ASP B CB    1 
ATOM   9051  C  CG    . ASP B 1 434 ? 134.778 159.352 164.771 1.00 31.05 ?  434 ASP B CG    1 
ATOM   9052  O  OD1   . ASP B 1 434 ? 133.889 159.975 164.156 1.00 36.85 ?  434 ASP B OD1   1 
ATOM   9053  O  OD2   . ASP B 1 434 ? 135.047 159.556 165.972 1.00 33.18 -1 434 ASP B OD2   1 
ATOM   9054  N  N     . SER B 1 435 ? 136.078 155.676 162.357 1.00 22.83 ?  435 SER B N     1 
ATOM   9055  C  CA    . SER B 1 435 ? 136.970 154.862 161.535 1.00 15.90 ?  435 SER B CA    1 
ATOM   9056  C  C     . SER B 1 435 ? 136.310 154.467 160.219 1.00 23.26 ?  435 SER B C     1 
ATOM   9057  O  O     . SER B 1 435 ? 136.951 154.498 159.161 1.00 31.44 ?  435 SER B O     1 
ATOM   9058  C  CB    . SER B 1 435 ? 137.411 153.621 162.311 1.00 21.15 ?  435 SER B CB    1 
ATOM   9059  O  OG    . SER B 1 435 ? 136.333 152.722 162.496 1.00 22.23 ?  435 SER B OG    1 
ATOM   9060  N  N     . LEU B 1 436 ? 135.032 154.090 160.263 1.00 18.81 ?  436 LEU B N     1 
ATOM   9061  C  CA    . LEU B 1 436 ? 134.314 153.743 159.042 1.00 11.47 ?  436 LEU B CA    1 
ATOM   9062  C  C     . LEU B 1 436 ? 134.163 154.953 158.132 1.00 19.15 ?  436 LEU B C     1 
ATOM   9063  O  O     . LEU B 1 436 ? 134.261 154.831 156.906 1.00 31.33 ?  436 LEU B O     1 
ATOM   9064  C  CB    . LEU B 1 436 ? 132.950 153.153 159.390 1.00 22.51 ?  436 LEU B CB    1 
ATOM   9065  C  CG    . LEU B 1 436 ? 132.976 151.767 160.032 1.00 18.95 ?  436 LEU B CG    1 
ATOM   9066  C  CD1   . LEU B 1 436 ? 131.669 151.486 160.744 1.00 16.54 ?  436 LEU B CD1   1 
ATOM   9067  C  CD2   . LEU B 1 436 ? 133.261 150.711 158.988 1.00 20.71 ?  436 LEU B CD2   1 
ATOM   9068  N  N     . THR B 1 437 ? 133.929 156.131 158.713 1.00 22.48 ?  437 THR B N     1 
ATOM   9069  C  CA    . THR B 1 437 ? 133.888 157.354 157.923 1.00 19.89 ?  437 THR B CA    1 
ATOM   9070  C  C     . THR B 1 437 ? 135.226 157.612 157.245 1.00 24.99 ?  437 THR B C     1 
ATOM   9071  O  O     . THR B 1 437 ? 135.269 157.969 156.064 1.00 35.50 ?  437 THR B O     1 
ATOM   9072  C  CB    . THR B 1 437 ? 133.502 158.537 158.810 1.00 15.98 ?  437 THR B CB    1 
ATOM   9073  O  OG1   . THR B 1 437 ? 132.254 158.261 159.454 1.00 16.78 ?  437 THR B OG1   1 
ATOM   9074  C  CG2   . THR B 1 437 ? 133.371 159.802 157.987 1.00 21.42 ?  437 THR B CG2   1 
ATOM   9075  N  N     . HIS B 1 438 ? 136.329 157.434 157.976 1.00 18.58 ?  438 HIS B N     1 
ATOM   9076  C  CA    . HIS B 1 438 ? 137.647 157.619 157.375 1.00 18.73 ?  438 HIS B CA    1 
ATOM   9077  C  C     . HIS B 1 438 ? 137.873 156.641 156.230 1.00 20.69 ?  438 HIS B C     1 
ATOM   9078  O  O     . HIS B 1 438 ? 138.392 157.020 155.172 1.00 32.55 ?  438 HIS B O     1 
ATOM   9079  C  CB    . HIS B 1 438 ? 138.739 157.461 158.432 1.00 25.97 ?  438 HIS B CB    1 
ATOM   9080  C  CG    . HIS B 1 438 ? 140.126 157.506 157.871 1.00 28.78 ?  438 HIS B CG    1 
ATOM   9081  N  ND1   . HIS B 1 438 ? 140.803 158.686 157.653 1.00 26.69 ?  438 HIS B ND1   1 
ATOM   9082  C  CD2   . HIS B 1 438 ? 140.958 156.516 157.469 1.00 30.25 ?  438 HIS B CD2   1 
ATOM   9083  C  CE1   . HIS B 1 438 ? 141.993 158.422 157.148 1.00 27.89 ?  438 HIS B CE1   1 
ATOM   9084  N  NE2   . HIS B 1 438 ? 142.112 157.112 157.025 1.00 30.94 ?  438 HIS B NE2   1 
ATOM   9085  N  N     . VAL B 1 439 ? 137.489 155.378 156.421 1.00 23.92 ?  439 VAL B N     1 
ATOM   9086  C  CA    . VAL B 1 439 ? 137.638 154.389 155.356 1.00 17.52 ?  439 VAL B CA    1 
ATOM   9087  C  C     . VAL B 1 439 ? 136.803 154.783 154.145 1.00 27.55 ?  439 VAL B C     1 
ATOM   9088  O  O     . VAL B 1 439 ? 137.229 154.617 152.996 1.00 34.37 ?  439 VAL B O     1 
ATOM   9089  C  CB    . VAL B 1 439 ? 137.267 152.985 155.872 1.00 22.88 ?  439 VAL B CB    1 
ATOM   9090  C  CG1   . VAL B 1 439 ? 137.241 151.983 154.730 1.00 25.20 ?  439 VAL B CG1   1 
ATOM   9091  C  CG2   . VAL B 1 439 ? 138.240 152.542 156.942 1.00 21.17 ?  439 VAL B CG2   1 
ATOM   9092  N  N     . SER B 1 440 ? 135.601 155.311 154.383 1.00 27.83 ?  440 SER B N     1 
ATOM   9093  C  CA    . SER B 1 440 ? 134.750 155.752 153.282 1.00 17.71 ?  440 SER B CA    1 
ATOM   9094  C  C     . SER B 1 440 ? 135.384 156.906 152.515 1.00 23.44 ?  440 SER B C     1 
ATOM   9095  O  O     . SER B 1 440 ? 135.384 156.911 151.279 1.00 33.92 ?  440 SER B O     1 
ATOM   9096  C  CB    . SER B 1 440 ? 133.375 156.150 153.818 1.00 26.57 ?  440 SER B CB    1 
ATOM   9097  O  OG    . SER B 1 440 ? 132.442 156.318 152.766 1.00 33.83 ?  440 SER B OG    1 
ATOM   9098  N  N     . GLU B 1 441 ? 135.927 157.896 153.228 1.00 24.94 ?  441 GLU B N     1 
ATOM   9099  C  CA    . GLU B 1 441 ? 136.540 159.039 152.551 1.00 20.17 ?  441 GLU B CA    1 
ATOM   9100  C  C     . GLU B 1 441 ? 137.795 158.636 151.787 1.00 29.91 ?  441 GLU B C     1 
ATOM   9101  O  O     . GLU B 1 441 ? 138.042 159.139 150.686 1.00 41.35 ?  441 GLU B O     1 
ATOM   9102  C  CB    . GLU B 1 441 ? 136.864 160.161 153.538 1.00 22.01 ?  441 GLU B CB    1 
ATOM   9103  C  CG    . GLU B 1 441 ? 135.798 160.453 154.572 1.00 30.91 ?  441 GLU B CG    1 
ATOM   9104  C  CD    . GLU B 1 441 ? 134.511 160.973 153.963 1.00 42.82 ?  441 GLU B CD    1 
ATOM   9105  O  OE1   . GLU B 1 441 ? 134.433 162.186 153.681 1.00 39.73 ?  441 GLU B OE1   1 
ATOM   9106  O  OE2   . GLU B 1 441 ? 133.575 160.170 153.769 1.00 47.27 -1 441 GLU B OE2   1 
ATOM   9107  N  N     . THR B 1 442 ? 138.602 157.739 152.349 1.00 32.89 ?  442 THR B N     1 
ATOM   9108  C  CA    . THR B 1 442 ? 139.862 157.382 151.710 1.00 29.78 ?  442 THR B CA    1 
ATOM   9109  C  C     . THR B 1 442 ? 139.698 156.358 150.595 1.00 29.77 ?  442 THR B C     1 
ATOM   9110  O  O     . THR B 1 442 ? 140.693 156.001 149.955 1.00 38.02 ?  442 THR B O     1 
ATOM   9111  C  CB    . THR B 1 442 ? 140.856 156.853 152.749 1.00 31.77 ?  442 THR B CB    1 
ATOM   9112  O  OG1   . THR B 1 442 ? 140.326 155.677 153.370 1.00 38.47 ?  442 THR B OG1   1 
ATOM   9113  C  CG2   . THR B 1 442 ? 141.126 157.908 153.806 1.00 28.66 ?  442 THR B CG2   1 
ATOM   9114  N  N     . THR B 1 443 ? 138.484 155.883 150.343 1.00 33.92 ?  443 THR B N     1 
ATOM   9115  C  CA    . THR B 1 443 ? 138.233 154.925 149.276 1.00 37.93 ?  443 THR B CA    1 
ATOM   9116  C  C     . THR B 1 443 ? 137.921 155.675 147.987 1.00 38.05 ?  443 THR B C     1 
ATOM   9117  O  O     . THR B 1 443 ? 136.984 156.478 147.941 1.00 39.87 ?  443 THR B O     1 
ATOM   9118  C  CB    . THR B 1 443 ? 137.080 153.991 149.641 1.00 36.18 ?  443 THR B CB    1 
ATOM   9119  O  OG1   . THR B 1 443 ? 137.396 153.288 150.848 1.00 40.97 ?  443 THR B OG1   1 
ATOM   9120  C  CG2   . THR B 1 443 ? 136.843 152.987 148.527 1.00 29.03 ?  443 THR B CG2   1 
ATOM   9121  N  N     . ASP B 1 444 ? 138.706 155.411 146.945 1.00 46.08 ?  444 ASP B N     1 
ATOM   9122  C  CA    . ASP B 1 444 ? 138.474 155.984 145.621 1.00 44.30 ?  444 ASP B CA    1 
ATOM   9123  C  C     . ASP B 1 444 ? 138.668 154.878 144.596 1.00 47.74 ?  444 ASP B C     1 
ATOM   9124  O  O     . ASP B 1 444 ? 139.777 154.354 144.449 1.00 49.21 ?  444 ASP B O     1 
ATOM   9125  C  CB    . ASP B 1 444 ? 139.412 157.160 145.348 1.00 47.29 ?  444 ASP B CB    1 
ATOM   9126  C  CG    . ASP B 1 444 ? 138.813 158.170 144.390 1.00 51.21 ?  444 ASP B CG    1 
ATOM   9127  O  OD1   . ASP B 1 444 ? 137.697 158.658 144.661 1.00 48.14 ?  444 ASP B OD1   1 
ATOM   9128  O  OD2   . ASP B 1 444 ? 139.460 158.479 143.367 1.00 52.79 -1 444 ASP B OD2   1 
ATOM   9129  N  N     . ILE B 1 445 ? 137.598 154.522 143.892 1.00 38.65 ?  445 ILE B N     1 
ATOM   9130  C  CA    . ILE B 1 445 ? 137.620 153.443 142.914 1.00 40.61 ?  445 ILE B CA    1 
ATOM   9131  C  C     . ILE B 1 445 ? 137.520 154.067 141.529 1.00 45.93 ?  445 ILE B C     1 
ATOM   9132  O  O     . ILE B 1 445 ? 136.555 154.778 141.225 1.00 48.01 ?  445 ILE B O     1 
ATOM   9133  C  CB    . ILE B 1 445 ? 136.487 152.437 143.168 1.00 38.89 ?  445 ILE B CB    1 
ATOM   9134  C  CG1   . ILE B 1 445 ? 136.932 151.410 144.208 1.00 38.21 ?  445 ILE B CG1   1 
ATOM   9135  C  CG2   . ILE B 1 445 ? 136.110 151.719 141.888 1.00 41.28 ?  445 ILE B CG2   1 
ATOM   9136  C  CD1   . ILE B 1 445 ? 135.826 150.948 145.114 1.00 37.47 ?  445 ILE B CD1   1 
ATOM   9137  N  N     . ARG B 1 446 ? 138.523 153.809 140.692 1.00 46.10 ?  446 ARG B N     1 
ATOM   9138  C  CA    . ARG B 1 446 ? 138.696 154.541 139.446 1.00 46.88 ?  446 ARG B CA    1 
ATOM   9139  C  C     . ARG B 1 446 ? 137.987 153.908 138.257 1.00 48.00 ?  446 ARG B C     1 
ATOM   9140  O  O     . ARG B 1 446 ? 137.967 154.511 137.179 1.00 43.19 ?  446 ARG B O     1 
ATOM   9141  C  CB    . ARG B 1 446 ? 140.189 154.683 139.126 1.00 43.09 ?  446 ARG B CB    1 
ATOM   9142  C  CG    . ARG B 1 446 ? 141.084 154.828 140.351 1.00 41.76 ?  446 ARG B CG    1 
ATOM   9143  C  CD    . ARG B 1 446 ? 140.838 156.088 141.196 1.00 46.98 ?  446 ARG B CD    1 
ATOM   9144  N  NE    . ARG B 1 446 ? 141.071 157.343 140.486 1.00 48.53 ?  446 ARG B NE    1 
ATOM   9145  C  CZ    . ARG B 1 446 ? 140.156 158.027 139.809 1.00 49.20 ?  446 ARG B CZ    1 
ATOM   9146  N  NH1   . ARG B 1 446 ? 138.890 157.648 139.778 1.00 45.47 1  446 ARG B NH1   1 
ATOM   9147  N  NH2   . ARG B 1 446 ? 140.518 159.136 139.171 1.00 41.80 ?  446 ARG B NH2   1 
ATOM   9148  N  N     . ASN B 1 447 ? 137.405 152.721 138.415 1.00 37.86 ?  447 ASN B N     1 
ATOM   9149  C  CA    . ASN B 1 447 ? 136.768 152.034 137.302 1.00 30.21 ?  447 ASN B CA    1 
ATOM   9150  C  C     . ASN B 1 447 ? 135.297 151.730 137.536 1.00 33.78 ?  447 ASN B C     1 
ATOM   9151  O  O     . ASN B 1 447 ? 134.678 151.063 136.700 1.00 41.74 ?  447 ASN B O     1 
ATOM   9152  C  CB    . ASN B 1 447 ? 137.517 150.736 136.981 1.00 35.06 ?  447 ASN B CB    1 
ATOM   9153  C  CG    . ASN B 1 447 ? 138.616 150.941 135.961 1.00 33.26 ?  447 ASN B CG    1 
ATOM   9154  O  OD1   . ASN B 1 447 ? 138.349 151.144 134.779 1.00 39.91 ?  447 ASN B OD1   1 
ATOM   9155  N  ND2   . ASN B 1 447 ? 139.861 150.893 136.417 1.00 29.19 ?  447 ASN B ND2   1 
ATOM   9156  N  N     . ALA B 1 448 ? 134.721 152.192 138.644 1.00 35.20 ?  448 ALA B N     1 
ATOM   9157  C  CA    . ALA B 1 448 ? 133.292 152.074 138.922 1.00 30.98 ?  448 ALA B CA    1 
ATOM   9158  C  C     . ALA B 1 448 ? 132.776 153.476 139.210 1.00 34.36 ?  448 ALA B C     1 
ATOM   9159  O  O     . ALA B 1 448 ? 132.756 153.913 140.370 1.00 35.04 ?  448 ALA B O     1 
ATOM   9160  C  CB    . ALA B 1 448 ? 133.027 151.129 140.090 1.00 26.58 ?  448 ALA B CB    1 
ATOM   9161  N  N     . PRO B 1 449 ? 132.366 154.224 138.181 1.00 32.91 ?  449 PRO B N     1 
ATOM   9162  C  CA    . PRO B 1 449 ? 131.983 155.626 138.417 1.00 25.26 ?  449 PRO B CA    1 
ATOM   9163  C  C     . PRO B 1 449 ? 130.775 155.773 139.321 1.00 30.13 ?  449 PRO B C     1 
ATOM   9164  O  O     . PRO B 1 449 ? 130.725 156.707 140.129 1.00 29.44 ?  449 PRO B O     1 
ATOM   9165  C  CB    . PRO B 1 449 ? 131.709 156.168 137.006 1.00 27.13 ?  449 PRO B CB    1 
ATOM   9166  C  CG    . PRO B 1 449 ? 131.894 155.022 136.062 1.00 30.35 ?  449 PRO B CG    1 
ATOM   9167  C  CD    . PRO B 1 449 ? 132.003 153.760 136.834 1.00 24.54 ?  449 PRO B CD    1 
ATOM   9168  N  N     . ALA B 1 450 ? 129.797 154.871 139.210 1.00 32.95 ?  450 ALA B N     1 
ATOM   9169  C  CA    . ALA B 1 450 ? 128.618 154.957 140.064 1.00 19.72 ?  450 ALA B CA    1 
ATOM   9170  C  C     . ALA B 1 450 ? 128.955 154.603 141.505 1.00 27.50 ?  450 ALA B C     1 
ATOM   9171  O  O     . ALA B 1 450 ? 128.445 155.231 142.439 1.00 33.23 ?  450 ALA B O     1 
ATOM   9172  C  CB    . ALA B 1 450 ? 127.515 154.050 139.525 1.00 23.31 ?  450 ALA B CB    1 
ATOM   9173  N  N     . VAL B 1 451 ? 129.824 153.610 141.706 1.00 29.00 ?  451 VAL B N     1 
ATOM   9174  C  CA    . VAL B 1 451 ? 130.255 153.256 143.056 1.00 19.78 ?  451 VAL B CA    1 
ATOM   9175  C  C     . VAL B 1 451 ? 130.987 154.426 143.698 1.00 24.03 ?  451 VAL B C     1 
ATOM   9176  O  O     . VAL B 1 451 ? 130.743 154.772 144.859 1.00 36.06 ?  451 VAL B O     1 
ATOM   9177  C  CB    . VAL B 1 451 ? 131.132 151.991 143.026 1.00 28.00 ?  451 VAL B CB    1 
ATOM   9178  C  CG1   . VAL B 1 451 ? 131.938 151.867 144.306 1.00 28.64 ?  451 VAL B CG1   1 
ATOM   9179  C  CG2   . VAL B 1 451 ? 130.282 150.757 142.811 1.00 23.50 ?  451 VAL B CG2   1 
ATOM   9180  N  N     . ARG B 1 452 ? 131.894 155.054 142.949 1.00 25.98 ?  452 ARG B N     1 
ATOM   9181  C  CA    . ARG B 1 452 ? 132.637 156.195 143.475 1.00 23.15 ?  452 ARG B CA    1 
ATOM   9182  C  C     . ARG B 1 452 ? 131.714 157.371 143.772 1.00 22.13 ?  452 ARG B C     1 
ATOM   9183  O  O     . ARG B 1 452 ? 131.840 158.024 144.817 1.00 36.39 ?  452 ARG B O     1 
ATOM   9184  C  CB    . ARG B 1 452 ? 133.732 156.594 142.486 1.00 23.46 ?  452 ARG B CB    1 
ATOM   9185  C  CG    . ARG B 1 452 ? 134.568 157.785 142.911 1.00 31.33 ?  452 ARG B CG    1 
ATOM   9186  C  CD    . ARG B 1 452 ? 134.905 158.668 141.721 1.00 29.52 ?  452 ARG B CD    1 
ATOM   9187  N  NE    . ARG B 1 452 ? 133.891 158.580 140.678 1.00 41.86 ?  452 ARG B NE    1 
ATOM   9188  C  CZ    . ARG B 1 452 ? 132.861 159.407 140.557 1.00 41.89 ?  452 ARG B CZ    1 
ATOM   9189  N  NH1   . ARG B 1 452 ? 132.681 160.415 141.394 1.00 34.62 1  452 ARG B NH1   1 
ATOM   9190  N  NH2   . ARG B 1 452 ? 131.988 159.216 139.572 1.00 28.38 ?  452 ARG B NH2   1 
ATOM   9191  N  N     . ARG B 1 453 ? 130.771 157.653 142.869 1.00 23.37 ?  453 ARG B N     1 
ATOM   9192  C  CA    . ARG B 1 453 ? 129.840 158.753 143.089 1.00 22.37 ?  453 ARG B CA    1 
ATOM   9193  C  C     . ARG B 1 453 ? 128.974 158.507 144.316 1.00 29.71 ?  453 ARG B C     1 
ATOM   9194  O  O     . ARG B 1 453 ? 128.750 159.419 145.120 1.00 32.37 ?  453 ARG B O     1 
ATOM   9195  C  CB    . ARG B 1 453 ? 128.971 158.962 141.848 1.00 25.06 ?  453 ARG B CB    1 
ATOM   9196  C  CG    . ARG B 1 453 ? 127.793 159.894 142.066 1.00 25.17 ?  453 ARG B CG    1 
ATOM   9197  C  CD    . ARG B 1 453 ? 127.200 160.357 140.750 1.00 24.76 ?  453 ARG B CD    1 
ATOM   9198  N  NE    . ARG B 1 453 ? 125.796 159.983 140.626 1.00 27.52 ?  453 ARG B NE    1 
ATOM   9199  C  CZ    . ARG B 1 453 ? 124.786 160.683 141.124 1.00 29.14 ?  453 ARG B CZ    1 
ATOM   9200  N  NH1   . ARG B 1 453 ? 124.987 161.804 141.796 1.00 30.68 1  453 ARG B NH1   1 
ATOM   9201  N  NH2   . ARG B 1 453 ? 123.544 160.246 140.945 1.00 25.55 ?  453 ARG B NH2   1 
ATOM   9202  N  N     . ALA B 1 454 ? 128.481 157.277 144.484 1.00 31.94 ?  454 ALA B N     1 
ATOM   9203  C  CA    . ALA B 1 454 ? 127.651 156.971 145.641 1.00 20.44 ?  454 ALA B CA    1 
ATOM   9204  C  C     . ALA B 1 454 ? 128.460 156.965 146.929 1.00 20.06 ?  454 ALA B C     1 
ATOM   9205  O  O     . ALA B 1 454 ? 127.935 157.331 147.983 1.00 29.70 ?  454 ALA B O     1 
ATOM   9206  C  CB    . ALA B 1 454 ? 126.947 155.632 145.447 1.00 22.79 ?  454 ALA B CB    1 
ATOM   9207  N  N     . ASN B 1 455 ? 129.726 156.553 146.874 1.00 26.92 ?  455 ASN B N     1 
ATOM   9208  C  CA    . ASN B 1 455 ? 130.573 156.638 148.056 1.00 20.39 ?  455 ASN B CA    1 
ATOM   9209  C  C     . ASN B 1 455 ? 130.804 158.087 148.458 1.00 26.77 ?  455 ASN B C     1 
ATOM   9210  O  O     . ASN B 1 455 ? 130.796 158.418 149.649 1.00 39.86 ?  455 ASN B O     1 
ATOM   9211  C  CB    . ASN B 1 455 ? 131.902 155.929 147.800 1.00 20.18 ?  455 ASN B CB    1 
ATOM   9212  C  CG    . ASN B 1 455 ? 132.786 155.884 149.031 1.00 29.85 ?  455 ASN B CG    1 
ATOM   9213  O  OD1   . ASN B 1 455 ? 132.491 155.179 149.993 1.00 38.69 ?  455 ASN B OD1   1 
ATOM   9214  N  ND2   . ASN B 1 455 ? 133.876 156.638 149.004 1.00 29.79 ?  455 ASN B ND2   1 
ATOM   9215  N  N     . LYS B 1 456 ? 131.011 158.967 147.477 1.00 27.60 ?  456 LYS B N     1 
ATOM   9216  C  CA    . LYS B 1 456 ? 131.225 160.376 147.787 1.00 26.83 ?  456 LYS B CA    1 
ATOM   9217  C  C     . LYS B 1 456 ? 129.950 161.055 148.271 1.00 26.99 ?  456 LYS B C     1 
ATOM   9218  O  O     . LYS B 1 456 ? 130.010 161.937 149.133 1.00 31.45 ?  456 LYS B O     1 
ATOM   9219  C  CB    . LYS B 1 456 ? 131.781 161.101 146.562 1.00 24.22 ?  456 LYS B CB    1 
ATOM   9220  C  CG    . LYS B 1 456 ? 132.772 162.201 146.895 1.00 29.52 ?  456 LYS B CG    1 
ATOM   9221  C  CD    . LYS B 1 456 ? 132.097 163.563 146.915 1.00 35.87 ?  456 LYS B CD    1 
ATOM   9222  C  CE    . LYS B 1 456 ? 133.020 164.632 147.477 1.00 37.12 ?  456 LYS B CE    1 
ATOM   9223  N  NZ    . LYS B 1 456 ? 132.921 164.730 148.960 1.00 31.89 1  456 LYS B NZ    1 
ATOM   9224  N  N     . ALA B 1 457 ? 128.794 160.668 147.734 1.00 25.36 ?  457 ALA B N     1 
ATOM   9225  C  CA    . ALA B 1 457 ? 127.540 161.348 148.032 1.00 17.19 ?  457 ALA B CA    1 
ATOM   9226  C  C     . ALA B 1 457 ? 126.851 160.798 149.276 1.00 23.78 ?  457 ALA B C     1 
ATOM   9227  O  O     . ALA B 1 457 ? 126.521 161.556 150.193 1.00 27.47 ?  457 ALA B O     1 
ATOM   9228  C  CB    . ALA B 1 457 ? 126.601 161.247 146.828 1.00 20.86 ?  457 ALA B CB    1 
ATOM   9229  N  N     . MET B 1 458 ? 126.626 159.486 149.316 1.00 34.34 ?  458 MET B N     1 
ATOM   9230  C  CA    . MET B 1 458 ? 125.866 158.873 150.397 1.00 17.01 ?  458 MET B CA    1 
ATOM   9231  C  C     . MET B 1 458 ? 126.673 158.797 151.686 1.00 25.08 ?  458 MET B C     1 
ATOM   9232  O  O     . MET B 1 458 ? 126.112 158.958 152.776 1.00 33.26 ?  458 MET B O     1 
ATOM   9233  C  CB    . MET B 1 458 ? 125.406 157.478 149.977 1.00 18.15 ?  458 MET B CB    1 
ATOM   9234  C  CG    . MET B 1 458 ? 124.683 157.429 148.637 1.00 21.57 ?  458 MET B CG    1 
ATOM   9235  S  SD    . MET B 1 458 ? 122.896 157.636 148.763 1.00 35.77 ?  458 MET B SD    1 
ATOM   9236  C  CE    . MET B 1 458 ? 122.750 159.420 148.771 1.00 27.87 ?  458 MET B CE    1 
ATOM   9237  N  N     . LYS B 1 459 ? 127.979 158.548 151.582 1.00 15.58 ?  459 LYS B N     1 
ATOM   9238  C  CA    . LYS B 1 459 ? 128.849 158.388 152.747 1.00 18.95 ?  459 LYS B CA    1 
ATOM   9239  C  C     . LYS B 1 459 ? 128.316 157.308 153.685 1.00 20.49 ?  459 LYS B C     1 
ATOM   9240  O  O     . LYS B 1 459 ? 128.372 157.432 154.909 1.00 32.27 ?  459 LYS B O     1 
ATOM   9241  C  CB    . LYS B 1 459 ? 129.030 159.713 153.491 1.00 26.05 ?  459 LYS B CB    1 
ATOM   9242  C  CG    . LYS B 1 459 ? 129.522 160.855 152.624 1.00 31.44 ?  459 LYS B CG    1 
ATOM   9243  C  CD    . LYS B 1 459 ? 128.803 162.145 152.971 1.00 23.51 ?  459 LYS B CD    1 
ATOM   9244  C  CE    . LYS B 1 459 ? 129.188 163.263 152.024 1.00 27.85 ?  459 LYS B CE    1 
ATOM   9245  N  NZ    . LYS B 1 459 ? 128.477 164.528 152.347 1.00 33.22 1  459 LYS B NZ    1 
ATOM   9246  N  N     . SER B 1 460 ? 127.792 156.235 153.102 1.00 16.22 ?  460 SER B N     1 
ATOM   9247  C  CA    . SER B 1 460 ? 127.190 155.169 153.885 1.00 9.49  ?  460 SER B CA    1 
ATOM   9248  C  C     . SER B 1 460 ? 128.260 154.253 154.463 1.00 19.62 ?  460 SER B C     1 
ATOM   9249  O  O     . SER B 1 460 ? 129.251 153.934 153.802 1.00 32.72 ?  460 SER B O     1 
ATOM   9250  C  CB    . SER B 1 460 ? 126.220 154.357 153.029 1.00 17.17 ?  460 SER B CB    1 
ATOM   9251  O  OG    . SER B 1 460 ? 126.917 153.591 152.065 1.00 26.49 ?  460 SER B OG    1 
ATOM   9252  N  N     . ILE B 1 461 ? 128.048 153.830 155.708 1.00 19.65 ?  461 ILE B N     1 
ATOM   9253  C  CA    . ILE B 1 461 ? 128.942 152.909 156.391 1.00 15.15 ?  461 ILE B CA    1 
ATOM   9254  C  C     . ILE B 1 461 ? 128.109 151.764 156.944 1.00 20.77 ?  461 ILE B C     1 
ATOM   9255  O  O     . ILE B 1 461 ? 126.890 151.863 157.086 1.00 23.59 ?  461 ILE B O     1 
ATOM   9256  C  CB    . ILE B 1 461 ? 129.737 153.590 157.525 1.00 12.55 ?  461 ILE B CB    1 
ATOM   9257  C  CG1   . ILE B 1 461 ? 128.783 154.226 158.535 1.00 7.21  ?  461 ILE B CG1   1 
ATOM   9258  C  CG2   . ILE B 1 461 ? 130.688 154.630 156.959 1.00 18.35 ?  461 ILE B CG2   1 
ATOM   9259  C  CD1   . ILE B 1 461 ? 129.437 154.618 159.832 1.00 12.29 ?  461 ILE B CD1   1 
ATOM   9260  N  N     . GLY B 1 462 ? 128.779 150.655 157.230 1.00 20.59 ?  462 GLY B N     1 
ATOM   9261  C  CA    . GLY B 1 462 ? 128.115 149.568 157.914 1.00 9.98  ?  462 GLY B CA    1 
ATOM   9262  C  C     . GLY B 1 462 ? 128.818 149.193 159.198 1.00 11.74 ?  462 GLY B C     1 
ATOM   9263  O  O     . GLY B 1 462 ? 129.922 148.645 159.168 1.00 27.20 ?  462 GLY B O     1 
ATOM   9264  N  N     . LEU B 1 463 ? 128.184 149.466 160.331 1.00 12.75 ?  463 LEU B N     1 
ATOM   9265  C  CA    . LEU B 1 463 ? 128.716 149.096 161.637 1.00 8.74  ?  463 LEU B CA    1 
ATOM   9266  C  C     . LEU B 1 463 ? 127.915 147.910 162.154 1.00 20.47 ?  463 LEU B C     1 
ATOM   9267  O  O     . LEU B 1 463 ? 126.758 148.062 162.556 1.00 28.83 ?  463 LEU B O     1 
ATOM   9268  C  CB    . LEU B 1 463 ? 128.657 150.270 162.610 1.00 18.78 ?  463 LEU B CB    1 
ATOM   9269  C  CG    . LEU B 1 463 ? 129.081 149.948 164.043 1.00 16.77 ?  463 LEU B CG    1 
ATOM   9270  C  CD1   . LEU B 1 463 ? 130.496 149.404 164.063 1.00 3.19  ?  463 LEU B CD1   1 
ATOM   9271  C  CD2   . LEU B 1 463 ? 128.957 151.172 164.934 1.00 16.93 ?  463 LEU B CD2   1 
ATOM   9272  N  N     . GLY B 1 464 ? 128.532 146.730 162.140 1.00 22.67 ?  464 GLY B N     1 
ATOM   9273  C  CA    . GLY B 1 464 ? 127.894 145.520 162.600 1.00 13.17 ?  464 GLY B CA    1 
ATOM   9274  C  C     . GLY B 1 464 ? 128.235 145.191 164.041 1.00 9.46  ?  464 GLY B C     1 
ATOM   9275  O  O     . GLY B 1 464 ? 128.879 145.959 164.759 1.00 18.19 ?  464 GLY B O     1 
ATOM   9276  N  N     . ALA B 1 465 ? 127.782 144.016 164.463 1.00 15.21 ?  465 ALA B N     1 
ATOM   9277  C  CA    . ALA B 1 465 ? 128.066 143.501 165.790 1.00 8.92  ?  465 ALA B CA    1 
ATOM   9278  C  C     . ALA B 1 465 ? 128.317 142.006 165.683 1.00 16.15 ?  465 ALA B C     1 
ATOM   9279  O  O     . ALA B 1 465 ? 127.876 141.347 164.741 1.00 33.48 ?  465 ALA B O     1 
ATOM   9280  C  CB    . ALA B 1 465 ? 126.923 143.786 166.770 1.00 18.90 ?  465 ALA B CB    1 
ATOM   9281  N  N     . MET B 1 466 ? 129.042 141.479 166.664 1.00 22.79 ?  466 MET B N     1 
ATOM   9282  C  CA    . MET B 1 466 ? 129.349 140.060 166.714 1.00 19.06 ?  466 MET B CA    1 
ATOM   9283  C  C     . MET B 1 466 ? 129.446 139.645 168.174 1.00 18.39 ?  466 MET B C     1 
ATOM   9284  O  O     . MET B 1 466 ? 129.353 140.475 169.082 1.00 23.63 ?  466 MET B O     1 
ATOM   9285  C  CB    . MET B 1 466 ? 130.639 139.749 165.951 1.00 24.49 ?  466 MET B CB    1 
ATOM   9286  C  CG    . MET B 1 466 ? 131.893 140.160 166.689 1.00 27.81 ?  466 MET B CG    1 
ATOM   9287  S  SD    . MET B 1 466 ? 133.350 140.212 165.639 1.00 41.52 ?  466 MET B SD    1 
ATOM   9288  C  CE    . MET B 1 466 ? 134.287 141.469 166.492 1.00 25.51 ?  466 MET B CE    1 
ATOM   9289  N  N     . ASN B 1 467 ? 129.628 138.342 168.393 1.00 16.44 ?  467 ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 467 ? 129.741 137.764 169.732 1.00 22.64 ?  467 ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 467 ? 128.470 137.968 170.549 1.00 26.97 ?  467 ASN B C     1 
ATOM   9292  O  O     . ASN B 1 467 ? 128.524 138.127 171.769 1.00 26.62 ?  467 ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 467 ? 130.951 138.323 170.487 1.00 21.75 ?  467 ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 467 ? 131.634 137.281 171.341 1.00 27.21 ?  467 ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 467 ? 131.275 136.106 171.313 1.00 27.28 ?  467 ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 467 ? 132.630 137.705 172.106 1.00 30.72 ?  467 ASN B ND2   1 
ATOM   9297  N  N     . LEU B 1 468 ? 127.314 137.980 169.884 1.00 17.65 ?  468 LEU B N     1 
ATOM   9298  C  CA    . LEU B 1 468 ? 126.053 138.046 170.612 1.00 14.70 ?  468 LEU B CA    1 
ATOM   9299  C  C     . LEU B 1 468 ? 125.798 136.750 171.372 1.00 29.01 ?  468 LEU B C     1 
ATOM   9300  O  O     . LEU B 1 468 ? 125.507 136.768 172.573 1.00 33.40 ?  468 LEU B O     1 
ATOM   9301  C  CB    . LEU B 1 468 ? 124.904 138.338 169.649 1.00 24.99 ?  468 LEU B CB    1 
ATOM   9302  C  CG    . LEU B 1 468 ? 123.515 138.406 170.285 1.00 19.41 ?  468 LEU B CG    1 
ATOM   9303  C  CD1   . LEU B 1 468 ? 123.464 139.490 171.345 1.00 16.93 ?  468 LEU B CD1   1 
ATOM   9304  C  CD2   . LEU B 1 468 ? 122.446 138.630 169.233 1.00 16.14 ?  468 LEU B CD2   1 
ATOM   9305  N  N     . HIS B 1 469 ? 125.926 135.612 170.687 1.00 31.57 ?  469 HIS B N     1 
ATOM   9306  C  CA    . HIS B 1 469 ? 125.706 134.332 171.347 1.00 16.43 ?  469 HIS B CA    1 
ATOM   9307  C  C     . HIS B 1 469 ? 126.787 134.052 172.378 1.00 27.60 ?  469 HIS B C     1 
ATOM   9308  O  O     . HIS B 1 469 ? 126.504 133.490 173.438 1.00 38.08 ?  469 HIS B O     1 
ATOM   9309  C  CB    . HIS B 1 469 ? 125.642 133.204 170.319 1.00 15.93 ?  469 HIS B CB    1 
ATOM   9310  C  CG    . HIS B 1 469 ? 125.050 131.940 170.857 1.00 20.95 ?  469 HIS B CG    1 
ATOM   9311  N  ND1   . HIS B 1 469 ? 125.081 130.749 170.167 1.00 33.35 ?  469 HIS B ND1   1 
ATOM   9312  C  CD2   . HIS B 1 469 ? 124.412 131.682 172.022 1.00 27.48 ?  469 HIS B CD2   1 
ATOM   9313  C  CE1   . HIS B 1 469 ? 124.487 129.812 170.883 1.00 26.03 ?  469 HIS B CE1   1 
ATOM   9314  N  NE2   . HIS B 1 469 ? 124.073 130.352 172.014 1.00 25.19 ?  469 HIS B NE2   1 
ATOM   9315  N  N     . GLY B 1 470 ? 128.031 134.430 172.087 1.00 20.38 ?  470 GLY B N     1 
ATOM   9316  C  CA    . GLY B 1 470 ? 129.086 134.263 173.071 1.00 23.00 ?  470 GLY B CA    1 
ATOM   9317  C  C     . GLY B 1 470 ? 128.836 135.075 174.325 1.00 16.85 ?  470 GLY B C     1 
ATOM   9318  O  O     . GLY B 1 470 ? 128.986 134.573 175.442 1.00 35.43 ?  470 GLY B O     1 
ATOM   9319  N  N     . TYR B 1 471 ? 128.429 136.334 174.159 1.00 17.13 ?  471 TYR B N     1 
ATOM   9320  C  CA    . TYR B 1 471 ? 128.136 137.175 175.313 1.00 20.16 ?  471 TYR B CA    1 
ATOM   9321  C  C     . TYR B 1 471 ? 126.955 136.633 176.106 1.00 25.71 ?  471 TYR B C     1 
ATOM   9322  O  O     . TYR B 1 471 ? 126.970 136.648 177.342 1.00 30.05 ?  471 TYR B O     1 
ATOM   9323  C  CB    . TYR B 1 471 ? 127.859 138.610 174.868 1.00 25.45 ?  471 TYR B CB    1 
ATOM   9324  C  CG    . TYR B 1 471 ? 127.277 139.467 175.967 1.00 24.40 ?  471 TYR B CG    1 
ATOM   9325  C  CD1   . TYR B 1 471 ? 128.086 139.982 176.969 1.00 25.10 ?  471 TYR B CD1   1 
ATOM   9326  C  CD2   . TYR B 1 471 ? 125.918 139.736 176.018 1.00 15.35 ?  471 TYR B CD2   1 
ATOM   9327  C  CE1   . TYR B 1 471 ? 127.559 140.755 177.980 1.00 22.93 ?  471 TYR B CE1   1 
ATOM   9328  C  CE2   . TYR B 1 471 ? 125.384 140.500 177.029 1.00 19.90 ?  471 TYR B CE2   1 
ATOM   9329  C  CZ    . TYR B 1 471 ? 126.207 141.010 178.003 1.00 26.35 ?  471 TYR B CZ    1 
ATOM   9330  O  OH    . TYR B 1 471 ? 125.673 141.780 179.009 1.00 36.38 ?  471 TYR B OH    1 
ATOM   9331  N  N     . LEU B 1 472 ? 125.916 136.160 175.414 1.00 28.49 ?  472 LEU B N     1 
ATOM   9332  C  CA    . LEU B 1 472 ? 124.736 135.660 176.112 1.00 21.62 ?  472 LEU B CA    1 
ATOM   9333  C  C     . LEU B 1 472 ? 125.036 134.359 176.849 1.00 28.12 ?  472 LEU B C     1 
ATOM   9334  O  O     . LEU B 1 472 ? 124.650 134.190 178.010 1.00 35.09 ?  472 LEU B O     1 
ATOM   9335  C  CB    . LEU B 1 472 ? 123.584 135.468 175.124 1.00 23.44 ?  472 LEU B CB    1 
ATOM   9336  C  CG    . LEU B 1 472 ? 122.988 136.739 174.517 1.00 25.83 ?  472 LEU B CG    1 
ATOM   9337  C  CD1   . LEU B 1 472 ? 122.043 136.391 173.379 1.00 24.57 ?  472 LEU B CD1   1 
ATOM   9338  C  CD2   . LEU B 1 472 ? 122.279 137.567 175.575 1.00 22.97 ?  472 LEU B CD2   1 
ATOM   9339  N  N     . ALA B 1 473 ? 125.726 133.426 176.188 1.00 24.54 ?  473 ALA B N     1 
ATOM   9340  C  CA    . ALA B 1 473 ? 126.039 132.148 176.812 1.00 24.14 ?  473 ALA B CA    1 
ATOM   9341  C  C     . ALA B 1 473 ? 127.030 132.304 177.955 1.00 32.15 ?  473 ALA B C     1 
ATOM   9342  O  O     . ALA B 1 473 ? 126.950 131.568 178.945 1.00 39.89 ?  473 ALA B O     1 
ATOM   9343  C  CB    . ALA B 1 473 ? 126.579 131.176 175.765 1.00 25.75 ?  473 ALA B CB    1 
ATOM   9344  N  N     . GLN B 1 474 ? 127.966 133.247 177.846 1.00 31.34 ?  474 GLN B N     1 
ATOM   9345  C  CA    . GLN B 1 474 ? 128.883 133.510 178.944 1.00 29.33 ?  474 GLN B CA    1 
ATOM   9346  C  C     . GLN B 1 474 ? 128.233 134.290 180.078 1.00 29.76 ?  474 GLN B C     1 
ATOM   9347  O  O     . GLN B 1 474 ? 128.857 134.456 181.131 1.00 40.96 ?  474 GLN B O     1 
ATOM   9348  C  CB    . GLN B 1 474 ? 130.114 134.261 178.433 1.00 31.56 ?  474 GLN B CB    1 
ATOM   9349  C  CG    . GLN B 1 474 ? 131.063 133.390 177.634 1.00 29.28 ?  474 GLN B CG    1 
ATOM   9350  C  CD    . GLN B 1 474 ? 132.203 134.175 177.027 1.00 36.08 ?  474 GLN B CD    1 
ATOM   9351  O  OE1   . GLN B 1 474 ? 133.072 134.677 177.737 1.00 42.48 ?  474 GLN B OE1   1 
ATOM   9352  N  NE2   . GLN B 1 474 ? 132.208 134.282 175.704 1.00 36.55 ?  474 GLN B NE2   1 
ATOM   9353  N  N     . ASN B 1 475 ? 127.005 134.771 179.889 1.00 32.74 ?  475 ASN B N     1 
ATOM   9354  C  CA    . ASN B 1 475 ? 126.252 135.449 180.934 1.00 35.35 ?  475 ASN B CA    1 
ATOM   9355  C  C     . ASN B 1 475 ? 125.040 134.646 181.388 1.00 36.04 ?  475 ASN B C     1 
ATOM   9356  O  O     . ASN B 1 475 ? 124.171 135.190 182.077 1.00 38.28 ?  475 ASN B O     1 
ATOM   9357  C  CB    . ASN B 1 475 ? 125.818 136.836 180.462 1.00 34.60 ?  475 ASN B CB    1 
ATOM   9358  C  CG    . ASN B 1 475 ? 126.974 137.808 180.373 1.00 32.50 ?  475 ASN B CG    1 
ATOM   9359  O  OD1   . ASN B 1 475 ? 127.231 138.568 181.305 1.00 39.35 ?  475 ASN B OD1   1 
ATOM   9360  N  ND2   . ASN B 1 475 ? 127.684 137.780 179.254 1.00 28.42 ?  475 ASN B ND2   1 
ATOM   9361  N  N     . GLY B 1 476 ? 124.960 133.372 181.019 1.00 35.89 ?  476 GLY B N     1 
ATOM   9362  C  CA    . GLY B 1 476 ? 123.860 132.521 181.434 1.00 32.40 ?  476 GLY B CA    1 
ATOM   9363  C  C     . GLY B 1 476 ? 122.511 132.900 180.862 1.00 35.20 ?  476 GLY B C     1 
ATOM   9364  O  O     . GLY B 1 476 ? 121.504 132.853 181.580 1.00 42.73 ?  476 GLY B O     1 
ATOM   9365  N  N     . ILE B 1 477 ? 122.463 133.276 179.587 1.00 32.50 ?  477 ILE B N     1 
ATOM   9366  C  CA    . ILE B 1 477 ? 121.221 133.635 178.916 1.00 32.21 ?  477 ILE B CA    1 
ATOM   9367  C  C     . ILE B 1 477 ? 121.092 132.789 177.659 1.00 32.56 ?  477 ILE B C     1 
ATOM   9368  O  O     . ILE B 1 477 ? 121.999 132.771 176.821 1.00 36.67 ?  477 ILE B O     1 
ATOM   9369  C  CB    . ILE B 1 477 ? 121.168 135.136 178.569 1.00 27.66 ?  477 ILE B CB    1 
ATOM   9370  C  CG1   . ILE B 1 477 ? 121.145 135.980 179.844 1.00 30.97 ?  477 ILE B CG1   1 
ATOM   9371  C  CG2   . ILE B 1 477 ? 119.956 135.442 177.715 1.00 26.18 ?  477 ILE B CG2   1 
ATOM   9372  C  CD1   . ILE B 1 477 ? 121.785 137.337 179.687 1.00 33.59 ?  477 ILE B CD1   1 
ATOM   9373  N  N     . ALA B 1 478 ? 119.971 132.084 177.534 1.00 33.33 ?  478 ALA B N     1 
ATOM   9374  C  CA    . ALA B 1 478 ? 119.716 131.297 176.336 1.00 28.73 ?  478 ALA B CA    1 
ATOM   9375  C  C     . ALA B 1 478 ? 119.429 132.214 175.157 1.00 34.04 ?  478 ALA B C     1 
ATOM   9376  O  O     . ALA B 1 478 ? 118.790 133.257 175.303 1.00 38.65 ?  478 ALA B O     1 
ATOM   9377  C  CB    . ALA B 1 478 ? 118.543 130.345 176.563 1.00 29.59 ?  478 ALA B CB    1 
ATOM   9378  N  N     . TYR B 1 479 ? 119.909 131.816 173.976 1.00 29.89 ?  479 TYR B N     1 
ATOM   9379  C  CA    . TYR B 1 479 ? 119.753 132.650 172.788 1.00 21.31 ?  479 TYR B CA    1 
ATOM   9380  C  C     . TYR B 1 479 ? 118.283 132.844 172.433 1.00 33.73 ?  479 TYR B C     1 
ATOM   9381  O  O     . TYR B 1 479 ? 117.878 133.935 172.014 1.00 36.22 ?  479 TYR B O     1 
ATOM   9382  C  CB    . TYR B 1 479 ? 120.517 132.031 171.620 1.00 19.78 ?  479 TYR B CB    1 
ATOM   9383  C  CG    . TYR B 1 479 ? 120.636 132.917 170.402 1.00 26.75 ?  479 TYR B CG    1 
ATOM   9384  C  CD1   . TYR B 1 479 ? 119.678 132.884 169.397 1.00 30.18 ?  479 TYR B CD1   1 
ATOM   9385  C  CD2   . TYR B 1 479 ? 121.714 133.779 170.250 1.00 23.61 ?  479 TYR B CD2   1 
ATOM   9386  C  CE1   . TYR B 1 479 ? 119.786 133.690 168.282 1.00 23.94 ?  479 TYR B CE1   1 
ATOM   9387  C  CE2   . TYR B 1 479 ? 121.831 134.586 169.139 1.00 22.72 ?  479 TYR B CE2   1 
ATOM   9388  C  CZ    . TYR B 1 479 ? 120.865 134.538 168.158 1.00 30.34 ?  479 TYR B CZ    1 
ATOM   9389  O  OH    . TYR B 1 479 ? 120.978 135.341 167.048 1.00 35.04 ?  479 TYR B OH    1 
ATOM   9390  N  N     . GLU B 1 480 ? 117.470 131.799 172.588 1.00 36.31 ?  480 GLU B N     1 
ATOM   9391  C  CA    . GLU B 1 480 ? 116.049 131.892 172.278 1.00 31.16 ?  480 GLU B CA    1 
ATOM   9392  C  C     . GLU B 1 480 ? 115.229 132.489 173.409 1.00 33.32 ?  480 GLU B C     1 
ATOM   9393  O  O     . GLU B 1 480 ? 114.023 132.695 173.233 1.00 38.14 ?  480 GLU B O     1 
ATOM   9394  C  CB    . GLU B 1 480 ? 115.485 130.510 171.942 1.00 34.29 ?  480 GLU B CB    1 
ATOM   9395  C  CG    . GLU B 1 480 ? 116.219 129.766 170.853 1.00 35.17 ?  480 GLU B CG    1 
ATOM   9396  C  CD    . GLU B 1 480 ? 116.148 128.267 171.049 1.00 43.07 ?  480 GLU B CD    1 
ATOM   9397  O  OE1   . GLU B 1 480 ? 116.903 127.744 171.894 1.00 44.45 ?  480 GLU B OE1   1 
ATOM   9398  O  OE2   . GLU B 1 480 ? 115.337 127.612 170.364 1.00 39.62 -1 480 GLU B OE2   1 
ATOM   9399  N  N     . SER B 1 481 ? 115.839 132.761 174.557 1.00 31.50 ?  481 SER B N     1 
ATOM   9400  C  CA    . SER B 1 481 ? 115.088 133.256 175.695 1.00 32.57 ?  481 SER B CA    1 
ATOM   9401  C  C     . SER B 1 481 ? 114.588 134.676 175.434 1.00 36.64 ?  481 SER B C     1 
ATOM   9402  O  O     . SER B 1 481 ? 115.199 135.429 174.671 1.00 38.79 ?  481 SER B O     1 
ATOM   9403  C  CB    . SER B 1 481 ? 115.952 133.231 176.952 1.00 30.75 ?  481 SER B CB    1 
ATOM   9404  O  OG    . SER B 1 481 ? 116.784 134.374 177.019 1.00 35.20 ?  481 SER B OG    1 
ATOM   9405  N  N     . PRO B 1 482 ? 113.462 135.058 176.041 1.00 42.31 ?  482 PRO B N     1 
ATOM   9406  C  CA    . PRO B 1 482 ? 113.016 136.455 175.932 1.00 37.58 ?  482 PRO B CA    1 
ATOM   9407  C  C     . PRO B 1 482 ? 114.009 137.445 176.510 1.00 32.77 ?  482 PRO B C     1 
ATOM   9408  O  O     . PRO B 1 482 ? 114.041 138.602 176.075 1.00 36.90 ?  482 PRO B O     1 
ATOM   9409  C  CB    . PRO B 1 482 ? 111.692 136.460 176.708 1.00 35.59 ?  482 PRO B CB    1 
ATOM   9410  C  CG    . PRO B 1 482 ? 111.235 135.044 176.686 1.00 37.34 ?  482 PRO B CG    1 
ATOM   9411  C  CD    . PRO B 1 482 ? 112.481 134.218 176.746 1.00 37.93 ?  482 PRO B CD    1 
ATOM   9412  N  N     . GLU B 1 483 ? 114.820 137.026 177.483 1.00 35.62 ?  483 GLU B N     1 
ATOM   9413  C  CA    . GLU B 1 483 ? 115.836 137.915 178.038 1.00 32.90 ?  483 GLU B CA    1 
ATOM   9414  C  C     . GLU B 1 483 ? 116.922 138.219 177.013 1.00 30.00 ?  483 GLU B C     1 
ATOM   9415  O  O     . GLU B 1 483 ? 117.463 139.330 176.986 1.00 36.41 ?  483 GLU B O     1 
ATOM   9416  C  CB    . GLU B 1 483 ? 116.441 137.295 179.297 1.00 37.13 ?  483 GLU B CB    1 
ATOM   9417  C  CG    . GLU B 1 483 ? 115.457 137.144 180.444 1.00 39.21 ?  483 GLU B CG    1 
ATOM   9418  C  CD    . GLU B 1 483 ? 114.806 135.775 180.477 1.00 45.79 ?  483 GLU B CD    1 
ATOM   9419  O  OE1   . GLU B 1 483 ? 114.933 135.033 179.483 1.00 42.62 ?  483 GLU B OE1   1 
ATOM   9420  O  OE2   . GLU B 1 483 ? 114.165 135.443 181.495 1.00 44.24 -1 483 GLU B OE2   1 
ATOM   9421  N  N     . ALA B 1 484 ? 117.259 137.244 176.168 1.00 28.45 ?  484 ALA B N     1 
ATOM   9422  C  CA    . ALA B 1 484 ? 118.224 137.495 175.103 1.00 29.24 ?  484 ALA B CA    1 
ATOM   9423  C  C     . ALA B 1 484 ? 117.703 138.536 174.122 1.00 29.55 ?  484 ALA B C     1 
ATOM   9424  O  O     . ALA B 1 484 ? 118.443 139.436 173.708 1.00 31.34 ?  484 ALA B O     1 
ATOM   9425  C  CB    . ALA B 1 484 ? 118.553 136.195 174.376 1.00 21.96 ?  484 ALA B CB    1 
ATOM   9426  N  N     . ARG B 1 485 ? 116.429 138.431 173.742 1.00 26.43 ?  485 ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 485 ? 115.838 139.437 172.869 1.00 26.24 ?  485 ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 485 ? 115.742 140.787 173.563 1.00 24.75 ?  485 ARG B C     1 
ATOM   9429  O  O     . ARG B 1 485 ? 115.890 141.823 172.912 1.00 35.19 ?  485 ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 485 ? 114.462 138.980 172.391 1.00 28.25 ?  485 ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 485 ? 114.514 137.912 171.319 1.00 26.08 ?  485 ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 485 ? 113.148 137.687 170.699 1.00 25.72 ?  485 ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 485 ? 112.182 137.182 171.666 1.00 29.58 ?  485 ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 485 ? 112.107 135.918 172.061 1.00 33.69 ?  485 ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 485 ? 112.927 134.995 171.588 1.00 35.12 1  485 ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 485 ? 111.183 135.572 172.953 1.00 29.72 ?  485 ARG B NH2   1 
ATOM   9437  N  N     . ASP B 1 486 ? 115.501 140.796 174.873 1.00 30.77 ?  486 ASP B N     1 
ATOM   9438  C  CA    . ASP B 1 486 ? 115.490 142.049 175.622 1.00 30.72 ?  486 ASP B CA    1 
ATOM   9439  C  C     . ASP B 1 486 ? 116.859 142.719 175.586 1.00 30.06 ?  486 ASP B C     1 
ATOM   9440  O  O     . ASP B 1 486 ? 116.971 143.933 175.352 1.00 32.61 ?  486 ASP B O     1 
ATOM   9441  C  CB    . ASP B 1 486 ? 115.048 141.775 177.059 1.00 34.22 ?  486 ASP B CB    1 
ATOM   9442  C  CG    . ASP B 1 486 ? 114.761 143.038 177.832 1.00 43.15 ?  486 ASP B CG    1 
ATOM   9443  O  OD1   . ASP B 1 486 ? 114.053 143.918 177.300 1.00 45.20 ?  486 ASP B OD1   1 
ATOM   9444  O  OD2   . ASP B 1 486 ? 115.238 143.144 178.979 1.00 34.53 -1 486 ASP B OD2   1 
ATOM   9445  N  N     . PHE B 1 487 ? 117.919 141.936 175.804 1.00 26.92 ?  487 PHE B N     1 
ATOM   9446  C  CA    . PHE B 1 487 ? 119.263 142.491 175.719 1.00 23.40 ?  487 PHE B CA    1 
ATOM   9447  C  C     . PHE B 1 487 ? 119.567 142.987 174.316 1.00 28.27 ?  487 PHE B C     1 
ATOM   9448  O  O     . PHE B 1 487 ? 120.177 144.045 174.149 1.00 30.97 ?  487 PHE B O     1 
ATOM   9449  C  CB    . PHE B 1 487 ? 120.321 141.472 176.132 1.00 24.72 ?  487 PHE B CB    1 
ATOM   9450  C  CG    . PHE B 1 487 ? 121.700 141.854 175.681 1.00 28.11 ?  487 PHE B CG    1 
ATOM   9451  C  CD1   . PHE B 1 487 ? 122.399 142.850 176.340 1.00 21.12 ?  487 PHE B CD1   1 
ATOM   9452  C  CD2   . PHE B 1 487 ? 122.278 141.262 174.571 1.00 27.86 ?  487 PHE B CD2   1 
ATOM   9453  C  CE1   . PHE B 1 487 ? 123.652 143.231 175.918 1.00 23.42 ?  487 PHE B CE1   1 
ATOM   9454  C  CE2   . PHE B 1 487 ? 123.533 141.642 174.148 1.00 26.23 ?  487 PHE B CE2   1 
ATOM   9455  C  CZ    . PHE B 1 487 ? 124.219 142.629 174.821 1.00 25.18 ?  487 PHE B CZ    1 
ATOM   9456  N  N     . ALA B 1 488 ? 119.195 142.214 173.294 1.00 26.01 ?  488 ALA B N     1 
ATOM   9457  C  CA    . ALA B 1 488 ? 119.450 142.647 171.924 1.00 20.12 ?  488 ALA B CA    1 
ATOM   9458  C  C     . ALA B 1 488 ? 118.725 143.951 171.626 1.00 29.34 ?  488 ALA B C     1 
ATOM   9459  O  O     . ALA B 1 488 ? 119.302 144.874 171.041 1.00 38.20 ?  488 ALA B O     1 
ATOM   9460  C  CB    . ALA B 1 488 ? 119.030 141.559 170.940 1.00 21.50 ?  488 ALA B CB    1 
ATOM   9461  N  N     . ASN B 1 489 ? 117.464 144.049 172.051 1.00 28.70 ?  489 ASN B N     1 
ATOM   9462  C  CA    . ASN B 1 489 ? 116.694 145.273 171.880 1.00 26.11 ?  489 ASN B CA    1 
ATOM   9463  C  C     . ASN B 1 489 ? 117.413 146.463 172.497 1.00 20.40 ?  489 ASN B C     1 
ATOM   9464  O  O     . ASN B 1 489 ? 117.668 147.466 171.822 1.00 29.68 ?  489 ASN B O     1 
ATOM   9465  C  CB    . ASN B 1 489 ? 115.313 145.091 172.508 1.00 21.16 ?  489 ASN B CB    1 
ATOM   9466  C  CG    . ASN B 1 489 ? 114.285 146.050 171.960 1.00 32.36 ?  489 ASN B CG    1 
ATOM   9467  O  OD1   . ASN B 1 489 ? 114.040 146.097 170.756 1.00 39.21 ?  489 ASN B OD1   1 
ATOM   9468  N  ND2   . ASN B 1 489 ? 113.663 146.814 172.847 1.00 31.79 ?  489 ASN B ND2   1 
ATOM   9469  N  N     . THR B 1 490 ? 117.788 146.352 173.774 1.00 22.72 ?  490 THR B N     1 
ATOM   9470  C  CA    . THR B 1 490 ? 118.412 147.485 174.453 1.00 22.67 ?  490 THR B CA    1 
ATOM   9471  C  C     . THR B 1 490 ? 119.774 147.817 173.850 1.00 24.87 ?  490 THR B C     1 
ATOM   9472  O  O     . THR B 1 490 ? 120.075 148.986 173.577 1.00 21.06 ?  490 THR B O     1 
ATOM   9473  C  CB    . THR B 1 490 ? 118.544 147.195 175.947 1.00 33.48 ?  490 THR B CB    1 
ATOM   9474  O  OG1   . THR B 1 490 ? 117.277 146.771 176.462 1.00 39.12 ?  490 THR B OG1   1 
ATOM   9475  C  CG2   . THR B 1 490 ? 118.998 148.441 176.690 1.00 27.80 ?  490 THR B CG2   1 
ATOM   9476  N  N     . PHE B 1 491 ? 120.602 146.796 173.623 1.00 25.08 ?  491 PHE B N     1 
ATOM   9477  C  CA    . PHE B 1 491 ? 121.957 147.012 173.131 1.00 19.01 ?  491 PHE B CA    1 
ATOM   9478  C  C     . PHE B 1 491 ? 121.947 147.662 171.758 1.00 25.49 ?  491 PHE B C     1 
ATOM   9479  O  O     . PHE B 1 491 ? 122.683 148.623 171.508 1.00 33.73 ?  491 PHE B O     1 
ATOM   9480  C  CB    . PHE B 1 491 ? 122.710 145.681 173.090 1.00 23.13 ?  491 PHE B CB    1 
ATOM   9481  C  CG    . PHE B 1 491 ? 124.108 145.786 172.546 1.00 25.07 ?  491 PHE B CG    1 
ATOM   9482  C  CD1   . PHE B 1 491 ? 125.174 146.047 173.388 1.00 23.22 ?  491 PHE B CD1   1 
ATOM   9483  C  CD2   . PHE B 1 491 ? 124.360 145.611 171.194 1.00 20.50 ?  491 PHE B CD2   1 
ATOM   9484  C  CE1   . PHE B 1 491 ? 126.458 146.143 172.894 1.00 14.85 ?  491 PHE B CE1   1 
ATOM   9485  C  CE2   . PHE B 1 491 ? 125.640 145.709 170.696 1.00 15.76 ?  491 PHE B CE2   1 
ATOM   9486  C  CZ    . PHE B 1 491 ? 126.691 145.975 171.548 1.00 19.74 ?  491 PHE B CZ    1 
ATOM   9487  N  N     . PHE B 1 492 ? 121.120 147.153 170.846 1.00 20.89 ?  492 PHE B N     1 
ATOM   9488  C  CA    . PHE B 1 492 ? 121.112 147.714 169.508 1.00 12.88 ?  492 PHE B CA    1 
ATOM   9489  C  C     . PHE B 1 492 ? 120.356 149.031 169.432 1.00 10.87 ?  492 PHE B C     1 
ATOM   9490  O  O     . PHE B 1 492 ? 120.673 149.850 168.566 1.00 24.78 ?  492 PHE B O     1 
ATOM   9491  C  CB    . PHE B 1 492 ? 120.560 146.688 168.522 1.00 14.12 ?  492 PHE B CB    1 
ATOM   9492  C  CG    . PHE B 1 492 ? 121.534 145.587 168.218 1.00 16.24 ?  492 PHE B CG    1 
ATOM   9493  C  CD1   . PHE B 1 492 ? 122.574 145.794 167.332 1.00 10.13 ?  492 PHE B CD1   1 
ATOM   9494  C  CD2   . PHE B 1 492 ? 121.436 144.362 168.852 1.00 18.24 ?  492 PHE B CD2   1 
ATOM   9495  C  CE1   . PHE B 1 492 ? 123.481 144.793 167.063 1.00 8.63  ?  492 PHE B CE1   1 
ATOM   9496  C  CE2   . PHE B 1 492 ? 122.340 143.357 168.588 1.00 12.97 ?  492 PHE B CE2   1 
ATOM   9497  C  CZ    . PHE B 1 492 ? 123.363 143.572 167.692 1.00 15.74 ?  492 PHE B CZ    1 
ATOM   9498  N  N     . MET B 1 493 ? 119.413 149.290 170.345 1.00 14.89 ?  493 MET B N     1 
ATOM   9499  C  CA    . MET B 1 493 ? 118.881 150.642 170.455 1.00 17.34 ?  493 MET B CA    1 
ATOM   9500  C  C     . MET B 1 493 ? 119.976 151.620 170.851 1.00 22.68 ?  493 MET B C     1 
ATOM   9501  O  O     . MET B 1 493 ? 120.068 152.717 170.294 1.00 29.67 ?  493 MET B O     1 
ATOM   9502  C  CB    . MET B 1 493 ? 117.748 150.694 171.477 1.00 19.23 ?  493 MET B CB    1 
ATOM   9503  C  CG    . MET B 1 493 ? 117.159 152.087 171.646 1.00 18.99 ?  493 MET B CG    1 
ATOM   9504  S  SD    . MET B 1 493 ? 117.738 152.956 173.116 1.00 37.89 ?  493 MET B SD    1 
ATOM   9505  C  CE    . MET B 1 493 ? 117.696 151.651 174.336 1.00 27.76 ?  493 MET B CE    1 
ATOM   9506  N  N     . MET B 1 494 ? 120.817 151.239 171.817 1.00 22.12 ?  494 MET B N     1 
ATOM   9507  C  CA    . MET B 1 494 ? 121.922 152.106 172.218 1.00 17.02 ?  494 MET B CA    1 
ATOM   9508  C  C     . MET B 1 494 ? 122.916 152.299 171.078 1.00 18.65 ?  494 MET B C     1 
ATOM   9509  O  O     . MET B 1 494 ? 123.421 153.408 170.864 1.00 31.25 ?  494 MET B O     1 
ATOM   9510  C  CB    . MET B 1 494 ? 122.627 151.533 173.446 1.00 23.61 ?  494 MET B CB    1 
ATOM   9511  C  CG    . MET B 1 494 ? 121.736 151.364 174.661 1.00 22.05 ?  494 MET B CG    1 
ATOM   9512  S  SD    . MET B 1 494 ? 122.664 150.961 176.150 1.00 42.56 ?  494 MET B SD    1 
ATOM   9513  C  CE    . MET B 1 494 ? 123.923 152.230 176.112 1.00 31.53 ?  494 MET B CE    1 
ATOM   9514  N  N     . VAL B 1 495 ? 123.216 151.224 170.347 1.00 19.82 ?  495 VAL B N     1 
ATOM   9515  C  CA    . VAL B 1 495 ? 124.135 151.321 169.217 1.00 13.54 ?  495 VAL B CA    1 
ATOM   9516  C  C     . VAL B 1 495 ? 123.580 152.266 168.161 1.00 18.91 ?  495 VAL B C     1 
ATOM   9517  O  O     . VAL B 1 495 ? 124.301 153.119 167.634 1.00 31.74 ?  495 VAL B O     1 
ATOM   9518  C  CB    . VAL B 1 495 ? 124.417 149.923 168.637 1.00 15.39 ?  495 VAL B CB    1 
ATOM   9519  C  CG1   . VAL B 1 495 ? 125.083 150.032 167.276 1.00 13.43 ?  495 VAL B CG1   1 
ATOM   9520  C  CG2   . VAL B 1 495 ? 125.279 149.120 169.592 1.00 14.04 ?  495 VAL B CG2   1 
ATOM   9521  N  N     . ASN B 1 496 ? 122.290 152.135 167.842 1.00 25.04 ?  496 ASN B N     1 
ATOM   9522  C  CA    . ASN B 1 496 ? 121.665 153.035 166.880 1.00 14.39 ?  496 ASN B CA    1 
ATOM   9523  C  C     . ASN B 1 496 ? 121.679 154.471 167.379 1.00 17.48 ?  496 ASN B C     1 
ATOM   9524  O  O     . ASN B 1 496 ? 121.959 155.399 166.614 1.00 27.82 ?  496 ASN B O     1 
ATOM   9525  C  CB    . ASN B 1 496 ? 120.233 152.579 166.597 1.00 13.17 ?  496 ASN B CB    1 
ATOM   9526  C  CG    . ASN B 1 496 ? 119.683 153.153 165.312 1.00 14.73 ?  496 ASN B CG    1 
ATOM   9527  O  OD1   . ASN B 1 496 ? 120.389 153.250 164.312 1.00 25.58 ?  496 ASN B OD1   1 
ATOM   9528  N  ND2   . ASN B 1 496 ? 118.414 153.533 165.332 1.00 17.11 ?  496 ASN B ND2   1 
ATOM   9529  N  N     . PHE B 1 497 ? 121.381 154.673 168.665 1.00 18.74 ?  497 PHE B N     1 
ATOM   9530  C  CA    . PHE B 1 497 ? 121.374 156.014 169.235 1.00 12.68 ?  497 PHE B CA    1 
ATOM   9531  C  C     . PHE B 1 497 ? 122.733 156.675 169.087 1.00 24.73 ?  497 PHE B C     1 
ATOM   9532  O  O     . PHE B 1 497 ? 122.837 157.813 168.615 1.00 30.72 ?  497 PHE B O     1 
ATOM   9533  C  CB    . PHE B 1 497 ? 120.969 155.945 170.709 1.00 15.59 ?  497 PHE B CB    1 
ATOM   9534  C  CG    . PHE B 1 497 ? 120.886 157.283 171.383 1.00 19.96 ?  497 PHE B CG    1 
ATOM   9535  C  CD1   . PHE B 1 497 ? 119.715 158.019 171.347 1.00 29.44 ?  497 PHE B CD1   1 
ATOM   9536  C  CD2   . PHE B 1 497 ? 121.975 157.799 172.064 1.00 22.87 ?  497 PHE B CD2   1 
ATOM   9537  C  CE1   . PHE B 1 497 ? 119.637 159.247 171.968 1.00 27.07 ?  497 PHE B CE1   1 
ATOM   9538  C  CE2   . PHE B 1 497 ? 121.900 159.027 172.686 1.00 25.28 ?  497 PHE B CE2   1 
ATOM   9539  C  CZ    . PHE B 1 497 ? 120.730 159.751 172.638 1.00 28.44 ?  497 PHE B CZ    1 
ATOM   9540  N  N     . TYR B 1 498 ? 123.792 155.965 169.468 1.00 28.15 ?  498 TYR B N     1 
ATOM   9541  C  CA    . TYR B 1 498 ? 125.113 156.576 169.445 1.00 19.30 ?  498 TYR B CA    1 
ATOM   9542  C  C     . TYR B 1 498 ? 125.673 156.678 168.034 1.00 24.34 ?  498 TYR B C     1 
ATOM   9543  O  O     . TYR B 1 498 ? 126.438 157.602 167.752 1.00 35.03 ?  498 TYR B O     1 
ATOM   9544  C  CB    . TYR B 1 498 ? 126.052 155.813 170.376 1.00 20.21 ?  498 TYR B CB    1 
ATOM   9545  C  CG    . TYR B 1 498 ? 125.708 156.064 171.824 1.00 26.02 ?  498 TYR B CG    1 
ATOM   9546  C  CD1   . TYR B 1 498 ? 125.692 157.354 172.332 1.00 29.24 ?  498 TYR B CD1   1 
ATOM   9547  C  CD2   . TYR B 1 498 ? 125.362 155.021 172.669 1.00 25.53 ?  498 TYR B CD2   1 
ATOM   9548  C  CE1   . TYR B 1 498 ? 125.362 157.598 173.648 1.00 29.00 ?  498 TYR B CE1   1 
ATOM   9549  C  CE2   . TYR B 1 498 ? 125.030 155.256 173.988 1.00 26.42 ?  498 TYR B CE2   1 
ATOM   9550  C  CZ    . TYR B 1 498 ? 125.032 156.547 174.472 1.00 33.24 ?  498 TYR B CZ    1 
ATOM   9551  O  OH    . TYR B 1 498 ? 124.704 156.790 175.785 1.00 37.24 ?  498 TYR B OH    1 
ATOM   9552  N  N     . SER B 1 499 ? 125.270 155.791 167.121 1.00 18.28 ?  499 SER B N     1 
ATOM   9553  C  CA    . SER B 1 499 ? 125.684 155.949 165.731 1.00 10.43 ?  499 SER B CA    1 
ATOM   9554  C  C     . SER B 1 499 ? 125.002 157.151 165.089 1.00 18.82 ?  499 SER B C     1 
ATOM   9555  O  O     . SER B 1 499 ? 125.640 157.911 164.353 1.00 27.20 ?  499 SER B O     1 
ATOM   9556  C  CB    . SER B 1 499 ? 125.394 154.672 164.943 1.00 8.27  ?  499 SER B CB    1 
ATOM   9557  O  OG    . SER B 1 499 ? 124.017 154.552 164.646 1.00 24.13 ?  499 SER B OG    1 
ATOM   9558  N  N     . ILE B 1 500 ? 123.711 157.355 165.371 1.00 16.69 ?  500 ILE B N     1 
ATOM   9559  C  CA    . ILE B 1 500 ? 123.021 158.545 164.881 1.00 20.33 ?  500 ILE B CA    1 
ATOM   9560  C  C     . ILE B 1 500 ? 123.638 159.799 165.480 1.00 21.42 ?  500 ILE B C     1 
ATOM   9561  O  O     . ILE B 1 500 ? 123.829 160.807 164.788 1.00 26.70 ?  500 ILE B O     1 
ATOM   9562  C  CB    . ILE B 1 500 ? 121.514 158.463 165.191 1.00 24.31 ?  500 ILE B CB    1 
ATOM   9563  C  CG1   . ILE B 1 500 ? 120.855 157.341 164.399 1.00 21.83 ?  500 ILE B CG1   1 
ATOM   9564  C  CG2   . ILE B 1 500 ? 120.832 159.778 164.867 1.00 19.07 ?  500 ILE B CG2   1 
ATOM   9565  C  CD1   . ILE B 1 500 ? 119.495 156.973 164.918 1.00 18.71 ?  500 ILE B CD1   1 
ATOM   9566  N  N     . GLN B 1 501 ? 123.949 159.762 166.777 1.00 29.10 ?  501 GLN B N     1 
ATOM   9567  C  CA    . GLN B 1 501 ? 124.555 160.918 167.426 1.00 25.39 ?  501 GLN B CA    1 
ATOM   9568  C  C     . GLN B 1 501 ? 125.918 161.239 166.830 1.00 26.73 ?  501 GLN B C     1 
ATOM   9569  O  O     . GLN B 1 501 ? 126.226 162.405 166.567 1.00 39.62 ?  501 GLN B O     1 
ATOM   9570  C  CB    . GLN B 1 501 ? 124.672 160.674 168.929 1.00 30.32 ?  501 GLN B CB    1 
ATOM   9571  C  CG    . GLN B 1 501 ? 124.549 161.933 169.762 1.00 29.00 ?  501 GLN B CG    1 
ATOM   9572  C  CD    . GLN B 1 501 ? 124.673 161.660 171.241 1.00 33.80 ?  501 GLN B CD    1 
ATOM   9573  O  OE1   . GLN B 1 501 ? 125.669 161.101 171.698 1.00 39.72 ?  501 GLN B OE1   1 
ATOM   9574  N  NE2   . GLN B 1 501 ? 123.660 162.054 172.003 1.00 34.98 ?  501 GLN B NE2   1 
ATOM   9575  N  N     . ARG B 1 502 ? 126.745 160.219 166.595 1.00 31.15 ?  502 ARG B N     1 
ATOM   9576  C  CA    . ARG B 1 502 ? 128.054 160.455 165.998 1.00 23.02 ?  502 ARG B CA    1 
ATOM   9577  C  C     . ARG B 1 502 ? 127.929 160.957 164.567 1.00 22.55 ?  502 ARG B C     1 
ATOM   9578  O  O     . ARG B 1 502 ? 128.705 161.815 164.139 1.00 30.10 ?  502 ARG B O     1 
ATOM   9579  C  CB    . ARG B 1 502 ? 128.897 159.184 166.046 1.00 20.77 ?  502 ARG B CB    1 
ATOM   9580  C  CG    . ARG B 1 502 ? 130.362 159.419 165.729 1.00 25.50 ?  502 ARG B CG    1 
ATOM   9581  C  CD    . ARG B 1 502 ? 130.936 160.527 166.591 1.00 28.07 ?  502 ARG B CD    1 
ATOM   9582  N  NE    . ARG B 1 502 ? 132.241 160.968 166.117 1.00 28.04 ?  502 ARG B NE    1 
ATOM   9583  C  CZ    . ARG B 1 502 ? 132.665 162.223 166.150 1.00 27.28 ?  502 ARG B CZ    1 
ATOM   9584  N  NH1   . ARG B 1 502 ? 131.908 163.195 166.630 1.00 32.98 1  502 ARG B NH1   1 
ATOM   9585  N  NH2   . ARG B 1 502 ? 133.878 162.509 165.690 1.00 29.36 ?  502 ARG B NH2   1 
ATOM   9586  N  N     . SER B 1 503 ? 126.967 160.432 163.808 1.00 23.22 ?  503 SER B N     1 
ATOM   9587  C  CA    . SER B 1 503 ? 126.768 160.901 162.441 1.00 22.24 ?  503 SER B CA    1 
ATOM   9588  C  C     . SER B 1 503 ? 126.335 162.361 162.417 1.00 26.36 ?  503 SER B C     1 
ATOM   9589  O  O     . SER B 1 503 ? 126.829 163.151 161.605 1.00 33.93 ?  503 SER B O     1 
ATOM   9590  C  CB    . SER B 1 503 ? 125.741 160.017 161.740 1.00 16.91 ?  503 SER B CB    1 
ATOM   9591  O  OG    . SER B 1 503 ? 125.900 160.053 160.336 1.00 25.82 ?  503 SER B OG    1 
ATOM   9592  N  N     . ALA B 1 504 ? 125.423 162.744 163.312 1.00 25.08 ?  504 ALA B N     1 
ATOM   9593  C  CA    . ALA B 1 504 ? 125.010 164.140 163.392 1.00 22.29 ?  504 ALA B CA    1 
ATOM   9594  C  C     . ALA B 1 504 ? 126.151 165.029 163.869 1.00 31.28 ?  504 ALA B C     1 
ATOM   9595  O  O     . ALA B 1 504 ? 126.286 166.170 163.417 1.00 38.19 ?  504 ALA B O     1 
ATOM   9596  C  CB    . ALA B 1 504 ? 123.797 164.275 164.309 1.00 22.33 ?  504 ALA B CB    1 
ATOM   9597  N  N     . GLU B 1 505 ? 126.987 164.525 164.780 1.00 29.93 ?  505 GLU B N     1 
ATOM   9598  C  CA    . GLU B 1 505 ? 128.152 165.284 165.225 1.00 26.45 ?  505 GLU B CA    1 
ATOM   9599  C  C     . GLU B 1 505 ? 129.142 165.497 164.087 1.00 34.37 ?  505 GLU B C     1 
ATOM   9600  O  O     . GLU B 1 505 ? 129.713 166.584 163.952 1.00 39.07 ?  505 GLU B O     1 
ATOM   9601  C  CB    . GLU B 1 505 ? 128.826 164.566 166.394 1.00 26.96 ?  505 GLU B CB    1 
ATOM   9602  C  CG    . GLU B 1 505 ? 128.114 164.737 167.722 1.00 31.27 ?  505 GLU B CG    1 
ATOM   9603  C  CD    . GLU B 1 505 ? 128.490 163.666 168.726 1.00 37.60 ?  505 GLU B CD    1 
ATOM   9604  O  OE1   . GLU B 1 505 ? 129.382 162.847 168.419 1.00 39.01 ?  505 GLU B OE1   1 
ATOM   9605  O  OE2   . GLU B 1 505 ? 127.896 163.643 169.823 1.00 41.19 -1 505 GLU B OE2   1 
ATOM   9606  N  N     . ILE B 1 506 ? 129.366 164.469 163.267 1.00 32.03 ?  506 ILE B N     1 
ATOM   9607  C  CA    . ILE B 1 506 ? 130.246 164.611 162.111 1.00 26.15 ?  506 ILE B CA    1 
ATOM   9608  C  C     . ILE B 1 506 ? 129.656 165.596 161.112 1.00 26.57 ?  506 ILE B C     1 
ATOM   9609  O  O     . ILE B 1 506 ? 130.377 166.404 160.515 1.00 37.47 ?  506 ILE B O     1 
ATOM   9610  C  CB    . ILE B 1 506 ? 130.511 163.237 161.469 1.00 27.51 ?  506 ILE B CB    1 
ATOM   9611  C  CG1   . ILE B 1 506 ? 131.294 162.341 162.430 1.00 32.53 ?  506 ILE B CG1   1 
ATOM   9612  C  CG2   . ILE B 1 506 ? 131.268 163.387 160.160 1.00 24.74 ?  506 ILE B CG2   1 
ATOM   9613  C  CD1   . ILE B 1 506 ? 131.327 160.886 162.019 1.00 24.63 ?  506 ILE B CD1   1 
ATOM   9614  N  N     . ALA B 1 507 ? 128.337 165.548 160.911 1.00 29.52 ?  507 ALA B N     1 
ATOM   9615  C  CA    . ALA B 1 507 ? 127.689 166.506 160.021 1.00 29.58 ?  507 ALA B CA    1 
ATOM   9616  C  C     . ALA B 1 507 ? 127.849 167.932 160.534 1.00 31.40 ?  507 ALA B C     1 
ATOM   9617  O  O     . ALA B 1 507 ? 128.093 168.857 159.753 1.00 37.98 ?  507 ALA B O     1 
ATOM   9618  C  CB    . ALA B 1 507 ? 126.212 166.155 159.859 1.00 26.16 ?  507 ALA B CB    1 
ATOM   9619  N  N     . LYS B 1 508 ? 127.708 168.127 161.846 1.00 35.98 ?  508 LYS B N     1 
ATOM   9620  C  CA    . LYS B 1 508 ? 127.909 169.448 162.433 1.00 36.46 ?  508 LYS B CA    1 
ATOM   9621  C  C     . LYS B 1 508 ? 129.356 169.907 162.290 1.00 39.38 ?  508 LYS B C     1 
ATOM   9622  O  O     . LYS B 1 508 ? 129.614 171.079 161.995 1.00 43.84 ?  508 LYS B O     1 
ATOM   9623  C  CB    . LYS B 1 508 ? 127.492 169.429 163.903 1.00 41.04 ?  508 LYS B CB    1 
ATOM   9624  C  CG    . LYS B 1 508 ? 127.720 170.735 164.637 1.00 38.72 ?  508 LYS B CG    1 
ATOM   9625  C  CD    . LYS B 1 508 ? 127.514 170.565 166.130 1.00 39.11 ?  508 LYS B CD    1 
ATOM   9626  C  CE    . LYS B 1 508 ? 127.581 171.899 166.853 1.00 41.74 ?  508 LYS B CE    1 
ATOM   9627  N  NZ    . LYS B 1 508 ? 126.728 171.913 168.073 1.00 46.13 1  508 LYS B NZ    1 
ATOM   9628  N  N     . GLU B 1 509 ? 130.311 169.000 162.504 1.00 42.09 ?  509 GLU B N     1 
ATOM   9629  C  CA    . GLU B 1 509 ? 131.721 169.363 162.413 1.00 40.27 ?  509 GLU B CA    1 
ATOM   9630  C  C     . GLU B 1 509 ? 132.109 169.735 160.988 1.00 42.88 ?  509 GLU B C     1 
ATOM   9631  O  O     . GLU B 1 509 ? 132.802 170.736 160.769 1.00 49.18 ?  509 GLU B O     1 
ATOM   9632  C  CB    . GLU B 1 509 ? 132.590 168.213 162.919 1.00 37.70 ?  509 GLU B CB    1 
ATOM   9633  C  CG    . GLU B 1 509 ? 132.865 168.247 164.413 1.00 46.70 ?  509 GLU B CG    1 
ATOM   9634  C  CD    . GLU B 1 509 ? 133.091 166.864 164.996 1.00 50.17 ?  509 GLU B CD    1 
ATOM   9635  O  OE1   . GLU B 1 509 ? 133.670 166.008 164.295 1.00 48.52 ?  509 GLU B OE1   1 
ATOM   9636  O  OE2   . GLU B 1 509 ? 132.689 166.633 166.156 1.00 45.41 -1 509 GLU B OE2   1 
ATOM   9637  N  N     . LYS B 1 510 ? 131.678 168.944 160.010 1.00 38.56 ?  510 LYS B N     1 
ATOM   9638  C  CA    . LYS B 1 510 ? 131.998 169.198 158.614 1.00 32.84 ?  510 LYS B CA    1 
ATOM   9639  C  C     . LYS B 1 510 ? 131.014 170.141 157.936 1.00 38.42 ?  510 LYS B C     1 
ATOM   9640  O  O     . LYS B 1 510 ? 131.267 170.562 156.804 1.00 46.93 ?  510 LYS B O     1 
ATOM   9641  C  CB    . LYS B 1 510 ? 132.052 167.878 157.838 1.00 29.42 ?  510 LYS B CB    1 
ATOM   9642  C  CG    . LYS B 1 510 ? 132.970 166.838 158.451 1.00 32.23 ?  510 LYS B CG    1 
ATOM   9643  C  CD    . LYS B 1 510 ? 133.160 165.655 157.520 1.00 35.69 ?  510 LYS B CD    1 
ATOM   9644  C  CE    . LYS B 1 510 ? 134.109 164.630 158.117 1.00 39.38 ?  510 LYS B CE    1 
ATOM   9645  N  NZ    . LYS B 1 510 ? 134.825 163.859 157.067 1.00 41.14 1  510 LYS B NZ    1 
ATOM   9646  N  N     . GLY B 1 511 ? 129.910 170.480 158.596 1.00 36.32 ?  511 GLY B N     1 
ATOM   9647  C  CA    . GLY B 1 511 ? 128.916 171.348 157.999 1.00 37.95 ?  511 GLY B CA    1 
ATOM   9648  C  C     . GLY B 1 511 ? 128.190 170.766 156.811 1.00 40.49 ?  511 GLY B C     1 
ATOM   9649  O  O     . GLY B 1 511 ? 127.513 171.507 156.093 1.00 43.77 ?  511 GLY B O     1 
ATOM   9650  N  N     . GLU B 1 512 ? 128.303 169.460 156.581 1.00 34.43 ?  512 GLU B N     1 
ATOM   9651  C  CA    . GLU B 1 512 ? 127.695 168.820 155.425 1.00 30.22 ?  512 GLU B CA    1 
ATOM   9652  C  C     . GLU B 1 512 ? 127.015 167.528 155.847 1.00 31.48 ?  512 GLU B C     1 
ATOM   9653  O  O     . GLU B 1 512 ? 127.503 166.816 156.727 1.00 36.31 ?  512 GLU B O     1 
ATOM   9654  C  CB    . GLU B 1 512 ? 128.736 168.524 154.341 1.00 33.01 ?  512 GLU B CB    1 
ATOM   9655  C  CG    . GLU B 1 512 ? 129.970 167.807 154.855 1.00 32.71 ?  512 GLU B CG    1 
ATOM   9656  C  CD    . GLU B 1 512 ? 130.780 167.171 153.745 1.00 38.28 ?  512 GLU B CD    1 
ATOM   9657  O  OE1   . GLU B 1 512 ? 130.204 166.896 152.671 1.00 37.92 ?  512 GLU B OE1   1 
ATOM   9658  O  OE2   . GLU B 1 512 ? 131.991 166.943 153.948 1.00 39.66 -1 512 GLU B OE2   1 
ATOM   9659  N  N     . THR B 1 513 ? 125.887 167.238 155.214 1.00 34.26 ?  513 THR B N     1 
ATOM   9660  C  CA    . THR B 1 513 ? 125.167 165.984 155.369 1.00 32.81 ?  513 THR B CA    1 
ATOM   9661  C  C     . THR B 1 513 ? 125.385 165.134 154.122 1.00 28.84 ?  513 THR B C     1 
ATOM   9662  O  O     . THR B 1 513 ? 126.135 165.505 153.216 1.00 38.58 ?  513 THR B O     1 
ATOM   9663  C  CB    . THR B 1 513 ? 123.681 166.247 155.611 1.00 31.71 ?  513 THR B CB    1 
ATOM   9664  O  OG1   . THR B 1 513 ? 123.086 166.770 154.418 1.00 33.73 ?  513 THR B OG1   1 
ATOM   9665  C  CG2   . THR B 1 513 ? 123.505 167.253 156.726 1.00 29.90 ?  513 THR B CG2   1 
ATOM   9666  N  N     . PHE B 1 514 ? 124.727 163.980 154.074 1.00 22.87 ?  514 PHE B N     1 
ATOM   9667  C  CA    . PHE B 1 514 ? 124.818 163.198 152.854 1.00 25.65 ?  514 PHE B CA    1 
ATOM   9668  C  C     . PHE B 1 514 ? 123.877 163.771 151.801 1.00 25.87 ?  514 PHE B C     1 
ATOM   9669  O  O     . PHE B 1 514 ? 122.947 164.522 152.101 1.00 32.72 ?  514 PHE B O     1 
ATOM   9670  C  CB    . PHE B 1 514 ? 124.516 161.718 153.110 1.00 20.36 ?  514 PHE B CB    1 
ATOM   9671  C  CG    . PHE B 1 514 ? 123.117 161.437 153.584 1.00 20.87 ?  514 PHE B CG    1 
ATOM   9672  C  CD1   . PHE B 1 514 ? 122.794 161.521 154.925 1.00 18.94 ?  514 PHE B CD1   1 
ATOM   9673  C  CD2   . PHE B 1 514 ? 122.135 161.051 152.689 1.00 20.33 ?  514 PHE B CD2   1 
ATOM   9674  C  CE1   . PHE B 1 514 ? 121.517 161.243 155.362 1.00 13.71 ?  514 PHE B CE1   1 
ATOM   9675  C  CE2   . PHE B 1 514 ? 120.856 160.773 153.121 1.00 17.18 ?  514 PHE B CE2   1 
ATOM   9676  C  CZ    . PHE B 1 514 ? 120.547 160.870 154.458 1.00 16.99 ?  514 PHE B CZ    1 
ATOM   9677  N  N     . ASP B 1 515 ? 124.149 163.426 150.545 1.00 27.24 ?  515 ASP B N     1 
ATOM   9678  C  CA    . ASP B 1 515 ? 123.374 163.979 149.445 1.00 29.97 ?  515 ASP B CA    1 
ATOM   9679  C  C     . ASP B 1 515 ? 121.918 163.543 149.543 1.00 33.38 ?  515 ASP B C     1 
ATOM   9680  O  O     . ASP B 1 515 ? 121.617 162.380 149.825 1.00 43.02 ?  515 ASP B O     1 
ATOM   9681  C  CB    . ASP B 1 515 ? 123.971 163.550 148.106 1.00 31.84 ?  515 ASP B CB    1 
ATOM   9682  C  CG    . ASP B 1 515 ? 125.230 164.321 147.761 1.00 34.96 ?  515 ASP B CG    1 
ATOM   9683  O  OD1   . ASP B 1 515 ? 125.827 164.927 148.674 1.00 34.91 ?  515 ASP B OD1   1 
ATOM   9684  O  OD2   . ASP B 1 515 ? 125.622 164.322 146.576 1.00 37.22 -1 515 ASP B OD2   1 
ATOM   9685  N  N     . GLN B 1 516 ? 121.015 164.498 149.311 1.00 33.32 ?  516 GLN B N     1 
ATOM   9686  C  CA    . GLN B 1 516 ? 119.573 164.276 149.412 1.00 29.64 ?  516 GLN B CA    1 
ATOM   9687  C  C     . GLN B 1 516 ? 119.174 163.833 150.818 1.00 32.54 ?  516 GLN B C     1 
ATOM   9688  O  O     . GLN B 1 516 ? 118.270 163.014 150.997 1.00 39.69 ?  516 GLN B O     1 
ATOM   9689  C  CB    . GLN B 1 516 ? 119.090 163.269 148.365 1.00 27.02 ?  516 GLN B CB    1 
ATOM   9690  C  CG    . GLN B 1 516 ? 119.452 163.637 146.940 1.00 30.65 ?  516 GLN B CG    1 
ATOM   9691  C  CD    . GLN B 1 516 ? 119.326 162.465 145.990 1.00 38.64 ?  516 GLN B CD    1 
ATOM   9692  O  OE1   . GLN B 1 516 ? 118.231 162.137 145.533 1.00 37.40 ?  516 GLN B OE1   1 
ATOM   9693  N  NE2   . GLN B 1 516 ? 120.449 161.823 145.690 1.00 38.99 ?  516 GLN B NE2   1 
ATOM   9694  N  N     . TYR B 1 517 ? 119.859 164.374 151.828 1.00 27.08 ?  517 TYR B N     1 
ATOM   9695  C  CA    . TYR B 1 517 ? 119.465 164.109 153.207 1.00 23.87 ?  517 TYR B CA    1 
ATOM   9696  C  C     . TYR B 1 517 ? 118.130 164.766 153.534 1.00 33.52 ?  517 TYR B C     1 
ATOM   9697  O  O     . TYR B 1 517 ? 117.334 164.217 154.303 1.00 42.64 ?  517 TYR B O     1 
ATOM   9698  C  CB    . TYR B 1 517 ? 120.545 164.594 154.176 1.00 21.30 ?  517 TYR B CB    1 
ATOM   9699  C  CG    . TYR B 1 517 ? 120.009 164.968 155.542 1.00 30.35 ?  517 TYR B CG    1 
ATOM   9700  C  CD1   . TYR B 1 517 ? 119.817 164.004 156.521 1.00 21.55 ?  517 TYR B CD1   1 
ATOM   9701  C  CD2   . TYR B 1 517 ? 119.695 166.287 155.852 1.00 31.64 ?  517 TYR B CD2   1 
ATOM   9702  C  CE1   . TYR B 1 517 ? 119.324 164.339 157.765 1.00 28.97 ?  517 TYR B CE1   1 
ATOM   9703  C  CE2   . TYR B 1 517 ? 119.200 166.628 157.092 1.00 27.98 ?  517 TYR B CE2   1 
ATOM   9704  C  CZ    . TYR B 1 517 ? 119.016 165.652 158.044 1.00 32.53 ?  517 TYR B CZ    1 
ATOM   9705  O  OH    . TYR B 1 517 ? 118.526 165.992 159.282 1.00 37.96 ?  517 TYR B OH    1 
ATOM   9706  N  N     . GLU B 1 518 ? 117.875 165.944 152.962 1.00 31.78 ?  518 GLU B N     1 
ATOM   9707  C  CA    . GLU B 1 518 ? 116.705 166.736 153.326 1.00 35.03 ?  518 GLU B CA    1 
ATOM   9708  C  C     . GLU B 1 518 ? 115.395 166.010 153.054 1.00 37.14 ?  518 GLU B C     1 
ATOM   9709  O  O     . GLU B 1 518 ? 114.392 166.300 153.714 1.00 41.81 ?  518 GLU B O     1 
ATOM   9710  C  CB    . GLU B 1 518 ? 116.725 168.072 152.579 1.00 33.49 ?  518 GLU B CB    1 
ATOM   9711  C  CG    . GLU B 1 518 ? 118.086 168.759 152.553 1.00 37.43 ?  518 GLU B CG    1 
ATOM   9712  C  CD    . GLU B 1 518 ? 118.983 168.256 151.435 1.00 46.20 ?  518 GLU B CD    1 
ATOM   9713  O  OE1   . GLU B 1 518 ? 118.519 168.205 150.276 1.00 44.98 ?  518 GLU B OE1   1 
ATOM   9714  O  OE2   . GLU B 1 518 ? 120.149 167.907 151.716 1.00 40.78 -1 518 GLU B OE2   1 
ATOM   9715  N  N     . GLY B 1 519 ? 115.376 165.083 152.102 1.00 28.86 ?  519 GLY B N     1 
ATOM   9716  C  CA    . GLY B 1 519 ? 114.194 164.280 151.864 1.00 23.81 ?  519 GLY B CA    1 
ATOM   9717  C  C     . GLY B 1 519 ? 114.067 163.045 152.720 1.00 25.57 ?  519 GLY B C     1 
ATOM   9718  O  O     . GLY B 1 519 ? 113.035 162.371 152.668 1.00 33.54 ?  519 GLY B O     1 
ATOM   9719  N  N     . SER B 1 520 ? 115.086 162.732 153.516 1.00 25.82 ?  520 SER B N     1 
ATOM   9720  C  CA    . SER B 1 520 ? 115.092 161.505 154.295 1.00 23.88 ?  520 SER B CA    1 
ATOM   9721  C  C     . SER B 1 520 ? 114.156 161.611 155.495 1.00 26.94 ?  520 SER B C     1 
ATOM   9722  O  O     . SER B 1 520 ? 113.720 162.695 155.890 1.00 27.18 ?  520 SER B O     1 
ATOM   9723  C  CB    . SER B 1 520 ? 116.508 161.175 154.764 1.00 21.54 ?  520 SER B CB    1 
ATOM   9724  O  OG    . SER B 1 520 ? 117.054 162.237 155.525 1.00 26.70 ?  520 SER B OG    1 
ATOM   9725  N  N     . THR B 1 521 ? 113.842 160.450 156.075 1.00 24.19 ?  521 THR B N     1 
ATOM   9726  C  CA    . THR B 1 521 ? 113.029 160.414 157.283 1.00 24.61 ?  521 THR B CA    1 
ATOM   9727  C  C     . THR B 1 521 ? 113.768 160.975 158.487 1.00 28.11 ?  521 THR B C     1 
ATOM   9728  O  O     . THR B 1 521 ? 113.125 161.363 159.468 1.00 32.01 ?  521 THR B O     1 
ATOM   9729  C  CB    . THR B 1 521 ? 112.572 158.985 157.569 1.00 28.66 ?  521 THR B CB    1 
ATOM   9730  O  OG1   . THR B 1 521 ? 113.704 158.184 157.927 1.00 30.86 ?  521 THR B OG1   1 
ATOM   9731  C  CG2   . THR B 1 521 ? 111.909 158.390 156.344 1.00 19.23 ?  521 THR B CG2   1 
ATOM   9732  N  N     . TYR B 1 522 ? 115.101 161.015 158.439 1.00 27.68 ?  522 TYR B N     1 
ATOM   9733  C  CA    . TYR B 1 522 ? 115.856 161.707 159.477 1.00 19.35 ?  522 TYR B CA    1 
ATOM   9734  C  C     . TYR B 1 522 ? 115.541 163.196 159.482 1.00 26.13 ?  522 TYR B C     1 
ATOM   9735  O  O     . TYR B 1 522 ? 115.382 163.804 160.546 1.00 31.32 ?  522 TYR B O     1 
ATOM   9736  C  CB    . TYR B 1 522 ? 117.353 161.490 159.272 1.00 21.34 ?  522 TYR B CB    1 
ATOM   9737  C  CG    . TYR B 1 522 ? 117.790 160.047 159.301 1.00 21.56 ?  522 TYR B CG    1 
ATOM   9738  C  CD1   . TYR B 1 522 ? 117.694 159.298 160.462 1.00 20.11 ?  522 TYR B CD1   1 
ATOM   9739  C  CD2   . TYR B 1 522 ? 118.323 159.443 158.171 1.00 22.80 ?  522 TYR B CD2   1 
ATOM   9740  C  CE1   . TYR B 1 522 ? 118.108 157.986 160.497 1.00 24.06 ?  522 TYR B CE1   1 
ATOM   9741  C  CE2   . TYR B 1 522 ? 118.735 158.130 158.197 1.00 19.98 ?  522 TYR B CE2   1 
ATOM   9742  C  CZ    . TYR B 1 522 ? 118.623 157.406 159.362 1.00 25.74 ?  522 TYR B CZ    1 
ATOM   9743  O  OH    . TYR B 1 522 ? 119.032 156.096 159.392 1.00 29.11 ?  522 TYR B OH    1 
ATOM   9744  N  N     . ALA B 1 523 ? 115.459 163.802 158.296 1.00 33.00 ?  523 ALA B N     1 
ATOM   9745  C  CA    . ALA B 1 523 ? 115.188 165.231 158.202 1.00 26.34 ?  523 ALA B CA    1 
ATOM   9746  C  C     . ALA B 1 523 ? 113.775 165.559 158.665 1.00 30.52 ?  523 ALA B C     1 
ATOM   9747  O  O     . ALA B 1 523 ? 113.559 166.563 159.353 1.00 34.10 ?  523 ALA B O     1 
ATOM   9748  C  CB    . ALA B 1 523 ? 115.409 165.711 156.770 1.00 24.96 ?  523 ALA B CB    1 
ATOM   9749  N  N     . THR B 1 524 ? 112.800 164.727 158.298 1.00 30.85 ?  524 THR B N     1 
ATOM   9750  C  CA    . THR B 1 524 ? 111.414 164.973 158.670 1.00 26.94 ?  524 THR B CA    1 
ATOM   9751  C  C     . THR B 1 524 ? 111.080 164.496 160.075 1.00 34.75 ?  524 THR B C     1 
ATOM   9752  O  O     . THR B 1 524 ? 109.995 164.813 160.576 1.00 41.72 ?  524 THR B O     1 
ATOM   9753  C  CB    . THR B 1 524 ? 110.472 164.301 157.669 1.00 33.13 ?  524 THR B CB    1 
ATOM   9754  O  OG1   . THR B 1 524 ? 110.380 162.902 157.961 1.00 35.03 ?  524 THR B OG1   1 
ATOM   9755  C  CG2   . THR B 1 524 ? 110.988 164.481 156.253 1.00 32.61 ?  524 THR B CG2   1 
ATOM   9756  N  N     . GLY B 1 525 ? 111.972 163.749 160.722 1.00 29.82 ?  525 GLY B N     1 
ATOM   9757  C  CA    . GLY B 1 525 ? 111.722 163.240 162.051 1.00 27.05 ?  525 GLY B CA    1 
ATOM   9758  C  C     . GLY B 1 525 ? 110.880 161.986 162.109 1.00 33.85 ?  525 GLY B C     1 
ATOM   9759  O  O     . GLY B 1 525 ? 110.655 161.462 163.207 1.00 32.98 ?  525 GLY B O     1 
ATOM   9760  N  N     . GLU B 1 526 ? 110.406 161.487 160.965 1.00 37.62 ?  526 GLU B N     1 
ATOM   9761  C  CA    . GLU B 1 526 ? 109.612 160.265 160.950 1.00 35.57 ?  526 GLU B CA    1 
ATOM   9762  C  C     . GLU B 1 526 ? 110.425 159.055 161.389 1.00 35.56 ?  526 GLU B C     1 
ATOM   9763  O  O     . GLU B 1 526 ? 109.853 158.081 161.889 1.00 41.96 ?  526 GLU B O     1 
ATOM   9764  C  CB    . GLU B 1 526 ? 109.028 160.058 159.548 1.00 36.25 ?  526 GLU B CB    1 
ATOM   9765  C  CG    . GLU B 1 526 ? 108.386 158.705 159.299 1.00 36.93 ?  526 GLU B CG    1 
ATOM   9766  C  CD    . GLU B 1 526 ? 108.392 158.321 157.833 1.00 44.72 ?  526 GLU B CD    1 
ATOM   9767  O  OE1   . GLU B 1 526 ? 108.377 159.234 156.981 1.00 43.21 ?  526 GLU B OE1   1 
ATOM   9768  O  OE2   . GLU B 1 526 ? 108.415 157.109 157.533 1.00 42.49 -1 526 GLU B OE2   1 
ATOM   9769  N  N     . TYR B 1 527 ? 111.750 159.111 161.240 1.00 35.15 ?  527 TYR B N     1 
ATOM   9770  C  CA    . TYR B 1 527 ? 112.599 158.010 161.680 1.00 25.96 ?  527 TYR B CA    1 
ATOM   9771  C  C     . TYR B 1 527 ? 112.513 157.810 163.189 1.00 28.26 ?  527 TYR B C     1 
ATOM   9772  O  O     . TYR B 1 527 ? 112.499 156.673 163.673 1.00 35.04 ?  527 TYR B O     1 
ATOM   9773  C  CB    . TYR B 1 527 ? 114.044 158.268 161.256 1.00 23.59 ?  527 TYR B CB    1 
ATOM   9774  C  CG    . TYR B 1 527 ? 115.003 157.168 161.639 1.00 28.20 ?  527 TYR B CG    1 
ATOM   9775  C  CD1   . TYR B 1 527 ? 115.238 156.099 160.788 1.00 23.69 ?  527 TYR B CD1   1 
ATOM   9776  C  CD2   . TYR B 1 527 ? 115.676 157.198 162.854 1.00 28.68 ?  527 TYR B CD2   1 
ATOM   9777  C  CE1   . TYR B 1 527 ? 116.111 155.094 161.134 1.00 23.79 ?  527 TYR B CE1   1 
ATOM   9778  C  CE2   . TYR B 1 527 ? 116.550 156.195 163.208 1.00 24.28 ?  527 TYR B CE2   1 
ATOM   9779  C  CZ    . TYR B 1 527 ? 116.764 155.146 162.344 1.00 23.27 ?  527 TYR B CZ    1 
ATOM   9780  O  OH    . TYR B 1 527 ? 117.636 154.144 162.693 1.00 32.61 ?  527 TYR B OH    1 
ATOM   9781  N  N     . PHE B 1 528 ? 112.458 158.903 163.944 1.00 32.99 ?  528 PHE B N     1 
ATOM   9782  C  CA    . PHE B 1 528 ? 112.558 158.864 165.396 1.00 27.64 ?  528 PHE B CA    1 
ATOM   9783  C  C     . PHE B 1 528 ? 111.223 158.620 166.088 1.00 36.60 ?  528 PHE B C     1 
ATOM   9784  O  O     . PHE B 1 528 ? 111.162 158.697 167.317 1.00 46.33 ?  528 PHE B O     1 
ATOM   9785  C  CB    . PHE B 1 528 ? 113.166 160.169 165.912 1.00 30.83 ?  528 PHE B CB    1 
ATOM   9786  C  CG    . PHE B 1 528 ? 114.533 160.462 165.368 1.00 33.47 ?  528 PHE B CG    1 
ATOM   9787  C  CD1   . PHE B 1 528 ? 115.663 159.985 166.007 1.00 24.97 ?  528 PHE B CD1   1 
ATOM   9788  C  CD2   . PHE B 1 528 ? 114.689 161.221 164.221 1.00 34.19 ?  528 PHE B CD2   1 
ATOM   9789  C  CE1   . PHE B 1 528 ? 116.921 160.254 165.510 1.00 28.35 ?  528 PHE B CE1   1 
ATOM   9790  C  CE2   . PHE B 1 528 ? 115.945 161.491 163.720 1.00 33.73 ?  528 PHE B CE2   1 
ATOM   9791  C  CZ    . PHE B 1 528 ? 117.062 161.007 164.367 1.00 31.75 ?  528 PHE B CZ    1 
ATOM   9792  N  N     . ASP B 1 529 ? 110.159 158.332 165.334 1.00 37.70 ?  529 ASP B N     1 
ATOM   9793  C  CA    . ASP B 1 529 ? 108.831 158.221 165.932 1.00 35.02 ?  529 ASP B CA    1 
ATOM   9794  C  C     . ASP B 1 529 ? 108.775 157.105 166.969 1.00 38.65 ?  529 ASP B C     1 
ATOM   9795  O  O     . ASP B 1 529 ? 108.353 157.319 168.112 1.00 42.72 ?  529 ASP B O     1 
ATOM   9796  C  CB    . ASP B 1 529 ? 107.788 157.991 164.840 1.00 32.50 ?  529 ASP B CB    1 
ATOM   9797  C  CG    . ASP B 1 529 ? 107.633 159.185 163.923 1.00 43.06 ?  529 ASP B CG    1 
ATOM   9798  O  OD1   . ASP B 1 529 ? 108.115 160.280 164.281 1.00 42.20 ?  529 ASP B OD1   1 
ATOM   9799  O  OD2   . ASP B 1 529 ? 107.029 159.026 162.841 1.00 48.54 -1 529 ASP B OD2   1 
ATOM   9800  N  N     . LYS B 1 530 ? 109.208 155.901 166.588 1.00 39.76 ?  530 LYS B N     1 
ATOM   9801  C  CA    . LYS B 1 530 ? 109.180 154.777 167.514 1.00 35.45 ?  530 LYS B CA    1 
ATOM   9802  C  C     . LYS B 1 530 ? 110.164 154.947 168.660 1.00 38.94 ?  530 LYS B C     1 
ATOM   9803  O  O     . LYS B 1 530 ? 110.016 154.284 169.691 1.00 43.21 ?  530 LYS B O     1 
ATOM   9804  C  CB    . LYS B 1 530 ? 109.469 153.475 166.769 1.00 37.18 ?  530 LYS B CB    1 
ATOM   9805  C  CG    . LYS B 1 530 ? 110.926 153.058 166.792 1.00 32.74 ?  530 LYS B CG    1 
ATOM   9806  C  CD    . LYS B 1 530 ? 111.141 151.812 165.963 1.00 38.19 ?  530 LYS B CD    1 
ATOM   9807  C  CE    . LYS B 1 530 ? 112.557 151.304 166.097 1.00 34.66 ?  530 LYS B CE    1 
ATOM   9808  N  NZ    . LYS B 1 530 ? 113.098 150.939 164.765 1.00 43.09 1  530 LYS B NZ    1 
ATOM   9809  N  N     . TYR B 1 531 ? 111.160 155.813 168.508 1.00 39.67 ?  531 TYR B N     1 
ATOM   9810  C  CA    . TYR B 1 531 ? 112.127 156.043 169.569 1.00 32.48 ?  531 TYR B CA    1 
ATOM   9811  C  C     . TYR B 1 531 ? 111.683 157.128 170.535 1.00 31.41 ?  531 TYR B C     1 
ATOM   9812  O  O     . TYR B 1 531 ? 111.998 157.052 171.728 1.00 40.60 ?  531 TYR B O     1 
ATOM   9813  C  CB    . TYR B 1 531 ? 113.485 156.405 168.969 1.00 27.04 ?  531 TYR B CB    1 
ATOM   9814  C  CG    . TYR B 1 531 ? 114.217 155.228 168.372 1.00 32.01 ?  531 TYR B CG    1 
ATOM   9815  C  CD1   . TYR B 1 531 ? 114.565 154.136 169.154 1.00 26.09 ?  531 TYR B CD1   1 
ATOM   9816  C  CD2   . TYR B 1 531 ? 114.560 155.207 167.028 1.00 28.89 ?  531 TYR B CD2   1 
ATOM   9817  C  CE1   . TYR B 1 531 ? 115.235 153.060 168.616 1.00 31.55 ?  531 TYR B CE1   1 
ATOM   9818  C  CE2   . TYR B 1 531 ? 115.231 154.135 166.482 1.00 25.44 ?  531 TYR B CE2   1 
ATOM   9819  C  CZ    . TYR B 1 531 ? 115.566 153.065 167.280 1.00 31.42 ?  531 TYR B CZ    1 
ATOM   9820  O  OH    . TYR B 1 531 ? 116.235 151.992 166.744 1.00 30.43 ?  531 TYR B OH    1 
ATOM   9821  N  N     . VAL B 1 532 ? 110.961 158.139 170.046 1.00 38.40 ?  532 VAL B N     1 
ATOM   9822  C  CA    . VAL B 1 532 ? 110.383 159.150 170.927 1.00 34.75 ?  532 VAL B CA    1 
ATOM   9823  C  C     . VAL B 1 532 ? 109.037 158.729 171.487 1.00 39.86 ?  532 VAL B C     1 
ATOM   9824  O  O     . VAL B 1 532 ? 108.485 159.435 172.341 1.00 47.83 ?  532 VAL B O     1 
ATOM   9825  C  CB    . VAL B 1 532 ? 110.217 160.501 170.204 1.00 40.64 ?  532 VAL B CB    1 
ATOM   9826  C  CG1   . VAL B 1 532 ? 111.540 160.957 169.614 1.00 37.44 ?  532 VAL B CG1   1 
ATOM   9827  C  CG2   . VAL B 1 532 ? 109.147 160.400 169.129 1.00 37.46 ?  532 VAL B CG2   1 
ATOM   9828  N  N     . SER B 1 533 ? 108.485 157.606 171.029 1.00 40.67 ?  533 SER B N     1 
ATOM   9829  C  CA    . SER B 1 533 ? 107.219 157.106 171.546 1.00 40.28 ?  533 SER B CA    1 
ATOM   9830  C  C     . SER B 1 533 ? 107.352 155.863 172.411 1.00 41.24 ?  533 SER B C     1 
ATOM   9831  O  O     . SER B 1 533 ? 106.572 155.696 173.349 1.00 46.20 ?  533 SER B O     1 
ATOM   9832  C  CB    . SER B 1 533 ? 106.257 156.797 170.391 1.00 45.12 ?  533 SER B CB    1 
ATOM   9833  O  OG    . SER B 1 533 ? 106.524 155.522 169.835 1.00 46.69 ?  533 SER B OG    1 
ATOM   9834  N  N     . THR B 1 534 ? 108.315 154.991 172.124 1.00 46.10 ?  534 THR B N     1 
ATOM   9835  C  CA    . THR B 1 534 ? 108.480 153.732 172.835 1.00 41.87 ?  534 THR B CA    1 
ATOM   9836  C  C     . THR B 1 534 ? 109.782 153.750 173.623 1.00 41.15 ?  534 THR B C     1 
ATOM   9837  O  O     . THR B 1 534 ? 110.792 154.288 173.159 1.00 49.01 ?  534 THR B O     1 
ATOM   9838  C  CB    . THR B 1 534 ? 108.475 152.543 171.865 1.00 42.71 ?  534 THR B CB    1 
ATOM   9839  O  OG1   . THR B 1 534 ? 107.356 152.651 170.978 1.00 42.40 ?  534 THR B OG1   1 
ATOM   9840  C  CG2   . THR B 1 534 ? 108.386 151.227 172.622 1.00 43.68 ?  534 THR B CG2   1 
ATOM   9841  N  N     . ASP B 1 535 ? 109.751 153.161 174.814 1.00 43.04 ?  535 ASP B N     1 
ATOM   9842  C  CA    . ASP B 1 535 ? 110.930 153.021 175.657 1.00 42.66 ?  535 ASP B CA    1 
ATOM   9843  C  C     . ASP B 1 535 ? 111.575 151.668 175.390 1.00 45.35 ?  535 ASP B C     1 
ATOM   9844  O  O     . ASP B 1 535 ? 110.894 150.638 175.397 1.00 47.18 ?  535 ASP B O     1 
ATOM   9845  C  CB    . ASP B 1 535 ? 110.561 153.152 177.135 1.00 41.53 ?  535 ASP B CB    1 
ATOM   9846  C  CG    . ASP B 1 535 ? 111.778 153.243 178.032 1.00 47.31 ?  535 ASP B CG    1 
ATOM   9847  O  OD1   . ASP B 1 535 ? 112.532 154.232 177.915 1.00 48.84 ?  535 ASP B OD1   1 
ATOM   9848  O  OD2   . ASP B 1 535 ? 111.980 152.327 178.854 1.00 47.75 -1 535 ASP B OD2   1 
ATOM   9849  N  N     . PHE B 1 536 ? 112.888 151.675 175.156 1.00 40.14 ?  536 PHE B N     1 
ATOM   9850  C  CA    . PHE B 1 536 ? 113.624 150.464 174.817 1.00 34.91 ?  536 PHE B CA    1 
ATOM   9851  C  C     . PHE B 1 536 ? 114.578 150.036 175.928 1.00 35.66 ?  536 PHE B C     1 
ATOM   9852  O  O     . PHE B 1 536 ? 115.560 149.336 175.661 1.00 43.03 ?  536 PHE B O     1 
ATOM   9853  C  CB    . PHE B 1 536 ? 114.381 150.658 173.505 1.00 34.94 ?  536 PHE B CB    1 
ATOM   9854  C  CG    . PHE B 1 536 ? 113.490 150.764 172.301 1.00 31.98 ?  536 PHE B CG    1 
ATOM   9855  C  CD1   . PHE B 1 536 ? 113.103 149.632 171.608 1.00 32.97 ?  536 PHE B CD1   1 
ATOM   9856  C  CD2   . PHE B 1 536 ? 113.037 151.995 171.865 1.00 32.10 ?  536 PHE B CD2   1 
ATOM   9857  C  CE1   . PHE B 1 536 ? 112.283 149.725 170.502 1.00 31.04 ?  536 PHE B CE1   1 
ATOM   9858  C  CE2   . PHE B 1 536 ? 112.216 152.094 170.760 1.00 39.85 ?  536 PHE B CE2   1 
ATOM   9859  C  CZ    . PHE B 1 536 ? 111.839 150.956 170.078 1.00 30.69 ?  536 PHE B CZ    1 
ATOM   9860  N  N     . SER B 1 537 ? 114.313 150.449 177.164 1.00 36.35 ?  537 SER B N     1 
ATOM   9861  C  CA    . SER B 1 537 ? 115.066 149.956 178.301 1.00 34.06 ?  537 SER B CA    1 
ATOM   9862  C  C     . SER B 1 537 ? 114.728 148.487 178.548 1.00 38.38 ?  537 SER B C     1 
ATOM   9863  O  O     . SER B 1 537 ? 113.657 148.015 178.160 1.00 41.45 ?  537 SER B O     1 
ATOM   9864  C  CB    . SER B 1 537 ? 114.758 150.791 179.542 1.00 34.61 ?  537 SER B CB    1 
ATOM   9865  O  OG    . SER B 1 537 ? 113.391 150.689 179.897 1.00 39.68 ?  537 SER B OG    1 
ATOM   9866  N  N     . PRO B 1 538 ? 115.636 147.736 179.173 1.00 37.30 ?  538 PRO B N     1 
ATOM   9867  C  CA    . PRO B 1 538 ? 115.368 146.313 179.407 1.00 35.39 ?  538 PRO B CA    1 
ATOM   9868  C  C     . PRO B 1 538 ? 114.150 146.109 180.295 1.00 40.61 ?  538 PRO B C     1 
ATOM   9869  O  O     . PRO B 1 538 ? 113.905 146.868 181.234 1.00 39.18 ?  538 PRO B O     1 
ATOM   9870  C  CB    . PRO B 1 538 ? 116.650 145.816 180.087 1.00 35.57 ?  538 PRO B CB    1 
ATOM   9871  C  CG    . PRO B 1 538 ? 117.686 146.832 179.759 1.00 34.04 ?  538 PRO B CG    1 
ATOM   9872  C  CD    . PRO B 1 538 ? 116.958 148.132 179.681 1.00 36.00 ?  538 PRO B CD    1 
ATOM   9873  N  N     . LYS B 1 539 ? 113.381 145.067 179.983 1.00 45.36 ?  539 LYS B N     1 
ATOM   9874  C  CA    . LYS B 1 539 ? 112.203 144.703 180.756 1.00 45.52 ?  539 LYS B CA    1 
ATOM   9875  C  C     . LYS B 1 539 ? 112.490 143.638 181.803 1.00 47.99 ?  539 LYS B C     1 
ATOM   9876  O  O     . LYS B 1 539 ? 111.579 143.249 182.538 1.00 48.24 ?  539 LYS B O     1 
ATOM   9877  C  CB    . LYS B 1 539 ? 111.087 144.219 179.824 1.00 45.74 ?  539 LYS B CB    1 
ATOM   9878  C  CG    . LYS B 1 539 ? 111.106 144.854 178.445 1.00 43.95 ?  539 LYS B CG    1 
ATOM   9879  C  CD    . LYS B 1 539 ? 110.579 146.279 178.481 1.00 48.13 ?  539 LYS B CD    1 
ATOM   9880  C  CE    . LYS B 1 539 ? 109.811 146.615 177.213 1.00 49.03 ?  539 LYS B CE    1 
ATOM   9881  N  NZ    . LYS B 1 539 ? 110.700 146.673 176.020 1.00 49.69 1  539 LYS B NZ    1 
ATOM   9882  N  N     . TYR B 1 540 ? 113.728 143.161 181.887 1.00 45.89 ?  540 TYR B N     1 
ATOM   9883  C  CA    . TYR B 1 540 ? 114.116 142.124 182.830 1.00 43.91 ?  540 TYR B CA    1 
ATOM   9884  C  C     . TYR B 1 540 ? 115.204 142.656 183.750 1.00 46.08 ?  540 TYR B C     1 
ATOM   9885  O  O     . TYR B 1 540 ? 116.108 143.373 183.310 1.00 47.79 ?  540 TYR B O     1 
ATOM   9886  C  CB    . TYR B 1 540 ? 114.607 140.871 182.100 1.00 44.43 ?  540 TYR B CB    1 
ATOM   9887  C  CG    . TYR B 1 540 ? 113.527 140.169 181.309 1.00 47.68 ?  540 TYR B CG    1 
ATOM   9888  C  CD1   . TYR B 1 540 ? 113.245 140.538 180.001 1.00 44.57 ?  540 TYR B CD1   1 
ATOM   9889  C  CD2   . TYR B 1 540 ? 112.786 139.141 181.873 1.00 48.48 ?  540 TYR B CD2   1 
ATOM   9890  C  CE1   . TYR B 1 540 ? 112.259 139.901 179.277 1.00 43.43 ?  540 TYR B CE1   1 
ATOM   9891  C  CE2   . TYR B 1 540 ? 111.796 138.498 181.156 1.00 45.36 ?  540 TYR B CE2   1 
ATOM   9892  C  CZ    . TYR B 1 540 ? 111.537 138.882 179.859 1.00 44.75 ?  540 TYR B CZ    1 
ATOM   9893  O  OH    . TYR B 1 540 ? 110.552 138.245 179.142 1.00 49.48 ?  540 TYR B OH    1 
ATOM   9894  N  N     . GLU B 1 541 ? 115.104 142.305 185.035 1.00 49.92 ?  541 GLU B N     1 
ATOM   9895  C  CA    . GLU B 1 541 ? 116.076 142.782 186.013 1.00 45.77 ?  541 GLU B CA    1 
ATOM   9896  C  C     . GLU B 1 541 ? 117.474 142.261 185.703 1.00 46.72 ?  541 GLU B C     1 
ATOM   9897  O  O     . GLU B 1 541 ? 118.465 142.978 185.888 1.00 46.88 ?  541 GLU B O     1 
ATOM   9898  C  CB    . GLU B 1 541 ? 115.648 142.372 187.421 1.00 46.79 ?  541 GLU B CB    1 
ATOM   9899  C  CG    . GLU B 1 541 ? 116.479 142.993 188.530 1.00 48.67 ?  541 GLU B CG    1 
ATOM   9900  C  CD    . GLU B 1 541 ? 117.302 141.968 189.286 1.00 53.09 ?  541 GLU B CD    1 
ATOM   9901  O  OE1   . GLU B 1 541 ? 117.099 140.757 189.057 1.00 50.43 ?  541 GLU B OE1   1 
ATOM   9902  O  OE2   . GLU B 1 541 ? 118.150 142.373 190.107 1.00 53.20 -1 541 GLU B OE2   1 
ATOM   9903  N  N     . LYS B 1 542 ? 117.575 141.012 185.243 1.00 43.44 ?  542 LYS B N     1 
ATOM   9904  C  CA    . LYS B 1 542 ? 118.878 140.460 184.884 1.00 39.82 ?  542 LYS B CA    1 
ATOM   9905  C  C     . LYS B 1 542 ? 119.506 141.229 183.729 1.00 44.78 ?  542 LYS B C     1 
ATOM   9906  O  O     . LYS B 1 542 ? 120.706 141.528 183.752 1.00 42.69 ?  542 LYS B O     1 
ATOM   9907  C  CB    . LYS B 1 542 ? 118.740 138.980 184.528 1.00 41.29 ?  542 LYS B CB    1 
ATOM   9908  C  CG    . LYS B 1 542 ? 120.023 138.344 184.024 1.00 43.38 ?  542 LYS B CG    1 
ATOM   9909  C  CD    . LYS B 1 542 ? 119.871 136.842 183.853 1.00 41.03 ?  542 LYS B CD    1 
ATOM   9910  C  CE    . LYS B 1 542 ? 121.206 136.190 183.533 1.00 44.05 ?  542 LYS B CE    1 
ATOM   9911  N  NZ    . LYS B 1 542 ? 121.125 134.706 183.589 1.00 44.68 1  542 LYS B NZ    1 
ATOM   9912  N  N     . ILE B 1 543 ? 118.711 141.559 182.710 1.00 43.71 ?  543 ILE B N     1 
ATOM   9913  C  CA    . ILE B 1 543 ? 119.233 142.314 181.576 1.00 37.51 ?  543 ILE B CA    1 
ATOM   9914  C  C     . ILE B 1 543 ? 119.562 143.742 181.989 1.00 37.39 ?  543 ILE B C     1 
ATOM   9915  O  O     . ILE B 1 543 ? 120.581 144.304 181.571 1.00 37.90 ?  543 ILE B O     1 
ATOM   9916  C  CB    . ILE B 1 543 ? 118.235 142.277 180.406 1.00 36.35 ?  543 ILE B CB    1 
ATOM   9917  C  CG1   . ILE B 1 543 ? 117.885 140.833 180.044 1.00 39.05 ?  543 ILE B CG1   1 
ATOM   9918  C  CG2   . ILE B 1 543 ? 118.807 143.001 179.205 1.00 36.17 ?  543 ILE B CG2   1 
ATOM   9919  C  CD1   . ILE B 1 543 ? 119.087 139.939 179.851 1.00 33.21 ?  543 ILE B CD1   1 
ATOM   9920  N  N     . ALA B 1 544 ? 118.707 144.355 182.812 1.00 35.49 ?  544 ALA B N     1 
ATOM   9921  C  CA    . ALA B 1 544 ? 118.979 145.709 183.282 1.00 39.29 ?  544 ALA B CA    1 
ATOM   9922  C  C     . ALA B 1 544 ? 120.246 145.765 184.124 1.00 44.33 ?  544 ALA B C     1 
ATOM   9923  O  O     . ALA B 1 544 ? 120.906 146.808 184.184 1.00 48.55 ?  544 ALA B O     1 
ATOM   9924  C  CB    . ALA B 1 544 ? 117.788 146.239 184.079 1.00 40.47 ?  544 ALA B CB    1 
ATOM   9925  N  N     . ASN B 1 545 ? 120.601 144.658 184.781 1.00 45.04 ?  545 ASN B N     1 
ATOM   9926  C  CA    . ASN B 1 545 ? 121.850 144.613 185.531 1.00 45.81 ?  545 ASN B CA    1 
ATOM   9927  C  C     . ASN B 1 545 ? 123.055 144.515 184.607 1.00 44.60 ?  545 ASN B C     1 
ATOM   9928  O  O     . ASN B 1 545 ? 124.158 144.931 184.982 1.00 46.40 ?  545 ASN B O     1 
ATOM   9929  C  CB    . ASN B 1 545 ? 121.837 143.440 186.510 1.00 47.28 ?  545 ASN B CB    1 
ATOM   9930  C  CG    . ASN B 1 545 ? 120.981 143.711 187.730 1.00 49.62 ?  545 ASN B CG    1 
ATOM   9931  O  OD1   . ASN B 1 545 ? 120.799 144.860 188.131 1.00 48.80 ?  545 ASN B OD1   1 
ATOM   9932  N  ND2   . ASN B 1 545 ? 120.453 142.651 188.331 1.00 44.89 ?  545 ASN B ND2   1 
ATOM   9933  N  N     . LEU B 1 546 ? 122.871 143.965 183.404 1.00 44.21 ?  546 LEU B N     1 
ATOM   9934  C  CA    . LEU B 1 546 ? 123.972 143.882 182.451 1.00 37.40 ?  546 LEU B CA    1 
ATOM   9935  C  C     . LEU B 1 546 ? 124.429 145.262 182.002 1.00 37.79 ?  546 LEU B C     1 
ATOM   9936  O  O     . LEU B 1 546 ? 125.604 145.450 181.672 1.00 39.54 ?  546 LEU B O     1 
ATOM   9937  C  CB    . LEU B 1 546 ? 123.559 143.044 181.241 1.00 36.36 ?  546 LEU B CB    1 
ATOM   9938  C  CG    . LEU B 1 546 ? 123.175 141.587 181.499 1.00 38.55 ?  546 LEU B CG    1 
ATOM   9939  C  CD1   . LEU B 1 546 ? 122.701 140.932 180.215 1.00 37.37 ?  546 LEU B CD1   1 
ATOM   9940  C  CD2   . LEU B 1 546 ? 124.341 140.819 182.094 1.00 37.55 ?  546 LEU B CD2   1 
ATOM   9941  N  N     . PHE B 1 547 ? 123.522 146.238 181.995 1.00 39.72 ?  547 PHE B N     1 
ATOM   9942  C  CA    . PHE B 1 547 ? 123.824 147.594 181.559 1.00 38.97 ?  547 PHE B CA    1 
ATOM   9943  C  C     . PHE B 1 547 ? 124.146 148.520 182.724 1.00 40.70 ?  547 PHE B C     1 
ATOM   9944  O  O     . PHE B 1 547 ? 124.081 149.744 182.570 1.00 44.69 ?  547 PHE B O     1 
ATOM   9945  C  CB    . PHE B 1 547 ? 122.657 148.158 180.746 1.00 37.62 ?  547 PHE B CB    1 
ATOM   9946  C  CG    . PHE B 1 547 ? 122.454 147.480 179.421 1.00 39.12 ?  547 PHE B CG    1 
ATOM   9947  C  CD1   . PHE B 1 547 ? 121.643 146.364 179.316 1.00 37.61 ?  547 PHE B CD1   1 
ATOM   9948  C  CD2   . PHE B 1 547 ? 123.071 147.961 178.280 1.00 38.44 ?  547 PHE B CD2   1 
ATOM   9949  C  CE1   . PHE B 1 547 ? 121.454 145.741 178.098 1.00 38.08 ?  547 PHE B CE1   1 
ATOM   9950  C  CE2   . PHE B 1 547 ? 122.885 147.342 177.061 1.00 33.49 ?  547 PHE B CE2   1 
ATOM   9951  C  CZ    . PHE B 1 547 ? 122.076 146.231 176.971 1.00 35.40 ?  547 PHE B CZ    1 
ATOM   9952  N  N     . GLU B 1 548 ? 124.480 147.963 183.886 1.00 47.33 ?  548 GLU B N     1 
ATOM   9953  C  CA    . GLU B 1 548 ? 124.818 148.781 185.041 1.00 48.82 ?  548 GLU B CA    1 
ATOM   9954  C  C     . GLU B 1 548 ? 126.067 149.607 184.760 1.00 52.47 ?  548 GLU B C     1 
ATOM   9955  O  O     . GLU B 1 548 ? 127.017 149.134 184.131 1.00 52.34 ?  548 GLU B O     1 
ATOM   9956  C  CB    . GLU B 1 548 ? 125.035 147.898 186.270 1.00 47.67 ?  548 GLU B CB    1 
ATOM   9957  C  CG    . GLU B 1 548 ? 123.788 147.682 187.111 1.00 50.67 ?  548 GLU B CG    1 
ATOM   9958  C  CD    . GLU B 1 548 ? 123.960 146.570 188.127 1.00 56.24 ?  548 GLU B CD    1 
ATOM   9959  O  OE1   . GLU B 1 548 ? 124.845 145.712 187.927 1.00 55.02 ?  548 GLU B OE1   1 
ATOM   9960  O  OE2   . GLU B 1 548 ? 123.212 146.554 189.128 1.00 55.23 -1 548 GLU B OE2   1 
ATOM   9961  N  N     . GLY B 1 549 ? 126.060 150.851 185.229 1.00 50.26 ?  549 GLY B N     1 
ATOM   9962  C  CA    . GLY B 1 549 ? 127.146 151.764 184.942 1.00 49.92 ?  549 GLY B CA    1 
ATOM   9963  C  C     . GLY B 1 549 ? 127.138 152.328 183.543 1.00 51.73 ?  549 GLY B C     1 
ATOM   9964  O  O     . GLY B 1 549 ? 128.148 152.895 183.113 1.00 54.70 ?  549 GLY B O     1 
ATOM   9965  N  N     . MET B 1 550 ? 126.031 152.189 182.818 1.00 48.89 ?  550 MET B N     1 
ATOM   9966  C  CA    . MET B 1 550 ? 125.927 152.639 181.438 1.00 44.47 ?  550 MET B CA    1 
ATOM   9967  C  C     . MET B 1 550 ? 124.567 153.285 181.237 1.00 46.73 ?  550 MET B C     1 
ATOM   9968  O  O     . MET B 1 550 ? 123.539 152.670 181.528 1.00 52.25 ?  550 MET B O     1 
ATOM   9969  C  CB    . MET B 1 550 ? 126.112 151.468 180.470 1.00 44.64 ?  550 MET B CB    1 
ATOM   9970  C  CG    . MET B 1 550 ? 126.843 151.821 179.195 1.00 51.54 ?  550 MET B CG    1 
ATOM   9971  S  SD    . MET B 1 550 ? 126.961 150.414 178.080 1.00 60.33 ?  550 MET B SD    1 
ATOM   9972  C  CE    . MET B 1 550 ? 126.915 149.046 179.232 1.00 48.02 ?  550 MET B CE    1 
ATOM   9973  N  N     . HIS B 1 551 ? 124.563 154.519 180.741 1.00 42.96 ?  551 HIS B N     1 
ATOM   9974  C  CA    . HIS B 1 551 ? 123.318 155.250 180.554 1.00 43.58 ?  551 HIS B CA    1 
ATOM   9975  C  C     . HIS B 1 551 ? 122.592 154.728 179.321 1.00 46.12 ?  551 HIS B C     1 
ATOM   9976  O  O     . HIS B 1 551 ? 123.088 154.857 178.197 1.00 44.91 ?  551 HIS B O     1 
ATOM   9977  C  CB    . HIS B 1 551 ? 123.583 156.747 180.422 1.00 41.99 ?  551 HIS B CB    1 
ATOM   9978  C  CG    . HIS B 1 551 ? 122.378 157.535 180.015 1.00 46.24 ?  551 HIS B CG    1 
ATOM   9979  N  ND1   . HIS B 1 551 ? 121.403 157.918 180.911 1.00 49.73 ?  551 HIS B ND1   1 
ATOM   9980  C  CD2   . HIS B 1 551 ? 121.986 158.006 178.808 1.00 46.93 ?  551 HIS B CD2   1 
ATOM   9981  C  CE1   . HIS B 1 551 ? 120.463 158.592 180.273 1.00 47.40 ?  551 HIS B CE1   1 
ATOM   9982  N  NE2   . HIS B 1 551 ? 120.794 158.661 178.997 1.00 46.40 ?  551 HIS B NE2   1 
ATOM   9983  N  N     . ILE B 1 552 ? 121.421 154.140 179.533 1.00 40.04 ?  552 ILE B N     1 
ATOM   9984  C  CA    . ILE B 1 552 ? 120.574 153.660 178.448 1.00 37.77 ?  552 ILE B CA    1 
ATOM   9985  C  C     . ILE B 1 552 ? 119.746 154.841 177.944 1.00 38.12 ?  552 ILE B C     1 
ATOM   9986  O  O     . ILE B 1 552 ? 119.045 155.472 178.751 1.00 37.71 ?  552 ILE B O     1 
ATOM   9987  C  CB    . ILE B 1 552 ? 119.671 152.512 178.909 1.00 36.38 ?  552 ILE B CB    1 
ATOM   9988  C  CG1   . ILE B 1 552 ? 120.522 151.344 179.406 1.00 35.67 ?  552 ILE B CG1   1 
ATOM   9989  C  CG2   . ILE B 1 552 ? 118.752 152.066 177.784 1.00 36.34 ?  552 ILE B CG2   1 
ATOM   9990  C  CD1   . ILE B 1 552 ? 119.745 150.314 180.180 1.00 38.89 ?  552 ILE B CD1   1 
ATOM   9991  N  N     . PRO B 1 553 ? 119.813 155.180 176.657 1.00 40.67 ?  553 PRO B N     1 
ATOM   9992  C  CA    . PRO B 1 553 ? 119.050 156.330 176.159 1.00 37.77 ?  553 PRO B CA    1 
ATOM   9993  C  C     . PRO B 1 553 ? 117.558 156.161 176.400 1.00 40.06 ?  553 PRO B C     1 
ATOM   9994  O  O     . PRO B 1 553 ? 116.992 155.086 176.199 1.00 41.00 ?  553 PRO B O     1 
ATOM   9995  C  CB    . PRO B 1 553 ? 119.378 156.349 174.663 1.00 34.16 ?  553 PRO B CB    1 
ATOM   9996  C  CG    . PRO B 1 553 ? 120.687 155.653 174.559 1.00 32.33 ?  553 PRO B CG    1 
ATOM   9997  C  CD    . PRO B 1 553 ? 120.679 154.599 175.620 1.00 33.34 ?  553 PRO B CD    1 
ATOM   9998  N  N     . THR B 1 554 ? 116.926 157.247 176.829 1.00 43.12 ?  554 THR B N     1 
ATOM   9999  C  CA    . THR B 1 554 ? 115.509 157.257 177.138 1.00 41.44 ?  554 THR B CA    1 
ATOM   10000 C  C     . THR B 1 554 ? 114.736 157.932 176.011 1.00 38.99 ?  554 THR B C     1 
ATOM   10001 O  O     . THR B 1 554 ? 115.283 158.285 174.964 1.00 37.79 ?  554 THR B O     1 
ATOM   10002 C  CB    . THR B 1 554 ? 115.256 157.962 178.472 1.00 37.55 ?  554 THR B CB    1 
ATOM   10003 O  OG1   . THR B 1 554 ? 115.421 159.375 178.304 1.00 43.39 ?  554 THR B OG1   1 
ATOM   10004 C  CG2   . THR B 1 554 ? 116.231 157.468 179.526 1.00 36.57 ?  554 THR B CG2   1 
ATOM   10005 N  N     . THR B 1 555 ? 113.432 158.102 176.232 1.00 42.76 ?  555 THR B N     1 
ATOM   10006 C  CA    . THR B 1 555 ? 112.605 158.817 175.269 1.00 39.77 ?  555 THR B CA    1 
ATOM   10007 C  C     . THR B 1 555 ? 113.027 160.279 175.162 1.00 40.86 ?  555 THR B C     1 
ATOM   10008 O  O     . THR B 1 555 ? 113.061 160.842 174.062 1.00 44.26 ?  555 THR B O     1 
ATOM   10009 C  CB    . THR B 1 555 ? 111.132 158.694 175.661 1.00 43.88 ?  555 THR B CB    1 
ATOM   10010 O  OG1   . THR B 1 555 ? 110.647 157.399 175.284 1.00 42.11 ?  555 THR B OG1   1 
ATOM   10011 C  CG2   . THR B 1 555 ? 110.294 159.758 174.979 1.00 42.31 ?  555 THR B CG2   1 
ATOM   10012 N  N     . GLU B 1 556 ? 113.362 160.908 176.290 1.00 37.54 ?  556 GLU B N     1 
ATOM   10013 C  CA    . GLU B 1 556 ? 113.834 162.289 176.257 1.00 41.22 ?  556 GLU B CA    1 
ATOM   10014 C  C     . GLU B 1 556 ? 115.176 162.400 175.542 1.00 41.20 ?  556 GLU B C     1 
ATOM   10015 O  O     . GLU B 1 556 ? 115.412 163.360 174.799 1.00 45.19 ?  556 GLU B O     1 
ATOM   10016 C  CB    . GLU B 1 556 ? 113.929 162.846 177.676 1.00 42.16 ?  556 GLU B CB    1 
ATOM   10017 C  CG    . GLU B 1 556 ? 112.582 163.079 178.346 1.00 43.79 ?  556 GLU B CG    1 
ATOM   10018 C  CD    . GLU B 1 556 ? 111.547 163.661 177.400 1.00 46.68 ?  556 GLU B CD    1 
ATOM   10019 O  OE1   . GLU B 1 556 ? 111.551 164.893 177.198 1.00 44.65 ?  556 GLU B OE1   1 
ATOM   10020 O  OE2   . GLU B 1 556 ? 110.723 162.889 176.865 1.00 46.96 -1 556 GLU B OE2   1 
ATOM   10021 N  N     . ASP B 1 557 ? 116.071 161.433 175.761 1.00 39.92 ?  557 ASP B N     1 
ATOM   10022 C  CA    . ASP B 1 557 ? 117.337 161.421 175.037 1.00 35.53 ?  557 ASP B CA    1 
ATOM   10023 C  C     . ASP B 1 557 ? 117.107 161.281 173.539 1.00 36.19 ?  557 ASP B C     1 
ATOM   10024 O  O     . ASP B 1 557 ? 117.788 161.926 172.734 1.00 39.67 ?  557 ASP B O     1 
ATOM   10025 C  CB    . ASP B 1 557 ? 118.227 160.289 175.548 1.00 35.05 ?  557 ASP B CB    1 
ATOM   10026 C  CG    . ASP B 1 557 ? 118.690 160.509 176.972 1.00 42.94 ?  557 ASP B CG    1 
ATOM   10027 O  OD1   . ASP B 1 557 ? 119.271 161.578 177.250 1.00 44.87 ?  557 ASP B OD1   1 
ATOM   10028 O  OD2   . ASP B 1 557 ? 118.475 159.612 177.812 1.00 43.75 -1 557 ASP B OD2   1 
ATOM   10029 N  N     . TRP B 1 558 ? 116.145 160.446 173.146 1.00 30.30 ?  558 TRP B N     1 
ATOM   10030 C  CA    . TRP B 1 558 ? 115.835 160.297 171.730 1.00 26.01 ?  558 TRP B CA    1 
ATOM   10031 C  C     . TRP B 1 558 ? 115.204 161.557 171.152 1.00 31.95 ?  558 TRP B C     1 
ATOM   10032 O  O     . TRP B 1 558 ? 115.454 161.890 169.991 1.00 37.89 ?  558 TRP B O     1 
ATOM   10033 C  CB    . TRP B 1 558 ? 114.924 159.091 171.522 1.00 32.42 ?  558 TRP B CB    1 
ATOM   10034 C  CG    . TRP B 1 558 ? 115.678 157.816 171.340 1.00 28.63 ?  558 TRP B CG    1 
ATOM   10035 C  CD1   . TRP B 1 558 ? 115.793 156.797 172.237 1.00 25.06 ?  558 TRP B CD1   1 
ATOM   10036 C  CD2   . TRP B 1 558 ? 116.426 157.421 170.186 1.00 29.59 ?  558 TRP B CD2   1 
ATOM   10037 N  NE1   . TRP B 1 558 ? 116.565 155.791 171.712 1.00 31.93 ?  558 TRP B NE1   1 
ATOM   10038 C  CE2   . TRP B 1 558 ? 116.964 156.148 170.452 1.00 29.94 ?  558 TRP B CE2   1 
ATOM   10039 C  CE3   . TRP B 1 558 ? 116.685 158.017 168.948 1.00 30.69 ?  558 TRP B CE3   1 
ATOM   10040 C  CZ2   . TRP B 1 558 ? 117.747 155.463 169.529 1.00 25.80 ?  558 TRP B CZ2   1 
ATOM   10041 C  CZ3   . TRP B 1 558 ? 117.464 157.337 168.036 1.00 28.24 ?  558 TRP B CZ3   1 
ATOM   10042 C  CH2   . TRP B 1 558 ? 117.985 156.073 168.330 1.00 23.67 ?  558 TRP B CH2   1 
ATOM   10043 N  N     . LYS B 1 559 ? 114.389 162.269 171.933 1.00 36.67 ?  559 LYS B N     1 
ATOM   10044 C  CA    . LYS B 1 559 ? 113.862 163.550 171.470 1.00 34.56 ?  559 LYS B CA    1 
ATOM   10045 C  C     . LYS B 1 559 ? 114.979 164.570 171.285 1.00 37.87 ?  559 LYS B C     1 
ATOM   10046 O  O     . LYS B 1 559 ? 114.979 165.335 170.311 1.00 38.90 ?  559 LYS B O     1 
ATOM   10047 C  CB    . LYS B 1 559 ? 112.816 164.076 172.450 1.00 37.71 ?  559 LYS B CB    1 
ATOM   10048 C  CG    . LYS B 1 559 ? 111.473 163.381 172.356 1.00 42.19 ?  559 LYS B CG    1 
ATOM   10049 C  CD    . LYS B 1 559 ? 110.544 163.829 173.469 1.00 38.05 ?  559 LYS B CD    1 
ATOM   10050 C  CE    . LYS B 1 559 ? 109.318 162.942 173.553 1.00 41.69 ?  559 LYS B CE    1 
ATOM   10051 N  NZ    . LYS B 1 559 ? 108.767 162.894 174.935 1.00 39.05 1  559 LYS B NZ    1 
ATOM   10052 N  N     . LYS B 1 560 ? 115.937 164.597 172.212 1.00 34.00 ?  560 LYS B N     1 
ATOM   10053 C  CA    . LYS B 1 560 ? 117.084 165.485 172.066 1.00 33.62 ?  560 LYS B CA    1 
ATOM   10054 C  C     . LYS B 1 560 ? 117.900 165.127 170.829 1.00 38.20 ?  560 LYS B C     1 
ATOM   10055 O  O     . LYS B 1 560 ? 118.360 166.014 170.102 1.00 42.72 ?  560 LYS B O     1 
ATOM   10056 C  CB    . LYS B 1 560 ? 117.954 165.429 173.321 1.00 37.36 ?  560 LYS B CB    1 
ATOM   10057 C  CG    . LYS B 1 560 ? 117.515 166.380 174.419 1.00 37.70 ?  560 LYS B CG    1 
ATOM   10058 C  CD    . LYS B 1 560 ? 118.257 166.105 175.716 1.00 42.97 ?  560 LYS B CD    1 
ATOM   10059 C  CE    . LYS B 1 560 ? 117.326 166.193 176.913 1.00 39.49 ?  560 LYS B CE    1 
ATOM   10060 N  NZ    . LYS B 1 560 ? 117.414 164.981 177.774 1.00 44.10 1  560 LYS B NZ    1 
ATOM   10061 N  N     . LEU B 1 561 ? 118.086 163.831 170.575 1.00 36.05 ?  561 LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 561 ? 118.793 163.404 169.371 1.00 30.62 ?  561 LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 561 ? 118.026 163.788 168.112 1.00 34.86 ?  561 LEU B C     1 
ATOM   10064 O  O     . LEU B 1 561 ? 118.630 164.172 167.106 1.00 39.07 ?  561 LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 561 ? 119.038 161.897 169.408 1.00 30.75 ?  561 LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 561 ? 119.851 161.347 168.236 1.00 32.12 ?  561 LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 561 ? 121.174 162.079 168.129 1.00 28.52 ?  561 LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 561 ? 120.071 159.856 168.382 1.00 29.41 ?  561 LEU B CD2   1 
ATOM   10069 N  N     . LYS B 1 562 ? 116.698 163.673 168.144 1.00 30.80 ?  562 LYS B N     1 
ATOM   10070 C  CA    . LYS B 1 562 ? 115.884 164.080 167.003 1.00 32.43 ?  562 LYS B CA    1 
ATOM   10071 C  C     . LYS B 1 562 ? 116.033 165.569 166.725 1.00 37.34 ?  562 LYS B C     1 
ATOM   10072 O  O     . LYS B 1 562 ? 116.182 165.983 165.569 1.00 41.07 ?  562 LYS B O     1 
ATOM   10073 C  CB    . LYS B 1 562 ? 114.421 163.723 167.264 1.00 30.73 ?  562 LYS B CB    1 
ATOM   10074 C  CG    . LYS B 1 562 ? 113.446 164.227 166.221 1.00 31.43 ?  562 LYS B CG    1 
ATOM   10075 C  CD    . LYS B 1 562 ? 112.020 163.930 166.645 1.00 29.50 ?  562 LYS B CD    1 
ATOM   10076 C  CE    . LYS B 1 562 ? 111.029 164.244 165.543 1.00 35.36 ?  562 LYS B CE    1 
ATOM   10077 N  NZ    . LYS B 1 562 ? 109.728 163.561 165.775 1.00 39.56 1  562 LYS B NZ    1 
ATOM   10078 N  N     . ALA B 1 563 ? 116.008 166.388 167.778 1.00 33.87 ?  563 ALA B N     1 
ATOM   10079 C  CA    . ALA B 1 563 ? 116.218 167.822 167.604 1.00 30.54 ?  563 ALA B CA    1 
ATOM   10080 C  C     . ALA B 1 563 ? 117.615 168.114 167.070 1.00 33.60 ?  563 ALA B C     1 
ATOM   10081 O  O     . ALA B 1 563 ? 117.789 168.973 166.198 1.00 40.23 ?  563 ALA B O     1 
ATOM   10082 C  CB    . ALA B 1 563 ? 115.984 168.551 168.926 1.00 34.80 ?  563 ALA B CB    1 
ATOM   10083 N  N     . PHE B 1 564 ? 118.624 167.403 167.581 1.00 36.35 ?  564 PHE B N     1 
ATOM   10084 C  CA    . PHE B 1 564 ? 119.993 167.602 167.119 1.00 31.55 ?  564 PHE B CA    1 
ATOM   10085 C  C     . PHE B 1 564 ? 120.139 167.238 165.647 1.00 36.66 ?  564 PHE B C     1 
ATOM   10086 O  O     . PHE B 1 564 ? 120.826 167.937 164.893 1.00 41.78 ?  564 PHE B O     1 
ATOM   10087 C  CB    . PHE B 1 564 ? 120.949 166.774 167.979 1.00 32.48 ?  564 PHE B CB    1 
ATOM   10088 C  CG    . PHE B 1 564 ? 122.392 167.147 167.817 1.00 35.64 ?  564 PHE B CG    1 
ATOM   10089 C  CD1   . PHE B 1 564 ? 122.903 168.277 168.431 1.00 35.29 ?  564 PHE B CD1   1 
ATOM   10090 C  CD2   . PHE B 1 564 ? 123.242 166.362 167.059 1.00 39.70 ?  564 PHE B CD2   1 
ATOM   10091 C  CE1   . PHE B 1 564 ? 124.233 168.618 168.287 1.00 41.01 ?  564 PHE B CE1   1 
ATOM   10092 C  CE2   . PHE B 1 564 ? 124.571 166.699 166.910 1.00 38.51 ?  564 PHE B CE2   1 
ATOM   10093 C  CZ    . PHE B 1 564 ? 125.068 167.829 167.524 1.00 38.19 ?  564 PHE B CZ    1 
ATOM   10094 N  N     . VAL B 1 565 ? 119.503 166.147 165.222 1.00 32.89 ?  565 VAL B N     1 
ATOM   10095 C  CA    . VAL B 1 565 ? 119.584 165.727 163.827 1.00 29.38 ?  565 VAL B CA    1 
ATOM   10096 C  C     . VAL B 1 565 ? 118.834 166.704 162.931 1.00 35.25 ?  565 VAL B C     1 
ATOM   10097 O  O     . VAL B 1 565 ? 119.280 167.017 161.821 1.00 39.02 ?  565 VAL B O     1 
ATOM   10098 C  CB    . VAL B 1 565 ? 119.057 164.288 163.678 1.00 29.93 ?  565 VAL B CB    1 
ATOM   10099 C  CG1   . VAL B 1 565 ? 118.724 163.978 162.227 1.00 32.07 ?  565 VAL B CG1   1 
ATOM   10100 C  CG2   . VAL B 1 565 ? 120.077 163.303 164.210 1.00 32.11 ?  565 VAL B CG2   1 
ATOM   10101 N  N     . ALA B 1 566 ? 117.690 167.208 163.397 1.00 36.92 ?  566 ALA B N     1 
ATOM   10102 C  CA    . ALA B 1 566 ? 116.965 168.211 162.625 1.00 34.67 ?  566 ALA B CA    1 
ATOM   10103 C  C     . ALA B 1 566 ? 117.785 169.484 162.471 1.00 37.50 ?  566 ALA B C     1 
ATOM   10104 O  O     . ALA B 1 566 ? 117.776 170.114 161.408 1.00 43.33 ?  566 ALA B O     1 
ATOM   10105 C  CB    . ALA B 1 566 ? 115.622 168.514 163.288 1.00 34.64 ?  566 ALA B CB    1 
ATOM   10106 N  N     . GLU B 1 567 ? 118.500 169.881 163.524 1.00 38.02 ?  567 GLU B N     1 
ATOM   10107 C  CA    . GLU B 1 567 ? 119.282 171.110 163.470 1.00 37.40 ?  567 GLU B CA    1 
ATOM   10108 C  C     . GLU B 1 567 ? 120.521 170.950 162.595 1.00 42.54 ?  567 GLU B C     1 
ATOM   10109 O  O     . GLU B 1 567 ? 120.820 171.814 161.763 1.00 50.47 ?  567 GLU B O     1 
ATOM   10110 C  CB    . GLU B 1 567 ? 119.678 171.534 164.883 1.00 39.50 ?  567 GLU B CB    1 
ATOM   10111 C  CG    . GLU B 1 567 ? 120.416 172.857 164.949 1.00 42.29 ?  567 GLU B CG    1 
ATOM   10112 C  CD    . GLU B 1 567 ? 120.956 173.147 166.335 1.00 49.53 ?  567 GLU B CD    1 
ATOM   10113 O  OE1   . GLU B 1 567 ? 120.495 172.501 167.299 1.00 50.64 ?  567 GLU B OE1   1 
ATOM   10114 O  OE2   . GLU B 1 567 ? 121.836 174.023 166.461 1.00 46.30 -1 567 GLU B OE2   1 
ATOM   10115 N  N     . HIS B 1 568 ? 121.255 169.849 162.764 1.00 44.69 ?  568 HIS B N     1 
ATOM   10116 C  CA    . HIS B 1 568 ? 122.577 169.713 162.172 1.00 40.43 ?  568 HIS B CA    1 
ATOM   10117 C  C     . HIS B 1 568 ? 122.647 168.708 161.033 1.00 35.70 ?  568 HIS B C     1 
ATOM   10118 O  O     . HIS B 1 568 ? 123.664 168.666 160.332 1.00 44.65 ?  568 HIS B O     1 
ATOM   10119 C  CB    . HIS B 1 568 ? 123.597 169.317 163.248 1.00 39.32 ?  568 HIS B CB    1 
ATOM   10120 C  CG    . HIS B 1 568 ? 123.844 170.385 164.266 1.00 39.80 ?  568 HIS B CG    1 
ATOM   10121 N  ND1   . HIS B 1 568 ? 123.440 170.270 165.578 1.00 41.70 ?  568 HIS B ND1   1 
ATOM   10122 C  CD2   . HIS B 1 568 ? 124.438 171.596 164.161 1.00 40.68 ?  568 HIS B CD2   1 
ATOM   10123 C  CE1   . HIS B 1 568 ? 123.784 171.359 166.241 1.00 41.70 ?  568 HIS B CE1   1 
ATOM   10124 N  NE2   . HIS B 1 568 ? 124.393 172.179 165.404 1.00 46.63 ?  568 HIS B NE2   1 
ATOM   10125 N  N     . GLY B 1 569 ? 121.616 167.908 160.827 1.00 30.82 ?  569 GLY B N     1 
ATOM   10126 C  CA    . GLY B 1 569 ? 121.646 166.935 159.761 1.00 29.68 ?  569 GLY B CA    1 
ATOM   10127 C  C     . GLY B 1 569 ? 122.320 165.644 160.167 1.00 30.05 ?  569 GLY B C     1 
ATOM   10128 O  O     . GLY B 1 569 ? 122.665 165.403 161.327 1.00 38.28 ?  569 GLY B O     1 
ATOM   10129 N  N     . MET B 1 570 ? 122.503 164.788 159.168 1.00 26.75 ?  570 MET B N     1 
ATOM   10130 C  CA    . MET B 1 570 ? 123.034 163.448 159.368 1.00 22.89 ?  570 MET B CA    1 
ATOM   10131 C  C     . MET B 1 570 ? 124.082 163.189 158.297 1.00 24.69 ?  570 MET B C     1 
ATOM   10132 O  O     . MET B 1 570 ? 123.817 163.397 157.110 1.00 30.73 ?  570 MET B O     1 
ATOM   10133 C  CB    . MET B 1 570 ? 121.901 162.421 159.306 1.00 31.01 ?  570 MET B CB    1 
ATOM   10134 C  CG    . MET B 1 570 ? 121.371 162.003 160.669 1.00 24.56 ?  570 MET B CG    1 
ATOM   10135 S  SD    . MET B 1 570 ? 120.889 160.275 160.762 1.00 46.73 ?  570 MET B SD    1 
ATOM   10136 C  CE    . MET B 1 570 ? 122.469 159.474 160.845 1.00 26.89 ?  570 MET B CE    1 
ATOM   10137 N  N     . TYR B 1 571 ? 125.272 162.754 158.713 1.00 21.99 ?  571 TYR B N     1 
ATOM   10138 C  CA    . TYR B 1 571 ? 126.379 162.629 157.771 1.00 13.75 ?  571 TYR B CA    1 
ATOM   10139 C  C     . TYR B 1 571 ? 126.303 161.359 156.935 1.00 22.97 ?  571 TYR B C     1 
ATOM   10140 O  O     . TYR B 1 571 ? 126.706 161.371 155.768 1.00 21.03 ?  571 TYR B O     1 
ATOM   10141 C  CB    . TYR B 1 571 ? 127.715 162.677 158.510 1.00 18.76 ?  571 TYR B CB    1 
ATOM   10142 C  CG    . TYR B 1 571 ? 128.910 162.777 157.588 1.00 21.18 ?  571 TYR B CG    1 
ATOM   10143 C  CD1   . TYR B 1 571 ? 129.242 163.980 156.979 1.00 23.79 ?  571 TYR B CD1   1 
ATOM   10144 C  CD2   . TYR B 1 571 ? 129.702 161.670 157.323 1.00 21.32 ?  571 TYR B CD2   1 
ATOM   10145 C  CE1   . TYR B 1 571 ? 130.329 164.075 156.136 1.00 22.28 ?  571 TYR B CE1   1 
ATOM   10146 C  CE2   . TYR B 1 571 ? 130.789 161.755 156.482 1.00 23.34 ?  571 TYR B CE2   1 
ATOM   10147 C  CZ    . TYR B 1 571 ? 131.099 162.960 155.892 1.00 28.65 ?  571 TYR B CZ    1 
ATOM   10148 O  OH    . TYR B 1 571 ? 132.185 163.048 155.053 1.00 30.16 ?  571 TYR B OH    1 
ATOM   10149 N  N     . HIS B 1 572 ? 125.798 160.267 157.500 1.00 25.77 ?  572 HIS B N     1 
ATOM   10150 C  CA    . HIS B 1 572 ? 125.747 158.981 156.819 1.00 11.39 ?  572 HIS B CA    1 
ATOM   10151 C  C     . HIS B 1 572 ? 124.308 158.637 156.473 1.00 16.85 ?  572 HIS B C     1 
ATOM   10152 O  O     . HIS B 1 572 ? 123.433 158.660 157.345 1.00 31.90 ?  572 HIS B O     1 
ATOM   10153 C  CB    . HIS B 1 572 ? 126.355 157.872 157.682 1.00 12.19 ?  572 HIS B CB    1 
ATOM   10154 C  CG    . HIS B 1 572 ? 127.676 158.226 158.287 1.00 9.40  ?  572 HIS B CG    1 
ATOM   10155 N  ND1   . HIS B 1 572 ? 127.795 158.813 159.528 1.00 15.89 ?  572 HIS B ND1   1 
ATOM   10156 C  CD2   . HIS B 1 572 ? 128.938 158.070 157.824 1.00 13.40 ?  572 HIS B CD2   1 
ATOM   10157 C  CE1   . HIS B 1 572 ? 129.071 159.007 159.802 1.00 14.22 ?  572 HIS B CE1   1 
ATOM   10158 N  NE2   . HIS B 1 572 ? 129.786 158.566 158.783 1.00 24.57 ?  572 HIS B NE2   1 
ATOM   10159 N  N     . SER B 1 573 ? 124.067 158.321 155.200 1.00 10.81 ?  573 SER B N     1 
ATOM   10160 C  CA    . SER B 1 573 ? 122.754 157.826 154.802 1.00 8.56  ?  573 SER B CA    1 
ATOM   10161 C  C     . SER B 1 573 ? 122.452 156.499 155.477 1.00 17.12 ?  573 SER B C     1 
ATOM   10162 O  O     . SER B 1 573 ? 121.313 156.239 155.879 1.00 29.36 ?  573 SER B O     1 
ATOM   10163 C  CB    . SER B 1 573 ? 122.684 157.680 153.284 1.00 13.78 ?  573 SER B CB    1 
ATOM   10164 O  OG    . SER B 1 573 ? 123.879 157.118 152.778 1.00 25.31 ?  573 SER B OG    1 
ATOM   10165 N  N     . TYR B 1 574 ? 123.462 155.647 155.604 1.00 14.91 ?  574 TYR B N     1 
ATOM   10166 C  CA    . TYR B 1 574 ? 123.336 154.344 156.231 1.00 0.00  ?  574 TYR B CA    1 
ATOM   10167 C  C     . TYR B 1 574 ? 124.510 154.146 157.173 1.00 10.00 ?  574 TYR B C     1 
ATOM   10168 O  O     . TYR B 1 574 ? 125.638 154.538 156.860 1.00 19.34 ?  574 TYR B O     1 
ATOM   10169 C  CB    . TYR B 1 574 ? 123.289 153.237 155.179 1.00 10.33 ?  574 TYR B CB    1 
ATOM   10170 C  CG    . TYR B 1 574 ? 122.243 153.476 154.117 1.00 0.00  ?  574 TYR B CG    1 
ATOM   10171 C  CD1   . TYR B 1 574 ? 120.946 153.015 154.279 1.00 3.61  ?  574 TYR B CD1   1 
ATOM   10172 C  CD2   . TYR B 1 574 ? 122.548 154.177 152.958 1.00 3.57  ?  574 TYR B CD2   1 
ATOM   10173 C  CE1   . TYR B 1 574 ? 119.987 153.237 153.317 1.00 5.96  ?  574 TYR B CE1   1 
ATOM   10174 C  CE2   . TYR B 1 574 ? 121.593 154.407 151.992 1.00 10.55 ?  574 TYR B CE2   1 
ATOM   10175 C  CZ    . TYR B 1 574 ? 120.315 153.931 152.176 1.00 2.73  ?  574 TYR B CZ    1 
ATOM   10176 O  OH    . TYR B 1 574 ? 119.360 154.150 151.216 1.00 15.62 ?  574 TYR B OH    1 
ATOM   10177 N  N     . ARG B 1 575 ? 124.243 153.546 158.325 1.00 12.14 ?  575 ARG B N     1 
ATOM   10178 C  CA    . ARG B 1 575 ? 125.248 153.419 159.372 1.00 0.00  ?  575 ARG B CA    1 
ATOM   10179 C  C     . ARG B 1 575 ? 125.489 151.992 159.825 1.00 11.16 ?  575 ARG B C     1 
ATOM   10180 O  O     . ARG B 1 575 ? 126.638 151.611 160.053 1.00 23.55 ?  575 ARG B O     1 
ATOM   10181 C  CB    . ARG B 1 575 ? 124.842 154.254 160.587 1.00 13.58 ?  575 ARG B CB    1 
ATOM   10182 C  CG    . ARG B 1 575 ? 124.774 155.735 160.332 1.00 8.83  ?  575 ARG B CG    1 
ATOM   10183 C  CD    . ARG B 1 575 ? 123.931 156.399 161.388 1.00 11.19 ?  575 ARG B CD    1 
ATOM   10184 N  NE    . ARG B 1 575 ? 122.515 156.107 161.204 1.00 16.96 ?  575 ARG B NE    1 
ATOM   10185 C  CZ    . ARG B 1 575 ? 121.821 155.258 161.947 1.00 11.69 ?  575 ARG B CZ    1 
ATOM   10186 N  NH1   . ARG B 1 575 ? 122.384 154.586 162.936 1.00 11.22 1  575 ARG B NH1   1 
ATOM   10187 N  NH2   . ARG B 1 575 ? 120.530 155.080 161.693 1.00 11.31 ?  575 ARG B NH2   1 
ATOM   10188 N  N     . LEU B 1 576 ? 124.439 151.191 159.964 1.00 21.07 ?  576 LEU B N     1 
ATOM   10189 C  CA    . LEU B 1 576 ? 124.523 149.902 160.633 1.00 12.04 ?  576 LEU B CA    1 
ATOM   10190 C  C     . LEU B 1 576 ? 124.109 148.793 159.680 1.00 4.46  ?  576 LEU B C     1 
ATOM   10191 O  O     . LEU B 1 576 ? 123.034 148.856 159.078 1.00 20.33 ?  576 LEU B O     1 
ATOM   10192 C  CB    . LEU B 1 576 ? 123.636 149.882 161.879 1.00 7.86  ?  576 LEU B CB    1 
ATOM   10193 C  CG    . LEU B 1 576 ? 123.790 151.058 162.844 1.00 7.05  ?  576 LEU B CG    1 
ATOM   10194 C  CD1   . LEU B 1 576 ? 122.746 150.986 163.942 1.00 12.34 ?  576 LEU B CD1   1 
ATOM   10195 C  CD2   . LEU B 1 576 ? 125.183 151.084 163.435 1.00 11.05 ?  576 LEU B CD2   1 
ATOM   10196 N  N     . CYS B 1 577 ? 124.969 147.788 159.542 1.00 10.65 ?  577 CYS B N     1 
ATOM   10197 C  CA    . CYS B 1 577 ? 124.630 146.558 158.842 1.00 7.20  ?  577 CYS B CA    1 
ATOM   10198 C  C     . CYS B 1 577 ? 125.438 145.437 159.473 1.00 21.29 ?  577 CYS B C     1 
ATOM   10199 O  O     . CYS B 1 577 ? 126.641 145.589 159.696 1.00 26.91 ?  577 CYS B O     1 
ATOM   10200 C  CB    . CYS B 1 577 ? 124.905 146.662 157.335 1.00 4.23  ?  577 CYS B CB    1 
ATOM   10201 S  SG    . CYS B 1 577 ? 126.626 146.488 156.808 1.00 34.79 ?  577 CYS B SG    1 
ATOM   10202 N  N     . ILE B 1 578 ? 124.777 144.326 159.776 1.00 15.00 ?  578 ILE B N     1 
ATOM   10203 C  CA    . ILE B 1 578 ? 125.398 143.218 160.488 1.00 12.69 ?  578 ILE B CA    1 
ATOM   10204 C  C     . ILE B 1 578 ? 125.836 142.194 159.447 1.00 5.09  ?  578 ILE B C     1 
ATOM   10205 O  O     . ILE B 1 578 ? 125.043 141.366 158.994 1.00 20.00 ?  578 ILE B O     1 
ATOM   10206 C  CB    . ILE B 1 578 ? 124.458 142.618 161.534 1.00 10.95 ?  578 ILE B CB    1 
ATOM   10207 C  CG1   . ILE B 1 578 ? 123.945 143.716 162.466 1.00 2.62  ?  578 ILE B CG1   1 
ATOM   10208 C  CG2   . ILE B 1 578 ? 125.172 141.557 162.343 1.00 8.83  ?  578 ILE B CG2   1 
ATOM   10209 C  CD1   . ILE B 1 578 ? 123.182 143.199 163.654 1.00 9.60  ?  578 ILE B CD1   1 
ATOM   10210 N  N     . ALA B 1 579 ? 127.108 142.260 159.065 1.00 14.77 ?  579 ALA B N     1 
ATOM   10211 C  CA    . ALA B 1 579 ? 127.720 141.334 158.129 1.00 4.76  ?  579 ALA B CA    1 
ATOM   10212 C  C     . ALA B 1 579 ? 128.023 140.001 158.810 1.00 18.65 ?  579 ALA B C     1 
ATOM   10213 O  O     . ALA B 1 579 ? 128.033 139.911 160.038 1.00 31.68 ?  579 ALA B O     1 
ATOM   10214 C  CB    . ALA B 1 579 ? 128.996 141.945 157.561 1.00 9.76  ?  579 ALA B CB    1 
ATOM   10215 N  N     . PRO B 1 580 ? 128.250 138.937 158.030 1.00 25.93 ?  580 PRO B N     1 
ATOM   10216 C  CA    . PRO B 1 580 ? 128.544 137.631 158.649 1.00 23.57 ?  580 PRO B CA    1 
ATOM   10217 C  C     . PRO B 1 580 ? 129.791 137.612 159.524 1.00 31.60 ?  580 PRO B C     1 
ATOM   10218 O  O     . PRO B 1 580 ? 129.821 136.854 160.502 1.00 37.76 ?  580 PRO B O     1 
ATOM   10219 C  CB    . PRO B 1 580 ? 128.690 136.691 157.441 1.00 23.45 ?  580 PRO B CB    1 
ATOM   10220 C  CG    . PRO B 1 580 ? 128.796 137.573 156.246 1.00 23.60 ?  580 PRO B CG    1 
ATOM   10221 C  CD    . PRO B 1 580 ? 128.055 138.817 156.576 1.00 20.84 ?  580 PRO B CD    1 
ATOM   10222 N  N     . THR B 1 581 ? 130.811 138.414 159.213 1.00 24.16 ?  581 THR B N     1 
ATOM   10223 C  CA    . THR B 1 581 ? 132.064 138.461 159.978 1.00 33.88 ?  581 THR B CA    1 
ATOM   10224 C  C     . THR B 1 581 ? 132.686 137.067 160.098 1.00 32.21 ?  581 THR B C     1 
ATOM   10225 O  O     . THR B 1 581 ? 132.814 136.495 161.181 1.00 34.51 ?  581 THR B O     1 
ATOM   10226 C  CB    . THR B 1 581 ? 131.866 139.078 161.368 1.00 28.70 ?  581 THR B CB    1 
ATOM   10227 O  OG1   . THR B 1 581 ? 131.396 138.076 162.277 1.00 24.16 ?  581 THR B OG1   1 
ATOM   10228 C  CG2   . THR B 1 581 ? 130.884 140.230 161.320 1.00 31.20 ?  581 THR B CG2   1 
ATOM   10229 N  N     . GLY B 1 582 ? 133.068 136.536 158.941 1.00 31.94 ?  582 GLY B N     1 
ATOM   10230 C  CA    . GLY B 1 582 ? 133.516 135.162 158.852 1.00 34.72 ?  582 GLY B CA    1 
ATOM   10231 C  C     . GLY B 1 582 ? 134.808 134.836 159.573 1.00 37.48 ?  582 GLY B C     1 
ATOM   10232 O  O     . GLY B 1 582 ? 134.798 134.078 160.547 1.00 41.71 ?  582 GLY B O     1 
ATOM   10233 N  N     . SER B 1 583 ? 135.927 135.398 159.116 1.00 37.76 ?  583 SER B N     1 
ATOM   10234 C  CA    . SER B 1 583 ? 137.233 134.995 159.625 1.00 42.54 ?  583 SER B CA    1 
ATOM   10235 C  C     . SER B 1 583 ? 137.740 135.879 160.756 1.00 39.80 ?  583 SER B C     1 
ATOM   10236 O  O     . SER B 1 583 ? 138.557 135.421 161.564 1.00 39.77 ?  583 SER B O     1 
ATOM   10237 C  CB    . SER B 1 583 ? 138.261 134.984 158.492 1.00 47.40 ?  583 SER B CB    1 
ATOM   10238 O  OG    . SER B 1 583 ? 138.135 133.813 157.703 1.00 49.21 ?  583 SER B OG    1 
ATOM   10239 N  N     . ILE B 1 584 ? 137.289 137.133 160.835 1.00 33.05 ?  584 ILE B N     1 
ATOM   10240 C  CA    . ILE B 1 584 ? 137.701 138.009 161.924 1.00 28.91 ?  584 ILE B CA    1 
ATOM   10241 C  C     . ILE B 1 584 ? 137.118 137.595 163.265 1.00 31.88 ?  584 ILE B C     1 
ATOM   10242 O  O     . ILE B 1 584 ? 137.569 138.088 164.303 1.00 36.84 ?  584 ILE B O     1 
ATOM   10243 C  CB    . ILE B 1 584 ? 137.314 139.474 161.634 1.00 36.81 ?  584 ILE B CB    1 
ATOM   10244 C  CG1   . ILE B 1 584 ? 135.827 139.576 161.283 1.00 34.43 ?  584 ILE B CG1   1 
ATOM   10245 C  CG2   . ILE B 1 584 ? 138.188 140.053 160.535 1.00 32.57 ?  584 ILE B CG2   1 
ATOM   10246 C  CD1   . ILE B 1 584 ? 135.313 140.997 161.209 1.00 33.31 ?  584 ILE B CD1   1 
ATOM   10247 N  N     . SER B 1 585 ? 136.121 136.707 163.271 1.00 31.76 ?  585 SER B N     1 
ATOM   10248 C  CA    . SER B 1 585 ? 135.546 136.252 164.530 1.00 29.12 ?  585 SER B CA    1 
ATOM   10249 C  C     . SER B 1 585 ? 136.522 135.382 165.310 1.00 28.92 ?  585 SER B C     1 
ATOM   10250 O  O     . SER B 1 585 ? 136.543 135.435 166.544 1.00 29.13 ?  585 SER B O     1 
ATOM   10251 C  CB    . SER B 1 585 ? 134.245 135.495 164.271 1.00 32.20 ?  585 SER B CB    1 
ATOM   10252 O  OG    . SER B 1 585 ? 134.453 134.409 163.385 1.00 36.22 ?  585 SER B OG    1 
ATOM   10253 N  N     . TYR B 1 586 ? 137.326 134.573 164.616 1.00 35.47 ?  586 TYR B N     1 
ATOM   10254 C  CA    . TYR B 1 586 ? 138.332 133.769 165.302 1.00 36.44 ?  586 TYR B CA    1 
ATOM   10255 C  C     . TYR B 1 586 ? 139.372 134.651 165.976 1.00 34.72 ?  586 TYR B C     1 
ATOM   10256 O  O     . TYR B 1 586 ? 139.739 134.420 167.133 1.00 41.06 ?  586 TYR B O     1 
ATOM   10257 C  CB    . TYR B 1 586 ? 139.012 132.817 164.321 1.00 32.67 ?  586 TYR B CB    1 
ATOM   10258 C  CG    . TYR B 1 586 ? 138.085 131.836 163.648 1.00 33.53 ?  586 TYR B CG    1 
ATOM   10259 C  CD1   . TYR B 1 586 ? 137.522 132.119 162.412 1.00 36.90 ?  586 TYR B CD1   1 
ATOM   10260 C  CD2   . TYR B 1 586 ? 137.776 130.623 164.245 1.00 35.45 ?  586 TYR B CD2   1 
ATOM   10261 C  CE1   . TYR B 1 586 ? 136.677 131.224 161.791 1.00 39.70 ?  586 TYR B CE1   1 
ATOM   10262 C  CE2   . TYR B 1 586 ? 136.931 129.721 163.632 1.00 37.85 ?  586 TYR B CE2   1 
ATOM   10263 C  CZ    . TYR B 1 586 ? 136.384 130.026 162.406 1.00 39.59 ?  586 TYR B CZ    1 
ATOM   10264 O  OH    . TYR B 1 586 ? 135.541 129.130 161.791 1.00 44.24 ?  586 TYR B OH    1 
ATOM   10265 N  N     . VAL B 1 587 ? 139.853 135.674 165.265 1.00 29.79 ?  587 VAL B N     1 
ATOM   10266 C  CA    . VAL B 1 587 ? 140.878 136.561 165.810 1.00 24.81 ?  587 VAL B CA    1 
ATOM   10267 C  C     . VAL B 1 587 ? 140.358 137.278 167.048 1.00 30.49 ?  587 VAL B C     1 
ATOM   10268 O  O     . VAL B 1 587 ? 141.092 137.480 168.023 1.00 39.87 ?  587 VAL B O     1 
ATOM   10269 C  CB    . VAL B 1 587 ? 141.342 137.555 164.731 1.00 31.15 ?  587 VAL B CB    1 
ATOM   10270 C  CG1   . VAL B 1 587 ? 142.353 138.531 165.303 1.00 34.30 ?  587 VAL B CG1   1 
ATOM   10271 C  CG2   . VAL B 1 587 ? 141.924 136.811 163.543 1.00 31.54 ?  587 VAL B CG2   1 
ATOM   10272 N  N     . GLN B 1 588 ? 139.087 137.665 167.034 1.00 34.77 ?  588 GLN B N     1 
ATOM   10273 C  CA    . GLN B 1 588 ? 138.482 138.373 168.151 1.00 29.40 ?  588 GLN B CA    1 
ATOM   10274 C  C     . GLN B 1 588 ? 137.989 137.442 169.248 1.00 34.28 ?  588 GLN B C     1 
ATOM   10275 O  O     . GLN B 1 588 ? 137.484 137.931 170.264 1.00 36.74 ?  588 GLN B O     1 
ATOM   10276 C  CB    . GLN B 1 588 ? 137.322 139.237 167.655 1.00 22.63 ?  588 GLN B CB    1 
ATOM   10277 C  CG    . GLN B 1 588 ? 137.757 140.484 166.916 1.00 24.46 ?  588 GLN B CG    1 
ATOM   10278 C  CD    . GLN B 1 588 ? 137.842 141.690 167.824 1.00 29.18 ?  588 GLN B CD    1 
ATOM   10279 O  OE1   . GLN B 1 588 ? 136.992 141.887 168.691 1.00 29.62 ?  588 GLN B OE1   1 
ATOM   10280 N  NE2   . GLN B 1 588 ? 138.868 142.506 167.631 1.00 33.47 ?  588 GLN B NE2   1 
ATOM   10281 N  N     . SER B 1 589 ? 138.129 136.129 169.071 1.00 34.31 ?  589 SER B N     1 
ATOM   10282 C  CA    . SER B 1 589 ? 137.589 135.136 169.997 1.00 28.15 ?  589 SER B CA    1 
ATOM   10283 C  C     . SER B 1 589 ? 136.107 135.405 170.246 1.00 31.62 ?  589 SER B C     1 
ATOM   10284 O  O     . SER B 1 589 ? 135.658 135.624 171.372 1.00 35.30 ?  589 SER B O     1 
ATOM   10285 C  CB    . SER B 1 589 ? 138.383 135.113 171.304 1.00 36.32 ?  589 SER B CB    1 
ATOM   10286 O  OG    . SER B 1 589 ? 138.227 133.876 171.975 1.00 45.26 ?  589 SER B OG    1 
ATOM   10287 N  N     . SER B 1 590 ? 135.350 135.400 169.154 1.00 30.54 ?  590 SER B N     1 
ATOM   10288 C  CA    . SER B 1 590 ? 133.955 135.798 169.178 1.00 23.07 ?  590 SER B CA    1 
ATOM   10289 C  C     . SER B 1 590 ? 133.137 134.860 168.305 1.00 28.21 ?  590 SER B C     1 
ATOM   10290 O  O     . SER B 1 590 ? 133.655 134.255 167.363 1.00 36.37 ?  590 SER B O     1 
ATOM   10291 C  CB    . SER B 1 590 ? 133.784 137.242 168.691 1.00 26.65 ?  590 SER B CB    1 
ATOM   10292 O  OG    . SER B 1 590 ? 133.629 137.290 167.286 1.00 36.42 ?  590 SER B OG    1 
ATOM   10293 N  N     . THR B 1 591 ? 131.856 134.737 168.635 1.00 30.26 ?  591 THR B N     1 
ATOM   10294 C  CA    . THR B 1 591 ? 130.927 134.019 167.776 1.00 27.61 ?  591 THR B CA    1 
ATOM   10295 C  C     . THR B 1 591 ? 130.560 134.892 166.583 1.00 30.48 ?  591 THR B C     1 
ATOM   10296 O  O     . THR B 1 591 ? 130.474 136.119 166.696 1.00 25.23 ?  591 THR B O     1 
ATOM   10297 C  CB    . THR B 1 591 ? 129.673 133.613 168.549 1.00 28.23 ?  591 THR B CB    1 
ATOM   10298 O  OG1   . THR B 1 591 ? 128.899 134.776 168.864 1.00 36.89 ?  591 THR B OG1   1 
ATOM   10299 C  CG2   . THR B 1 591 ? 130.058 132.906 169.836 1.00 26.83 ?  591 THR B CG2   1 
ATOM   10300 N  N     . ALA B 1 592 ? 130.354 134.254 165.435 1.00 26.62 ?  592 ALA B N     1 
ATOM   10301 C  CA    . ALA B 1 592 ? 130.189 134.990 164.189 1.00 25.14 ?  592 ALA B CA    1 
ATOM   10302 C  C     . ALA B 1 592 ? 128.883 135.772 164.185 1.00 24.71 ?  592 ALA B C     1 
ATOM   10303 O  O     . ALA B 1 592 ? 127.799 135.193 164.310 1.00 32.62 ?  592 ALA B O     1 
ATOM   10304 C  CB    . ALA B 1 592 ? 130.232 134.031 163.002 1.00 31.49 ?  592 ALA B CB    1 
ATOM   10305 N  N     . SER B 1 593 ? 128.996 137.088 164.040 1.00 27.77 ?  593 SER B N     1 
ATOM   10306 C  CA    . SER B 1 593 ? 127.857 137.991 163.832 1.00 16.57 ?  593 SER B CA    1 
ATOM   10307 C  C     . SER B 1 593 ? 126.886 137.855 165.007 1.00 14.42 ?  593 SER B C     1 
ATOM   10308 O  O     . SER B 1 593 ? 127.290 137.535 166.132 1.00 29.93 ?  593 SER B O     1 
ATOM   10309 C  CB    . SER B 1 593 ? 127.246 137.713 162.472 1.00 28.74 ?  593 SER B CB    1 
ATOM   10310 O  OG    . SER B 1 593 ? 126.152 138.568 162.217 1.00 24.93 ?  593 SER B OG    1 
ATOM   10311 N  N     . VAL B 1 594 ? 125.600 138.098 164.756 1.00 20.91 ?  594 VAL B N     1 
ATOM   10312 C  CA    . VAL B 1 594 ? 124.561 137.894 165.754 1.00 17.98 ?  594 VAL B CA    1 
ATOM   10313 C  C     . VAL B 1 594 ? 123.935 136.510 165.638 1.00 15.70 ?  594 VAL B C     1 
ATOM   10314 O  O     . VAL B 1 594 ? 122.981 136.201 166.357 1.00 25.92 ?  594 VAL B O     1 
ATOM   10315 C  CB    . VAL B 1 594 ? 123.487 138.989 165.667 1.00 23.80 ?  594 VAL B CB    1 
ATOM   10316 C  CG1   . VAL B 1 594 ? 124.043 140.316 166.155 1.00 14.10 ?  594 VAL B CG1   1 
ATOM   10317 C  CG2   . VAL B 1 594 ? 122.969 139.114 164.246 1.00 22.03 ?  594 VAL B CG2   1 
ATOM   10318 N  N     . MET B 1 595 ? 124.453 135.670 164.747 1.00 25.63 ?  595 MET B N     1 
ATOM   10319 C  CA    . MET B 1 595 ? 123.929 134.328 164.580 1.00 19.42 ?  595 MET B CA    1 
ATOM   10320 C  C     . MET B 1 595 ? 124.311 133.451 165.769 1.00 24.87 ?  595 MET B C     1 
ATOM   10321 O  O     . MET B 1 595 ? 125.337 133.676 166.415 1.00 32.63 ?  595 MET B O     1 
ATOM   10322 C  CB    . MET B 1 595 ? 124.466 133.703 163.294 1.00 22.58 ?  595 MET B CB    1 
ATOM   10323 C  CG    . MET B 1 595 ? 124.058 134.386 161.991 1.00 24.99 ?  595 MET B CG    1 
ATOM   10324 S  SD    . MET B 1 595 ? 122.386 134.051 161.393 1.00 37.28 ?  595 MET B SD    1 
ATOM   10325 C  CE    . MET B 1 595 ? 121.383 135.104 162.435 1.00 16.63 ?  595 MET B CE    1 
ATOM   10326 N  N     . PRO B 1 596 ? 123.500 132.442 166.078 1.00 32.04 ?  596 PRO B N     1 
ATOM   10327 C  CA    . PRO B 1 596 ? 123.915 131.447 167.070 1.00 20.66 ?  596 PRO B CA    1 
ATOM   10328 C  C     . PRO B 1 596 ? 124.964 130.510 166.493 1.00 31.12 ?  596 PRO B C     1 
ATOM   10329 O  O     . PRO B 1 596 ? 125.131 130.385 165.278 1.00 37.74 ?  596 PRO B O     1 
ATOM   10330 C  CB    . PRO B 1 596 ? 122.616 130.707 167.394 1.00 22.35 ?  596 PRO B CB    1 
ATOM   10331 C  CG    . PRO B 1 596 ? 121.800 130.840 166.162 1.00 27.79 ?  596 PRO B CG    1 
ATOM   10332 C  CD    . PRO B 1 596 ? 122.151 132.172 165.553 1.00 32.26 ?  596 PRO B CD    1 
ATOM   10333 N  N     . ILE B 1 597 ? 125.685 129.846 167.397 1.00 28.45 ?  597 ILE B N     1 
ATOM   10334 C  CA    . ILE B 1 597 ? 126.805 129.009 166.986 1.00 28.60 ?  597 ILE B CA    1 
ATOM   10335 C  C     . ILE B 1 597 ? 126.294 127.760 166.281 1.00 37.55 ?  597 ILE B C     1 
ATOM   10336 O  O     . ILE B 1 597 ? 125.283 127.165 166.676 1.00 40.72 ?  597 ILE B O     1 
ATOM   10337 C  CB    . ILE B 1 597 ? 127.681 128.648 168.199 1.00 33.65 ?  597 ILE B CB    1 
ATOM   10338 C  CG1   . ILE B 1 597 ? 126.866 127.894 169.249 1.00 34.53 ?  597 ILE B CG1   1 
ATOM   10339 C  CG2   . ILE B 1 597 ? 128.285 129.899 168.800 1.00 31.62 ?  597 ILE B CG2   1 
ATOM   10340 C  CD1   . ILE B 1 597 ? 127.685 126.955 170.093 1.00 33.96 ?  597 ILE B CD1   1 
ATOM   10341 N  N     . MET B 1 598 ? 126.989 127.368 165.213 1.00 44.87 ?  598 MET B N     1 
ATOM   10342 C  CA    . MET B 1 598 ? 126.635 126.142 164.507 1.00 41.70 ?  598 MET B CA    1 
ATOM   10343 C  C     . MET B 1 598 ? 127.042 124.913 165.310 1.00 38.38 ?  598 MET B C     1 
ATOM   10344 O  O     . MET B 1 598 ? 126.265 123.961 165.444 1.00 46.97 ?  598 MET B O     1 
ATOM   10345 C  CB    . MET B 1 598 ? 127.293 126.125 163.129 1.00 40.80 ?  598 MET B CB    1 
ATOM   10346 C  CG    . MET B 1 598 ? 126.930 127.307 162.255 1.00 39.04 ?  598 MET B CG    1 
ATOM   10347 S  SD    . MET B 1 598 ? 127.276 127.007 160.513 1.00 59.89 ?  598 MET B SD    1 
ATOM   10348 C  CE    . MET B 1 598 ? 128.690 128.076 160.269 1.00 42.97 ?  598 MET B CE    1 
ATOM   10349 N  N     . GLU B 1 599 ? 128.258 124.919 165.850 1.00 42.37 ?  599 GLU B N     1 
ATOM   10350 C  CA    . GLU B 1 599 ? 128.785 123.812 166.633 1.00 42.26 ?  599 GLU B CA    1 
ATOM   10351 C  C     . GLU B 1 599 ? 129.373 124.346 167.929 1.00 40.25 ?  599 GLU B C     1 
ATOM   10352 O  O     . GLU B 1 599 ? 129.871 125.472 167.983 1.00 46.11 ?  599 GLU B O     1 
ATOM   10353 C  CB    . GLU B 1 599 ? 129.863 123.034 165.866 1.00 44.07 ?  599 GLU B CB    1 
ATOM   10354 C  CG    . GLU B 1 599 ? 129.767 123.149 164.355 1.00 43.73 ?  599 GLU B CG    1 
ATOM   10355 C  CD    . GLU B 1 599 ? 130.947 122.514 163.648 1.00 50.12 ?  599 GLU B CD    1 
ATOM   10356 O  OE1   . GLU B 1 599 ? 131.382 121.424 164.073 1.00 49.97 ?  599 GLU B OE1   1 
ATOM   10357 O  OE2   . GLU B 1 599 ? 131.439 123.107 162.665 1.00 48.55 -1 599 GLU B OE2   1 
ATOM   10358 N  N     . ARG B 1 600 ? 129.308 123.529 168.980 1.00 43.29 ?  600 ARG B N     1 
ATOM   10359 C  CA    . ARG B 1 600 ? 129.918 123.919 170.247 1.00 35.78 ?  600 ARG B CA    1 
ATOM   10360 C  C     . ARG B 1 600 ? 131.437 123.908 170.147 1.00 37.20 ?  600 ARG B C     1 
ATOM   10361 O  O     . ARG B 1 600 ? 132.107 124.839 170.609 1.00 41.36 ?  600 ARG B O     1 
ATOM   10362 C  CB    . ARG B 1 600 ? 129.443 122.998 171.368 1.00 38.87 ?  600 ARG B CB    1 
ATOM   10363 C  CG    . ARG B 1 600 ? 128.115 123.408 171.959 1.00 39.64 ?  600 ARG B CG    1 
ATOM   10364 C  CD    . ARG B 1 600 ? 127.838 122.666 173.245 1.00 36.65 ?  600 ARG B CD    1 
ATOM   10365 N  NE    . ARG B 1 600 ? 126.517 122.967 173.779 1.00 36.86 ?  600 ARG B NE    1 
ATOM   10366 C  CZ    . ARG B 1 600 ? 125.398 122.379 173.382 1.00 40.58 ?  600 ARG B CZ    1 
ATOM   10367 N  NH1   . ARG B 1 600 ? 125.401 121.457 172.434 1.00 39.73 1  600 ARG B NH1   1 
ATOM   10368 N  NH2   . ARG B 1 600 ? 124.246 122.723 173.951 1.00 41.50 ?  600 ARG B NH2   1 
ATOM   10369 N  N     . ILE B 1 601 ? 131.997 122.862 169.550 1.00 49.15 ?  601 ILE B N     1 
ATOM   10370 C  CA    . ILE B 1 601 ? 133.429 122.759 169.306 1.00 43.12 ?  601 ILE B CA    1 
ATOM   10371 C  C     . ILE B 1 601 ? 133.634 122.557 167.815 1.00 43.56 ?  601 ILE B C     1 
ATOM   10372 O  O     . ILE B 1 601 ? 133.044 121.649 167.218 1.00 46.37 ?  601 ILE B O     1 
ATOM   10373 C  CB    . ILE B 1 601 ? 134.067 121.618 170.116 1.00 40.56 ?  601 ILE B CB    1 
ATOM   10374 C  CG1   . ILE B 1 601 ? 133.769 121.803 171.604 1.00 42.38 ?  601 ILE B CG1   1 
ATOM   10375 C  CG2   . ILE B 1 601 ? 135.562 121.581 169.873 1.00 41.67 ?  601 ILE B CG2   1 
ATOM   10376 C  CD1   . ILE B 1 601 ? 133.944 120.558 172.428 1.00 44.89 ?  601 ILE B CD1   1 
ATOM   10377 N  N     . GLU B 1 602 ? 134.466 123.400 167.217 1.00 53.69 ?  602 GLU B N     1 
ATOM   10378 C  CA    . GLU B 1 602 ? 134.636 123.453 165.774 1.00 50.17 ?  602 GLU B CA    1 
ATOM   10379 C  C     . GLU B 1 602 ? 135.796 122.553 165.367 1.00 53.61 ?  602 GLU B C     1 
ATOM   10380 O  O     . GLU B 1 602 ? 136.937 122.778 165.784 1.00 57.39 ?  602 GLU B O     1 
ATOM   10381 C  CB    . GLU B 1 602 ? 134.881 124.894 165.328 1.00 50.44 ?  602 GLU B CB    1 
ATOM   10382 C  CG    . GLU B 1 602 ? 134.547 125.176 163.886 1.00 50.20 ?  602 GLU B CG    1 
ATOM   10383 C  CD    . GLU B 1 602 ? 134.555 126.658 163.575 1.00 56.99 ?  602 GLU B CD    1 
ATOM   10384 O  OE1   . GLU B 1 602 ? 133.737 127.393 164.166 1.00 55.91 ?  602 GLU B OE1   1 
ATOM   10385 O  OE2   . GLU B 1 602 ? 135.381 127.086 162.744 1.00 58.72 -1 602 GLU B OE2   1 
ATOM   10386 N  N     . GLU B 1 603 ? 135.503 121.538 164.558 1.00 56.22 ?  603 GLU B N     1 
ATOM   10387 C  CA    . GLU B 1 603 ? 136.510 120.610 164.059 1.00 55.13 ?  603 GLU B CA    1 
ATOM   10388 C  C     . GLU B 1 603 ? 136.870 120.991 162.629 1.00 57.66 ?  603 GLU B C     1 
ATOM   10389 O  O     . GLU B 1 603 ? 136.023 120.921 161.732 1.00 59.08 ?  603 GLU B O     1 
ATOM   10390 C  CB    . GLU B 1 603 ? 136.004 119.168 164.113 1.00 58.25 ?  603 GLU B CB    1 
ATOM   10391 C  CG    . GLU B 1 603 ? 135.460 118.738 165.466 1.00 60.56 ?  603 GLU B CG    1 
ATOM   10392 C  CD    . GLU B 1 603 ? 133.954 118.886 165.567 1.00 60.85 ?  603 GLU B CD    1 
ATOM   10393 O  OE1   . GLU B 1 603 ? 133.297 119.040 164.516 1.00 54.69 ?  603 GLU B OE1   1 
ATOM   10394 O  OE2   . GLU B 1 603 ? 133.427 118.844 166.699 1.00 59.56 -1 603 GLU B OE2   1 
ATOM   10395 N  N     . ARG B 1 604 ? 138.121 121.392 162.420 1.00 60.93 ?  604 ARG B N     1 
ATOM   10396 C  CA    . ARG B 1 604 ? 138.611 121.797 161.112 1.00 61.64 ?  604 ARG B CA    1 
ATOM   10397 C  C     . ARG B 1 604 ? 139.984 121.196 160.856 1.00 62.36 ?  604 ARG B C     1 
ATOM   10398 O  O     . ARG B 1 604 ? 140.736 120.900 161.788 1.00 61.58 ?  604 ARG B O     1 
ATOM   10399 C  CB    . ARG B 1 604 ? 138.677 123.325 160.984 1.00 61.50 ?  604 ARG B CB    1 
ATOM   10400 C  CG    . ARG B 1 604 ? 137.330 124.011 161.104 1.00 61.72 ?  604 ARG B CG    1 
ATOM   10401 C  CD    . ARG B 1 604 ? 136.653 124.075 159.740 1.00 61.06 ?  604 ARG B CD    1 
ATOM   10402 N  NE    . ARG B 1 604 ? 135.606 125.088 159.680 1.00 64.58 ?  604 ARG B NE    1 
ATOM   10403 C  CZ    . ARG B 1 604 ? 134.446 125.011 160.317 1.00 62.16 ?  604 ARG B CZ    1 
ATOM   10404 N  NH1   . ARG B 1 604 ? 134.102 123.932 161.001 1.00 59.27 1  604 ARG B NH1   1 
ATOM   10405 N  NH2   . ARG B 1 604 ? 133.599 126.034 160.247 1.00 60.26 ?  604 ARG B NH2   1 
ATOM   10406 N  N     . THR B 1 605 ? 140.299 121.019 159.577 1.00 68.88 ?  605 THR B N     1 
ATOM   10407 C  CA    . THR B 1 605 ? 141.573 120.464 159.141 1.00 69.05 ?  605 THR B CA    1 
ATOM   10408 C  C     . THR B 1 605 ? 142.341 121.533 158.376 1.00 68.94 ?  605 THR B C     1 
ATOM   10409 O  O     . THR B 1 605 ? 141.838 122.076 157.386 1.00 68.34 ?  605 THR B O     1 
ATOM   10410 C  CB    . THR B 1 605 ? 141.362 119.230 158.264 1.00 68.77 ?  605 THR B CB    1 
ATOM   10411 O  OG1   . THR B 1 605 ? 140.716 118.202 159.026 1.00 68.65 ?  605 THR B OG1   1 
ATOM   10412 C  CG2   . THR B 1 605 ? 142.695 118.710 157.749 1.00 69.06 ?  605 THR B CG2   1 
ATOM   10413 N  N     . TYR B 1 606 ? 143.552 121.831 158.835 1.00 70.93 ?  606 TYR B N     1 
ATOM   10414 C  CA    . TYR B 1 606 ? 144.442 122.772 158.166 1.00 72.42 ?  606 TYR B CA    1 
ATOM   10415 C  C     . TYR B 1 606 ? 145.707 122.026 157.770 1.00 73.83 ?  606 TYR B C     1 
ATOM   10416 O  O     . TYR B 1 606 ? 146.379 121.443 158.628 1.00 71.71 ?  606 TYR B O     1 
ATOM   10417 C  CB    . TYR B 1 606 ? 144.761 123.964 159.070 1.00 70.45 ?  606 TYR B CB    1 
ATOM   10418 C  CG    . TYR B 1 606 ? 143.548 124.805 159.390 1.00 71.00 ?  606 TYR B CG    1 
ATOM   10419 C  CD1   . TYR B 1 606 ? 143.071 125.742 158.484 1.00 68.19 ?  606 TYR B CD1   1 
ATOM   10420 C  CD2   . TYR B 1 606 ? 142.873 124.654 160.593 1.00 71.01 ?  606 TYR B CD2   1 
ATOM   10421 C  CE1   . TYR B 1 606 ? 141.960 126.509 158.770 1.00 69.99 ?  606 TYR B CE1   1 
ATOM   10422 C  CE2   . TYR B 1 606 ? 141.762 125.415 160.888 1.00 68.85 ?  606 TYR B CE2   1 
ATOM   10423 C  CZ    . TYR B 1 606 ? 141.310 126.341 159.974 1.00 72.54 ?  606 TYR B CZ    1 
ATOM   10424 O  OH    . TYR B 1 606 ? 140.201 127.101 160.265 1.00 74.18 ?  606 TYR B OH    1 
ATOM   10425 N  N     . GLY B 1 607 ? 146.031 122.056 156.483 1.00 79.93 ?  607 GLY B N     1 
ATOM   10426 C  CA    . GLY B 1 607 ? 147.103 121.208 155.992 1.00 79.31 ?  607 GLY B CA    1 
ATOM   10427 C  C     . GLY B 1 607 ? 146.728 119.750 156.165 1.00 79.82 ?  607 GLY B C     1 
ATOM   10428 O  O     . GLY B 1 607 ? 145.629 119.319 155.799 1.00 79.29 ?  607 GLY B O     1 
ATOM   10429 N  N     . ASN B 1 608 ? 147.648 118.972 156.732 1.00 81.39 ?  608 ASN B N     1 
ATOM   10430 C  CA    . ASN B 1 608 ? 147.407 117.564 157.014 1.00 82.54 ?  608 ASN B CA    1 
ATOM   10431 C  C     . ASN B 1 608 ? 147.040 117.318 158.472 1.00 83.77 ?  608 ASN B C     1 
ATOM   10432 O  O     . ASN B 1 608 ? 146.846 116.164 158.867 1.00 83.08 ?  608 ASN B O     1 
ATOM   10433 C  CB    . ASN B 1 608 ? 148.633 116.732 156.631 1.00 83.72 ?  608 ASN B CB    1 
ATOM   10434 C  CG    . ASN B 1 608 ? 148.943 116.803 155.147 1.00 84.36 ?  608 ASN B CG    1 
ATOM   10435 O  OD1   . ASN B 1 608 ? 148.140 117.297 154.356 1.00 82.31 ?  608 ASN B OD1   1 
ATOM   10436 N  ND2   . ASN B 1 608 ? 150.113 116.306 154.763 1.00 83.01 ?  608 ASN B ND2   1 
ATOM   10437 N  N     . SER B 1 609 ? 146.934 118.372 159.277 1.00 76.85 ?  609 SER B N     1 
ATOM   10438 C  CA    . SER B 1 609 ? 146.636 118.256 160.696 1.00 76.36 ?  609 SER B CA    1 
ATOM   10439 C  C     . SER B 1 609 ? 145.258 118.832 160.993 1.00 74.44 ?  609 SER B C     1 
ATOM   10440 O  O     . SER B 1 609 ? 144.902 119.905 160.496 1.00 74.33 ?  609 SER B O     1 
ATOM   10441 C  CB    . SER B 1 609 ? 147.696 118.973 161.539 1.00 73.85 ?  609 SER B CB    1 
ATOM   10442 O  OG    . SER B 1 609 ? 147.702 120.364 161.272 1.00 73.50 ?  609 SER B OG    1 
ATOM   10443 N  N     . LYS B 1 610 ? 144.488 118.110 161.801 1.00 64.40 ?  610 LYS B N     1 
ATOM   10444 C  CA    . LYS B 1 610 ? 143.151 118.534 162.187 1.00 63.80 ?  610 LYS B CA    1 
ATOM   10445 C  C     . LYS B 1 610 ? 143.199 119.360 163.466 1.00 63.31 ?  610 LYS B C     1 
ATOM   10446 O  O     . LYS B 1 610 ? 143.989 119.083 164.374 1.00 64.06 ?  610 LYS B O     1 
ATOM   10447 C  CB    . LYS B 1 610 ? 142.237 117.314 162.345 1.00 64.70 ?  610 LYS B CB    1 
ATOM   10448 C  CG    . LYS B 1 610 ? 142.158 116.721 163.742 1.00 63.25 ?  610 LYS B CG    1 
ATOM   10449 C  CD    . LYS B 1 610 ? 141.614 115.300 163.683 1.00 64.78 ?  610 LYS B CD    1 
ATOM   10450 C  CE    . LYS B 1 610 ? 142.259 114.406 164.732 1.00 64.56 ?  610 LYS B CE    1 
ATOM   10451 N  NZ    . LYS B 1 610 ? 141.790 114.700 166.110 1.00 64.14 1  610 LYS B NZ    1 
ATOM   10452 N  N     . THR B 1 611 ? 142.370 120.399 163.515 1.00 63.68 ?  611 THR B N     1 
ATOM   10453 C  CA    . THR B 1 611 ? 142.355 121.349 164.616 1.00 61.02 ?  611 THR B CA    1 
ATOM   10454 C  C     . THR B 1 611 ? 140.973 121.389 165.252 1.00 56.76 ?  611 THR B C     1 
ATOM   10455 O  O     . THR B 1 611 ? 139.963 121.107 164.601 1.00 60.25 ?  611 THR B O     1 
ATOM   10456 C  CB    . THR B 1 611 ? 142.747 122.755 164.147 1.00 61.00 ?  611 THR B CB    1 
ATOM   10457 O  OG1   . THR B 1 611 ? 143.728 122.659 163.106 1.00 61.18 ?  611 THR B OG1   1 
ATOM   10458 C  CG2   . THR B 1 611 ? 143.332 123.546 165.296 1.00 60.84 ?  611 THR B CG2   1 
ATOM   10459 N  N     . TYR B 1 612 ? 140.937 121.742 166.535 1.00 51.00 ?  612 TYR B N     1 
ATOM   10460 C  CA    . TYR B 1 612 ? 139.703 121.819 167.304 1.00 52.40 ?  612 TYR B CA    1 
ATOM   10461 C  C     . TYR B 1 612 ? 139.556 123.220 167.874 1.00 54.60 ?  612 TYR B C     1 
ATOM   10462 O  O     . TYR B 1 612 ? 140.491 123.747 168.485 1.00 53.52 ?  612 TYR B O     1 
ATOM   10463 C  CB    . TYR B 1 612 ? 139.702 120.781 168.425 1.00 54.04 ?  612 TYR B CB    1 
ATOM   10464 C  CG    . TYR B 1 612 ? 139.676 119.366 167.908 1.00 57.49 ?  612 TYR B CG    1 
ATOM   10465 C  CD1   . TYR B 1 612 ? 138.605 118.900 167.161 1.00 55.55 ?  612 TYR B CD1   1 
ATOM   10466 C  CD2   . TYR B 1 612 ? 140.739 118.505 168.138 1.00 56.40 ?  612 TYR B CD2   1 
ATOM   10467 C  CE1   . TYR B 1 612 ? 138.580 117.610 166.676 1.00 54.86 ?  612 TYR B CE1   1 
ATOM   10468 C  CE2   . TYR B 1 612 ? 140.725 117.215 167.656 1.00 59.31 ?  612 TYR B CE2   1 
ATOM   10469 C  CZ    . TYR B 1 612 ? 139.643 116.771 166.927 1.00 59.22 ?  612 TYR B CZ    1 
ATOM   10470 O  OH    . TYR B 1 612 ? 139.625 115.483 166.446 1.00 60.84 ?  612 TYR B OH    1 
ATOM   10471 N  N     . TYR B 1 613 ? 138.386 123.819 167.674 1.00 51.35 ?  613 TYR B N     1 
ATOM   10472 C  CA    . TYR B 1 613 ? 138.110 125.177 168.138 1.00 45.38 ?  613 TYR B CA    1 
ATOM   10473 C  C     . TYR B 1 613 ? 136.832 125.197 168.964 1.00 43.07 ?  613 TYR B C     1 
ATOM   10474 O  O     . TYR B 1 613 ? 135.727 125.275 168.401 1.00 43.80 ?  613 TYR B O     1 
ATOM   10475 C  CB    . TYR B 1 613 ? 138.003 126.147 166.969 1.00 42.88 ?  613 TYR B CB    1 
ATOM   10476 C  CG    . TYR B 1 613 ? 137.681 127.562 167.387 1.00 43.43 ?  613 TYR B CG    1 
ATOM   10477 C  CD1   . TYR B 1 613 ? 138.427 128.202 168.367 1.00 42.09 ?  613 TYR B CD1   1 
ATOM   10478 C  CD2   . TYR B 1 613 ? 136.632 128.257 166.804 1.00 45.50 ?  613 TYR B CD2   1 
ATOM   10479 C  CE1   . TYR B 1 613 ? 138.138 129.494 168.752 1.00 44.64 ?  613 TYR B CE1   1 
ATOM   10480 C  CE2   . TYR B 1 613 ? 136.336 129.549 167.183 1.00 45.24 ?  613 TYR B CE2   1 
ATOM   10481 C  CZ    . TYR B 1 613 ? 137.091 130.163 168.156 1.00 48.46 ?  613 TYR B CZ    1 
ATOM   10482 O  OH    . TYR B 1 613 ? 136.799 131.451 168.536 1.00 47.39 ?  613 TYR B OH    1 
ATOM   10483 N  N     . PRO B 1 614 ? 136.934 125.125 170.287 1.00 39.22 ?  614 PRO B N     1 
ATOM   10484 C  CA    . PRO B 1 614 ? 135.752 125.354 171.121 1.00 42.67 ?  614 PRO B CA    1 
ATOM   10485 C  C     . PRO B 1 614 ? 135.275 126.788 170.981 1.00 41.86 ?  614 PRO B C     1 
ATOM   10486 O  O     . PRO B 1 614 ? 136.061 127.708 170.740 1.00 42.89 ?  614 PRO B O     1 
ATOM   10487 C  CB    . PRO B 1 614 ? 136.251 125.071 172.545 1.00 39.16 ?  614 PRO B CB    1 
ATOM   10488 C  CG    . PRO B 1 614 ? 137.581 124.400 172.381 1.00 42.11 ?  614 PRO B CG    1 
ATOM   10489 C  CD    . PRO B 1 614 ? 138.141 124.890 171.092 1.00 40.31 ?  614 PRO B CD    1 
ATOM   10490 N  N     . MET B 1 615 ? 133.969 126.974 171.124 1.00 40.49 ?  615 MET B N     1 
ATOM   10491 C  CA    . MET B 1 615 ? 133.415 128.314 171.027 1.00 40.16 ?  615 MET B CA    1 
ATOM   10492 C  C     . MET B 1 615 ? 133.951 129.180 172.165 1.00 44.34 ?  615 MET B C     1 
ATOM   10493 O  O     . MET B 1 615 ? 134.188 128.677 173.269 1.00 42.90 ?  615 MET B O     1 
ATOM   10494 C  CB    . MET B 1 615 ? 131.887 128.271 171.051 1.00 38.52 ?  615 MET B CB    1 
ATOM   10495 C  CG    . MET B 1 615 ? 131.289 127.911 169.702 1.00 41.18 ?  615 MET B CG    1 
ATOM   10496 S  SD    . MET B 1 615 ? 132.361 128.452 168.355 1.00 52.06 ?  615 MET B SD    1 
ATOM   10497 C  CE    . MET B 1 615 ? 131.404 127.983 166.920 1.00 41.46 ?  615 MET B CE    1 
ATOM   10498 N  N     . PRO B 1 616 ? 134.177 130.470 171.925 1.00 45.96 ?  616 PRO B N     1 
ATOM   10499 C  CA    . PRO B 1 616 ? 134.844 131.308 172.931 1.00 39.83 ?  616 PRO B CA    1 
ATOM   10500 C  C     . PRO B 1 616 ? 134.052 131.369 174.227 1.00 41.31 ?  616 PRO B C     1 
ATOM   10501 O  O     . PRO B 1 616 ? 132.870 131.720 174.238 1.00 42.63 ?  616 PRO B O     1 
ATOM   10502 C  CB    . PRO B 1 616 ? 134.922 132.679 172.252 1.00 36.23 ?  616 PRO B CB    1 
ATOM   10503 C  CG    . PRO B 1 616 ? 134.755 132.399 170.797 1.00 41.50 ?  616 PRO B CG    1 
ATOM   10504 C  CD    . PRO B 1 616 ? 133.855 131.223 170.702 1.00 40.52 ?  616 PRO B CD    1 
ATOM   10505 N  N     . GLY B 1 617 ? 134.721 131.035 175.325 1.00 40.43 ?  617 GLY B N     1 
ATOM   10506 C  CA    . GLY B 1 617 ? 134.086 130.992 176.622 1.00 36.58 ?  617 GLY B CA    1 
ATOM   10507 C  C     . GLY B 1 617 ? 133.368 129.703 176.943 1.00 41.88 ?  617 GLY B C     1 
ATOM   10508 O  O     . GLY B 1 617 ? 132.724 129.622 177.996 1.00 45.55 ?  617 GLY B O     1 
ATOM   10509 N  N     . LEU B 1 618 ? 133.451 128.698 176.076 1.00 44.70 ?  618 LEU B N     1 
ATOM   10510 C  CA    . LEU B 1 618 ? 132.811 127.419 176.348 1.00 38.50 ?  618 LEU B CA    1 
ATOM   10511 C  C     . LEU B 1 618 ? 133.476 126.733 177.534 1.00 39.94 ?  618 LEU B C     1 
ATOM   10512 O  O     . LEU B 1 618 ? 134.704 126.693 177.643 1.00 44.64 ?  618 LEU B O     1 
ATOM   10513 C  CB    . LEU B 1 618 ? 132.875 126.515 175.118 1.00 38.04 ?  618 LEU B CB    1 
ATOM   10514 C  CG    . LEU B 1 618 ? 132.157 125.170 175.201 1.00 40.00 ?  618 LEU B CG    1 
ATOM   10515 C  CD1   . LEU B 1 618 ? 130.674 125.366 175.444 1.00 41.29 ?  618 LEU B CD1   1 
ATOM   10516 C  CD2   . LEU B 1 618 ? 132.390 124.368 173.936 1.00 40.82 ?  618 LEU B CD2   1 
ATOM   10517 N  N     . ALA B 1 619 ? 132.651 126.194 178.424 1.00 47.78 ?  619 ALA B N     1 
ATOM   10518 C  CA    . ALA B 1 619 ? 133.126 125.494 179.607 1.00 47.23 ?  619 ALA B CA    1 
ATOM   10519 C  C     . ALA B 1 619 ? 132.050 124.505 180.031 1.00 49.90 ?  619 ALA B C     1 
ATOM   10520 O  O     . ALA B 1 619 ? 131.102 124.236 179.288 1.00 54.00 ?  619 ALA B O     1 
ATOM   10521 C  CB    . ALA B 1 619 ? 133.479 126.488 180.721 1.00 46.77 ?  619 ALA B CB    1 
ATOM   10522 N  N     . SER B 1 620 ? 132.202 123.951 181.233 1.00 56.15 ?  620 SER B N     1 
ATOM   10523 C  CA    . SER B 1 620 ? 131.195 123.035 181.753 1.00 55.66 ?  620 SER B CA    1 
ATOM   10524 C  C     . SER B 1 620 ? 129.966 123.780 182.259 1.00 55.44 ?  620 SER B C     1 
ATOM   10525 O  O     . SER B 1 620 ? 128.839 123.296 182.110 1.00 57.57 ?  620 SER B O     1 
ATOM   10526 C  CB    . SER B 1 620 ? 131.796 122.177 182.866 1.00 57.26 ?  620 SER B CB    1 
ATOM   10527 O  OG    . SER B 1 620 ? 133.027 121.611 182.457 1.00 59.15 ?  620 SER B OG    1 
ATOM   10528 N  N     . ASN B 1 621 ? 130.164 124.958 182.855 1.00 50.85 ?  621 ASN B N     1 
ATOM   10529 C  CA    . ASN B 1 621 ? 129.045 125.687 183.445 1.00 52.15 ?  621 ASN B CA    1 
ATOM   10530 C  C     . ASN B 1 621 ? 128.128 126.273 182.377 1.00 54.39 ?  621 ASN B C     1 
ATOM   10531 O  O     . ASN B 1 621 ? 126.906 126.318 182.561 1.00 56.25 ?  621 ASN B O     1 
ATOM   10532 C  CB    . ASN B 1 621 ? 129.565 126.785 184.374 1.00 53.65 ?  621 ASN B CB    1 
ATOM   10533 C  CG    . ASN B 1 621 ? 130.332 127.863 183.632 1.00 57.66 ?  621 ASN B CG    1 
ATOM   10534 O  OD1   . ASN B 1 621 ? 131.371 127.599 183.027 1.00 59.16 ?  621 ASN B OD1   1 
ATOM   10535 N  ND2   . ASN B 1 621 ? 129.824 129.090 183.679 1.00 55.87 ?  621 ASN B ND2   1 
ATOM   10536 N  N     . ASN B 1 622 ? 128.691 126.726 181.257 1.00 46.91 ?  622 ASN B N     1 
ATOM   10537 C  CA    . ASN B 1 622 ? 127.916 127.348 180.191 1.00 45.83 ?  622 ASN B CA    1 
ATOM   10538 C  C     . ASN B 1 622 ? 127.799 126.458 178.959 1.00 47.47 ?  622 ASN B C     1 
ATOM   10539 O  O     . ASN B 1 622 ? 127.570 126.960 177.856 1.00 53.86 ?  622 ASN B O     1 
ATOM   10540 C  CB    . ASN B 1 622 ? 128.515 128.709 179.822 1.00 46.81 ?  622 ASN B CB    1 
ATOM   10541 C  CG    . ASN B 1 622 ? 129.937 128.611 179.285 1.00 46.56 ?  622 ASN B CG    1 
ATOM   10542 O  OD1   . ASN B 1 622 ? 130.418 127.535 178.937 1.00 52.25 ?  622 ASN B OD1   1 
ATOM   10543 N  ND2   . ASN B 1 622 ? 130.615 129.748 179.222 1.00 43.47 ?  622 ASN B ND2   1 
ATOM   10544 N  N     . TRP B 1 623 ? 127.964 125.144 179.126 1.00 41.95 ?  623 TRP B N     1 
ATOM   10545 C  CA    . TRP B 1 623 ? 127.932 124.242 177.980 1.00 40.84 ?  623 TRP B CA    1 
ATOM   10546 C  C     . TRP B 1 623 ? 126.571 124.252 177.297 1.00 42.27 ?  623 TRP B C     1 
ATOM   10547 O  O     . TRP B 1 623 ? 126.489 124.287 176.063 1.00 42.30 ?  623 TRP B O     1 
ATOM   10548 C  CB    . TRP B 1 623 ? 128.297 122.824 178.421 1.00 45.73 ?  623 TRP B CB    1 
ATOM   10549 C  CG    . TRP B 1 623 ? 128.109 121.788 177.356 1.00 43.63 ?  623 TRP B CG    1 
ATOM   10550 C  CD1   . TRP B 1 623 ? 126.978 121.071 177.101 1.00 40.76 ?  623 TRP B CD1   1 
ATOM   10551 C  CD2   . TRP B 1 623 ? 129.084 121.349 176.404 1.00 42.24 ?  623 TRP B CD2   1 
ATOM   10552 N  NE1   . TRP B 1 623 ? 127.187 120.216 176.049 1.00 42.99 ?  623 TRP B NE1   1 
ATOM   10553 C  CE2   . TRP B 1 623 ? 128.473 120.365 175.604 1.00 40.39 ?  623 TRP B CE2   1 
ATOM   10554 C  CE3   . TRP B 1 623 ? 130.416 121.693 176.152 1.00 39.81 ?  623 TRP B CE3   1 
ATOM   10555 C  CZ2   . TRP B 1 623 ? 129.146 119.723 174.568 1.00 38.39 ?  623 TRP B CZ2   1 
ATOM   10556 C  CZ3   . TRP B 1 623 ? 131.080 121.054 175.123 1.00 42.86 ?  623 TRP B CZ3   1 
ATOM   10557 C  CH2   . TRP B 1 623 ? 130.445 120.081 174.343 1.00 42.62 ?  623 TRP B CH2   1 
ATOM   10558 N  N     . PHE B 1 624 ? 125.492 124.225 178.075 1.00 48.20 ?  624 PHE B N     1 
ATOM   10559 C  CA    . PHE B 1 624 ? 124.156 124.138 177.506 1.00 45.50 ?  624 PHE B CA    1 
ATOM   10560 C  C     . PHE B 1 624 ? 123.565 125.493 177.144 1.00 45.25 ?  624 PHE B C     1 
ATOM   10561 O  O     . PHE B 1 624 ? 122.522 125.538 176.484 1.00 52.40 ?  624 PHE B O     1 
ATOM   10562 C  CB    . PHE B 1 624 ? 123.222 123.399 178.469 1.00 49.11 ?  624 PHE B CB    1 
ATOM   10563 C  CG    . PHE B 1 624 ? 123.442 121.914 178.490 1.00 50.34 ?  624 PHE B CG    1 
ATOM   10564 C  CD1   . PHE B 1 624 ? 123.059 121.130 177.415 1.00 44.39 ?  624 PHE B CD1   1 
ATOM   10565 C  CD2   . PHE B 1 624 ? 124.045 121.305 179.577 1.00 48.19 ?  624 PHE B CD2   1 
ATOM   10566 C  CE1   . PHE B 1 624 ? 123.264 119.766 177.427 1.00 44.64 ?  624 PHE B CE1   1 
ATOM   10567 C  CE2   . PHE B 1 624 ? 124.254 119.940 179.595 1.00 49.33 ?  624 PHE B CE2   1 
ATOM   10568 C  CZ    . PHE B 1 624 ? 123.863 119.169 178.519 1.00 48.15 ?  624 PHE B CZ    1 
ATOM   10569 N  N     . PHE B 1 625 ? 124.199 126.591 177.552 1.00 39.83 ?  625 PHE B N     1 
ATOM   10570 C  CA    . PHE B 1 625 ? 123.840 127.892 177.008 1.00 37.08 ?  625 PHE B CA    1 
ATOM   10571 C  C     . PHE B 1 625 ? 124.424 128.109 175.622 1.00 36.39 ?  625 PHE B C     1 
ATOM   10572 O  O     . PHE B 1 625 ? 123.942 128.975 174.886 1.00 41.33 ?  625 PHE B O     1 
ATOM   10573 C  CB    . PHE B 1 625 ? 124.293 129.011 177.945 1.00 32.77 ?  625 PHE B CB    1 
ATOM   10574 C  CG    . PHE B 1 625 ? 123.486 129.109 179.203 1.00 35.96 ?  625 PHE B CG    1 
ATOM   10575 C  CD1   . PHE B 1 625 ? 122.153 129.477 179.155 1.00 37.62 ?  625 PHE B CD1   1 
ATOM   10576 C  CD2   . PHE B 1 625 ? 124.057 128.838 180.434 1.00 37.97 ?  625 PHE B CD2   1 
ATOM   10577 C  CE1   . PHE B 1 625 ? 121.405 129.570 180.310 1.00 40.00 ?  625 PHE B CE1   1 
ATOM   10578 C  CE2   . PHE B 1 625 ? 123.314 128.931 181.592 1.00 37.58 ?  625 PHE B CE2   1 
ATOM   10579 C  CZ    . PHE B 1 625 ? 121.986 129.298 181.530 1.00 40.99 ?  625 PHE B CZ    1 
ATOM   10580 N  N     . TYR B 1 626 ? 125.444 127.341 175.253 1.00 29.50 ?  626 TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 626 ? 125.989 127.362 173.898 1.00 33.44 ?  626 TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 626 ? 125.237 126.387 173.000 1.00 30.15 ?  626 TYR B C     1 
ATOM   10583 O  O     . TYR B 1 626 ? 125.825 125.542 172.331 1.00 36.11 ?  626 TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 626 ? 127.477 127.038 173.932 1.00 32.29 ?  626 TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 626 ? 128.358 128.248 174.109 1.00 34.18 ?  626 TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 626 ? 128.608 129.109 173.051 1.00 35.39 ?  626 TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 626 ? 128.939 128.531 175.337 1.00 34.34 ?  626 TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 626 ? 129.413 130.216 173.209 1.00 35.36 ?  626 TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 626 ? 129.744 129.636 175.505 1.00 31.69 ?  626 TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 626 ? 129.978 130.474 174.438 1.00 30.87 ?  626 TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 626 ? 130.777 131.577 174.599 1.00 38.82 ?  626 TYR B OH    1 
ATOM   10592 N  N     . LYS B 1 627 ? 123.914 126.508 172.991 1.00 33.87 ?  627 LYS B N     1 
ATOM   10593 C  CA    . LYS B 1 627 ? 123.082 125.621 172.192 1.00 34.18 ?  627 LYS B CA    1 
ATOM   10594 C  C     . LYS B 1 627 ? 123.393 125.797 170.713 1.00 37.69 ?  627 LYS B C     1 
ATOM   10595 O  O     . LYS B 1 627 ? 123.508 126.922 170.219 1.00 44.50 ?  627 LYS B O     1 
ATOM   10596 C  CB    . LYS B 1 627 ? 121.608 125.907 172.474 1.00 37.36 ?  627 LYS B CB    1 
ATOM   10597 C  CG    . LYS B 1 627 ? 120.631 124.966 171.803 1.00 37.26 ?  627 LYS B CG    1 
ATOM   10598 C  CD    . LYS B 1 627 ? 119.231 125.183 172.352 1.00 32.29 ?  627 LYS B CD    1 
ATOM   10599 C  CE    . LYS B 1 627 ? 118.220 124.290 171.665 1.00 39.91 ?  627 LYS B CE    1 
ATOM   10600 N  NZ    . LYS B 1 627 ? 116.850 124.498 172.206 1.00 41.71 1  627 LYS B NZ    1 
ATOM   10601 N  N     . GLU B 1 628 ? 123.548 124.682 170.007 1.00 39.03 ?  628 GLU B N     1 
ATOM   10602 C  CA    . GLU B 1 628 ? 123.863 124.744 168.589 1.00 35.29 ?  628 GLU B CA    1 
ATOM   10603 C  C     . GLU B 1 628 ? 122.678 125.294 167.804 1.00 40.27 ?  628 GLU B C     1 
ATOM   10604 O  O     . GLU B 1 628 ? 121.516 125.113 168.179 1.00 45.56 ?  628 GLU B O     1 
ATOM   10605 C  CB    . GLU B 1 628 ? 124.256 123.366 168.065 1.00 39.70 ?  628 GLU B CB    1 
ATOM   10606 C  CG    . GLU B 1 628 ? 125.413 122.733 168.820 1.00 41.43 ?  628 GLU B CG    1 
ATOM   10607 C  CD    . GLU B 1 628 ? 126.170 121.722 167.986 1.00 47.84 ?  628 GLU B CD    1 
ATOM   10608 O  OE1   . GLU B 1 628 ? 125.659 121.334 166.913 1.00 43.73 ?  628 GLU B OE1   1 
ATOM   10609 O  OE2   . GLU B 1 628 ? 127.276 121.316 168.399 1.00 45.74 -1 628 GLU B OE2   1 
ATOM   10610 N  N     . ALA B 1 629 ? 122.991 125.982 166.705 1.00 41.50 ?  629 ALA B N     1 
ATOM   10611 C  CA    . ALA B 1 629 ? 121.958 126.657 165.925 1.00 32.10 ?  629 ALA B CA    1 
ATOM   10612 C  C     . ALA B 1 629 ? 120.949 125.667 165.356 1.00 37.00 ?  629 ALA B C     1 
ATOM   10613 O  O     . ALA B 1 629 ? 119.749 125.958 165.301 1.00 44.16 ?  629 ALA B O     1 
ATOM   10614 C  CB    . ALA B 1 629 ? 122.602 127.472 164.806 1.00 30.45 ?  629 ALA B CB    1 
ATOM   10615 N  N     . TYR B 1 630 ? 121.417 124.497 164.919 1.00 40.68 ?  630 TYR B N     1 
ATOM   10616 C  CA    . TYR B 1 630 ? 120.509 123.508 164.346 1.00 39.14 ?  630 TYR B CA    1 
ATOM   10617 C  C     . TYR B 1 630 ? 119.533 122.967 165.383 1.00 42.65 ?  630 TYR B C     1 
ATOM   10618 O  O     . TYR B 1 630 ? 118.385 122.657 165.047 1.00 49.05 ?  630 TYR B O     1 
ATOM   10619 C  CB    . TYR B 1 630 ? 121.309 122.371 163.718 1.00 37.55 ?  630 TYR B CB    1 
ATOM   10620 C  CG    . TYR B 1 630 ? 122.283 122.838 162.664 1.00 37.64 ?  630 TYR B CG    1 
ATOM   10621 C  CD1   . TYR B 1 630 ? 121.862 123.082 161.365 1.00 38.02 ?  630 TYR B CD1   1 
ATOM   10622 C  CD2   . TYR B 1 630 ? 123.620 123.043 162.968 1.00 37.73 ?  630 TYR B CD2   1 
ATOM   10623 C  CE1   . TYR B 1 630 ? 122.746 123.511 160.398 1.00 38.57 ?  630 TYR B CE1   1 
ATOM   10624 C  CE2   . TYR B 1 630 ? 124.512 123.472 162.007 1.00 40.36 ?  630 TYR B CE2   1 
ATOM   10625 C  CZ    . TYR B 1 630 ? 124.068 123.705 160.724 1.00 45.55 ?  630 TYR B CZ    1 
ATOM   10626 O  OH    . TYR B 1 630 ? 124.953 124.132 159.763 1.00 51.53 ?  630 TYR B OH    1 
ATOM   10627 N  N     . ASP B 1 631 ? 119.964 122.848 166.639 1.00 42.26 ?  631 ASP B N     1 
ATOM   10628 C  CA    . ASP B 1 631 ? 119.072 122.408 167.704 1.00 37.01 ?  631 ASP B CA    1 
ATOM   10629 C  C     . ASP B 1 631 ? 118.057 123.472 168.099 1.00 43.14 ?  631 ASP B C     1 
ATOM   10630 O  O     . ASP B 1 631 ? 117.135 123.170 168.864 1.00 47.63 ?  631 ASP B O     1 
ATOM   10631 C  CB    . ASP B 1 631 ? 119.884 121.998 168.933 1.00 41.58 ?  631 ASP B CB    1 
ATOM   10632 C  CG    . ASP B 1 631 ? 120.883 120.900 168.632 1.00 48.57 ?  631 ASP B CG    1 
ATOM   10633 O  OD1   . ASP B 1 631 ? 120.572 120.020 167.803 1.00 49.25 ?  631 ASP B OD1   1 
ATOM   10634 O  OD2   . ASP B 1 631 ? 121.981 120.915 169.228 1.00 50.10 -1 631 ASP B OD2   1 
ATOM   10635 N  N     . MET B 1 632 ? 118.198 124.692 167.599 1.00 37.56 ?  632 MET B N     1 
ATOM   10636 C  CA    . MET B 1 632 ? 117.358 125.805 168.008 1.00 38.15 ?  632 MET B CA    1 
ATOM   10637 C  C     . MET B 1 632 ? 116.065 125.845 167.206 1.00 37.21 ?  632 MET B C     1 
ATOM   10638 O  O     . MET B 1 632 ? 115.947 125.256 166.130 1.00 36.18 ?  632 MET B O     1 
ATOM   10639 C  CB    . MET B 1 632 ? 118.103 127.128 167.839 1.00 36.52 ?  632 MET B CB    1 
ATOM   10640 C  CG    . MET B 1 632 ? 118.744 127.645 169.104 1.00 35.34 ?  632 MET B CG    1 
ATOM   10641 S  SD    . MET B 1 632 ? 120.123 128.740 168.770 1.00 45.68 ?  632 MET B SD    1 
ATOM   10642 C  CE    . MET B 1 632 ? 120.932 128.744 170.362 1.00 33.51 ?  632 MET B CE    1 
ATOM   10643 N  N     . ASP B 1 633 ? 115.085 126.560 167.752 1.00 37.50 ?  633 ASP B N     1 
ATOM   10644 C  CA    . ASP B 1 633 ? 113.851 126.845 167.036 1.00 33.40 ?  633 ASP B CA    1 
ATOM   10645 C  C     . ASP B 1 633 ? 114.077 128.050 166.132 1.00 36.19 ?  633 ASP B C     1 
ATOM   10646 O  O     . ASP B 1 633 ? 114.345 129.154 166.619 1.00 43.42 ?  633 ASP B O     1 
ATOM   10647 C  CB    . ASP B 1 633 ? 112.712 127.111 168.018 1.00 30.86 ?  633 ASP B CB    1 
ATOM   10648 C  CG    . ASP B 1 633 ? 111.371 127.272 167.330 1.00 40.37 ?  633 ASP B CG    1 
ATOM   10649 O  OD1   . ASP B 1 633 ? 111.276 126.974 166.121 1.00 43.37 ?  633 ASP B OD1   1 
ATOM   10650 O  OD2   . ASP B 1 633 ? 110.409 127.700 168.000 1.00 41.05 -1 633 ASP B OD2   1 
ATOM   10651 N  N     . MET B 1 634 ? 113.978 127.839 164.818 1.00 30.22 ?  634 MET B N     1 
ATOM   10652 C  CA    . MET B 1 634 ? 114.224 128.926 163.878 1.00 23.54 ?  634 MET B CA    1 
ATOM   10653 C  C     . MET B 1 634 ? 113.226 130.063 164.030 1.00 26.50 ?  634 MET B C     1 
ATOM   10654 O  O     . MET B 1 634 ? 113.536 131.193 163.644 1.00 31.39 ?  634 MET B O     1 
ATOM   10655 C  CB    . MET B 1 634 ? 114.201 128.400 162.443 1.00 26.08 ?  634 MET B CB    1 
ATOM   10656 C  CG    . MET B 1 634 ? 115.506 127.763 162.006 1.00 31.31 ?  634 MET B CG    1 
ATOM   10657 S  SD    . MET B 1 634 ? 116.923 128.854 162.251 1.00 43.09 ?  634 MET B SD    1 
ATOM   10658 C  CE    . MET B 1 634 ? 117.779 128.014 163.582 1.00 29.75 ?  634 MET B CE    1 
ATOM   10659 N  N     . PHE B 1 635 ? 112.041 129.797 164.581 1.00 26.09 ?  635 PHE B N     1 
ATOM   10660 C  CA    . PHE B 1 635 ? 111.104 130.881 164.857 1.00 23.44 ?  635 PHE B CA    1 
ATOM   10661 C  C     . PHE B 1 635 ? 111.660 131.829 165.912 1.00 21.59 ?  635 PHE B C     1 
ATOM   10662 O  O     . PHE B 1 635 ? 111.529 133.051 165.790 1.00 26.28 ?  635 PHE B O     1 
ATOM   10663 C  CB    . PHE B 1 635 ? 109.756 130.311 165.298 1.00 27.07 ?  635 PHE B CB    1 
ATOM   10664 C  CG    . PHE B 1 635 ? 108.799 130.082 164.165 1.00 30.07 ?  635 PHE B CG    1 
ATOM   10665 C  CD1   . PHE B 1 635 ? 109.229 129.497 162.987 1.00 26.06 ?  635 PHE B CD1   1 
ATOM   10666 C  CD2   . PHE B 1 635 ? 107.471 130.452 164.277 1.00 25.64 ?  635 PHE B CD2   1 
ATOM   10667 C  CE1   . PHE B 1 635 ? 108.353 129.284 161.943 1.00 24.41 ?  635 PHE B CE1   1 
ATOM   10668 C  CE2   . PHE B 1 635 ? 106.590 130.241 163.234 1.00 28.30 ?  635 PHE B CE2   1 
ATOM   10669 C  CZ    . PHE B 1 635 ? 107.032 129.655 162.067 1.00 25.18 ?  635 PHE B CZ    1 
ATOM   10670 N  N     . LYS B 1 636 ? 112.299 131.286 166.948 1.00 27.48 ?  636 LYS B N     1 
ATOM   10671 C  CA    . LYS B 1 636 ? 112.885 132.136 167.977 1.00 30.38 ?  636 LYS B CA    1 
ATOM   10672 C  C     . LYS B 1 636 ? 114.112 132.879 167.462 1.00 26.86 ?  636 LYS B C     1 
ATOM   10673 O  O     . LYS B 1 636 ? 114.365 134.017 167.873 1.00 36.77 ?  636 LYS B O     1 
ATOM   10674 C  CB    . LYS B 1 636 ? 113.235 131.300 169.205 1.00 30.54 ?  636 LYS B CB    1 
ATOM   10675 C  CG    . LYS B 1 636 ? 112.044 130.573 169.803 1.00 29.29 ?  636 LYS B CG    1 
ATOM   10676 C  CD    . LYS B 1 636 ? 111.542 131.274 171.051 1.00 34.76 ?  636 LYS B CD    1 
ATOM   10677 C  CE    . LYS B 1 636 ? 110.076 130.970 171.305 1.00 33.40 ?  636 LYS B CE    1 
ATOM   10678 N  NZ    . LYS B 1 636 ? 109.285 132.211 171.527 1.00 35.79 1  636 LYS B NZ    1 
ATOM   10679 N  N     . VAL B 1 637 ? 114.878 132.263 166.562 1.00 24.28 ?  637 VAL B N     1 
ATOM   10680 C  CA    . VAL B 1 637 ? 115.988 132.972 165.931 1.00 17.58 ?  637 VAL B CA    1 
ATOM   10681 C  C     . VAL B 1 637 ? 115.461 134.108 165.064 1.00 27.32 ?  637 VAL B C     1 
ATOM   10682 O  O     . VAL B 1 637 ? 116.041 135.201 165.024 1.00 31.76 ?  637 VAL B O     1 
ATOM   10683 C  CB    . VAL B 1 637 ? 116.857 131.991 165.125 1.00 21.70 ?  637 VAL B CB    1 
ATOM   10684 C  CG1   . VAL B 1 637 ? 118.034 132.715 164.498 1.00 22.34 ?  637 VAL B CG1   1 
ATOM   10685 C  CG2   . VAL B 1 637 ? 117.334 130.857 166.016 1.00 23.89 ?  637 VAL B CG2   1 
ATOM   10686 N  N     . VAL B 1 638 ? 114.353 133.870 164.357 1.00 25.42 ?  638 VAL B N     1 
ATOM   10687 C  CA    . VAL B 1 638 ? 113.702 134.934 163.598 1.00 22.70 ?  638 VAL B CA    1 
ATOM   10688 C  C     . VAL B 1 638 ? 113.264 136.053 164.531 1.00 19.58 ?  638 VAL B C     1 
ATOM   10689 O  O     . VAL B 1 638 ? 113.409 137.238 164.215 1.00 30.46 ?  638 VAL B O     1 
ATOM   10690 C  CB    . VAL B 1 638 ? 112.510 134.375 162.799 1.00 24.93 ?  638 VAL B CB    1 
ATOM   10691 C  CG1   . VAL B 1 638 ? 111.601 135.501 162.345 1.00 14.67 ?  638 VAL B CG1   1 
ATOM   10692 C  CG2   . VAL B 1 638 ? 112.986 133.566 161.608 1.00 23.91 ?  638 VAL B CG2   1 
ATOM   10693 N  N     . ASP B 1 639 ? 112.711 135.693 165.689 1.00 17.63 ?  639 ASP B N     1 
ATOM   10694 C  CA    . ASP B 1 639 ? 112.293 136.697 166.663 1.00 21.91 ?  639 ASP B CA    1 
ATOM   10695 C  C     . ASP B 1 639 ? 113.476 137.535 167.130 1.00 26.76 ?  639 ASP B C     1 
ATOM   10696 O  O     . ASP B 1 639 ? 113.377 138.763 167.231 1.00 34.74 ?  639 ASP B O     1 
ATOM   10697 C  CB    . ASP B 1 639 ? 111.620 136.017 167.854 1.00 25.22 ?  639 ASP B CB    1 
ATOM   10698 C  CG    . ASP B 1 639 ? 110.165 135.696 167.595 1.00 36.03 ?  639 ASP B CG    1 
ATOM   10699 O  OD1   . ASP B 1 639 ? 109.519 136.431 166.821 1.00 33.39 ?  639 ASP B OD1   1 
ATOM   10700 O  OD2   . ASP B 1 639 ? 109.666 134.705 168.168 1.00 39.17 -1 639 ASP B OD2   1 
ATOM   10701 N  N     . MET B 1 640 ? 114.607 136.886 167.407 1.00 24.69 ?  640 MET B N     1 
ATOM   10702 C  CA    . MET B 1 640 ? 115.805 137.611 167.822 1.00 17.97 ?  640 MET B CA    1 
ATOM   10703 C  C     . MET B 1 640 ? 116.289 138.559 166.730 1.00 23.27 ?  640 MET B C     1 
ATOM   10704 O  O     . MET B 1 640 ? 116.589 139.731 166.994 1.00 32.90 ?  640 MET B O     1 
ATOM   10705 C  CB    . MET B 1 640 ? 116.907 136.621 168.194 1.00 22.73 ?  640 MET B CB    1 
ATOM   10706 C  CG    . MET B 1 640 ? 118.298 137.223 168.205 1.00 28.17 ?  640 MET B CG    1 
ATOM   10707 S  SD    . MET B 1 640 ? 118.585 138.243 169.657 1.00 39.52 ?  640 MET B SD    1 
ATOM   10708 C  CE    . MET B 1 640 ? 118.951 136.986 170.871 1.00 26.08 ?  640 MET B CE    1 
ATOM   10709 N  N     . ILE B 1 641 ? 116.368 138.069 165.492 1.00 28.94 ?  641 ILE B N     1 
ATOM   10710 C  CA    . ILE B 1 641 ? 116.885 138.897 164.408 1.00 21.13 ?  641 ILE B CA    1 
ATOM   10711 C  C     . ILE B 1 641 ? 115.940 140.052 164.110 1.00 19.87 ?  641 ILE B C     1 
ATOM   10712 O  O     . ILE B 1 641 ? 116.386 141.157 163.780 1.00 29.61 ?  641 ILE B O     1 
ATOM   10713 C  CB    . ILE B 1 641 ? 117.156 138.038 163.160 1.00 25.85 ?  641 ILE B CB    1 
ATOM   10714 C  CG1   . ILE B 1 641 ? 118.169 136.943 163.490 1.00 18.83 ?  641 ILE B CG1   1 
ATOM   10715 C  CG2   . ILE B 1 641 ? 117.687 138.894 162.023 1.00 18.72 ?  641 ILE B CG2   1 
ATOM   10716 C  CD1   . ILE B 1 641 ? 119.379 137.444 164.248 1.00 20.70 ?  641 ILE B CD1   1 
ATOM   10717 N  N     . ALA B 1 642 ? 114.629 139.831 164.228 1.00 17.45 ?  642 ALA B N     1 
ATOM   10718 C  CA    . ALA B 1 642 ? 113.674 140.916 164.046 1.00 20.38 ?  642 ALA B CA    1 
ATOM   10719 C  C     . ALA B 1 642 ? 113.752 141.922 165.184 1.00 21.19 ?  642 ALA B C     1 
ATOM   10720 O  O     . ALA B 1 642 ? 113.517 143.117 164.969 1.00 25.52 ?  642 ALA B O     1 
ATOM   10721 C  CB    . ALA B 1 642 ? 112.258 140.357 163.926 1.00 15.88 ?  642 ALA B CB    1 
ATOM   10722 N  N     . THR B 1 643 ? 114.061 141.461 166.396 1.00 21.94 ?  643 THR B N     1 
ATOM   10723 C  CA    . THR B 1 643 ? 114.321 142.388 167.491 1.00 18.28 ?  643 THR B CA    1 
ATOM   10724 C  C     . THR B 1 643 ? 115.536 143.255 167.193 1.00 24.19 ?  643 THR B C     1 
ATOM   10725 O  O     . THR B 1 643 ? 115.525 144.465 167.446 1.00 26.56 ?  643 THR B O     1 
ATOM   10726 C  CB    . THR B 1 643 ? 114.519 141.615 168.793 1.00 17.26 ?  643 THR B CB    1 
ATOM   10727 O  OG1   . THR B 1 643 ? 113.366 140.805 169.047 1.00 22.86 ?  643 THR B OG1   1 
ATOM   10728 C  CG2   . THR B 1 643 ? 114.725 142.569 169.949 1.00 17.83 ?  643 THR B CG2   1 
ATOM   10729 N  N     . ILE B 1 644 ? 116.599 142.650 166.661 1.00 22.78 ?  644 ILE B N     1 
ATOM   10730 C  CA    . ILE B 1 644 ? 117.776 143.425 166.285 1.00 10.33 ?  644 ILE B CA    1 
ATOM   10731 C  C     . ILE B 1 644 ? 117.489 144.285 165.060 1.00 16.72 ?  644 ILE B C     1 
ATOM   10732 O  O     . ILE B 1 644 ? 117.926 145.438 164.980 1.00 22.18 ?  644 ILE B O     1 
ATOM   10733 C  CB    . ILE B 1 644 ? 118.978 142.493 166.050 1.00 12.86 ?  644 ILE B CB    1 
ATOM   10734 C  CG1   . ILE B 1 644 ? 119.242 141.636 167.287 1.00 16.38 ?  644 ILE B CG1   1 
ATOM   10735 C  CG2   . ILE B 1 644 ? 120.209 143.298 165.695 1.00 8.54  ?  644 ILE B CG2   1 
ATOM   10736 C  CD1   . ILE B 1 644 ? 120.081 140.416 167.002 1.00 22.52 ?  644 ILE B CD1   1 
ATOM   10737 N  N     . GLN B 1 645 ? 116.747 143.740 164.090 1.00 12.43 ?  645 GLN B N     1 
ATOM   10738 C  CA    . GLN B 1 645 ? 116.547 144.425 162.815 1.00 13.88 ?  645 GLN B CA    1 
ATOM   10739 C  C     . GLN B 1 645 ? 115.832 145.759 162.983 1.00 17.48 ?  645 GLN B C     1 
ATOM   10740 O  O     . GLN B 1 645 ? 116.017 146.667 162.166 1.00 29.59 ?  645 GLN B O     1 
ATOM   10741 C  CB    . GLN B 1 645 ? 115.765 143.526 161.858 1.00 12.98 ?  645 GLN B CB    1 
ATOM   10742 C  CG    . GLN B 1 645 ? 115.603 144.087 160.458 1.00 3.84  ?  645 GLN B CG    1 
ATOM   10743 C  CD    . GLN B 1 645 ? 116.880 144.013 159.653 1.00 19.17 ?  645 GLN B CD    1 
ATOM   10744 O  OE1   . GLN B 1 645 ? 117.667 144.955 159.630 1.00 13.42 ?  645 GLN B OE1   1 
ATOM   10745 N  NE2   . GLN B 1 645 ? 117.091 142.887 158.984 1.00 16.27 ?  645 GLN B NE2   1 
ATOM   10746 N  N     . GLN B 1 646 ? 115.025 145.906 164.032 1.00 19.98 ?  646 GLN B N     1 
ATOM   10747 C  CA    . GLN B 1 646 ? 114.299 147.153 164.229 1.00 11.37 ?  646 GLN B CA    1 
ATOM   10748 C  C     . GLN B 1 646 ? 115.205 148.309 164.629 1.00 11.49 ?  646 GLN B C     1 
ATOM   10749 O  O     . GLN B 1 646 ? 114.745 149.454 164.640 1.00 15.53 ?  646 GLN B O     1 
ATOM   10750 C  CB    . GLN B 1 646 ? 113.200 146.961 165.273 1.00 19.79 ?  646 GLN B CB    1 
ATOM   10751 C  CG    . GLN B 1 646 ? 113.687 146.958 166.702 1.00 22.80 ?  646 GLN B CG    1 
ATOM   10752 C  CD    . GLN B 1 646 ? 112.585 146.627 167.683 1.00 27.77 ?  646 GLN B CD    1 
ATOM   10753 O  OE1   . GLN B 1 646 ? 112.650 145.624 168.391 1.00 26.85 ?  646 GLN B OE1   1 
ATOM   10754 N  NE2   . GLN B 1 646 ? 111.563 147.472 167.729 1.00 23.34 ?  646 GLN B NE2   1 
ATOM   10755 N  N     . HIS B 1 647 ? 116.470 148.048 164.949 1.00 29.18 ?  647 HIS B N     1 
ATOM   10756 C  CA    . HIS B 1 647 ? 117.425 149.100 165.262 1.00 12.41 ?  647 HIS B CA    1 
ATOM   10757 C  C     . HIS B 1 647 ? 118.554 149.197 164.247 1.00 13.61 ?  647 HIS B C     1 
ATOM   10758 O  O     . HIS B 1 647 ? 119.447 150.034 164.415 1.00 27.00 ?  647 HIS B O     1 
ATOM   10759 C  CB    . HIS B 1 647 ? 118.013 148.888 166.663 1.00 5.67  ?  647 HIS B CB    1 
ATOM   10760 C  CG    . HIS B 1 647 ? 116.980 148.680 167.725 1.00 14.52 ?  647 HIS B CG    1 
ATOM   10761 N  ND1   . HIS B 1 647 ? 116.060 149.646 168.068 1.00 18.16 ?  647 HIS B ND1   1 
ATOM   10762 C  CD2   . HIS B 1 647 ? 116.723 147.616 168.523 1.00 12.29 ?  647 HIS B CD2   1 
ATOM   10763 C  CE1   . HIS B 1 647 ? 115.280 149.187 169.029 1.00 20.52 ?  647 HIS B CE1   1 
ATOM   10764 N  NE2   . HIS B 1 647 ? 115.663 147.958 169.324 1.00 15.87 ?  647 HIS B NE2   1 
ATOM   10765 N  N     . ILE B 1 648 ? 118.538 148.374 163.204 1.00 14.96 ?  648 ILE B N     1 
ATOM   10766 C  CA    . ILE B 1 648 ? 119.561 148.375 162.165 1.00 16.22 ?  648 ILE B CA    1 
ATOM   10767 C  C     . ILE B 1 648 ? 118.935 148.965 160.909 1.00 14.31 ?  648 ILE B C     1 
ATOM   10768 O  O     . ILE B 1 648 ? 117.903 148.474 160.437 1.00 28.02 ?  648 ILE B O     1 
ATOM   10769 C  CB    . ILE B 1 648 ? 120.099 146.957 161.910 1.00 10.01 ?  648 ILE B CB    1 
ATOM   10770 C  CG1   . ILE B 1 648 ? 120.681 146.364 163.196 1.00 10.50 ?  648 ILE B CG1   1 
ATOM   10771 C  CG2   . ILE B 1 648 ? 121.146 146.964 160.816 1.00 3.67  ?  648 ILE B CG2   1 
ATOM   10772 C  CD1   . ILE B 1 648 ? 121.820 147.161 163.781 1.00 4.55  ?  648 ILE B CD1   1 
ATOM   10773 N  N     . ASP B 1 649 ? 119.549 150.023 160.371 1.00 7.88  ?  649 ASP B N     1 
ATOM   10774 C  CA    . ASP B 1 649 ? 118.957 150.694 159.217 1.00 9.36  ?  649 ASP B CA    1 
ATOM   10775 C  C     . ASP B 1 649 ? 119.116 149.874 157.944 1.00 7.99  ?  649 ASP B C     1 
ATOM   10776 O  O     . ASP B 1 649 ? 118.229 149.893 157.084 1.00 32.55 ?  649 ASP B O     1 
ATOM   10777 C  CB    . ASP B 1 649 ? 119.561 152.090 159.040 1.00 21.54 ?  649 ASP B CB    1 
ATOM   10778 C  CG    . ASP B 1 649 ? 121.075 152.083 159.036 1.00 16.61 ?  649 ASP B CG    1 
ATOM   10779 O  OD1   . ASP B 1 649 ? 121.671 152.324 160.103 1.00 20.43 ?  649 ASP B OD1   1 
ATOM   10780 O  OD2   . ASP B 1 649 ? 121.670 151.849 157.966 1.00 28.60 -1 649 ASP B OD2   1 
ATOM   10781 N  N     . GLN B 1 650 ? 120.226 149.164 157.801 1.00 10.05 ?  650 GLN B N     1 
ATOM   10782 C  CA    . GLN B 1 650 ? 120.407 148.204 156.723 1.00 2.07  ?  650 GLN B CA    1 
ATOM   10783 C  C     . GLN B 1 650 ? 119.949 146.831 157.213 1.00 5.15  ?  650 GLN B C     1 
ATOM   10784 O  O     . GLN B 1 650 ? 119.266 146.721 158.233 1.00 22.73 ?  650 GLN B O     1 
ATOM   10785 C  CB    . GLN B 1 650 ? 121.857 148.221 156.243 1.00 9.86  ?  650 GLN B CB    1 
ATOM   10786 C  CG    . GLN B 1 650 ? 122.301 149.555 155.692 1.00 8.84  ?  650 GLN B CG    1 
ATOM   10787 C  CD    . GLN B 1 650 ? 123.677 149.494 155.083 1.00 14.00 ?  650 GLN B CD    1 
ATOM   10788 O  OE1   . GLN B 1 650 ? 123.877 148.878 154.040 1.00 17.40 ?  650 GLN B OE1   1 
ATOM   10789 N  NE2   . GLN B 1 650 ? 124.640 150.140 155.728 1.00 8.23  ?  650 GLN B NE2   1 
ATOM   10790 N  N     . GLY B 1 651 ? 120.287 145.771 156.484 1.00 12.16 ?  651 GLY B N     1 
ATOM   10791 C  CA    . GLY B 1 651 ? 119.860 144.439 156.846 1.00 13.22 ?  651 GLY B CA    1 
ATOM   10792 C  C     . GLY B 1 651 ? 120.857 143.703 157.722 1.00 7.23  ?  651 GLY B C     1 
ATOM   10793 O  O     . GLY B 1 651 ? 121.885 144.229 158.141 1.00 12.16 ?  651 GLY B O     1 
ATOM   10794 N  N     . ILE B 1 652 ? 120.517 142.449 158.004 1.00 20.05 ?  652 ILE B N     1 
ATOM   10795 C  CA    . ILE B 1 652 ? 121.331 141.547 158.806 1.00 4.72  ?  652 ILE B CA    1 
ATOM   10796 C  C     . ILE B 1 652 ? 121.492 140.249 158.029 1.00 13.37 ?  652 ILE B C     1 
ATOM   10797 O  O     . ILE B 1 652 ? 120.517 139.732 157.475 1.00 24.03 ?  652 ILE B O     1 
ATOM   10798 C  CB    . ILE B 1 652 ? 120.697 141.270 160.184 1.00 2.58  ?  652 ILE B CB    1 
ATOM   10799 C  CG1   . ILE B 1 652 ? 120.467 142.573 160.949 1.00 3.36  ?  652 ILE B CG1   1 
ATOM   10800 C  CG2   . ILE B 1 652 ? 121.553 140.313 160.992 1.00 7.53  ?  652 ILE B CG2   1 
ATOM   10801 C  CD1   . ILE B 1 652 ? 119.667 142.393 162.210 1.00 8.68  ?  652 ILE B CD1   1 
ATOM   10802 N  N     . SER B 1 653 ? 122.713 139.728 157.983 1.00 14.90 ?  653 SER B N     1 
ATOM   10803 C  CA    . SER B 1 653 ? 122.967 138.444 157.335 1.00 13.87 ?  653 SER B CA    1 
ATOM   10804 C  C     . SER B 1 653 ? 122.331 137.345 158.175 1.00 20.31 ?  653 SER B C     1 
ATOM   10805 O  O     . SER B 1 653 ? 122.878 136.928 159.198 1.00 26.45 ?  653 SER B O     1 
ATOM   10806 C  CB    . SER B 1 653 ? 124.463 138.218 157.165 1.00 16.66 ?  653 SER B CB    1 
ATOM   10807 O  OG    . SER B 1 653 ? 124.880 138.568 155.860 1.00 22.31 ?  653 SER B OG    1 
ATOM   10808 N  N     . PHE B 1 654 ? 121.168 136.871 157.742 1.00 23.30 ?  654 PHE B N     1 
ATOM   10809 C  CA    . PHE B 1 654 ? 120.358 135.925 158.501 1.00 6.98  ?  654 PHE B CA    1 
ATOM   10810 C  C     . PHE B 1 654 ? 120.450 134.557 157.836 1.00 18.15 ?  654 PHE B C     1 
ATOM   10811 O  O     . PHE B 1 654 ? 119.820 134.318 156.801 1.00 27.86 ?  654 PHE B O     1 
ATOM   10812 C  CB    . PHE B 1 654 ? 118.912 136.407 158.581 1.00 13.53 ?  654 PHE B CB    1 
ATOM   10813 C  CG    . PHE B 1 654 ? 118.040 135.585 159.485 1.00 17.85 ?  654 PHE B CG    1 
ATOM   10814 C  CD1   . PHE B 1 654 ? 118.591 134.693 160.389 1.00 21.93 ?  654 PHE B CD1   1 
ATOM   10815 C  CD2   . PHE B 1 654 ? 116.667 135.710 159.434 1.00 20.97 ?  654 PHE B CD2   1 
ATOM   10816 C  CE1   . PHE B 1 654 ? 117.791 133.941 161.215 1.00 18.47 ?  654 PHE B CE1   1 
ATOM   10817 C  CE2   . PHE B 1 654 ? 115.862 134.962 160.262 1.00 24.46 ?  654 PHE B CE2   1 
ATOM   10818 C  CZ    . PHE B 1 654 ? 116.426 134.076 161.153 1.00 16.24 ?  654 PHE B CZ    1 
ATOM   10819 N  N     . THR B 1 655 ? 121.217 133.659 158.445 1.00 22.48 ?  655 THR B N     1 
ATOM   10820 C  CA    . THR B 1 655 ? 121.360 132.296 157.956 1.00 19.91 ?  655 THR B CA    1 
ATOM   10821 C  C     . THR B 1 655 ? 120.335 131.398 158.636 1.00 20.63 ?  655 THR B C     1 
ATOM   10822 O  O     . THR B 1 655 ? 120.187 131.430 159.861 1.00 29.03 ?  655 THR B O     1 
ATOM   10823 C  CB    . THR B 1 655 ? 122.774 131.777 158.219 1.00 29.28 ?  655 THR B CB    1 
ATOM   10824 O  OG1   . THR B 1 655 ? 123.717 132.556 157.475 1.00 35.51 ?  655 THR B OG1   1 
ATOM   10825 C  CG2   . THR B 1 655 ? 122.898 130.319 157.805 1.00 29.23 ?  655 THR B CG2   1 
ATOM   10826 N  N     . LEU B 1 656 ? 119.623 130.608 157.838 1.00 31.41 ?  656 LEU B N     1 
ATOM   10827 C  CA    . LEU B 1 656 ? 118.704 129.609 158.361 1.00 31.82 ?  656 LEU B CA    1 
ATOM   10828 C  C     . LEU B 1 656 ? 119.462 128.317 158.622 1.00 28.18 ?  656 LEU B C     1 
ATOM   10829 O  O     . LEU B 1 656 ? 120.148 127.803 157.736 1.00 33.03 ?  656 LEU B O     1 
ATOM   10830 C  CB    . LEU B 1 656 ? 117.555 129.357 157.385 1.00 34.25 ?  656 LEU B CB    1 
ATOM   10831 C  CG    . LEU B 1 656 ? 116.639 130.540 157.080 1.00 34.34 ?  656 LEU B CG    1 
ATOM   10832 C  CD1   . LEU B 1 656 ? 115.400 130.068 156.337 1.00 29.57 ?  656 LEU B CD1   1 
ATOM   10833 C  CD2   . LEU B 1 656 ? 116.262 131.275 158.355 1.00 25.37 ?  656 LEU B CD2   1 
ATOM   10834 N  N     . PHE B 1 657 ? 119.340 127.801 159.838 1.00 30.01 ?  657 PHE B N     1 
ATOM   10835 C  CA    . PHE B 1 657 ? 119.993 126.562 160.241 1.00 27.17 ?  657 PHE B CA    1 
ATOM   10836 C  C     . PHE B 1 657 ? 118.918 125.494 160.367 1.00 36.86 ?  657 PHE B C     1 
ATOM   10837 O  O     . PHE B 1 657 ? 118.086 125.545 161.278 1.00 39.95 ?  657 PHE B O     1 
ATOM   10838 C  CB    . PHE B 1 657 ? 120.755 126.753 161.548 1.00 31.39 ?  657 PHE B CB    1 
ATOM   10839 C  CG    . PHE B 1 657 ? 121.734 127.887 161.512 1.00 38.03 ?  657 PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 1 657 ? 123.008 127.702 161.006 1.00 32.64 ?  657 PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 1 657 ? 121.378 129.142 161.975 1.00 35.57 ?  657 PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 1 657 ? 123.910 128.742 160.968 1.00 34.17 ?  657 PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 1 657 ? 122.276 130.186 161.939 1.00 34.07 ?  657 PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 1 657 ? 123.544 129.987 161.435 1.00 38.39 ?  657 PHE B CZ    1 
ATOM   10845 N  N     . LEU B 1 658 ? 118.937 124.531 159.451 1.00 40.65 ?  658 LEU B N     1 
ATOM   10846 C  CA    . LEU B 1 658 ? 117.874 123.550 159.320 1.00 41.19 ?  658 LEU B CA    1 
ATOM   10847 C  C     . LEU B 1 658 ? 118.405 122.152 159.599 1.00 45.56 ?  658 LEU B C     1 
ATOM   10848 O  O     . LEU B 1 658 ? 119.577 121.854 159.359 1.00 48.21 ?  658 LEU B O     1 
ATOM   10849 C  CB    . LEU B 1 658 ? 117.259 123.592 157.918 1.00 41.13 ?  658 LEU B CB    1 
ATOM   10850 C  CG    . LEU B 1 658 ? 117.134 124.979 157.286 1.00 40.87 ?  658 LEU B CG    1 
ATOM   10851 C  CD1   . LEU B 1 658 ? 117.066 124.864 155.776 1.00 38.06 ?  658 LEU B CD1   1 
ATOM   10852 C  CD2   . LEU B 1 658 ? 115.916 125.706 157.828 1.00 41.11 ?  658 LEU B CD2   1 
ATOM   10853 N  N     . LYS B 1 659 ? 117.530 121.302 160.120 1.00 49.14 ?  659 LYS B N     1 
ATOM   10854 C  CA    . LYS B 1 659 ? 117.831 119.889 160.268 1.00 50.62 ?  659 LYS B CA    1 
ATOM   10855 C  C     . LYS B 1 659 ? 117.530 119.152 158.968 1.00 52.29 ?  659 LYS B C     1 
ATOM   10856 O  O     . LYS B 1 659 ? 116.833 119.657 158.086 1.00 52.44 ?  659 LYS B O     1 
ATOM   10857 C  CB    . LYS B 1 659 ? 117.030 119.283 161.421 1.00 49.58 ?  659 LYS B CB    1 
ATOM   10858 C  CG    . LYS B 1 659 ? 117.366 119.873 162.776 1.00 52.09 ?  659 LYS B CG    1 
ATOM   10859 C  CD    . LYS B 1 659 ? 116.806 119.029 163.907 1.00 52.73 ?  659 LYS B CD    1 
ATOM   10860 C  CE    . LYS B 1 659 ? 117.230 119.576 165.261 1.00 51.17 ?  659 LYS B CE    1 
ATOM   10861 N  NZ    . LYS B 1 659 ? 117.068 118.571 166.346 1.00 53.28 1  659 LYS B NZ    1 
ATOM   10862 N  N     . ASP B 1 660 ? 118.080 117.941 158.854 1.00 57.27 ?  660 ASP B N     1 
ATOM   10863 C  CA    . ASP B 1 660 ? 117.804 117.123 157.678 1.00 56.83 ?  660 ASP B CA    1 
ATOM   10864 C  C     . ASP B 1 660 ? 116.348 116.680 157.633 1.00 55.41 ?  660 ASP B C     1 
ATOM   10865 O  O     . ASP B 1 660 ? 115.807 116.442 156.549 1.00 55.37 ?  660 ASP B O     1 
ATOM   10866 C  CB    . ASP B 1 660 ? 118.731 115.908 157.650 1.00 57.50 ?  660 ASP B CB    1 
ATOM   10867 C  CG    . ASP B 1 660 ? 118.691 115.110 158.941 1.00 58.83 ?  660 ASP B CG    1 
ATOM   10868 O  OD1   . ASP B 1 660 ? 118.218 115.650 159.963 1.00 57.20 ?  660 ASP B OD1   1 
ATOM   10869 O  OD2   . ASP B 1 660 ? 119.133 113.942 158.932 1.00 59.06 -1 660 ASP B OD2   1 
ATOM   10870 N  N     . THR B 1 661 ? 115.701 116.568 158.794 1.00 52.39 ?  661 THR B N     1 
ATOM   10871 C  CA    . THR B 1 661 ? 114.310 116.143 158.849 1.00 53.63 ?  661 THR B CA    1 
ATOM   10872 C  C     . THR B 1 661 ? 113.338 117.234 158.421 1.00 56.03 ?  661 THR B C     1 
ATOM   10873 O  O     . THR B 1 661 ? 112.175 116.930 158.134 1.00 54.76 ?  661 THR B O     1 
ATOM   10874 C  CB    . THR B 1 661 ? 113.958 115.680 160.264 1.00 54.73 ?  661 THR B CB    1 
ATOM   10875 O  OG1   . THR B 1 661 ? 114.210 116.744 161.190 1.00 52.56 ?  661 THR B OG1   1 
ATOM   10876 C  CG2   . THR B 1 661 ? 114.795 114.473 160.648 1.00 54.63 ?  661 THR B CG2   1 
ATOM   10877 N  N     . MET B 1 662 ? 113.780 118.487 158.374 1.00 55.39 ?  662 MET B N     1 
ATOM   10878 C  CA    . MET B 1 662 ? 112.892 119.578 158.001 1.00 51.19 ?  662 MET B CA    1 
ATOM   10879 C  C     . MET B 1 662 ? 112.500 119.472 156.533 1.00 52.53 ?  662 MET B C     1 
ATOM   10880 O  O     . MET B 1 662 ? 113.333 119.186 155.668 1.00 53.26 ?  662 MET B O     1 
ATOM   10881 C  CB    . MET B 1 662 ? 113.560 120.924 158.277 1.00 51.81 ?  662 MET B CB    1 
ATOM   10882 C  CG    . MET B 1 662 ? 113.149 121.548 159.599 1.00 51.85 ?  662 MET B CG    1 
ATOM   10883 S  SD    . MET B 1 662 ? 114.141 122.984 160.042 1.00 60.76 ?  662 MET B SD    1 
ATOM   10884 C  CE    . MET B 1 662 ? 113.022 123.834 161.150 1.00 51.82 ?  662 MET B CE    1 
ATOM   10885 N  N     . THR B 1 663 ? 111.220 119.702 156.257 1.00 48.30 ?  663 THR B N     1 
ATOM   10886 C  CA    . THR B 1 663 ? 110.682 119.568 154.915 1.00 45.04 ?  663 THR B CA    1 
ATOM   10887 C  C     . THR B 1 663 ? 110.736 120.906 154.180 1.00 46.54 ?  663 THR B C     1 
ATOM   10888 O  O     . THR B 1 663 ? 111.207 121.919 154.702 1.00 49.48 ?  663 THR B O     1 
ATOM   10889 C  CB    . THR B 1 663 ? 109.247 119.045 154.966 1.00 41.89 ?  663 THR B CB    1 
ATOM   10890 O  OG1   . THR B 1 663 ? 108.555 119.655 156.062 1.00 42.37 ?  663 THR B OG1   1 
ATOM   10891 C  CG2   . THR B 1 663 ? 109.236 117.539 155.156 1.00 44.20 ?  663 THR B CG2   1 
ATOM   10892 N  N     . THR B 1 664 ? 110.249 120.901 152.938 1.00 41.28 ?  664 THR B N     1 
ATOM   10893 C  CA    . THR B 1 664 ? 110.079 122.148 152.200 1.00 38.99 ?  664 THR B CA    1 
ATOM   10894 C  C     . THR B 1 664 ? 109.062 123.051 152.889 1.00 38.44 ?  664 THR B C     1 
ATOM   10895 O  O     . THR B 1 664 ? 109.243 124.275 152.950 1.00 41.92 ?  664 THR B O     1 
ATOM   10896 C  CB    . THR B 1 664 ? 109.657 121.838 150.761 1.00 41.98 ?  664 THR B CB    1 
ATOM   10897 O  OG1   . THR B 1 664 ? 110.807 121.452 149.997 1.00 40.54 ?  664 THR B OG1   1 
ATOM   10898 C  CG2   . THR B 1 664 ? 108.989 123.034 150.103 1.00 41.48 ?  664 THR B CG2   1 
ATOM   10899 N  N     . ARG B 1 665 ? 107.997 122.460 153.434 1.00 39.22 ?  665 ARG B N     1 
ATOM   10900 C  CA    . ARG B 1 665 ? 106.981 123.246 154.124 1.00 38.75 ?  665 ARG B CA    1 
ATOM   10901 C  C     . ARG B 1 665 ? 107.558 123.952 155.343 1.00 41.96 ?  665 ARG B C     1 
ATOM   10902 O  O     . ARG B 1 665 ? 107.170 125.082 155.649 1.00 47.88 ?  665 ARG B O     1 
ATOM   10903 C  CB    . ARG B 1 665 ? 105.811 122.353 154.532 1.00 40.49 ?  665 ARG B CB    1 
ATOM   10904 C  CG    . ARG B 1 665 ? 104.519 123.108 154.783 1.00 37.78 ?  665 ARG B CG    1 
ATOM   10905 C  CD    . ARG B 1 665 ? 103.587 122.321 155.683 1.00 41.85 ?  665 ARG B CD    1 
ATOM   10906 N  NE    . ARG B 1 665 ? 103.851 122.573 157.094 1.00 46.72 ?  665 ARG B NE    1 
ATOM   10907 C  CZ    . ARG B 1 665 ? 103.029 122.245 158.080 1.00 48.71 ?  665 ARG B CZ    1 
ATOM   10908 N  NH1   . ARG B 1 665 ? 101.877 121.639 157.848 1.00 43.92 1  665 ARG B NH1   1 
ATOM   10909 N  NH2   . ARG B 1 665 ? 103.372 122.534 159.333 1.00 46.34 ?  665 ARG B NH2   1 
ATOM   10910 N  N     . ASP B 1 666 ? 108.480 123.304 156.055 1.00 39.87 ?  666 ASP B N     1 
ATOM   10911 C  CA    . ASP B 1 666 ? 109.078 123.936 157.228 1.00 35.12 ?  666 ASP B CA    1 
ATOM   10912 C  C     . ASP B 1 666 ? 109.942 125.131 156.839 1.00 40.01 ?  666 ASP B C     1 
ATOM   10913 O  O     . ASP B 1 666 ? 109.897 126.177 157.497 1.00 42.48 ?  666 ASP B O     1 
ATOM   10914 C  CB    . ASP B 1 666 ? 109.895 122.913 158.015 1.00 42.29 ?  666 ASP B CB    1 
ATOM   10915 C  CG    . ASP B 1 666 ? 109.037 121.813 158.599 1.00 49.42 ?  666 ASP B CG    1 
ATOM   10916 O  OD1   . ASP B 1 666 ? 107.910 122.114 159.048 1.00 46.16 ?  666 ASP B OD1   1 
ATOM   10917 O  OD2   . ASP B 1 666 ? 109.485 120.648 158.613 1.00 50.89 -1 666 ASP B OD2   1 
ATOM   10918 N  N     . LEU B 1 667 ? 110.732 124.998 155.771 1.00 35.25 ?  667 LEU B N     1 
ATOM   10919 C  CA    . LEU B 1 667 ? 111.525 126.127 155.297 1.00 28.35 ?  667 LEU B CA    1 
ATOM   10920 C  C     . LEU B 1 667 ? 110.626 127.267 154.837 1.00 30.94 ?  667 LEU B C     1 
ATOM   10921 O  O     . LEU B 1 667 ? 110.902 128.440 155.115 1.00 32.33 ?  667 LEU B O     1 
ATOM   10922 C  CB    . LEU B 1 667 ? 112.450 125.677 154.166 1.00 31.84 ?  667 LEU B CB    1 
ATOM   10923 C  CG    . LEU B 1 667 ? 113.848 126.296 154.084 1.00 33.11 ?  667 LEU B CG    1 
ATOM   10924 C  CD1   . LEU B 1 667 ? 114.676 125.572 153.040 1.00 33.42 ?  667 LEU B CD1   1 
ATOM   10925 C  CD2   . LEU B 1 667 ? 113.795 127.780 153.775 1.00 38.02 ?  667 LEU B CD2   1 
ATOM   10926 N  N     . ASN B 1 668 ? 109.542 126.940 154.130 1.00 36.62 ?  668 ASN B N     1 
ATOM   10927 C  CA    . ASN B 1 668 ? 108.599 127.968 153.706 1.00 23.50 ?  668 ASN B CA    1 
ATOM   10928 C  C     . ASN B 1 668 ? 107.951 128.650 154.903 1.00 22.91 ?  668 ASN B C     1 
ATOM   10929 O  O     . ASN B 1 668 ? 107.736 129.866 154.891 1.00 31.40 ?  668 ASN B O     1 
ATOM   10930 C  CB    . ASN B 1 668 ? 107.536 127.361 152.794 1.00 28.51 ?  668 ASN B CB    1 
ATOM   10931 C  CG    . ASN B 1 668 ? 107.983 127.284 151.353 1.00 33.12 ?  668 ASN B CG    1 
ATOM   10932 O  OD1   . ASN B 1 668 ? 107.699 126.313 150.655 1.00 40.18 ?  668 ASN B OD1   1 
ATOM   10933 N  ND2   . ASN B 1 668 ? 108.691 128.310 150.899 1.00 30.35 ?  668 ASN B ND2   1 
ATOM   10934 N  N     . ARG B 1 669 ? 107.621 127.881 155.941 1.00 31.32 ?  669 ARG B N     1 
ATOM   10935 C  CA    . ARG B 1 669 ? 107.049 128.464 157.148 1.00 32.98 ?  669 ARG B CA    1 
ATOM   10936 C  C     . ARG B 1 669 ? 108.035 129.407 157.821 1.00 29.08 ?  669 ARG B C     1 
ATOM   10937 O  O     . ARG B 1 669 ? 107.650 130.480 158.298 1.00 28.03 ?  669 ARG B O     1 
ATOM   10938 C  CB    . ARG B 1 669 ? 106.624 127.358 158.112 1.00 32.09 ?  669 ARG B CB    1 
ATOM   10939 C  CG    . ARG B 1 669 ? 105.128 127.133 158.166 1.00 28.78 ?  669 ARG B CG    1 
ATOM   10940 C  CD    . ARG B 1 669 ? 104.762 126.133 159.249 1.00 33.13 ?  669 ARG B CD    1 
ATOM   10941 N  NE    . ARG B 1 669 ? 104.716 126.737 160.576 1.00 35.06 ?  669 ARG B NE    1 
ATOM   10942 C  CZ    . ARG B 1 669 ? 103.809 127.620 160.973 1.00 36.71 ?  669 ARG B CZ    1 
ATOM   10943 N  NH1   . ARG B 1 669 ? 102.839 128.026 160.171 1.00 35.18 1  669 ARG B NH1   1 
ATOM   10944 N  NH2   . ARG B 1 669 ? 103.875 128.105 162.210 1.00 38.29 ?  669 ARG B NH2   1 
ATOM   10945 N  N     . ILE B 1 670 ? 109.312 129.022 157.873 1.00 25.86 ?  670 ILE B N     1 
ATOM   10946 C  CA    . ILE B 1 670 ? 110.325 129.905 158.446 1.00 25.29 ?  670 ILE B CA    1 
ATOM   10947 C  C     . ILE B 1 670 ? 110.431 131.191 157.635 1.00 24.13 ?  670 ILE B C     1 
ATOM   10948 O  O     . ILE B 1 670 ? 110.500 132.290 158.197 1.00 27.90 ?  670 ILE B O     1 
ATOM   10949 C  CB    . ILE B 1 670 ? 111.681 129.182 158.541 1.00 32.05 ?  670 ILE B CB    1 
ATOM   10950 C  CG1   . ILE B 1 670 ? 111.595 128.002 159.507 1.00 31.60 ?  670 ILE B CG1   1 
ATOM   10951 C  CG2   . ILE B 1 670 ? 112.766 130.145 158.989 1.00 28.90 ?  670 ILE B CG2   1 
ATOM   10952 C  CD1   . ILE B 1 670 ? 112.623 126.929 159.242 1.00 27.50 ?  670 ILE B CD1   1 
ATOM   10953 N  N     . ASP B 1 671 ? 110.438 131.076 156.305 1.00 25.07 ?  671 ASP B N     1 
ATOM   10954 C  CA    . ASP B 1 671 ? 110.522 132.264 155.457 1.00 20.62 ?  671 ASP B CA    1 
ATOM   10955 C  C     . ASP B 1 671 ? 109.310 133.172 155.643 1.00 21.54 ?  671 ASP B C     1 
ATOM   10956 O  O     . ASP B 1 671 ? 109.447 134.398 155.713 1.00 30.77 ?  671 ASP B O     1 
ATOM   10957 C  CB    . ASP B 1 671 ? 110.663 131.859 153.991 1.00 21.88 ?  671 ASP B CB    1 
ATOM   10958 C  CG    . ASP B 1 671 ? 111.870 130.976 153.742 1.00 40.20 ?  671 ASP B CG    1 
ATOM   10959 O  OD1   . ASP B 1 671 ? 112.795 130.981 154.580 1.00 39.79 ?  671 ASP B OD1   1 
ATOM   10960 O  OD2   . ASP B 1 671 ? 111.893 130.275 152.708 1.00 39.34 -1 671 ASP B OD2   1 
ATOM   10961 N  N     . LEU B 1 672 ? 108.115 132.587 155.731 1.00 21.76 ?  672 LEU B N     1 
ATOM   10962 C  CA    . LEU B 1 672 ? 106.906 133.387 155.880 1.00 16.89 ?  672 LEU B CA    1 
ATOM   10963 C  C     . LEU B 1 672 ? 106.813 134.020 157.261 1.00 18.59 ?  672 LEU B C     1 
ATOM   10964 O  O     . LEU B 1 672 ? 106.281 135.127 157.395 1.00 24.78 ?  672 LEU B O     1 
ATOM   10965 C  CB    . LEU B 1 672 ? 105.671 132.531 155.605 1.00 24.55 ?  672 LEU B CB    1 
ATOM   10966 C  CG    . LEU B 1 672 ? 105.523 132.040 154.165 1.00 24.78 ?  672 LEU B CG    1 
ATOM   10967 C  CD1   . LEU B 1 672 ? 104.544 130.882 154.093 1.00 20.61 ?  672 LEU B CD1   1 
ATOM   10968 C  CD2   . LEU B 1 672 ? 105.096 133.176 153.251 1.00 23.39 ?  672 LEU B CD2   1 
ATOM   10969 N  N     . TYR B 1 673 ? 107.313 133.344 158.296 1.00 22.69 ?  673 TYR B N     1 
ATOM   10970 C  CA    . TYR B 1 673 ? 107.346 133.954 159.619 1.00 14.92 ?  673 TYR B CA    1 
ATOM   10971 C  C     . TYR B 1 673 ? 108.384 135.065 159.684 1.00 18.79 ?  673 TYR B C     1 
ATOM   10972 O  O     . TYR B 1 673 ? 108.182 136.072 160.373 1.00 25.74 ?  673 TYR B O     1 
ATOM   10973 C  CB    . TYR B 1 673 ? 107.625 132.896 160.683 1.00 19.00 ?  673 TYR B CB    1 
ATOM   10974 C  CG    . TYR B 1 673 ? 107.639 133.448 162.089 1.00 20.29 ?  673 TYR B CG    1 
ATOM   10975 C  CD1   . TYR B 1 673 ? 106.497 134.000 162.648 1.00 22.11 ?  673 TYR B CD1   1 
ATOM   10976 C  CD2   . TYR B 1 673 ? 108.794 133.415 162.854 1.00 15.22 ?  673 TYR B CD2   1 
ATOM   10977 C  CE1   . TYR B 1 673 ? 106.505 134.504 163.930 1.00 20.83 ?  673 TYR B CE1   1 
ATOM   10978 C  CE2   . TYR B 1 673 ? 108.812 133.916 164.136 1.00 24.30 ?  673 TYR B CE2   1 
ATOM   10979 C  CZ    . TYR B 1 673 ? 107.666 134.459 164.670 1.00 25.45 ?  673 TYR B CZ    1 
ATOM   10980 O  OH    . TYR B 1 673 ? 107.681 134.961 165.949 1.00 29.84 ?  673 TYR B OH    1 
ATOM   10981 N  N     . ALA B 1 674 ? 109.507 134.894 158.986 1.00 21.72 ?  674 ALA B N     1 
ATOM   10982 C  CA    . ALA B 1 674 ? 110.479 135.975 158.876 1.00 12.28 ?  674 ALA B CA    1 
ATOM   10983 C  C     . ALA B 1 674 ? 109.870 137.182 158.176 1.00 17.86 ?  674 ALA B C     1 
ATOM   10984 O  O     . ALA B 1 674 ? 110.041 138.321 158.623 1.00 30.35 ?  674 ALA B O     1 
ATOM   10985 C  CB    . ALA B 1 674 ? 111.720 135.484 158.132 1.00 10.16 ?  674 ALA B CB    1 
ATOM   10986 N  N     . HIS B 1 675 ? 109.139 136.948 157.088 1.00 15.42 ?  675 HIS B N     1 
ATOM   10987 C  CA    . HIS B 1 675 ? 108.443 138.038 156.412 1.00 16.56 ?  675 HIS B CA    1 
ATOM   10988 C  C     . HIS B 1 675 ? 107.422 138.695 157.334 1.00 21.20 ?  675 HIS B C     1 
ATOM   10989 O  O     . HIS B 1 675 ? 107.284 139.923 157.347 1.00 26.90 ?  675 HIS B O     1 
ATOM   10990 C  CB    . HIS B 1 675 ? 107.768 137.517 155.145 1.00 18.38 ?  675 HIS B CB    1 
ATOM   10991 C  CG    . HIS B 1 675 ? 106.896 138.527 154.468 1.00 21.58 ?  675 HIS B CG    1 
ATOM   10992 N  ND1   . HIS B 1 675 ? 105.543 138.627 154.716 1.00 27.58 ?  675 HIS B ND1   1 
ATOM   10993 C  CD2   . HIS B 1 675 ? 107.182 139.486 153.557 1.00 15.77 ?  675 HIS B CD2   1 
ATOM   10994 C  CE1   . HIS B 1 675 ? 105.035 139.603 153.987 1.00 25.50 ?  675 HIS B CE1   1 
ATOM   10995 N  NE2   . HIS B 1 675 ? 106.008 140.139 153.274 1.00 29.27 ?  675 HIS B NE2   1 
ATOM   10996 N  N     . HIS B 1 676 ? 106.697 137.889 158.109 1.00 22.09 ?  676 HIS B N     1 
ATOM   10997 C  CA    . HIS B 1 676 ? 105.686 138.421 159.017 1.00 20.05 ?  676 HIS B CA    1 
ATOM   10998 C  C     . HIS B 1 676 ? 106.315 139.259 160.123 1.00 26.00 ?  676 HIS B C     1 
ATOM   10999 O  O     . HIS B 1 676 ? 105.744 140.271 160.543 1.00 25.33 ?  676 HIS B O     1 
ATOM   11000 C  CB    . HIS B 1 676 ? 104.871 137.273 159.610 1.00 24.17 ?  676 HIS B CB    1 
ATOM   11001 C  CG    . HIS B 1 676 ? 103.932 137.694 160.697 1.00 22.97 ?  676 HIS B CG    1 
ATOM   11002 N  ND1   . HIS B 1 676 ? 102.881 138.560 160.479 1.00 21.33 ?  676 HIS B ND1   1 
ATOM   11003 C  CD2   . HIS B 1 676 ? 103.884 137.367 162.009 1.00 25.21 ?  676 HIS B CD2   1 
ATOM   11004 C  CE1   . HIS B 1 676 ? 102.227 138.747 161.611 1.00 28.69 ?  676 HIS B CE1   1 
ATOM   11005 N  NE2   . HIS B 1 676 ? 102.816 138.036 162.555 1.00 27.27 ?  676 HIS B NE2   1 
ATOM   11006 N  N     . ARG B 1 677 ? 107.486 138.856 160.604 1.00 24.54 ?  677 ARG B N     1 
ATOM   11007 C  CA    . ARG B 1 677 ? 108.134 139.511 161.731 1.00 19.48 ?  677 ARG B CA    1 
ATOM   11008 C  C     . ARG B 1 677 ? 108.976 140.711 161.322 1.00 23.24 ?  677 ARG B C     1 
ATOM   11009 O  O     . ARG B 1 677 ? 109.604 141.330 162.187 1.00 30.96 ?  677 ARG B O     1 
ATOM   11010 C  CB    . ARG B 1 677 ? 109.004 138.508 162.490 1.00 19.00 ?  677 ARG B CB    1 
ATOM   11011 C  CG    . ARG B 1 677 ? 108.230 137.627 163.445 1.00 19.85 ?  677 ARG B CG    1 
ATOM   11012 C  CD    . ARG B 1 677 ? 107.676 138.428 164.606 1.00 23.48 ?  677 ARG B CD    1 
ATOM   11013 N  NE    . ARG B 1 677 ? 108.665 138.600 165.662 1.00 30.10 ?  677 ARG B NE    1 
ATOM   11014 C  CZ    . ARG B 1 677 ? 109.080 139.774 166.114 1.00 34.53 ?  677 ARG B CZ    1 
ATOM   11015 N  NH1   . ARG B 1 677 ? 108.608 140.909 165.624 1.00 29.29 1  677 ARG B NH1   1 
ATOM   11016 N  NH2   . ARG B 1 677 ? 109.993 139.812 167.080 1.00 29.06 ?  677 ARG B NH2   1 
ATOM   11017 N  N     . GLY B 1 678 ? 109.009 141.054 160.040 1.00 22.05 ?  678 GLY B N     1 
ATOM   11018 C  CA    . GLY B 1 678 ? 109.764 142.199 159.583 1.00 12.98 ?  678 GLY B CA    1 
ATOM   11019 C  C     . GLY B 1 678 ? 111.188 141.914 159.171 1.00 16.33 ?  678 GLY B C     1 
ATOM   11020 O  O     . GLY B 1 678 ? 111.976 142.857 159.041 1.00 24.40 ?  678 GLY B O     1 
ATOM   11021 N  N     . ILE B 1 679 ? 111.549 140.646 158.969 1.00 18.05 ?  679 ILE B N     1 
ATOM   11022 C  CA    . ILE B 1 679 ? 112.890 140.319 158.503 1.00 15.19 ?  679 ILE B CA    1 
ATOM   11023 C  C     . ILE B 1 679 ? 113.071 140.867 157.097 1.00 21.06 ?  679 ILE B C     1 
ATOM   11024 O  O     . ILE B 1 679 ? 112.201 140.707 156.233 1.00 28.13 ?  679 ILE B O     1 
ATOM   11025 C  CB    . ILE B 1 679 ? 113.121 138.802 158.558 1.00 13.44 ?  679 ILE B CB    1 
ATOM   11026 C  CG1   . ILE B 1 679 ? 113.168 138.318 160.011 1.00 13.99 ?  679 ILE B CG1   1 
ATOM   11027 C  CG2   . ILE B 1 679 ? 114.388 138.414 157.818 1.00 15.28 ?  679 ILE B CG2   1 
ATOM   11028 C  CD1   . ILE B 1 679 ? 114.279 138.919 160.813 1.00 18.66 ?  679 ILE B CD1   1 
ATOM   11029 N  N     . LYS B 1 680 ? 114.199 141.533 156.866 1.00 10.64 ?  680 LYS B N     1 
ATOM   11030 C  CA    . LYS B 1 680 ? 114.452 142.169 155.580 1.00 5.62  ?  680 LYS B CA    1 
ATOM   11031 C  C     . LYS B 1 680 ? 115.061 141.202 154.570 1.00 0.15  ?  680 LYS B C     1 
ATOM   11032 O  O     . LYS B 1 680 ? 114.633 141.159 153.415 1.00 19.15 ?  680 LYS B O     1 
ATOM   11033 C  CB    . LYS B 1 680 ? 115.367 143.379 155.769 1.00 11.81 ?  680 LYS B CB    1 
ATOM   11034 C  CG    . LYS B 1 680 ? 114.764 144.497 156.590 1.00 0.00  ?  680 LYS B CG    1 
ATOM   11035 C  CD    . LYS B 1 680 ? 115.679 145.704 156.602 1.00 2.10  ?  680 LYS B CD    1 
ATOM   11036 C  CE    . LYS B 1 680 ? 115.245 146.710 157.643 1.00 12.27 ?  680 LYS B CE    1 
ATOM   11037 N  NZ    . LYS B 1 680 ? 116.085 147.934 157.622 1.00 15.62 1  680 LYS B NZ    1 
ATOM   11038 N  N     . THR B 1 681 ? 116.062 140.434 154.985 1.00 6.84  ?  681 THR B N     1 
ATOM   11039 C  CA    . THR B 1 681 ? 116.742 139.509 154.092 1.00 7.07  ?  681 THR B CA    1 
ATOM   11040 C  C     . THR B 1 681 ? 116.974 138.187 154.806 1.00 12.62 ?  681 THR B C     1 
ATOM   11041 O  O     . THR B 1 681 ? 117.089 138.137 156.033 1.00 25.64 ?  681 THR B O     1 
ATOM   11042 C  CB    . THR B 1 681 ? 118.088 140.069 153.597 1.00 13.07 ?  681 THR B CB    1 
ATOM   11043 O  OG1   . THR B 1 681 ? 118.835 140.585 154.705 1.00 29.37 ?  681 THR B OG1   1 
ATOM   11044 C  CG2   . THR B 1 681 ? 117.878 141.175 152.580 1.00 7.92  ?  681 THR B CG2   1 
ATOM   11045 N  N     . ILE B 1 682 ? 117.039 137.115 154.023 1.00 13.30 ?  682 ILE B N     1 
ATOM   11046 C  CA    . ILE B 1 682 ? 117.425 135.797 154.508 1.00 8.69  ?  682 ILE B CA    1 
ATOM   11047 C  C     . ILE B 1 682 ? 118.647 135.350 153.720 1.00 17.51 ?  682 ILE B C     1 
ATOM   11048 O  O     . ILE B 1 682 ? 118.615 135.309 152.486 1.00 13.41 ?  682 ILE B O     1 
ATOM   11049 C  CB    . ILE B 1 682 ? 116.280 134.777 154.374 1.00 11.16 ?  682 ILE B CB    1 
ATOM   11050 C  CG1   . ILE B 1 682 ? 115.029 135.285 155.091 1.00 19.69 ?  682 ILE B CG1   1 
ATOM   11051 C  CG2   . ILE B 1 682 ? 116.703 133.448 154.948 1.00 18.50 ?  682 ILE B CG2   1 
ATOM   11052 C  CD1   . ILE B 1 682 ? 113.915 134.270 155.167 1.00 21.11 ?  682 ILE B CD1   1 
ATOM   11053 N  N     . TYR B 1 683 ? 119.725 135.022 154.433 1.00 23.45 ?  683 TYR B N     1 
ATOM   11054 C  CA    . TYR B 1 683 ? 121.005 134.770 153.774 1.00 18.72 ?  683 TYR B CA    1 
ATOM   11055 C  C     . TYR B 1 683 ? 121.106 133.346 153.237 1.00 21.31 ?  683 TYR B C     1 
ATOM   11056 O  O     . TYR B 1 683 ? 121.160 133.128 152.025 1.00 36.30 ?  683 TYR B O     1 
ATOM   11057 C  CB    . TYR B 1 683 ? 122.149 135.064 154.749 1.00 18.95 ?  683 TYR B CB    1 
ATOM   11058 C  CG    . TYR B 1 683 ? 123.523 135.061 154.126 1.00 13.76 ?  683 TYR B CG    1 
ATOM   11059 C  CD1   . TYR B 1 683 ? 123.692 135.290 152.768 1.00 10.60 ?  683 TYR B CD1   1 
ATOM   11060 C  CD2   . TYR B 1 683 ? 124.654 134.839 154.898 1.00 10.01 ?  683 TYR B CD2   1 
ATOM   11061 C  CE1   . TYR B 1 683 ? 124.943 135.290 152.198 1.00 19.38 ?  683 TYR B CE1   1 
ATOM   11062 C  CE2   . TYR B 1 683 ? 125.912 134.840 154.334 1.00 19.11 ?  683 TYR B CE2   1 
ATOM   11063 C  CZ    . TYR B 1 683 ? 126.050 135.067 152.984 1.00 21.30 ?  683 TYR B CZ    1 
ATOM   11064 O  OH    . TYR B 1 683 ? 127.301 135.069 152.413 1.00 23.65 ?  683 TYR B OH    1 
ATOM   11065 N  N     . TYR B 1 684 ? 121.107 132.359 154.124 1.00 29.13 ?  684 TYR B N     1 
ATOM   11066 C  CA    . TYR B 1 684 ? 121.469 131.009 153.732 1.00 22.22 ?  684 TYR B CA    1 
ATOM   11067 C  C     . TYR B 1 684 ? 120.559 130.008 154.420 1.00 37.02 ?  684 TYR B C     1 
ATOM   11068 O  O     . TYR B 1 684 ? 120.074 130.244 155.528 1.00 37.92 ?  684 TYR B O     1 
ATOM   11069 C  CB    . TYR B 1 684 ? 122.927 130.692 154.084 1.00 24.34 ?  684 TYR B CB    1 
ATOM   11070 C  CG    . TYR B 1 684 ? 123.894 130.852 152.939 1.00 25.68 ?  684 TYR B CG    1 
ATOM   11071 C  CD1   . TYR B 1 684 ? 123.552 130.454 151.655 1.00 26.99 ?  684 TYR B CD1   1 
ATOM   11072 C  CD2   . TYR B 1 684 ? 125.151 131.399 153.143 1.00 30.41 ?  684 TYR B CD2   1 
ATOM   11073 C  CE1   . TYR B 1 684 ? 124.436 130.598 150.605 1.00 33.90 ?  684 TYR B CE1   1 
ATOM   11074 C  CE2   . TYR B 1 684 ? 126.042 131.549 152.101 1.00 25.07 ?  684 TYR B CE2   1 
ATOM   11075 C  CZ    . TYR B 1 684 ? 125.680 131.147 150.835 1.00 30.64 ?  684 TYR B CZ    1 
ATOM   11076 O  OH    . TYR B 1 684 ? 126.566 131.294 149.793 1.00 35.44 ?  684 TYR B OH    1 
ATOM   11077 N  N     . ALA B 1 685 ? 120.340 128.887 153.747 1.00 37.12 ?  685 ALA B N     1 
ATOM   11078 C  CA    . ALA B 1 685 ? 119.653 127.737 154.319 1.00 33.67 ?  685 ALA B CA    1 
ATOM   11079 C  C     . ALA B 1 685 ? 120.715 126.661 154.530 1.00 34.24 ?  685 ALA B C     1 
ATOM   11080 O  O     . ALA B 1 685 ? 121.066 125.923 153.608 1.00 42.25 ?  685 ALA B O     1 
ATOM   11081 C  CB    . ALA B 1 685 ? 118.527 127.260 153.413 1.00 31.43 ?  685 ALA B CB    1 
ATOM   11082 N  N     . ARG B 1 686 ? 121.233 126.584 155.752 1.00 32.67 ?  686 ARG B N     1 
ATOM   11083 C  CA    . ARG B 1 686 ? 122.251 125.603 156.101 1.00 38.58 ?  686 ARG B CA    1 
ATOM   11084 C  C     . ARG B 1 686 ? 121.581 124.401 156.749 1.00 41.88 ?  686 ARG B C     1 
ATOM   11085 O  O     . ARG B 1 686 ? 120.909 124.537 157.777 1.00 42.46 ?  686 ARG B O     1 
ATOM   11086 C  CB    . ARG B 1 686 ? 123.292 126.213 157.038 1.00 40.04 ?  686 ARG B CB    1 
ATOM   11087 C  CG    . ARG B 1 686 ? 124.377 126.993 156.324 1.00 40.60 ?  686 ARG B CG    1 
ATOM   11088 C  CD    . ARG B 1 686 ? 125.616 127.130 157.191 1.00 44.30 ?  686 ARG B CD    1 
ATOM   11089 N  NE    . ARG B 1 686 ? 126.467 125.950 157.121 1.00 46.43 ?  686 ARG B NE    1 
ATOM   11090 C  CZ    . ARG B 1 686 ? 127.793 125.983 157.086 1.00 48.20 ?  686 ARG B CZ    1 
ATOM   11091 N  NH1   . ARG B 1 686 ? 128.455 127.128 157.092 1.00 43.79 1  686 ARG B NH1   1 
ATOM   11092 N  NH2   . ARG B 1 686 ? 128.471 124.840 157.039 1.00 47.81 ?  686 ARG B NH2   1 
ATOM   11093 N  N     . THR B 1 687 ? 121.765 123.228 156.152 1.00 46.89 ?  687 THR B N     1 
ATOM   11094 C  CA    . THR B 1 687 ? 121.147 121.998 156.621 1.00 50.40 ?  687 THR B CA    1 
ATOM   11095 C  C     . THR B 1 687 ? 122.194 121.104 157.270 1.00 49.85 ?  687 THR B C     1 
ATOM   11096 O  O     . THR B 1 687 ? 123.319 120.988 156.776 1.00 51.44 ?  687 THR B O     1 
ATOM   11097 C  CB    . THR B 1 687 ? 120.462 121.252 155.473 1.00 47.33 ?  687 THR B CB    1 
ATOM   11098 O  OG1   . THR B 1 687 ? 119.832 122.194 154.596 1.00 44.31 ?  687 THR B OG1   1 
ATOM   11099 C  CG2   . THR B 1 687 ? 119.414 120.294 156.011 1.00 45.39 ?  687 THR B CG2   1 
ATOM   11100 N  N     . LYS B 1 688 ? 121.818 120.478 158.380 1.00 47.38 ?  688 LYS B N     1 
ATOM   11101 C  CA    . LYS B 1 688 ? 122.713 119.573 159.090 1.00 49.75 ?  688 LYS B CA    1 
ATOM   11102 C  C     . LYS B 1 688 ? 122.540 118.140 158.597 1.00 54.70 ?  688 LYS B C     1 
ATOM   11103 O  O     . LYS B 1 688 ? 121.419 117.675 158.395 1.00 55.57 ?  688 LYS B O     1 
ATOM   11104 C  CB    . LYS B 1 688 ? 122.464 119.642 160.597 1.00 47.73 ?  688 LYS B CB    1 
ATOM   11105 C  CG    . LYS B 1 688 ? 123.530 118.953 161.429 1.00 49.97 ?  688 LYS B CG    1 
ATOM   11106 C  CD    . LYS B 1 688 ? 123.494 119.426 162.870 1.00 50.55 ?  688 LYS B CD    1 
ATOM   11107 C  CE    . LYS B 1 688 ? 124.693 118.913 163.648 1.00 52.82 ?  688 LYS B CE    1 
ATOM   11108 N  NZ    . LYS B 1 688 ? 124.722 119.455 165.034 1.00 54.26 ?  688 LYS B NZ    1 
ATOM   11109 N  N     . ASP C 2 37  ? 134.884 76.538  118.370 1.00 45.99 ?  16  ASP C N     1 
ATOM   11110 C  CA    . ASP C 2 37  ? 134.434 76.910  117.024 1.00 45.47 ?  16  ASP C CA    1 
ATOM   11111 C  C     . ASP C 2 37  ? 133.358 77.996  116.993 1.00 44.13 ?  16  ASP C C     1 
ATOM   11112 O  O     . ASP C 2 37  ? 132.975 78.455  115.915 1.00 44.46 ?  16  ASP C O     1 
ATOM   11113 C  CB    . ASP C 2 37  ? 133.918 75.670  116.291 1.00 45.90 ?  16  ASP C CB    1 
ATOM   11114 C  CG    . ASP C 2 37  ? 134.884 74.513  116.364 1.00 47.25 ?  16  ASP C CG    1 
ATOM   11115 O  OD1   . ASP C 2 37  ? 136.108 74.749  116.272 1.00 47.99 ?  16  ASP C OD1   1 
ATOM   11116 O  OD2   . ASP C 2 37  ? 134.416 73.366  116.518 1.00 49.50 -1 16  ASP C OD2   1 
ATOM   11117 N  N     . PHE C 2 38  ? 132.874 78.409  118.161 1.00 42.17 ?  17  PHE C N     1 
ATOM   11118 C  CA    . PHE C 2 38  ? 131.687 79.270  118.217 1.00 40.67 ?  17  PHE C CA    1 
ATOM   11119 C  C     . PHE C 2 38  ? 131.745 80.495  119.137 1.00 39.46 ?  17  PHE C C     1 
ATOM   11120 O  O     . PHE C 2 38  ? 131.011 81.461  118.916 1.00 39.17 ?  17  PHE C O     1 
ATOM   11121 C  CB    . PHE C 2 38  ? 130.438 78.429  118.537 1.00 40.24 ?  17  PHE C CB    1 
ATOM   11122 C  CG    . PHE C 2 38  ? 130.556 77.601  119.795 1.00 39.58 ?  17  PHE C CG    1 
ATOM   11123 C  CD1   . PHE C 2 38  ? 130.229 78.144  121.038 1.00 38.78 ?  17  PHE C CD1   1 
ATOM   11124 C  CD2   . PHE C 2 38  ? 130.981 76.273  119.736 1.00 39.43 ?  17  PHE C CD2   1 
ATOM   11125 C  CE1   . PHE C 2 38  ? 130.325 77.382  122.203 1.00 38.07 ?  17  PHE C CE1   1 
ATOM   11126 C  CE2   . PHE C 2 38  ? 131.082 75.501  120.898 1.00 39.10 ?  17  PHE C CE2   1 
ATOM   11127 C  CZ    . PHE C 2 38  ? 130.755 76.059  122.134 1.00 38.63 ?  17  PHE C CZ    1 
ATOM   11128 N  N     . THR C 2 39  ? 132.598 80.459  120.163 1.00 38.22 ?  18  THR C N     1 
ATOM   11129 C  CA    . THR C 2 39  ? 132.612 81.527  121.177 1.00 37.09 ?  18  THR C CA    1 
ATOM   11130 C  C     . THR C 2 39  ? 132.837 82.925  120.576 1.00 36.84 ?  18  THR C C     1 
ATOM   11131 O  O     . THR C 2 39  ? 132.120 83.877  120.926 1.00 36.13 ?  18  THR C O     1 
ATOM   11132 C  CB    . THR C 2 39  ? 133.578 81.228  122.361 1.00 36.59 ?  18  THR C CB    1 
ATOM   11133 O  OG1   . THR C 2 39  ? 132.998 80.219  123.193 1.00 36.50 ?  18  THR C OG1   1 
ATOM   11134 C  CG2   . THR C 2 39  ? 133.794 82.460  123.217 1.00 36.06 ?  18  THR C CG2   1 
ATOM   11135 N  N     . GLN C 2 40  ? 133.808 83.038  119.665 1.00 37.01 ?  19  GLN C N     1 
ATOM   11136 C  CA    . GLN C 2 40  ? 134.124 84.329  119.035 1.00 37.33 ?  19  GLN C CA    1 
ATOM   11137 C  C     . GLN C 2 40  ? 132.939 84.948  118.312 1.00 36.63 ?  19  GLN C C     1 
ATOM   11138 O  O     . GLN C 2 40  ? 132.700 86.149  118.428 1.00 36.10 ?  19  GLN C O     1 
ATOM   11139 C  CB    . GLN C 2 40  ? 135.320 84.229  118.088 1.00 38.24 ?  19  GLN C CB    1 
ATOM   11140 C  CG    . GLN C 2 40  ? 136.647 84.319  118.807 1.00 41.33 ?  19  GLN C CG    1 
ATOM   11141 C  CD    . GLN C 2 40  ? 137.710 85.049  118.011 1.00 45.15 ?  19  GLN C CD    1 
ATOM   11142 O  OE1   . GLN C 2 40  ? 137.749 84.974  116.776 1.00 47.33 ?  19  GLN C OE1   1 
ATOM   11143 N  NE2   . GLN C 2 40  ? 138.586 85.763  118.716 1.00 46.51 ?  19  GLN C NE2   1 
ATOM   11144 N  N     . MET C 2 41  ? 132.192 84.124  117.582 1.00 36.23 ?  20  MET C N     1 
ATOM   11145 C  CA    . MET C 2 41  ? 131.013 84.617  116.884 1.00 36.40 ?  20  MET C CA    1 
ATOM   11146 C  C     . MET C 2 41  ? 129.878 84.983  117.859 1.00 34.93 ?  20  MET C C     1 
ATOM   11147 O  O     . MET C 2 41  ? 129.150 85.944  117.619 1.00 34.20 ?  20  MET C O     1 
ATOM   11148 C  CB    . MET C 2 41  ? 130.586 83.678  115.735 1.00 37.35 ?  20  MET C CB    1 
ATOM   11149 C  CG    . MET C 2 41  ? 129.657 82.526  116.072 1.00 40.49 ?  20  MET C CG    1 
ATOM   11150 S  SD    . MET C 2 41  ? 129.103 81.687  114.554 1.00 48.68 ?  20  MET C SD    1 
ATOM   11151 C  CE    . MET C 2 41  ? 130.432 80.504  114.293 1.00 47.17 ?  20  MET C CE    1 
ATOM   11152 N  N     . PHE C 2 42  ? 129.764 84.255  118.973 1.00 33.75 ?  21  PHE C N     1 
ATOM   11153 C  CA    . PHE C 2 42  ? 128.819 84.642  120.031 1.00 32.62 ?  21  PHE C CA    1 
ATOM   11154 C  C     . PHE C 2 42  ? 129.248 85.918  120.746 1.00 32.59 ?  21  PHE C C     1 
ATOM   11155 O  O     . PHE C 2 42  ? 128.411 86.766  121.068 1.00 32.23 ?  21  PHE C O     1 
ATOM   11156 C  CB    . PHE C 2 42  ? 128.583 83.504  121.023 1.00 32.12 ?  21  PHE C CB    1 
ATOM   11157 C  CG    . PHE C 2 42  ? 127.579 82.495  120.548 1.00 31.04 ?  21  PHE C CG    1 
ATOM   11158 C  CD1   . PHE C 2 42  ? 126.237 82.605  120.909 1.00 30.75 ?  21  PHE C CD1   1 
ATOM   11159 C  CD2   . PHE C 2 42  ? 127.970 81.439  119.732 1.00 30.99 ?  21  PHE C CD2   1 
ATOM   11160 C  CE1   . PHE C 2 42  ? 125.296 81.669  120.464 1.00 30.30 ?  21  PHE C CE1   1 
ATOM   11161 C  CE2   . PHE C 2 42  ? 127.036 80.494  119.276 1.00 30.74 ?  21  PHE C CE2   1 
ATOM   11162 C  CZ    . PHE C 2 42  ? 125.699 80.610  119.644 1.00 30.48 ?  21  PHE C CZ    1 
ATOM   11163 N  N     . TYR C 2 43  ? 130.552 86.055  120.982 1.00 32.33 ?  22  TYR C N     1 
ATOM   11164 C  CA    . TYR C 2 43  ? 131.096 87.286  121.550 1.00 32.50 ?  22  TYR C CA    1 
ATOM   11165 C  C     . TYR C 2 43  ? 130.708 88.486  120.689 1.00 33.01 ?  22  TYR C C     1 
ATOM   11166 O  O     . TYR C 2 43  ? 130.175 89.475  121.198 1.00 32.50 ?  22  TYR C O     1 
ATOM   11167 C  CB    . TYR C 2 43  ? 132.624 87.211  121.733 1.00 32.53 ?  22  TYR C CB    1 
ATOM   11168 C  CG    . TYR C 2 43  ? 133.227 88.559  122.087 1.00 33.27 ?  22  TYR C CG    1 
ATOM   11169 C  CD1   . TYR C 2 43  ? 133.196 89.038  123.400 1.00 32.34 ?  22  TYR C CD1   1 
ATOM   11170 C  CD2   . TYR C 2 43  ? 133.791 89.371  121.101 1.00 33.71 ?  22  TYR C CD2   1 
ATOM   11171 C  CE1   . TYR C 2 43  ? 133.729 90.286  123.724 1.00 33.58 ?  22  TYR C CE1   1 
ATOM   11172 C  CE2   . TYR C 2 43  ? 134.322 90.625  121.410 1.00 35.12 ?  22  TYR C CE2   1 
ATOM   11173 C  CZ    . TYR C 2 43  ? 134.292 91.073  122.724 1.00 35.30 ?  22  TYR C CZ    1 
ATOM   11174 O  OH    . TYR C 2 43  ? 134.818 92.309  123.029 1.00 36.54 ?  22  TYR C OH    1 
ATOM   11175 N  N     . ASN C 2 44  ? 130.966 88.382  119.382 1.00 33.80 ?  23  ASN C N     1 
ATOM   11176 C  CA    . ASN C 2 44  ? 130.668 89.458  118.447 1.00 34.80 ?  23  ASN C CA    1 
ATOM   11177 C  C     . ASN C 2 44  ? 129.172 89.757  118.373 1.00 34.40 ?  23  ASN C C     1 
ATOM   11178 O  O     . ASN C 2 44  ? 128.773 90.917  118.359 1.00 33.99 ?  23  ASN C O     1 
ATOM   11179 C  CB    . ASN C 2 44  ? 131.235 89.152  117.051 1.00 35.46 ?  23  ASN C CB    1 
ATOM   11180 C  CG    . ASN C 2 44  ? 132.767 89.047  117.034 1.00 38.28 ?  23  ASN C CG    1 
ATOM   11181 O  OD1   . ASN C 2 44  ? 133.466 89.598  117.898 1.00 41.01 ?  23  ASN C OD1   1 
ATOM   11182 N  ND2   . ASN C 2 44  ? 133.292 88.341  116.035 1.00 39.13 ?  23  ASN C ND2   1 
ATOM   11183 N  N     . GLN C 2 45  ? 128.351 88.707  118.344 1.00 34.49 ?  24  GLN C N     1 
ATOM   11184 C  CA    . GLN C 2 45  ? 126.902 88.867  118.300 1.00 34.81 ?  24  GLN C CA    1 
ATOM   11185 C  C     . GLN C 2 45  ? 126.366 89.526  119.578 1.00 34.68 ?  24  GLN C C     1 
ATOM   11186 O  O     . GLN C 2 45  ? 125.545 90.443  119.510 1.00 34.59 ?  24  GLN C O     1 
ATOM   11187 C  CB    . GLN C 2 45  ? 126.212 87.525  118.035 1.00 34.83 ?  24  GLN C CB    1 
ATOM   11188 C  CG    . GLN C 2 45  ? 124.749 87.634  117.597 1.00 36.14 ?  24  GLN C CG    1 
ATOM   11189 C  CD    . GLN C 2 45  ? 124.559 88.402  116.286 1.00 38.04 ?  24  GLN C CD    1 
ATOM   11190 O  OE1   . GLN C 2 45  ? 125.435 88.417  115.417 1.00 38.57 ?  24  GLN C OE1   1 
ATOM   11191 N  NE2   . GLN C 2 45  ? 123.402 89.049  116.146 1.00 38.67 ?  24  GLN C NE2   1 
ATOM   11192 N  N     . ASN C 2 46  ? 126.842 89.075  120.736 1.00 34.71 ?  25  ASN C N     1 
ATOM   11193 C  CA    . ASN C 2 46  ? 126.402 89.655  122.005 1.00 34.99 ?  25  ASN C CA    1 
ATOM   11194 C  C     . ASN C 2 46  ? 126.740 91.140  122.126 1.00 35.69 ?  25  ASN C C     1 
ATOM   11195 O  O     . ASN C 2 46  ? 125.878 91.956  122.470 1.00 35.41 ?  25  ASN C O     1 
ATOM   11196 C  CB    . ASN C 2 46  ? 126.939 88.861  123.202 1.00 34.64 ?  25  ASN C CB    1 
ATOM   11197 C  CG    . ASN C 2 46  ? 126.107 87.631  123.498 1.00 34.71 ?  25  ASN C CG    1 
ATOM   11198 O  OD1   . ASN C 2 46  ? 125.188 87.685  124.310 1.00 35.68 ?  25  ASN C OD1   1 
ATOM   11199 N  ND2   . ASN C 2 46  ? 126.400 86.522  122.811 1.00 34.71 ?  25  ASN C ND2   1 
ATOM   11200 N  N     . VAL C 2 47  ? 127.983 91.500  121.819 1.00 36.69 ?  26  VAL C N     1 
ATOM   11201 C  CA    . VAL C 2 47  ? 128.397 92.899  121.949 1.00 38.00 ?  26  VAL C CA    1 
ATOM   11202 C  C     . VAL C 2 47  ? 127.742 93.815  120.906 1.00 38.90 ?  26  VAL C C     1 
ATOM   11203 O  O     . VAL C 2 47  ? 127.499 94.985  121.186 1.00 39.46 ?  26  VAL C O     1 
ATOM   11204 C  CB    . VAL C 2 47  ? 129.937 93.083  121.986 1.00 38.16 ?  26  VAL C CB    1 
ATOM   11205 C  CG1   . VAL C 2 47  ? 130.530 92.293  123.136 1.00 37.75 ?  26  VAL C CG1   1 
ATOM   11206 C  CG2   . VAL C 2 47  ? 130.583 92.697  120.657 1.00 38.81 ?  26  VAL C CG2   1 
ATOM   11207 N  N     . LYS C 2 48  ? 127.427 93.277  119.727 1.00 39.67 ?  27  LYS C N     1 
ATOM   11208 C  CA    . LYS C 2 48  ? 126.754 94.068  118.694 1.00 40.50 ?  27  LYS C CA    1 
ATOM   11209 C  C     . LYS C 2 48  ? 125.257 94.230  118.985 1.00 40.02 ?  27  LYS C C     1 
ATOM   11210 O  O     . LYS C 2 48  ? 124.586 95.077  118.391 1.00 40.55 ?  27  LYS C O     1 
ATOM   11211 C  CB    . LYS C 2 48  ? 126.990 93.480  117.290 1.00 41.23 ?  27  LYS C CB    1 
ATOM   11212 C  CG    . LYS C 2 48  ? 126.043 92.346  116.897 1.00 42.50 ?  27  LYS C CG    1 
ATOM   11213 C  CD    . LYS C 2 48  ? 126.282 91.847  115.465 1.00 44.92 ?  27  LYS C CD    1 
ATOM   11214 C  CE    . LYS C 2 48  ? 125.633 92.753  114.420 1.00 46.66 ?  27  LYS C CE    1 
ATOM   11215 N  NZ    . LYS C 2 48  ? 124.153 92.837  114.590 1.00 47.26 1  27  LYS C NZ    1 
ATOM   11216 N  N     . GLN C 2 49  ? 124.734 93.411  119.890 1.00 39.10 ?  28  GLN C N     1 
ATOM   11217 C  CA    . GLN C 2 49  ? 123.343 93.513  120.277 1.00 38.22 ?  28  GLN C CA    1 
ATOM   11218 C  C     . GLN C 2 49  ? 123.154 94.437  121.480 1.00 37.23 ?  28  GLN C C     1 
ATOM   11219 O  O     . GLN C 2 49  ? 122.023 94.636  121.916 1.00 37.40 ?  28  GLN C O     1 
ATOM   11220 C  CB    . GLN C 2 49  ? 122.736 92.124  120.542 1.00 38.69 ?  28  GLN C CB    1 
ATOM   11221 C  CG    . GLN C 2 49  ? 122.468 91.306  119.269 1.00 39.57 ?  28  GLN C CG    1 
ATOM   11222 C  CD    . GLN C 2 49  ? 121.691 90.016  119.516 1.00 41.20 ?  28  GLN C CD    1 
ATOM   11223 O  OE1   . GLN C 2 49  ? 121.479 89.231  118.591 1.00 42.94 ?  28  GLN C OE1   1 
ATOM   11224 N  NE2   . GLN C 2 49  ? 121.264 89.791  120.762 1.00 41.23 ?  28  GLN C NE2   1 
ATOM   11225 N  N     . PHE C 2 50  ? 124.246 95.012  121.996 1.00 35.83 ?  29  PHE C N     1 
ATOM   11226 C  CA    . PHE C 2 50  ? 124.169 95.848  123.202 1.00 34.51 ?  29  PHE C CA    1 
ATOM   11227 C  C     . PHE C 2 50  ? 123.152 96.987  123.082 1.00 33.81 ?  29  PHE C C     1 
ATOM   11228 O  O     . PHE C 2 50  ? 123.114 97.686  122.069 1.00 33.66 ?  29  PHE C O     1 
ATOM   11229 C  CB    . PHE C 2 50  ? 125.535 96.403  123.617 1.00 34.59 ?  29  PHE C CB    1 
ATOM   11230 C  CG    . PHE C 2 50  ? 125.489 97.243  124.881 1.00 34.59 ?  29  PHE C CG    1 
ATOM   11231 C  CD1   . PHE C 2 50  ? 125.299 96.645  126.132 1.00 34.34 ?  29  PHE C CD1   1 
ATOM   11232 C  CD2   . PHE C 2 50  ? 125.615 98.630  124.818 1.00 35.49 ?  29  PHE C CD2   1 
ATOM   11233 C  CE1   . PHE C 2 50  ? 125.248 97.416  127.303 1.00 33.88 ?  29  PHE C CE1   1 
ATOM   11234 C  CE2   . PHE C 2 50  ? 125.563 99.417  125.984 1.00 34.12 ?  29  PHE C CE2   1 
ATOM   11235 C  CZ    . PHE C 2 50  ? 125.380 98.810  127.225 1.00 33.87 ?  29  PHE C CZ    1 
ATOM   11236 N  N     . TRP C 2 51  ? 122.343 97.160  124.130 1.00 32.24 ?  30  TRP C N     1 
ATOM   11237 C  CA    . TRP C 2 51  ? 121.304 98.187  124.165 1.00 31.28 ?  30  TRP C CA    1 
ATOM   11238 C  C     . TRP C 2 51  ? 120.987 98.623  125.597 1.00 31.12 ?  30  TRP C C     1 
ATOM   11239 O  O     . TRP C 2 51  ? 121.366 97.940  126.556 1.00 30.71 ?  30  TRP C O     1 
ATOM   11240 C  CB    . TRP C 2 51  ? 120.034 97.691  123.459 1.00 30.85 ?  30  TRP C CB    1 
ATOM   11241 C  CG    . TRP C 2 51  ? 119.401 96.482  124.102 1.00 29.31 ?  30  TRP C CG    1 
ATOM   11242 C  CD1   . TRP C 2 51  ? 119.759 95.173  123.928 1.00 29.07 ?  30  TRP C CD1   1 
ATOM   11243 C  CD2   . TRP C 2 51  ? 118.316 96.478  125.036 1.00 28.33 ?  30  TRP C CD2   1 
ATOM   11244 N  NE1   . TRP C 2 51  ? 118.959 94.356  124.688 1.00 28.01 ?  30  TRP C NE1   1 
ATOM   11245 C  CE2   . TRP C 2 51  ? 118.064 95.129  125.378 1.00 27.67 ?  30  TRP C CE2   1 
ATOM   11246 C  CE3   . TRP C 2 51  ? 117.534 97.483  125.622 1.00 27.27 ?  30  TRP C CE3   1 
ATOM   11247 C  CZ2   . TRP C 2 51  ? 117.064 94.760  126.276 1.00 26.54 ?  30  TRP C CZ2   1 
ATOM   11248 C  CZ3   . TRP C 2 51  ? 116.532 97.115  126.509 1.00 27.07 ?  30  TRP C CZ3   1 
ATOM   11249 C  CH2   . TRP C 2 51  ? 116.311 95.763  126.833 1.00 26.52 ?  30  TRP C CH2   1 
ATOM   11250 N  N     . LEU C 2 52  ? 120.297 99.760  125.728 1.00 30.65 ?  31  LEU C N     1 
ATOM   11251 C  CA    . LEU C 2 52  ? 119.787 100.255 127.009 1.00 30.38 ?  31  LEU C CA    1 
ATOM   11252 C  C     . LEU C 2 52  ? 118.321 100.651 126.858 1.00 30.51 ?  31  LEU C C     1 
ATOM   11253 O  O     . LEU C 2 52  ? 117.946 101.199 125.820 1.00 30.77 ?  31  LEU C O     1 
ATOM   11254 C  CB    . LEU C 2 52  ? 120.605 101.464 127.494 1.00 30.45 ?  31  LEU C CB    1 
ATOM   11255 C  CG    . LEU C 2 52  ? 122.073 101.184 127.831 1.00 30.29 ?  31  LEU C CG    1 
ATOM   11256 C  CD1   . LEU C 2 52  ? 122.921 102.463 127.845 1.00 30.69 ?  31  LEU C CD1   1 
ATOM   11257 C  CD2   . LEU C 2 52  ? 122.198 100.408 129.152 1.00 29.91 ?  31  LEU C CD2   1 
ATOM   11258 N  N     . PRO C 2 53  ? 117.486 100.387 127.888 1.00 30.73 ?  32  PRO C N     1 
ATOM   11259 C  CA    . PRO C 2 53  ? 116.051 100.707 127.793 1.00 31.17 ?  32  PRO C CA    1 
ATOM   11260 C  C     . PRO C 2 53  ? 115.772 102.179 127.498 1.00 32.18 ?  32  PRO C C     1 
ATOM   11261 O  O     . PRO C 2 53  ? 114.767 102.492 126.838 1.00 32.66 ?  32  PRO C O     1 
ATOM   11262 C  CB    . PRO C 2 53  ? 115.506 100.333 129.176 1.00 30.99 ?  32  PRO C CB    1 
ATOM   11263 C  CG    . PRO C 2 53  ? 116.718 100.215 130.069 1.00 30.50 ?  32  PRO C CG    1 
ATOM   11264 C  CD    . PRO C 2 53  ? 117.814 99.744  129.176 1.00 30.46 ?  32  PRO C CD    1 
ATOM   11265 N  N     . GLU C 2 54  ? 116.657 103.064 127.964 1.00 32.62 ?  33  GLU C N     1 
ATOM   11266 C  CA    . GLU C 2 54  ? 116.519 104.513 127.743 1.00 33.44 ?  33  GLU C CA    1 
ATOM   11267 C  C     . GLU C 2 54  ? 116.556 104.917 126.264 1.00 33.59 ?  33  GLU C C     1 
ATOM   11268 O  O     . GLU C 2 54  ? 116.163 106.030 125.922 1.00 34.05 ?  33  GLU C O     1 
ATOM   11269 C  CB    . GLU C 2 54  ? 117.581 105.306 128.526 1.00 33.72 ?  33  GLU C CB    1 
ATOM   11270 C  CG    . GLU C 2 54  ? 117.367 105.349 130.052 1.00 34.53 ?  33  GLU C CG    1 
ATOM   11271 C  CD    . GLU C 2 54  ? 117.723 104.034 130.747 1.00 35.09 ?  33  GLU C CD    1 
ATOM   11272 O  OE1   . GLU C 2 54  ? 118.517 103.240 130.180 1.00 34.38 ?  33  GLU C OE1   1 
ATOM   11273 O  OE2   . GLU C 2 54  ? 117.205 103.796 131.862 1.00 35.53 -1 33  GLU C OE2   1 
ATOM   11274 N  N     . GLU C 2 55  ? 117.028 104.018 125.398 1.00 33.82 ?  34  GLU C N     1 
ATOM   11275 C  CA    . GLU C 2 55  ? 117.020 104.246 123.950 1.00 34.19 ?  34  GLU C CA    1 
ATOM   11276 C  C     . GLU C 2 55  ? 115.589 104.278 123.391 1.00 33.83 ?  34  GLU C C     1 
ATOM   11277 O  O     . GLU C 2 55  ? 115.353 104.824 122.314 1.00 33.93 ?  34  GLU C O     1 
ATOM   11278 C  CB    . GLU C 2 55  ? 117.824 103.165 123.207 1.00 34.52 ?  34  GLU C CB    1 
ATOM   11279 C  CG    . GLU C 2 55  ? 119.314 103.095 123.534 1.00 36.50 ?  34  GLU C CG    1 
ATOM   11280 C  CD    . GLU C 2 55  ? 120.079 102.198 122.565 1.00 40.03 ?  34  GLU C CD    1 
ATOM   11281 O  OE1   . GLU C 2 55  ? 120.479 102.679 121.482 1.00 42.43 ?  34  GLU C OE1   1 
ATOM   11282 O  OE2   . GLU C 2 55  ? 120.289 101.012 122.885 1.00 39.35 -1 34  GLU C OE2   1 
ATOM   11283 N  N     . ILE C 2 56  ? 114.659 103.663 124.122 1.00 33.31 ?  35  ILE C N     1 
ATOM   11284 C  CA    . ILE C 2 56  ? 113.254 103.546 123.727 1.00 33.14 ?  35  ILE C CA    1 
ATOM   11285 C  C     . ILE C 2 56  ? 112.408 104.470 124.609 1.00 32.58 ?  35  ILE C C     1 
ATOM   11286 O  O     . ILE C 2 56  ? 112.357 104.288 125.820 1.00 32.12 ?  35  ILE C O     1 
ATOM   11287 C  CB    . ILE C 2 56  ? 112.741 102.074 123.896 1.00 33.03 ?  35  ILE C CB    1 
ATOM   11288 C  CG1   . ILE C 2 56  ? 113.671 101.053 123.205 1.00 34.76 ?  35  ILE C CG1   1 
ATOM   11289 C  CG2   . ILE C 2 56  ? 111.286 101.925 123.435 1.00 33.61 ?  35  ILE C CG2   1 
ATOM   11290 C  CD1   . ILE C 2 56  ? 113.707 101.114 121.676 1.00 36.75 ?  35  ILE C CD1   1 
ATOM   11291 N  N     . ALA C 2 57  ? 111.758 105.463 124.006 1.00 32.36 ?  36  ALA C N     1 
ATOM   11292 C  CA    . ALA C 2 57  ? 110.851 106.344 124.747 1.00 32.17 ?  36  ALA C CA    1 
ATOM   11293 C  C     . ALA C 2 57  ? 109.514 105.634 124.987 1.00 31.76 ?  36  ALA C C     1 
ATOM   11294 O  O     . ALA C 2 57  ? 108.934 105.062 124.063 1.00 31.95 ?  36  ALA C O     1 
ATOM   11295 C  CB    . ALA C 2 57  ? 110.640 107.647 123.991 1.00 33.01 ?  36  ALA C CB    1 
ATOM   11296 N  N     . LEU C 2 58  ? 109.027 105.673 126.224 1.00 30.68 ?  37  LEU C N     1 
ATOM   11297 C  CA    . LEU C 2 58  ? 107.898 104.829 126.613 1.00 30.14 ?  37  LEU C CA    1 
ATOM   11298 C  C     . LEU C 2 58  ? 106.564 105.555 126.749 1.00 30.21 ?  37  LEU C C     1 
ATOM   11299 O  O     . LEU C 2 58  ? 105.513 104.910 126.852 1.00 29.91 ?  37  LEU C O     1 
ATOM   11300 C  CB    . LEU C 2 58  ? 108.226 104.062 127.900 1.00 29.46 ?  37  LEU C CB    1 
ATOM   11301 C  CG    . LEU C 2 58  ? 109.327 103.000 127.777 1.00 29.08 ?  37  LEU C CG    1 
ATOM   11302 C  CD1   . LEU C 2 58  ? 109.690 102.438 129.139 1.00 29.23 ?  37  LEU C CD1   1 
ATOM   11303 C  CD2   . LEU C 2 58  ? 108.914 101.874 126.829 1.00 28.84 ?  37  LEU C CD2   1 
ATOM   11304 N  N     . ASN C 2 59  ? 106.605 106.884 126.725 1.00 30.50 ?  38  ASN C N     1 
ATOM   11305 C  CA    . ASN C 2 59  ? 105.396 107.694 126.899 1.00 31.23 ?  38  ASN C CA    1 
ATOM   11306 C  C     . ASN C 2 59  ? 104.330 107.469 125.814 1.00 31.03 ?  38  ASN C C     1 
ATOM   11307 O  O     . ASN C 2 59  ? 103.157 107.758 126.028 1.00 30.82 ?  38  ASN C O     1 
ATOM   11308 C  CB    . ASN C 2 59  ? 105.741 109.186 127.070 1.00 31.98 ?  38  ASN C CB    1 
ATOM   11309 C  CG    . ASN C 2 59  ? 106.521 109.757 125.897 1.00 33.59 ?  38  ASN C CG    1 
ATOM   11310 O  OD1   . ASN C 2 59  ? 107.582 109.239 125.524 1.00 36.48 ?  38  ASN C OD1   1 
ATOM   11311 N  ND2   . ASN C 2 59  ? 106.008 110.838 125.315 1.00 34.77 ?  38  ASN C ND2   1 
ATOM   11312 N  N     . GLY C 2 60  ? 104.745 106.921 124.674 1.00 30.88 ?  39  GLY C N     1 
ATOM   11313 C  CA    . GLY C 2 60  ? 103.824 106.525 123.602 1.00 31.37 ?  39  GLY C CA    1 
ATOM   11314 C  C     . GLY C 2 60  ? 102.859 105.396 123.947 1.00 31.05 ?  39  GLY C C     1 
ATOM   11315 O  O     . GLY C 2 60  ? 101.784 105.322 123.368 1.00 31.21 ?  39  GLY C O     1 
ATOM   11316 N  N     . ASP C 2 61  ? 103.233 104.526 124.889 1.00 30.63 ?  40  ASP C N     1 
ATOM   11317 C  CA    . ASP C 2 61  ? 102.331 103.471 125.389 1.00 30.65 ?  40  ASP C CA    1 
ATOM   11318 C  C     . ASP C 2 61  ? 101.268 103.947 126.384 1.00 31.00 ?  40  ASP C C     1 
ATOM   11319 O  O     . ASP C 2 61  ? 100.380 103.172 126.741 1.00 30.91 ?  40  ASP C O     1 
ATOM   11320 C  CB    . ASP C 2 61  ? 103.121 102.343 126.064 1.00 30.00 ?  40  ASP C CB    1 
ATOM   11321 C  CG    . ASP C 2 61  ? 103.980 101.561 125.100 1.00 30.88 ?  40  ASP C CG    1 
ATOM   11322 O  OD1   . ASP C 2 61  ? 104.003 101.882 123.888 1.00 30.42 ?  40  ASP C OD1   1 
ATOM   11323 O  OD2   . ASP C 2 61  ? 104.647 100.615 125.572 1.00 31.17 -1 40  ASP C OD2   1 
ATOM   11324 N  N     . LEU C 2 62  ? 101.366 105.194 126.843 1.00 31.54 ?  41  LEU C N     1 
ATOM   11325 C  CA    . LEU C 2 62  ? 100.502 105.694 127.925 1.00 32.47 ?  41  LEU C CA    1 
ATOM   11326 C  C     . LEU C 2 62  ? 99.010  105.522 127.665 1.00 33.21 ?  41  LEU C C     1 
ATOM   11327 O  O     . LEU C 2 62  ? 98.257  105.142 128.569 1.00 32.84 ?  41  LEU C O     1 
ATOM   11328 C  CB    . LEU C 2 62  ? 100.804 107.160 128.248 1.00 33.14 ?  41  LEU C CB    1 
ATOM   11329 C  CG    . LEU C 2 62  ? 101.951 107.448 129.217 1.00 34.44 ?  41  LEU C CG    1 
ATOM   11330 C  CD1   . LEU C 2 62  ? 102.302 108.928 129.179 1.00 35.04 ?  41  LEU C CD1   1 
ATOM   11331 C  CD2   . LEU C 2 62  ? 101.586 107.004 130.639 1.00 35.52 ?  41  LEU C CD2   1 
ATOM   11332 N  N     . LEU C 2 63  ? 98.590  105.795 126.432 1.00 33.75 ?  42  LEU C N     1 
ATOM   11333 C  CA    . LEU C 2 63  ? 97.180  105.693 126.080 1.00 34.79 ?  42  LEU C CA    1 
ATOM   11334 C  C     . LEU C 2 63  ? 96.665  104.268 125.885 1.00 34.66 ?  42  LEU C C     1 
ATOM   11335 O  O     . LEU C 2 63  ? 95.604  103.941 126.413 1.00 34.67 ?  42  LEU C O     1 
ATOM   11336 C  CB    . LEU C 2 63  ? 96.834  106.578 124.880 1.00 35.27 ?  42  LEU C CB    1 
ATOM   11337 C  CG    . LEU C 2 63  ? 96.584  108.045 125.251 1.00 36.82 ?  42  LEU C CG    1 
ATOM   11338 C  CD1   . LEU C 2 63  ? 96.290  108.851 123.991 1.00 37.93 ?  42  LEU C CD1   1 
ATOM   11339 C  CD2   . LEU C 2 63  ? 95.439  108.199 126.251 1.00 37.85 ?  42  LEU C CD2   1 
ATOM   11340 N  N     . THR C 2 64  ? 97.388  103.425 125.142 1.00 34.70 ?  43  THR C N     1 
ATOM   11341 C  CA    . THR C 2 64  ? 96.952  102.026 124.993 1.00 35.10 ?  43  THR C CA    1 
ATOM   11342 C  C     . THR C 2 64  ? 96.950  101.279 126.336 1.00 34.78 ?  43  THR C C     1 
ATOM   11343 O  O     . THR C 2 64  ? 96.187  100.337 126.514 1.00 35.04 ?  43  THR C O     1 
ATOM   11344 C  CB    . THR C 2 64  ? 97.715  101.225 123.892 1.00 35.30 ?  43  THR C CB    1 
ATOM   11345 O  OG1   . THR C 2 64  ? 99.131  101.260 124.128 1.00 36.01 ?  43  THR C OG1   1 
ATOM   11346 C  CG2   . THR C 2 64  ? 97.406  101.776 122.500 1.00 35.96 ?  43  THR C CG2   1 
ATOM   11347 N  N     . TRP C 2 65  ? 97.779  101.725 127.283 1.00 34.63 ?  44  TRP C N     1 
ATOM   11348 C  CA    . TRP C 2 65  ? 97.791  101.162 128.640 1.00 34.37 ?  44  TRP C CA    1 
ATOM   11349 C  C     . TRP C 2 65  ? 96.551  101.586 129.426 1.00 35.13 ?  44  TRP C C     1 
ATOM   11350 O  O     . TRP C 2 65  ? 95.860  100.752 130.027 1.00 34.98 ?  44  TRP C O     1 
ATOM   11351 C  CB    . TRP C 2 65  ? 99.052  101.592 129.388 1.00 33.95 ?  44  TRP C CB    1 
ATOM   11352 C  CG    . TRP C 2 65  ? 99.045  101.241 130.841 1.00 33.26 ?  44  TRP C CG    1 
ATOM   11353 C  CD1   . TRP C 2 65  ? 98.816  102.086 131.891 1.00 32.51 ?  44  TRP C CD1   1 
ATOM   11354 C  CD2   . TRP C 2 65  ? 99.283  99.946  131.411 1.00 30.93 ?  44  TRP C CD2   1 
ATOM   11355 N  NE1   . TRP C 2 65  ? 98.903  101.398 133.082 1.00 31.66 ?  44  TRP C NE1   1 
ATOM   11356 C  CE2   . TRP C 2 65  ? 99.188  100.083 132.816 1.00 30.39 ?  44  TRP C CE2   1 
ATOM   11357 C  CE3   . TRP C 2 65  ? 99.574  98.686  130.870 1.00 30.36 ?  44  TRP C CE3   1 
ATOM   11358 C  CZ2   . TRP C 2 65  ? 99.362  99.005  133.687 1.00 29.16 ?  44  TRP C CZ2   1 
ATOM   11359 C  CZ3   . TRP C 2 65  ? 99.752  97.608  131.740 1.00 28.84 ?  44  TRP C CZ3   1 
ATOM   11360 C  CH2   . TRP C 2 65  ? 99.651  97.779  133.132 1.00 29.34 ?  44  TRP C CH2   1 
ATOM   11361 N  N     . LYS C 2 66  ? 96.294  102.892 129.428 1.00 35.69 ?  45  LYS C N     1 
ATOM   11362 C  CA    . LYS C 2 66  ? 95.113  103.469 130.053 1.00 36.38 ?  45  LYS C CA    1 
ATOM   11363 C  C     . LYS C 2 66  ? 93.824  102.760 129.623 1.00 36.24 ?  45  LYS C C     1 
ATOM   11364 O  O     . LYS C 2 66  ? 92.905  102.629 130.422 1.00 36.78 ?  45  LYS C O     1 
ATOM   11365 C  CB    . LYS C 2 66  ? 95.039  104.955 129.697 1.00 37.14 ?  45  LYS C CB    1 
ATOM   11366 C  CG    . LYS C 2 66  ? 93.881  105.720 130.315 1.00 38.91 ?  45  LYS C CG    1 
ATOM   11367 C  CD    . LYS C 2 66  ? 93.769  107.111 129.691 1.00 41.12 ?  45  LYS C CD    1 
ATOM   11368 C  CE    . LYS C 2 66  ? 92.862  108.012 130.514 1.00 43.00 ?  45  LYS C CE    1 
ATOM   11369 N  NZ    . LYS C 2 66  ? 93.230  107.981 131.963 1.00 44.38 1  45  LYS C NZ    1 
ATOM   11370 N  N     . TYR C 2 67  ? 93.796  102.278 128.376 1.00 36.03 ?  46  TYR C N     1 
ATOM   11371 C  CA    . TYR C 2 67  ? 92.604  101.694 127.739 1.00 36.03 ?  46  TYR C CA    1 
ATOM   11372 C  C     . TYR C 2 67  ? 92.356  100.211 128.044 1.00 35.25 ?  46  TYR C C     1 
ATOM   11373 O  O     . TYR C 2 67  ? 91.287  99.678  127.731 1.00 35.32 ?  46  TYR C O     1 
ATOM   11374 C  CB    . TYR C 2 67  ? 92.676  101.864 126.210 1.00 36.60 ?  46  TYR C CB    1 
ATOM   11375 C  CG    . TYR C 2 67  ? 92.699  103.302 125.707 1.00 37.85 ?  46  TYR C CG    1 
ATOM   11376 C  CD1   . TYR C 2 67  ? 92.357  104.365 126.542 1.00 38.97 ?  46  TYR C CD1   1 
ATOM   11377 C  CD2   . TYR C 2 67  ? 93.050  103.592 124.380 1.00 40.06 ?  46  TYR C CD2   1 
ATOM   11378 C  CE1   . TYR C 2 67  ? 92.385  105.683 126.090 1.00 40.36 ?  46  TYR C CE1   1 
ATOM   11379 C  CE2   . TYR C 2 67  ? 93.076  104.915 123.911 1.00 40.53 ?  46  TYR C CE2   1 
ATOM   11380 C  CZ    . TYR C 2 67  ? 92.738  105.954 124.778 1.00 41.43 ?  46  TYR C CZ    1 
ATOM   11381 O  OH    . TYR C 2 67  ? 92.744  107.268 124.346 1.00 41.48 ?  46  TYR C OH    1 
ATOM   11382 N  N     . LEU C 2 68  ? 93.346  99.543  128.629 1.00 33.80 ?  47  LEU C N     1 
ATOM   11383 C  CA    . LEU C 2 68  ? 93.201  98.136  128.985 1.00 32.77 ?  47  LEU C CA    1 
ATOM   11384 C  C     . LEU C 2 68  ? 92.311  97.991  130.212 1.00 31.84 ?  47  LEU C C     1 
ATOM   11385 O  O     . LEU C 2 68  ? 92.283  98.870  131.070 1.00 31.90 ?  47  LEU C O     1 
ATOM   11386 C  CB    . LEU C 2 68  ? 94.566  97.504  129.271 1.00 32.39 ?  47  LEU C CB    1 
ATOM   11387 C  CG    . LEU C 2 68  ? 95.629  97.371  128.179 1.00 32.68 ?  47  LEU C CG    1 
ATOM   11388 C  CD1   . LEU C 2 68  ? 96.876  96.719  128.768 1.00 33.03 ?  47  LEU C CD1   1 
ATOM   11389 C  CD2   . LEU C 2 68  ? 95.130  96.580  126.966 1.00 32.78 ?  47  LEU C CD2   1 
ATOM   11390 N  N     . GLY C 2 69  ? 91.601  96.872  130.301 1.00 30.99 ?  48  GLY C N     1 
ATOM   11391 C  CA    . GLY C 2 69  ? 90.829  96.553  131.501 1.00 30.58 ?  48  GLY C CA    1 
ATOM   11392 C  C     . GLY C 2 69  ? 91.714  96.338  132.722 1.00 29.87 ?  48  GLY C C     1 
ATOM   11393 O  O     . GLY C 2 69  ? 92.914  96.101  132.594 1.00 28.79 ?  48  GLY C O     1 
ATOM   11394 N  N     . LYS C 2 70  ? 91.124  96.433  133.908 1.00 29.89 ?  49  LYS C N     1 
ATOM   11395 C  CA    . LYS C 2 70  ? 91.868  96.220  135.149 1.00 29.49 ?  49  LYS C CA    1 
ATOM   11396 C  C     . LYS C 2 70  ? 92.504  94.818  135.210 1.00 28.74 ?  49  LYS C C     1 
ATOM   11397 O  O     . LYS C 2 70  ? 93.646  94.674  135.665 1.00 27.27 ?  49  LYS C O     1 
ATOM   11398 C  CB    . LYS C 2 70  ? 90.989  96.505  136.370 1.00 30.67 ?  49  LYS C CB    1 
ATOM   11399 C  CG    . LYS C 2 70  ? 90.846  98.017  136.672 1.00 33.73 ?  49  LYS C CG    1 
ATOM   11400 C  CD    . LYS C 2 70  ? 89.667  98.339  137.607 1.00 38.93 ?  49  LYS C CD    1 
ATOM   11401 C  CE    . LYS C 2 70  ? 89.969  98.054  139.084 1.00 41.04 ?  49  LYS C CE    1 
ATOM   11402 N  NZ    . LYS C 2 70  ? 90.915  99.033  139.698 1.00 42.21 1  49  LYS C NZ    1 
ATOM   11403 N  N     . ASN C 2 71  ? 91.766  93.810  134.733 1.00 27.54 ?  50  ASN C N     1 
ATOM   11404 C  CA    . ASN C 2 71  ? 92.276  92.440  134.634 1.00 27.00 ?  50  ASN C CA    1 
ATOM   11405 C  C     . ASN C 2 71  ? 93.518  92.338  133.748 1.00 26.19 ?  50  ASN C C     1 
ATOM   11406 O  O     . ASN C 2 71  ? 94.492  91.636  134.092 1.00 25.38 ?  50  ASN C O     1 
ATOM   11407 C  CB    . ASN C 2 71  ? 91.182  91.473  134.129 1.00 27.08 ?  50  ASN C CB    1 
ATOM   11408 C  CG    . ASN C 2 71  ? 90.634  91.839  132.729 1.00 28.69 ?  50  ASN C CG    1 
ATOM   11409 O  OD1   . ASN C 2 71  ? 90.356  93.013  132.418 1.00 30.45 ?  50  ASN C OD1   1 
ATOM   11410 N  ND2   . ASN C 2 71  ? 90.449  90.811  131.885 1.00 29.42 ?  50  ASN C ND2   1 
ATOM   11411 N  N     . GLU C 2 72  ? 93.477  93.038  132.616 1.00 24.91 ?  51  GLU C N     1 
ATOM   11412 C  CA    . GLU C 2 72  ? 94.572  93.016  131.655 1.00 24.97 ?  51  GLU C CA    1 
ATOM   11413 C  C     . GLU C 2 72  ? 95.828  93.687  132.221 1.00 24.45 ?  51  GLU C C     1 
ATOM   11414 O  O     . GLU C 2 72  ? 96.942  93.154  132.091 1.00 23.90 ?  51  GLU C O     1 
ATOM   11415 C  CB    . GLU C 2 72  ? 94.146  93.682  130.346 1.00 25.27 ?  51  GLU C CB    1 
ATOM   11416 C  CG    . GLU C 2 72  ? 93.049  92.930  129.595 1.00 26.16 ?  51  GLU C CG    1 
ATOM   11417 C  CD    . GLU C 2 72  ? 92.624  93.660  128.327 1.00 28.70 ?  51  GLU C CD    1 
ATOM   11418 O  OE1   . GLU C 2 72  ? 91.884  94.659  128.436 1.00 28.70 ?  51  GLU C OE1   1 
ATOM   11419 O  OE2   . GLU C 2 72  ? 93.029  93.235  127.222 1.00 28.92 -1 51  GLU C OE2   1 
ATOM   11420 N  N     . GLN C 2 73  ? 95.637  94.837  132.867 1.00 23.75 ?  52  GLN C N     1 
ATOM   11421 C  CA    . GLN C 2 73  ? 96.744  95.563  133.484 1.00 23.94 ?  52  GLN C CA    1 
ATOM   11422 C  C     . GLN C 2 73  ? 97.374  94.749  134.616 1.00 23.36 ?  52  GLN C C     1 
ATOM   11423 O  O     . GLN C 2 73  ? 98.589  94.748  134.774 1.00 22.95 ?  52  GLN C O     1 
ATOM   11424 C  CB    . GLN C 2 73  ? 96.277  96.921  134.029 1.00 24.28 ?  52  GLN C CB    1 
ATOM   11425 C  CG    . GLN C 2 73  ? 95.975  97.992  132.963 1.00 25.22 ?  52  GLN C CG    1 
ATOM   11426 C  CD    . GLN C 2 73  ? 95.607  99.354  133.564 1.00 29.02 ?  52  GLN C CD    1 
ATOM   11427 O  OE1   . GLN C 2 73  ? 95.559  99.515  134.782 1.00 32.08 ?  52  GLN C OE1   1 
ATOM   11428 N  NE2   . GLN C 2 73  ? 95.349  100.333 132.705 1.00 29.13 ?  52  GLN C NE2   1 
ATOM   11429 N  N     . ASP C 2 74  ? 96.531  94.087  135.411 1.00 23.02 ?  53  ASP C N     1 
ATOM   11430 C  CA    . ASP C 2 74  ? 96.990  93.262  136.520 1.00 23.44 ?  53  ASP C CA    1 
ATOM   11431 C  C     . ASP C 2 74  ? 97.874  92.116  136.012 1.00 23.00 ?  53  ASP C C     1 
ATOM   11432 O  O     . ASP C 2 74  ? 98.968  91.904  136.527 1.00 22.96 ?  53  ASP C O     1 
ATOM   11433 C  CB    . ASP C 2 74  ? 95.798  92.697  137.305 1.00 23.31 ?  53  ASP C CB    1 
ATOM   11434 C  CG    . ASP C 2 74  ? 96.219  91.974  138.568 1.00 25.80 ?  53  ASP C CG    1 
ATOM   11435 O  OD1   . ASP C 2 74  ? 96.838  92.613  139.459 1.00 27.95 ?  53  ASP C OD1   1 
ATOM   11436 O  OD2   . ASP C 2 74  ? 95.923  90.768  138.675 1.00 26.30 -1 53  ASP C OD2   1 
ATOM   11437 N  N     . THR C 2 75  ? 97.382  91.382  135.016 1.00 22.20 ?  54  THR C N     1 
ATOM   11438 C  CA    . THR C 2 75  ? 98.129  90.278  134.429 1.00 21.84 ?  54  THR C CA    1 
ATOM   11439 C  C     . THR C 2 75  ? 99.438  90.779  133.829 1.00 22.09 ?  54  THR C C     1 
ATOM   11440 O  O     . THR C 2 75  ? 100.485 90.177  134.040 1.00 21.88 ?  54  THR C O     1 
ATOM   11441 C  CB    . THR C 2 75  ? 97.289  89.502  133.376 1.00 21.74 ?  54  THR C CB    1 
ATOM   11442 O  OG1   . THR C 2 75  ? 96.195  88.867  134.041 1.00 22.09 ?  54  THR C OG1   1 
ATOM   11443 C  CG2   . THR C 2 75  ? 98.124  88.411  132.694 1.00 19.76 ?  54  THR C CG2   1 
ATOM   11444 N  N     . TYR C 2 76  ? 99.374  91.888  133.098 1.00 22.38 ?  55  TYR C N     1 
ATOM   11445 C  CA    . TYR C 2 76  ? 100.570 92.471  132.494 1.00 22.85 ?  55  TYR C CA    1 
ATOM   11446 C  C     . TYR C 2 76  ? 101.653 92.824  133.528 1.00 22.56 ?  55  TYR C C     1 
ATOM   11447 O  O     . TYR C 2 76  ? 102.816 92.481  133.331 1.00 21.97 ?  55  TYR C O     1 
ATOM   11448 C  CB    . TYR C 2 76  ? 100.201 93.697  131.670 1.00 23.57 ?  55  TYR C CB    1 
ATOM   11449 C  CG    . TYR C 2 76  ? 101.263 94.152  130.691 1.00 25.59 ?  55  TYR C CG    1 
ATOM   11450 C  CD1   . TYR C 2 76  ? 101.274 93.683  129.373 1.00 27.49 ?  55  TYR C CD1   1 
ATOM   11451 C  CD2   . TYR C 2 76  ? 102.235 95.077  131.071 1.00 27.70 ?  55  TYR C CD2   1 
ATOM   11452 C  CE1   . TYR C 2 76  ? 102.239 94.122  128.459 1.00 30.28 ?  55  TYR C CE1   1 
ATOM   11453 C  CE2   . TYR C 2 76  ? 103.211 95.519  130.166 1.00 30.38 ?  55  TYR C CE2   1 
ATOM   11454 C  CZ    . TYR C 2 76  ? 103.205 95.035  128.864 1.00 31.39 ?  55  TYR C CZ    1 
ATOM   11455 O  OH    . TYR C 2 76  ? 104.159 95.481  127.968 1.00 32.67 ?  55  TYR C OH    1 
ATOM   11456 N  N     . MET C 2 77  ? 101.271 93.508  134.609 1.00 23.14 ?  56  MET C N     1 
ATOM   11457 C  CA    . MET C 2 77  ? 102.217 93.892  135.674 1.00 23.90 ?  56  MET C CA    1 
ATOM   11458 C  C     . MET C 2 77  ? 102.869 92.661  136.290 1.00 23.24 ?  56  MET C C     1 
ATOM   11459 O  O     . MET C 2 77  ? 104.079 92.634  136.549 1.00 22.47 ?  56  MET C O     1 
ATOM   11460 C  CB    . MET C 2 77  ? 101.509 94.661  136.795 1.00 24.38 ?  56  MET C CB    1 
ATOM   11461 C  CG    . MET C 2 77  ? 100.928 96.015  136.416 1.00 28.52 ?  56  MET C CG    1 
ATOM   11462 S  SD    . MET C 2 77  ? 102.176 97.283  136.242 1.00 34.32 ?  56  MET C SD    1 
ATOM   11463 C  CE    . MET C 2 77  ? 102.786 97.432  137.925 1.00 33.84 ?  56  MET C CE    1 
ATOM   11464 N  N     . LYS C 2 78  ? 102.046 91.644  136.531 1.00 23.25 ?  57  LYS C N     1 
ATOM   11465 C  CA    . LYS C 2 78  ? 102.491 90.460  137.255 1.00 22.98 ?  57  LYS C CA    1 
ATOM   11466 C  C     . LYS C 2 78  ? 103.434 89.642  136.386 1.00 22.77 ?  57  LYS C C     1 
ATOM   11467 O  O     . LYS C 2 78  ? 104.469 89.176  136.854 1.00 22.56 ?  57  LYS C O     1 
ATOM   11468 C  CB    . LYS C 2 78  ? 101.286 89.650  137.747 1.00 22.99 ?  57  LYS C CB    1 
ATOM   11469 C  CG    . LYS C 2 78  ? 100.610 90.284  138.966 1.00 24.86 ?  57  LYS C CG    1 
ATOM   11470 C  CD    . LYS C 2 78  ? 99.300  89.588  139.338 1.00 27.37 ?  57  LYS C CD    1 
ATOM   11471 C  CE    . LYS C 2 78  ? 98.782  90.084  140.694 1.00 28.99 ?  57  LYS C CE    1 
ATOM   11472 N  NZ    . LYS C 2 78  ? 97.412  89.544  140.941 1.00 29.82 1  57  LYS C NZ    1 
ATOM   11473 N  N     . VAL C 2 79  ? 103.067 89.503  135.114 1.00 22.70 ?  58  VAL C N     1 
ATOM   11474 C  CA    . VAL C 2 79  ? 103.878 88.848  134.091 1.00 23.48 ?  58  VAL C CA    1 
ATOM   11475 C  C     . VAL C 2 79  ? 105.302 89.452  134.025 1.00 23.04 ?  58  VAL C C     1 
ATOM   11476 O  O     . VAL C 2 79  ? 106.308 88.720  134.106 1.00 22.83 ?  58  VAL C O     1 
ATOM   11477 C  CB    . VAL C 2 79  ? 103.103 88.900  132.737 1.00 24.24 ?  58  VAL C CB    1 
ATOM   11478 C  CG1   . VAL C 2 79  ? 104.009 89.094  131.534 1.00 25.71 ?  58  VAL C CG1   1 
ATOM   11479 C  CG2   . VAL C 2 79  ? 102.180 87.669  132.603 1.00 25.04 ?  58  VAL C CG2   1 
ATOM   11480 N  N     . LEU C 2 80  ? 105.385 90.776  133.933 1.00 22.84 ?  59  LEU C N     1 
ATOM   11481 C  CA    . LEU C 2 80  ? 106.682 91.453  133.865 1.00 23.35 ?  59  LEU C CA    1 
ATOM   11482 C  C     . LEU C 2 80  ? 107.449 91.336  135.188 1.00 22.75 ?  59  LEU C C     1 
ATOM   11483 O  O     . LEU C 2 80  ? 108.674 91.246  135.180 1.00 22.75 ?  59  LEU C O     1 
ATOM   11484 C  CB    . LEU C 2 80  ? 106.539 92.927  133.460 1.00 23.91 ?  59  LEU C CB    1 
ATOM   11485 C  CG    . LEU C 2 80  ? 106.061 93.360  132.061 1.00 26.63 ?  59  LEU C CG    1 
ATOM   11486 C  CD1   . LEU C 2 80  ? 106.440 94.811  131.807 1.00 26.99 ?  59  LEU C CD1   1 
ATOM   11487 C  CD2   . LEU C 2 80  ? 106.608 92.488  130.943 1.00 27.23 ?  59  LEU C CD2   1 
ATOM   11488 N  N     . ALA C 2 81  ? 106.725 91.310  136.309 1.00 22.28 ?  60  ALA C N     1 
ATOM   11489 C  CA    . ALA C 2 81  ? 107.340 91.129  137.627 1.00 22.21 ?  60  ALA C CA    1 
ATOM   11490 C  C     . ALA C 2 81  ? 107.983 89.744  137.759 1.00 22.07 ?  60  ALA C C     1 
ATOM   11491 O  O     . ALA C 2 81  ? 109.084 89.632  138.288 1.00 21.97 ?  60  ALA C O     1 
ATOM   11492 C  CB    . ALA C 2 81  ? 106.318 91.390  138.754 1.00 22.38 ?  60  ALA C CB    1 
ATOM   11493 N  N     . GLY C 2 82  ? 107.307 88.714  137.237 1.00 21.67 ?  61  GLY C N     1 
ATOM   11494 C  CA    . GLY C 2 82  ? 107.834 87.353  137.180 1.00 21.74 ?  61  GLY C CA    1 
ATOM   11495 C  C     . GLY C 2 82  ? 109.091 87.267  136.331 1.00 21.79 ?  61  GLY C C     1 
ATOM   11496 O  O     . GLY C 2 82  ? 110.048 86.557  136.675 1.00 21.93 ?  61  GLY C O     1 
ATOM   11497 N  N     . LEU C 2 83  ? 109.093 88.014  135.228 1.00 21.54 ?  62  LEU C N     1 
ATOM   11498 C  CA    . LEU C 2 83  ? 110.267 88.126  134.364 1.00 21.12 ?  62  LEU C CA    1 
ATOM   11499 C  C     . LEU C 2 83  ? 111.409 88.828  135.085 1.00 20.89 ?  62  LEU C C     1 
ATOM   11500 O  O     . LEU C 2 83  ? 112.558 88.393  134.983 1.00 20.84 ?  62  LEU C O     1 
ATOM   11501 C  CB    . LEU C 2 83  ? 109.940 88.877  133.068 1.00 21.23 ?  62  LEU C CB    1 
ATOM   11502 C  CG    . LEU C 2 83  ? 108.963 88.250  132.064 1.00 21.98 ?  62  LEU C CG    1 
ATOM   11503 C  CD1   . LEU C 2 83  ? 108.643 89.220  130.924 1.00 24.12 ?  62  LEU C CD1   1 
ATOM   11504 C  CD2   . LEU C 2 83  ? 109.487 86.944  131.499 1.00 22.03 ?  62  LEU C CD2   1 
ATOM   11505 N  N     . THR C 2 84  ? 111.088 89.906  135.801 1.00 19.93 ?  63  THR C N     1 
ATOM   11506 C  CA    . THR C 2 84  ? 112.088 90.663  136.551 1.00 19.71 ?  63  THR C CA    1 
ATOM   11507 C  C     . THR C 2 84  ? 112.799 89.771  137.556 1.00 19.63 ?  63  THR C C     1 
ATOM   11508 O  O     . THR C 2 84  ? 114.021 89.855  137.706 1.00 19.62 ?  63  THR C O     1 
ATOM   11509 C  CB    . THR C 2 84  ? 111.461 91.871  137.288 1.00 20.22 ?  63  THR C CB    1 
ATOM   11510 O  OG1   . THR C 2 84  ? 110.675 92.648  136.367 1.00 19.37 ?  63  THR C OG1   1 
ATOM   11511 C  CG2   . THR C 2 84  ? 112.536 92.731  137.908 1.00 19.45 ?  63  THR C CG2   1 
ATOM   11512 N  N     . LEU C 2 85  ? 112.034 88.926  138.243 1.00 19.66 ?  64  LEU C N     1 
ATOM   11513 C  CA    . LEU C 2 85  ? 112.594 88.014  139.237 1.00 20.51 ?  64  LEU C CA    1 
ATOM   11514 C  C     . LEU C 2 85  ? 113.586 87.041  138.590 1.00 20.84 ?  64  LEU C C     1 
ATOM   11515 O  O     . LEU C 2 85  ? 114.714 86.893  139.064 1.00 21.30 ?  64  LEU C O     1 
ATOM   11516 C  CB    . LEU C 2 85  ? 111.491 87.262  140.001 1.00 20.03 ?  64  LEU C CB    1 
ATOM   11517 C  CG    . LEU C 2 85  ? 112.021 86.252  141.045 1.00 21.43 ?  64  LEU C CG    1 
ATOM   11518 C  CD1   . LEU C 2 85  ? 112.766 86.949  142.208 1.00 21.61 ?  64  LEU C CD1   1 
ATOM   11519 C  CD2   . LEU C 2 85  ? 110.921 85.346  141.594 1.00 20.99 ?  64  LEU C CD2   1 
ATOM   11520 N  N     . LEU C 2 86  ? 113.162 86.402  137.506 1.00 21.37 ?  65  LEU C N     1 
ATOM   11521 C  CA    . LEU C 2 86  ? 114.020 85.485  136.750 1.00 21.92 ?  65  LEU C CA    1 
ATOM   11522 C  C     . LEU C 2 86  ? 115.339 86.135  136.302 1.00 21.76 ?  65  LEU C C     1 
ATOM   11523 O  O     . LEU C 2 86  ? 116.407 85.554  136.496 1.00 21.72 ?  65  LEU C O     1 
ATOM   11524 C  CB    . LEU C 2 86  ? 113.271 84.914  135.537 1.00 22.42 ?  65  LEU C CB    1 
ATOM   11525 C  CG    . LEU C 2 86  ? 112.092 83.934  135.720 1.00 24.26 ?  65  LEU C CG    1 
ATOM   11526 C  CD1   . LEU C 2 86  ? 111.454 83.638  134.364 1.00 24.67 ?  65  LEU C CD1   1 
ATOM   11527 C  CD2   . LEU C 2 86  ? 112.534 82.642  136.385 1.00 25.60 ?  65  LEU C CD2   1 
ATOM   11528 N  N     . ASP C 2 87  ? 115.262 87.326  135.706 1.00 21.75 ?  66  ASP C N     1 
ATOM   11529 C  CA    . ASP C 2 87  ? 116.466 88.067  135.282 1.00 21.99 ?  66  ASP C CA    1 
ATOM   11530 C  C     . ASP C 2 87  ? 117.352 88.534  136.442 1.00 21.76 ?  66  ASP C C     1 
ATOM   11531 O  O     . ASP C 2 87  ? 118.583 88.593  136.310 1.00 21.65 ?  66  ASP C O     1 
ATOM   11532 C  CB    . ASP C 2 87  ? 116.090 89.287  134.437 1.00 22.23 ?  66  ASP C CB    1 
ATOM   11533 C  CG    . ASP C 2 87  ? 116.112 88.999  132.961 1.00 24.59 ?  66  ASP C CG    1 
ATOM   11534 O  OD1   . ASP C 2 87  ? 117.055 88.323  132.489 1.00 27.46 ?  66  ASP C OD1   1 
ATOM   11535 O  OD2   . ASP C 2 87  ? 115.185 89.465  132.269 1.00 27.98 -1 66  ASP C OD2   1 
ATOM   11536 N  N     . THR C 2 88  ? 116.722 88.899  137.556 1.00 21.50 ?  67  THR C N     1 
ATOM   11537 C  CA    . THR C 2 88  ? 117.452 89.243  138.771 1.00 21.80 ?  67  THR C CA    1 
ATOM   11538 C  C     . THR C 2 88  ? 118.375 88.084  139.193 1.00 22.04 ?  67  THR C C     1 
ATOM   11539 O  O     . THR C 2 88  ? 119.568 88.294  139.459 1.00 22.21 ?  67  THR C O     1 
ATOM   11540 C  CB    . THR C 2 88  ? 116.488 89.632  139.905 1.00 22.15 ?  67  THR C CB    1 
ATOM   11541 O  OG1   . THR C 2 88  ? 115.715 90.761  139.493 1.00 22.23 ?  67  THR C OG1   1 
ATOM   11542 C  CG2   . THR C 2 88  ? 117.240 89.992  141.189 1.00 21.19 ?  67  THR C CG2   1 
ATOM   11543 N  N     . GLU C 2 89  ? 117.831 86.871  139.219 1.00 21.55 ?  68  GLU C N     1 
ATOM   11544 C  CA    . GLU C 2 89  ? 118.599 85.714  139.659 1.00 21.81 ?  68  GLU C CA    1 
ATOM   11545 C  C     . GLU C 2 89  ? 119.567 85.212  138.576 1.00 21.35 ?  68  GLU C C     1 
ATOM   11546 O  O     . GLU C 2 89  ? 120.667 84.760  138.886 1.00 21.34 ?  68  GLU C O     1 
ATOM   11547 C  CB    . GLU C 2 89  ? 117.671 84.614  140.187 1.00 22.25 ?  68  GLU C CB    1 
ATOM   11548 C  CG    . GLU C 2 89  ? 117.175 84.888  141.636 1.00 24.02 ?  68  GLU C CG    1 
ATOM   11549 C  CD    . GLU C 2 89  ? 118.320 85.168  142.611 1.00 25.78 ?  68  GLU C CD    1 
ATOM   11550 O  OE1   . GLU C 2 89  ? 119.327 84.429  142.595 1.00 26.69 ?  68  GLU C OE1   1 
ATOM   11551 O  OE2   . GLU C 2 89  ? 118.217 86.133  143.404 1.00 28.98 -1 68  GLU C OE2   1 
ATOM   11552 N  N     . GLN C 2 90  ? 119.176 85.343  137.310 1.00 20.82 ?  69  GLN C N     1 
ATOM   11553 C  CA    . GLN C 2 90  ? 120.054 84.983  136.203 1.00 21.28 ?  69  GLN C CA    1 
ATOM   11554 C  C     . GLN C 2 90  ? 121.285 85.895  136.161 1.00 21.24 ?  69  GLN C C     1 
ATOM   11555 O  O     . GLN C 2 90  ? 122.392 85.435  135.869 1.00 20.99 ?  69  GLN C O     1 
ATOM   11556 C  CB    . GLN C 2 90  ? 119.296 85.006  134.864 1.00 21.86 ?  69  GLN C CB    1 
ATOM   11557 C  CG    . GLN C 2 90  ? 120.042 84.304  133.706 1.00 24.29 ?  69  GLN C CG    1 
ATOM   11558 C  CD    . GLN C 2 90  ? 120.116 82.783  133.875 1.00 27.14 ?  69  GLN C CD    1 
ATOM   11559 O  OE1   . GLN C 2 90  ? 119.979 82.262  134.985 1.00 27.13 ?  69  GLN C OE1   1 
ATOM   11560 N  NE2   . GLN C 2 90  ? 120.352 82.070  132.770 1.00 27.69 ?  69  GLN C NE2   1 
ATOM   11561 N  N     . GLY C 2 91  ? 121.086 87.174  136.491 1.00 20.62 ?  70  GLY C N     1 
ATOM   11562 C  CA    . GLY C 2 91  ? 122.173 88.158  136.511 1.00 22.00 ?  70  GLY C CA    1 
ATOM   11563 C  C     . GLY C 2 91  ? 123.015 88.107  137.770 1.00 22.45 ?  70  GLY C C     1 
ATOM   11564 O  O     . GLY C 2 91  ? 124.239 88.162  137.685 1.00 23.53 ?  70  GLY C O     1 
ATOM   11565 N  N     . ASN C 2 92  ? 122.363 88.001  138.931 1.00 22.79 ?  71  ASN C N     1 
ATOM   11566 C  CA    . ASN C 2 92  ? 123.057 87.972  140.228 1.00 23.85 ?  71  ASN C CA    1 
ATOM   11567 C  C     . ASN C 2 92  ? 123.812 86.669  140.462 1.00 24.33 ?  71  ASN C C     1 
ATOM   11568 O  O     . ASN C 2 92  ? 124.882 86.669  141.081 1.00 24.17 ?  71  ASN C O     1 
ATOM   11569 C  CB    . ASN C 2 92  ? 122.069 88.141  141.390 1.00 23.74 ?  71  ASN C CB    1 
ATOM   11570 C  CG    . ASN C 2 92  ? 121.464 89.532  141.474 1.00 24.38 ?  71  ASN C CG    1 
ATOM   11571 O  OD1   . ASN C 2 92  ? 121.733 90.414  140.648 1.00 25.16 ?  71  ASN C OD1   1 
ATOM   11572 N  ND2   . ASN C 2 92  ? 120.628 89.730  142.479 1.00 24.07 ?  71  ASN C ND2   1 
ATOM   11573 N  N     . THR C 2 93  ? 123.253 85.564  139.964 1.00 23.97 ?  72  THR C N     1 
ATOM   11574 C  CA    . THR C 2 93  ? 123.674 84.230  140.416 1.00 24.97 ?  72  THR C CA    1 
ATOM   11575 C  C     . THR C 2 93  ? 124.035 83.305  139.264 1.00 24.52 ?  72  THR C C     1 
ATOM   11576 O  O     . THR C 2 93  ? 125.160 82.826  139.191 1.00 25.39 ?  72  THR C O     1 
ATOM   11577 C  CB    . THR C 2 93  ? 122.582 83.558  141.291 1.00 24.54 ?  72  THR C CB    1 
ATOM   11578 O  OG1   . THR C 2 93  ? 122.222 84.430  142.370 1.00 26.43 ?  72  THR C OG1   1 
ATOM   11579 C  CG2   . THR C 2 93  ? 123.075 82.240  141.869 1.00 26.83 ?  72  THR C CG2   1 
ATOM   11580 N  N     . GLY C 2 94  ? 123.080 83.072  138.375 1.00 24.37 ?  73  GLY C N     1 
ATOM   11581 C  CA    . GLY C 2 94  ? 123.194 82.052  137.321 1.00 24.24 ?  73  GLY C CA    1 
ATOM   11582 C  C     . GLY C 2 94  ? 124.356 82.257  136.373 1.00 24.94 ?  73  GLY C C     1 
ATOM   11583 O  O     . GLY C 2 94  ? 125.246 81.406  136.274 1.00 25.86 ?  73  GLY C O     1 
ATOM   11584 N  N     . MET C 2 95  ? 124.355 83.385  135.672 1.00 24.07 ?  74  MET C N     1 
ATOM   11585 C  CA    . MET C 2 95  ? 125.426 83.660  134.723 1.00 24.35 ?  74  MET C CA    1 
ATOM   11586 C  C     . MET C 2 95  ? 126.823 83.824  135.354 1.00 23.52 ?  74  MET C C     1 
ATOM   11587 O  O     . MET C 2 95  ? 127.769 83.254  134.820 1.00 23.40 ?  74  MET C O     1 
ATOM   11588 C  CB    . MET C 2 95  ? 125.069 84.821  133.794 1.00 24.38 ?  74  MET C CB    1 
ATOM   11589 C  CG    . MET C 2 95  ? 123.974 84.489  132.780 1.00 27.47 ?  74  MET C CG    1 
ATOM   11590 S  SD    . MET C 2 95  ? 124.507 83.163  131.662 1.00 32.54 ?  74  MET C SD    1 
ATOM   11591 C  CE    . MET C 2 95  ? 125.699 84.015  130.690 1.00 34.32 ?  74  MET C CE    1 
ATOM   11592 N  N     . PRO C 2 96  ? 126.957 84.585  136.477 1.00 23.36 ?  75  PRO C N     1 
ATOM   11593 C  CA    . PRO C 2 96  ? 128.270 84.683  137.150 1.00 23.27 ?  75  PRO C CA    1 
ATOM   11594 C  C     . PRO C 2 96  ? 128.827 83.350  137.640 1.00 23.77 ?  75  PRO C C     1 
ATOM   11595 O  O     . PRO C 2 96  ? 130.025 83.106  137.500 1.00 23.46 ?  75  PRO C O     1 
ATOM   11596 C  CB    . PRO C 2 96  ? 127.988 85.583  138.365 1.00 23.55 ?  75  PRO C CB    1 
ATOM   11597 C  CG    . PRO C 2 96  ? 126.823 86.415  137.953 1.00 23.85 ?  75  PRO C CG    1 
ATOM   11598 C  CD    . PRO C 2 96  ? 125.969 85.485  137.105 1.00 22.76 ?  75  PRO C CD    1 
ATOM   11599 N  N     . ILE C 2 97  ? 127.977 82.505  138.228 1.00 23.81 ?  76  ILE C N     1 
ATOM   11600 C  CA    . ILE C 2 97  ? 128.428 81.201  138.721 1.00 24.52 ?  76  ILE C CA    1 
ATOM   11601 C  C     . ILE C 2 97  ? 128.867 80.244  137.592 1.00 23.92 ?  76  ILE C C     1 
ATOM   11602 O  O     . ILE C 2 97  ? 129.895 79.562  137.706 1.00 23.99 ?  76  ILE C O     1 
ATOM   11603 C  CB    . ILE C 2 97  ? 127.395 80.551  139.684 1.00 24.49 ?  76  ILE C CB    1 
ATOM   11604 C  CG1   . ILE C 2 97  ? 128.078 79.533  140.595 1.00 27.08 ?  76  ILE C CG1   1 
ATOM   11605 C  CG2   . ILE C 2 97  ? 126.222 79.895  138.925 1.00 26.06 ?  76  ILE C CG2   1 
ATOM   11606 C  CD1   . ILE C 2 97  ? 127.329 79.312  141.901 1.00 31.37 ?  76  ILE C CD1   1 
ATOM   11607 N  N     . VAL C 2 98  ? 128.113 80.218  136.497 1.00 23.97 ?  77  VAL C N     1 
ATOM   11608 C  CA    . VAL C 2 98  ? 128.521 79.446  135.315 1.00 24.01 ?  77  VAL C CA    1 
ATOM   11609 C  C     . VAL C 2 98  ? 129.840 80.013  134.747 1.00 25.23 ?  77  VAL C C     1 
ATOM   11610 O  O     . VAL C 2 98  ? 130.758 79.253  134.423 1.00 25.77 ?  77  VAL C O     1 
ATOM   11611 C  CB    . VAL C 2 98  ? 127.399 79.399  134.246 1.00 23.98 ?  77  VAL C CB    1 
ATOM   11612 C  CG1   . VAL C 2 98  ? 127.918 78.844  132.922 1.00 23.17 ?  77  VAL C CG1   1 
ATOM   11613 C  CG2   . VAL C 2 98  ? 126.226 78.553  134.760 1.00 22.55 ?  77  VAL C CG2   1 
ATOM   11614 N  N     . ALA C 2 99  ? 129.951 81.341  134.682 1.00 25.42 ?  78  ALA C N     1 
ATOM   11615 C  CA    . ALA C 2 99  ? 131.203 81.977  134.236 1.00 26.72 ?  78  ALA C CA    1 
ATOM   11616 C  C     . ALA C 2 99  ? 132.396 81.514  135.077 1.00 27.46 ?  78  ALA C C     1 
ATOM   11617 O  O     . ALA C 2 99  ? 133.463 81.223  134.536 1.00 28.07 ?  78  ALA C O     1 
ATOM   11618 C  CB    . ALA C 2 99  ? 131.088 83.489  134.268 1.00 26.52 ?  78  ALA C CB    1 
ATOM   11619 N  N     . GLU C 2 100 ? 132.194 81.408  136.389 1.00 28.33 ?  79  GLU C N     1 
ATOM   11620 C  CA    . GLU C 2 100 ? 133.258 81.004  137.311 1.00 29.60 ?  79  GLU C CA    1 
ATOM   11621 C  C     . GLU C 2 100 ? 133.801 79.606  137.001 1.00 29.64 ?  79  GLU C C     1 
ATOM   11622 O  O     . GLU C 2 100 ? 135.007 79.356  137.115 1.00 29.72 ?  79  GLU C O     1 
ATOM   11623 C  CB    . GLU C 2 100 ? 132.773 81.082  138.759 1.00 29.70 ?  79  GLU C CB    1 
ATOM   11624 C  CG    . GLU C 2 100 ? 133.847 80.752  139.795 1.00 33.58 ?  79  GLU C CG    1 
ATOM   11625 C  CD    . GLU C 2 100 ? 133.327 80.707  141.218 1.00 37.83 ?  79  GLU C CD    1 
ATOM   11626 O  OE1   . GLU C 2 100 ? 132.158 81.088  141.469 1.00 40.64 ?  79  GLU C OE1   1 
ATOM   11627 O  OE2   . GLU C 2 100 ? 134.101 80.276  142.101 1.00 41.40 -1 79  GLU C OE2   1 
ATOM   11628 N  N     . HIS C 2 101 ? 132.914 78.703  136.588 1.00 29.43 ?  80  HIS C N     1 
ATOM   11629 C  CA    . HIS C 2 101 ? 133.281 77.302  136.432 1.00 29.74 ?  80  HIS C CA    1 
ATOM   11630 C  C     . HIS C 2 101 ? 133.679 76.890  135.013 1.00 30.18 ?  80  HIS C C     1 
ATOM   11631 O  O     . HIS C 2 101 ? 134.285 75.843  134.823 1.00 30.30 ?  80  HIS C O     1 
ATOM   11632 C  CB    . HIS C 2 101 ? 132.188 76.396  137.023 1.00 29.21 ?  80  HIS C CB    1 
ATOM   11633 C  CG    . HIS C 2 101 ? 132.113 76.467  138.517 1.00 29.60 ?  80  HIS C CG    1 
ATOM   11634 N  ND1   . HIS C 2 101 ? 131.292 77.354  139.183 1.00 30.06 ?  80  HIS C ND1   1 
ATOM   11635 C  CD2   . HIS C 2 101 ? 132.790 75.791  139.475 1.00 29.49 ?  80  HIS C CD2   1 
ATOM   11636 C  CE1   . HIS C 2 101 ? 131.458 77.212  140.488 1.00 29.56 ?  80  HIS C CE1   1 
ATOM   11637 N  NE2   . HIS C 2 101 ? 132.359 76.269  140.691 1.00 30.20 ?  80  HIS C NE2   1 
ATOM   11638 N  N     . VAL C 2 102 ? 133.351 77.722  134.029 1.00 30.70 ?  81  VAL C N     1 
ATOM   11639 C  CA    . VAL C 2 102 ? 133.700 77.460  132.635 1.00 31.47 ?  81  VAL C CA    1 
ATOM   11640 C  C     . VAL C 2 102 ? 135.113 77.967  132.357 1.00 32.45 ?  81  VAL C C     1 
ATOM   11641 O  O     . VAL C 2 102 ? 135.442 79.108  132.703 1.00 32.50 ?  81  VAL C O     1 
ATOM   11642 C  CB    . VAL C 2 102 ? 132.694 78.116  131.652 1.00 31.18 ?  81  VAL C CB    1 
ATOM   11643 C  CG1   . VAL C 2 102 ? 133.184 78.012  130.206 1.00 31.20 ?  81  VAL C CG1   1 
ATOM   11644 C  CG2   . VAL C 2 102 ? 131.326 77.463  131.779 1.00 31.28 ?  81  VAL C CG2   1 
ATOM   11645 N  N     . ASP C 2 103 ? 135.931 77.121  131.728 1.00 33.38 ?  82  ASP C N     1 
ATOM   11646 C  CA    . ASP C 2 103 ? 137.326 77.450  131.422 1.00 34.82 ?  82  ASP C CA    1 
ATOM   11647 C  C     . ASP C 2 103 ? 137.492 78.202  130.107 1.00 34.74 ?  82  ASP C C     1 
ATOM   11648 O  O     . ASP C 2 103 ? 136.806 77.910  129.119 1.00 35.00 ?  82  ASP C O     1 
ATOM   11649 C  CB    . ASP C 2 103 ? 138.192 76.181  131.403 1.00 35.82 ?  82  ASP C CB    1 
ATOM   11650 C  CG    . ASP C 2 103 ? 138.451 75.622  132.799 1.00 38.29 ?  82  ASP C CG    1 
ATOM   11651 O  OD1   . ASP C 2 103 ? 138.535 76.410  133.772 1.00 41.49 ?  82  ASP C OD1   1 
ATOM   11652 O  OD2   . ASP C 2 103 ? 138.574 74.388  132.925 1.00 41.10 -1 82  ASP C OD2   1 
ATOM   11653 N  N     . GLY C 2 104 ? 138.413 79.166  130.106 1.00 34.89 ?  83  GLY C N     1 
ATOM   11654 C  CA    . GLY C 2 104 ? 138.757 79.930  128.902 1.00 35.11 ?  83  GLY C CA    1 
ATOM   11655 C  C     . GLY C 2 104 ? 138.309 81.377  128.974 1.00 34.96 ?  83  GLY C C     1 
ATOM   11656 O  O     . GLY C 2 104 ? 137.120 81.651  129.155 1.00 34.57 ?  83  GLY C O     1 
ATOM   11657 N  N     . HIS C 2 105 ? 139.260 82.301  128.815 1.00 35.02 ?  84  HIS C N     1 
ATOM   11658 C  CA    . HIS C 2 105 ? 138.999 83.739  128.970 1.00 34.83 ?  84  HIS C CA    1 
ATOM   11659 C  C     . HIS C 2 105 ? 137.929 84.285  128.034 1.00 33.77 ?  84  HIS C C     1 
ATOM   11660 O  O     . HIS C 2 105 ? 137.161 85.169  128.419 1.00 33.25 ?  84  HIS C O     1 
ATOM   11661 C  CB    . HIS C 2 105 ? 140.288 84.560  128.848 1.00 36.09 ?  84  HIS C CB    1 
ATOM   11662 C  CG    . HIS C 2 105 ? 141.166 84.478  130.059 1.00 39.17 ?  84  HIS C CG    1 
ATOM   11663 N  ND1   . HIS C 2 105 ? 142.544 84.523  129.986 1.00 43.00 ?  84  HIS C ND1   1 
ATOM   11664 C  CD2   . HIS C 2 105 ? 140.864 84.332  131.373 1.00 41.84 ?  84  HIS C CD2   1 
ATOM   11665 C  CE1   . HIS C 2 105 ? 143.050 84.418  131.204 1.00 43.47 ?  84  HIS C CE1   1 
ATOM   11666 N  NE2   . HIS C 2 105 ? 142.052 84.301  132.064 1.00 43.10 ?  84  HIS C NE2   1 
ATOM   11667 N  N     . GLN C 2 106 ? 137.865 83.753  126.819 1.00 32.84 ?  85  GLN C N     1 
ATOM   11668 C  CA    . GLN C 2 106 ? 136.848 84.197  125.870 1.00 32.29 ?  85  GLN C CA    1 
ATOM   11669 C  C     . GLN C 2 106 ? 135.450 83.682  126.234 1.00 30.88 ?  85  GLN C C     1 
ATOM   11670 O  O     . GLN C 2 106 ? 134.467 84.424  126.125 1.00 30.44 ?  85  GLN C O     1 
ATOM   11671 C  CB    . GLN C 2 106 ? 137.216 83.797  124.450 1.00 32.85 ?  85  GLN C CB    1 
ATOM   11672 C  CG    . GLN C 2 106 ? 138.467 84.490  123.927 1.00 35.55 ?  85  GLN C CG    1 
ATOM   11673 C  CD    . GLN C 2 106 ? 138.862 83.991  122.561 1.00 38.12 ?  85  GLN C CD    1 
ATOM   11674 O  OE1   . GLN C 2 106 ? 138.008 83.712  121.721 1.00 39.96 ?  85  GLN C OE1   1 
ATOM   11675 N  NE2   . GLN C 2 106 ? 140.168 83.877  122.327 1.00 40.39 ?  85  GLN C NE2   1 
ATOM   11676 N  N     . ARG C 2 107 ? 135.365 82.422  126.657 1.00 29.75 ?  86  ARG C N     1 
ATOM   11677 C  CA    . ARG C 2 107 ? 134.092 81.863  127.127 1.00 28.87 ?  86  ARG C CA    1 
ATOM   11678 C  C     . ARG C 2 107 ? 133.610 82.645  128.341 1.00 28.16 ?  86  ARG C C     1 
ATOM   11679 O  O     . ARG C 2 107 ? 132.427 82.966  128.442 1.00 27.55 ?  86  ARG C O     1 
ATOM   11680 C  CB    . ARG C 2 107 ? 134.225 80.381  127.474 1.00 28.48 ?  86  ARG C CB    1 
ATOM   11681 C  CG    . ARG C 2 107 ? 134.374 79.489  126.254 1.00 29.86 ?  86  ARG C CG    1 
ATOM   11682 C  CD    . ARG C 2 107 ? 134.542 78.026  126.627 1.00 30.23 ?  86  ARG C CD    1 
ATOM   11683 N  NE    . ARG C 2 107 ? 134.226 77.202  125.467 1.00 33.04 ?  86  ARG C NE    1 
ATOM   11684 C  CZ    . ARG C 2 107 ? 133.920 75.917  125.510 1.00 31.54 ?  86  ARG C CZ    1 
ATOM   11685 N  NH1   . ARG C 2 107 ? 133.903 75.267  126.665 1.00 31.85 1  86  ARG C NH1   1 
ATOM   11686 N  NH2   . ARG C 2 107 ? 133.638 75.284  124.383 1.00 34.74 ?  86  ARG C NH2   1 
ATOM   11687 N  N     . LYS C 2 108 ? 134.532 82.960  129.249 1.00 27.65 ?  87  LYS C N     1 
ATOM   11688 C  CA    . LYS C 2 108 ? 134.196 83.762  130.430 1.00 27.96 ?  87  LYS C CA    1 
ATOM   11689 C  C     . LYS C 2 108 ? 133.740 85.170  130.078 1.00 27.75 ?  87  LYS C C     1 
ATOM   11690 O  O     . LYS C 2 108 ? 132.841 85.704  130.726 1.00 28.29 ?  87  LYS C O     1 
ATOM   11691 C  CB    . LYS C 2 108 ? 135.360 83.828  131.419 1.00 27.80 ?  87  LYS C CB    1 
ATOM   11692 C  CG    . LYS C 2 108 ? 135.651 82.511  132.108 1.00 29.04 ?  87  LYS C CG    1 
ATOM   11693 C  CD    . LYS C 2 108 ? 136.800 82.683  133.092 1.00 31.15 ?  87  LYS C CD    1 
ATOM   11694 C  CE    . LYS C 2 108 ? 137.265 81.346  133.640 1.00 32.05 ?  87  LYS C CE    1 
ATOM   11695 N  NZ    . LYS C 2 108 ? 136.332 80.849  134.681 1.00 30.88 1  87  LYS C NZ    1 
ATOM   11696 N  N     . ALA C 2 109 ? 134.353 85.769  129.056 1.00 27.69 ?  88  ALA C N     1 
ATOM   11697 C  CA    . ALA C 2 109 ? 133.957 87.110  128.605 1.00 27.46 ?  88  ALA C CA    1 
ATOM   11698 C  C     . ALA C 2 109 ? 132.527 87.150  128.059 1.00 26.87 ?  88  ALA C C     1 
ATOM   11699 O  O     . ALA C 2 109 ? 131.794 88.108  128.302 1.00 26.47 ?  88  ALA C O     1 
ATOM   11700 C  CB    . ALA C 2 109 ? 134.929 87.634  127.567 1.00 27.98 ?  88  ALA C CB    1 
ATOM   11701 N  N     . VAL C 2 110 ? 132.145 86.117  127.310 1.00 25.98 ?  89  VAL C N     1 
ATOM   11702 C  CA    . VAL C 2 110 ? 130.782 85.997  126.786 1.00 25.46 ?  89  VAL C CA    1 
ATOM   11703 C  C     . VAL C 2 110 ? 129.792 85.838  127.945 1.00 24.57 ?  89  VAL C C     1 
ATOM   11704 O  O     . VAL C 2 110 ? 128.796 86.564  128.027 1.00 23.62 ?  89  VAL C O     1 
ATOM   11705 C  CB    . VAL C 2 110 ? 130.657 84.820  125.788 1.00 25.80 ?  89  VAL C CB    1 
ATOM   11706 C  CG1   . VAL C 2 110 ? 129.192 84.539  125.429 1.00 25.44 ?  89  VAL C CG1   1 
ATOM   11707 C  CG2   . VAL C 2 110 ? 131.476 85.103  124.529 1.00 26.23 ?  89  VAL C CG2   1 
ATOM   11708 N  N     . LEU C 2 111 ? 130.091 84.914  128.855 1.00 24.33 ?  90  LEU C N     1 
ATOM   11709 C  CA    . LEU C 2 111 ? 129.210 84.670  129.998 1.00 23.93 ?  90  LEU C CA    1 
ATOM   11710 C  C     . LEU C 2 111 ? 129.087 85.878  130.928 1.00 23.77 ?  90  LEU C C     1 
ATOM   11711 O  O     . LEU C 2 111 ? 128.001 86.152  131.438 1.00 23.04 ?  90  LEU C O     1 
ATOM   11712 C  CB    . LEU C 2 111 ? 129.628 83.416  130.771 1.00 23.73 ?  90  LEU C CB    1 
ATOM   11713 C  CG    . LEU C 2 111 ? 129.523 82.110  129.977 1.00 24.50 ?  90  LEU C CG    1 
ATOM   11714 C  CD1   . LEU C 2 111 ? 130.372 81.019  130.610 1.00 24.02 ?  90  LEU C CD1   1 
ATOM   11715 C  CD2   . LEU C 2 111 ? 128.070 81.655  129.827 1.00 25.38 ?  90  LEU C CD2   1 
ATOM   11716 N  N     . ASN C 2 112 ? 130.198 86.588  131.152 1.00 24.24 ?  91  ASN C N     1 
ATOM   11717 C  CA    . ASN C 2 112 ? 130.167 87.849  131.911 1.00 24.95 ?  91  ASN C CA    1 
ATOM   11718 C  C     . ASN C 2 112 ? 129.314 88.928  131.251 1.00 24.25 ?  91  ASN C C     1 
ATOM   11719 O  O     . ASN C 2 112 ? 128.598 89.658  131.936 1.00 23.99 ?  91  ASN C O     1 
ATOM   11720 C  CB    . ASN C 2 112 ? 131.578 88.401  132.134 1.00 25.81 ?  91  ASN C CB    1 
ATOM   11721 C  CG    . ASN C 2 112 ? 132.236 87.819  133.356 1.00 29.96 ?  91  ASN C CG    1 
ATOM   11722 O  OD1   . ASN C 2 112 ? 132.125 88.375  134.450 1.00 35.44 ?  91  ASN C OD1   1 
ATOM   11723 N  ND2   . ASN C 2 112 ? 132.925 86.690  133.188 1.00 32.37 ?  91  ASN C ND2   1 
ATOM   11724 N  N     . PHE C 2 113 ? 129.425 89.049  129.929 1.00 23.60 ?  92  PHE C N     1 
ATOM   11725 C  CA    . PHE C 2 113 ? 128.602 89.992  129.179 1.00 23.32 ?  92  PHE C CA    1 
ATOM   11726 C  C     . PHE C 2 113 ? 127.110 89.649  129.301 1.00 22.63 ?  92  PHE C C     1 
ATOM   11727 O  O     . PHE C 2 113 ? 126.287 90.537  129.529 1.00 21.94 ?  92  PHE C O     1 
ATOM   11728 C  CB    . PHE C 2 113 ? 128.987 90.016  127.693 1.00 23.27 ?  92  PHE C CB    1 
ATOM   11729 C  CG    . PHE C 2 113 ? 128.346 91.142  126.930 1.00 24.66 ?  92  PHE C CG    1 
ATOM   11730 C  CD1   . PHE C 2 113 ? 128.975 92.392  126.845 1.00 25.72 ?  92  PHE C CD1   1 
ATOM   11731 C  CD2   . PHE C 2 113 ? 127.106 90.970  126.319 1.00 25.36 ?  92  PHE C CD2   1 
ATOM   11732 C  CE1   . PHE C 2 113 ? 128.377 93.446  126.155 1.00 25.92 ?  92  PHE C CE1   1 
ATOM   11733 C  CE2   . PHE C 2 113 ? 126.495 92.022  125.625 1.00 25.82 ?  92  PHE C CE2   1 
ATOM   11734 C  CZ    . PHE C 2 113 ? 127.130 93.263  125.547 1.00 25.80 ?  92  PHE C CZ    1 
ATOM   11735 N  N     . MET C 2 114 ? 126.778 88.368  129.121 1.00 22.03 ?  93  MET C N     1 
ATOM   11736 C  CA    . MET C 2 114 ? 125.398 87.891  129.283 1.00 22.14 ?  93  MET C CA    1 
ATOM   11737 C  C     . MET C 2 114 ? 124.848 88.176  130.692 1.00 21.64 ?  93  MET C C     1 
ATOM   11738 O  O     . MET C 2 114 ? 123.705 88.623  130.831 1.00 21.59 ?  93  MET C O     1 
ATOM   11739 C  CB    . MET C 2 114 ? 125.302 86.404  128.960 1.00 22.46 ?  93  MET C CB    1 
ATOM   11740 C  CG    . MET C 2 114 ? 125.524 86.082  127.490 1.00 23.80 ?  93  MET C CG    1 
ATOM   11741 S  SD    . MET C 2 114 ? 125.593 84.304  127.182 1.00 28.07 ?  93  MET C SD    1 
ATOM   11742 C  CE    . MET C 2 114 ? 125.503 84.310  125.373 1.00 26.42 ?  93  MET C CE    1 
ATOM   11743 N  N     . ALA C 2 115 ? 125.672 87.949  131.720 1.00 20.98 ?  94  ALA C N     1 
ATOM   11744 C  CA    . ALA C 2 115 ? 125.316 88.284  133.112 1.00 20.58 ?  94  ALA C CA    1 
ATOM   11745 C  C     . ALA C 2 115 ? 124.978 89.761  133.302 1.00 21.01 ?  94  ALA C C     1 
ATOM   11746 O  O     . ALA C 2 115 ? 124.005 90.114  133.995 1.00 21.06 ?  94  ALA C O     1 
ATOM   11747 C  CB    . ALA C 2 115 ? 126.456 87.867  134.071 1.00 20.83 ?  94  ALA C CB    1 
ATOM   11748 N  N     . MET C 2 116 ? 125.802 90.629  132.719 1.00 20.36 ?  95  MET C N     1 
ATOM   11749 C  CA    . MET C 2 116 ? 125.569 92.060  132.783 1.00 20.83 ?  95  MET C CA    1 
ATOM   11750 C  C     . MET C 2 116 ? 124.218 92.413  132.139 1.00 20.55 ?  95  MET C C     1 
ATOM   11751 O  O     . MET C 2 116 ? 123.434 93.174  132.704 1.00 20.70 ?  95  MET C O     1 
ATOM   11752 C  CB    . MET C 2 116 ? 126.729 92.809  132.114 1.00 20.64 ?  95  MET C CB    1 
ATOM   11753 C  CG    . MET C 2 116 ? 126.551 94.324  132.001 1.00 21.42 ?  95  MET C CG    1 
ATOM   11754 S  SD    . MET C 2 116 ? 125.497 94.787  130.612 1.00 22.51 ?  95  MET C SD    1 
ATOM   11755 C  CE    . MET C 2 116 ? 126.418 94.124  129.222 1.00 20.66 ?  95  MET C CE    1 
ATOM   11756 N  N     . MET C 2 117 ? 123.947 91.838  130.972 1.00 20.50 ?  96  MET C N     1 
ATOM   11757 C  CA    . MET C 2 117 ? 122.687 92.081  130.283 1.00 21.22 ?  96  MET C CA    1 
ATOM   11758 C  C     . MET C 2 117 ? 121.492 91.715  131.162 1.00 21.11 ?  96  MET C C     1 
ATOM   11759 O  O     . MET C 2 117 ? 120.527 92.479  131.236 1.00 20.71 ?  96  MET C O     1 
ATOM   11760 C  CB    . MET C 2 117 ? 122.634 91.342  128.939 1.00 21.35 ?  96  MET C CB    1 
ATOM   11761 C  CG    . MET C 2 117 ? 123.547 91.935  127.821 1.00 22.54 ?  96  MET C CG    1 
ATOM   11762 S  SD    . MET C 2 117 ? 123.313 93.690  127.458 1.00 24.89 ?  96  MET C SD    1 
ATOM   11763 C  CE    . MET C 2 117 ? 121.774 93.656  126.540 1.00 24.95 ?  96  MET C CE    1 
ATOM   11764 N  N     . GLU C 2 118 ? 121.575 90.567  131.836 1.00 21.18 ?  97  GLU C N     1 
ATOM   11765 C  CA    . GLU C 2 118 ? 120.495 90.086  132.704 1.00 21.99 ?  97  GLU C CA    1 
ATOM   11766 C  C     . GLU C 2 118 ? 120.080 91.115  133.757 1.00 22.10 ?  97  GLU C C     1 
ATOM   11767 O  O     . GLU C 2 118 ? 118.906 91.483  133.840 1.00 22.22 ?  97  GLU C O     1 
ATOM   11768 C  CB    . GLU C 2 118 ? 120.855 88.760  133.394 1.00 22.01 ?  97  GLU C CB    1 
ATOM   11769 C  CG    . GLU C 2 118 ? 121.316 87.605  132.497 1.00 24.38 ?  97  GLU C CG    1 
ATOM   11770 C  CD    . GLU C 2 118 ? 120.296 87.145  131.447 1.00 26.32 ?  97  GLU C CD    1 
ATOM   11771 O  OE1   . GLU C 2 118 ? 119.505 87.957  130.945 1.00 29.86 ?  97  GLU C OE1   1 
ATOM   11772 O  OE2   . GLU C 2 118 ? 120.323 85.959  131.079 1.00 29.19 -1 97  GLU C OE2   1 
ATOM   11773 N  N     . ASN C 2 119 ? 121.033 91.581  134.563 1.00 22.26 ?  98  ASN C N     1 
ATOM   11774 C  CA    . ASN C 2 119 ? 120.670 92.457  135.677 1.00 21.91 ?  98  ASN C CA    1 
ATOM   11775 C  C     . ASN C 2 119 ? 120.847 93.967  135.459 1.00 22.41 ?  98  ASN C C     1 
ATOM   11776 O  O     . ASN C 2 119 ? 120.122 94.763  136.053 1.00 23.07 ?  98  ASN C O     1 
ATOM   11777 C  CB    . ASN C 2 119 ? 121.222 91.958  137.029 1.00 21.93 ?  98  ASN C CB    1 
ATOM   11778 C  CG    . ASN C 2 119 ? 122.734 91.935  137.093 1.00 21.31 ?  98  ASN C CG    1 
ATOM   11779 O  OD1   . ASN C 2 119 ? 123.425 92.257  136.124 1.00 21.88 ?  98  ASN C OD1   1 
ATOM   11780 N  ND2   . ASN C 2 119 ? 123.262 91.561  138.256 1.00 21.73 ?  98  ASN C ND2   1 
ATOM   11781 N  N     . ALA C 2 120 ? 121.808 94.356  134.626 1.00 22.75 ?  99  ALA C N     1 
ATOM   11782 C  CA    . ALA C 2 120 ? 122.043 95.769  134.332 1.00 23.12 ?  99  ALA C CA    1 
ATOM   11783 C  C     . ALA C 2 120 ? 121.176 96.289  133.203 1.00 23.60 ?  99  ALA C C     1 
ATOM   11784 O  O     . ALA C 2 120 ? 120.930 97.498  133.132 1.00 24.14 ?  99  ALA C O     1 
ATOM   11785 C  CB    . ALA C 2 120 ? 123.533 96.046  134.044 1.00 23.28 ?  99  ALA C CB    1 
ATOM   11786 N  N     . VAL C 2 121 ? 120.705 95.395  132.327 1.00 23.23 ?  100 VAL C N     1 
ATOM   11787 C  CA    . VAL C 2 121 ? 119.859 95.827  131.198 1.00 23.74 ?  100 VAL C CA    1 
ATOM   11788 C  C     . VAL C 2 121 ? 118.430 95.287  131.258 1.00 23.62 ?  100 VAL C C     1 
ATOM   11789 O  O     . VAL C 2 121 ? 117.485 96.070  131.284 1.00 24.51 ?  100 VAL C O     1 
ATOM   11790 C  CB    . VAL C 2 121 ? 120.498 95.516  129.827 1.00 23.19 ?  100 VAL C CB    1 
ATOM   11791 C  CG1   . VAL C 2 121 ? 119.563 95.936  128.679 1.00 24.10 ?  100 VAL C CG1   1 
ATOM   11792 C  CG2   . VAL C 2 121 ? 121.857 96.225  129.702 1.00 23.48 ?  100 VAL C CG2   1 
ATOM   11793 N  N     . HIS C 2 122 ? 118.282 93.964  131.288 1.00 23.45 ?  101 HIS C N     1 
ATOM   11794 C  CA    . HIS C 2 122 ? 116.959 93.337  131.235 1.00 23.81 ?  101 HIS C CA    1 
ATOM   11795 C  C     . HIS C 2 122 ? 116.113 93.614  132.460 1.00 24.33 ?  101 HIS C C     1 
ATOM   11796 O  O     . HIS C 2 122 ? 115.001 94.134  132.331 1.00 24.80 ?  101 HIS C O     1 
ATOM   11797 C  CB    . HIS C 2 122 ? 117.053 91.827  131.033 1.00 23.30 ?  101 HIS C CB    1 
ATOM   11798 C  CG    . HIS C 2 122 ? 117.695 91.425  129.744 1.00 22.96 ?  101 HIS C CG    1 
ATOM   11799 N  ND1   . HIS C 2 122 ? 117.986 90.111  129.440 1.00 22.78 ?  101 HIS C ND1   1 
ATOM   11800 C  CD2   . HIS C 2 122 ? 118.135 92.163  128.698 1.00 23.25 ?  101 HIS C CD2   1 
ATOM   11801 C  CE1   . HIS C 2 122 ? 118.562 90.058  128.254 1.00 22.57 ?  101 HIS C CE1   1 
ATOM   11802 N  NE2   . HIS C 2 122 ? 118.664 91.288  127.782 1.00 21.75 ?  101 HIS C NE2   1 
ATOM   11803 N  N     . ALA C 2 123 ? 116.620 93.238  133.638 1.00 24.40 ?  102 ALA C N     1 
ATOM   11804 C  CA    . ALA C 2 123 ? 115.865 93.417  134.880 1.00 24.00 ?  102 ALA C CA    1 
ATOM   11805 C  C     . ALA C 2 123 ? 115.492 94.888  135.074 1.00 24.05 ?  102 ALA C C     1 
ATOM   11806 O  O     . ALA C 2 123 ? 114.379 95.194  135.494 1.00 23.89 ?  102 ALA C O     1 
ATOM   11807 C  CB    . ALA C 2 123 ? 116.645 92.881  136.080 1.00 23.73 ?  102 ALA C CB    1 
ATOM   11808 N  N     . LYS C 2 124 ? 116.417 95.790  134.746 1.00 24.36 ?  103 LYS C N     1 
ATOM   11809 C  CA    . LYS C 2 124 ? 116.183 97.232  134.883 1.00 24.31 ?  103 LYS C CA    1 
ATOM   11810 C  C     . LYS C 2 124 ? 115.125 97.790  133.923 1.00 23.84 ?  103 LYS C C     1 
ATOM   11811 O  O     . LYS C 2 124 ? 114.327 98.652  134.315 1.00 24.21 ?  103 LYS C O     1 
ATOM   11812 C  CB    . LYS C 2 124 ? 117.486 98.031  134.787 1.00 24.93 ?  103 LYS C CB    1 
ATOM   11813 C  CG    . LYS C 2 124 ? 117.309 99.514  135.147 1.00 26.37 ?  103 LYS C CG    1 
ATOM   11814 C  CD    . LYS C 2 124 ? 118.636 100.250 135.224 1.00 29.42 ?  103 LYS C CD    1 
ATOM   11815 C  CE    . LYS C 2 124 ? 118.413 101.753 135.413 1.00 31.51 ?  103 LYS C CE    1 
ATOM   11816 N  NZ    . LYS C 2 124 ? 117.741 102.378 134.235 1.00 32.37 1  103 LYS C NZ    1 
ATOM   11817 N  N     . SER C 2 125 ? 115.108 97.295  132.684 1.00 23.52 ?  104 SER C N     1 
ATOM   11818 C  CA    . SER C 2 125 ? 114.118 97.708  131.683 0.50 23.23 ?  104 SER C CA    1 
ATOM   11819 C  C     . SER C 2 125 ? 112.684 97.546  132.188 1.00 22.91 ?  104 SER C C     1 
ATOM   11820 O  O     . SER C 2 125 ? 111.813 98.345  131.871 1.00 22.33 ?  104 SER C O     1 
ATOM   11821 C  CB    . SER C 2 125 ? 114.288 96.909  130.385 0.50 23.25 ?  104 SER C CB    1 
ATOM   11822 O  OG    . SER C 2 125 ? 115.574 97.096  129.825 0.50 24.57 ?  104 SER C OG    1 
ATOM   11823 N  N     . TYR C 2 126 ? 112.433 96.494  132.965 1.00 22.72 ?  105 TYR C N     1 
ATOM   11824 C  CA    . TYR C 2 126 ? 111.084 96.278  133.487 1.00 23.34 ?  105 TYR C CA    1 
ATOM   11825 C  C     . TYR C 2 126 ? 110.665 97.389  134.421 1.00 23.32 ?  105 TYR C C     1 
ATOM   11826 O  O     . TYR C 2 126 ? 109.502 97.765  134.425 1.00 23.17 ?  105 TYR C O     1 
ATOM   11827 C  CB    . TYR C 2 126 ? 110.928 94.929  134.192 1.00 23.45 ?  105 TYR C CB    1 
ATOM   11828 C  CG    . TYR C 2 126 ? 111.283 93.738  133.333 1.00 25.16 ?  105 TYR C CG    1 
ATOM   11829 C  CD1   . TYR C 2 126 ? 110.584 93.458  132.162 1.00 26.75 ?  105 TYR C CD1   1 
ATOM   11830 C  CD2   . TYR C 2 126 ? 112.327 92.889  133.701 1.00 26.36 ?  105 TYR C CD2   1 
ATOM   11831 C  CE1   . TYR C 2 126 ? 110.930 92.360  131.365 1.00 28.22 ?  105 TYR C CE1   1 
ATOM   11832 C  CE2   . TYR C 2 126 ? 112.679 91.801  132.918 1.00 27.17 ?  105 TYR C CE2   1 
ATOM   11833 C  CZ    . TYR C 2 126 ? 111.970 91.533  131.762 1.00 29.26 ?  105 TYR C CZ    1 
ATOM   11834 O  OH    . TYR C 2 126 ? 112.313 90.439  130.992 1.00 30.76 ?  105 TYR C OH    1 
ATOM   11835 N  N     . SER C 2 127 ? 111.616 97.905  135.204 1.00 23.61 ?  106 SER C N     1 
ATOM   11836 C  CA    . SER C 2 127 ? 111.352 99.041  136.079 1.00 24.40 ?  106 SER C CA    1 
ATOM   11837 C  C     . SER C 2 127 ? 111.075 100.306 135.278 1.00 24.55 ?  106 SER C C     1 
ATOM   11838 O  O     . SER C 2 127 ? 110.284 101.131 135.707 1.00 24.74 ?  106 SER C O     1 
ATOM   11839 C  CB    . SER C 2 127 ? 112.490 99.277  137.071 1.00 24.54 ?  106 SER C CB    1 
ATOM   11840 O  OG    . SER C 2 127 ? 112.436 98.336  138.138 1.00 24.69 ?  106 SER C OG    1 
ATOM   11841 N  N     . ASN C 2 128 ? 111.731 100.458 134.128 1.00 25.28 ?  107 ASN C N     1 
ATOM   11842 C  CA    . ASN C 2 128 ? 111.448 101.586 133.234 1.00 25.88 ?  107 ASN C CA    1 
ATOM   11843 C  C     . ASN C 2 128 ? 110.005 101.512 132.753 1.00 25.48 ?  107 ASN C C     1 
ATOM   11844 O  O     . ASN C 2 128 ? 109.290 102.512 132.745 1.00 25.23 ?  107 ASN C O     1 
ATOM   11845 C  CB    . ASN C 2 128 ? 112.402 101.615 132.033 1.00 26.40 ?  107 ASN C CB    1 
ATOM   11846 C  CG    . ASN C 2 128 ? 113.788 102.142 132.381 1.00 27.90 ?  107 ASN C CG    1 
ATOM   11847 O  OD1   . ASN C 2 128 ? 114.274 101.972 133.501 1.00 30.62 ?  107 ASN C OD1   1 
ATOM   11848 N  ND2   . ASN C 2 128 ? 114.436 102.774 131.408 1.00 27.91 ?  107 ASN C ND2   1 
ATOM   11849 N  N     . ILE C 2 129 ? 109.581 100.314 132.365 1.00 25.44 ?  108 ILE C N     1 
ATOM   11850 C  CA    . ILE C 2 129 ? 108.192 100.103 131.957 1.00 25.48 ?  108 ILE C CA    1 
ATOM   11851 C  C     . ILE C 2 129 ? 107.236 100.393 133.126 1.00 25.93 ?  108 ILE C C     1 
ATOM   11852 O  O     . ILE C 2 129 ? 106.297 101.180 132.967 1.00 25.54 ?  108 ILE C O     1 
ATOM   11853 C  CB    . ILE C 2 129 ? 107.964 98.706  131.324 1.00 25.21 ?  108 ILE C CB    1 
ATOM   11854 C  CG1   . ILE C 2 129 ? 108.816 98.567  130.051 1.00 25.96 ?  108 ILE C CG1   1 
ATOM   11855 C  CG2   . ILE C 2 129 ? 106.467 98.482  131.020 1.00 24.43 ?  108 ILE C CG2   1 
ATOM   11856 C  CD1   . ILE C 2 129 ? 108.909 97.153  129.478 1.00 26.11 ?  108 ILE C CD1   1 
ATOM   11857 N  N     . PHE C 2 130 ? 107.485 99.785  134.290 1.00 26.04 ?  109 PHE C N     1 
ATOM   11858 C  CA    . PHE C 2 130 ? 106.645 100.012 135.481 1.00 26.66 ?  109 PHE C CA    1 
ATOM   11859 C  C     . PHE C 2 130 ? 106.533 101.495 135.845 1.00 27.38 ?  109 PHE C C     1 
ATOM   11860 O  O     . PHE C 2 130 ? 105.433 101.993 136.137 1.00 27.22 ?  109 PHE C O     1 
ATOM   11861 C  CB    . PHE C 2 130 ? 107.186 99.249  136.710 1.00 26.98 ?  109 PHE C CB    1 
ATOM   11862 C  CG    . PHE C 2 130 ? 107.020 97.751  136.648 1.00 27.46 ?  109 PHE C CG    1 
ATOM   11863 C  CD1   . PHE C 2 130 ? 105.975 97.167  135.941 1.00 28.57 ?  109 PHE C CD1   1 
ATOM   11864 C  CD2   . PHE C 2 130 ? 107.914 96.921  137.325 1.00 28.51 ?  109 PHE C CD2   1 
ATOM   11865 C  CE1   . PHE C 2 130 ? 105.832 95.781  135.893 1.00 29.17 ?  109 PHE C CE1   1 
ATOM   11866 C  CE2   . PHE C 2 130 ? 107.775 95.527  137.290 1.00 29.27 ?  109 PHE C CE2   1 
ATOM   11867 C  CZ    . PHE C 2 130 ? 106.733 94.954  136.578 1.00 28.83 ?  109 PHE C CZ    1 
ATOM   11868 N  N     . MET C 2 131 ? 107.663 102.201 135.829 1.00 27.52 ?  110 MET C N     1 
ATOM   11869 C  CA    . MET C 2 131 ? 107.693 103.604 136.260 1.00 29.07 ?  110 MET C CA    1 
ATOM   11870 C  C     . MET C 2 131 ? 106.940 104.534 135.325 1.00 29.58 ?  110 MET C C     1 
ATOM   11871 O  O     . MET C 2 131 ? 106.456 105.584 135.748 1.00 30.07 ?  110 MET C O     1 
ATOM   11872 C  CB    . MET C 2 131 ? 109.122 104.102 136.457 1.00 28.96 ?  110 MET C CB    1 
ATOM   11873 C  CG    . MET C 2 131 ? 109.724 103.672 137.778 1.00 31.09 ?  110 MET C CG    1 
ATOM   11874 S  SD    . MET C 2 131 ? 111.436 104.208 138.012 1.00 35.43 ?  110 MET C SD    1 
ATOM   11875 C  CE    . MET C 2 131 ? 112.301 103.277 136.751 1.00 33.13 ?  110 MET C CE    1 
ATOM   11876 N  N     . THR C 2 132 ? 106.842 104.137 134.062 1.00 30.25 ?  111 THR C N     1 
ATOM   11877 C  CA    . THR C 2 132 ? 106.072 104.874 133.064 1.00 30.97 ?  111 THR C CA    1 
ATOM   11878 C  C     . THR C 2 132 ? 104.566 104.647 133.231 1.00 31.36 ?  111 THR C C     1 
ATOM   11879 O  O     . THR C 2 132 ? 103.786 105.605 133.323 1.00 31.60 ?  111 THR C O     1 
ATOM   11880 C  CB    . THR C 2 132 ? 106.526 104.474 131.631 1.00 30.88 ?  111 THR C CB    1 
ATOM   11881 O  OG1   . THR C 2 132 ? 107.902 104.829 131.461 1.00 29.86 ?  111 THR C OG1   1 
ATOM   11882 C  CG2   . THR C 2 132 ? 105.693 105.179 130.549 1.00 31.44 ?  111 THR C CG2   1 
ATOM   11883 N  N     . LEU C 2 133 ? 104.167 103.380 133.284 1.00 31.34 ?  112 LEU C N     1 
ATOM   11884 C  CA    . LEU C 2 133 ? 102.753 103.008 133.228 1.00 31.68 ?  112 LEU C CA    1 
ATOM   11885 C  C     . LEU C 2 133 ? 101.993 103.031 134.557 1.00 31.96 ?  112 LEU C C     1 
ATOM   11886 O  O     . LEU C 2 133 ? 100.792 103.297 134.581 1.00 31.69 ?  112 LEU C O     1 
ATOM   11887 C  CB    . LEU C 2 133 ? 102.603 101.630 132.589 1.00 31.35 ?  112 LEU C CB    1 
ATOM   11888 C  CG    . LEU C 2 133 ? 103.266 101.410 131.226 1.00 32.14 ?  112 LEU C CG    1 
ATOM   11889 C  CD1   . LEU C 2 133 ? 103.066 99.974  130.802 1.00 32.15 ?  112 LEU C CD1   1 
ATOM   11890 C  CD2   . LEU C 2 133 ? 102.718 102.375 130.177 1.00 32.39 ?  112 LEU C CD2   1 
ATOM   11891 N  N     . ALA C 2 134 ? 102.687 102.752 135.655 1.00 32.12 ?  113 ALA C N     1 
ATOM   11892 C  CA    . ALA C 2 134 ? 102.018 102.492 136.922 1.00 32.53 ?  113 ALA C CA    1 
ATOM   11893 C  C     . ALA C 2 134 ? 102.401 103.467 138.028 1.00 33.15 ?  113 ALA C C     1 
ATOM   11894 O  O     . ALA C 2 134 ? 103.537 103.933 138.076 1.00 32.47 ?  113 ALA C O     1 
ATOM   11895 C  CB    . ALA C 2 134 ? 102.279 101.048 137.370 1.00 32.20 ?  113 ALA C CB    1 
ATOM   11896 N  N     . PRO C 2 135 ? 101.447 103.762 138.935 1.00 34.27 ?  114 PRO C N     1 
ATOM   11897 C  CA    . PRO C 2 135 ? 101.760 104.553 140.118 1.00 35.35 ?  114 PRO C CA    1 
ATOM   11898 C  C     . PRO C 2 135 ? 102.570 103.729 141.113 1.00 36.17 ?  114 PRO C C     1 
ATOM   11899 O  O     . PRO C 2 135 ? 102.503 102.497 141.096 1.00 35.92 ?  114 PRO C O     1 
ATOM   11900 C  CB    . PRO C 2 135 ? 100.382 104.915 140.685 1.00 35.48 ?  114 PRO C CB    1 
ATOM   11901 C  CG    . PRO C 2 135 ? 99.457  103.882 140.171 1.00 34.94 ?  114 PRO C CG    1 
ATOM   11902 C  CD    . PRO C 2 135 ? 100.030 103.351 138.889 1.00 34.50 ?  114 PRO C CD    1 
ATOM   11903 N  N     . THR C 2 136 ? 103.336 104.412 141.957 1.00 37.30 ?  115 THR C N     1 
ATOM   11904 C  CA    . THR C 2 136 ? 104.258 103.770 142.901 1.00 38.49 ?  115 THR C CA    1 
ATOM   11905 C  C     . THR C 2 136 ? 103.640 102.649 143.750 1.00 38.48 ?  115 THR C C     1 
ATOM   11906 O  O     . THR C 2 136 ? 104.299 101.634 144.000 1.00 38.74 ?  115 THR C O     1 
ATOM   11907 C  CB    . THR C 2 136 ? 104.910 104.818 143.824 1.00 38.95 ?  115 THR C CB    1 
ATOM   11908 O  OG1   . THR C 2 136 ? 105.477 105.856 143.020 1.00 40.08 ?  115 THR C OG1   1 
ATOM   11909 C  CG2   . THR C 2 136 ? 106.009 104.196 144.688 1.00 39.82 ?  115 THR C CG2   1 
ATOM   11910 N  N     . GLU C 2 137 ? 102.392 102.834 144.182 1.00 38.89 ?  116 GLU C N     1 
ATOM   11911 C  CA    . GLU C 2 137 ? 101.713 101.864 145.053 1.00 38.65 ?  116 GLU C CA    1 
ATOM   11912 C  C     . GLU C 2 137 ? 101.455 100.542 144.339 1.00 37.38 ?  116 GLU C C     1 
ATOM   11913 O  O     . GLU C 2 137 ? 101.578 99.475  144.937 1.00 37.22 ?  116 GLU C O     1 
ATOM   11914 C  CB    . GLU C 2 137 ? 100.409 102.430 145.657 1.00 39.52 ?  116 GLU C CB    1 
ATOM   11915 C  CG    . GLU C 2 137 ? 99.228  102.634 144.679 1.00 41.90 ?  116 GLU C CG    1 
ATOM   11916 C  CD    . GLU C 2 137 ? 98.740  104.089 144.581 1.00 46.43 ?  116 GLU C CD    1 
ATOM   11917 O  OE1   . GLU C 2 137 ? 99.429  105.010 145.081 1.00 47.84 ?  116 GLU C OE1   1 
ATOM   11918 O  OE2   . GLU C 2 137 ? 97.651  104.311 143.995 1.00 47.52 -1 116 GLU C OE2   1 
ATOM   11919 N  N     . THR C 2 138 ? 101.109 100.629 143.058 1.00 36.05 ?  117 THR C N     1 
ATOM   11920 C  CA    . THR C 2 138 ? 100.887 99.451  142.233 1.00 34.88 ?  117 THR C CA    1 
ATOM   11921 C  C     . THR C 2 138 ? 102.212 98.740  141.981 1.00 33.58 ?  117 THR C C     1 
ATOM   11922 O  O     . THR C 2 138 ? 102.263 97.507  141.968 1.00 33.61 ?  117 THR C O     1 
ATOM   11923 C  CB    . THR C 2 138 ? 100.212 99.820  140.905 1.00 34.85 ?  117 THR C CB    1 
ATOM   11924 O  OG1   . THR C 2 138 ? 99.045  100.605 141.178 1.00 35.98 ?  117 THR C OG1   1 
ATOM   11925 C  CG2   . THR C 2 138 ? 99.805  98.572  140.135 1.00 34.92 ?  117 THR C CG2   1 
ATOM   11926 N  N     . ILE C 2 139 ? 103.274 99.521  141.787 1.00 32.29 ?  118 ILE C N     1 
ATOM   11927 C  CA    . ILE C 2 139 ? 104.622 98.971  141.645 1.00 31.19 ?  118 ILE C CA    1 
ATOM   11928 C  C     . ILE C 2 139 ? 105.053 98.253  142.937 1.00 30.85 ?  118 ILE C C     1 
ATOM   11929 O  O     . ILE C 2 139 ? 105.506 97.110  142.885 1.00 29.77 ?  118 ILE C O     1 
ATOM   11930 C  CB    . ILE C 2 139 ? 105.668 100.043 141.216 1.00 31.25 ?  118 ILE C CB    1 
ATOM   11931 C  CG1   . ILE C 2 139 ? 105.275 100.703 139.883 1.00 30.12 ?  118 ILE C CG1   1 
ATOM   11932 C  CG2   . ILE C 2 139 ? 107.072 99.428  141.104 1.00 30.21 ?  118 ILE C CG2   1 
ATOM   11933 C  CD1   . ILE C 2 139 ? 106.185 101.876 139.475 1.00 29.41 ?  118 ILE C CD1   1 
ATOM   11934 N  N     . ASN C 2 140 ? 104.890 98.919  144.086 1.00 31.17 ?  119 ASN C N     1 
ATOM   11935 C  CA    . ASN C 2 140 ? 105.205 98.317  145.392 1.00 31.76 ?  119 ASN C CA    1 
ATOM   11936 C  C     . ASN C 2 140 ? 104.445 97.006  145.621 1.00 31.25 ?  119 ASN C C     1 
ATOM   11937 O  O     . ASN C 2 140 ? 105.033 96.012  146.050 1.00 31.47 ?  119 ASN C O     1 
ATOM   11938 C  CB    . ASN C 2 140 ? 104.902 99.281  146.550 1.00 32.65 ?  119 ASN C CB    1 
ATOM   11939 C  CG    . ASN C 2 140 ? 105.879 100.448 146.637 1.00 35.14 ?  119 ASN C CG    1 
ATOM   11940 O  OD1   . ASN C 2 140 ? 107.035 100.361 146.211 1.00 36.75 ?  119 ASN C OD1   1 
ATOM   11941 N  ND2   . ASN C 2 140 ? 105.412 101.554 147.225 1.00 38.05 ?  119 ASN C ND2   1 
ATOM   11942 N  N     . GLU C 2 141 ? 103.149 97.019  145.317 1.00 30.96 ?  120 GLU C N     1 
ATOM   11943 C  CA    . GLU C 2 141 ? 102.279 95.854  145.471 1.00 30.36 ?  120 GLU C CA    1 
ATOM   11944 C  C     . GLU C 2 141 ? 102.720 94.671  144.605 1.00 28.60 ?  120 GLU C C     1 
ATOM   11945 O  O     . GLU C 2 141 ? 102.716 93.535  145.071 1.00 27.94 ?  120 GLU C O     1 
ATOM   11946 C  CB    . GLU C 2 141 ? 100.826 96.216  145.151 1.00 30.86 ?  120 GLU C CB    1 
ATOM   11947 C  CG    . GLU C 2 141 ? 100.105 96.985  146.252 1.00 34.89 ?  120 GLU C CG    1 
ATOM   11948 C  CD    . GLU C 2 141 ? 98.738  97.493  145.812 1.00 39.82 ?  120 GLU C CD    1 
ATOM   11949 O  OE1   . GLU C 2 141 ? 98.224  97.030  144.763 1.00 41.95 ?  120 GLU C OE1   1 
ATOM   11950 O  OE2   . GLU C 2 141 ? 98.171  98.354  146.517 1.00 41.94 -1 120 GLU C OE2   1 
ATOM   11951 N  N     . VAL C 2 142 ? 103.095 94.927  143.354 1.00 27.29 ?  121 VAL C N     1 
ATOM   11952 C  CA    . VAL C 2 142 ? 103.504 93.809  142.477 1.00 25.89 ?  121 VAL C CA    1 
ATOM   11953 C  C     . VAL C 2 142 ? 104.826 93.169  142.916 1.00 25.11 ?  121 VAL C C     1 
ATOM   11954 O  O     . VAL C 2 142 ? 105.007 91.959  142.784 1.00 24.23 ?  121 VAL C O     1 
ATOM   11955 C  CB    . VAL C 2 142 ? 103.475 94.164  140.950 1.00 25.99 ?  121 VAL C CB    1 
ATOM   11956 C  CG1   . VAL C 2 142 ? 104.771 94.829  140.477 1.00 25.21 ?  121 VAL C CG1   1 
ATOM   11957 C  CG2   . VAL C 2 142 ? 103.211 92.915  140.123 1.00 25.78 ?  121 VAL C CG2   1 
ATOM   11958 N  N     . PHE C 2 143 ? 105.744 93.966  143.455 1.00 24.69 ?  122 PHE C N     1 
ATOM   11959 C  CA    . PHE C 2 143 ? 106.993 93.398  143.983 1.00 24.77 ?  122 PHE C CA    1 
ATOM   11960 C  C     . PHE C 2 143 ? 106.754 92.614  145.285 1.00 24.99 ?  122 PHE C C     1 
ATOM   11961 O  O     . PHE C 2 143 ? 107.409 91.603  145.543 1.00 24.73 ?  122 PHE C O     1 
ATOM   11962 C  CB    . PHE C 2 143 ? 108.088 94.464  144.121 1.00 24.83 ?  122 PHE C CB    1 
ATOM   11963 C  CG    . PHE C 2 143 ? 108.747 94.811  142.804 1.00 25.12 ?  122 PHE C CG    1 
ATOM   11964 C  CD1   . PHE C 2 143 ? 109.630 93.923  142.195 1.00 26.58 ?  122 PHE C CD1   1 
ATOM   11965 C  CD2   . PHE C 2 143 ? 108.469 96.011  142.165 1.00 24.49 ?  122 PHE C CD2   1 
ATOM   11966 C  CE1   . PHE C 2 143 ? 110.230 94.234  140.968 1.00 26.96 ?  122 PHE C CE1   1 
ATOM   11967 C  CE2   . PHE C 2 143 ? 109.060 96.331  140.952 1.00 25.79 ?  122 PHE C CE2   1 
ATOM   11968 C  CZ    . PHE C 2 143 ? 109.942 95.442  140.345 1.00 26.45 ?  122 PHE C CZ    1 
ATOM   11969 N  N     . GLU C 2 144 ? 105.796 93.069  146.090 1.00 25.22 ?  123 GLU C N     1 
ATOM   11970 C  CA    . GLU C 2 144 ? 105.351 92.288  147.249 1.00 25.72 ?  123 GLU C CA    1 
ATOM   11971 C  C     . GLU C 2 144 ? 104.700 90.981  146.801 1.00 25.08 ?  123 GLU C C     1 
ATOM   11972 O  O     . GLU C 2 144 ? 104.924 89.929  147.402 1.00 24.67 ?  123 GLU C O     1 
ATOM   11973 C  CB    . GLU C 2 144 ? 104.406 93.102  148.129 1.00 26.23 ?  123 GLU C CB    1 
ATOM   11974 C  CG    . GLU C 2 144 ? 105.123 94.203  148.893 1.00 29.96 ?  123 GLU C CG    1 
ATOM   11975 C  CD    . GLU C 2 144 ? 106.305 93.674  149.688 1.00 33.82 ?  123 GLU C CD    1 
ATOM   11976 O  OE1   . GLU C 2 144 ? 106.078 92.891  150.635 1.00 36.54 ?  123 GLU C OE1   1 
ATOM   11977 O  OE2   . GLU C 2 144 ? 107.459 94.024  149.358 1.00 35.84 -1 123 GLU C OE2   1 
ATOM   11978 N  N     . TRP C 2 145 ? 103.921 91.053  145.724 1.00 24.21 ?  124 TRP C N     1 
ATOM   11979 C  CA    . TRP C 2 145 ? 103.277 89.875  145.146 1.00 23.99 ?  124 TRP C CA    1 
ATOM   11980 C  C     . TRP C 2 145 ? 104.270 88.812  144.653 1.00 23.95 ?  124 TRP C C     1 
ATOM   11981 O  O     . TRP C 2 145 ? 104.012 87.605  144.818 1.00 23.31 ?  124 TRP C O     1 
ATOM   11982 C  CB    . TRP C 2 145 ? 102.311 90.280  144.022 1.00 24.13 ?  124 TRP C CB    1 
ATOM   11983 C  CG    . TRP C 2 145 ? 101.835 89.114  143.185 1.00 24.37 ?  124 TRP C CG    1 
ATOM   11984 C  CD1   . TRP C 2 145 ? 100.740 88.316  143.417 1.00 24.76 ?  124 TRP C CD1   1 
ATOM   11985 C  CD2   . TRP C 2 145 ? 102.442 88.625  141.982 1.00 23.31 ?  124 TRP C CD2   1 
ATOM   11986 N  NE1   . TRP C 2 145 ? 100.641 87.355  142.428 1.00 24.97 ?  124 TRP C NE1   1 
ATOM   11987 C  CE2   . TRP C 2 145 ? 101.669 87.524  141.537 1.00 24.20 ?  124 TRP C CE2   1 
ATOM   11988 C  CE3   . TRP C 2 145 ? 103.571 89.001  141.242 1.00 23.76 ?  124 TRP C CE3   1 
ATOM   11989 C  CZ2   . TRP C 2 145 ? 101.989 86.801  140.380 1.00 23.41 ?  124 TRP C CZ2   1 
ATOM   11990 C  CZ3   . TRP C 2 145 ? 103.893 88.280  140.093 1.00 23.29 ?  124 TRP C CZ3   1 
ATOM   11991 C  CH2   . TRP C 2 145 ? 103.096 87.195  139.672 1.00 22.93 ?  124 TRP C CH2   1 
ATOM   11992 N  N     . VAL C 2 146 ? 105.389 89.222  144.048 1.00 23.35 ?  125 VAL C N     1 
ATOM   11993 C  CA    . VAL C 2 146 ? 106.394 88.198  143.661 1.00 23.53 ?  125 VAL C CA    1 
ATOM   11994 C  C     . VAL C 2 146 ? 106.936 87.426  144.871 1.00 23.73 ?  125 VAL C C     1 
ATOM   11995 O  O     . VAL C 2 146 ? 107.085 86.216  144.798 1.00 23.03 ?  125 VAL C O     1 
ATOM   11996 C  CB    . VAL C 2 146 ? 107.522 88.656  142.622 1.00 23.63 ?  125 VAL C CB    1 
ATOM   11997 C  CG1   . VAL C 2 146 ? 107.333 90.051  142.089 1.00 24.40 ?  125 VAL C CG1   1 
ATOM   11998 C  CG2   . VAL C 2 146 ? 108.962 88.400  143.106 1.00 22.97 ?  125 VAL C CG2   1 
ATOM   11999 N  N     . LYS C 2 147 ? 107.168 88.125  145.986 1.00 24.06 ?  126 LYS C N     1 
ATOM   12000 C  CA    . LYS C 2 147 ? 107.716 87.491  147.197 1.00 25.41 ?  126 LYS C CA    1 
ATOM   12001 C  C     . LYS C 2 147 ? 106.817 86.394  147.773 1.00 25.82 ?  126 LYS C C     1 
ATOM   12002 O  O     . LYS C 2 147 ? 107.318 85.421  148.340 1.00 26.08 ?  126 LYS C O     1 
ATOM   12003 C  CB    . LYS C 2 147 ? 107.981 88.532  148.287 1.00 25.49 ?  126 LYS C CB    1 
ATOM   12004 C  CG    . LYS C 2 147 ? 109.102 89.507  147.990 1.00 27.52 ?  126 LYS C CG    1 
ATOM   12005 C  CD    . LYS C 2 147 ? 109.188 90.529  149.117 1.00 30.43 ?  126 LYS C CD    1 
ATOM   12006 C  CE    . LYS C 2 147 ? 110.037 91.722  148.730 1.00 33.10 ?  126 LYS C CE    1 
ATOM   12007 N  NZ    . LYS C 2 147 ? 109.999 92.750  149.806 1.00 34.86 1  126 LYS C NZ    1 
ATOM   12008 N  N     . GLN C 2 148 ? 105.502 86.556  147.627 1.00 26.45 ?  127 GLN C N     1 
ATOM   12009 C  CA    . GLN C 2 148 ? 104.534 85.645  148.244 1.00 26.85 ?  127 GLN C CA    1 
ATOM   12010 C  C     . GLN C 2 148 ? 103.879 84.660  147.274 1.00 26.01 ?  127 GLN C C     1 
ATOM   12011 O  O     . GLN C 2 148 ? 103.132 83.779  147.706 1.00 26.12 ?  127 GLN C O     1 
ATOM   12012 C  CB    . GLN C 2 148 ? 103.460 86.426  149.025 1.00 28.08 ?  127 GLN C CB    1 
ATOM   12013 C  CG    . GLN C 2 148 ? 102.584 87.359  148.184 1.00 30.69 ?  127 GLN C CG    1 
ATOM   12014 C  CD    . GLN C 2 148 ? 101.535 86.620  147.356 1.00 34.64 ?  127 GLN C CD    1 
ATOM   12015 O  OE1   . GLN C 2 148 ? 101.582 86.628  146.113 1.00 33.80 ?  127 GLN C OE1   1 
ATOM   12016 N  NE2   . GLN C 2 148 ? 100.588 85.966  148.040 1.00 36.24 ?  127 GLN C NE2   1 
ATOM   12017 N  N     . ASN C 2 149 ? 104.146 84.809  145.974 1.00 24.97 ?  128 ASN C N     1 
ATOM   12018 C  CA    . ASN C 2 149 ? 103.576 83.916  144.969 1.00 24.03 ?  128 ASN C CA    1 
ATOM   12019 C  C     . ASN C 2 149 ? 104.284 82.571  144.982 1.00 24.13 ?  128 ASN C C     1 
ATOM   12020 O  O     . ASN C 2 149 ? 105.494 82.518  144.744 1.00 22.93 ?  128 ASN C O     1 
ATOM   12021 C  CB    . ASN C 2 149 ? 103.702 84.525  143.581 1.00 23.97 ?  128 ASN C CB    1 
ATOM   12022 C  CG    . ASN C 2 149 ? 103.002 83.699  142.529 1.00 23.94 ?  128 ASN C CG    1 
ATOM   12023 O  OD1   . ASN C 2 149 ? 103.592 82.796  141.938 1.00 24.85 ?  128 ASN C OD1   1 
ATOM   12024 N  ND2   . ASN C 2 149 ? 101.721 83.970  142.321 1.00 24.76 ?  128 ASN C ND2   1 
ATOM   12025 N  N     . LYS C 2 150 ? 103.535 81.492  145.227 1.00 24.32 ?  129 LYS C N     1 
ATOM   12026 C  CA    . LYS C 2 150 ? 104.151 80.172  145.463 1.00 24.77 ?  129 LYS C CA    1 
ATOM   12027 C  C     . LYS C 2 150 ? 104.814 79.528  144.243 1.00 24.54 ?  129 LYS C C     1 
ATOM   12028 O  O     . LYS C 2 150 ? 105.805 78.809  144.387 1.00 24.17 ?  129 LYS C O     1 
ATOM   12029 C  CB    . LYS C 2 150 ? 103.175 79.202  146.141 1.00 25.27 ?  129 LYS C CB    1 
ATOM   12030 C  CG    . LYS C 2 150 ? 101.929 78.861  145.350 1.00 28.72 ?  129 LYS C CG    1 
ATOM   12031 C  CD    . LYS C 2 150 ? 101.238 77.646  145.972 1.00 33.40 ?  129 LYS C CD    1 
ATOM   12032 C  CE    . LYS C 2 150 ? 99.775  77.582  145.580 1.00 36.77 ?  129 LYS C CE    1 
ATOM   12033 N  NZ    . LYS C 2 150 ? 99.074  76.520  146.367 1.00 39.66 1  129 LYS C NZ    1 
ATOM   12034 N  N     . TYR C 2 151 ? 104.266 79.782  143.050 1.00 23.92 ?  130 TYR C N     1 
ATOM   12035 C  CA    . TYR C 2 151 ? 104.831 79.236  141.809 1.00 24.12 ?  130 TYR C CA    1 
ATOM   12036 C  C     . TYR C 2 151 ? 106.130 79.921  141.416 1.00 23.54 ?  130 TYR C C     1 
ATOM   12037 O  O     . TYR C 2 151 ? 107.075 79.270  140.946 1.00 23.32 ?  130 TYR C O     1 
ATOM   12038 C  CB    . TYR C 2 151 ? 103.797 79.312  140.669 1.00 24.53 ?  130 TYR C CB    1 
ATOM   12039 C  CG    . TYR C 2 151 ? 102.420 78.869  141.113 1.00 25.83 ?  130 TYR C CG    1 
ATOM   12040 C  CD1   . TYR C 2 151 ? 102.192 77.553  141.520 1.00 26.57 ?  130 TYR C CD1   1 
ATOM   12041 C  CD2   . TYR C 2 151 ? 101.356 79.776  141.171 1.00 27.87 ?  130 TYR C CD2   1 
ATOM   12042 C  CE1   . TYR C 2 151 ? 100.936 77.139  141.951 1.00 29.65 ?  130 TYR C CE1   1 
ATOM   12043 C  CE2   . TYR C 2 151 ? 100.089 79.370  141.607 1.00 29.91 ?  130 TYR C CE2   1 
ATOM   12044 C  CZ    . TYR C 2 151 ? 99.892  78.053  141.995 1.00 31.19 ?  130 TYR C CZ    1 
ATOM   12045 O  OH    . TYR C 2 151 ? 98.649  77.634  142.427 1.00 34.44 ?  130 TYR C OH    1 
ATOM   12046 N  N     . LEU C 2 152 ? 106.173 81.234  141.610 1.00 23.38 ?  131 LEU C N     1 
ATOM   12047 C  CA    . LEU C 2 152 ? 107.360 82.018  141.321 1.00 23.43 ?  131 LEU C CA    1 
ATOM   12048 C  C     . LEU C 2 152 ? 108.465 81.683  142.328 1.00 23.37 ?  131 LEU C C     1 
ATOM   12049 O  O     . LEU C 2 152 ? 109.629 81.528  141.944 1.00 23.05 ?  131 LEU C O     1 
ATOM   12050 C  CB    . LEU C 2 152 ? 107.000 83.503  141.360 1.00 23.73 ?  131 LEU C CB    1 
ATOM   12051 C  CG    . LEU C 2 152 ? 107.434 84.533  140.324 1.00 24.71 ?  131 LEU C CG    1 
ATOM   12052 C  CD1   . LEU C 2 152 ? 107.885 83.956  138.972 1.00 21.63 ?  131 LEU C CD1   1 
ATOM   12053 C  CD2   . LEU C 2 152 ? 106.310 85.524  140.131 1.00 26.87 ?  131 LEU C CD2   1 
ATOM   12054 N  N     . GLN C 2 153 ? 108.111 81.568  143.611 1.00 22.80 ?  132 GLN C N     1 
ATOM   12055 C  CA    . GLN C 2 153 ? 109.087 81.104  144.610 1.00 22.70 ?  132 GLN C CA    1 
ATOM   12056 C  C     . GLN C 2 153 ? 109.598 79.686  144.341 1.00 22.54 ?  132 GLN C C     1 
ATOM   12057 O  O     . GLN C 2 153 ? 110.809 79.436  144.439 1.00 21.73 ?  132 GLN C O     1 
ATOM   12058 C  CB    . GLN C 2 153 ? 108.563 81.250  146.041 1.00 23.07 ?  132 GLN C CB    1 
ATOM   12059 C  CG    . GLN C 2 153 ? 108.324 82.707  146.438 1.00 21.83 ?  132 GLN C CG    1 
ATOM   12060 C  CD    . GLN C 2 153 ? 109.575 83.581  146.328 1.00 22.34 ?  132 GLN C CD    1 
ATOM   12061 O  OE1   . GLN C 2 153 ? 110.653 83.213  146.800 1.00 24.07 ?  132 GLN C OE1   1 
ATOM   12062 N  NE2   . GLN C 2 153 ? 109.428 84.748  145.715 1.00 22.26 ?  132 GLN C NE2   1 
ATOM   12063 N  N     . LYS C 2 154 ? 108.693 78.767  143.992 1.00 22.53 ?  133 LYS C N     1 
ATOM   12064 C  CA    . LYS C 2 154 ? 109.113 77.406  143.660 1.00 22.84 ?  133 LYS C CA    1 
ATOM   12065 C  C     . LYS C 2 154 ? 110.092 77.374  142.485 1.00 22.42 ?  133 LYS C C     1 
ATOM   12066 O  O     . LYS C 2 154 ? 111.105 76.688  142.561 1.00 21.90 ?  133 LYS C O     1 
ATOM   12067 C  CB    . LYS C 2 154 ? 107.920 76.451  143.421 1.00 22.96 ?  133 LYS C CB    1 
ATOM   12068 C  CG    . LYS C 2 154 ? 108.332 74.979  143.108 1.00 23.45 ?  133 LYS C CG    1 
ATOM   12069 C  CD    . LYS C 2 154 ? 109.048 74.278  144.283 1.00 26.74 ?  133 LYS C CD    1 
ATOM   12070 C  CE    . LYS C 2 154 ? 109.393 72.821  143.944 1.00 27.93 ?  133 LYS C CE    1 
ATOM   12071 N  NZ    . LYS C 2 154 ? 110.261 72.166  144.959 1.00 27.86 1  133 LYS C NZ    1 
ATOM   12072 N  N     . LYS C 2 155 ? 109.814 78.123  141.413 1.00 22.77 ?  134 LYS C N     1 
ATOM   12073 C  CA    . LYS C 2 155 ? 110.684 78.048  140.235 1.00 22.87 ?  134 LYS C CA    1 
ATOM   12074 C  C     . LYS C 2 155 ? 112.057 78.655  140.508 1.00 22.30 ?  134 LYS C C     1 
ATOM   12075 O  O     . LYS C 2 155 ? 113.078 78.079  140.098 1.00 21.89 ?  134 LYS C O     1 
ATOM   12076 C  CB    . LYS C 2 155 ? 110.019 78.585  138.947 1.00 23.33 ?  134 LYS C CB    1 
ATOM   12077 C  CG    . LYS C 2 155 ? 109.912 80.081  138.793 1.00 24.25 ?  134 LYS C CG    1 
ATOM   12078 C  CD    . LYS C 2 155 ? 109.244 80.457  137.460 1.00 26.87 ?  134 LYS C CD    1 
ATOM   12079 C  CE    . LYS C 2 155 ? 107.723 80.448  137.580 1.00 28.26 ?  134 LYS C CE    1 
ATOM   12080 N  NZ    . LYS C 2 155 ? 107.104 81.114  136.394 1.00 28.97 1  134 LYS C NZ    1 
ATOM   12081 N  N     . ALA C 2 156 ? 112.078 79.774  141.233 1.00 21.96 ?  135 ALA C N     1 
ATOM   12082 C  CA    . ALA C 2 156 ? 113.337 80.361  141.731 1.00 22.43 ?  135 ALA C CA    1 
ATOM   12083 C  C     . ALA C 2 156 ? 114.109 79.414  142.651 1.00 22.02 ?  135 ALA C C     1 
ATOM   12084 O  O     . ALA C 2 156 ? 115.325 79.292  142.527 1.00 22.60 ?  135 ALA C O     1 
ATOM   12085 C  CB    . ALA C 2 156 ? 113.083 81.700  142.456 1.00 22.05 ?  135 ALA C CB    1 
ATOM   12086 N  N     . GLN C 2 157 ? 113.411 78.765  143.584 1.00 21.97 ?  136 GLN C N     1 
ATOM   12087 C  CA    . GLN C 2 157 ? 114.050 77.804  144.493 1.00 22.10 ?  136 GLN C CA    1 
ATOM   12088 C  C     . GLN C 2 157 ? 114.754 76.707  143.721 1.00 21.87 ?  136 GLN C C     1 
ATOM   12089 O  O     . GLN C 2 157 ? 115.882 76.344  144.050 1.00 21.75 ?  136 GLN C O     1 
ATOM   12090 C  CB    . GLN C 2 157 ? 113.031 77.141  145.419 1.00 22.50 ?  136 GLN C CB    1 
ATOM   12091 C  CG    . GLN C 2 157 ? 112.610 77.976  146.619 1.00 23.55 ?  136 GLN C CG    1 
ATOM   12092 C  CD    . GLN C 2 157 ? 111.314 77.453  147.212 1.00 26.93 ?  136 GLN C CD    1 
ATOM   12093 O  OE1   . GLN C 2 157 ? 110.978 76.284  147.036 1.00 26.36 ?  136 GLN C OE1   1 
ATOM   12094 N  NE2   . GLN C 2 157 ? 110.569 78.320  147.889 1.00 28.09 ?  136 GLN C NE2   1 
ATOM   12095 N  N     . MET C 2 158 ? 114.068 76.177  142.710 1.00 21.38 ?  137 MET C N     1 
ATOM   12096 C  CA    . MET C 2 158 ? 114.572 75.055  141.933 1.00 22.08 ?  137 MET C CA    1 
ATOM   12097 C  C     . MET C 2 158 ? 115.763 75.442  141.063 1.00 21.70 ?  137 MET C C     1 
ATOM   12098 O  O     . MET C 2 158 ? 116.751 74.710  140.976 1.00 21.83 ?  137 MET C O     1 
ATOM   12099 C  CB    . MET C 2 158 ? 113.473 74.494  141.037 1.00 22.05 ?  137 MET C CB    1 
ATOM   12100 C  CG    . MET C 2 158 ? 112.415 73.664  141.774 1.00 23.93 ?  137 MET C CG    1 
ATOM   12101 S  SD    . MET C 2 158 ? 111.063 73.251  140.652 1.00 27.75 ?  137 MET C SD    1 
ATOM   12102 C  CE    . MET C 2 158 ? 111.913 72.094  139.567 1.00 26.00 ?  137 MET C CE    1 
ATOM   12103 N  N     . ILE C 2 159 ? 115.647 76.577  140.389 1.00 20.90 ?  138 ILE C N     1 
ATOM   12104 C  CA    . ILE C 2 159 ? 116.687 76.995  139.464 1.00 20.60 ?  138 ILE C CA    1 
ATOM   12105 C  C     . ILE C 2 159 ? 117.936 77.436  140.234 1.00 20.36 ?  138 ILE C C     1 
ATOM   12106 O  O     . ILE C 2 159 ? 119.038 76.971  139.937 1.00 19.65 ?  138 ILE C O     1 
ATOM   12107 C  CB    . ILE C 2 159 ? 116.179 78.095  138.486 1.00 20.17 ?  138 ILE C CB    1 
ATOM   12108 C  CG1   . ILE C 2 159 ? 115.100 77.530  137.544 1.00 20.66 ?  138 ILE C CG1   1 
ATOM   12109 C  CG2   . ILE C 2 159 ? 117.352 78.762  137.746 1.00 20.62 ?  138 ILE C CG2   1 
ATOM   12110 C  CD1   . ILE C 2 159 ? 115.535 76.433  136.568 1.00 22.17 ?  138 ILE C CD1   1 
ATOM   12111 N  N     . VAL C 2 160 ? 117.754 78.303  141.230 1.00 19.58 ?  139 VAL C N     1 
ATOM   12112 C  CA    . VAL C 2 160 ? 118.873 78.834  142.015 1.00 19.88 ?  139 VAL C CA    1 
ATOM   12113 C  C     . VAL C 2 160 ? 119.526 77.724  142.843 1.00 19.44 ?  139 VAL C C     1 
ATOM   12114 O  O     . VAL C 2 160 ? 120.727 77.750  143.088 1.00 19.88 ?  139 VAL C O     1 
ATOM   12115 C  CB    . VAL C 2 160 ? 118.448 80.026  142.946 1.00 19.52 ?  139 VAL C CB    1 
ATOM   12116 C  CG1   . VAL C 2 160 ? 119.627 80.493  143.819 1.00 20.75 ?  139 VAL C CG1   1 
ATOM   12117 C  CG2   . VAL C 2 160 ? 117.945 81.204  142.121 1.00 20.03 ?  139 VAL C CG2   1 
ATOM   12118 N  N     . GLY C 2 161 ? 118.734 76.744  143.266 1.00 19.13 ?  140 GLY C N     1 
ATOM   12119 C  CA    . GLY C 2 161 ? 119.278 75.627  144.021 1.00 18.05 ?  140 GLY C CA    1 
ATOM   12120 C  C     . GLY C 2 161 ? 120.304 74.886  143.202 1.00 17.86 ?  140 GLY C C     1 
ATOM   12121 O  O     . GLY C 2 161 ? 121.385 74.543  143.692 1.00 17.47 ?  140 GLY C O     1 
ATOM   12122 N  N     . LEU C 2 162 ? 119.959 74.625  141.945 1.00 17.92 ?  141 LEU C N     1 
ATOM   12123 C  CA    . LEU C 2 162 ? 120.884 73.967  141.029 1.00 18.32 ?  141 LEU C CA    1 
ATOM   12124 C  C     . LEU C 2 162 ? 122.150 74.806  140.750 1.00 18.55 ?  141 LEU C C     1 
ATOM   12125 O  O     . LEU C 2 162 ? 123.254 74.262  140.721 1.00 18.49 ?  141 LEU C O     1 
ATOM   12126 C  CB    . LEU C 2 162 ? 120.158 73.596  139.729 1.00 18.50 ?  141 LEU C CB    1 
ATOM   12127 C  CG    . LEU C 2 162 ? 119.142 72.462  139.888 1.00 19.32 ?  141 LEU C CG    1 
ATOM   12128 C  CD1   . LEU C 2 162 ? 118.203 72.413  138.688 1.00 20.38 ?  141 LEU C CD1   1 
ATOM   12129 C  CD2   . LEU C 2 162 ? 119.845 71.118  140.097 1.00 19.94 ?  141 LEU C CD2   1 
ATOM   12130 N  N     . TYR C 2 163 ? 122.002 76.117  140.580 1.00 19.16 ?  142 TYR C N     1 
ATOM   12131 C  CA    . TYR C 2 163 ? 123.174 77.006  140.443 1.00 20.16 ?  142 TYR C CA    1 
ATOM   12132 C  C     . TYR C 2 163 ? 124.109 76.908  141.635 1.00 20.78 ?  142 TYR C C     1 
ATOM   12133 O  O     . TYR C 2 163 ? 125.333 76.857  141.483 1.00 20.36 ?  142 TYR C O     1 
ATOM   12134 C  CB    . TYR C 2 163 ? 122.759 78.479  140.284 1.00 20.34 ?  142 TYR C CB    1 
ATOM   12135 C  CG    . TYR C 2 163 ? 121.992 78.802  139.009 1.00 22.46 ?  142 TYR C CG    1 
ATOM   12136 C  CD1   . TYR C 2 163 ? 122.107 78.006  137.874 1.00 23.88 ?  142 TYR C CD1   1 
ATOM   12137 C  CD2   . TYR C 2 163 ? 121.161 79.914  138.945 1.00 22.41 ?  142 TYR C CD2   1 
ATOM   12138 C  CE1   . TYR C 2 163 ? 121.393 78.311  136.700 1.00 25.93 ?  142 TYR C CE1   1 
ATOM   12139 C  CE2   . TYR C 2 163 ? 120.455 80.225  137.786 1.00 22.07 ?  142 TYR C CE2   1 
ATOM   12140 C  CZ    . TYR C 2 163 ? 120.581 79.431  136.672 1.00 25.19 ?  142 TYR C CZ    1 
ATOM   12141 O  OH    . TYR C 2 163 ? 119.867 79.762  135.537 1.00 27.43 ?  142 TYR C OH    1 
ATOM   12142 N  N     . LYS C 2 164 ? 123.529 76.878  142.829 1.00 21.39 ?  143 LYS C N     1 
ATOM   12143 C  CA    . LYS C 2 164 ? 124.344 76.901  144.033 1.00 22.49 ?  143 LYS C CA    1 
ATOM   12144 C  C     . LYS C 2 164 ? 124.888 75.524  144.404 1.00 22.49 ?  143 LYS C C     1 
ATOM   12145 O  O     . LYS C 2 164 ? 125.771 75.418  145.249 1.00 22.45 ?  143 LYS C O     1 
ATOM   12146 C  CB    . LYS C 2 164 ? 123.607 77.588  145.180 1.00 23.16 ?  143 LYS C CB    1 
ATOM   12147 C  CG    . LYS C 2 164 ? 123.423 79.080  144.910 1.00 26.08 ?  143 LYS C CG    1 
ATOM   12148 C  CD    . LYS C 2 164 ? 123.208 79.867  146.170 1.00 30.38 ?  143 LYS C CD    1 
ATOM   12149 C  CE    . LYS C 2 164 ? 123.222 81.349  145.885 1.00 32.69 ?  143 LYS C CE    1 
ATOM   12150 N  NZ    . LYS C 2 164 ? 122.959 82.117  147.134 1.00 35.60 1  143 LYS C NZ    1 
ATOM   12151 N  N     . ALA C 2 165 ? 124.415 74.487  143.712 1.00 22.02 ?  144 ALA C N     1 
ATOM   12152 C  CA    . ALA C 2 165 ? 124.925 73.145  143.922 1.00 22.69 ?  144 ALA C CA    1 
ATOM   12153 C  C     . ALA C 2 165 ? 126.171 72.833  143.075 1.00 23.20 ?  144 ALA C C     1 
ATOM   12154 O  O     . ALA C 2 165 ? 126.790 71.792  143.255 1.00 23.80 ?  144 ALA C O     1 
ATOM   12155 C  CB    . ALA C 2 165 ? 123.811 72.096  143.683 1.00 21.79 ?  144 ALA C CB    1 
ATOM   12156 N  N     . ILE C 2 166 ? 126.546 73.725  142.155 1.00 23.97 ?  145 ILE C N     1 
ATOM   12157 C  CA    . ILE C 2 166 ? 127.739 73.495  141.332 1.00 24.29 ?  145 ILE C CA    1 
ATOM   12158 C  C     . ILE C 2 166 ? 128.973 73.319  142.221 1.00 25.49 ?  145 ILE C C     1 
ATOM   12159 O  O     . ILE C 2 166 ? 129.197 74.096  143.143 1.00 25.82 ?  145 ILE C O     1 
ATOM   12160 C  CB    . ILE C 2 166 ? 127.997 74.633  140.303 1.00 24.22 ?  145 ILE C CB    1 
ATOM   12161 C  CG1   . ILE C 2 166 ? 126.825 74.778  139.337 1.00 23.45 ?  145 ILE C CG1   1 
ATOM   12162 C  CG2   . ILE C 2 166 ? 129.281 74.366  139.516 1.00 23.42 ?  145 ILE C CG2   1 
ATOM   12163 C  CD1   . ILE C 2 166 ? 126.867 76.081  138.499 1.00 21.99 ?  145 ILE C CD1   1 
ATOM   12164 N  N     . GLN C 2 167 ? 129.733 72.263  141.963 1.00 26.83 ?  146 GLN C N     1 
ATOM   12165 C  CA    . GLN C 2 167 ? 130.960 72.001  142.701 1.00 28.85 ?  146 GLN C CA    1 
ATOM   12166 C  C     . GLN C 2 167 ? 132.130 72.221  141.762 1.00 29.77 ?  146 GLN C C     1 
ATOM   12167 O  O     . GLN C 2 167 ? 132.087 71.808  140.599 1.00 29.74 ?  146 GLN C O     1 
ATOM   12168 C  CB    . GLN C 2 167 ? 130.986 70.568  143.255 1.00 28.99 ?  146 GLN C CB    1 
ATOM   12169 C  CG    . GLN C 2 167 ? 130.027 70.316  144.419 1.00 30.30 ?  146 GLN C CG    1 
ATOM   12170 C  CD    . GLN C 2 167 ? 130.457 71.010  145.706 1.00 33.32 ?  146 GLN C CD    1 
ATOM   12171 O  OE1   . GLN C 2 167 ? 131.569 71.531  145.801 1.00 34.63 ?  146 GLN C OE1   1 
ATOM   12172 N  NE2   . GLN C 2 167 ? 129.583 70.997  146.709 1.00 32.32 ?  146 GLN C NE2   1 
ATOM   12173 N  N     . LYS C 2 168 ? 133.169 72.876  142.267 1.00 31.29 ?  147 LYS C N     1 
ATOM   12174 C  CA    . LYS C 2 168 ? 134.371 73.143  141.477 1.00 33.14 ?  147 LYS C CA    1 
ATOM   12175 C  C     . LYS C 2 168 ? 134.897 71.836  140.899 1.00 33.79 ?  147 LYS C C     1 
ATOM   12176 O  O     . LYS C 2 168 ? 134.857 70.791  141.558 1.00 34.06 ?  147 LYS C O     1 
ATOM   12177 C  CB    . LYS C 2 168 ? 135.429 73.833  142.333 1.00 33.44 ?  147 LYS C CB    1 
ATOM   12178 C  CG    . LYS C 2 168 ? 136.496 74.607  141.561 1.00 35.61 ?  147 LYS C CG    1 
ATOM   12179 C  CD    . LYS C 2 168 ? 137.452 75.280  142.540 1.00 38.40 ?  147 LYS C CD    1 
ATOM   12180 C  CE    . LYS C 2 168 ? 138.364 76.292  141.867 1.00 40.48 ?  147 LYS C CE    1 
ATOM   12181 N  NZ    . LYS C 2 168 ? 139.687 75.688  141.559 1.00 41.56 1  147 LYS C NZ    1 
ATOM   12182 N  N     . ASP C 2 169 ? 135.342 71.897  139.648 1.00 35.10 ?  148 ASP C N     1 
ATOM   12183 C  CA    . ASP C 2 169 ? 135.890 70.732  138.933 1.00 36.27 ?  148 ASP C CA    1 
ATOM   12184 C  C     . ASP C 2 169 ? 134.943 69.537  138.814 1.00 36.29 ?  148 ASP C C     1 
ATOM   12185 O  O     . ASP C 2 169 ? 135.375 68.424  138.507 1.00 36.95 ?  148 ASP C O     1 
ATOM   12186 C  CB    . ASP C 2 169 ? 137.207 70.282  139.574 1.00 37.15 ?  148 ASP C CB    1 
ATOM   12187 C  CG    . ASP C 2 169 ? 138.328 71.259  139.346 1.00 38.94 ?  148 ASP C CG    1 
ATOM   12188 O  OD1   . ASP C 2 169 ? 138.247 72.058  138.384 1.00 41.71 ?  148 ASP C OD1   1 
ATOM   12189 O  OD2   . ASP C 2 169 ? 139.295 71.227  140.134 1.00 41.64 -1 148 ASP C OD2   1 
ATOM   12190 N  N     . ASP C 2 170 ? 133.657 69.757  139.060 1.00 35.87 ?  149 ASP C N     1 
ATOM   12191 C  CA    . ASP C 2 170 ? 132.675 68.689  138.924 1.00 35.24 ?  149 ASP C CA    1 
ATOM   12192 C  C     . ASP C 2 170 ? 131.744 69.059  137.777 1.00 34.12 ?  149 ASP C C     1 
ATOM   12193 O  O     . ASP C 2 170 ? 130.828 69.892  137.925 1.00 33.52 ?  149 ASP C O     1 
ATOM   12194 C  CB    . ASP C 2 170 ? 131.932 68.456  140.244 1.00 36.09 ?  149 ASP C CB    1 
ATOM   12195 C  CG    . ASP C 2 170 ? 130.761 67.482  140.112 1.00 38.39 ?  149 ASP C CG    1 
ATOM   12196 O  OD1   . ASP C 2 170 ? 130.653 66.752  139.098 1.00 42.06 ?  149 ASP C OD1   1 
ATOM   12197 O  OD2   . ASP C 2 170 ? 129.939 67.439  141.048 1.00 42.21 -1 149 ASP C OD2   1 
ATOM   12198 N  N     . GLU C 2 171 ? 132.013 68.440  136.632 1.00 32.48 ?  150 GLU C N     1 
ATOM   12199 C  CA    . GLU C 2 171 ? 131.346 68.773  135.385 1.00 30.93 ?  150 GLU C CA    1 
ATOM   12200 C  C     . GLU C 2 171 ? 129.865 68.383  135.382 1.00 29.37 ?  150 GLU C C     1 
ATOM   12201 O  O     . GLU C 2 171 ? 129.063 69.012  134.693 1.00 28.99 ?  150 GLU C O     1 
ATOM   12202 C  CB    . GLU C 2 171 ? 132.099 68.169  134.184 1.00 31.30 ?  150 GLU C CB    1 
ATOM   12203 C  CG    . GLU C 2 171 ? 132.011 66.634  134.014 1.00 33.64 ?  150 GLU C CG    1 
ATOM   12204 C  CD    . GLU C 2 171 ? 133.019 66.056  132.991 1.00 36.40 ?  150 GLU C CD    1 
ATOM   12205 O  OE1   . GLU C 2 171 ? 133.778 66.830  132.366 1.00 38.62 ?  150 GLU C OE1   1 
ATOM   12206 O  OE2   . GLU C 2 171 ? 133.055 64.818  132.811 1.00 37.42 -1 150 GLU C OE2   1 
ATOM   12207 N  N     . ILE C 2 172 ? 129.509 67.350  136.147 1.00 27.68 ?  151 ILE C N     1 
ATOM   12208 C  CA    . ILE C 2 172 ? 128.116 66.899  136.207 1.00 26.26 ?  151 ILE C CA    1 
ATOM   12209 C  C     . ILE C 2 172 ? 127.231 67.926  136.917 1.00 24.85 ?  151 ILE C C     1 
ATOM   12210 O  O     . ILE C 2 172 ? 126.142 68.227  136.433 1.00 23.53 ?  151 ILE C O     1 
ATOM   12211 C  CB    . ILE C 2 172 ? 127.974 65.487  136.839 1.00 26.53 ?  151 ILE C CB    1 
ATOM   12212 C  CG1   . ILE C 2 172 ? 128.731 64.440  136.007 1.00 27.59 ?  151 ILE C CG1   1 
ATOM   12213 C  CG2   . ILE C 2 172 ? 126.495 65.103  137.035 1.00 26.51 ?  151 ILE C CG2   1 
ATOM   12214 C  CD1   . ILE C 2 172 ? 128.165 64.175  134.604 1.00 26.91 ?  151 ILE C CD1   1 
ATOM   12215 N  N     . SER C 2 173 ? 127.694 68.473  138.044 1.00 23.58 ?  152 SER C N     1 
ATOM   12216 C  CA    . SER C 2 173 ? 126.911 69.502  138.725 1.00 22.36 ?  152 SER C CA    1 
ATOM   12217 C  C     . SER C 2 173 ? 126.786 70.747  137.845 1.00 21.79 ?  152 SER C C     1 
ATOM   12218 O  O     . SER C 2 173 ? 125.754 71.431  137.865 1.00 20.91 ?  152 SER C O     1 
ATOM   12219 C  CB    . SER C 2 173 ? 127.476 69.838  140.111 1.00 22.43 ?  152 SER C CB    1 
ATOM   12220 O  OG    . SER C 2 173 ? 128.800 70.340  140.032 1.00 24.02 ?  152 SER C OG    1 
ATOM   12221 N  N     . LEU C 2 174 ? 127.839 71.033  137.079 1.00 21.65 ?  153 LEU C N     1 
ATOM   12222 C  CA    . LEU C 2 174 ? 127.836 72.163  136.152 1.00 21.86 ?  153 LEU C CA    1 
ATOM   12223 C  C     . LEU C 2 174 ? 126.820 71.947  135.027 1.00 21.98 ?  153 LEU C C     1 
ATOM   12224 O  O     . LEU C 2 174 ? 126.047 72.858  134.722 1.00 21.64 ?  153 LEU C O     1 
ATOM   12225 C  CB    . LEU C 2 174 ? 129.246 72.452  135.596 1.00 21.71 ?  153 LEU C CB    1 
ATOM   12226 C  CG    . LEU C 2 174 ? 129.423 73.607  134.590 1.00 22.04 ?  153 LEU C CG    1 
ATOM   12227 C  CD1   . LEU C 2 174 ? 128.833 74.924  135.093 1.00 21.99 ?  153 LEU C CD1   1 
ATOM   12228 C  CD2   . LEU C 2 174 ? 130.908 73.779  134.251 1.00 23.37 ?  153 LEU C CD2   1 
ATOM   12229 N  N     . PHE C 2 175 ? 126.821 70.751  134.430 1.00 22.17 ?  154 PHE C N     1 
ATOM   12230 C  CA    . PHE C 2 175 ? 125.829 70.376  133.397 1.00 22.02 ?  154 PHE C CA    1 
ATOM   12231 C  C     . PHE C 2 175 ? 124.398 70.583  133.878 1.00 21.86 ?  154 PHE C C     1 
ATOM   12232 O  O     . PHE C 2 175 ? 123.549 71.101  133.142 1.00 21.62 ?  154 PHE C O     1 
ATOM   12233 C  CB    . PHE C 2 175 ? 125.997 68.905  132.984 1.00 22.08 ?  154 PHE C CB    1 
ATOM   12234 C  CG    . PHE C 2 175 ? 124.911 68.399  132.054 1.00 21.99 ?  154 PHE C CG    1 
ATOM   12235 C  CD1   . PHE C 2 175 ? 124.985 68.634  130.678 1.00 20.87 ?  154 PHE C CD1   1 
ATOM   12236 C  CD2   . PHE C 2 175 ? 123.804 67.702  132.561 1.00 20.82 ?  154 PHE C CD2   1 
ATOM   12237 C  CE1   . PHE C 2 175 ? 123.976 68.197  129.819 1.00 20.27 ?  154 PHE C CE1   1 
ATOM   12238 C  CE2   . PHE C 2 175 ? 122.790 67.248  131.714 1.00 20.19 ?  154 PHE C CE2   1 
ATOM   12239 C  CZ    . PHE C 2 175 ? 122.877 67.491  130.331 1.00 20.93 ?  154 PHE C CZ    1 
ATOM   12240 N  N     . LYS C 2 176 ? 124.128 70.134  135.104 1.00 21.98 ?  155 LYS C N     1 
ATOM   12241 C  CA    . LYS C 2 176 ? 122.787 70.243  135.684 1.00 21.79 ?  155 LYS C CA    1 
ATOM   12242 C  C     . LYS C 2 176 ? 122.348 71.707  135.803 1.00 21.70 ?  155 LYS C C     1 
ATOM   12243 O  O     . LYS C 2 176 ? 121.204 72.049  135.472 1.00 21.10 ?  155 LYS C O     1 
ATOM   12244 C  CB    . LYS C 2 176 ? 122.725 69.522  137.037 1.00 22.00 ?  155 LYS C CB    1 
ATOM   12245 C  CG    . LYS C 2 176 ? 122.889 68.011  136.940 1.00 21.93 ?  155 LYS C CG    1 
ATOM   12246 C  CD    . LYS C 2 176 ? 122.889 67.356  138.310 1.00 23.06 ?  155 LYS C CD    1 
ATOM   12247 C  CE    . LYS C 2 176 ? 122.986 65.848  138.204 1.00 24.91 ?  155 LYS C CE    1 
ATOM   12248 N  NZ    . LYS C 2 176 ? 123.316 65.226  139.530 1.00 25.16 1  155 LYS C NZ    1 
ATOM   12249 N  N     . ALA C 2 177 ? 123.261 72.565  136.272 1.00 21.49 ?  156 ALA C N     1 
ATOM   12250 C  CA    . ALA C 2 177 ? 122.992 73.999  136.327 1.00 20.60 ?  156 ALA C CA    1 
ATOM   12251 C  C     . ALA C 2 177 ? 122.811 74.639  134.933 1.00 20.37 ?  156 ALA C C     1 
ATOM   12252 O  O     . ALA C 2 177 ? 121.987 75.529  134.771 1.00 19.61 ?  156 ALA C O     1 
ATOM   12253 C  CB    . ALA C 2 177 ? 124.072 74.729  137.119 1.00 20.88 ?  156 ALA C CB    1 
ATOM   12254 N  N     . MET C 2 178 ? 123.568 74.176  133.939 1.00 20.70 ?  157 MET C N     1 
ATOM   12255 C  CA    . MET C 2 178 ? 123.419 74.675  132.561 1.00 21.06 ?  157 MET C CA    1 
ATOM   12256 C  C     . MET C 2 178 ? 122.091 74.266  131.954 1.00 20.83 ?  157 MET C C     1 
ATOM   12257 O  O     . MET C 2 178 ? 121.527 75.006  131.142 1.00 21.28 ?  157 MET C O     1 
ATOM   12258 C  CB    . MET C 2 178 ? 124.558 74.187  131.646 1.00 20.68 ?  157 MET C CB    1 
ATOM   12259 C  CG    . MET C 2 178 ? 125.940 74.768  131.936 1.00 21.61 ?  157 MET C CG    1 
ATOM   12260 S  SD    . MET C 2 178 ? 127.203 73.921  130.958 1.00 24.32 ?  157 MET C SD    1 
ATOM   12261 C  CE    . MET C 2 178 ? 128.612 75.022  131.203 1.00 23.64 ?  157 MET C CE    1 
ATOM   12262 N  N     . VAL C 2 179 ? 121.605 73.076  132.306 1.00 20.76 ?  158 VAL C N     1 
ATOM   12263 C  CA    . VAL C 2 179 ? 120.276 72.638  131.863 1.00 20.14 ?  158 VAL C CA    1 
ATOM   12264 C  C     . VAL C 2 179 ? 119.221 73.567  132.474 1.00 20.35 ?  158 VAL C C     1 
ATOM   12265 O  O     . VAL C 2 179 ? 118.304 74.028  131.789 1.00 19.82 ?  158 VAL C O     1 
ATOM   12266 C  CB    . VAL C 2 179 ? 119.973 71.172  132.274 1.00 20.07 ?  158 VAL C CB    1 
ATOM   12267 C  CG1   . VAL C 2 179 ? 118.500 70.835  132.027 1.00 20.07 ?  158 VAL C CG1   1 
ATOM   12268 C  CG2   . VAL C 2 179 ? 120.872 70.205  131.508 1.00 20.57 ?  158 VAL C CG2   1 
ATOM   12269 N  N     . ALA C 2 180 ? 119.372 73.833  133.768 1.00 19.89 ?  159 ALA C N     1 
ATOM   12270 C  CA    . ALA C 2 180 ? 118.484 74.746  134.489 1.00 20.50 ?  159 ALA C CA    1 
ATOM   12271 C  C     . ALA C 2 180 ? 118.484 76.135  133.828 1.00 20.67 ?  159 ALA C C     1 
ATOM   12272 O  O     . ALA C 2 180 ? 117.422 76.721  133.612 1.00 21.27 ?  159 ALA C O     1 
ATOM   12273 C  CB    . ALA C 2 180 ? 118.920 74.850  135.934 1.00 20.03 ?  159 ALA C CB    1 
ATOM   12274 N  N     . SER C 2 181 ? 119.673 76.640  133.502 1.00 20.78 ?  160 SER C N     1 
ATOM   12275 C  CA    . SER C 2 181 ? 119.823 77.929  132.818 1.00 21.26 ?  160 SER C CA    1 
ATOM   12276 C  C     . SER C 2 181 ? 119.167 77.935  131.429 1.00 21.19 ?  160 SER C C     1 
ATOM   12277 O  O     . SER C 2 181 ? 118.448 78.869  131.093 1.00 20.89 ?  160 SER C O     1 
ATOM   12278 C  CB    . SER C 2 181 ? 121.302 78.333  132.725 1.00 21.42 ?  160 SER C CB    1 
ATOM   12279 O  OG    . SER C 2 181 ? 121.448 79.621  132.144 1.00 23.69 ?  160 SER C OG    1 
ATOM   12280 N  N     . VAL C 2 182 ? 119.412 76.899  130.619 1.00 20.99 ?  161 VAL C N     1 
ATOM   12281 C  CA    . VAL C 2 182 ? 118.706 76.803  129.336 1.00 21.18 ?  161 VAL C CA    1 
ATOM   12282 C  C     . VAL C 2 182 ? 117.182 76.796  129.544 1.00 21.15 ?  161 VAL C C     1 
ATOM   12283 O  O     . VAL C 2 182 ? 116.449 77.490  128.820 1.00 21.18 ?  161 VAL C O     1 
ATOM   12284 C  CB    . VAL C 2 182 ? 119.165 75.576  128.484 1.00 21.11 ?  161 VAL C CB    1 
ATOM   12285 C  CG1   . VAL C 2 182 ? 118.265 75.402  127.263 1.00 21.75 ?  161 VAL C CG1   1 
ATOM   12286 C  CG2   . VAL C 2 182 ? 120.621 75.742  128.051 1.00 20.98 ?  161 VAL C CG2   1 
ATOM   12287 N  N     . TYR C 2 183 ? 116.695 76.035  130.534 1.00 21.10 ?  162 TYR C N     1 
ATOM   12288 C  CA    . TYR C 2 183 ? 115.252 76.016  130.818 1.00 21.21 ?  162 TYR C CA    1 
ATOM   12289 C  C     . TYR C 2 183 ? 114.710 77.379  131.247 1.00 21.38 ?  162 TYR C C     1 
ATOM   12290 O  O     . TYR C 2 183 ? 113.574 77.719  130.935 1.00 20.97 ?  162 TYR C O     1 
ATOM   12291 C  CB    . TYR C 2 183 ? 114.864 74.946  131.860 1.00 21.50 ?  162 TYR C CB    1 
ATOM   12292 C  CG    . TYR C 2 183 ? 114.955 73.532  131.354 1.00 22.20 ?  162 TYR C CG    1 
ATOM   12293 C  CD1   . TYR C 2 183 ? 114.935 73.257  129.988 1.00 23.80 ?  162 TYR C CD1   1 
ATOM   12294 C  CD2   . TYR C 2 183 ? 115.043 72.456  132.245 1.00 23.71 ?  162 TYR C CD2   1 
ATOM   12295 C  CE1   . TYR C 2 183 ? 115.020 71.943  129.514 1.00 25.52 ?  162 TYR C CE1   1 
ATOM   12296 C  CE2   . TYR C 2 183 ? 115.123 71.151  131.786 1.00 24.01 ?  162 TYR C CE2   1 
ATOM   12297 C  CZ    . TYR C 2 183 ? 115.121 70.899  130.424 1.00 25.47 ?  162 TYR C CZ    1 
ATOM   12298 O  OH    . TYR C 2 183 ? 115.217 69.603  129.962 1.00 25.37 ?  162 TYR C OH    1 
ATOM   12299 N  N     . LEU C 2 184 ? 115.517 78.140  131.970 1.00 22.12 ?  163 LEU C N     1 
ATOM   12300 C  CA    . LEU C 2 184 ? 115.149 79.525  132.322 1.00 23.80 ?  163 LEU C CA    1 
ATOM   12301 C  C     . LEU C 2 184 ? 115.134 80.410  131.068 1.00 24.21 ?  163 LEU C C     1 
ATOM   12302 O  O     . LEU C 2 184 ? 114.185 81.137  130.858 1.00 24.72 ?  163 LEU C O     1 
ATOM   12303 C  CB    . LEU C 2 184 ? 116.097 80.095  133.382 1.00 23.52 ?  163 LEU C CB    1 
ATOM   12304 C  CG    . LEU C 2 184 ? 115.849 81.495  133.977 1.00 24.91 ?  163 LEU C CG    1 
ATOM   12305 C  CD1   . LEU C 2 184 ? 116.293 81.522  135.418 1.00 24.81 ?  163 LEU C CD1   1 
ATOM   12306 C  CD2   . LEU C 2 184 ? 116.534 82.621  133.189 1.00 26.39 ?  163 LEU C CD2   1 
ATOM   12307 N  N     . GLU C 2 185 ? 116.179 80.322  130.234 1.00 25.17 ?  164 GLU C N     1 
ATOM   12308 C  CA    . GLU C 2 185 ? 116.321 81.195  129.058 1.00 25.30 ?  164 GLU C CA    1 
ATOM   12309 C  C     . GLU C 2 185 ? 115.262 80.940  127.973 1.00 25.07 ?  164 GLU C C     1 
ATOM   12310 O  O     . GLU C 2 185 ? 114.699 81.881  127.388 1.00 24.49 ?  164 GLU C O     1 
ATOM   12311 C  CB    . GLU C 2 185 ? 117.719 81.032  128.415 1.00 26.17 ?  164 GLU C CB    1 
ATOM   12312 C  CG    . GLU C 2 185 ? 118.902 81.507  129.286 1.00 27.05 ?  164 GLU C CG    1 
ATOM   12313 C  CD    . GLU C 2 185 ? 119.066 83.032  129.305 1.00 29.23 ?  164 GLU C CD    1 
ATOM   12314 O  OE1   . GLU C 2 185 ? 118.266 83.764  128.655 1.00 28.79 ?  164 GLU C OE1   1 
ATOM   12315 O  OE2   . GLU C 2 185 ? 120.028 83.518  129.944 1.00 28.65 -1 164 GLU C OE2   1 
ATOM   12316 N  N     . SER C 2 186 ? 115.024 79.662  127.706 1.00 24.23 ?  165 SER C N     1 
ATOM   12317 C  CA    . SER C 2 186 ? 114.347 79.222  126.492 1.00 24.71 ?  165 SER C CA    1 
ATOM   12318 C  C     . SER C 2 186 ? 112.956 78.647  126.740 1.00 24.51 ?  165 SER C C     1 
ATOM   12319 O  O     . SER C 2 186 ? 112.224 78.383  125.789 1.00 24.87 ?  165 SER C O     1 
ATOM   12320 C  CB    . SER C 2 186 ? 115.206 78.170  125.776 1.00 25.06 ?  165 SER C CB    1 
ATOM   12321 O  OG    . SER C 2 186 ? 116.486 78.679  125.453 1.00 26.29 ?  165 SER C OG    1 
ATOM   12322 N  N     . PHE C 2 187 ? 112.607 78.441  128.007 1.00 24.71 ?  166 PHE C N     1 
ATOM   12323 C  CA    . PHE C 2 187 ? 111.305 77.891  128.383 1.00 25.69 ?  166 PHE C CA    1 
ATOM   12324 C  C     . PHE C 2 187 ? 110.559 78.785  129.385 1.00 25.87 ?  166 PHE C C     1 
ATOM   12325 O  O     . PHE C 2 187 ? 109.472 79.272  129.068 1.00 26.03 ?  166 PHE C O     1 
ATOM   12326 C  CB    . PHE C 2 187 ? 111.443 76.454  128.923 1.00 25.54 ?  166 PHE C CB    1 
ATOM   12327 C  CG    . PHE C 2 187 ? 110.189 75.913  129.579 1.00 26.64 ?  166 PHE C CG    1 
ATOM   12328 C  CD1   . PHE C 2 187 ? 109.001 75.769  128.851 1.00 25.90 ?  166 PHE C CD1   1 
ATOM   12329 C  CD2   . PHE C 2 187 ? 110.201 75.535  130.924 1.00 27.45 ?  166 PHE C CD2   1 
ATOM   12330 C  CE1   . PHE C 2 187 ? 107.834 75.270  129.460 1.00 25.64 ?  166 PHE C CE1   1 
ATOM   12331 C  CE2   . PHE C 2 187 ? 109.036 75.029  131.548 1.00 26.52 ?  166 PHE C CE2   1 
ATOM   12332 C  CZ    . PHE C 2 187 ? 107.856 74.897  130.811 1.00 27.18 ?  166 PHE C CZ    1 
ATOM   12333 N  N     . LEU C 2 188 ? 111.149 79.003  130.563 1.00 26.13 ?  167 LEU C N     1 
ATOM   12334 C  CA    . LEU C 2 188 ? 110.475 79.697  131.691 1.00 27.13 ?  167 LEU C CA    1 
ATOM   12335 C  C     . LEU C 2 188 ? 110.083 81.166  131.446 1.00 27.22 ?  167 LEU C C     1 
ATOM   12336 O  O     . LEU C 2 188 ? 109.093 81.649  132.012 1.00 28.03 ?  167 LEU C O     1 
ATOM   12337 C  CB    . LEU C 2 188 ? 111.324 79.627  132.971 1.00 26.89 ?  167 LEU C CB    1 
ATOM   12338 C  CG    . LEU C 2 188 ? 111.613 78.303  133.695 1.00 28.64 ?  167 LEU C CG    1 
ATOM   12339 C  CD1   . LEU C 2 188 ? 112.515 78.550  134.903 1.00 28.34 ?  167 LEU C CD1   1 
ATOM   12340 C  CD2   . LEU C 2 188 ? 110.345 77.589  134.130 1.00 27.90 ?  167 LEU C CD2   1 
ATOM   12341 N  N     . PHE C 2 189 ? 110.873 81.881  130.653 1.00 26.79 ?  168 PHE C N     1 
ATOM   12342 C  CA    . PHE C 2 189 ? 110.562 83.275  130.341 1.00 26.90 ?  168 PHE C CA    1 
ATOM   12343 C  C     . PHE C 2 189 ? 109.270 83.389  129.524 1.00 26.52 ?  168 PHE C C     1 
ATOM   12344 O  O     . PHE C 2 189 ? 108.640 84.455  129.489 1.00 26.02 ?  168 PHE C O     1 
ATOM   12345 C  CB    . PHE C 2 189 ? 111.700 83.937  129.538 1.00 27.03 ?  168 PHE C CB    1 
ATOM   12346 C  CG    . PHE C 2 189 ? 112.821 84.535  130.386 1.00 28.09 ?  168 PHE C CG    1 
ATOM   12347 C  CD1   . PHE C 2 189 ? 112.557 85.483  131.377 1.00 28.69 ?  168 PHE C CD1   1 
ATOM   12348 C  CD2   . PHE C 2 189 ? 114.146 84.200  130.135 1.00 29.15 ?  168 PHE C CD2   1 
ATOM   12349 C  CE1   . PHE C 2 189 ? 113.590 86.048  132.141 1.00 28.50 ?  168 PHE C CE1   1 
ATOM   12350 C  CE2   . PHE C 2 189 ? 115.194 84.757  130.890 1.00 30.19 ?  168 PHE C CE2   1 
ATOM   12351 C  CZ    . PHE C 2 189 ? 114.907 85.690  131.904 1.00 29.81 ?  168 PHE C CZ    1 
ATOM   12352 N  N     . TYR C 2 190 ? 108.884 82.305  128.851 1.00 26.18 ?  169 TYR C N     1 
ATOM   12353 C  CA    . TYR C 2 190 ? 107.891 82.432  127.790 1.00 26.24 ?  169 TYR C CA    1 
ATOM   12354 C  C     . TYR C 2 190 ? 106.427 82.571  128.233 1.00 25.94 ?  169 TYR C C     1 
ATOM   12355 O  O     . TYR C 2 190 ? 105.607 83.138  127.508 1.00 25.71 ?  169 TYR C O     1 
ATOM   12356 C  CB    . TYR C 2 190 ? 108.136 81.389  126.697 1.00 27.13 ?  169 TYR C CB    1 
ATOM   12357 C  CG    . TYR C 2 190 ? 109.315 81.816  125.848 1.00 28.07 ?  169 TYR C CG    1 
ATOM   12358 C  CD1   . TYR C 2 190 ? 110.627 81.525  126.239 1.00 29.54 ?  169 TYR C CD1   1 
ATOM   12359 C  CD2   . TYR C 2 190 ? 109.125 82.573  124.692 1.00 29.31 ?  169 TYR C CD2   1 
ATOM   12360 C  CE1   . TYR C 2 190 ? 111.718 81.947  125.474 1.00 30.44 ?  169 TYR C CE1   1 
ATOM   12361 C  CE2   . TYR C 2 190 ? 110.214 82.999  123.915 1.00 30.64 ?  169 TYR C CE2   1 
ATOM   12362 C  CZ    . TYR C 2 190 ? 111.505 82.685  124.317 1.00 30.40 ?  169 TYR C CZ    1 
ATOM   12363 O  OH    . TYR C 2 190 ? 112.577 83.109  123.565 1.00 28.85 ?  169 TYR C OH    1 
ATOM   12364 N  N     . SER C 2 191 ? 106.121 82.112  129.444 1.00 25.17 ?  170 SER C N     1 
ATOM   12365 C  CA    . SER C 2 191 ? 104.803 82.338  130.030 1.00 25.10 ?  170 SER C CA    1 
ATOM   12366 C  C     . SER C 2 191 ? 104.618 83.843  130.261 1.00 25.16 ?  170 SER C C     1 
ATOM   12367 O  O     . SER C 2 191 ? 103.493 84.352  130.207 1.00 25.30 ?  170 SER C O     1 
ATOM   12368 C  CB    . SER C 2 191 ? 104.640 81.554  131.333 1.00 24.56 ?  170 SER C CB    1 
ATOM   12369 O  OG    . SER C 2 191 ? 105.542 82.011  132.323 1.00 24.98 ?  170 SER C OG    1 
ATOM   12370 N  N     . GLY C 2 192 ? 105.741 84.529  130.504 1.00 24.32 ?  171 GLY C N     1 
ATOM   12371 C  CA    . GLY C 2 192 ? 105.800 85.977  130.649 1.00 23.97 ?  171 GLY C CA    1 
ATOM   12372 C  C     . GLY C 2 192 ? 105.823 86.721  129.324 1.00 23.85 ?  171 GLY C C     1 
ATOM   12373 O  O     . GLY C 2 192 ? 105.022 87.636  129.131 1.00 23.99 ?  171 GLY C O     1 
ATOM   12374 N  N     . PHE C 2 193 ? 106.714 86.324  128.413 1.00 23.28 ?  172 PHE C N     1 
ATOM   12375 C  CA    . PHE C 2 193 ? 106.834 86.968  127.092 1.00 23.85 ?  172 PHE C CA    1 
ATOM   12376 C  C     . PHE C 2 193 ? 105.545 86.960  126.269 1.00 23.72 ?  172 PHE C C     1 
ATOM   12377 O  O     . PHE C 2 193 ? 105.345 87.843  125.437 1.00 23.92 ?  172 PHE C O     1 
ATOM   12378 C  CB    . PHE C 2 193 ? 107.929 86.320  126.234 1.00 23.47 ?  172 PHE C CB    1 
ATOM   12379 C  CG    . PHE C 2 193 ? 109.340 86.652  126.665 1.00 24.32 ?  172 PHE C CG    1 
ATOM   12380 C  CD1   . PHE C 2 193 ? 109.623 87.811  127.389 1.00 22.28 ?  172 PHE C CD1   1 
ATOM   12381 C  CD2   . PHE C 2 193 ? 110.393 85.805  126.313 1.00 23.82 ?  172 PHE C CD2   1 
ATOM   12382 C  CE1   . PHE C 2 193 ? 110.931 88.116  127.785 1.00 23.41 ?  172 PHE C CE1   1 
ATOM   12383 C  CE2   . PHE C 2 193 ? 111.714 86.096  126.700 1.00 24.70 ?  172 PHE C CE2   1 
ATOM   12384 C  CZ    . PHE C 2 193 ? 111.984 87.260  127.436 1.00 24.87 ?  172 PHE C CZ    1 
ATOM   12385 N  N     . TYR C 2 194 ? 104.695 85.952  126.478 1.00 23.31 ?  173 TYR C N     1 
ATOM   12386 C  CA    . TYR C 2 194 ? 103.476 85.793  125.682 1.00 23.26 ?  173 TYR C CA    1 
ATOM   12387 C  C     . TYR C 2 194 ? 102.670 87.093  125.607 1.00 23.04 ?  173 TYR C C     1 
ATOM   12388 O  O     . TYR C 2 194 ? 102.236 87.504  124.527 1.00 23.47 ?  173 TYR C O     1 
ATOM   12389 C  CB    . TYR C 2 194 ? 102.578 84.669  126.228 1.00 23.13 ?  173 TYR C CB    1 
ATOM   12390 C  CG    . TYR C 2 194 ? 101.352 84.404  125.363 1.00 24.10 ?  173 TYR C CG    1 
ATOM   12391 C  CD1   . TYR C 2 194 ? 101.374 83.414  124.379 1.00 25.72 ?  173 TYR C CD1   1 
ATOM   12392 C  CD2   . TYR C 2 194 ? 100.186 85.157  125.511 1.00 27.04 ?  173 TYR C CD2   1 
ATOM   12393 C  CE1   . TYR C 2 194 ? 100.253 83.166  123.575 1.00 28.94 ?  173 TYR C CE1   1 
ATOM   12394 C  CE2   . TYR C 2 194 ? 99.058  84.924  124.702 1.00 27.84 ?  173 TYR C CE2   1 
ATOM   12395 C  CZ    . TYR C 2 194 ? 99.107  83.927  123.740 1.00 29.97 ?  173 TYR C CZ    1 
ATOM   12396 O  OH    . TYR C 2 194 ? 98.013  83.686  122.928 1.00 34.34 ?  173 TYR C OH    1 
ATOM   12397 N  N     . TYR C 2 195 ? 102.471 87.725  126.753 1.00 22.51 ?  174 TYR C N     1 
ATOM   12398 C  CA    . TYR C 2 195 ? 101.500 88.808  126.858 1.00 22.60 ?  174 TYR C CA    1 
ATOM   12399 C  C     . TYR C 2 195 ? 101.961 90.115  126.187 1.00 22.64 ?  174 TYR C C     1 
ATOM   12400 O  O     . TYR C 2 195 ? 101.186 90.699  125.422 1.00 22.39 ?  174 TYR C O     1 
ATOM   12401 C  CB    . TYR C 2 195 ? 101.074 89.004  128.313 1.00 22.32 ?  174 TYR C CB    1 
ATOM   12402 C  CG    . TYR C 2 195 ? 99.656  89.507  128.500 1.00 23.39 ?  174 TYR C CG    1 
ATOM   12403 C  CD1   . TYR C 2 195 ? 98.632  89.161  127.604 1.00 22.84 ?  174 TYR C CD1   1 
ATOM   12404 C  CD2   . TYR C 2 195 ? 99.332  90.301  129.598 1.00 22.23 ?  174 TYR C CD2   1 
ATOM   12405 C  CE1   . TYR C 2 195 ? 97.324  89.623  127.793 1.00 24.05 ?  174 TYR C CE1   1 
ATOM   12406 C  CE2   . TYR C 2 195 ? 98.027  90.755  129.804 1.00 24.11 ?  174 TYR C CE2   1 
ATOM   12407 C  CZ    . TYR C 2 195 ? 97.034  90.412  128.902 1.00 23.92 ?  174 TYR C CZ    1 
ATOM   12408 O  OH    . TYR C 2 195 ? 95.766  90.885  129.105 1.00 25.00 ?  174 TYR C OH    1 
ATOM   12409 N  N     . PRO C 2 196 ? 103.224 90.567  126.449 1.00 22.25 ?  175 PRO C N     1 
ATOM   12410 C  CA    . PRO C 2 196 ? 103.733 91.710  125.674 1.00 22.45 ?  175 PRO C CA    1 
ATOM   12411 C  C     . PRO C 2 196 ? 103.723 91.456  124.166 1.00 22.59 ?  175 PRO C C     1 
ATOM   12412 O  O     . PRO C 2 196 ? 103.420 92.378  123.399 1.00 22.19 ?  175 PRO C O     1 
ATOM   12413 C  CB    . PRO C 2 196 ? 105.175 91.886  126.171 1.00 22.25 ?  175 PRO C CB    1 
ATOM   12414 C  CG    . PRO C 2 196 ? 105.225 91.223  127.508 1.00 22.22 ?  175 PRO C CG    1 
ATOM   12415 C  CD    . PRO C 2 196 ? 104.193 90.122  127.477 1.00 22.32 ?  175 PRO C CD    1 
ATOM   12416 N  N     . LEU C 2 197 ? 104.040 90.226  123.748 1.00 21.92 ?  176 LEU C N     1 
ATOM   12417 C  CA    . LEU C 2 197 ? 104.017 89.871  122.327 1.00 22.35 ?  176 LEU C CA    1 
ATOM   12418 C  C     . LEU C 2 197 ? 102.589 89.882  121.773 1.00 22.60 ?  176 LEU C C     1 
ATOM   12419 O  O     . LEU C 2 197 ? 102.350 90.311  120.640 1.00 22.41 ?  176 LEU C O     1 
ATOM   12420 C  CB    . LEU C 2 197 ? 104.644 88.499  122.085 1.00 22.69 ?  176 LEU C CB    1 
ATOM   12421 C  CG    . LEU C 2 197 ? 106.133 88.263  122.374 1.00 23.68 ?  176 LEU C CG    1 
ATOM   12422 C  CD1   . LEU C 2 197 ? 106.487 86.797  122.072 1.00 23.70 ?  176 LEU C CD1   1 
ATOM   12423 C  CD2   . LEU C 2 197 ? 107.009 89.207  121.558 1.00 23.09 ?  176 LEU C CD2   1 
ATOM   12424 N  N     . TYR C 2 198 ? 101.648 89.405  122.585 1.00 22.64 ?  177 TYR C N     1 
ATOM   12425 C  CA    . TYR C 2 198 ? 100.241 89.347  122.215 1.00 22.92 ?  177 TYR C CA    1 
ATOM   12426 C  C     . TYR C 2 198 ? 99.714  90.770  121.953 1.00 23.68 ?  177 TYR C C     1 
ATOM   12427 O  O     . TYR C 2 198 ? 99.009  91.011  120.969 1.00 23.81 ?  177 TYR C O     1 
ATOM   12428 C  CB    . TYR C 2 198 ? 99.477  88.644  123.333 1.00 22.73 ?  177 TYR C CB    1 
ATOM   12429 C  CG    . TYR C 2 198 ? 97.987  88.516  123.176 1.00 22.91 ?  177 TYR C CG    1 
ATOM   12430 C  CD1   . TYR C 2 198 ? 97.439  87.588  122.289 1.00 23.49 ?  177 TYR C CD1   1 
ATOM   12431 C  CD2   . TYR C 2 198 ? 97.121  89.276  123.963 1.00 21.97 ?  177 TYR C CD2   1 
ATOM   12432 C  CE1   . TYR C 2 198 ? 96.057  87.442  122.161 1.00 23.57 ?  177 TYR C CE1   1 
ATOM   12433 C  CE2   . TYR C 2 198 ? 95.727  89.136  123.847 1.00 22.54 ?  177 TYR C CE2   1 
ATOM   12434 C  CZ    . TYR C 2 198 ? 95.209  88.222  122.942 1.00 22.88 ?  177 TYR C CZ    1 
ATOM   12435 O  OH    . TYR C 2 198 ? 93.842  88.059  122.817 1.00 23.17 ?  177 TYR C OH    1 
ATOM   12436 N  N     . PHE C 2 199 ? 100.093 91.716  122.804 1.00 23.50 ?  178 PHE C N     1 
ATOM   12437 C  CA    . PHE C 2 199 ? 99.724  93.114  122.583 1.00 24.60 ?  178 PHE C CA    1 
ATOM   12438 C  C     . PHE C 2 199 ? 100.445 93.778  121.402 1.00 24.72 ?  178 PHE C C     1 
ATOM   12439 O  O     . PHE C 2 199 ? 99.817  94.447  120.582 1.00 24.19 ?  178 PHE C O     1 
ATOM   12440 C  CB    . PHE C 2 199 ? 99.905  93.932  123.865 1.00 24.35 ?  178 PHE C CB    1 
ATOM   12441 C  CG    . PHE C 2 199 ? 98.829  93.694  124.881 1.00 26.36 ?  178 PHE C CG    1 
ATOM   12442 C  CD1   . PHE C 2 199 ? 97.486  93.669  124.503 1.00 28.53 ?  178 PHE C CD1   1 
ATOM   12443 C  CD2   . PHE C 2 199 ? 99.146  93.512  126.220 1.00 28.23 ?  178 PHE C CD2   1 
ATOM   12444 C  CE1   . PHE C 2 199 ? 96.479  93.443  125.448 1.00 29.37 ?  178 PHE C CE1   1 
ATOM   12445 C  CE2   . PHE C 2 199 ? 98.136  93.296  127.174 1.00 28.69 ?  178 PHE C CE2   1 
ATOM   12446 C  CZ    . PHE C 2 199 ? 96.814  93.261  126.787 1.00 28.43 ?  178 PHE C CZ    1 
ATOM   12447 N  N     . TYR C 2 200 ? 101.759 93.581  121.324 1.00 25.36 ?  179 TYR C N     1 
ATOM   12448 C  CA    . TYR C 2 200 ? 102.577 94.103  120.222 1.00 26.02 ?  179 TYR C CA    1 
ATOM   12449 C  C     . TYR C 2 200 ? 101.961 93.712  118.878 1.00 26.57 ?  179 TYR C C     1 
ATOM   12450 O  O     . TYR C 2 200 ? 101.839 94.540  117.969 1.00 26.30 ?  179 TYR C O     1 
ATOM   12451 C  CB    . TYR C 2 200 ? 104.005 93.549  120.318 1.00 26.19 ?  179 TYR C CB    1 
ATOM   12452 C  CG    . TYR C 2 200 ? 104.995 94.182  119.366 1.00 27.82 ?  179 TYR C CG    1 
ATOM   12453 C  CD1   . TYR C 2 200 ? 105.370 93.532  118.186 1.00 30.77 ?  179 TYR C CD1   1 
ATOM   12454 C  CD2   . TYR C 2 200 ? 105.567 95.425  119.647 1.00 29.20 ?  179 TYR C CD2   1 
ATOM   12455 C  CE1   . TYR C 2 200 ? 106.281 94.107  117.308 1.00 31.82 ?  179 TYR C CE1   1 
ATOM   12456 C  CE2   . TYR C 2 200 ? 106.477 96.011  118.779 1.00 30.44 ?  179 TYR C CE2   1 
ATOM   12457 C  CZ    . TYR C 2 200 ? 106.830 95.344  117.610 1.00 32.74 ?  179 TYR C CZ    1 
ATOM   12458 O  OH    . TYR C 2 200 ? 107.722 95.911  116.734 1.00 34.58 ?  179 TYR C OH    1 
ATOM   12459 N  N     . GLY C 2 201 ? 101.554 92.449  118.779 1.00 26.71 ?  180 GLY C N     1 
ATOM   12460 C  CA    . GLY C 2 201 ? 100.955 91.913  117.565 1.00 27.38 ?  180 GLY C CA    1 
ATOM   12461 C  C     . GLY C 2 201 ? 99.618  92.530  117.185 1.00 27.62 ?  180 GLY C C     1 
ATOM   12462 O  O     . GLY C 2 201 ? 99.200  92.405  116.046 1.00 28.25 ?  180 GLY C O     1 
ATOM   12463 N  N     . GLN C 2 202 ? 98.958  93.191  118.135 1.00 27.60 ?  181 GLN C N     1 
ATOM   12464 C  CA    . GLN C 2 202 ? 97.687  93.892  117.887 1.00 28.24 ?  181 GLN C CA    1 
ATOM   12465 C  C     . GLN C 2 202 ? 97.891  95.393  117.749 1.00 28.30 ?  181 GLN C C     1 
ATOM   12466 O  O     . GLN C 2 202 ? 96.914  96.141  117.667 1.00 27.98 ?  181 GLN C O     1 
ATOM   12467 C  CB    . GLN C 2 202 ? 96.709  93.689  119.047 1.00 27.90 ?  181 GLN C CB    1 
ATOM   12468 C  CG    . GLN C 2 202 ? 96.292  92.279  119.316 1.00 29.54 ?  181 GLN C CG    1 
ATOM   12469 C  CD    . GLN C 2 202 ? 95.430  92.182  120.554 1.00 31.54 ?  181 GLN C CD    1 
ATOM   12470 O  OE1   . GLN C 2 202 ? 94.282  92.637  120.566 1.00 32.11 ?  181 GLN C OE1   1 
ATOM   12471 N  NE2   . GLN C 2 202 ? 95.978  91.597  121.611 1.00 31.29 ?  181 GLN C NE2   1 
ATOM   12472 N  N     . GLY C 2 203 ? 99.150  95.828  117.775 1.00 28.14 ?  182 GLY C N     1 
ATOM   12473 C  CA    . GLY C 2 203 ? 99.492  97.239  117.701 1.00 28.38 ?  182 GLY C CA    1 
ATOM   12474 C  C     . GLY C 2 203 ? 99.258  97.977  119.002 1.00 28.71 ?  182 GLY C C     1 
ATOM   12475 O  O     . GLY C 2 203 ? 98.952  99.165  118.993 1.00 28.80 ?  182 GLY C O     1 
ATOM   12476 N  N     . LYS C 2 204 ? 99.387  97.263  120.120 1.00 28.24 ?  183 LYS C N     1 
ATOM   12477 C  CA    . LYS C 2 204 ? 99.173  97.841  121.437 1.00 28.48 ?  183 LYS C CA    1 
ATOM   12478 C  C     . LYS C 2 204 ? 100.431 97.700  122.289 1.00 27.82 ?  183 LYS C C     1 
ATOM   12479 O  O     . LYS C 2 204 ? 101.141 96.688  122.204 1.00 26.73 ?  183 LYS C O     1 
ATOM   12480 C  CB    . LYS C 2 204 ? 97.986  97.178  122.138 1.00 29.13 ?  183 LYS C CB    1 
ATOM   12481 C  CG    . LYS C 2 204 ? 96.639  97.427  121.458 1.00 30.41 ?  183 LYS C CG    1 
ATOM   12482 C  CD    . LYS C 2 204 ? 95.636  96.345  121.829 1.00 33.74 ?  183 LYS C CD    1 
ATOM   12483 C  CE    . LYS C 2 204 ? 94.259  96.634  121.211 1.00 36.26 ?  183 LYS C CE    1 
ATOM   12484 N  NZ    . LYS C 2 204 ? 93.276  95.585  121.608 1.00 39.17 1  183 LYS C NZ    1 
ATOM   12485 N  N     . LEU C 2 205 ? 100.693 98.718  123.106 1.00 27.77 ?  184 LEU C N     1 
ATOM   12486 C  CA    . LEU C 2 205 ? 101.876 98.761  123.975 1.00 27.79 ?  184 LEU C CA    1 
ATOM   12487 C  C     . LEU C 2 205 ? 103.157 98.462  123.192 1.00 27.85 ?  184 LEU C C     1 
ATOM   12488 O  O     . LEU C 2 205 ? 103.976 97.614  123.573 1.00 27.07 ?  184 LEU C O     1 
ATOM   12489 C  CB    . LEU C 2 205 ? 101.708 97.805  125.174 1.00 27.76 ?  184 LEU C CB    1 
ATOM   12490 C  CG    . LEU C 2 205 ? 100.463 98.035  126.041 1.00 28.62 ?  184 LEU C CG    1 
ATOM   12491 C  CD1   . LEU C 2 205 ? 100.336 96.962  127.104 1.00 29.18 ?  184 LEU C CD1   1 
ATOM   12492 C  CD2   . LEU C 2 205 ? 100.485 99.414  126.684 1.00 28.43 ?  184 LEU C CD2   1 
ATOM   12493 N  N     . MET C 2 206 ? 103.339 99.181  122.095 1.00 28.15 ?  185 MET C N     1 
ATOM   12494 C  CA    . MET C 2 206 ? 104.390 98.827  121.167 1.00 28.80 ?  185 MET C CA    1 
ATOM   12495 C  C     . MET C 2 206 ? 105.789 99.256  121.587 1.00 28.77 ?  185 MET C C     1 
ATOM   12496 O  O     . MET C 2 206 ? 106.766 98.647  121.156 1.00 28.79 ?  185 MET C O     1 
ATOM   12497 C  CB    . MET C 2 206 ? 104.031 99.302  119.772 1.00 29.96 ?  185 MET C CB    1 
ATOM   12498 C  CG    . MET C 2 206 ? 102.830 98.530  119.216 1.00 31.23 ?  185 MET C CG    1 
ATOM   12499 S  SD    . MET C 2 206 ? 102.747 98.706  117.454 1.00 40.10 ?  185 MET C SD    1 
ATOM   12500 C  CE    . MET C 2 206 ? 104.111 97.693  116.917 1.00 35.10 ?  185 MET C CE    1 
ATOM   12501 N  N     . GLN C 2 207 ? 105.891 100.270 122.441 1.00 28.62 ?  186 GLN C N     1 
ATOM   12502 C  CA    . GLN C 2 207 ? 107.199 100.706 122.941 1.00 29.10 ?  186 GLN C CA    1 
ATOM   12503 C  C     . GLN C 2 207 ? 107.735 99.724  123.986 1.00 28.52 ?  186 GLN C C     1 
ATOM   12504 O  O     . GLN C 2 207 ? 108.883 99.294  123.890 1.00 28.28 ?  186 GLN C O     1 
ATOM   12505 C  CB    . GLN C 2 207 ? 107.153 102.135 123.492 1.00 29.21 ?  186 GLN C CB    1 
ATOM   12506 C  CG    . GLN C 2 207 ? 106.811 103.197 122.446 1.00 31.41 ?  186 GLN C CG    1 
ATOM   12507 C  CD    . GLN C 2 207 ? 107.869 103.315 121.369 1.00 34.70 ?  186 GLN C CD    1 
ATOM   12508 O  OE1   . GLN C 2 207 ? 107.788 102.659 120.334 1.00 37.69 ?  186 GLN C OE1   1 
ATOM   12509 N  NE2   . GLN C 2 207 ? 108.887 104.130 121.620 1.00 34.75 ?  186 GLN C NE2   1 
ATOM   12510 N  N     . SER C 2 208 ? 106.894 99.376  124.968 1.00 28.38 ?  187 SER C N     1 
ATOM   12511 C  CA    . SER C 2 208 ? 107.182 98.297  125.921 1.00 28.25 ?  187 SER C CA    1 
ATOM   12512 C  C     . SER C 2 208 ? 107.488 97.011  125.164 1.00 28.00 ?  187 SER C C     1 
ATOM   12513 O  O     . SER C 2 208 ? 108.411 96.279  125.523 1.00 27.90 ?  187 SER C O     1 
ATOM   12514 C  CB    . SER C 2 208 ? 105.980 98.038  126.832 1.00 27.88 ?  187 SER C CB    1 
ATOM   12515 O  OG    . SER C 2 208 ? 105.659 99.172  127.610 1.00 30.27 ?  187 SER C OG    1 
ATOM   12516 N  N     . GLY C 2 209 ? 106.691 96.745  124.123 1.00 27.31 ?  188 GLY C N     1 
ATOM   12517 C  CA    . GLY C 2 209 ? 106.861 95.567  123.275 1.00 27.86 ?  188 GLY C CA    1 
ATOM   12518 C  C     . GLY C 2 209 ? 108.196 95.529  122.555 1.00 27.96 ?  188 GLY C C     1 
ATOM   12519 O  O     . GLY C 2 209 ? 108.776 94.453  122.366 1.00 27.84 ?  188 GLY C O     1 
ATOM   12520 N  N     . GLU C 2 210 ? 108.681 96.702  122.147 1.00 28.21 ?  189 GLU C N     1 
ATOM   12521 C  CA    . GLU C 2 210 ? 109.992 96.821  121.516 1.00 29.15 ?  189 GLU C CA    1 
ATOM   12522 C  C     . GLU C 2 210 ? 111.111 96.415  122.496 1.00 28.02 ?  189 GLU C C     1 
ATOM   12523 O  O     . GLU C 2 210 ? 112.047 95.699  122.133 1.00 27.15 ?  189 GLU C O     1 
ATOM   12524 C  CB    . GLU C 2 210 ? 110.203 98.249  121.007 1.00 30.17 ?  189 GLU C CB    1 
ATOM   12525 C  CG    . GLU C 2 210 ? 110.667 98.337  119.562 1.00 35.68 ?  189 GLU C CG    1 
ATOM   12526 C  CD    . GLU C 2 210 ? 109.530 98.134  118.556 1.00 40.25 ?  189 GLU C CD    1 
ATOM   12527 O  OE1   . GLU C 2 210 ? 108.568 98.939  118.532 1.00 42.98 ?  189 GLU C OE1   1 
ATOM   12528 O  OE2   . GLU C 2 210 ? 109.602 97.169  117.772 1.00 43.59 -1 189 GLU C OE2   1 
ATOM   12529 N  N     . ILE C 2 211 ? 111.004 96.876  123.740 1.00 27.57 ?  190 ILE C N     1 
ATOM   12530 C  CA    . ILE C 2 211 ? 111.932 96.466  124.799 1.00 27.47 ?  190 ILE C CA    1 
ATOM   12531 C  C     . ILE C 2 211 ? 111.931 94.945  124.984 1.00 26.69 ?  190 ILE C C     1 
ATOM   12532 O  O     . ILE C 2 211 ? 112.985 94.296  124.982 1.00 26.56 ?  190 ILE C O     1 
ATOM   12533 C  CB    . ILE C 2 211 ? 111.621 97.200  126.137 1.00 27.84 ?  190 ILE C CB    1 
ATOM   12534 C  CG1   . ILE C 2 211 ? 112.009 98.683  126.018 1.00 28.56 ?  190 ILE C CG1   1 
ATOM   12535 C  CG2   . ILE C 2 211 ? 112.338 96.510  127.320 1.00 27.27 ?  190 ILE C CG2   1 
ATOM   12536 C  CD1   . ILE C 2 211 ? 111.798 99.497  127.289 1.00 30.09 ?  190 ILE C CD1   1 
ATOM   12537 N  N     . ILE C 2 212 ? 110.736 94.378  125.104 1.00 26.33 ?  191 ILE C N     1 
ATOM   12538 C  CA    . ILE C 2 212 ? 110.568 92.942  125.299 1.00 25.96 ?  191 ILE C CA    1 
ATOM   12539 C  C     . ILE C 2 212 ? 111.167 92.125  124.146 1.00 25.46 ?  191 ILE C C     1 
ATOM   12540 O  O     . ILE C 2 212 ? 111.797 91.098  124.388 1.00 24.84 ?  191 ILE C O     1 
ATOM   12541 C  CB    . ILE C 2 212 ? 109.073 92.575  125.552 1.00 26.00 ?  191 ILE C CB    1 
ATOM   12542 C  CG1   . ILE C 2 212 ? 108.584 93.187  126.875 1.00 27.16 ?  191 ILE C CG1   1 
ATOM   12543 C  CG2   . ILE C 2 212 ? 108.849 91.069  125.546 1.00 26.87 ?  191 ILE C CG2   1 
ATOM   12544 C  CD1   . ILE C 2 212 ? 109.283 92.669  128.119 1.00 29.84 ?  191 ILE C CD1   1 
ATOM   12545 N  N     . ASN C 2 213 ? 110.975 92.580  122.905 1.00 25.35 ?  192 ASN C N     1 
ATOM   12546 C  CA    . ASN C 2 213 ? 111.567 91.917  121.739 1.00 25.60 ?  192 ASN C CA    1 
ATOM   12547 C  C     . ASN C 2 213 ? 113.092 91.927  121.768 1.00 25.14 ?  192 ASN C C     1 
ATOM   12548 O  O     . ASN C 2 213 ? 113.744 90.955  121.358 1.00 25.61 ?  192 ASN C O     1 
ATOM   12549 C  CB    . ASN C 2 213 ? 111.070 92.536  120.426 1.00 26.55 ?  192 ASN C CB    1 
ATOM   12550 C  CG    . ASN C 2 213 ? 109.776 91.917  119.946 1.00 28.10 ?  192 ASN C CG    1 
ATOM   12551 O  OD1   . ASN C 2 213 ? 109.715 90.722  119.639 1.00 31.67 ?  192 ASN C OD1   1 
ATOM   12552 N  ND2   . ASN C 2 213 ? 108.735 92.726  119.866 1.00 30.36 ?  192 ASN C ND2   1 
ATOM   12553 N  N     . LEU C 2 214 ? 113.661 93.023  122.255 1.00 24.54 ?  193 LEU C N     1 
ATOM   12554 C  CA    . LEU C 2 214 ? 115.115 93.102  122.423 1.00 24.40 ?  193 LEU C CA    1 
ATOM   12555 C  C     . LEU C 2 214 ? 115.599 92.123  123.494 1.00 23.55 ?  193 LEU C C     1 
ATOM   12556 O  O     . LEU C 2 214 ? 116.590 91.418  123.288 1.00 23.09 ?  193 LEU C O     1 
ATOM   12557 C  CB    . LEU C 2 214 ? 115.557 94.534  122.711 1.00 24.00 ?  193 LEU C CB    1 
ATOM   12558 C  CG    . LEU C 2 214 ? 115.473 95.510  121.516 1.00 25.69 ?  193 LEU C CG    1 
ATOM   12559 C  CD1   . LEU C 2 214 ? 115.651 96.962  121.962 1.00 26.28 ?  193 LEU C CD1   1 
ATOM   12560 C  CD2   . LEU C 2 214 ? 116.502 95.176  120.433 1.00 26.05 ?  193 LEU C CD2   1 
ATOM   12561 N  N     . ILE C 2 215 ? 114.890 92.073  124.625 1.00 23.19 ?  194 ILE C N     1 
ATOM   12562 C  CA    . ILE C 2 215 ? 115.165 91.090  125.679 1.00 22.88 ?  194 ILE C CA    1 
ATOM   12563 C  C     . ILE C 2 215 ? 115.068 89.670  125.099 1.00 23.81 ?  194 ILE C C     1 
ATOM   12564 O  O     . ILE C 2 215 ? 115.967 88.852  125.302 1.00 23.83 ?  194 ILE C O     1 
ATOM   12565 C  CB    . ILE C 2 215 ? 114.211 91.255  126.896 1.00 22.92 ?  194 ILE C CB    1 
ATOM   12566 C  CG1   . ILE C 2 215 ? 114.379 92.637  127.530 1.00 21.11 ?  194 ILE C CG1   1 
ATOM   12567 C  CG2   . ILE C 2 215 ? 114.430 90.148  127.941 1.00 21.89 ?  194 ILE C CG2   1 
ATOM   12568 C  CD1   . ILE C 2 215 ? 113.467 92.895  128.712 1.00 22.26 ?  194 ILE C CD1   1 
ATOM   12569 N  N     . LEU C 2 216 ? 114.006 89.391  124.344 1.00 24.23 ?  195 LEU C N     1 
ATOM   12570 C  CA    . LEU C 2 216 ? 113.795 88.049  123.788 1.00 25.41 ?  195 LEU C CA    1 
ATOM   12571 C  C     . LEU C 2 216 ? 114.896 87.659  122.800 1.00 25.63 ?  195 LEU C C     1 
ATOM   12572 O  O     . LEU C 2 216 ? 115.387 86.520  122.821 1.00 25.46 ?  195 LEU C O     1 
ATOM   12573 C  CB    . LEU C 2 216 ? 112.405 87.939  123.133 1.00 26.03 ?  195 LEU C CB    1 
ATOM   12574 C  CG    . LEU C 2 216 ? 111.929 86.613  122.525 1.00 28.00 ?  195 LEU C CG    1 
ATOM   12575 C  CD1   . LEU C 2 216 ? 110.411 86.625  122.445 1.00 31.45 ?  195 LEU C CD1   1 
ATOM   12576 C  CD2   . LEU C 2 216 ? 112.539 86.348  121.144 1.00 29.83 ?  195 LEU C CD2   1 
ATOM   12577 N  N     . ARG C 2 217 ? 115.283 88.605  121.949 1.00 25.98 ?  196 ARG C N     1 
ATOM   12578 C  CA    . ARG C 2 217 ? 116.390 88.414  121.018 1.00 26.73 ?  196 ARG C CA    1 
ATOM   12579 C  C     . ARG C 2 217 ? 117.681 88.007  121.772 1.00 25.95 ?  196 ARG C C     1 
ATOM   12580 O  O     . ARG C 2 217 ? 118.376 87.082  121.336 1.00 25.75 ?  196 ARG C O     1 
ATOM   12581 C  CB    . ARG C 2 217 ? 116.609 89.686  120.197 1.00 27.29 ?  196 ARG C CB    1 
ATOM   12582 C  CG    . ARG C 2 217 ? 117.553 89.546  118.994 1.00 30.12 ?  196 ARG C CG    1 
ATOM   12583 C  CD    . ARG C 2 217 ? 118.263 90.864  118.750 1.00 35.40 ?  196 ARG C CD    1 
ATOM   12584 N  NE    . ARG C 2 217 ? 118.726 91.389  120.035 1.00 39.87 ?  196 ARG C NE    1 
ATOM   12585 C  CZ    . ARG C 2 217 ? 119.184 92.614  120.258 1.00 40.55 ?  196 ARG C CZ    1 
ATOM   12586 N  NH1   . ARG C 2 217 ? 119.272 93.507  119.273 1.00 40.77 1  196 ARG C NH1   1 
ATOM   12587 N  NH2   . ARG C 2 217 ? 119.553 92.939  121.491 1.00 41.10 ?  196 ARG C NH2   1 
ATOM   12588 N  N     . ASP C 2 218 ? 117.976 88.682  122.889 1.00 24.70 ?  197 ASP C N     1 
ATOM   12589 C  CA    . ASP C 2 218 ? 119.112 88.320  123.760 1.00 24.55 ?  197 ASP C CA    1 
ATOM   12590 C  C     . ASP C 2 218 ? 118.959 86.903  124.348 1.00 24.23 ?  197 ASP C C     1 
ATOM   12591 O  O     . ASP C 2 218 ? 119.884 86.090  124.248 1.00 23.69 ?  197 ASP C O     1 
ATOM   12592 C  CB    . ASP C 2 218 ? 119.317 89.321  124.915 1.00 24.50 ?  197 ASP C CB    1 
ATOM   12593 C  CG    . ASP C 2 218 ? 119.760 90.721  124.453 1.00 25.84 ?  197 ASP C CG    1 
ATOM   12594 O  OD1   . ASP C 2 218 ? 120.350 90.877  123.361 1.00 26.91 ?  197 ASP C OD1   1 
ATOM   12595 O  OD2   . ASP C 2 218 ? 119.529 91.681  125.213 1.00 25.72 -1 197 ASP C OD2   1 
ATOM   12596 N  N     . GLU C 2 219 ? 117.797 86.597  124.934 1.00 23.92 ?  198 GLU C N     1 
ATOM   12597 C  CA    . GLU C 2 219 ? 117.635 85.298  125.609 1.00 24.20 ?  198 GLU C CA    1 
ATOM   12598 C  C     . GLU C 2 219 ? 117.770 84.141  124.637 1.00 24.02 ?  198 GLU C C     1 
ATOM   12599 O  O     . GLU C 2 219 ? 118.295 83.098  125.009 1.00 24.24 ?  198 GLU C O     1 
ATOM   12600 C  CB    . GLU C 2 219 ? 116.316 85.166  126.375 1.00 24.05 ?  198 GLU C CB    1 
ATOM   12601 C  CG    . GLU C 2 219 ? 115.830 86.393  127.126 1.00 25.03 ?  198 GLU C CG    1 
ATOM   12602 C  CD    . GLU C 2 219 ? 116.625 86.780  128.388 1.00 26.31 ?  198 GLU C CD    1 
ATOM   12603 O  OE1   . GLU C 2 219 ? 117.836 86.443  128.545 1.00 27.65 ?  198 GLU C OE1   1 
ATOM   12604 O  OE2   . GLU C 2 219 ? 116.003 87.479  129.234 1.00 26.87 -1 198 GLU C OE2   1 
ATOM   12605 N  N     . ALA C 2 220 ? 117.297 84.321  123.402 1.00 24.00 ?  199 ALA C N     1 
ATOM   12606 C  CA    . ALA C 2 220 ? 117.422 83.285  122.383 1.00 24.72 ?  199 ALA C CA    1 
ATOM   12607 C  C     . ALA C 2 220 ? 118.888 82.886  122.144 1.00 24.80 ?  199 ALA C C     1 
ATOM   12608 O  O     . ALA C 2 220 ? 119.204 81.694  122.088 1.00 25.04 ?  199 ALA C O     1 
ATOM   12609 C  CB    . ALA C 2 220 ? 116.740 83.711  121.058 1.00 24.66 ?  199 ALA C CB    1 
ATOM   12610 N  N     . ILE C 2 221 ? 119.773 83.872  122.017 1.00 24.85 ?  200 ILE C N     1 
ATOM   12611 C  CA    . ILE C 2 221 ? 121.207 83.585  121.836 1.00 25.07 ?  200 ILE C CA    1 
ATOM   12612 C  C     . ILE C 2 221 ? 121.872 83.088  123.129 1.00 23.86 ?  200 ILE C C     1 
ATOM   12613 O  O     . ILE C 2 221 ? 122.782 82.257  123.070 1.00 23.72 ?  200 ILE C O     1 
ATOM   12614 C  CB    . ILE C 2 221 ? 122.018 84.763  121.184 1.00 25.71 ?  200 ILE C CB    1 
ATOM   12615 C  CG1   . ILE C 2 221 ? 122.229 85.920  122.166 1.00 27.10 ?  200 ILE C CG1   1 
ATOM   12616 C  CG2   . ILE C 2 221 ? 121.361 85.216  119.865 1.00 27.18 ?  200 ILE C CG2   1 
ATOM   12617 C  CD1   . ILE C 2 221 ? 123.173 87.024  121.674 1.00 29.63 ?  200 ILE C CD1   1 
ATOM   12618 N  N     . HIS C 2 222 ? 121.409 83.578  124.280 1.00 22.79 ?  201 HIS C N     1 
ATOM   12619 C  CA    . HIS C 2 222 ? 121.896 83.078  125.586 1.00 22.48 ?  201 HIS C CA    1 
ATOM   12620 C  C     . HIS C 2 222 ? 121.578 81.595  125.766 1.00 22.04 ?  201 HIS C C     1 
ATOM   12621 O  O     . HIS C 2 222 ? 122.419 80.839  126.237 1.00 22.06 ?  201 HIS C O     1 
ATOM   12622 C  CB    . HIS C 2 222 ? 121.259 83.819  126.762 1.00 21.77 ?  201 HIS C CB    1 
ATOM   12623 C  CG    . HIS C 2 222 ? 121.629 85.262  126.863 1.00 21.76 ?  201 HIS C CG    1 
ATOM   12624 N  ND1   . HIS C 2 222 ? 121.228 86.048  127.920 1.00 20.70 ?  201 HIS C ND1   1 
ATOM   12625 C  CD2   . HIS C 2 222 ? 122.360 86.062  126.054 1.00 22.07 ?  201 HIS C CD2   1 
ATOM   12626 C  CE1   . HIS C 2 222 ? 121.687 87.274  127.753 1.00 22.26 ?  201 HIS C CE1   1 
ATOM   12627 N  NE2   . HIS C 2 222 ? 122.369 87.311  126.626 1.00 22.52 ?  201 HIS C NE2   1 
ATOM   12628 N  N     . GLY C 2 223 ? 120.349 81.200  125.427 1.00 22.35 ?  202 GLY C N     1 
ATOM   12629 C  CA    . GLY C 2 223 ? 119.913 79.797  125.503 1.00 22.01 ?  202 GLY C CA    1 
ATOM   12630 C  C     . GLY C 2 223 ? 120.682 78.871  124.565 1.00 22.73 ?  202 GLY C C     1 
ATOM   12631 O  O     . GLY C 2 223 ? 121.029 77.737  124.937 1.00 21.99 ?  202 GLY C O     1 
ATOM   12632 N  N     . VAL C 2 224 ? 120.961 79.347  123.349 1.00 22.45 ?  203 VAL C N     1 
ATOM   12633 C  CA    . VAL C 2 224 ? 121.765 78.571  122.402 1.00 22.54 ?  203 VAL C CA    1 
ATOM   12634 C  C     . VAL C 2 224 ? 123.188 78.380  122.930 1.00 22.28 ?  203 VAL C C     1 
ATOM   12635 O  O     . VAL C 2 224 ? 123.689 77.259  122.973 1.00 22.44 ?  203 VAL C O     1 
ATOM   12636 C  CB    . VAL C 2 224 ? 121.798 79.209  120.971 1.00 23.00 ?  203 VAL C CB    1 
ATOM   12637 C  CG1   . VAL C 2 224 ? 122.823 78.485  120.079 1.00 23.10 ?  203 VAL C CG1   1 
ATOM   12638 C  CG2   . VAL C 2 224 ? 120.395 79.165  120.309 1.00 23.14 ?  203 VAL C CG2   1 
ATOM   12639 N  N     . TYR C 2 225 ? 123.816 79.471  123.362 1.00 22.41 ?  204 TYR C N     1 
ATOM   12640 C  CA    . TYR C 2 225 ? 125.193 79.425  123.852 1.00 22.03 ?  204 TYR C CA    1 
ATOM   12641 C  C     . TYR C 2 225 ? 125.367 78.485  125.044 1.00 21.66 ?  204 TYR C C     1 
ATOM   12642 O  O     . TYR C 2 225 ? 126.220 77.586  125.012 1.00 21.72 ?  204 TYR C O     1 
ATOM   12643 C  CB    . TYR C 2 225 ? 125.723 80.828  124.189 1.00 22.22 ?  204 TYR C CB    1 
ATOM   12644 C  CG    . TYR C 2 225 ? 127.210 80.834  124.483 1.00 21.92 ?  204 TYR C CG    1 
ATOM   12645 C  CD1   . TYR C 2 225 ? 128.139 80.583  123.473 1.00 22.36 ?  204 TYR C CD1   1 
ATOM   12646 C  CD2   . TYR C 2 225 ? 127.683 81.080  125.773 1.00 21.43 ?  204 TYR C CD2   1 
ATOM   12647 C  CE1   . TYR C 2 225 ? 129.507 80.570  123.741 1.00 23.82 ?  204 TYR C CE1   1 
ATOM   12648 C  CE2   . TYR C 2 225 ? 129.052 81.080  126.056 1.00 21.49 ?  204 TYR C CE2   1 
ATOM   12649 C  CZ    . TYR C 2 225 ? 129.951 80.826  125.037 1.00 23.58 ?  204 TYR C CZ    1 
ATOM   12650 O  OH    . TYR C 2 225 ? 131.293 80.825  125.313 1.00 25.42 ?  204 TYR C OH    1 
ATOM   12651 N  N     . VAL C 2 226 ? 124.560 78.682  126.090 1.00 20.95 ?  205 VAL C N     1 
ATOM   12652 C  CA    . VAL C 2 226 ? 124.613 77.801  127.263 1.00 20.49 ?  205 VAL C CA    1 
ATOM   12653 C  C     . VAL C 2 226 ? 124.287 76.347  126.873 1.00 20.84 ?  205 VAL C C     1 
ATOM   12654 O  O     . VAL C 2 226 ? 124.930 75.405  127.355 1.00 21.10 ?  205 VAL C O     1 
ATOM   12655 C  CB    . VAL C 2 226 ? 123.735 78.318  128.435 1.00 20.57 ?  205 VAL C CB    1 
ATOM   12656 C  CG1   . VAL C 2 226 ? 123.786 77.348  129.616 1.00 20.35 ?  205 VAL C CG1   1 
ATOM   12657 C  CG2   . VAL C 2 226 ? 124.222 79.707  128.876 1.00 19.60 ?  205 VAL C CG2   1 
ATOM   12658 N  N     . GLY C 2 227 ? 123.331 76.174  125.966 1.00 21.08 ?  206 GLY C N     1 
ATOM   12659 C  CA    . GLY C 2 227 ? 123.039 74.846  125.403 1.00 21.43 ?  206 GLY C CA    1 
ATOM   12660 C  C     . GLY C 2 227 ? 124.250 74.155  124.791 1.00 21.95 ?  206 GLY C C     1 
ATOM   12661 O  O     . GLY C 2 227 ? 124.472 72.951  125.010 1.00 21.84 ?  206 GLY C O     1 
ATOM   12662 N  N     . LEU C 2 228 ? 125.043 74.905  124.027 1.00 22.09 ?  207 LEU C N     1 
ATOM   12663 C  CA    . LEU C 2 228 ? 126.257 74.345  123.425 1.00 22.96 ?  207 LEU C CA    1 
ATOM   12664 C  C     . LEU C 2 228 ? 127.293 73.930  124.480 1.00 22.60 ?  207 LEU C C     1 
ATOM   12665 O  O     . LEU C 2 228 ? 127.938 72.886  124.346 1.00 22.04 ?  207 LEU C O     1 
ATOM   12666 C  CB    . LEU C 2 228 ? 126.862 75.298  122.385 1.00 23.39 ?  207 LEU C CB    1 
ATOM   12667 C  CG    . LEU C 2 228 ? 126.050 75.566  121.104 1.00 24.35 ?  207 LEU C CG    1 
ATOM   12668 C  CD1   . LEU C 2 228 ? 126.574 76.828  120.407 1.00 25.01 ?  207 LEU C CD1   1 
ATOM   12669 C  CD2   . LEU C 2 228 ? 126.073 74.382  120.144 1.00 25.11 ?  207 LEU C CD2   1 
ATOM   12670 N  N     . LEU C 2 229 ? 127.431 74.725  125.539 1.00 22.37 ?  208 LEU C N     1 
ATOM   12671 C  CA    . LEU C 2 229 ? 128.329 74.361  126.652 1.00 22.62 ?  208 LEU C CA    1 
ATOM   12672 C  C     . LEU C 2 229 ? 127.865 73.099  127.388 1.00 22.77 ?  208 LEU C C     1 
ATOM   12673 O  O     . LEU C 2 229 ? 128.684 72.233  127.741 1.00 22.57 ?  208 LEU C O     1 
ATOM   12674 C  CB    . LEU C 2 229 ? 128.514 75.530  127.624 1.00 22.44 ?  208 LEU C CB    1 
ATOM   12675 C  CG    . LEU C 2 229 ? 129.059 76.831  127.016 1.00 23.54 ?  208 LEU C CG    1 
ATOM   12676 C  CD1   . LEU C 2 229 ? 129.100 77.939  128.065 1.00 23.37 ?  208 LEU C CD1   1 
ATOM   12677 C  CD2   . LEU C 2 229 ? 130.448 76.624  126.384 1.00 23.91 ?  208 LEU C CD2   1 
ATOM   12678 N  N     . ALA C 2 230 ? 126.554 72.993  127.607 1.00 22.42 ?  209 ALA C N     1 
ATOM   12679 C  CA    . ALA C 2 230 ? 125.966 71.802  128.219 1.00 22.02 ?  209 ALA C CA    1 
ATOM   12680 C  C     . ALA C 2 230 ? 126.228 70.552  127.373 1.00 22.58 ?  209 ALA C C     1 
ATOM   12681 O  O     . ALA C 2 230 ? 126.620 69.519  127.900 1.00 22.14 ?  209 ALA C O     1 
ATOM   12682 C  CB    . ALA C 2 230 ? 124.482 71.992  128.432 1.00 22.04 ?  209 ALA C CB    1 
ATOM   12683 N  N     . GLN C 2 231 ? 126.027 70.666  126.062 1.00 22.96 ?  210 GLN C N     1 
ATOM   12684 C  CA    . GLN C 2 231 ? 126.302 69.550  125.138 1.00 24.30 ?  210 GLN C CA    1 
ATOM   12685 C  C     . GLN C 2 231 ? 127.750 69.096  125.165 1.00 25.11 ?  210 GLN C C     1 
ATOM   12686 O  O     . GLN C 2 231 ? 128.027 67.900  125.024 1.00 24.97 ?  210 GLN C O     1 
ATOM   12687 C  CB    . GLN C 2 231 ? 125.901 69.915  123.713 1.00 24.38 ?  210 GLN C CB    1 
ATOM   12688 C  CG    . GLN C 2 231 ? 124.380 70.054  123.534 1.00 25.12 ?  210 GLN C CG    1 
ATOM   12689 C  CD    . GLN C 2 231 ? 123.998 70.414  122.114 1.00 28.08 ?  210 GLN C CD    1 
ATOM   12690 O  OE1   . GLN C 2 231 ? 124.374 69.720  121.168 1.00 27.83 ?  210 GLN C OE1   1 
ATOM   12691 N  NE2   . GLN C 2 231 ? 123.262 71.515  121.952 1.00 26.38 ?  210 GLN C NE2   1 
ATOM   12692 N  N     . GLU C 2 232 ? 128.673 70.044  125.340 1.00 25.80 ?  211 GLU C N     1 
ATOM   12693 C  CA    . GLU C 2 232 ? 130.093 69.706  125.483 1.00 27.16 ?  211 GLU C CA    1 
ATOM   12694 C  C     . GLU C 2 232 ? 130.313 68.730  126.636 1.00 26.47 ?  211 GLU C C     1 
ATOM   12695 O  O     . GLU C 2 232 ? 131.048 67.746  126.498 1.00 26.10 ?  211 GLU C O     1 
ATOM   12696 C  CB    . GLU C 2 232 ? 130.927 70.951  125.757 1.00 27.59 ?  211 GLU C CB    1 
ATOM   12697 C  CG    . GLU C 2 232 ? 131.461 71.632  124.534 1.00 32.55 ?  211 GLU C CG    1 
ATOM   12698 C  CD    . GLU C 2 232 ? 132.809 72.294  124.788 1.00 36.72 ?  211 GLU C CD    1 
ATOM   12699 O  OE1   . GLU C 2 232 ? 133.281 72.299  125.951 1.00 38.32 ?  211 GLU C OE1   1 
ATOM   12700 O  OE2   . GLU C 2 232 ? 133.400 72.805  123.816 1.00 40.62 -1 211 GLU C OE2   1 
ATOM   12701 N  N     . ILE C 2 233 ? 129.688 69.022  127.775 1.00 25.55 ?  212 ILE C N     1 
ATOM   12702 C  CA    . ILE C 2 233 ? 129.843 68.189  128.968 1.00 25.32 ?  212 ILE C CA    1 
ATOM   12703 C  C     . ILE C 2 233 ? 129.156 66.840  128.796 1.00 25.48 ?  212 ILE C C     1 
ATOM   12704 O  O     . ILE C 2 233 ? 129.752 65.795  129.067 1.00 25.82 ?  212 ILE C O     1 
ATOM   12705 C  CB    . ILE C 2 233 ? 129.339 68.902  130.242 1.00 25.39 ?  212 ILE C CB    1 
ATOM   12706 C  CG1   . ILE C 2 233 ? 130.244 70.097  130.553 1.00 24.37 ?  212 ILE C CG1   1 
ATOM   12707 C  CG2   . ILE C 2 233 ? 129.283 67.922  131.419 1.00 24.86 ?  212 ILE C CG2   1 
ATOM   12708 C  CD1   . ILE C 2 233 ? 129.625 71.096  131.518 1.00 25.10 ?  212 ILE C CD1   1 
ATOM   12709 N  N     . TYR C 2 234 ? 127.914 66.870  128.320 1.00 25.27 ?  213 TYR C N     1 
ATOM   12710 C  CA    . TYR C 2 234 ? 127.156 65.656  128.005 1.00 25.77 ?  213 TYR C CA    1 
ATOM   12711 C  C     . TYR C 2 234 ? 127.930 64.713  127.066 1.00 26.44 ?  213 TYR C C     1 
ATOM   12712 O  O     . TYR C 2 234 ? 127.945 63.497  127.266 1.00 26.29 ?  213 TYR C O     1 
ATOM   12713 C  CB    . TYR C 2 234 ? 125.808 66.053  127.382 1.00 25.67 ?  213 TYR C CB    1 
ATOM   12714 C  CG    . TYR C 2 234 ? 124.904 64.925  126.930 1.00 25.65 ?  213 TYR C CG    1 
ATOM   12715 C  CD1   . TYR C 2 234 ? 123.933 64.400  127.787 1.00 25.02 ?  213 TYR C CD1   1 
ATOM   12716 C  CD2   . TYR C 2 234 ? 124.979 64.421  125.622 1.00 26.59 ?  213 TYR C CD2   1 
ATOM   12717 C  CE1   . TYR C 2 234 ? 123.081 63.383  127.369 1.00 26.52 ?  213 TYR C CE1   1 
ATOM   12718 C  CE2   . TYR C 2 234 ? 124.134 63.396  125.193 1.00 27.00 ?  213 TYR C CE2   1 
ATOM   12719 C  CZ    . TYR C 2 234 ? 123.192 62.884  126.076 1.00 27.79 ?  213 TYR C CZ    1 
ATOM   12720 O  OH    . TYR C 2 234 ? 122.348 61.892  125.661 1.00 29.00 ?  213 TYR C OH    1 
ATOM   12721 N  N     . ASN C 2 235 ? 128.570 65.275  126.043 1.00 26.96 ?  214 ASN C N     1 
ATOM   12722 C  CA    . ASN C 2 235 ? 129.273 64.454  125.057 1.00 28.05 ?  214 ASN C CA    1 
ATOM   12723 C  C     . ASN C 2 235 ? 130.521 63.752  125.582 1.00 28.24 ?  214 ASN C C     1 
ATOM   12724 O  O     . ASN C 2 235 ? 131.018 62.829  124.944 1.00 28.63 ?  214 ASN C O     1 
ATOM   12725 C  CB    . ASN C 2 235 ? 129.569 65.246  123.775 1.00 28.38 ?  214 ASN C CB    1 
ATOM   12726 C  CG    . ASN C 2 235 ? 128.301 65.603  123.006 1.00 31.14 ?  214 ASN C CG    1 
ATOM   12727 O  OD1   . ASN C 2 235 ? 127.317 64.858  123.020 1.00 34.16 ?  214 ASN C OD1   1 
ATOM   12728 N  ND2   . ASN C 2 235 ? 128.320 66.748  122.335 1.00 32.42 ?  214 ASN C ND2   1 
ATOM   12729 N  N     . LYS C 2 236 ? 131.008 64.172  126.749 1.00 27.91 ?  215 LYS C N     1 
ATOM   12730 C  CA    . LYS C 2 236 ? 132.147 63.528  127.406 1.00 28.49 ?  215 LYS C CA    1 
ATOM   12731 C  C     . LYS C 2 236 ? 131.771 62.253  128.169 1.00 28.50 ?  215 LYS C C     1 
ATOM   12732 O  O     . LYS C 2 236 ? 132.645 61.478  128.566 1.00 28.98 ?  215 LYS C O     1 
ATOM   12733 C  CB    . LYS C 2 236 ? 132.840 64.502  128.365 1.00 28.10 ?  215 LYS C CB    1 
ATOM   12734 C  CG    . LYS C 2 236 ? 133.475 65.707  127.685 1.00 29.25 ?  215 LYS C CG    1 
ATOM   12735 C  CD    . LYS C 2 236 ? 134.161 66.616  128.692 1.00 30.19 ?  215 LYS C CD    1 
ATOM   12736 C  CE    . LYS C 2 236 ? 134.503 67.937  128.045 1.00 32.63 ?  215 LYS C CE    1 
ATOM   12737 N  NZ    . LYS C 2 236 ? 135.166 68.854  129.001 1.00 35.39 1  215 LYS C NZ    1 
ATOM   12738 N  N     . GLN C 2 237 ? 130.477 62.022  128.360 1.00 28.25 ?  216 GLN C N     1 
ATOM   12739 C  CA    . GLN C 2 237 ? 130.032 60.950  129.252 1.00 28.34 ?  216 GLN C CA    1 
ATOM   12740 C  C     . GLN C 2 237 ? 129.921 59.575  128.572 1.00 28.92 ?  216 GLN C C     1 
ATOM   12741 O  O     . GLN C 2 237 ? 129.827 59.482  127.348 1.00 28.53 ?  216 GLN C O     1 
ATOM   12742 C  CB    . GLN C 2 237 ? 128.709 61.346  129.924 1.00 27.68 ?  216 GLN C CB    1 
ATOM   12743 C  CG    . GLN C 2 237 ? 128.723 62.746  130.584 1.00 26.67 ?  216 GLN C CG    1 
ATOM   12744 C  CD    . GLN C 2 237 ? 129.904 62.974  131.523 1.00 25.32 ?  216 GLN C CD    1 
ATOM   12745 O  OE1   . GLN C 2 237 ? 130.250 62.110  132.332 1.00 25.49 ?  216 GLN C OE1   1 
ATOM   12746 N  NE2   . GLN C 2 237 ? 130.525 64.146  131.421 1.00 23.63 ?  216 GLN C NE2   1 
ATOM   12747 N  N     . THR C 2 238 ? 129.929 58.514  129.380 1.00 29.53 ?  217 THR C N     1 
ATOM   12748 C  CA    . THR C 2 238 ? 129.578 57.173  128.900 1.00 30.73 ?  217 THR C CA    1 
ATOM   12749 C  C     . THR C 2 238 ? 128.106 57.163  128.471 1.00 31.13 ?  217 THR C C     1 
ATOM   12750 O  O     . THR C 2 238 ? 127.334 58.069  128.836 1.00 30.17 ?  217 THR C O     1 
ATOM   12751 C  CB    . THR C 2 238 ? 129.739 56.105  129.996 1.00 30.79 ?  217 THR C CB    1 
ATOM   12752 O  OG1   . THR C 2 238 ? 128.749 56.317  131.011 1.00 31.16 ?  217 THR C OG1   1 
ATOM   12753 C  CG2   . THR C 2 238 ? 131.138 56.146  130.621 1.00 31.22 ?  217 THR C CG2   1 
ATOM   12754 N  N     . GLU C 2 239 ? 127.711 56.130  127.723 1.00 31.67 ?  218 GLU C N     1 
ATOM   12755 C  CA    . GLU C 2 239 ? 126.313 55.991  127.313 1.00 32.25 ?  218 GLU C CA    1 
ATOM   12756 C  C     . GLU C 2 239 ? 125.372 55.859  128.516 1.00 31.86 ?  218 GLU C C     1 
ATOM   12757 O  O     . GLU C 2 239 ? 124.274 56.422  128.521 1.00 31.09 ?  218 GLU C O     1 
ATOM   12758 C  CB    . GLU C 2 239 ? 126.140 54.827  126.322 1.00 33.29 ?  218 GLU C CB    1 
ATOM   12759 C  CG    . GLU C 2 239 ? 126.793 55.089  124.951 1.00 35.65 ?  218 GLU C CG    1 
ATOM   12760 C  CD    . GLU C 2 239 ? 126.240 56.337  124.253 1.00 39.17 ?  218 GLU C CD    1 
ATOM   12761 O  OE1   . GLU C 2 239 ? 124.995 56.508  124.212 1.00 41.08 ?  218 GLU C OE1   1 
ATOM   12762 O  OE2   . GLU C 2 239 ? 127.049 57.153  123.748 1.00 39.64 -1 218 GLU C OE2   1 
ATOM   12763 N  N     . GLU C 2 240 ? 125.832 55.144  129.543 1.00 31.72 ?  219 GLU C N     1 
ATOM   12764 C  CA    . GLU C 2 240 ? 125.078 54.962  130.776 1.00 31.76 ?  219 GLU C CA    1 
ATOM   12765 C  C     . GLU C 2 240 ? 124.853 56.300  131.496 1.00 30.21 ?  219 GLU C C     1 
ATOM   12766 O  O     . GLU C 2 240 ? 123.735 56.599  131.942 1.00 29.63 ?  219 GLU C O     1 
ATOM   12767 C  CB    . GLU C 2 240 ? 125.803 53.962  131.679 1.00 32.58 ?  219 GLU C CB    1 
ATOM   12768 C  CG    . GLU C 2 240 ? 125.011 53.503  132.893 1.00 36.93 ?  219 GLU C CG    1 
ATOM   12769 C  CD    . GLU C 2 240 ? 125.598 52.249  133.530 1.00 42.06 ?  219 GLU C CD    1 
ATOM   12770 O  OE1   . GLU C 2 240 ? 126.091 52.332  134.678 1.00 44.09 ?  219 GLU C OE1   1 
ATOM   12771 O  OE2   . GLU C 2 240 ? 125.574 51.178  132.880 1.00 44.45 -1 219 GLU C OE2   1 
ATOM   12772 N  N     . LYS C 2 241 ? 125.914 57.100  131.589 1.00 28.91 ?  220 LYS C N     1 
ATOM   12773 C  CA    . LYS C 2 241 ? 125.845 58.416  132.209 1.00 28.14 ?  220 LYS C CA    1 
ATOM   12774 C  C     . LYS C 2 241 ? 124.939 59.373  131.431 1.00 27.03 ?  220 LYS C C     1 
ATOM   12775 O  O     . LYS C 2 241 ? 124.162 60.121  132.033 1.00 26.72 ?  220 LYS C O     1 
ATOM   12776 C  CB    . LYS C 2 241 ? 127.242 59.021  132.376 1.00 27.83 ?  220 LYS C CB    1 
ATOM   12777 C  CG    . LYS C 2 241 ? 127.250 60.358  133.130 1.00 29.68 ?  220 LYS C CG    1 
ATOM   12778 C  CD    . LYS C 2 241 ? 127.593 60.188  134.603 1.00 33.58 ?  220 LYS C CD    1 
ATOM   12779 C  CE    . LYS C 2 241 ? 126.396 59.799  135.424 1.00 33.71 ?  220 LYS C CE    1 
ATOM   12780 N  NZ    . LYS C 2 241 ? 126.758 59.472  136.842 1.00 34.69 1  220 LYS C NZ    1 
ATOM   12781 N  N     . LYS C 2 242 ? 125.055 59.344  130.102 1.00 26.38 ?  221 LYS C N     1 
ATOM   12782 C  CA    . LYS C 2 242 ? 124.192 60.116  129.204 1.00 25.87 ?  221 LYS C CA    1 
ATOM   12783 C  C     . LYS C 2 242 ? 122.722 59.814  129.427 1.00 25.72 ?  221 LYS C C     1 
ATOM   12784 O  O     . LYS C 2 242 ? 121.897 60.737  129.482 1.00 24.52 ?  221 LYS C O     1 
ATOM   12785 C  CB    . LYS C 2 242 ? 124.538 59.855  127.737 1.00 25.83 ?  221 LYS C CB    1 
ATOM   12786 C  CG    . LYS C 2 242 ? 125.795 60.536  127.245 1.00 26.76 ?  221 LYS C CG    1 
ATOM   12787 C  CD    . LYS C 2 242 ? 125.953 60.308  125.746 1.00 28.40 ?  221 LYS C CD    1 
ATOM   12788 C  CE    . LYS C 2 242 ? 127.296 60.767  125.251 1.00 29.84 ?  221 LYS C CE    1 
ATOM   12789 N  NZ    . LYS C 2 242 ? 127.511 60.336  123.849 1.00 30.96 1  221 LYS C NZ    1 
ATOM   12790 N  N     . ALA C 2 243 ? 122.404 58.521  129.544 1.00 25.97 ?  222 ALA C N     1 
ATOM   12791 C  CA    . ALA C 2 243 ? 121.035 58.082  129.830 1.00 25.79 ?  222 ALA C CA    1 
ATOM   12792 C  C     . ALA C 2 243 ? 120.507 58.688  131.130 1.00 25.24 ?  222 ALA C C     1 
ATOM   12793 O  O     . ALA C 2 243 ? 119.346 59.120  131.190 1.00 25.37 ?  222 ALA C O     1 
ATOM   12794 C  CB    . ALA C 2 243 ? 120.949 56.555  129.853 1.00 26.17 ?  222 ALA C CB    1 
ATOM   12795 N  N     . GLU C 2 244 ? 121.352 58.752  132.157 1.00 25.02 ?  223 GLU C N     1 
ATOM   12796 C  CA    . GLU C 2 244 ? 120.975 59.399  133.423 1.00 25.08 ?  223 GLU C CA    1 
ATOM   12797 C  C     . GLU C 2 244 ? 120.784 60.919  133.275 1.00 24.70 ?  223 GLU C C     1 
ATOM   12798 O  O     . GLU C 2 244 ? 119.868 61.504  133.871 1.00 24.20 ?  223 GLU C O     1 
ATOM   12799 C  CB    . GLU C 2 244 ? 121.994 59.095  134.527 1.00 25.35 ?  223 GLU C CB    1 
ATOM   12800 C  CG    . GLU C 2 244 ? 121.611 59.702  135.888 1.00 26.67 ?  223 GLU C CG    1 
ATOM   12801 C  CD    . GLU C 2 244 ? 122.738 59.653  136.903 1.00 28.29 ?  223 GLU C CD    1 
ATOM   12802 O  OE1   . GLU C 2 244 ? 123.639 58.802  136.774 1.00 29.51 ?  223 GLU C OE1   1 
ATOM   12803 O  OE2   . GLU C 2 244 ? 122.723 60.477  137.836 1.00 29.09 -1 223 GLU C OE2   1 
ATOM   12804 N  N     . LEU C 2 245 ? 121.652 61.553  132.492 1.00 24.27 ?  224 LEU C N     1 
ATOM   12805 C  CA    . LEU C 2 245 ? 121.554 62.996  132.266 1.00 24.54 ?  224 LEU C CA    1 
ATOM   12806 C  C     . LEU C 2 245 ? 120.280 63.394  131.506 1.00 24.42 ?  224 LEU C C     1 
ATOM   12807 O  O     . LEU C 2 245 ? 119.672 64.423  131.808 1.00 24.10 ?  224 LEU C O     1 
ATOM   12808 C  CB    . LEU C 2 245 ? 122.825 63.534  131.582 1.00 23.86 ?  224 LEU C CB    1 
ATOM   12809 C  CG    . LEU C 2 245 ? 124.105 63.481  132.427 1.00 24.78 ?  224 LEU C CG    1 
ATOM   12810 C  CD1   . LEU C 2 245 ? 125.288 64.094  131.669 1.00 25.54 ?  224 LEU C CD1   1 
ATOM   12811 C  CD2   . LEU C 2 245 ? 123.934 64.168  133.790 1.00 25.29 ?  224 LEU C CD2   1 
ATOM   12812 N  N     . ARG C 2 246 ? 119.878 62.570  130.539 1.00 25.26 ?  225 ARG C N     1 
ATOM   12813 C  CA    . ARG C 2 246 ? 118.605 62.762  129.830 1.00 25.97 ?  225 ARG C CA    1 
ATOM   12814 C  C     . ARG C 2 246 ? 117.438 62.625  130.798 1.00 25.85 ?  225 ARG C C     1 
ATOM   12815 O  O     . ARG C 2 246 ? 116.496 63.418  130.747 1.00 25.01 ?  225 ARG C O     1 
ATOM   12816 C  CB    . ARG C 2 246 ? 118.450 61.779  128.650 1.00 26.65 ?  225 ARG C CB    1 
ATOM   12817 C  CG    . ARG C 2 246 ? 119.445 62.013  127.516 1.00 28.90 ?  225 ARG C CG    1 
ATOM   12818 C  CD    . ARG C 2 246 ? 119.051 61.307  126.196 1.00 31.26 ?  225 ARG C CD    1 
ATOM   12819 N  NE    . ARG C 2 246 ? 118.934 59.853  126.336 1.00 34.01 ?  225 ARG C NE    1 
ATOM   12820 C  CZ    . ARG C 2 246 ? 119.962 59.006  126.400 1.00 35.64 ?  225 ARG C CZ    1 
ATOM   12821 N  NH1   . ARG C 2 246 ? 121.212 59.449  126.342 1.00 36.11 1  225 ARG C NH1   1 
ATOM   12822 N  NH2   . ARG C 2 246 ? 119.735 57.704  126.525 1.00 37.05 ?  225 ARG C NH2   1 
ATOM   12823 N  N     . GLU C 2 247 ? 117.508 61.629  131.685 1.00 26.01 ?  226 GLU C N     1 
ATOM   12824 C  CA    . GLU C 2 247 ? 116.500 61.459  132.738 1.00 26.48 ?  226 GLU C CA    1 
ATOM   12825 C  C     . GLU C 2 247 ? 116.414 62.705  133.618 1.00 25.72 ?  226 GLU C C     1 
ATOM   12826 O  O     . GLU C 2 247 ? 115.312 63.204  133.892 1.00 25.16 ?  226 GLU C O     1 
ATOM   12827 C  CB    . GLU C 2 247 ? 116.797 60.240  133.616 1.00 27.18 ?  226 GLU C CB    1 
ATOM   12828 C  CG    . GLU C 2 247 ? 115.589 59.784  134.426 1.00 30.38 ?  226 GLU C CG    1 
ATOM   12829 C  CD    . GLU C 2 247 ? 115.923 59.273  135.814 1.00 35.77 ?  226 GLU C CD    1 
ATOM   12830 O  OE1   . GLU C 2 247 ? 117.034 58.745  136.037 1.00 38.02 ?  226 GLU C OE1   1 
ATOM   12831 O  OE2   . GLU C 2 247 ? 115.051 59.398  136.702 1.00 40.39 -1 226 GLU C OE2   1 
ATOM   12832 N  N     . PHE C 2 248 ? 117.573 63.204  134.052 1.00 24.71 ?  227 PHE C N     1 
ATOM   12833 C  CA    . PHE C 2 248 ? 117.621 64.429  134.849 1.00 23.71 ?  227 PHE C CA    1 
ATOM   12834 C  C     . PHE C 2 248 ? 116.937 65.577  134.105 1.00 23.14 ?  227 PHE C C     1 
ATOM   12835 O  O     . PHE C 2 248 ? 116.095 66.271  134.677 1.00 22.40 ?  227 PHE C O     1 
ATOM   12836 C  CB    . PHE C 2 248 ? 119.060 64.829  135.220 1.00 23.85 ?  227 PHE C CB    1 
ATOM   12837 C  CG    . PHE C 2 248 ? 119.168 66.244  135.729 1.00 23.64 ?  227 PHE C CG    1 
ATOM   12838 C  CD1   . PHE C 2 248 ? 118.883 66.536  137.065 1.00 23.07 ?  227 PHE C CD1   1 
ATOM   12839 C  CD2   . PHE C 2 248 ? 119.484 67.297  134.853 1.00 23.04 ?  227 PHE C CD2   1 
ATOM   12840 C  CE1   . PHE C 2 248 ? 118.952 67.845  137.542 1.00 22.73 ?  227 PHE C CE1   1 
ATOM   12841 C  CE2   . PHE C 2 248 ? 119.549 68.613  135.312 1.00 23.31 ?  227 PHE C CE2   1 
ATOM   12842 C  CZ    . PHE C 2 248 ? 119.286 68.892  136.664 1.00 21.51 ?  227 PHE C CZ    1 
ATOM   12843 N  N     . ALA C 2 249 ? 117.300 65.759  132.834 1.00 22.95 ?  228 ALA C N     1 
ATOM   12844 C  CA    . ALA C 2 249 ? 116.814 66.893  132.037 1.00 22.96 ?  228 ALA C CA    1 
ATOM   12845 C  C     . ALA C 2 249 ? 115.304 66.828  131.824 1.00 23.31 ?  228 ALA C C     1 
ATOM   12846 O  O     . ALA C 2 249 ? 114.606 67.837  131.944 1.00 22.63 ?  228 ALA C O     1 
ATOM   12847 C  CB    . ALA C 2 249 ? 117.541 66.959  130.695 1.00 22.40 ?  228 ALA C CB    1 
ATOM   12848 N  N     . ILE C 2 250 ? 114.813 65.634  131.512 1.00 23.66 ?  229 ILE C N     1 
ATOM   12849 C  CA    . ILE C 2 250 ? 113.385 65.419  131.272 1.00 25.00 ?  229 ILE C CA    1 
ATOM   12850 C  C     . ILE C 2 250 ? 112.564 65.498  132.567 1.00 24.64 ?  229 ILE C C     1 
ATOM   12851 O  O     . ILE C 2 250 ? 111.507 66.140  132.591 1.00 24.26 ?  229 ILE C O     1 
ATOM   12852 C  CB    . ILE C 2 250 ? 113.132 64.111  130.459 1.00 25.43 ?  229 ILE C CB    1 
ATOM   12853 C  CG1   . ILE C 2 250 ? 113.604 64.317  129.013 1.00 27.27 ?  229 ILE C CG1   1 
ATOM   12854 C  CG2   . ILE C 2 250 ? 111.620 63.755  130.437 1.00 27.62 ?  229 ILE C CG2   1 
ATOM   12855 C  CD1   . ILE C 2 250 ? 114.228 63.081  128.350 1.00 31.32 ?  229 ILE C CD1   1 
ATOM   12856 N  N     . ASP C 2 251 ? 113.059 64.887  133.643 1.00 24.78 ?  230 ASP C N     1 
ATOM   12857 C  CA    . ASP C 2 251 ? 112.407 65.021  134.960 1.00 25.20 ?  230 ASP C CA    1 
ATOM   12858 C  C     . ASP C 2 251 ? 112.328 66.479  135.413 1.00 24.08 ?  230 ASP C C     1 
ATOM   12859 O  O     . ASP C 2 251 ? 111.301 66.924  135.949 1.00 23.34 ?  230 ASP C O     1 
ATOM   12860 C  CB    . ASP C 2 251 ? 113.152 64.230  136.044 1.00 25.73 ?  230 ASP C CB    1 
ATOM   12861 C  CG    . ASP C 2 251 ? 112.911 62.741  135.961 1.00 28.78 ?  230 ASP C CG    1 
ATOM   12862 O  OD1   . ASP C 2 251 ? 112.084 62.292  135.133 1.00 29.99 ?  230 ASP C OD1   1 
ATOM   12863 O  OD2   . ASP C 2 251 ? 113.567 62.014  136.737 1.00 33.31 -1 230 ASP C OD2   1 
ATOM   12864 N  N     . LEU C 2 252 ? 113.418 67.215  135.214 1.00 22.98 ?  231 LEU C N     1 
ATOM   12865 C  CA    . LEU C 2 252 ? 113.449 68.625  135.606 1.00 21.63 ?  231 LEU C CA    1 
ATOM   12866 C  C     . LEU C 2 252 ? 112.474 69.433  134.758 1.00 21.66 ?  231 LEU C C     1 
ATOM   12867 O  O     . LEU C 2 252 ? 111.751 70.292  135.266 1.00 19.41 ?  231 LEU C O     1 
ATOM   12868 C  CB    . LEU C 2 252 ? 114.856 69.206  135.470 1.00 21.89 ?  231 LEU C CB    1 
ATOM   12869 C  CG    . LEU C 2 252 ? 115.029 70.708  135.763 1.00 21.33 ?  231 LEU C CG    1 
ATOM   12870 C  CD1   . LEU C 2 252 ? 114.573 71.072  137.192 1.00 20.89 ?  231 LEU C CD1   1 
ATOM   12871 C  CD2   . LEU C 2 252 ? 116.489 71.102  135.522 1.00 20.31 ?  231 LEU C CD2   1 
ATOM   12872 N  N     . LEU C 2 253 ? 112.465 69.156  133.457 1.00 22.28 ?  232 LEU C N     1 
ATOM   12873 C  CA    . LEU C 2 253 ? 111.570 69.874  132.556 1.00 23.05 ?  232 LEU C CA    1 
ATOM   12874 C  C     . LEU C 2 253 ? 110.114 69.655  132.953 1.00 23.36 ?  232 LEU C C     1 
ATOM   12875 O  O     . LEU C 2 253 ? 109.352 70.629  133.083 1.00 22.96 ?  232 LEU C O     1 
ATOM   12876 C  CB    . LEU C 2 253 ? 111.811 69.475  131.099 1.00 23.53 ?  232 LEU C CB    1 
ATOM   12877 C  CG    . LEU C 2 253 ? 110.905 70.203  130.098 1.00 25.63 ?  232 LEU C CG    1 
ATOM   12878 C  CD1   . LEU C 2 253 ? 111.176 71.708  130.081 1.00 25.88 ?  232 LEU C CD1   1 
ATOM   12879 C  CD2   . LEU C 2 253 ? 111.091 69.603  128.712 1.00 27.67 ?  232 LEU C CD2   1 
ATOM   12880 N  N     . ASN C 2 254 ? 109.737 68.389  133.161 1.00 23.55 ?  233 ASN C N     1 
ATOM   12881 C  CA    . ASN C 2 254 ? 108.373 68.051  133.607 1.00 24.61 ?  233 ASN C CA    1 
ATOM   12882 C  C     . ASN C 2 254 ? 107.980 68.708  134.932 1.00 23.57 ?  233 ASN C C     1 
ATOM   12883 O  O     . ASN C 2 254 ? 106.864 69.202  135.083 1.00 23.52 ?  233 ASN C O     1 
ATOM   12884 C  CB    . ASN C 2 254 ? 108.175 66.535  133.684 1.00 24.99 ?  233 ASN C CB    1 
ATOM   12885 C  CG    . ASN C 2 254 ? 107.793 65.925  132.341 1.00 28.92 ?  233 ASN C CG    1 
ATOM   12886 O  OD1   . ASN C 2 254 ? 106.794 66.305  131.727 1.00 33.75 ?  233 ASN C OD1   1 
ATOM   12887 N  ND2   . ASN C 2 254 ? 108.586 64.974  131.885 1.00 30.99 ?  233 ASN C ND2   1 
ATOM   12888 N  N     . GLN C 2 255 ? 108.901 68.718  135.891 1.00 23.22 ?  234 GLN C N     1 
ATOM   12889 C  CA    . GLN C 2 255 ? 108.636 69.359  137.172 1.00 22.54 ?  234 GLN C CA    1 
ATOM   12890 C  C     . GLN C 2 255 ? 108.417 70.878  137.013 1.00 22.00 ?  234 GLN C C     1 
ATOM   12891 O  O     . GLN C 2 255 ? 107.480 71.452  137.595 1.00 21.73 ?  234 GLN C O     1 
ATOM   12892 C  CB    . GLN C 2 255 ? 109.767 69.069  138.158 1.00 22.85 ?  234 GLN C CB    1 
ATOM   12893 C  CG    . GLN C 2 255 ? 109.427 69.438  139.587 1.00 23.87 ?  234 GLN C CG    1 
ATOM   12894 C  CD    . GLN C 2 255 ? 110.569 69.177  140.561 1.00 24.95 ?  234 GLN C CD    1 
ATOM   12895 O  OE1   . GLN C 2 255 ? 111.579 68.557  140.209 1.00 24.21 ?  234 GLN C OE1   1 
ATOM   12896 N  NE2   . GLN C 2 255 ? 110.421 69.677  141.790 1.00 25.97 ?  234 GLN C NE2   1 
ATOM   12897 N  N     . LEU C 2 256 ? 109.277 71.519  136.230 1.00 21.27 ?  235 LEU C N     1 
ATOM   12898 C  CA    . LEU C 2 256 ? 109.134 72.943  135.945 1.00 21.37 ?  235 LEU C CA    1 
ATOM   12899 C  C     . LEU C 2 256 ? 107.854 73.216  135.150 1.00 21.21 ?  235 LEU C C     1 
ATOM   12900 O  O     . LEU C 2 256 ? 107.155 74.198  135.396 1.00 20.75 ?  235 LEU C O     1 
ATOM   12901 C  CB    . LEU C 2 256 ? 110.353 73.447  135.160 1.00 20.93 ?  235 LEU C CB    1 
ATOM   12902 C  CG    . LEU C 2 256 ? 111.694 73.584  135.886 1.00 21.74 ?  235 LEU C CG    1 
ATOM   12903 C  CD1   . LEU C 2 256 ? 112.792 73.977  134.886 1.00 20.15 ?  235 LEU C CD1   1 
ATOM   12904 C  CD2   . LEU C 2 256 ? 111.628 74.589  137.036 1.00 20.90 ?  235 LEU C CD2   1 
ATOM   12905 N  N     . TYR C 2 257 ? 107.575 72.343  134.189 1.00 21.68 ?  236 TYR C N     1 
ATOM   12906 C  CA    . TYR C 2 257 ? 106.392 72.456  133.335 1.00 22.40 ?  236 TYR C CA    1 
ATOM   12907 C  C     . TYR C 2 257 ? 105.096 72.434  134.163 1.00 23.31 ?  236 TYR C C     1 
ATOM   12908 O  O     . TYR C 2 257 ? 104.242 73.330  134.013 1.00 22.99 ?  236 TYR C O     1 
ATOM   12909 C  CB    . TYR C 2 257 ? 106.399 71.350  132.276 1.00 22.81 ?  236 TYR C CB    1 
ATOM   12910 C  CG    . TYR C 2 257 ? 105.152 71.275  131.417 1.00 23.76 ?  236 TYR C CG    1 
ATOM   12911 C  CD1   . TYR C 2 257 ? 104.836 72.297  130.517 1.00 24.05 ?  236 TYR C CD1   1 
ATOM   12912 C  CD2   . TYR C 2 257 ? 104.284 70.190  131.515 1.00 24.04 ?  236 TYR C CD2   1 
ATOM   12913 C  CE1   . TYR C 2 257 ? 103.687 72.239  129.736 1.00 24.40 ?  236 TYR C CE1   1 
ATOM   12914 C  CE2   . TYR C 2 257 ? 103.132 70.123  130.734 1.00 26.30 ?  236 TYR C CE2   1 
ATOM   12915 C  CZ    . TYR C 2 257 ? 102.852 71.146  129.847 1.00 25.80 ?  236 TYR C CZ    1 
ATOM   12916 O  OH    . TYR C 2 257 ? 101.726 71.072  129.076 1.00 28.42 ?  236 TYR C OH    1 
ATOM   12917 N  N     . GLU C 2 258 ? 104.973 71.449  135.057 1.00 22.99 ?  237 GLU C N     1 
ATOM   12918 C  CA    . GLU C 2 258 ? 103.777 71.311  135.896 1.00 24.46 ?  237 GLU C CA    1 
ATOM   12919 C  C     . GLU C 2 258 ? 103.551 72.537  136.765 1.00 23.86 ?  237 GLU C C     1 
ATOM   12920 O  O     . GLU C 2 258 ? 102.420 73.000  136.909 1.00 24.01 ?  237 GLU C O     1 
ATOM   12921 C  CB    . GLU C 2 258 ? 103.820 70.027  136.744 1.00 25.21 ?  237 GLU C CB    1 
ATOM   12922 C  CG    . GLU C 2 258 ? 103.686 68.730  135.912 1.00 30.12 ?  237 GLU C CG    1 
ATOM   12923 C  CD    . GLU C 2 258 ? 102.316 68.585  135.243 1.00 35.29 ?  237 GLU C CD    1 
ATOM   12924 O  OE1   . GLU C 2 258 ? 101.312 69.103  135.783 1.00 37.71 ?  237 GLU C OE1   1 
ATOM   12925 O  OE2   . GLU C 2 258 ? 102.242 67.942  134.169 1.00 39.07 -1 237 GLU C OE2   1 
ATOM   12926 N  N     . ASN C 2 259 ? 104.634 73.080  137.320 1.00 23.25 ?  238 ASN C N     1 
ATOM   12927 C  CA    . ASN C 2 259 ? 104.561 74.326  138.079 1.00 23.10 ?  238 ASN C CA    1 
ATOM   12928 C  C     . ASN C 2 259 ? 104.166 75.515  137.184 1.00 22.68 ?  238 ASN C C     1 
ATOM   12929 O  O     . ASN C 2 259 ? 103.358 76.362  137.576 1.00 22.73 ?  238 ASN C O     1 
ATOM   12930 C  CB    . ASN C 2 259 ? 105.893 74.581  138.789 1.00 23.22 ?  238 ASN C CB    1 
ATOM   12931 C  CG    . ASN C 2 259 ? 105.873 75.841  139.629 1.00 24.46 ?  238 ASN C CG    1 
ATOM   12932 O  OD1   . ASN C 2 259 ? 105.208 75.904  140.668 1.00 26.28 ?  238 ASN C OD1   1 
ATOM   12933 N  ND2   . ASN C 2 259 ? 106.605 76.856  139.184 1.00 24.93 ?  238 ASN C ND2   1 
ATOM   12934 N  N     . GLU C 2 260 ? 104.715 75.562  135.972 1.00 22.64 ?  239 GLU C N     1 
ATOM   12935 C  CA    . GLU C 2 260 ? 104.432 76.662  135.049 1.00 23.18 ?  239 GLU C CA    1 
ATOM   12936 C  C     . GLU C 2 260 ? 102.961 76.668  134.598 1.00 23.40 ?  239 GLU C C     1 
ATOM   12937 O  O     . GLU C 2 260 ? 102.368 77.740  134.395 1.00 23.57 ?  239 GLU C O     1 
ATOM   12938 C  CB    . GLU C 2 260 ? 105.378 76.625  133.841 1.00 23.19 ?  239 GLU C CB    1 
ATOM   12939 C  CG    . GLU C 2 260 ? 105.632 78.009  133.196 1.00 24.33 ?  239 GLU C CG    1 
ATOM   12940 C  CD    . GLU C 2 260 ? 106.366 78.994  134.124 1.00 27.99 ?  239 GLU C CD    1 
ATOM   12941 O  OE1   . GLU C 2 260 ? 106.823 78.602  135.220 1.00 27.36 ?  239 GLU C OE1   1 
ATOM   12942 O  OE2   . GLU C 2 260 ? 106.479 80.184  133.756 1.00 28.98 -1 239 GLU C OE2   1 
ATOM   12943 N  N     . LEU C 2 261 ? 102.377 75.478  134.456 1.00 23.35 ?  240 LEU C N     1 
ATOM   12944 C  CA    . LEU C 2 261 ? 100.942 75.354  134.157 1.00 23.74 ?  240 LEU C CA    1 
ATOM   12945 C  C     . LEU C 2 261 ? 100.070 76.056  135.202 1.00 23.80 ?  240 LEU C C     1 
ATOM   12946 O  O     . LEU C 2 261 ? 99.161  76.828  134.858 1.00 23.33 ?  240 LEU C O     1 
ATOM   12947 C  CB    . LEU C 2 261 ? 100.527 73.884  134.041 1.00 24.09 ?  240 LEU C CB    1 
ATOM   12948 C  CG    . LEU C 2 261 ? 101.042 73.106  132.830 1.00 24.07 ?  240 LEU C CG    1 
ATOM   12949 C  CD1   . LEU C 2 261 ? 100.546 71.667  132.894 1.00 24.77 ?  240 LEU C CD1   1 
ATOM   12950 C  CD2   . LEU C 2 261 ? 100.612 73.781  131.512 1.00 24.38 ?  240 LEU C CD2   1 
ATOM   12951 N  N     . GLU C 2 262 ? 100.347 75.777  136.470 1.00 23.41 ?  241 GLU C N     1 
ATOM   12952 C  CA    . GLU C 2 262 ? 99.620  76.402  137.573 1.00 24.02 ?  241 GLU C CA    1 
ATOM   12953 C  C     . GLU C 2 262 ? 99.833  77.924  137.616 1.00 22.91 ?  241 GLU C C     1 
ATOM   12954 O  O     . GLU C 2 262 ? 98.891  78.672  137.841 1.00 22.94 ?  241 GLU C O     1 
ATOM   12955 C  CB    . GLU C 2 262 ? 100.039 75.766  138.899 1.00 24.92 ?  241 GLU C CB    1 
ATOM   12956 C  CG    . GLU C 2 262 ? 99.648  74.305  139.044 1.00 27.82 ?  241 GLU C CG    1 
ATOM   12957 C  CD    . GLU C 2 262 ? 100.058 73.728  140.388 1.00 33.08 ?  241 GLU C CD    1 
ATOM   12958 O  OE1   . GLU C 2 262 ? 101.239 73.345  140.555 1.00 36.94 ?  241 GLU C OE1   1 
ATOM   12959 O  OE2   . GLU C 2 262 ? 99.194  73.650  141.280 1.00 37.48 -1 241 GLU C OE2   1 
ATOM   12960 N  N     . TYR C 2 263 ? 101.077 78.361  137.407 1.00 21.84 ?  242 TYR C N     1 
ATOM   12961 C  CA    . TYR C 2 263 ? 101.425 79.777  137.302 1.00 21.66 ?  242 TYR C CA    1 
ATOM   12962 C  C     . TYR C 2 263 ? 100.666 80.441  136.160 1.00 21.28 ?  242 TYR C C     1 
ATOM   12963 O  O     . TYR C 2 263 ? 100.122 81.543  136.320 1.00 21.14 ?  242 TYR C O     1 
ATOM   12964 C  CB    . TYR C 2 263 ? 102.933 79.923  137.047 1.00 21.44 ?  242 TYR C CB    1 
ATOM   12965 C  CG    . TYR C 2 263 ? 103.462 81.347  136.937 1.00 21.89 ?  242 TYR C CG    1 
ATOM   12966 C  CD1   . TYR C 2 263 ? 103.523 82.179  138.055 1.00 22.52 ?  242 TYR C CD1   1 
ATOM   12967 C  CD2   . TYR C 2 263 ? 103.936 81.844  135.720 1.00 22.58 ?  242 TYR C CD2   1 
ATOM   12968 C  CE1   . TYR C 2 263 ? 104.030 83.476  137.961 1.00 22.67 ?  242 TYR C CE1   1 
ATOM   12969 C  CE2   . TYR C 2 263 ? 104.450 83.142  135.615 1.00 24.03 ?  242 TYR C CE2   1 
ATOM   12970 C  CZ    . TYR C 2 263 ? 104.500 83.946  136.749 1.00 23.75 ?  242 TYR C CZ    1 
ATOM   12971 O  OH    . TYR C 2 263 ? 104.998 85.231  136.667 1.00 26.82 ?  242 TYR C OH    1 
ATOM   12972 N  N     . THR C 2 264 ? 100.638 79.770  135.011 1.00 20.66 ?  243 THR C N     1 
ATOM   12973 C  CA    . THR C 2 264 ? 99.965  80.299  133.816 1.00 20.99 ?  243 THR C CA    1 
ATOM   12974 C  C     . THR C 2 264 ? 98.462  80.472  134.066 1.00 21.22 ?  243 THR C C     1 
ATOM   12975 O  O     . THR C 2 264 ? 97.893  81.530  133.753 1.00 20.95 ?  243 THR C O     1 
ATOM   12976 C  CB    . THR C 2 264 ? 100.219 79.394  132.580 1.00 20.58 ?  243 THR C CB    1 
ATOM   12977 O  OG1   . THR C 2 264 ? 101.611 79.433  132.252 1.00 20.84 ?  243 THR C OG1   1 
ATOM   12978 C  CG2   . THR C 2 264 ? 99.414  79.863  131.366 1.00 20.90 ?  243 THR C CG2   1 
ATOM   12979 N  N     . GLU C 2 265 ? 97.831  79.454  134.653 1.00 21.62 ?  244 GLU C N     1 
ATOM   12980 C  CA    . GLU C 2 265 ? 96.404  79.534  134.965 1.00 23.46 ?  244 GLU C CA    1 
ATOM   12981 C  C     . GLU C 2 265 ? 96.115  80.651  135.948 1.00 23.33 ?  244 GLU C C     1 
ATOM   12982 O  O     . GLU C 2 265 ? 95.159  81.410  135.786 1.00 22.86 ?  244 GLU C O     1 
ATOM   12983 C  CB    . GLU C 2 265 ? 95.871  78.208  135.510 1.00 24.31 ?  244 GLU C CB    1 
ATOM   12984 C  CG    . GLU C 2 265 ? 95.765  77.115  134.453 1.00 27.63 ?  244 GLU C CG    1 
ATOM   12985 C  CD    . GLU C 2 265 ? 95.221  75.805  135.017 1.00 33.27 ?  244 GLU C CD    1 
ATOM   12986 O  OE1   . GLU C 2 265 ? 94.429  75.846  135.985 1.00 35.56 ?  244 GLU C OE1   1 
ATOM   12987 O  OE2   . GLU C 2 265 ? 95.581  74.732  134.481 1.00 35.96 -1 244 GLU C OE2   1 
ATOM   12988 N  N     . ASP C 2 266 ? 96.958  80.753  136.965 1.00 23.36 ?  245 ASP C N     1 
ATOM   12989 C  CA    . ASP C 2 266 ? 96.815  81.790  137.973 1.00 24.18 ?  245 ASP C CA    1 
ATOM   12990 C  C     . ASP C 2 266 ? 96.840  83.205  137.363 1.00 23.96 ?  245 ASP C C     1 
ATOM   12991 O  O     . ASP C 2 266 ? 96.064  84.071  137.760 1.00 24.19 ?  245 ASP C O     1 
ATOM   12992 C  CB    . ASP C 2 266 ? 97.924  81.639  139.011 1.00 25.14 ?  245 ASP C CB    1 
ATOM   12993 C  CG    . ASP C 2 266 ? 97.707  82.508  140.211 1.00 27.35 ?  245 ASP C CG    1 
ATOM   12994 O  OD1   . ASP C 2 266 ? 96.632  82.397  140.838 1.00 28.45 ?  245 ASP C OD1   1 
ATOM   12995 O  OD2   . ASP C 2 266 ? 98.617  83.306  140.523 1.00 31.99 -1 245 ASP C OD2   1 
ATOM   12996 N  N     . LEU C 2 267 ? 97.716  83.427  136.391 1.00 23.34 ?  246 LEU C N     1 
ATOM   12997 C  CA    . LEU C 2 267 ? 97.842  84.748  135.765 1.00 23.53 ?  246 LEU C CA    1 
ATOM   12998 C  C     . LEU C 2 267 ? 96.850  85.019  134.645 1.00 22.94 ?  246 LEU C C     1 
ATOM   12999 O  O     . LEU C 2 267 ? 96.315  86.123  134.542 1.00 23.14 ?  246 LEU C O     1 
ATOM   13000 C  CB    . LEU C 2 267 ? 99.257  84.942  135.226 1.00 23.37 ?  246 LEU C CB    1 
ATOM   13001 C  CG    . LEU C 2 267 ? 100.378 85.142  136.249 1.00 26.17 ?  246 LEU C CG    1 
ATOM   13002 C  CD1   . LEU C 2 267 ? 101.678 85.336  135.501 1.00 27.31 ?  246 LEU C CD1   1 
ATOM   13003 C  CD2   . LEU C 2 267 ? 100.095 86.352  137.133 1.00 28.08 ?  246 LEU C CD2   1 
ATOM   13004 N  N     . TYR C 2 268 ? 96.629  84.019  133.795 1.00 22.46 ?  247 TYR C N     1 
ATOM   13005 C  CA    . TYR C 2 268 ? 95.893  84.233  132.553 1.00 22.00 ?  247 TYR C CA    1 
ATOM   13006 C  C     . TYR C 2 268 ? 94.407  83.916  132.544 1.00 22.26 ?  247 TYR C C     1 
ATOM   13007 O  O     . TYR C 2 268 ? 93.714  84.347  131.622 1.00 22.17 ?  247 TYR C O     1 
ATOM   13008 C  CB    . TYR C 2 268 ? 96.578  83.502  131.390 1.00 21.73 ?  247 TYR C CB    1 
ATOM   13009 C  CG    . TYR C 2 268 ? 97.885  84.131  130.972 1.00 21.49 ?  247 TYR C CG    1 
ATOM   13010 C  CD1   . TYR C 2 268 ? 99.106  83.591  131.391 1.00 19.45 ?  247 TYR C CD1   1 
ATOM   13011 C  CD2   . TYR C 2 268 ? 97.903  85.277  130.169 1.00 22.71 ?  247 TYR C CD2   1 
ATOM   13012 C  CE1   . TYR C 2 268 ? 100.317 84.178  131.013 1.00 20.30 ?  247 TYR C CE1   1 
ATOM   13013 C  CE2   . TYR C 2 268 ? 99.112  85.875  129.776 1.00 21.69 ?  247 TYR C CE2   1 
ATOM   13014 C  CZ    . TYR C 2 268 ? 100.308 85.309  130.193 1.00 21.40 ?  247 TYR C CZ    1 
ATOM   13015 O  OH    . TYR C 2 268 ? 101.489 85.887  129.804 1.00 22.11 ?  247 TYR C OH    1 
ATOM   13016 N  N     . ASP C 2 269 ? 93.909  83.154  133.524 1.00 22.40 ?  248 ASP C N     1 
ATOM   13017 C  CA    . ASP C 2 269 ? 92.467  82.854  133.564 1.00 22.75 ?  248 ASP C CA    1 
ATOM   13018 C  C     . ASP C 2 269 ? 91.617  84.126  133.562 1.00 22.55 ?  248 ASP C C     1 
ATOM   13019 O  O     . ASP C 2 269 ? 90.569  84.170  132.907 1.00 22.22 ?  248 ASP C O     1 
ATOM   13020 C  CB    . ASP C 2 269 ? 92.083  81.951  134.752 1.00 23.03 ?  248 ASP C CB    1 
ATOM   13021 C  CG    . ASP C 2 269 ? 92.362  80.480  134.492 1.00 25.02 ?  248 ASP C CG    1 
ATOM   13022 O  OD1   . ASP C 2 269 ? 92.664  80.098  133.342 1.00 26.85 ?  248 ASP C OD1   1 
ATOM   13023 O  OD2   . ASP C 2 269 ? 92.271  79.689  135.453 1.00 28.74 -1 248 ASP C OD2   1 
ATOM   13024 N  N     . GLN C 2 270 ? 92.074  85.158  134.276 1.00 22.21 ?  249 GLN C N     1 
ATOM   13025 C  CA    . GLN C 2 270 ? 91.315  86.428  134.351 1.00 22.39 ?  249 GLN C CA    1 
ATOM   13026 C  C     . GLN C 2 270 ? 91.280  87.227  133.041 1.00 21.65 ?  249 GLN C C     1 
ATOM   13027 O  O     . GLN C 2 270 ? 90.494  88.166  132.915 1.00 21.70 ?  249 GLN C O     1 
ATOM   13028 C  CB    . GLN C 2 270 ? 91.790  87.313  135.513 1.00 22.53 ?  249 GLN C CB    1 
ATOM   13029 C  CG    . GLN C 2 270 ? 93.265  87.785  135.446 1.00 22.73 ?  249 GLN C CG    1 
ATOM   13030 C  CD    . GLN C 2 270 ? 93.632  88.650  136.634 1.00 25.39 ?  249 GLN C CD    1 
ATOM   13031 O  OE1   . GLN C 2 270 ? 92.925  88.664  137.643 1.00 27.88 ?  249 GLN C OE1   1 
ATOM   13032 N  NE2   . GLN C 2 270 ? 94.734  89.387  136.523 1.00 24.88 ?  249 GLN C NE2   1 
ATOM   13033 N  N     . VAL C 2 271 ? 92.128  86.857  132.079 1.00 20.91 ?  250 VAL C N     1 
ATOM   13034 C  CA    . VAL C 2 271 ? 92.138  87.503  130.747 1.00 20.62 ?  250 VAL C CA    1 
ATOM   13035 C  C     . VAL C 2 271 ? 91.767  86.517  129.624 1.00 20.53 ?  250 VAL C C     1 
ATOM   13036 O  O     . VAL C 2 271 ? 91.752  86.878  128.436 1.00 20.05 ?  250 VAL C O     1 
ATOM   13037 C  CB    . VAL C 2 271 ? 93.481  88.266  130.439 1.00 20.32 ?  250 VAL C CB    1 
ATOM   13038 C  CG1   . VAL C 2 271 ? 93.676  89.433  131.401 1.00 20.35 ?  250 VAL C CG1   1 
ATOM   13039 C  CG2   . VAL C 2 271 ? 94.702  87.335  130.490 1.00 19.32 ?  250 VAL C CG2   1 
ATOM   13040 N  N     . GLY C 2 272 ? 91.459  85.279  130.016 1.00 20.29 ?  251 GLY C N     1 
ATOM   13041 C  CA    . GLY C 2 272 ? 90.908  84.273  129.104 1.00 20.51 ?  251 GLY C CA    1 
ATOM   13042 C  C     . GLY C 2 272 ? 91.901  83.589  128.179 1.00 20.99 ?  251 GLY C C     1 
ATOM   13043 O  O     . GLY C 2 272 ? 91.507  83.040  127.137 1.00 20.22 ?  251 GLY C O     1 
ATOM   13044 N  N     . LEU C 2 273 ? 93.186  83.613  128.546 1.00 20.76 ?  252 LEU C N     1 
ATOM   13045 C  CA    . LEU C 2 273 ? 94.235  83.194  127.611 1.00 21.38 ?  252 LEU C CA    1 
ATOM   13046 C  C     . LEU C 2 273 ? 95.063  81.980  128.024 1.00 21.86 ?  252 LEU C C     1 
ATOM   13047 O  O     . LEU C 2 273 ? 96.023  81.630  127.340 1.00 22.45 ?  252 LEU C O     1 
ATOM   13048 C  CB    . LEU C 2 273 ? 95.159  84.376  127.268 1.00 21.44 ?  252 LEU C CB    1 
ATOM   13049 C  CG    . LEU C 2 273 ? 94.546  85.634  126.650 1.00 22.02 ?  252 LEU C CG    1 
ATOM   13050 C  CD1   . LEU C 2 273 ? 95.628  86.692  126.467 1.00 22.86 ?  252 LEU C CD1   1 
ATOM   13051 C  CD2   . LEU C 2 273 ? 93.847  85.317  125.309 1.00 23.88 ?  252 LEU C CD2   1 
ATOM   13052 N  N     . SER C 2 274 ? 94.688  81.321  129.119 1.00 22.19 ?  253 SER C N     1 
ATOM   13053 C  CA    . SER C 2 274 ? 95.545  80.299  129.715 1.00 22.47 ?  253 SER C CA    1 
ATOM   13054 C  C     . SER C 2 274 ? 95.892  79.162  128.753 1.00 22.94 ?  253 SER C C     1 
ATOM   13055 O  O     . SER C 2 274 ? 97.047  78.760  128.658 1.00 22.07 ?  253 SER C O     1 
ATOM   13056 C  CB    . SER C 2 274 ? 94.908  79.742  130.991 1.00 22.91 ?  253 SER C CB    1 
ATOM   13057 O  OG    . SER C 2 274 ? 94.899  80.740  131.993 1.00 24.25 ?  253 SER C OG    1 
ATOM   13058 N  N     . HIS C 2 275 ? 94.894  78.676  128.018 1.00 24.59 ?  254 HIS C N     1 
ATOM   13059 C  CA    . HIS C 2 275 ? 95.099  77.568  127.078 1.00 25.66 ?  254 HIS C CA    1 
ATOM   13060 C  C     . HIS C 2 275 ? 96.070  77.944  125.947 1.00 26.01 ?  254 HIS C C     1 
ATOM   13061 O  O     . HIS C 2 275 ? 96.922  77.136  125.539 1.00 26.23 ?  254 HIS C O     1 
ATOM   13062 C  CB    . HIS C 2 275 ? 93.754  77.103  126.505 1.00 26.89 ?  254 HIS C CB    1 
ATOM   13063 C  CG    . HIS C 2 275 ? 93.859  75.907  125.610 1.00 29.10 ?  254 HIS C CG    1 
ATOM   13064 N  ND1   . HIS C 2 275 ? 94.463  74.731  126.007 1.00 32.70 ?  254 HIS C ND1   1 
ATOM   13065 C  CD2   . HIS C 2 275 ? 93.437  75.703  124.341 1.00 31.68 ?  254 HIS C CD2   1 
ATOM   13066 C  CE1   . HIS C 2 275 ? 94.411  73.857  125.018 1.00 33.55 ?  254 HIS C CE1   1 
ATOM   13067 N  NE2   . HIS C 2 275 ? 93.780  74.415  124.002 1.00 33.71 ?  254 HIS C NE2   1 
ATOM   13068 N  N     . ASP C 2 276 ? 95.931  79.168  125.450 1.00 25.93 ?  255 ASP C N     1 
ATOM   13069 C  CA    . ASP C 2 276 ? 96.808  79.697  124.410 1.00 26.65 ?  255 ASP C CA    1 
ATOM   13070 C  C     . ASP C 2 276 ? 98.261  79.803  124.878 1.00 25.61 ?  255 ASP C C     1 
ATOM   13071 O  O     . ASP C 2 276 ? 99.178  79.392  124.155 1.00 25.34 ?  255 ASP C O     1 
ATOM   13072 C  CB    . ASP C 2 276 ? 96.308  81.060  123.928 1.00 27.44 ?  255 ASP C CB    1 
ATOM   13073 C  CG    . ASP C 2 276 ? 95.816  81.022  122.498 1.00 32.09 ?  255 ASP C CG    1 
ATOM   13074 O  OD1   . ASP C 2 276 ? 96.510  80.412  121.648 1.00 36.67 ?  255 ASP C OD1   1 
ATOM   13075 O  OD2   . ASP C 2 276 ? 94.733  81.586  122.220 1.00 36.30 -1 255 ASP C OD2   1 
ATOM   13076 N  N     . VAL C 2 277 ? 98.456  80.353  126.082 1.00 24.17 ?  256 VAL C N     1 
ATOM   13077 C  CA    . VAL C 2 277 ? 99.793  80.480  126.676 1.00 23.71 ?  256 VAL C CA    1 
ATOM   13078 C  C     . VAL C 2 277 ? 100.429 79.103  126.886 1.00 23.48 ?  256 VAL C C     1 
ATOM   13079 O  O     . VAL C 2 277 ? 101.619 78.920  126.625 1.00 23.08 ?  256 VAL C O     1 
ATOM   13080 C  CB    . VAL C 2 277 ? 99.774  81.252  128.025 1.00 23.27 ?  256 VAL C CB    1 
ATOM   13081 C  CG1   . VAL C 2 277 ? 101.186 81.366  128.610 1.00 24.02 ?  256 VAL C CG1   1 
ATOM   13082 C  CG2   . VAL C 2 277 ? 99.165  82.637  127.854 1.00 23.35 ?  256 VAL C CG2   1 
ATOM   13083 N  N     . LYS C 2 278 ? 99.637  78.142  127.355 1.00 23.36 ?  257 LYS C N     1 
ATOM   13084 C  CA    . LYS C 2 278 ? 100.115 76.773  127.548 1.00 24.12 ?  257 LYS C CA    1 
ATOM   13085 C  C     . LYS C 2 278 ? 100.687 76.161  126.271 1.00 24.30 ?  257 LYS C C     1 
ATOM   13086 O  O     . LYS C 2 278 ? 101.724 75.485  126.307 1.00 24.37 ?  257 LYS C O     1 
ATOM   13087 C  CB    . LYS C 2 278 ? 99.012  75.880  128.114 1.00 24.22 ?  257 LYS C CB    1 
ATOM   13088 C  CG    . LYS C 2 278 ? 98.710  76.126  129.583 1.00 24.96 ?  257 LYS C CG    1 
ATOM   13089 C  CD    . LYS C 2 278 ? 97.506  75.294  130.002 1.00 26.34 ?  257 LYS C CD    1 
ATOM   13090 C  CE    . LYS C 2 278 ? 97.140  75.536  131.440 1.00 27.16 ?  257 LYS C CE    1 
ATOM   13091 N  NZ    . LYS C 2 278 ? 95.962  74.686  131.789 1.00 29.60 1  257 LYS C NZ    1 
ATOM   13092 N  N     . LYS C 2 279 ? 100.018 76.401  125.145 1.00 24.55 ?  258 LYS C N     1 
ATOM   13093 C  CA    . LYS C 2 279 ? 100.528 75.941  123.856 1.00 24.85 ?  258 LYS C CA    1 
ATOM   13094 C  C     . LYS C 2 279 ? 101.875 76.593  123.551 1.00 24.57 ?  258 LYS C C     1 
ATOM   13095 O  O     . LYS C 2 279 ? 102.786 75.932  123.056 1.00 24.07 ?  258 LYS C O     1 
ATOM   13096 C  CB    . LYS C 2 279 ? 99.531  76.247  122.738 1.00 25.30 ?  258 LYS C CB    1 
ATOM   13097 C  CG    . LYS C 2 279 ? 98.192  75.566  122.902 1.00 26.63 ?  258 LYS C CG    1 
ATOM   13098 C  CD    . LYS C 2 279 ? 97.282  75.945  121.740 1.00 29.30 ?  258 LYS C CD    1 
ATOM   13099 C  CE    . LYS C 2 279 ? 96.003  75.165  121.789 1.00 31.79 ?  258 LYS C CE    1 
ATOM   13100 N  NZ    . LYS C 2 279 ? 95.012  75.789  120.877 1.00 33.80 1  258 LYS C NZ    1 
ATOM   13101 N  N     . PHE C 2 280 ? 101.994 77.880  123.879 1.00 24.29 ?  259 PHE C N     1 
ATOM   13102 C  CA    . PHE C 2 280 ? 103.220 78.652  123.638 1.00 24.90 ?  259 PHE C CA    1 
ATOM   13103 C  C     . PHE C 2 280 ? 104.409 78.136  124.469 1.00 24.86 ?  259 PHE C C     1 
ATOM   13104 O  O     . PHE C 2 280 ? 105.526 78.006  123.957 1.00 24.68 ?  259 PHE C O     1 
ATOM   13105 C  CB    . PHE C 2 280 ? 102.946 80.139  123.902 1.00 24.70 ?  259 PHE C CB    1 
ATOM   13106 C  CG    . PHE C 2 280 ? 104.049 81.076  123.467 1.00 25.70 ?  259 PHE C CG    1 
ATOM   13107 C  CD1   . PHE C 2 280 ? 104.471 81.121  122.137 1.00 26.86 ?  259 PHE C CD1   1 
ATOM   13108 C  CD2   . PHE C 2 280 ? 104.636 81.952  124.388 1.00 26.19 ?  259 PHE C CD2   1 
ATOM   13109 C  CE1   . PHE C 2 280 ? 105.478 82.008  121.730 1.00 26.66 ?  259 PHE C CE1   1 
ATOM   13110 C  CE2   . PHE C 2 280 ? 105.635 82.845  123.990 1.00 26.52 ?  259 PHE C CE2   1 
ATOM   13111 C  CZ    . PHE C 2 280 ? 106.061 82.869  122.655 1.00 26.23 ?  259 PHE C CZ    1 
ATOM   13112 N  N     . ILE C 2 281 ? 104.165 77.833  125.745 1.00 25.53 ?  260 ILE C N     1 
ATOM   13113 C  CA    . ILE C 2 281 ? 105.237 77.339  126.612 1.00 26.21 ?  260 ILE C CA    1 
ATOM   13114 C  C     . ILE C 2 281 ? 105.705 75.934  126.209 1.00 26.47 ?  260 ILE C C     1 
ATOM   13115 O  O     . ILE C 2 281 ? 106.887 75.626  126.320 1.00 26.52 ?  260 ILE C O     1 
ATOM   13116 C  CB    . ILE C 2 281 ? 104.915 77.459  128.142 1.00 26.27 ?  260 ILE C CB    1 
ATOM   13117 C  CG1   . ILE C 2 281 ? 103.973 76.352  128.620 1.00 27.37 ?  260 ILE C CG1   1 
ATOM   13118 C  CG2   . ILE C 2 281 ? 104.386 78.872  128.475 1.00 26.92 ?  260 ILE C CG2   1 
ATOM   13119 C  CD1   . ILE C 2 281 ? 103.682 76.377  130.121 1.00 29.51 ?  260 ILE C CD1   1 
ATOM   13120 N  N     . ARG C 2 282 ? 104.787 75.108  125.702 1.00 26.57 ?  261 ARG C N     1 
ATOM   13121 C  CA    . ARG C 2 282 ? 105.154 73.784  125.190 1.00 26.84 ?  261 ARG C CA    1 
ATOM   13122 C  C     . ARG C 2 282 ? 106.034 73.905  123.946 1.00 27.34 ?  261 ARG C C     1 
ATOM   13123 O  O     . ARG C 2 282 ? 107.038 73.209  123.822 1.00 27.54 ?  261 ARG C O     1 
ATOM   13124 C  CB    . ARG C 2 282 ? 103.920 72.925  124.907 1.00 26.98 ?  261 ARG C CB    1 
ATOM   13125 C  CG    . ARG C 2 282 ? 103.299 72.295  126.138 1.00 26.53 ?  261 ARG C CG    1 
ATOM   13126 C  CD    . ARG C 2 282 ? 102.254 71.224  125.766 1.00 27.77 ?  261 ARG C CD    1 
ATOM   13127 N  NE    . ARG C 2 282 ? 101.043 71.793  125.180 1.00 28.67 ?  261 ARG C NE    1 
ATOM   13128 C  CZ    . ARG C 2 282 ? 100.007 72.256  125.882 1.00 29.68 ?  261 ARG C CZ    1 
ATOM   13129 N  NH1   . ARG C 2 282 ? 100.016 72.224  127.214 1.00 28.31 1  261 ARG C NH1   1 
ATOM   13130 N  NH2   . ARG C 2 282 ? 98.952  72.747  125.251 1.00 29.15 ?  261 ARG C NH2   1 
ATOM   13131 N  N     . TYR C 2 283 ? 105.648 74.805  123.044 1.00 27.78 ?  262 TYR C N     1 
ATOM   13132 C  CA    . TYR C 2 283 ? 106.443 75.152  121.867 1.00 28.18 ?  262 TYR C CA    1 
ATOM   13133 C  C     . TYR C 2 283 ? 107.884 75.526  122.258 1.00 27.08 ?  262 TYR C C     1 
ATOM   13134 O  O     . TYR C 2 283 ? 108.862 75.004  121.701 1.00 26.51 ?  262 TYR C O     1 
ATOM   13135 C  CB    . TYR C 2 283 ? 105.771 76.316  121.128 1.00 29.11 ?  262 TYR C CB    1 
ATOM   13136 C  CG    . TYR C 2 283 ? 106.480 76.767  119.875 1.00 32.56 ?  262 TYR C CG    1 
ATOM   13137 C  CD1   . TYR C 2 283 ? 106.400 76.017  118.700 1.00 36.59 ?  262 TYR C CD1   1 
ATOM   13138 C  CD2   . TYR C 2 283 ? 107.219 77.954  119.854 1.00 36.34 ?  262 TYR C CD2   1 
ATOM   13139 C  CE1   . TYR C 2 283 ? 107.048 76.428  117.531 1.00 39.47 ?  262 TYR C CE1   1 
ATOM   13140 C  CE2   . TYR C 2 283 ? 107.871 78.380  118.682 1.00 39.23 ?  262 TYR C CE2   1 
ATOM   13141 C  CZ    . TYR C 2 283 ? 107.779 77.607  117.529 1.00 40.48 ?  262 TYR C CZ    1 
ATOM   13142 O  OH    . TYR C 2 283 ? 108.413 78.003  116.373 1.00 44.00 ?  262 TYR C OH    1 
ATOM   13143 N  N     . ASN C 2 284 ? 108.006 76.411  123.238 1.00 26.08 ?  263 ASN C N     1 
ATOM   13144 C  CA    . ASN C 2 284 ? 109.316 76.851  123.692 1.00 25.73 ?  263 ASN C CA    1 
ATOM   13145 C  C     . ASN C 2 284 ? 110.093 75.820  124.514 1.00 25.24 ?  263 ASN C C     1 
ATOM   13146 O  O     . ASN C 2 284 ? 111.329 75.780  124.439 1.00 25.56 ?  263 ASN C O     1 
ATOM   13147 C  CB    . ASN C 2 284 ? 109.208 78.208  124.389 1.00 25.69 ?  263 ASN C CB    1 
ATOM   13148 C  CG    . ASN C 2 284 ? 108.999 79.334  123.403 1.00 26.39 ?  263 ASN C CG    1 
ATOM   13149 O  OD1   . ASN C 2 284 ? 109.934 79.753  122.715 1.00 26.91 ?  263 ASN C OD1   1 
ATOM   13150 N  ND2   . ASN C 2 284 ? 107.772 79.827  123.317 1.00 27.56 ?  263 ASN C ND2   1 
ATOM   13151 N  N     . ALA C 2 285 ? 109.388 74.971  125.266 1.00 24.51 ?  264 ALA C N     1 
ATOM   13152 C  CA    . ALA C 2 285 ? 110.029 73.806  125.904 1.00 24.19 ?  264 ALA C CA    1 
ATOM   13153 C  C     . ALA C 2 285 ? 110.787 72.932  124.884 1.00 24.63 ?  264 ALA C C     1 
ATOM   13154 O  O     . ALA C 2 285 ? 111.907 72.496  125.144 1.00 24.01 ?  264 ALA C O     1 
ATOM   13155 C  CB    . ALA C 2 285 ? 109.016 72.966  126.659 1.00 23.63 ?  264 ALA C CB    1 
ATOM   13156 N  N     . ASN C 2 286 ? 110.168 72.685  123.730 1.00 24.66 ?  265 ASN C N     1 
ATOM   13157 C  CA    . ASN C 2 286 ? 110.823 71.953  122.646 1.00 25.24 ?  265 ASN C CA    1 
ATOM   13158 C  C     . ASN C 2 286 ? 112.088 72.624  122.121 1.00 25.09 ?  265 ASN C C     1 
ATOM   13159 O  O     . ASN C 2 286 ? 113.055 71.928  121.767 1.00 24.14 ?  265 ASN C O     1 
ATOM   13160 C  CB    . ASN C 2 286 ? 109.850 71.688  121.482 1.00 25.62 ?  265 ASN C CB    1 
ATOM   13161 C  CG    . ASN C 2 286 ? 108.842 70.597  121.805 1.00 26.46 ?  265 ASN C CG    1 
ATOM   13162 O  OD1   . ASN C 2 286 ? 108.982 69.874  122.794 1.00 27.14 ?  265 ASN C OD1   1 
ATOM   13163 N  ND2   . ASN C 2 286 ? 107.803 70.485  120.974 1.00 27.89 ?  265 ASN C ND2   1 
ATOM   13164 N  N     . LYS C 2 287 ? 112.066 73.958  122.057 1.00 24.99 ?  266 LYS C N     1 
ATOM   13165 C  CA    . LYS C 2 287 ? 113.227 74.756  121.658 1.00 25.91 ?  266 LYS C CA    1 
ATOM   13166 C  C     . LYS C 2 287 ? 114.344 74.653  122.691 1.00 25.23 ?  266 LYS C C     1 
ATOM   13167 O  O     . LYS C 2 287 ? 115.520 74.576  122.329 1.00 25.34 ?  266 LYS C O     1 
ATOM   13168 C  CB    . LYS C 2 287 ? 112.861 76.230  121.482 1.00 25.96 ?  266 LYS C CB    1 
ATOM   13169 C  CG    . LYS C 2 287 ? 112.079 76.573  120.224 1.00 29.60 ?  266 LYS C CG    1 
ATOM   13170 C  CD    . LYS C 2 287 ? 112.031 78.100  120.074 1.00 34.20 ?  266 LYS C CD    1 
ATOM   13171 C  CE    . LYS C 2 287 ? 111.357 78.534  118.796 1.00 37.67 ?  266 LYS C CE    1 
ATOM   13172 N  NZ    . LYS C 2 287 ? 111.466 80.022  118.639 1.00 39.48 1  266 LYS C NZ    1 
ATOM   13173 N  N     . ALA C 2 288 ? 113.978 74.669  123.970 1.00 24.87 ?  267 ALA C N     1 
ATOM   13174 C  CA    . ALA C 2 288 ? 114.956 74.458  125.054 1.00 24.23 ?  267 ALA C CA    1 
ATOM   13175 C  C     . ALA C 2 288 ? 115.613 73.075  124.954 1.00 24.24 ?  267 ALA C C     1 
ATOM   13176 O  O     . ALA C 2 288 ? 116.836 72.956  125.046 1.00 23.96 ?  267 ALA C O     1 
ATOM   13177 C  CB    . ALA C 2 288 ? 114.300 74.638  126.410 1.00 24.23 ?  267 ALA C CB    1 
ATOM   13178 N  N     . LEU C 2 289 ? 114.804 72.034  124.758 1.00 24.63 ?  268 LEU C N     1 
ATOM   13179 C  CA    . LEU C 2 289 ? 115.341 70.685  124.565 1.00 25.14 ?  268 LEU C CA    1 
ATOM   13180 C  C     . LEU C 2 289 ? 116.285 70.649  123.373 1.00 25.58 ?  268 LEU C C     1 
ATOM   13181 O  O     . LEU C 2 289 ? 117.366 70.076  123.455 1.00 25.42 ?  268 LEU C O     1 
ATOM   13182 C  CB    . LEU C 2 289 ? 114.225 69.642  124.399 1.00 25.28 ?  268 LEU C CB    1 
ATOM   13183 C  CG    . LEU C 2 289 ? 113.468 69.283  125.682 1.00 25.93 ?  268 LEU C CG    1 
ATOM   13184 C  CD1   . LEU C 2 289 ? 112.141 68.626  125.360 1.00 26.50 ?  268 LEU C CD1   1 
ATOM   13185 C  CD2   . LEU C 2 289 ? 114.307 68.415  126.638 1.00 25.20 ?  268 LEU C CD2   1 
ATOM   13186 N  N     . MET C 2 290 ? 115.884 71.281  122.270 1.00 26.32 ?  269 MET C N     1 
ATOM   13187 C  CA    . MET C 2 290 ? 116.737 71.309  121.086 1.00 27.41 ?  269 MET C CA    1 
ATOM   13188 C  C     . MET C 2 290 ? 118.060 72.034  121.324 1.00 26.66 ?  269 MET C C     1 
ATOM   13189 O  O     . MET C 2 290 ? 119.101 71.591  120.833 1.00 26.69 ?  269 MET C O     1 
ATOM   13190 C  CB    . MET C 2 290 ? 115.989 71.861  119.877 1.00 28.28 ?  269 MET C CB    1 
ATOM   13191 C  CG    . MET C 2 290 ? 115.302 70.747  119.088 1.00 32.91 ?  269 MET C CG    1 
ATOM   13192 S  SD    . MET C 2 290 ? 114.139 71.362  117.867 1.00 42.49 ?  269 MET C SD    1 
ATOM   13193 C  CE    . MET C 2 290 ? 112.576 70.961  118.648 1.00 38.74 ?  269 MET C CE    1 
ATOM   13194 N  N     . ASN C 2 291 ? 118.022 73.118  122.101 1.00 25.48 ?  270 ASN C N     1 
ATOM   13195 C  CA    . ASN C 2 291 ? 119.239 73.843  122.500 1.00 25.39 ?  270 ASN C CA    1 
ATOM   13196 C  C     . ASN C 2 291 ? 120.214 72.952  123.288 1.00 25.18 ?  270 ASN C C     1 
ATOM   13197 O  O     . ASN C 2 291 ? 121.433 73.174  123.272 1.00 24.73 ?  270 ASN C O     1 
ATOM   13198 C  CB    . ASN C 2 291 ? 118.885 75.096  123.311 1.00 24.83 ?  270 ASN C CB    1 
ATOM   13199 C  CG    . ASN C 2 291 ? 118.333 76.231  122.440 1.00 25.58 ?  270 ASN C CG    1 
ATOM   13200 O  OD1   . ASN C 2 291 ? 118.426 76.197  121.217 1.00 25.58 ?  270 ASN C OD1   1 
ATOM   13201 N  ND2   . ASN C 2 291 ? 117.756 77.236  123.080 1.00 24.32 ?  270 ASN C ND2   1 
ATOM   13202 N  N     . LEU C 2 292 ? 119.652 71.933  123.945 1.00 25.09 ?  271 LEU C N     1 
ATOM   13203 C  CA    . LEU C 2 292 ? 120.409 70.923  124.697 1.00 25.46 ?  271 LEU C CA    1 
ATOM   13204 C  C     . LEU C 2 292 ? 120.783 69.674  123.883 1.00 26.18 ?  271 LEU C C     1 
ATOM   13205 O  O     . LEU C 2 292 ? 121.401 68.730  124.408 1.00 26.06 ?  271 LEU C O     1 
ATOM   13206 C  CB    . LEU C 2 292 ? 119.630 70.531  125.960 1.00 25.19 ?  271 LEU C CB    1 
ATOM   13207 C  CG    . LEU C 2 292 ? 119.460 71.646  127.006 1.00 25.03 ?  271 LEU C CG    1 
ATOM   13208 C  CD1   . LEU C 2 292 ? 118.438 71.247  128.046 1.00 24.50 ?  271 LEU C CD1   1 
ATOM   13209 C  CD2   . LEU C 2 292 ? 120.811 71.978  127.661 1.00 25.64 ?  271 LEU C CD2   1 
ATOM   13210 N  N     . GLY C 2 293 ? 120.415 69.669  122.602 1.00 26.71 ?  272 GLY C N     1 
ATOM   13211 C  CA    . GLY C 2 293 ? 120.692 68.533  121.714 1.00 28.06 ?  272 GLY C CA    1 
ATOM   13212 C  C     . GLY C 2 293 ? 119.757 67.345  121.877 1.00 29.34 ?  272 GLY C C     1 
ATOM   13213 O  O     . GLY C 2 293 ? 120.105 66.214  121.506 1.00 29.73 ?  272 GLY C O     1 
ATOM   13214 N  N     . PHE C 2 294 ? 118.571 67.594  122.431 1.00 29.88 ?  273 PHE C N     1 
ATOM   13215 C  CA    . PHE C 2 294 ? 117.576 66.549  122.656 1.00 31.24 ?  273 PHE C CA    1 
ATOM   13216 C  C     . PHE C 2 294 ? 116.389 66.696  121.694 1.00 32.42 ?  273 PHE C C     1 
ATOM   13217 O  O     . PHE C 2 294 ? 116.133 67.786  121.163 1.00 32.30 ?  273 PHE C O     1 
ATOM   13218 C  CB    . PHE C 2 294 ? 117.089 66.561  124.111 1.00 30.82 ?  273 PHE C CB    1 
ATOM   13219 C  CG    . PHE C 2 294 ? 118.181 66.315  125.132 1.00 30.93 ?  273 PHE C CG    1 
ATOM   13220 C  CD1   . PHE C 2 294 ? 119.076 65.255  124.990 1.00 30.85 ?  273 PHE C CD1   1 
ATOM   13221 C  CD2   . PHE C 2 294 ? 118.301 67.139  126.242 1.00 30.30 ?  273 PHE C CD2   1 
ATOM   13222 C  CE1   . PHE C 2 294 ? 120.082 65.037  125.930 1.00 30.75 ?  273 PHE C CE1   1 
ATOM   13223 C  CE2   . PHE C 2 294 ? 119.295 66.921  127.199 1.00 30.41 ?  273 PHE C CE2   1 
ATOM   13224 C  CZ    . PHE C 2 294 ? 120.184 65.865  127.045 1.00 30.88 ?  273 PHE C CZ    1 
ATOM   13225 N  N     . ASP C 2 295 ? 115.684 65.590  121.467 1.00 33.81 ?  274 ASP C N     1 
ATOM   13226 C  CA    . ASP C 2 295 ? 114.481 65.576  120.628 1.00 35.32 ?  274 ASP C CA    1 
ATOM   13227 C  C     . ASP C 2 295 ? 113.318 66.337  121.290 1.00 35.36 ?  274 ASP C C     1 
ATOM   13228 O  O     . ASP C 2 295 ? 113.214 66.351  122.514 1.00 34.78 ?  274 ASP C O     1 
ATOM   13229 C  CB    . ASP C 2 295 ? 114.041 64.130  120.360 1.00 35.95 ?  274 ASP C CB    1 
ATOM   13230 C  CG    . ASP C 2 295 ? 115.067 63.331  119.561 1.00 37.98 ?  274 ASP C CG    1 
ATOM   13231 O  OD1   . ASP C 2 295 ? 115.842 63.924  118.779 1.00 39.83 ?  274 ASP C OD1   1 
ATOM   13232 O  OD2   . ASP C 2 295 ? 115.090 62.091  119.718 1.00 40.03 -1 274 ASP C OD2   1 
ATOM   13233 N  N     . PRO C 2 296 ? 112.439 66.960  120.483 1.00 36.33 ?  275 PRO C N     1 
ATOM   13234 C  CA    . PRO C 2 296 ? 111.226 67.601  121.037 1.00 36.92 ?  275 PRO C CA    1 
ATOM   13235 C  C     . PRO C 2 296 ? 110.360 66.629  121.854 1.00 37.68 ?  275 PRO C C     1 
ATOM   13236 O  O     . PRO C 2 296 ? 110.265 65.448  121.509 1.00 38.07 ?  275 PRO C O     1 
ATOM   13237 C  CB    . PRO C 2 296 ? 110.470 68.080  119.788 1.00 36.82 ?  275 PRO C CB    1 
ATOM   13238 C  CG    . PRO C 2 296 ? 111.138 67.381  118.612 1.00 37.42 ?  275 PRO C CG    1 
ATOM   13239 C  CD    . PRO C 2 296 ? 112.557 67.173  119.029 1.00 36.41 ?  275 PRO C CD    1 
ATOM   13240 N  N     . TYR C 2 297 ? 109.741 67.128  122.924 1.00 38.10 ?  276 TYR C N     1 
ATOM   13241 C  CA    . TYR C 2 297 ? 108.989 66.293  123.872 1.00 38.96 ?  276 TYR C CA    1 
ATOM   13242 C  C     . TYR C 2 297 ? 107.471 66.471  123.749 1.00 39.71 ?  276 TYR C C     1 
ATOM   13243 O  O     . TYR C 2 297 ? 106.704 65.550  124.049 1.00 40.18 ?  276 TYR C O     1 
ATOM   13244 C  CB    . TYR C 2 297 ? 109.439 66.624  125.300 1.00 38.94 ?  276 TYR C CB    1 
ATOM   13245 C  CG    . TYR C 2 297 ? 108.857 65.793  126.424 1.00 39.64 ?  276 TYR C CG    1 
ATOM   13246 C  CD1   . TYR C 2 297 ? 109.387 64.542  126.748 1.00 40.43 ?  276 TYR C CD1   1 
ATOM   13247 C  CD2   . TYR C 2 297 ? 107.818 66.286  127.207 1.00 41.04 ?  276 TYR C CD2   1 
ATOM   13248 C  CE1   . TYR C 2 297 ? 108.864 63.786  127.798 1.00 41.69 ?  276 TYR C CE1   1 
ATOM   13249 C  CE2   . TYR C 2 297 ? 107.285 65.540  128.259 1.00 41.60 ?  276 TYR C CE2   1 
ATOM   13250 C  CZ    . TYR C 2 297 ? 107.815 64.295  128.552 1.00 41.92 ?  276 TYR C CZ    1 
ATOM   13251 O  OH    . TYR C 2 297 ? 107.291 63.566  129.597 1.00 42.52 ?  276 TYR C OH    1 
ATOM   13252 N  N     . PHE C 2 298 ? 107.040 67.654  123.324 1.00 39.85 ?  277 PHE C N     1 
ATOM   13253 C  CA    . PHE C 2 298 ? 105.616 67.937  123.185 1.00 40.77 ?  277 PHE C CA    1 
ATOM   13254 C  C     . PHE C 2 298 ? 105.211 67.945  121.719 1.00 41.95 ?  277 PHE C C     1 
ATOM   13255 O  O     . PHE C 2 298 ? 106.015 68.296  120.857 1.00 41.91 ?  277 PHE C O     1 
ATOM   13256 C  CB    . PHE C 2 298 ? 105.270 69.280  123.837 1.00 39.94 ?  277 PHE C CB    1 
ATOM   13257 C  CG    . PHE C 2 298 ? 105.508 69.318  125.322 1.00 39.09 ?  277 PHE C CG    1 
ATOM   13258 C  CD1   . PHE C 2 298 ? 106.583 70.023  125.848 1.00 37.84 ?  277 PHE C CD1   1 
ATOM   13259 C  CD2   . PHE C 2 298 ? 104.646 68.661  126.197 1.00 38.97 ?  277 PHE C CD2   1 
ATOM   13260 C  CE1   . PHE C 2 298 ? 106.808 70.070  127.222 1.00 37.46 ?  277 PHE C CE1   1 
ATOM   13261 C  CE2   . PHE C 2 298 ? 104.858 68.700  127.570 1.00 38.20 ?  277 PHE C CE2   1 
ATOM   13262 C  CZ    . PHE C 2 298 ? 105.943 69.407  128.086 1.00 37.91 ?  277 PHE C CZ    1 
ATOM   13263 N  N     . GLU C 2 299 ? 103.970 67.555  121.429 1.00 43.74 ?  278 GLU C N     1 
ATOM   13264 C  CA    . GLU C 2 299 ? 103.483 67.580  120.046 1.00 45.61 ?  278 GLU C CA    1 
ATOM   13265 C  C     . GLU C 2 299 ? 103.239 69.018  119.586 1.00 46.04 ?  278 GLU C C     1 
ATOM   13266 O  O     . GLU C 2 299 ? 102.909 69.889  120.391 1.00 45.88 ?  278 GLU C O     1 
ATOM   13267 C  CB    . GLU C 2 299 ? 102.211 66.742  119.874 1.00 46.43 ?  278 GLU C CB    1 
ATOM   13268 C  CG    . GLU C 2 299 ? 102.076 66.121  118.473 1.00 48.82 ?  278 GLU C CG    1 
ATOM   13269 C  CD    . GLU C 2 299 ? 100.651 65.725  118.117 1.00 51.86 ?  278 GLU C CD    1 
ATOM   13270 O  OE1   . GLU C 2 299 ? 100.443 65.226  116.988 1.00 53.35 ?  278 GLU C OE1   1 
ATOM   13271 O  OE2   . GLU C 2 299 ? 99.737  65.913  118.954 1.00 53.10 -1 278 GLU C OE2   1 
ATOM   13272 N  N     . GLU C 2 300 ? 103.420 69.255  118.288 1.00 47.16 ?  279 GLU C N     1 
ATOM   13273 C  CA    . GLU C 2 300 ? 103.208 70.576  117.686 1.00 47.75 ?  279 GLU C CA    1 
ATOM   13274 C  C     . GLU C 2 300 ? 101.739 71.022  117.741 1.00 47.71 ?  279 GLU C C     1 
ATOM   13275 O  O     . GLU C 2 300 ? 100.827 70.207  117.559 1.00 47.77 ?  279 GLU C O     1 
ATOM   13276 C  CB    . GLU C 2 300 ? 103.737 70.596  116.240 1.00 48.42 ?  279 GLU C CB    1 
ATOM   13277 C  CG    . GLU C 2 300 ? 103.239 69.445  115.359 1.00 50.63 ?  279 GLU C CG    1 
ATOM   13278 C  CD    . GLU C 2 300 ? 104.158 69.157  114.170 1.00 53.06 ?  279 GLU C CD    1 
ATOM   13279 O  OE1   . GLU C 2 300 ? 104.455 70.096  113.393 1.00 54.35 ?  279 GLU C OE1   1 
ATOM   13280 O  OE2   . GLU C 2 300 ? 104.571 67.986  114.008 1.00 53.32 -1 279 GLU C OE2   1 
ATOM   13281 N  N     . GLU C 2 301 ? 101.531 72.310  118.014 1.00 47.40 ?  280 GLU C N     1 
ATOM   13282 C  CA    . GLU C 2 301 ? 100.196 72.919  118.072 1.00 47.46 ?  280 GLU C CA    1 
ATOM   13283 C  C     . GLU C 2 301 ? 100.204 74.296  117.397 1.00 47.31 ?  280 GLU C C     1 
ATOM   13284 O  O     . GLU C 2 301 ? 101.256 74.932  117.291 1.00 47.21 ?  280 GLU C O     1 
ATOM   13285 C  CB    . GLU C 2 301 ? 99.729  73.075  119.526 1.00 47.19 ?  280 GLU C CB    1 
ATOM   13286 C  CG    . GLU C 2 301 ? 99.595  71.779  120.327 1.00 47.14 ?  280 GLU C CG    1 
ATOM   13287 C  CD    . GLU C 2 301 ? 99.637  72.019  121.834 1.00 47.21 ?  280 GLU C CD    1 
ATOM   13288 O  OE1   . GLU C 2 301 ? 98.574  71.918  122.480 1.00 46.97 ?  280 GLU C OE1   1 
ATOM   13289 O  OE2   . GLU C 2 301 ? 100.730 72.321  122.370 1.00 46.13 -1 280 GLU C OE2   1 
ATOM   13290 N  N     . ASP C 2 302 ? 99.035  74.753  116.948 1.00 47.15 ?  281 ASP C N     1 
ATOM   13291 C  CA    . ASP C 2 302 ? 98.909  76.083  116.342 1.00 47.04 ?  281 ASP C CA    1 
ATOM   13292 C  C     . ASP C 2 302 ? 98.963  77.176  117.415 1.00 46.05 ?  281 ASP C C     1 
ATOM   13293 O  O     . ASP C 2 302 ? 98.115  77.218  118.313 1.00 46.10 ?  281 ASP C O     1 
ATOM   13294 C  CB    . ASP C 2 302 ? 97.607  76.210  115.530 1.00 47.66 ?  281 ASP C CB    1 
ATOM   13295 C  CG    . ASP C 2 302 ? 97.643  75.434  114.210 1.00 49.53 ?  281 ASP C CG    1 
ATOM   13296 O  OD1   . ASP C 2 302 ? 98.720  75.342  113.580 1.00 50.58 ?  281 ASP C OD1   1 
ATOM   13297 O  OD2   . ASP C 2 302 ? 96.571  74.934  113.788 1.00 51.14 -1 281 ASP C OD2   1 
ATOM   13298 N  N     . ILE C 2 303 ? 99.969  78.042  117.320 1.00 44.96 ?  282 ILE C N     1 
ATOM   13299 C  CA    . ILE C 2 303 ? 100.121 79.187  118.225 1.00 43.99 ?  282 ILE C CA    1 
ATOM   13300 C  C     . ILE C 2 303 ? 99.290  80.366  117.708 1.00 43.53 ?  282 ILE C C     1 
ATOM   13301 O  O     . ILE C 2 303 ? 99.141  80.532  116.496 1.00 43.52 ?  282 ILE C O     1 
ATOM   13302 C  CB    . ILE C 2 303 ? 101.614 79.609  118.361 1.00 43.84 ?  282 ILE C CB    1 
ATOM   13303 C  CG1   . ILE C 2 303 ? 102.494 78.420  118.793 1.00 43.91 ?  282 ILE C CG1   1 
ATOM   13304 C  CG2   . ILE C 2 303 ? 101.778 80.816  119.300 1.00 43.55 ?  282 ILE C CG2   1 
ATOM   13305 C  CD1   . ILE C 2 303 ? 102.109 77.770  120.126 1.00 42.76 ?  282 ILE C CD1   1 
ATOM   13306 N  N     . ASN C 2 304 ? 98.745  81.168  118.624 1.00 42.51 ?  283 ASN C N     1 
ATOM   13307 C  CA    . ASN C 2 304 ? 97.979  82.359  118.257 1.00 41.93 ?  283 ASN C CA    1 
ATOM   13308 C  C     . ASN C 2 304 ? 98.761  83.208  117.242 1.00 41.78 ?  283 ASN C C     1 
ATOM   13309 O  O     . ASN C 2 304 ? 99.887  83.634  117.534 1.00 41.13 ?  283 ASN C O     1 
ATOM   13310 C  CB    . ASN C 2 304 ? 97.643  83.184  119.509 1.00 41.83 ?  283 ASN C CB    1 
ATOM   13311 C  CG    . ASN C 2 304 ? 96.468  84.139  119.300 1.00 41.27 ?  283 ASN C CG    1 
ATOM   13312 O  OD1   . ASN C 2 304 ? 96.379  84.835  118.291 1.00 41.28 ?  283 ASN C OD1   1 
ATOM   13313 N  ND2   . ASN C 2 304 ? 95.568  84.178  120.271 1.00 40.67 ?  283 ASN C ND2   1 
ATOM   13314 N  N     . PRO C 2 305 ? 98.178  83.440  116.040 1.00 41.74 ?  284 PRO C N     1 
ATOM   13315 C  CA    . PRO C 2 305 ? 98.900  84.180  114.992 1.00 41.82 ?  284 PRO C CA    1 
ATOM   13316 C  C     . PRO C 2 305 ? 99.227  85.623  115.390 1.00 41.56 ?  284 PRO C C     1 
ATOM   13317 O  O     . PRO C 2 305 ? 100.158 86.216  114.841 1.00 41.46 ?  284 PRO C O     1 
ATOM   13318 C  CB    . PRO C 2 305 ? 97.940  84.137  113.787 1.00 42.14 ?  284 PRO C CB    1 
ATOM   13319 C  CG    . PRO C 2 305 ? 96.601  83.848  114.359 1.00 42.59 ?  284 PRO C CG    1 
ATOM   13320 C  CD    . PRO C 2 305 ? 96.846  82.999  115.582 1.00 42.05 ?  284 PRO C CD    1 
ATOM   13321 N  N     . ILE C 2 306 ? 98.476  86.166  116.346 1.00 41.19 ?  285 ILE C N     1 
ATOM   13322 C  CA    . ILE C 2 306 ? 98.751  87.489  116.907 1.00 41.47 ?  285 ILE C CA    1 
ATOM   13323 C  C     . ILE C 2 306 ? 100.145 87.517  117.547 1.00 41.71 ?  285 ILE C C     1 
ATOM   13324 O  O     . ILE C 2 306 ? 100.924 88.440  117.315 1.00 41.38 ?  285 ILE C O     1 
ATOM   13325 C  CB    . ILE C 2 306 ? 97.685  87.892  117.961 1.00 41.22 ?  285 ILE C CB    1 
ATOM   13326 C  CG1   . ILE C 2 306 ? 96.294  87.983  117.320 1.00 41.27 ?  285 ILE C CG1   1 
ATOM   13327 C  CG2   . ILE C 2 306 ? 98.064  89.202  118.649 1.00 40.37 ?  285 ILE C CG2   1 
ATOM   13328 C  CD1   . ILE C 2 306 ? 95.154  88.000  118.329 1.00 41.85 ?  285 ILE C CD1   1 
ATOM   13329 N  N     . VAL C 2 307 ? 100.439 86.493  118.348 1.00 42.33 ?  286 VAL C N     1 
ATOM   13330 C  CA    . VAL C 2 307 ? 101.740 86.350  119.010 1.00 43.36 ?  286 VAL C CA    1 
ATOM   13331 C  C     . VAL C 2 307 ? 102.883 86.169  118.003 1.00 44.51 ?  286 VAL C C     1 
ATOM   13332 O  O     . VAL C 2 307 ? 103.987 86.663  118.225 1.00 44.57 ?  286 VAL C O     1 
ATOM   13333 C  CB    . VAL C 2 307 ? 101.708 85.212  120.059 1.00 42.97 ?  286 VAL C CB    1 
ATOM   13334 C  CG1   . VAL C 2 307 ? 103.123 84.809  120.505 1.00 42.86 ?  286 VAL C CG1   1 
ATOM   13335 C  CG2   . VAL C 2 307 ? 100.873 85.649  121.248 1.00 41.93 ?  286 VAL C CG2   1 
ATOM   13336 N  N     . LEU C 2 308 ? 102.595 85.484  116.897 1.00 46.21 ?  287 LEU C N     1 
ATOM   13337 C  CA    . LEU C 2 308 ? 103.550 85.292  115.795 1.00 47.66 ?  287 LEU C CA    1 
ATOM   13338 C  C     . LEU C 2 308 ? 103.844 86.593  115.050 1.00 48.82 ?  287 LEU C C     1 
ATOM   13339 O  O     . LEU C 2 308 ? 104.976 86.814  114.598 1.00 49.02 ?  287 LEU C O     1 
ATOM   13340 C  CB    . LEU C 2 308 ? 103.045 84.214  114.825 1.00 47.95 ?  287 LEU C CB    1 
ATOM   13341 C  CG    . LEU C 2 308 ? 103.455 82.752  115.074 1.00 48.23 ?  287 LEU C CG    1 
ATOM   13342 C  CD1   . LEU C 2 308 ? 103.773 82.435  116.543 1.00 48.10 ?  287 LEU C CD1   1 
ATOM   13343 C  CD2   . LEU C 2 308 ? 102.412 81.785  114.521 1.00 48.81 ?  287 LEU C CD2   1 
ATOM   13344 N  N     . ASN C 2 309 ? 102.824 87.444  114.924 1.00 49.80 ?  288 ASN C N     1 
ATOM   13345 C  CA    . ASN C 2 309 ? 103.007 88.811  114.445 1.00 51.09 ?  288 ASN C CA    1 
ATOM   13346 C  C     . ASN C 2 309 ? 103.736 89.698  115.459 1.00 51.08 ?  288 ASN C C     1 
ATOM   13347 O  O     . ASN C 2 309 ? 104.366 90.685  115.083 1.00 51.41 ?  288 ASN C O     1 
ATOM   13348 C  CB    . ASN C 2 309 ? 101.672 89.436  114.035 1.00 51.37 ?  288 ASN C CB    1 
ATOM   13349 C  CG    . ASN C 2 309 ? 101.232 89.009  112.649 1.00 53.22 ?  288 ASN C CG    1 
ATOM   13350 O  OD1   . ASN C 2 309 ? 101.276 87.824  112.302 1.00 54.39 ?  288 ASN C OD1   1 
ATOM   13351 N  ND2   . ASN C 2 309 ? 100.805 89.976  111.843 1.00 54.70 ?  288 ASN C ND2   1 
ATOM   13352 N  N     . GLY C 2 310 ? 103.644 89.338  116.740 1.00 51.25 ?  289 GLY C N     1 
ATOM   13353 C  CA    . GLY C 2 310 ? 104.401 90.002  117.803 1.00 51.35 ?  289 GLY C CA    1 
ATOM   13354 C  C     . GLY C 2 310 ? 105.906 89.796  117.691 1.00 51.86 ?  289 GLY C C     1 
ATOM   13355 O  O     . GLY C 2 310 ? 106.689 90.577  118.244 1.00 51.49 ?  289 GLY C O     1 
ATOM   13356 N  N     . LEU C 2 311 ? 106.311 88.743  116.980 1.00 52.45 ?  290 LEU C N     1 
ATOM   13357 C  CA    . LEU C 2 311 ? 107.726 88.454  116.735 1.00 52.99 ?  290 LEU C CA    1 
ATOM   13358 C  C     . LEU C 2 311 ? 108.240 89.185  115.491 1.00 53.65 ?  290 LEU C C     1 
ATOM   13359 O  O     . LEU C 2 311 ? 107.878 88.853  114.356 1.00 54.22 ?  290 LEU C O     1 
ATOM   13360 C  CB    . LEU C 2 311 ? 107.956 86.945  116.597 1.00 53.08 ?  290 LEU C CB    1 
ATOM   13361 C  CG    . LEU C 2 311 ? 107.873 86.060  117.843 1.00 53.33 ?  290 LEU C CG    1 
ATOM   13362 C  CD1   . LEU C 2 311 ? 107.752 84.596  117.444 1.00 53.79 ?  290 LEU C CD1   1 
ATOM   13363 C  CD2   . LEU C 2 311 ? 109.077 86.271  118.764 1.00 53.22 ?  290 LEU C CD2   1 
ATOM   13364 N  N     . LYS C 2 330 ? 139.678 110.368 113.573 1.00 57.38 ?  309 LYS C N     1 
ATOM   13365 C  CA    . LYS C 2 330 ? 140.901 111.142 113.397 1.00 58.57 ?  309 LYS C CA    1 
ATOM   13366 C  C     . LYS C 2 330 ? 141.632 110.735 112.123 1.00 57.73 ?  309 LYS C C     1 
ATOM   13367 O  O     . LYS C 2 330 ? 141.464 109.621 111.628 1.00 59.72 ?  309 LYS C O     1 
ATOM   13368 C  CB    . LYS C 2 330 ? 141.827 110.967 114.603 1.00 55.66 ?  309 LYS C CB    1 
ATOM   13369 C  CG    . LYS C 2 330 ? 141.528 111.897 115.766 1.00 56.05 ?  309 LYS C CG    1 
ATOM   13370 C  CD    . LYS C 2 330 ? 142.662 111.880 116.779 1.00 57.52 ?  309 LYS C CD    1 
ATOM   13371 C  CE    . LYS C 2 330 ? 142.359 112.771 117.972 1.00 58.27 ?  309 LYS C CE    1 
ATOM   13372 N  NZ    . LYS C 2 330 ? 141.547 112.064 119.001 1.00 57.81 1  309 LYS C NZ    1 
ATOM   13373 N  N     . ALA C 2 331 ? 142.445 111.645 111.596 1.00 46.74 ?  310 ALA C N     1 
ATOM   13374 C  CA    . ALA C 2 331 ? 143.297 111.344 110.458 1.00 47.69 ?  310 ALA C CA    1 
ATOM   13375 C  C     . ALA C 2 331 ? 144.619 110.765 110.943 1.00 44.34 ?  310 ALA C C     1 
ATOM   13376 O  O     . ALA C 2 331 ? 145.125 111.129 112.008 1.00 44.88 ?  310 ALA C O     1 
ATOM   13377 C  CB    . ALA C 2 331 ? 143.548 112.594 109.615 1.00 44.94 ?  310 ALA C CB    1 
ATOM   13378 N  N     . THR C 2 332 ? 145.169 109.847 110.152 1.00 40.86 ?  311 THR C N     1 
ATOM   13379 C  CA    . THR C 2 332 ? 146.399 109.161 110.527 1.00 38.81 ?  311 THR C CA    1 
ATOM   13380 C  C     . THR C 2 332 ? 147.537 110.153 110.710 1.00 36.15 ?  311 THR C C     1 
ATOM   13381 O  O     . THR C 2 332 ? 147.752 111.031 109.870 1.00 43.30 ?  311 THR C O     1 
ATOM   13382 C  CB    . THR C 2 332 ? 146.767 108.120 109.467 1.00 39.78 ?  311 THR C CB    1 
ATOM   13383 O  OG1   . THR C 2 332 ? 145.721 107.145 109.369 1.00 41.99 ?  311 THR C OG1   1 
ATOM   13384 C  CG2   . THR C 2 332 ? 148.071 107.426 109.828 1.00 37.37 ?  311 THR C CG2   1 
ATOM   13385 N  N     . VAL C 2 333 ? 148.261 110.011 111.815 1.00 29.00 ?  312 VAL C N     1 
ATOM   13386 C  CA    . VAL C 2 333 ? 149.367 110.908 112.128 1.00 27.73 ?  312 VAL C CA    1 
ATOM   13387 C  C     . VAL C 2 333 ? 150.655 110.307 111.581 1.00 34.73 ?  312 VAL C C     1 
ATOM   13388 O  O     . VAL C 2 333 ? 151.050 109.202 111.966 1.00 34.24 ?  312 VAL C O     1 
ATOM   13389 C  CB    . VAL C 2 333 ? 149.468 111.152 113.640 1.00 29.67 ?  312 VAL C CB    1 
ATOM   13390 C  CG1   . VAL C 2 333 ? 150.749 111.900 113.973 1.00 33.09 ?  312 VAL C CG1   1 
ATOM   13391 C  CG2   . VAL C 2 333 ? 148.252 111.919 114.133 1.00 33.00 ?  312 VAL C CG2   1 
ATOM   13392 N  N     . GLU C 2 334 ? 151.309 111.034 110.680 1.00 31.99 ?  313 GLU C N     1 
ATOM   13393 C  CA    . GLU C 2 334 ? 152.566 110.610 110.097 1.00 30.19 ?  313 GLU C CA    1 
ATOM   13394 C  C     . GLU C 2 334 ? 153.623 111.676 110.349 1.00 35.47 ?  313 GLU C C     1 
ATOM   13395 O  O     . GLU C 2 334 ? 153.394 112.852 110.031 1.00 39.91 ?  313 GLU C O     1 
ATOM   13396 C  CB    . GLU C 2 334 ? 152.415 110.359 108.588 1.00 31.98 ?  313 GLU C CB    1 
ATOM   13397 C  CG    . GLU C 2 334 ? 153.467 109.432 108.006 1.00 30.40 ?  313 GLU C CG    1 
ATOM   13398 C  CD    . GLU C 2 334 ? 153.497 109.459 106.491 1.00 36.69 ?  313 GLU C CD    1 
ATOM   13399 O  OE1   . GLU C 2 334 ? 152.413 109.447 105.873 1.00 35.22 ?  313 GLU C OE1   1 
ATOM   13400 O  OE2   . GLU C 2 334 ? 154.606 109.473 105.916 1.00 37.50 -1 313 GLU C OE2   1 
ATOM   13401 N  N     . PRO C 2 335 ? 154.771 111.322 110.921 1.00 33.23 ?  314 PRO C N     1 
ATOM   13402 C  CA    . PRO C 2 335 ? 155.769 112.341 111.260 1.00 32.48 ?  314 PRO C CA    1 
ATOM   13403 C  C     . PRO C 2 335 ? 156.338 113.018 110.024 1.00 32.75 ?  314 PRO C C     1 
ATOM   13404 O  O     . PRO C 2 335 ? 156.451 112.422 108.951 1.00 33.62 ?  314 PRO C O     1 
ATOM   13405 C  CB    . PRO C 2 335 ? 156.848 111.544 112.001 1.00 27.14 ?  314 PRO C CB    1 
ATOM   13406 C  CG    . PRO C 2 335 ? 156.714 110.160 111.467 1.00 33.25 ?  314 PRO C CG    1 
ATOM   13407 C  CD    . PRO C 2 335 ? 155.242 109.962 111.235 1.00 31.97 ?  314 PRO C CD    1 
ATOM   13408 N  N     . LEU C 2 336 ? 156.694 114.289 110.193 1.00 31.37 ?  315 LEU C N     1 
ATOM   13409 C  CA    . LEU C 2 336 ? 157.298 115.061 109.119 1.00 25.32 ?  315 LEU C CA    1 
ATOM   13410 C  C     . LEU C 2 336 ? 158.745 114.640 108.911 1.00 30.05 ?  315 LEU C C     1 
ATOM   13411 O  O     . LEU C 2 336 ? 159.501 114.464 109.871 1.00 28.04 ?  315 LEU C O     1 
ATOM   13412 C  CB    . LEU C 2 336 ? 157.239 116.554 109.434 1.00 24.68 ?  315 LEU C CB    1 
ATOM   13413 C  CG    . LEU C 2 336 ? 156.023 117.352 108.969 1.00 29.53 ?  315 LEU C CG    1 
ATOM   13414 C  CD1   . LEU C 2 336 ? 155.947 118.660 109.737 1.00 23.58 ?  315 LEU C CD1   1 
ATOM   13415 C  CD2   . LEU C 2 336 ? 156.084 117.609 107.475 1.00 23.76 ?  315 LEU C CD2   1 
ATOM   13416 N  N     . LYS C 2 337 ? 159.131 114.485 107.650 1.00 29.08 ?  316 LYS C N     1 
ATOM   13417 C  CA    . LYS C 2 337 ? 160.512 114.196 107.307 1.00 24.90 ?  316 LYS C CA    1 
ATOM   13418 C  C     . LYS C 2 337 ? 161.273 115.492 107.045 1.00 25.51 ?  316 LYS C C     1 
ATOM   13419 O  O     . LYS C 2 337 ? 160.692 116.568 106.894 1.00 33.13 ?  316 LYS C O     1 
ATOM   13420 C  CB    . LYS C 2 337 ? 160.586 113.279 106.086 1.00 29.23 ?  316 LYS C CB    1 
ATOM   13421 C  CG    . LYS C 2 337 ? 159.685 112.061 106.155 1.00 29.66 ?  316 LYS C CG    1 
ATOM   13422 C  CD    . LYS C 2 337 ? 160.135 110.994 105.169 1.00 30.93 ?  316 LYS C CD    1 
ATOM   13423 C  CE    . LYS C 2 337 ? 159.564 109.631 105.524 1.00 33.14 ?  316 LYS C CE    1 
ATOM   13424 N  NZ    . LYS C 2 337 ? 158.199 109.736 106.111 1.00 33.67 1  316 LYS C NZ    1 
ATOM   13425 N  N     . ASP C 2 338 ? 162.601 115.379 107.002 1.00 26.51 ?  317 ASP C N     1 
ATOM   13426 C  CA    . ASP C 2 338 ? 163.423 116.535 106.665 1.00 29.94 ?  317 ASP C CA    1 
ATOM   13427 C  C     . ASP C 2 338 ? 163.167 116.989 105.234 1.00 29.65 ?  317 ASP C C     1 
ATOM   13428 O  O     . ASP C 2 338 ? 163.107 118.191 104.957 1.00 24.94 ?  317 ASP C O     1 
ATOM   13429 C  CB    . ASP C 2 338 ? 164.902 116.209 106.870 1.00 32.12 ?  317 ASP C CB    1 
ATOM   13430 C  CG    . ASP C 2 338 ? 165.369 116.487 108.284 1.00 35.61 ?  317 ASP C CG    1 
ATOM   13431 O  OD1   . ASP C 2 338 ? 165.181 115.614 109.157 1.00 36.45 ?  317 ASP C OD1   1 
ATOM   13432 O  OD2   . ASP C 2 338 ? 165.924 117.580 108.525 1.00 32.88 -1 317 ASP C OD2   1 
ATOM   13433 N  N     . ASP C 2 339 ? 163.002 116.038 104.313 1.00 31.98 ?  318 ASP C N     1 
ATOM   13434 C  CA    . ASP C 2 339 ? 162.770 116.365 102.912 1.00 23.82 ?  318 ASP C CA    1 
ATOM   13435 C  C     . ASP C 2 339 ? 161.410 117.004 102.666 1.00 21.90 ?  318 ASP C C     1 
ATOM   13436 O  O     . ASP C 2 339 ? 161.187 117.539 101.574 1.00 29.62 ?  318 ASP C O     1 
ATOM   13437 C  CB    . ASP C 2 339 ? 162.910 115.106 102.052 1.00 24.61 ?  318 ASP C CB    1 
ATOM   13438 C  CG    . ASP C 2 339 ? 164.350 114.650 101.919 1.00 36.61 ?  318 ASP C CG    1 
ATOM   13439 O  OD1   . ASP C 2 339 ? 165.253 115.511 101.940 1.00 34.94 ?  318 ASP C OD1   1 
ATOM   13440 O  OD2   . ASP C 2 339 ? 164.577 113.427 101.795 1.00 37.02 -1 318 ASP C OD2   1 
ATOM   13441 N  N     . ASP C 2 340 ? 160.498 116.958 103.639 1.00 21.75 ?  319 ASP C N     1 
ATOM   13442 C  CA    . ASP C 2 340 ? 159.197 117.597 103.487 1.00 12.52 ?  319 ASP C CA    1 
ATOM   13443 C  C     . ASP C 2 340 ? 159.278 119.116 103.523 1.00 11.68 ?  319 ASP C C     1 
ATOM   13444 O  O     . ASP C 2 340 ? 158.326 119.779 103.099 1.00 29.94 ?  319 ASP C O     1 
ATOM   13445 C  CB    . ASP C 2 340 ? 158.246 117.114 104.582 1.00 15.38 ?  319 ASP C CB    1 
ATOM   13446 C  CG    . ASP C 2 340 ? 157.780 115.693 104.361 1.00 27.80 ?  319 ASP C CG    1 
ATOM   13447 O  OD1   . ASP C 2 340 ? 157.078 115.157 105.243 1.00 35.11 ?  319 ASP C OD1   1 
ATOM   13448 O  OD2   . ASP C 2 340 ? 158.112 115.113 103.307 1.00 32.85 -1 319 ASP C OD2   1 
ATOM   13449 N  N     . PHE C 2 341 ? 160.379 119.677 104.014 1.00 19.10 ?  320 PHE C N     1 
ATOM   13450 C  CA    . PHE C 2 341 ? 160.535 121.117 104.156 1.00 9.08  ?  320 PHE C CA    1 
ATOM   13451 C  C     . PHE C 2 341 ? 161.213 121.763 102.957 1.00 17.46 ?  320 PHE C C     1 
ATOM   13452 O  O     . PHE C 2 341 ? 161.395 122.984 102.952 1.00 21.47 ?  320 PHE C O     1 
ATOM   13453 C  CB    . PHE C 2 341 ? 161.324 121.431 105.428 1.00 14.57 ?  320 PHE C CB    1 
ATOM   13454 C  CG    . PHE C 2 341 ? 160.556 121.179 106.691 1.00 10.84 ?  320 PHE C CG    1 
ATOM   13455 C  CD1   . PHE C 2 341 ? 159.822 122.190 107.283 1.00 9.48  ?  320 PHE C CD1   1 
ATOM   13456 C  CD2   . PHE C 2 341 ? 160.562 119.928 107.283 1.00 12.36 ?  320 PHE C CD2   1 
ATOM   13457 C  CE1   . PHE C 2 341 ? 159.113 121.959 108.444 1.00 7.91  ?  320 PHE C CE1   1 
ATOM   13458 C  CE2   . PHE C 2 341 ? 159.853 119.693 108.441 1.00 13.16 ?  320 PHE C CE2   1 
ATOM   13459 C  CZ    . PHE C 2 341 ? 159.128 120.710 109.023 1.00 4.56  ?  320 PHE C CZ    1 
ATOM   13460 N  N     . TYR C 2 342 ? 161.590 120.985 101.948 1.00 9.53  ?  321 TYR C N     1 
ATOM   13461 C  CA    . TYR C 2 342 ? 162.203 121.516 100.740 1.00 17.23 ?  321 TYR C CA    1 
ATOM   13462 C  C     . TYR C 2 342 ? 161.401 121.079 99.525  1.00 16.10 ?  321 TYR C C     1 
ATOM   13463 O  O     . TYR C 2 342 ? 160.844 119.979 99.486  1.00 16.88 ?  321 TYR C O     1 
ATOM   13464 C  CB    . TYR C 2 342 ? 163.677 121.086 100.584 1.00 17.88 ?  321 TYR C CB    1 
ATOM   13465 C  CG    . TYR C 2 342 ? 164.497 121.128 101.856 1.00 13.83 ?  321 TYR C CG    1 
ATOM   13466 C  CD1   . TYR C 2 342 ? 164.347 120.169 102.848 1.00 18.12 ?  321 TYR C CD1   1 
ATOM   13467 C  CD2   . TYR C 2 342 ? 165.421 122.142 102.065 1.00 16.03 ?  321 TYR C CD2   1 
ATOM   13468 C  CE1   . TYR C 2 342 ? 165.099 120.217 104.006 1.00 15.48 ?  321 TYR C CE1   1 
ATOM   13469 C  CE2   . TYR C 2 342 ? 166.175 122.197 103.220 1.00 17.80 ?  321 TYR C CE2   1 
ATOM   13470 C  CZ    . TYR C 2 342 ? 166.010 121.233 104.187 1.00 19.62 ?  321 TYR C CZ    1 
ATOM   13471 O  OH    . TYR C 2 342 ? 166.759 121.284 105.339 1.00 28.71 ?  321 TYR C OH    1 
ATOM   13472 N  N     . PHE C 2 343 ? 161.349 121.962 98.534  1.00 7.71  ?  322 PHE C N     1 
ATOM   13473 C  CA    . PHE C 2 343 ? 160.512 121.761 97.360  1.00 20.35 ?  322 PHE C CA    1 
ATOM   13474 C  C     . PHE C 2 343 ? 161.271 122.102 96.083  1.00 25.47 ?  322 PHE C C     1 
ATOM   13475 O  O     . PHE C 2 343 ? 162.240 122.860 96.107  1.00 26.11 ?  322 PHE C O     1 
ATOM   13476 C  CB    . PHE C 2 343 ? 159.244 122.610 97.470  1.00 15.28 ?  322 PHE C CB    1 
ATOM   13477 C  CG    . PHE C 2 343 ? 158.464 122.366 98.728  1.00 13.74 ?  322 PHE C CG    1 
ATOM   13478 C  CD1   . PHE C 2 343 ? 157.572 121.312 98.813  1.00 17.31 ?  322 PHE C CD1   1 
ATOM   13479 C  CD2   . PHE C 2 343 ? 158.638 123.178 99.833  1.00 4.75  ?  322 PHE C CD2   1 
ATOM   13480 C  CE1   . PHE C 2 343 ? 156.861 121.083 99.972  1.00 16.31 ?  322 PHE C CE1   1 
ATOM   13481 C  CE2   . PHE C 2 343 ? 157.932 122.952 100.993 1.00 5.64  ?  322 PHE C CE2   1 
ATOM   13482 C  CZ    . PHE C 2 343 ? 157.040 121.904 101.063 1.00 10.19 ?  322 PHE C CZ    1 
ATOM   13483 N  N     . ASP D 2 37  ? 122.647 105.868 148.444 1.00 32.44 ?  16  ASP D N     1 
ATOM   13484 C  CA    . ASP D 2 37  ? 122.672 107.259 147.983 1.00 32.83 ?  16  ASP D CA    1 
ATOM   13485 C  C     . ASP D 2 37  ? 123.379 107.458 146.643 1.00 31.65 ?  16  ASP D C     1 
ATOM   13486 O  O     . ASP D 2 37  ? 123.364 108.568 146.104 1.00 32.65 ?  16  ASP D O     1 
ATOM   13487 C  CB    . ASP D 2 37  ? 123.371 108.159 149.013 1.00 33.73 ?  16  ASP D CB    1 
ATOM   13488 C  CG    . ASP D 2 37  ? 122.621 108.255 150.333 1.00 36.81 ?  16  ASP D CG    1 
ATOM   13489 O  OD1   . ASP D 2 37  ? 123.263 108.651 151.336 1.00 39.69 ?  16  ASP D OD1   1 
ATOM   13490 O  OD2   . ASP D 2 37  ? 121.410 107.938 150.380 1.00 39.67 -1 16  ASP D OD2   1 
ATOM   13491 N  N     . PHE D 2 38  ? 124.000 106.410 146.106 1.00 29.55 ?  17  PHE D N     1 
ATOM   13492 C  CA    . PHE D 2 38  ? 124.964 106.613 145.024 1.00 27.75 ?  17  PHE D CA    1 
ATOM   13493 C  C     . PHE D 2 38  ? 124.945 105.612 143.858 1.00 26.21 ?  17  PHE D C     1 
ATOM   13494 O  O     . PHE D 2 38  ? 125.464 105.914 142.789 1.00 25.93 ?  17  PHE D O     1 
ATOM   13495 C  CB    . PHE D 2 38  ? 126.387 106.717 145.619 1.00 27.37 ?  17  PHE D CB    1 
ATOM   13496 C  CG    . PHE D 2 38  ? 126.812 105.494 146.387 1.00 27.32 ?  17  PHE D CG    1 
ATOM   13497 C  CD1   . PHE D 2 38  ? 127.361 104.400 145.726 1.00 27.01 ?  17  PHE D CD1   1 
ATOM   13498 C  CD2   . PHE D 2 38  ? 126.663 105.432 147.767 1.00 28.02 ?  17  PHE D CD2   1 
ATOM   13499 C  CE1   . PHE D 2 38  ? 127.750 103.261 146.429 1.00 27.66 ?  17  PHE D CE1   1 
ATOM   13500 C  CE2   . PHE D 2 38  ? 127.043 104.298 148.473 1.00 27.68 ?  17  PHE D CE2   1 
ATOM   13501 C  CZ    . PHE D 2 38  ? 127.589 103.209 147.801 1.00 27.47 ?  17  PHE D CZ    1 
ATOM   13502 N  N     . THR D 2 39  ? 124.359 104.435 144.056 1.00 24.88 ?  18  THR D N     1 
ATOM   13503 C  CA    . THR D 2 39  ? 124.454 103.355 143.061 1.00 23.81 ?  18  THR D CA    1 
ATOM   13504 C  C     . THR D 2 39  ? 123.793 103.677 141.708 1.00 23.56 ?  18  THR D C     1 
ATOM   13505 O  O     . THR D 2 39  ? 124.349 103.384 140.650 1.00 23.02 ?  18  THR D O     1 
ATOM   13506 C  CB    . THR D 2 39  ? 123.988 101.998 143.642 1.00 23.40 ?  18  THR D CB    1 
ATOM   13507 O  OG1   . THR D 2 39  ? 125.032 101.460 144.464 1.00 23.77 ?  18  THR D OG1   1 
ATOM   13508 C  CG2   . THR D 2 39  ? 123.686 100.991 142.545 1.00 22.31 ?  18  THR D CG2   1 
ATOM   13509 N  N     . GLN D 2 40  ? 122.619 104.294 141.732 1.00 23.78 ?  19  GLN D N     1 
ATOM   13510 C  CA    . GLN D 2 40  ? 121.970 104.655 140.468 1.00 23.88 ?  19  GLN D CA    1 
ATOM   13511 C  C     . GLN D 2 40  ? 122.765 105.706 139.689 1.00 24.09 ?  19  GLN D C     1 
ATOM   13512 O  O     . GLN D 2 40  ? 122.911 105.603 138.479 1.00 23.15 ?  19  GLN D O     1 
ATOM   13513 C  CB    . GLN D 2 40  ? 120.517 105.083 140.685 1.00 24.53 ?  19  GLN D CB    1 
ATOM   13514 C  CG    . GLN D 2 40  ? 119.641 103.924 141.134 1.00 24.06 ?  19  GLN D CG    1 
ATOM   13515 C  CD    . GLN D 2 40  ? 118.165 104.172 140.927 1.00 25.83 ?  19  GLN D CD    1 
ATOM   13516 O  OE1   . GLN D 2 40  ? 117.776 105.111 140.236 1.00 25.90 ?  19  GLN D OE1   1 
ATOM   13517 N  NE2   . GLN D 2 40  ? 117.331 103.312 141.511 1.00 23.56 ?  19  GLN D NE2   1 
ATOM   13518 N  N     . MET D 2 41  ? 123.316 106.688 140.392 1.00 24.07 ?  20  MET D N     1 
ATOM   13519 C  CA    . MET D 2 41  ? 124.208 107.660 139.759 1.00 25.53 ?  20  MET D CA    1 
ATOM   13520 C  C     . MET D 2 41  ? 125.435 106.996 139.101 1.00 24.24 ?  20  MET D C     1 
ATOM   13521 O  O     . MET D 2 41  ? 125.803 107.342 137.974 1.00 23.16 ?  20  MET D O     1 
ATOM   13522 C  CB    . MET D 2 41  ? 124.637 108.719 140.779 1.00 26.79 ?  20  MET D CB    1 
ATOM   13523 C  CG    . MET D 2 41  ? 125.591 109.770 140.245 1.00 32.62 ?  20  MET D CG    1 
ATOM   13524 S  SD    . MET D 2 41  ? 126.271 110.740 141.611 1.00 44.01 ?  20  MET D SD    1 
ATOM   13525 C  CE    . MET D 2 41  ? 127.815 111.313 140.894 1.00 41.93 ?  20  MET D CE    1 
ATOM   13526 N  N     . PHE D 2 42  ? 126.056 106.039 139.793 1.00 23.31 ?  21  PHE D N     1 
ATOM   13527 C  CA    . PHE D 2 42  ? 127.209 105.341 139.223 1.00 23.44 ?  21  PHE D CA    1 
ATOM   13528 C  C     . PHE D 2 42  ? 126.814 104.417 138.088 1.00 23.55 ?  21  PHE D C     1 
ATOM   13529 O  O     . PHE D 2 42  ? 127.567 104.255 137.134 1.00 23.74 ?  21  PHE D O     1 
ATOM   13530 C  CB    . PHE D 2 42  ? 128.001 104.588 140.294 1.00 22.97 ?  21  PHE D CB    1 
ATOM   13531 C  CG    . PHE D 2 42  ? 129.009 105.445 140.976 1.00 23.86 ?  21  PHE D CG    1 
ATOM   13532 C  CD1   . PHE D 2 42  ? 130.332 105.462 140.544 1.00 24.55 ?  21  PHE D CD1   1 
ATOM   13533 C  CD2   . PHE D 2 42  ? 128.634 106.270 142.020 1.00 24.06 ?  21  PHE D CD2   1 
ATOM   13534 C  CE1   . PHE D 2 42  ? 131.275 106.281 141.169 1.00 25.78 ?  21  PHE D CE1   1 
ATOM   13535 C  CE2   . PHE D 2 42  ? 129.571 107.094 142.651 1.00 25.25 ?  21  PHE D CE2   1 
ATOM   13536 C  CZ    . PHE D 2 42  ? 130.883 107.103 142.225 1.00 25.79 ?  21  PHE D CZ    1 
ATOM   13537 N  N     . TYR D 2 43  ? 125.622 103.833 138.192 1.00 24.08 ?  22  TYR D N     1 
ATOM   13538 C  CA    . TYR D 2 43  ? 125.067 103.046 137.102 1.00 24.74 ?  22  TYR D CA    1 
ATOM   13539 C  C     . TYR D 2 43  ? 125.051 103.888 135.824 1.00 25.72 ?  22  TYR D C     1 
ATOM   13540 O  O     . TYR D 2 43  ? 125.537 103.452 134.776 1.00 25.56 ?  22  TYR D O     1 
ATOM   13541 C  CB    . TYR D 2 43  ? 123.652 102.538 137.425 1.00 24.90 ?  22  TYR D CB    1 
ATOM   13542 C  CG    . TYR D 2 43  ? 123.005 101.863 136.223 1.00 24.38 ?  22  TYR D CG    1 
ATOM   13543 C  CD1   . TYR D 2 43  ? 123.169 100.503 135.997 1.00 23.96 ?  22  TYR D CD1   1 
ATOM   13544 C  CD2   . TYR D 2 43  ? 122.280 102.606 135.287 1.00 24.73 ?  22  TYR D CD2   1 
ATOM   13545 C  CE1   . TYR D 2 43  ? 122.608 99.886  134.876 1.00 23.42 ?  22  TYR D CE1   1 
ATOM   13546 C  CE2   . TYR D 2 43  ? 121.702 102.002 134.168 1.00 26.65 ?  22  TYR D CE2   1 
ATOM   13547 C  CZ    . TYR D 2 43  ? 121.876 100.642 133.972 1.00 25.68 ?  22  TYR D CZ    1 
ATOM   13548 O  OH    . TYR D 2 43  ? 121.311 100.042 132.870 1.00 26.57 ?  22  TYR D OH    1 
ATOM   13549 N  N     . ASN D 2 44  ? 124.484 105.088 135.928 1.00 26.77 ?  23  ASN D N     1 
ATOM   13550 C  CA    . ASN D 2 44  ? 124.370 106.000 134.797 1.00 28.57 ?  23  ASN D CA    1 
ATOM   13551 C  C     . ASN D 2 44  ? 125.718 106.343 134.191 1.00 28.70 ?  23  ASN D C     1 
ATOM   13552 O  O     . ASN D 2 44  ? 125.909 106.193 132.981 1.00 28.99 ?  23  ASN D O     1 
ATOM   13553 C  CB    . ASN D 2 44  ? 123.598 107.260 135.200 1.00 29.62 ?  23  ASN D CB    1 
ATOM   13554 C  CG    . ASN D 2 44  ? 122.123 106.977 135.451 1.00 32.44 ?  23  ASN D CG    1 
ATOM   13555 O  OD1   . ASN D 2 44  ? 121.574 105.982 134.960 1.00 34.30 ?  23  ASN D OD1   1 
ATOM   13556 N  ND2   . ASN D 2 44  ? 121.471 107.847 136.220 1.00 35.17 ?  23  ASN D ND2   1 
ATOM   13557 N  N     . GLN D 2 45  ? 126.657 106.756 135.038 1.00 28.97 ?  24  GLN D N     1 
ATOM   13558 C  CA    . GLN D 2 45  ? 127.990 107.128 134.578 1.00 29.99 ?  24  GLN D CA    1 
ATOM   13559 C  C     . GLN D 2 45  ? 128.736 105.951 133.932 1.00 29.69 ?  24  GLN D C     1 
ATOM   13560 O  O     . GLN D 2 45  ? 129.411 106.126 132.919 1.00 30.01 ?  24  GLN D O     1 
ATOM   13561 C  CB    . GLN D 2 45  ? 128.812 107.746 135.715 1.00 30.27 ?  24  GLN D CB    1 
ATOM   13562 C  CG    . GLN D 2 45  ? 130.145 108.377 135.250 1.00 32.29 ?  24  GLN D CG    1 
ATOM   13563 C  CD    . GLN D 2 45  ? 129.955 109.546 134.292 1.00 35.95 ?  24  GLN D CD    1 
ATOM   13564 O  OE1   . GLN D 2 45  ? 128.936 110.242 134.329 1.00 36.72 ?  24  GLN D OE1   1 
ATOM   13565 N  NE2   . GLN D 2 45  ? 130.941 109.769 133.429 1.00 37.05 ?  24  GLN D NE2   1 
ATOM   13566 N  N     . ASN D 2 46  ? 128.588 104.756 134.502 1.00 28.93 ?  25  ASN D N     1 
ATOM   13567 C  CA    . ASN D 2 46  ? 129.202 103.564 133.942 1.00 28.70 ?  25  ASN D CA    1 
ATOM   13568 C  C     . ASN D 2 46  ? 128.690 103.207 132.553 1.00 29.05 ?  25  ASN D C     1 
ATOM   13569 O  O     . ASN D 2 46  ? 129.487 103.019 131.630 1.00 28.51 ?  25  ASN D O     1 
ATOM   13570 C  CB    . ASN D 2 46  ? 129.056 102.365 134.889 1.00 28.36 ?  25  ASN D CB    1 
ATOM   13571 C  CG    . ASN D 2 46  ? 130.181 102.286 135.898 1.00 28.45 ?  25  ASN D CG    1 
ATOM   13572 O  OD1   . ASN D 2 46  ? 131.149 101.558 135.690 1.00 28.03 ?  25  ASN D OD1   1 
ATOM   13573 N  ND2   . ASN D 2 46  ? 130.077 103.055 136.980 1.00 26.53 ?  25  ASN D ND2   1 
ATOM   13574 N  N     . VAL D 2 47  ? 127.368 103.140 132.399 1.00 29.66 ?  26  VAL D N     1 
ATOM   13575 C  CA    . VAL D 2 47  ? 126.785 102.693 131.133 1.00 31.15 ?  26  VAL D CA    1 
ATOM   13576 C  C     . VAL D 2 47  ? 126.962 103.734 130.031 1.00 32.39 ?  26  VAL D C     1 
ATOM   13577 O  O     . VAL D 2 47  ? 127.083 103.383 128.859 1.00 32.80 ?  26  VAL D O     1 
ATOM   13578 C  CB    . VAL D 2 47  ? 125.295 102.226 131.252 1.00 31.08 ?  26  VAL D CB    1 
ATOM   13579 C  CG1   . VAL D 2 47  ? 125.155 101.129 132.300 1.00 31.09 ?  26  VAL D CG1   1 
ATOM   13580 C  CG2   . VAL D 2 47  ? 124.347 103.399 131.544 1.00 30.81 ?  26  VAL D CG2   1 
ATOM   13581 N  N     . LYS D 2 48  ? 127.011 105.009 130.399 1.00 33.28 ?  27  LYS D N     1 
ATOM   13582 C  CA    . LYS D 2 48  ? 127.226 106.027 129.384 1.00 34.87 ?  27  LYS D CA    1 
ATOM   13583 C  C     . LYS D 2 48  ? 128.692 106.123 128.913 1.00 34.91 ?  27  LYS D C     1 
ATOM   13584 O  O     . LYS D 2 48  ? 128.977 106.760 127.902 1.00 34.92 ?  27  LYS D O     1 
ATOM   13585 C  CB    . LYS D 2 48  ? 126.638 107.381 129.810 1.00 35.45 ?  27  LYS D CB    1 
ATOM   13586 C  CG    . LYS D 2 48  ? 127.521 108.261 130.664 1.00 37.41 ?  27  LYS D CG    1 
ATOM   13587 C  CD    . LYS D 2 48  ? 126.971 109.696 130.672 1.00 40.91 ?  27  LYS D CD    1 
ATOM   13588 C  CE    . LYS D 2 48  ? 128.024 110.688 131.175 1.00 42.46 ?  27  LYS D CE    1 
ATOM   13589 N  NZ    . LYS D 2 48  ? 127.587 112.110 131.055 1.00 45.13 1  27  LYS D NZ    1 
ATOM   13590 N  N     . GLN D 2 49  ? 129.599 105.467 129.640 1.00 34.66 ?  28  GLN D N     1 
ATOM   13591 C  CA    . GLN D 2 49  ? 131.011 105.387 129.276 1.00 34.64 ?  28  GLN D CA    1 
ATOM   13592 C  C     . GLN D 2 49  ? 131.315 104.132 128.461 1.00 34.20 ?  28  GLN D C     1 
ATOM   13593 O  O     . GLN D 2 49  ? 132.484 103.836 128.206 1.00 34.53 ?  28  GLN D O     1 
ATOM   13594 C  CB    . GLN D 2 49  ? 131.903 105.399 130.534 1.00 34.89 ?  28  GLN D CB    1 
ATOM   13595 C  CG    . GLN D 2 49  ? 132.282 106.788 131.043 1.00 36.47 ?  28  GLN D CG    1 
ATOM   13596 C  CD    . GLN D 2 49  ? 132.999 106.768 132.396 1.00 38.37 ?  28  GLN D CD    1 
ATOM   13597 O  OE1   . GLN D 2 49  ? 132.862 107.702 133.187 1.00 40.68 ?  28  GLN D OE1   1 
ATOM   13598 N  NE2   . GLN D 2 49  ? 133.760 105.707 132.666 1.00 38.57 ?  28  GLN D NE2   1 
ATOM   13599 N  N     . PHE D 2 50  ? 130.282 103.391 128.058 1.00 33.42 ?  29  PHE D N     1 
ATOM   13600 C  CA    . PHE D 2 50  ? 130.494 102.131 127.348 1.00 32.57 ?  29  PHE D CA    1 
ATOM   13601 C  C     . PHE D 2 50  ? 131.217 102.381 126.023 1.00 32.60 ?  29  PHE D C     1 
ATOM   13602 O  O     . PHE D 2 50  ? 130.924 103.348 125.314 1.00 32.39 ?  29  PHE D O     1 
ATOM   13603 C  CB    . PHE D 2 50  ? 129.178 101.368 127.125 1.00 32.77 ?  29  PHE D CB    1 
ATOM   13604 C  CG    . PHE D 2 50  ? 129.351 100.037 126.420 1.00 32.24 ?  29  PHE D CG    1 
ATOM   13605 C  CD1   . PHE D 2 50  ? 129.860 98.932  127.097 1.00 31.50 ?  29  PHE D CD1   1 
ATOM   13606 C  CD2   . PHE D 2 50  ? 129.007 99.895  125.081 1.00 33.60 ?  29  PHE D CD2   1 
ATOM   13607 C  CE1   . PHE D 2 50  ? 130.023 97.714  126.457 1.00 33.02 ?  29  PHE D CE1   1 
ATOM   13608 C  CE2   . PHE D 2 50  ? 129.170 98.674  124.423 1.00 33.78 ?  29  PHE D CE2   1 
ATOM   13609 C  CZ    . PHE D 2 50  ? 129.671 97.581  125.112 1.00 33.13 ?  29  PHE D CZ    1 
ATOM   13610 N  N     . TRP D 2 51  ? 132.167 101.508 125.711 1.00 31.95 ?  30  TRP D N     1 
ATOM   13611 C  CA    . TRP D 2 51  ? 132.959 101.611 124.485 1.00 32.03 ?  30  TRP D CA    1 
ATOM   13612 C  C     . TRP D 2 51  ? 133.451 100.226 124.086 1.00 33.03 ?  30  TRP D C     1 
ATOM   13613 O  O     . TRP D 2 51  ? 133.357 99.275  124.866 1.00 32.54 ?  30  TRP D O     1 
ATOM   13614 C  CB    . TRP D 2 51  ? 134.132 102.588 124.660 1.00 31.19 ?  30  TRP D CB    1 
ATOM   13615 C  CG    . TRP D 2 51  ? 135.118 102.184 125.738 1.00 28.11 ?  30  TRP D CG    1 
ATOM   13616 C  CD1   . TRP D 2 51  ? 134.970 102.348 127.080 1.00 26.51 ?  30  TRP D CD1   1 
ATOM   13617 C  CD2   . TRP D 2 51  ? 136.390 101.545 125.549 1.00 25.93 ?  30  TRP D CD2   1 
ATOM   13618 N  NE1   . TRP D 2 51  ? 136.075 101.857 127.745 1.00 24.52 ?  30  TRP D NE1   1 
ATOM   13619 C  CE2   . TRP D 2 51  ? 136.958 101.356 126.830 1.00 24.42 ?  30  TRP D CE2   1 
ATOM   13620 C  CE3   . TRP D 2 51  ? 137.109 101.119 124.422 1.00 25.37 ?  30  TRP D CE3   1 
ATOM   13621 C  CZ2   . TRP D 2 51  ? 138.215 100.764 127.017 1.00 24.00 ?  30  TRP D CZ2   1 
ATOM   13622 C  CZ3   . TRP D 2 51  ? 138.356 100.521 124.609 1.00 24.99 ?  30  TRP D CZ3   1 
ATOM   13623 C  CH2   . TRP D 2 51  ? 138.894 100.350 125.897 1.00 23.72 ?  30  TRP D CH2   1 
ATOM   13624 N  N     . LEU D 2 52  ? 133.956 100.122 122.861 1.00 34.81 ?  31  LEU D N     1 
ATOM   13625 C  CA    . LEU D 2 52  ? 134.450 98.868  122.314 1.00 36.58 ?  31  LEU D CA    1 
ATOM   13626 C  C     . LEU D 2 52  ? 135.812 99.084  121.658 1.00 37.80 ?  31  LEU D C     1 
ATOM   13627 O  O     . LEU D 2 52  ? 136.064 100.153 121.109 1.00 37.92 ?  31  LEU D O     1 
ATOM   13628 C  CB    . LEU D 2 52  ? 133.448 98.290  121.302 1.00 36.95 ?  31  LEU D CB    1 
ATOM   13629 C  CG    . LEU D 2 52  ? 132.231 97.516  121.820 1.00 38.15 ?  31  LEU D CG    1 
ATOM   13630 C  CD1   . LEU D 2 52  ? 131.575 96.745  120.681 1.00 39.50 ?  31  LEU D CD1   1 
ATOM   13631 C  CD2   . LEU D 2 52  ? 132.601 96.553  122.942 1.00 37.94 ?  31  LEU D CD2   1 
ATOM   13632 N  N     . PRO D 2 53  ? 136.695 98.067  121.706 1.00 39.26 ?  32  PRO D N     1 
ATOM   13633 C  CA    . PRO D 2 53  ? 138.047 98.164  121.126 1.00 40.41 ?  32  PRO D CA    1 
ATOM   13634 C  C     . PRO D 2 53  ? 138.055 98.577  119.647 1.00 41.91 ?  32  PRO D C     1 
ATOM   13635 O  O     . PRO D 2 53  ? 138.846 99.439  119.248 1.00 42.52 ?  32  PRO D O     1 
ATOM   13636 C  CB    . PRO D 2 53  ? 138.590 96.737  121.264 1.00 40.42 ?  32  PRO D CB    1 
ATOM   13637 C  CG    . PRO D 2 53  ? 137.781 96.114  122.328 1.00 40.01 ?  32  PRO D CG    1 
ATOM   13638 C  CD    . PRO D 2 53  ? 136.427 96.727  122.257 1.00 39.30 ?  32  PRO D CD    1 
ATOM   13639 N  N     . GLU D 2 54  ? 137.166 97.978  118.860 1.00 43.27 ?  33  GLU D N     1 
ATOM   13640 C  CA    . GLU D 2 54  ? 137.059 98.220  117.411 1.00 45.17 ?  33  GLU D CA    1 
ATOM   13641 C  C     . GLU D 2 54  ? 136.914 99.694  116.999 1.00 45.57 ?  33  GLU D C     1 
ATOM   13642 O  O     . GLU D 2 54  ? 137.207 100.053 115.855 1.00 46.08 ?  33  GLU D O     1 
ATOM   13643 C  CB    . GLU D 2 54  ? 135.890 97.409  116.832 1.00 45.55 ?  33  GLU D CB    1 
ATOM   13644 C  CG    . GLU D 2 54  ? 136.207 95.940  116.540 1.00 48.19 ?  33  GLU D CG    1 
ATOM   13645 C  CD    . GLU D 2 54  ? 136.552 95.130  117.782 1.00 50.61 ?  33  GLU D CD    1 
ATOM   13646 O  OE1   . GLU D 2 54  ? 135.811 95.221  118.789 1.00 51.10 ?  33  GLU D OE1   1 
ATOM   13647 O  OE2   . GLU D 2 54  ? 137.574 94.403  117.747 1.00 52.64 -1 33  GLU D OE2   1 
ATOM   13648 N  N     . GLU D 2 55  ? 136.463 100.535 117.930 1.00 45.74 ?  34  GLU D N     1 
ATOM   13649 C  CA    . GLU D 2 55  ? 136.220 101.957 117.655 1.00 46.28 ?  34  GLU D CA    1 
ATOM   13650 C  C     . GLU D 2 55  ? 137.500 102.744 117.346 1.00 46.49 ?  34  GLU D C     1 
ATOM   13651 O  O     . GLU D 2 55  ? 137.468 103.722 116.594 1.00 46.73 ?  34  GLU D O     1 
ATOM   13652 C  CB    . GLU D 2 55  ? 135.463 102.615 118.814 1.00 46.17 ?  34  GLU D CB    1 
ATOM   13653 C  CG    . GLU D 2 55  ? 134.058 102.059 119.065 1.00 47.10 ?  34  GLU D CG    1 
ATOM   13654 C  CD    . GLU D 2 55  ? 133.336 102.794 120.192 1.00 48.43 ?  34  GLU D CD    1 
ATOM   13655 O  OE1   . GLU D 2 55  ? 133.076 104.009 120.047 1.00 49.62 ?  34  GLU D OE1   1 
ATOM   13656 O  OE2   . GLU D 2 55  ? 133.026 102.159 121.222 1.00 47.11 -1 34  GLU D OE2   1 
ATOM   13657 N  N     . ILE D 2 56  ? 138.618 102.317 117.933 1.00 46.23 ?  35  ILE D N     1 
ATOM   13658 C  CA    . ILE D 2 56  ? 139.909 102.957 117.696 1.00 46.25 ?  35  ILE D CA    1 
ATOM   13659 C  C     . ILE D 2 56  ? 140.732 102.101 116.734 1.00 46.30 ?  35  ILE D C     1 
ATOM   13660 O  O     . ILE D 2 56  ? 141.023 100.936 117.023 1.00 46.36 ?  35  ILE D O     1 
ATOM   13661 C  CB    . ILE D 2 56  ? 140.713 103.172 119.026 1.00 45.84 ?  35  ILE D CB    1 
ATOM   13662 C  CG1   . ILE D 2 56  ? 139.815 103.670 120.178 1.00 46.15 ?  35  ILE D CG1   1 
ATOM   13663 C  CG2   . ILE D 2 56  ? 141.939 104.080 118.798 1.00 45.72 ?  35  ILE D CG2   1 
ATOM   13664 C  CD1   . ILE D 2 56  ? 139.161 105.031 119.974 1.00 47.27 ?  35  ILE D CD1   1 
ATOM   13665 N  N     . ALA D 2 57  ? 141.094 102.672 115.589 1.00 46.51 ?  36  ALA D N     1 
ATOM   13666 C  CA    . ALA D 2 57  ? 141.990 102.002 114.642 1.00 46.56 ?  36  ALA D CA    1 
ATOM   13667 C  C     . ALA D 2 57  ? 143.428 102.087 115.163 1.00 46.08 ?  36  ALA D C     1 
ATOM   13668 O  O     . ALA D 2 57  ? 143.915 103.179 115.451 1.00 45.70 ?  36  ALA D O     1 
ATOM   13669 C  CB    . ALA D 2 57  ? 141.878 102.633 113.257 1.00 47.10 ?  36  ALA D CB    1 
ATOM   13670 N  N     . LEU D 2 58  ? 144.099 100.942 115.267 1.00 45.66 ?  37  LEU D N     1 
ATOM   13671 C  CA    . LEU D 2 58  ? 145.426 100.886 115.899 1.00 45.27 ?  37  LEU D CA    1 
ATOM   13672 C  C     . LEU D 2 58  ? 146.632 100.963 114.965 1.00 45.25 ?  37  LEU D C     1 
ATOM   13673 O  O     . LEU D 2 58  ? 147.734 101.312 115.401 1.00 44.82 ?  37  LEU D O     1 
ATOM   13674 C  CB    . LEU D 2 58  ? 145.545 99.642  116.780 1.00 45.05 ?  37  LEU D CB    1 
ATOM   13675 C  CG    . LEU D 2 58  ? 144.861 99.755  118.140 1.00 45.41 ?  37  LEU D CG    1 
ATOM   13676 C  CD1   . LEU D 2 58  ? 144.987 98.444  118.891 1.00 45.40 ?  37  LEU D CD1   1 
ATOM   13677 C  CD2   . LEU D 2 58  ? 145.450 100.906 118.953 1.00 44.70 ?  37  LEU D CD2   1 
ATOM   13678 N  N     . ASN D 2 59  ? 146.427 100.655 113.687 1.00 45.33 ?  38  ASN D N     1 
ATOM   13679 C  CA    . ASN D 2 59  ? 147.546 100.470 112.759 1.00 45.22 ?  38  ASN D CA    1 
ATOM   13680 C  C     . ASN D 2 59  ? 148.480 101.677 112.593 1.00 44.39 ?  38  ASN D C     1 
ATOM   13681 O  O     . ASN D 2 59  ? 149.687 101.503 112.388 1.00 44.33 ?  38  ASN D O     1 
ATOM   13682 C  CB    . ASN D 2 59  ? 147.039 99.986  111.403 1.00 46.22 ?  38  ASN D CB    1 
ATOM   13683 C  CG    . ASN D 2 59  ? 147.995 99.010  110.740 1.00 47.90 ?  38  ASN D CG    1 
ATOM   13684 O  OD1   . ASN D 2 59  ? 148.525 99.278  109.663 1.00 49.28 ?  38  ASN D OD1   1 
ATOM   13685 N  ND2   . ASN D 2 59  ? 148.220 97.864  111.386 1.00 49.18 ?  38  ASN D ND2   1 
ATOM   13686 N  N     . GLY D 2 60  ? 147.926 102.885 112.706 1.00 43.45 ?  39  GLY D N     1 
ATOM   13687 C  CA    . GLY D 2 60  ? 148.699 104.126 112.587 1.00 42.42 ?  39  GLY D CA    1 
ATOM   13688 C  C     . GLY D 2 60  ? 149.733 104.380 113.681 1.00 41.55 ?  39  GLY D C     1 
ATOM   13689 O  O     . GLY D 2 60  ? 150.526 105.322 113.590 1.00 41.29 ?  39  GLY D O     1 
ATOM   13690 N  N     . ASP D 2 61  ? 149.726 103.550 114.723 1.00 40.35 ?  40  ASP D N     1 
ATOM   13691 C  CA    . ASP D 2 61  ? 150.748 103.625 115.773 1.00 39.53 ?  40  ASP D CA    1 
ATOM   13692 C  C     . ASP D 2 61  ? 152.117 103.146 115.311 1.00 39.38 ?  40  ASP D C     1 
ATOM   13693 O  O     . ASP D 2 61  ? 153.138 103.531 115.878 1.00 38.90 ?  40  ASP D O     1 
ATOM   13694 C  CB    . ASP D 2 61  ? 150.322 102.817 116.990 1.00 38.93 ?  40  ASP D CB    1 
ATOM   13695 C  CG    . ASP D 2 61  ? 149.445 103.600 117.925 1.00 38.21 ?  40  ASP D CG    1 
ATOM   13696 O  OD1   . ASP D 2 61  ? 149.171 104.791 117.654 1.00 38.79 ?  40  ASP D OD1   1 
ATOM   13697 O  OD2   . ASP D 2 61  ? 149.035 103.022 118.944 1.00 38.02 -1 40  ASP D OD2   1 
ATOM   13698 N  N     . LEU D 2 62  ? 152.128 102.306 114.282 1.00 39.82 ?  41  LEU D N     1 
ATOM   13699 C  CA    . LEU D 2 62  ? 153.365 101.754 113.742 1.00 40.22 ?  41  LEU D CA    1 
ATOM   13700 C  C     . LEU D 2 62  ? 154.268 102.844 113.165 1.00 40.40 ?  41  LEU D C     1 
ATOM   13701 O  O     . LEU D 2 62  ? 155.476 102.645 113.029 1.00 40.91 ?  41  LEU D O     1 
ATOM   13702 C  CB    . LEU D 2 62  ? 153.052 100.681 112.696 1.00 40.52 ?  41  LEU D CB    1 
ATOM   13703 C  CG    . LEU D 2 62  ? 152.354 99.418  113.214 1.00 41.03 ?  41  LEU D CG    1 
ATOM   13704 C  CD1   . LEU D 2 62  ? 152.013 98.482  112.062 1.00 42.53 ?  41  LEU D CD1   1 
ATOM   13705 C  CD2   . LEU D 2 62  ? 153.201 98.700  114.274 1.00 41.89 ?  41  LEU D CD2   1 
ATOM   13706 N  N     . LEU D 2 63  ? 153.669 103.997 112.855 1.00 40.20 ?  42  LEU D N     1 
ATOM   13707 C  CA    . LEU D 2 63  ? 154.373 105.159 112.313 1.00 39.85 ?  42  LEU D CA    1 
ATOM   13708 C  C     . LEU D 2 63  ? 155.179 105.934 113.372 1.00 38.90 ?  42  LEU D C     1 
ATOM   13709 O  O     . LEU D 2 63  ? 156.040 106.754 113.032 1.00 39.48 ?  42  LEU D O     1 
ATOM   13710 C  CB    . LEU D 2 63  ? 153.365 106.084 111.611 1.00 40.50 ?  42  LEU D CB    1 
ATOM   13711 C  CG    . LEU D 2 63  ? 153.741 106.915 110.374 1.00 41.98 ?  42  LEU D CG    1 
ATOM   13712 C  CD1   . LEU D 2 63  ? 154.298 106.059 109.242 1.00 43.07 ?  42  LEU D CD1   1 
ATOM   13713 C  CD2   . LEU D 2 63  ? 152.518 107.668 109.880 1.00 43.17 ?  42  LEU D CD2   1 
ATOM   13714 N  N     . THR D 2 64  ? 154.903 105.694 114.652 1.00 37.28 ?  43  THR D N     1 
ATOM   13715 C  CA    . THR D 2 64  ? 155.738 106.268 115.718 1.00 35.53 ?  43  THR D CA    1 
ATOM   13716 C  C     . THR D 2 64  ? 156.499 105.196 116.489 1.00 34.57 ?  43  THR D C     1 
ATOM   13717 O  O     . THR D 2 64  ? 157.588 105.453 117.008 1.00 34.23 ?  43  THR D O     1 
ATOM   13718 C  CB    . THR D 2 64  ? 154.956 107.175 116.695 1.00 35.18 ?  43  THR D CB    1 
ATOM   13719 O  OG1   . THR D 2 64  ? 153.760 106.521 117.133 1.00 34.59 ?  43  THR D OG1   1 
ATOM   13720 C  CG2   . THR D 2 64  ? 154.598 108.476 116.032 1.00 35.48 ?  43  THR D CG2   1 
ATOM   13721 N  N     . TRP D 2 65  ? 155.920 103.997 116.545 1.00 33.62 ?  44  TRP D N     1 
ATOM   13722 C  CA    . TRP D 2 65  ? 156.533 102.840 117.218 1.00 32.87 ?  44  TRP D CA    1 
ATOM   13723 C  C     . TRP D 2 65  ? 157.918 102.513 116.645 1.00 33.46 ?  44  TRP D C     1 
ATOM   13724 O  O     . TRP D 2 65  ? 158.862 102.258 117.393 1.00 32.58 ?  44  TRP D O     1 
ATOM   13725 C  CB    . TRP D 2 65  ? 155.604 101.621 117.108 1.00 32.09 ?  44  TRP D CB    1 
ATOM   13726 C  CG    . TRP D 2 65  ? 156.149 100.352 117.703 1.00 30.42 ?  44  TRP D CG    1 
ATOM   13727 C  CD1   . TRP D 2 65  ? 156.623 99.268  117.018 1.00 29.35 ?  44  TRP D CD1   1 
ATOM   13728 C  CD2   . TRP D 2 65  ? 156.270 100.031 119.097 1.00 28.04 ?  44  TRP D CD2   1 
ATOM   13729 N  NE1   . TRP D 2 65  ? 157.031 98.292  117.898 1.00 28.44 ?  44  TRP D NE1   1 
ATOM   13730 C  CE2   . TRP D 2 65  ? 156.829 98.736  119.179 1.00 28.14 ?  44  TRP D CE2   1 
ATOM   13731 C  CE3   . TRP D 2 65  ? 155.968 100.714 120.284 1.00 27.11 ?  44  TRP D CE3   1 
ATOM   13732 C  CZ2   . TRP D 2 65  ? 157.086 98.102  120.402 1.00 27.21 ?  44  TRP D CZ2   1 
ATOM   13733 C  CZ3   . TRP D 2 65  ? 156.217 100.078 121.504 1.00 27.45 ?  44  TRP D CZ3   1 
ATOM   13734 C  CH2   . TRP D 2 65  ? 156.767 98.782  121.548 1.00 27.25 ?  44  TRP D CH2   1 
ATOM   13735 N  N     . LYS D 2 66  ? 158.016 102.532 115.316 1.00 34.52 ?  45  LYS D N     1 
ATOM   13736 C  CA    . LYS D 2 66  ? 159.262 102.265 114.605 1.00 36.41 ?  45  LYS D CA    1 
ATOM   13737 C  C     . LYS D 2 66  ? 160.390 103.240 114.940 1.00 36.26 ?  45  LYS D C     1 
ATOM   13738 O  O     . LYS D 2 66  ? 161.560 102.919 114.736 1.00 36.52 ?  45  LYS D O     1 
ATOM   13739 C  CB    . LYS D 2 66  ? 159.023 102.243 113.089 1.00 36.98 ?  45  LYS D CB    1 
ATOM   13740 C  CG    . LYS D 2 66  ? 158.952 100.840 112.492 1.00 40.03 ?  45  LYS D CG    1 
ATOM   13741 C  CD    . LYS D 2 66  ? 157.680 100.089 112.901 1.00 43.70 ?  45  LYS D CD    1 
ATOM   13742 C  CE    . LYS D 2 66  ? 157.610 98.708  112.242 1.00 45.57 ?  45  LYS D CE    1 
ATOM   13743 N  NZ    . LYS D 2 66  ? 157.561 98.779  110.752 1.00 46.59 1  45  LYS D NZ    1 
ATOM   13744 N  N     . TYR D 2 67  ? 160.037 104.411 115.465 1.00 36.26 ?  46  TYR D N     1 
ATOM   13745 C  CA    . TYR D 2 67  ? 161.043 105.424 115.799 1.00 36.90 ?  46  TYR D CA    1 
ATOM   13746 C  C     . TYR D 2 67  ? 161.507 105.420 117.257 1.00 36.28 ?  46  TYR D C     1 
ATOM   13747 O  O     . TYR D 2 67  ? 162.365 106.216 117.627 1.00 36.44 ?  46  TYR D O     1 
ATOM   13748 C  CB    . TYR D 2 67  ? 160.581 106.825 115.383 1.00 37.15 ?  46  TYR D CB    1 
ATOM   13749 C  CG    . TYR D 2 67  ? 160.250 106.942 113.913 1.00 39.40 ?  46  TYR D CG    1 
ATOM   13750 C  CD1   . TYR D 2 67  ? 161.077 106.367 112.943 1.00 41.26 ?  46  TYR D CD1   1 
ATOM   13751 C  CD2   . TYR D 2 67  ? 159.129 107.647 113.488 1.00 41.06 ?  46  TYR D CD2   1 
ATOM   13752 C  CE1   . TYR D 2 67  ? 160.776 106.469 111.586 1.00 43.03 ?  46  TYR D CE1   1 
ATOM   13753 C  CE2   . TYR D 2 67  ? 158.822 107.762 112.130 1.00 43.05 ?  46  TYR D CE2   1 
ATOM   13754 C  CZ    . TYR D 2 67  ? 159.647 107.174 111.185 1.00 43.80 ?  46  TYR D CZ    1 
ATOM   13755 O  OH    . TYR D 2 67  ? 159.338 107.286 109.842 1.00 45.18 ?  46  TYR D OH    1 
ATOM   13756 N  N     . LEU D 2 68  ? 160.943 104.542 118.083 1.00 35.71 ?  47  LEU D N     1 
ATOM   13757 C  CA    . LEU D 2 68  ? 161.389 104.426 119.473 1.00 34.92 ?  47  LEU D CA    1 
ATOM   13758 C  C     . LEU D 2 68  ? 162.639 103.546 119.570 1.00 34.32 ?  47  LEU D C     1 
ATOM   13759 O  O     . LEU D 2 68  ? 162.810 102.606 118.789 1.00 34.50 ?  47  LEU D O     1 
ATOM   13760 C  CB    . LEU D 2 68  ? 160.277 103.874 120.377 1.00 35.00 ?  47  LEU D CB    1 
ATOM   13761 C  CG    . LEU D 2 68  ? 158.888 104.537 120.363 1.00 35.82 ?  47  LEU D CG    1 
ATOM   13762 C  CD1   . LEU D 2 68  ? 157.961 103.824 121.336 1.00 35.95 ?  47  LEU D CD1   1 
ATOM   13763 C  CD2   . LEU D 2 68  ? 158.939 106.033 120.673 1.00 35.97 ?  47  LEU D CD2   1 
ATOM   13764 N  N     . GLY D 2 69  ? 163.505 103.859 120.532 1.00 33.50 ?  48  GLY D N     1 
ATOM   13765 C  CA    . GLY D 2 69  ? 164.654 103.017 120.856 1.00 32.41 ?  48  GLY D CA    1 
ATOM   13766 C  C     . GLY D 2 69  ? 164.249 101.677 121.453 1.00 32.15 ?  48  GLY D C     1 
ATOM   13767 O  O     . GLY D 2 69  ? 163.092 101.479 121.847 1.00 30.98 ?  48  GLY D O     1 
ATOM   13768 N  N     . LYS D 2 70  ? 165.210 100.759 121.528 1.00 32.14 ?  49  LYS D N     1 
ATOM   13769 C  CA    . LYS D 2 70  ? 164.974 99.431  122.087 1.00 32.25 ?  49  LYS D CA    1 
ATOM   13770 C  C     . LYS D 2 70  ? 164.511 99.482  123.542 1.00 31.24 ?  49  LYS D C     1 
ATOM   13771 O  O     . LYS D 2 70  ? 163.596 98.748  123.909 1.00 31.34 ?  49  LYS D O     1 
ATOM   13772 C  CB    . LYS D 2 70  ? 166.221 98.553  121.959 1.00 33.07 ?  49  LYS D CB    1 
ATOM   13773 C  CG    . LYS D 2 70  ? 166.647 98.293  120.523 1.00 35.74 ?  49  LYS D CG    1 
ATOM   13774 C  CD    . LYS D 2 70  ? 168.038 97.667  120.489 1.00 39.67 ?  49  LYS D CD    1 
ATOM   13775 C  CE    . LYS D 2 70  ? 168.625 97.695  119.087 1.00 40.96 ?  49  LYS D CE    1 
ATOM   13776 N  NZ    . LYS D 2 70  ? 170.071 97.365  119.134 1.00 42.55 1  49  LYS D NZ    1 
ATOM   13777 N  N     . ASN D 2 71  ? 165.129 100.345 124.354 1.00 29.92 ?  50  ASN D N     1 
ATOM   13778 C  CA    . ASN D 2 71  ? 164.747 100.486 125.764 1.00 29.37 ?  50  ASN D CA    1 
ATOM   13779 C  C     . ASN D 2 71  ? 163.320 101.003 125.918 1.00 28.35 ?  50  ASN D C     1 
ATOM   13780 O  O     . ASN D 2 71  ? 162.583 100.533 126.794 1.00 27.64 ?  50  ASN D O     1 
ATOM   13781 C  CB    . ASN D 2 71  ? 165.718 101.387 126.552 1.00 29.38 ?  50  ASN D CB    1 
ATOM   13782 C  CG    . ASN D 2 71  ? 167.038 100.694 126.886 1.00 31.22 ?  50  ASN D CG    1 
ATOM   13783 O  OD1   . ASN D 2 71  ? 167.098 99.477  127.068 1.00 33.03 ?  50  ASN D OD1   1 
ATOM   13784 N  ND2   . ASN D 2 71  ? 168.106 101.480 126.979 1.00 31.97 ?  50  ASN D ND2   1 
ATOM   13785 N  N     . GLU D 2 72  ? 162.936 101.953 125.062 1.00 27.72 ?  51  GLU D N     1 
ATOM   13786 C  CA    . GLU D 2 72  ? 161.567 102.492 125.072 1.00 27.70 ?  51  GLU D CA    1 
ATOM   13787 C  C     . GLU D 2 72  ? 160.539 101.423 124.691 1.00 27.62 ?  51  GLU D C     1 
ATOM   13788 O  O     . GLU D 2 72  ? 159.477 101.318 125.312 1.00 27.56 ?  51  GLU D O     1 
ATOM   13789 C  CB    . GLU D 2 72  ? 161.432 103.693 124.130 1.00 27.55 ?  51  GLU D CB    1 
ATOM   13790 C  CG    . GLU D 2 72  ? 162.350 104.878 124.452 1.00 28.77 ?  51  GLU D CG    1 
ATOM   13791 C  CD    . GLU D 2 72  ? 162.066 106.067 123.553 1.00 31.18 ?  51  GLU D CD    1 
ATOM   13792 O  OE1   . GLU D 2 72  ? 162.410 106.005 122.353 1.00 33.17 ?  51  GLU D OE1   1 
ATOM   13793 O  OE2   . GLU D 2 72  ? 161.489 107.058 124.044 1.00 31.66 -1 51  GLU D OE2   1 
ATOM   13794 N  N     . GLN D 2 73  ? 160.864 100.636 123.669 1.00 27.32 ?  52  GLN D N     1 
ATOM   13795 C  CA    . GLN D 2 73  ? 159.980 99.571  123.206 1.00 27.33 ?  52  GLN D CA    1 
ATOM   13796 C  C     . GLN D 2 73  ? 159.873 98.473  124.267 1.00 26.85 ?  52  GLN D C     1 
ATOM   13797 O  O     . GLN D 2 73  ? 158.780 97.963  124.533 1.00 26.24 ?  52  GLN D O     1 
ATOM   13798 C  CB    . GLN D 2 73  ? 160.466 99.004  121.877 1.00 27.65 ?  52  GLN D CB    1 
ATOM   13799 C  CG    . GLN D 2 73  ? 160.241 99.923  120.662 1.00 29.66 ?  52  GLN D CG    1 
ATOM   13800 C  CD    . GLN D 2 73  ? 160.563 99.244  119.330 1.00 32.60 ?  52  GLN D CD    1 
ATOM   13801 O  OE1   . GLN D 2 73  ? 161.290 98.255  119.284 1.00 34.76 ?  52  GLN D OE1   1 
ATOM   13802 N  NE2   . GLN D 2 73  ? 160.034 99.788  118.245 1.00 33.42 ?  52  GLN D NE2   1 
ATOM   13803 N  N     . ASP D 2 74  ? 161.006 98.150  124.886 1.00 26.26 ?  53  ASP D N     1 
ATOM   13804 C  CA    . ASP D 2 74  ? 161.084 97.153  125.960 1.00 26.50 ?  53  ASP D CA    1 
ATOM   13805 C  C     . ASP D 2 74  ? 160.262 97.575  127.169 1.00 25.81 ?  53  ASP D C     1 
ATOM   13806 O  O     . ASP D 2 74  ? 159.482 96.785  127.695 1.00 26.12 ?  53  ASP D O     1 
ATOM   13807 C  CB    . ASP D 2 74  ? 162.549 96.948  126.373 1.00 26.84 ?  53  ASP D CB    1 
ATOM   13808 C  CG    . ASP D 2 74  ? 162.740 95.817  127.383 1.00 29.50 ?  53  ASP D CG    1 
ATOM   13809 O  OD1   . ASP D 2 74  ? 162.463 94.644  127.053 1.00 32.08 ?  53  ASP D OD1   1 
ATOM   13810 O  OD2   . ASP D 2 74  ? 163.218 96.099  128.501 1.00 33.52 -1 53  ASP D OD2   1 
ATOM   13811 N  N     . THR D 2 75  ? 160.432 98.820  127.612 1.00 25.10 ?  54  THR D N     1 
ATOM   13812 C  CA    . THR D 2 75  ? 159.678 99.320  128.765 1.00 24.11 ?  54  THR D CA    1 
ATOM   13813 C  C     . THR D 2 75  ? 158.175 99.299  128.472 1.00 23.82 ?  54  THR D C     1 
ATOM   13814 O  O     . THR D 2 75  ? 157.388 98.812  129.284 1.00 23.81 ?  54  THR D O     1 
ATOM   13815 C  CB    . THR D 2 75  ? 160.145 100.726 129.191 1.00 23.80 ?  54  THR D CB    1 
ATOM   13816 O  OG1   . THR D 2 75  ? 161.514 100.655 129.611 1.00 24.62 ?  54  THR D OG1   1 
ATOM   13817 C  CG2   . THR D 2 75  ? 159.289 101.262 130.352 1.00 23.25 ?  54  THR D CG2   1 
ATOM   13818 N  N     . TYR D 2 76  ? 157.790 99.836  127.323 1.00 24.06 ?  55  TYR D N     1 
ATOM   13819 C  CA    . TYR D 2 76  ? 156.392 99.837  126.903 1.00 24.76 ?  55  TYR D CA    1 
ATOM   13820 C  C     . TYR D 2 76  ? 155.767 98.434  126.915 1.00 24.85 ?  55  TYR D C     1 
ATOM   13821 O  O     . TYR D 2 76  ? 154.684 98.243  127.474 1.00 24.83 ?  55  TYR D O     1 
ATOM   13822 C  CB    . TYR D 2 76  ? 156.238 100.465 125.518 1.00 24.78 ?  55  TYR D CB    1 
ATOM   13823 C  CG    . TYR D 2 76  ? 154.829 100.945 125.238 1.00 26.19 ?  55  TYR D CG    1 
ATOM   13824 C  CD1   . TYR D 2 76  ? 154.452 102.252 125.552 1.00 27.81 ?  55  TYR D CD1   1 
ATOM   13825 C  CD2   . TYR D 2 76  ? 153.868 100.097 124.678 1.00 28.03 ?  55  TYR D CD2   1 
ATOM   13826 C  CE1   . TYR D 2 76  ? 153.166 102.712 125.304 1.00 29.32 ?  55  TYR D CE1   1 
ATOM   13827 C  CE2   . TYR D 2 76  ? 152.564 100.549 124.427 1.00 29.01 ?  55  TYR D CE2   1 
ATOM   13828 C  CZ    . TYR D 2 76  ? 152.228 101.860 124.746 1.00 30.76 ?  55  TYR D CZ    1 
ATOM   13829 O  OH    . TYR D 2 76  ? 150.963 102.344 124.508 1.00 34.50 ?  55  TYR D OH    1 
ATOM   13830 N  N     . MET D 2 77  ? 156.448 97.469  126.299 1.00 25.76 ?  56  MET D N     1 
ATOM   13831 C  CA    . MET D 2 77  ? 155.980 96.079  126.281 1.00 26.81 ?  56  MET D CA    1 
ATOM   13832 C  C     . MET D 2 77  ? 155.780 95.527  127.696 1.00 26.23 ?  56  MET D C     1 
ATOM   13833 O  O     . MET D 2 77  ? 154.753 94.913  127.993 1.00 25.00 ?  56  MET D O     1 
ATOM   13834 C  CB    . MET D 2 77  ? 156.952 95.188  125.511 1.00 28.11 ?  56  MET D CB    1 
ATOM   13835 C  CG    . MET D 2 77  ? 156.999 95.428  123.997 1.00 32.52 ?  56  MET D CG    1 
ATOM   13836 S  SD    . MET D 2 77  ? 155.548 94.833  123.113 1.00 42.68 ?  56  MET D SD    1 
ATOM   13837 C  CE    . MET D 2 77  ? 154.417 96.218  123.245 1.00 38.97 ?  56  MET D CE    1 
ATOM   13838 N  N     . LYS D 2 78  ? 156.776 95.748  128.555 1.00 26.01 ?  57  LYS D N     1 
ATOM   13839 C  CA    . LYS D 2 78  ? 156.746 95.237  129.928 1.00 26.07 ?  57  LYS D CA    1 
ATOM   13840 C  C     . LYS D 2 78  ? 155.637 95.878  130.761 1.00 25.69 ?  57  LYS D C     1 
ATOM   13841 O  O     . LYS D 2 78  ? 154.969 95.199  131.551 1.00 25.58 ?  57  LYS D O     1 
ATOM   13842 C  CB    . LYS D 2 78  ? 158.106 95.419  130.614 1.00 26.08 ?  57  LYS D CB    1 
ATOM   13843 C  CG    . LYS D 2 78  ? 159.210 94.513  130.049 1.00 27.64 ?  57  LYS D CG    1 
ATOM   13844 C  CD    . LYS D 2 78  ? 160.572 94.854  130.641 1.00 29.47 ?  57  LYS D CD    1 
ATOM   13845 C  CE    . LYS D 2 78  ? 161.607 93.817  130.234 1.00 31.69 ?  57  LYS D CE    1 
ATOM   13846 N  NZ    . LYS D 2 78  ? 162.947 94.104  130.813 1.00 33.36 1  57  LYS D NZ    1 
ATOM   13847 N  N     . VAL D 2 79  ? 155.451 97.184  130.583 1.00 25.32 ?  58  VAL D N     1 
ATOM   13848 C  CA    . VAL D 2 79  ? 154.400 97.931  131.284 1.00 25.47 ?  58  VAL D CA    1 
ATOM   13849 C  C     . VAL D 2 79  ? 153.036 97.415  130.836 1.00 25.09 ?  58  VAL D C     1 
ATOM   13850 O  O     . VAL D 2 79  ? 152.161 97.128  131.658 1.00 24.46 ?  58  VAL D O     1 
ATOM   13851 C  CB    . VAL D 2 79  ? 154.539 99.453  130.999 1.00 25.83 ?  58  VAL D CB    1 
ATOM   13852 C  CG1   . VAL D 2 79  ? 153.210 100.165 131.113 1.00 27.35 ?  58  VAL D CG1   1 
ATOM   13853 C  CG2   . VAL D 2 79  ? 155.596 100.064 131.919 1.00 26.42 ?  58  VAL D CG2   1 
ATOM   13854 N  N     . LEU D 2 80  ? 152.890 97.255  129.523 1.00 25.27 ?  59  LEU D N     1 
ATOM   13855 C  CA    . LEU D 2 80  ? 151.644 96.814  128.936 1.00 25.55 ?  59  LEU D CA    1 
ATOM   13856 C  C     . LEU D 2 80  ? 151.266 95.432  129.466 1.00 24.94 ?  59  LEU D C     1 
ATOM   13857 O  O     . LEU D 2 80  ? 150.112 95.201  129.819 1.00 24.82 ?  59  LEU D O     1 
ATOM   13858 C  CB    . LEU D 2 80  ? 151.763 96.786  127.411 1.00 25.80 ?  59  LEU D CB    1 
ATOM   13859 C  CG    . LEU D 2 80  ? 150.815 97.583  126.508 1.00 28.76 ?  59  LEU D CG    1 
ATOM   13860 C  CD1   . LEU D 2 80  ? 150.644 96.814  125.198 1.00 30.25 ?  59  LEU D CD1   1 
ATOM   13861 C  CD2   . LEU D 2 80  ? 149.459 97.885  127.124 1.00 27.79 ?  59  LEU D CD2   1 
ATOM   13862 N  N     . ALA D 2 81  ? 152.244 94.527  129.522 1.00 24.86 ?  60  ALA D N     1 
ATOM   13863 C  CA    . ALA D 2 81  ? 152.018 93.162  130.019 1.00 24.60 ?  60  ALA D CA    1 
ATOM   13864 C  C     . ALA D 2 81  ? 151.650 93.183  131.500 1.00 23.80 ?  60  ALA D C     1 
ATOM   13865 O  O     . ALA D 2 81  ? 150.802 92.420  131.947 1.00 24.07 ?  60  ALA D O     1 
ATOM   13866 C  CB    . ALA D 2 81  ? 153.253 92.293  129.787 1.00 24.48 ?  60  ALA D CB    1 
ATOM   13867 N  N     . GLY D 2 82  ? 152.291 94.069  132.253 1.00 23.54 ?  61  GLY D N     1 
ATOM   13868 C  CA    . GLY D 2 82  ? 151.967 94.266  133.662 1.00 22.53 ?  61  GLY D CA    1 
ATOM   13869 C  C     . GLY D 2 82  ? 150.515 94.654  133.850 1.00 22.23 ?  61  GLY D C     1 
ATOM   13870 O  O     . GLY D 2 82  ? 149.806 94.057  134.659 1.00 21.27 ?  61  GLY D O     1 
ATOM   13871 N  N     . LEU D 2 83  ? 150.067 95.657  133.095 1.00 22.36 ?  62  LEU D N     1 
ATOM   13872 C  CA    . LEU D 2 83  ? 148.670 96.099  133.160 1.00 22.42 ?  62  LEU D CA    1 
ATOM   13873 C  C     . LEU D 2 83  ? 147.716 94.982  132.759 1.00 22.91 ?  62  LEU D C     1 
ATOM   13874 O  O     . LEU D 2 83  ? 146.689 94.767  133.416 1.00 22.99 ?  62  LEU D O     1 
ATOM   13875 C  CB    . LEU D 2 83  ? 148.432 97.325  132.269 1.00 22.19 ?  62  LEU D CB    1 
ATOM   13876 C  CG    . LEU D 2 83  ? 149.155 98.621  132.667 1.00 22.17 ?  62  LEU D CG    1 
ATOM   13877 C  CD1   . LEU D 2 83  ? 149.100 99.625  131.508 1.00 21.55 ?  62  LEU D CD1   1 
ATOM   13878 C  CD2   . LEU D 2 83  ? 148.523 99.200  133.920 1.00 22.42 ?  62  LEU D CD2   1 
ATOM   13879 N  N     . THR D 2 84  ? 148.070 94.263  131.699 1.00 23.39 ?  63  THR D N     1 
ATOM   13880 C  CA    . THR D 2 84  ? 147.227 93.185  131.189 1.00 24.42 ?  63  THR D CA    1 
ATOM   13881 C  C     . THR D 2 84  ? 147.020 92.101  132.250 1.00 24.55 ?  63  THR D C     1 
ATOM   13882 O  O     . THR D 2 84  ? 145.889 91.695  132.525 1.00 23.68 ?  63  THR D O     1 
ATOM   13883 C  CB    . THR D 2 84  ? 147.817 92.550  129.903 1.00 24.70 ?  63  THR D CB    1 
ATOM   13884 O  OG1   . THR D 2 84  ? 147.948 93.557  128.891 1.00 25.57 ?  63  THR D OG1   1 
ATOM   13885 C  CG2   . THR D 2 84  ? 146.897 91.459  129.382 1.00 25.36 ?  63  THR D CG2   1 
ATOM   13886 N  N     . LEU D 2 85  ? 148.128 91.654  132.833 1.00 25.38 ?  64  LEU D N     1 
ATOM   13887 C  CA    . LEU D 2 85  ? 148.103 90.607  133.846 1.00 26.44 ?  64  LEU D CA    1 
ATOM   13888 C  C     . LEU D 2 85  ? 147.296 91.015  135.082 1.00 25.96 ?  64  LEU D C     1 
ATOM   13889 O  O     . LEU D 2 85  ? 146.446 90.239  135.541 1.00 25.83 ?  64  LEU D O     1 
ATOM   13890 C  CB    . LEU D 2 85  ? 149.525 90.134  134.186 1.00 26.65 ?  64  LEU D CB    1 
ATOM   13891 C  CG    . LEU D 2 85  ? 150.119 89.219  133.097 1.00 29.62 ?  64  LEU D CG    1 
ATOM   13892 C  CD1   . LEU D 2 85  ? 151.636 89.210  133.125 1.00 31.57 ?  64  LEU D CD1   1 
ATOM   13893 C  CD2   . LEU D 2 85  ? 149.582 87.779  133.197 1.00 30.96 ?  64  LEU D CD2   1 
ATOM   13894 N  N     . LEU D 2 86  ? 147.513 92.231  135.588 1.00 25.63 ?  65  LEU D N     1 
ATOM   13895 C  CA    . LEU D 2 86  ? 146.730 92.709  136.730 1.00 25.59 ?  65  LEU D CA    1 
ATOM   13896 C  C     . LEU D 2 86  ? 145.241 92.859  136.424 1.00 25.60 ?  65  LEU D C     1 
ATOM   13897 O  O     . LEU D 2 86  ? 144.392 92.568  137.271 1.00 25.47 ?  65  LEU D O     1 
ATOM   13898 C  CB    . LEU D 2 86  ? 147.295 94.017  137.315 1.00 25.76 ?  65  LEU D CB    1 
ATOM   13899 C  CG    . LEU D 2 86  ? 148.649 93.910  138.029 1.00 26.71 ?  65  LEU D CG    1 
ATOM   13900 C  CD1   . LEU D 2 86  ? 149.264 95.284  138.277 1.00 28.01 ?  65  LEU D CD1   1 
ATOM   13901 C  CD2   . LEU D 2 86  ? 148.528 93.155  139.332 1.00 28.01 ?  65  LEU D CD2   1 
ATOM   13902 N  N     . ASP D 2 87  ? 144.918 93.322  135.222 1.00 25.49 ?  66  ASP D N     1 
ATOM   13903 C  CA    . ASP D 2 87  ? 143.529 93.558  134.867 1.00 25.83 ?  66  ASP D CA    1 
ATOM   13904 C  C     . ASP D 2 87  ? 142.743 92.251  134.698 1.00 26.20 ?  66  ASP D C     1 
ATOM   13905 O  O     . ASP D 2 87  ? 141.548 92.202  134.968 1.00 25.99 ?  66  ASP D O     1 
ATOM   13906 C  CB    . ASP D 2 87  ? 143.433 94.421  133.615 1.00 25.50 ?  66  ASP D CB    1 
ATOM   13907 C  CG    . ASP D 2 87  ? 142.214 95.298  133.624 1.00 25.76 ?  66  ASP D CG    1 
ATOM   13908 O  OD1   . ASP D 2 87  ? 141.746 95.649  134.734 1.00 26.91 ?  66  ASP D OD1   1 
ATOM   13909 O  OD2   . ASP D 2 87  ? 141.717 95.643  132.534 1.00 23.11 -1 66  ASP D OD2   1 
ATOM   13910 N  N     . THR D 2 88  ? 143.435 91.196  134.273 1.00 27.12 ?  67  THR D N     1 
ATOM   13911 C  CA    . THR D 2 88  ? 142.853 89.865  134.166 1.00 28.40 ?  67  THR D CA    1 
ATOM   13912 C  C     . THR D 2 88  ? 142.438 89.331  135.527 1.00 28.28 ?  67  THR D C     1 
ATOM   13913 O  O     . THR D 2 88  ? 141.366 88.743  135.660 1.00 28.10 ?  67  THR D O     1 
ATOM   13914 C  CB    . THR D 2 88  ? 143.822 88.878  133.486 1.00 29.04 ?  67  THR D CB    1 
ATOM   13915 O  OG1   . THR D 2 88  ? 144.137 89.364  132.180 1.00 31.00 ?  67  THR D OG1   1 
ATOM   13916 C  CG2   . THR D 2 88  ? 143.180 87.499  133.351 1.00 30.16 ?  67  THR D CG2   1 
ATOM   13917 N  N     . GLU D 2 89  ? 143.278 89.536  136.539 1.00 28.28 ?  68  GLU D N     1 
ATOM   13918 C  CA    . GLU D 2 89  ? 142.911 89.149  137.897 1.00 29.16 ?  68  GLU D CA    1 
ATOM   13919 C  C     . GLU D 2 89  ? 141.644 89.887  138.325 1.00 28.65 ?  68  GLU D C     1 
ATOM   13920 O  O     . GLU D 2 89  ? 140.762 89.298  138.934 1.00 28.44 ?  68  GLU D O     1 
ATOM   13921 C  CB    . GLU D 2 89  ? 144.045 89.426  138.895 1.00 29.32 ?  68  GLU D CB    1 
ATOM   13922 C  CG    . GLU D 2 89  ? 145.353 88.675  138.602 1.00 31.95 ?  68  GLU D CG    1 
ATOM   13923 C  CD    . GLU D 2 89  ? 145.233 87.158  138.706 1.00 35.19 ?  68  GLU D CD    1 
ATOM   13924 O  OE1   . GLU D 2 89  ? 144.253 86.645  139.293 1.00 35.47 ?  68  GLU D OE1   1 
ATOM   13925 O  OE2   . GLU D 2 89  ? 146.136 86.470  138.186 1.00 38.06 -1 68  GLU D OE2   1 
ATOM   13926 N  N     . GLN D 2 90  ? 141.555 91.170  137.987 1.00 28.45 ?  69  GLN D N     1 
ATOM   13927 C  CA    . GLN D 2 90  ? 140.392 91.972  138.370 1.00 28.47 ?  69  GLN D CA    1 
ATOM   13928 C  C     . GLN D 2 90  ? 139.110 91.491  137.676 1.00 28.97 ?  69  GLN D C     1 
ATOM   13929 O  O     . GLN D 2 90  ? 138.045 91.462  138.291 1.00 28.84 ?  69  GLN D O     1 
ATOM   13930 C  CB    . GLN D 2 90  ? 140.650 93.460  138.114 1.00 28.21 ?  69  GLN D CB    1 
ATOM   13931 C  CG    . GLN D 2 90  ? 139.700 94.405  138.849 1.00 27.75 ?  69  GLN D CG    1 
ATOM   13932 C  CD    . GLN D 2 90  ? 139.935 94.476  140.354 1.00 28.91 ?  69  GLN D CD    1 
ATOM   13933 O  OE1   . GLN D 2 90  ? 140.519 93.568  140.962 1.00 27.62 ?  69  GLN D OE1   1 
ATOM   13934 N  NE2   . GLN D 2 90  ? 139.455 95.558  140.969 1.00 28.23 ?  69  GLN D NE2   1 
ATOM   13935 N  N     . GLY D 2 91  ? 139.224 91.092  136.409 1.00 29.62 ?  70  GLY D N     1 
ATOM   13936 C  CA    . GLY D 2 91  ? 138.087 90.560  135.656 1.00 30.43 ?  70  GLY D CA    1 
ATOM   13937 C  C     . GLY D 2 91  ? 137.642 89.161  136.067 1.00 31.11 ?  70  GLY D C     1 
ATOM   13938 O  O     . GLY D 2 91  ? 136.443 88.871  136.137 1.00 30.77 ?  70  GLY D O     1 
ATOM   13939 N  N     . ASN D 2 92  ? 138.601 88.286  136.330 1.00 31.69 ?  71  ASN D N     1 
ATOM   13940 C  CA    . ASN D 2 92  ? 138.268 86.915  136.697 1.00 32.72 ?  71  ASN D CA    1 
ATOM   13941 C  C     . ASN D 2 92  ? 137.911 86.706  138.162 1.00 32.60 ?  71  ASN D C     1 
ATOM   13942 O  O     . ASN D 2 92  ? 137.125 85.808  138.477 1.00 33.12 ?  71  ASN D O     1 
ATOM   13943 C  CB    . ASN D 2 92  ? 139.383 85.964  136.283 1.00 33.68 ?  71  ASN D CB    1 
ATOM   13944 C  CG    . ASN D 2 92  ? 139.444 85.769  134.782 1.00 35.15 ?  71  ASN D CG    1 
ATOM   13945 O  OD1   . ASN D 2 92  ? 140.500 85.468  134.240 1.00 40.21 ?  71  ASN D OD1   1 
ATOM   13946 N  ND2   . ASN D 2 92  ? 138.310 85.950  134.102 1.00 36.91 ?  71  ASN D ND2   1 
ATOM   13947 N  N     . THR D 2 93  ? 138.466 87.541  139.041 1.00 31.76 ?  72  THR D N     1 
ATOM   13948 C  CA    . THR D 2 93  ? 138.302 87.359  140.478 1.00 31.47 ?  72  THR D CA    1 
ATOM   13949 C  C     . THR D 2 93  ? 137.813 88.607  141.209 1.00 30.62 ?  72  THR D C     1 
ATOM   13950 O  O     . THR D 2 93  ? 136.766 88.572  141.850 1.00 30.71 ?  72  THR D O     1 
ATOM   13951 C  CB    . THR D 2 93  ? 139.602 86.872  141.113 1.00 31.60 ?  72  THR D CB    1 
ATOM   13952 O  OG1   . THR D 2 93  ? 140.023 85.673  140.449 1.00 33.14 ?  72  THR D OG1   1 
ATOM   13953 C  CG2   . THR D 2 93  ? 139.406 86.590  142.594 1.00 31.89 ?  72  THR D CG2   1 
ATOM   13954 N  N     . GLY D 2 94  ? 138.567 89.699  141.103 1.00 29.61 ?  73  GLY D N     1 
ATOM   13955 C  CA    . GLY D 2 94  ? 138.300 90.915  141.873 1.00 28.47 ?  73  GLY D CA    1 
ATOM   13956 C  C     . GLY D 2 94  ? 136.884 91.448  141.800 1.00 27.90 ?  73  GLY D C     1 
ATOM   13957 O  O     . GLY D 2 94  ? 136.224 91.643  142.830 1.00 28.27 ?  73  GLY D O     1 
ATOM   13958 N  N     . MET D 2 95  ? 136.406 91.717  140.593 1.00 26.67 ?  74  MET D N     1 
ATOM   13959 C  CA    . MET D 2 95  ? 135.051 92.249  140.476 1.00 26.00 ?  74  MET D CA    1 
ATOM   13960 C  C     . MET D 2 95  ? 133.995 91.181  140.733 1.00 25.25 ?  74  MET D C     1 
ATOM   13961 O  O     . MET D 2 95  ? 133.027 91.457  141.430 1.00 24.97 ?  74  MET D O     1 
ATOM   13962 C  CB    . MET D 2 95  ? 134.806 92.960  139.139 1.00 26.00 ?  74  MET D CB    1 
ATOM   13963 C  CG    . MET D 2 95  ? 135.363 94.362  139.081 1.00 26.40 ?  74  MET D CG    1 
ATOM   13964 S  SD    . MET D 2 95  ? 134.648 95.491  140.303 1.00 28.10 ?  74  MET D SD    1 
ATOM   13965 C  CE    . MET D 2 95  ? 135.693 96.915  140.021 1.00 28.95 ?  74  MET D CE    1 
ATOM   13966 N  N     . PRO D 2 96  ? 134.166 89.970  140.171 1.00 24.98 ?  75  PRO D N     1 
ATOM   13967 C  CA    . PRO D 2 96  ? 133.098 88.989  140.436 1.00 24.59 ?  75  PRO D CA    1 
ATOM   13968 C  C     . PRO D 2 96  ? 132.983 88.568  141.899 1.00 23.90 ?  75  PRO D C     1 
ATOM   13969 O  O     . PRO D 2 96  ? 131.880 88.273  142.345 1.00 23.45 ?  75  PRO D O     1 
ATOM   13970 C  CB    . PRO D 2 96  ? 133.492 87.782  139.574 1.00 24.80 ?  75  PRO D CB    1 
ATOM   13971 C  CG    . PRO D 2 96  ? 134.334 88.370  138.464 1.00 25.75 ?  75  PRO D CG    1 
ATOM   13972 C  CD    . PRO D 2 96  ? 135.083 89.510  139.104 1.00 25.07 ?  75  PRO D CD    1 
ATOM   13973 N  N     . ILE D 2 97  ? 134.098 88.528  142.633 1.00 23.36 ?  76  ILE D N     1 
ATOM   13974 C  CA    . ILE D 2 97  ? 134.046 88.103  144.028 1.00 23.48 ?  76  ILE D CA    1 
ATOM   13975 C  C     . ILE D 2 97  ? 133.359 89.154  144.885 1.00 23.30 ?  76  ILE D C     1 
ATOM   13976 O  O     . ILE D 2 97  ? 132.614 88.814  145.800 1.00 23.45 ?  76  ILE D O     1 
ATOM   13977 C  CB    . ILE D 2 97  ? 135.440 87.715  144.597 1.00 23.96 ?  76  ILE D CB    1 
ATOM   13978 C  CG1   . ILE D 2 97  ? 135.296 86.727  145.750 1.00 24.71 ?  76  ILE D CG1   1 
ATOM   13979 C  CG2   . ILE D 2 97  ? 136.267 88.953  145.021 1.00 24.02 ?  76  ILE D CG2   1 
ATOM   13980 C  CD1   . ILE D 2 97  ? 136.467 85.717  145.815 1.00 29.17 ?  76  ILE D CD1   1 
ATOM   13981 N  N     . VAL D 2 98  ? 133.600 90.429  144.578 1.00 22.71 ?  77  VAL D N     1 
ATOM   13982 C  CA    . VAL D 2 98  ? 132.943 91.526  145.306 1.00 22.78 ?  77  VAL D CA    1 
ATOM   13983 C  C     . VAL D 2 98  ? 131.447 91.554  144.989 1.00 22.89 ?  77  VAL D C     1 
ATOM   13984 O  O     . VAL D 2 98  ? 130.618 91.710  145.886 1.00 23.72 ?  77  VAL D O     1 
ATOM   13985 C  CB    . VAL D 2 98  ? 133.635 92.891  145.032 1.00 22.49 ?  77  VAL D CB    1 
ATOM   13986 C  CG1   . VAL D 2 98  ? 132.819 94.067  145.602 1.00 21.91 ?  77  VAL D CG1   1 
ATOM   13987 C  CG2   . VAL D 2 98  ? 135.028 92.888  145.640 1.00 23.02 ?  77  VAL D CG2   1 
ATOM   13988 N  N     . ALA D 2 99  ? 131.099 91.365  143.716 1.00 23.19 ?  78  ALA D N     1 
ATOM   13989 C  CA    . ALA D 2 99  ? 129.688 91.295  143.312 1.00 23.05 ?  78  ALA D CA    1 
ATOM   13990 C  C     . ALA D 2 99  ? 128.962 90.163  144.046 1.00 23.52 ?  78  ALA D C     1 
ATOM   13991 O  O     . ALA D 2 99  ? 127.798 90.297  144.438 1.00 23.68 ?  78  ALA D O     1 
ATOM   13992 C  CB    . ALA D 2 99  ? 129.576 91.126  141.806 1.00 22.81 ?  78  ALA D CB    1 
ATOM   13993 N  N     . GLU D 2 100 ? 129.655 89.045  144.240 1.00 23.68 ?  79  GLU D N     1 
ATOM   13994 C  CA    . GLU D 2 100 ? 129.083 87.905  144.951 1.00 24.14 ?  79  GLU D CA    1 
ATOM   13995 C  C     . GLU D 2 100 ? 128.731 88.193  146.420 1.00 23.66 ?  79  GLU D C     1 
ATOM   13996 O  O     . GLU D 2 100 ? 127.673 87.780  146.905 1.00 22.94 ?  79  GLU D O     1 
ATOM   13997 C  CB    . GLU D 2 100 ? 130.036 86.714  144.860 1.00 24.47 ?  79  GLU D CB    1 
ATOM   13998 C  CG    . GLU D 2 100 ? 129.444 85.410  145.358 1.00 27.90 ?  79  GLU D CG    1 
ATOM   13999 C  CD    . GLU D 2 100 ? 130.467 84.290  145.421 1.00 32.30 ?  79  GLU D CD    1 
ATOM   14000 O  OE1   . GLU D 2 100 ? 131.460 84.332  144.660 1.00 32.88 ?  79  GLU D OE1   1 
ATOM   14001 O  OE2   . GLU D 2 100 ? 130.274 83.370  146.242 1.00 34.74 -1 79  GLU D OE2   1 
ATOM   14002 N  N     . HIS D 2 101 ? 129.617 88.891  147.129 1.00 23.62 ?  80  HIS D N     1 
ATOM   14003 C  CA    . HIS D 2 101 ? 129.429 89.130  148.572 1.00 23.99 ?  80  HIS D CA    1 
ATOM   14004 C  C     . HIS D 2 101 ? 128.667 90.405  148.957 1.00 24.35 ?  80  HIS D C     1 
ATOM   14005 O  O     . HIS D 2 101 ? 128.186 90.516  150.086 1.00 24.21 ?  80  HIS D O     1 
ATOM   14006 C  CB    . HIS D 2 101 ? 130.775 89.053  149.306 1.00 24.13 ?  80  HIS D CB    1 
ATOM   14007 C  CG    . HIS D 2 101 ? 131.391 87.685  149.276 1.00 24.76 ?  80  HIS D CG    1 
ATOM   14008 N  ND1   . HIS D 2 101 ? 131.203 86.762  150.284 1.00 25.68 ?  80  HIS D ND1   1 
ATOM   14009 C  CD2   . HIS D 2 101 ? 132.168 87.077  148.349 1.00 25.75 ?  80  HIS D CD2   1 
ATOM   14010 C  CE1   . HIS D 2 101 ? 131.844 85.646  149.980 1.00 26.21 ?  80  HIS D CE1   1 
ATOM   14011 N  NE2   . HIS D 2 101 ? 132.438 85.811  148.812 1.00 25.35 ?  80  HIS D NE2   1 
ATOM   14012 N  N     . VAL D 2 102 ? 128.567 91.366  148.041 1.00 24.50 ?  81  VAL D N     1 
ATOM   14013 C  CA    . VAL D 2 102 ? 127.812 92.593  148.295 1.00 25.50 ?  81  VAL D CA    1 
ATOM   14014 C  C     . VAL D 2 102 ? 126.303 92.317  148.199 1.00 26.14 ?  81  VAL D C     1 
ATOM   14015 O  O     . VAL D 2 102 ? 125.858 91.658  147.263 1.00 26.96 ?  81  VAL D O     1 
ATOM   14016 C  CB    . VAL D 2 102 ? 128.222 93.723  147.305 1.00 25.30 ?  81  VAL D CB    1 
ATOM   14017 C  CG1   . VAL D 2 102 ? 127.265 94.888  147.380 1.00 27.08 ?  81  VAL D CG1   1 
ATOM   14018 C  CG2   . VAL D 2 102 ? 129.631 94.205  147.610 1.00 25.41 ?  81  VAL D CG2   1 
ATOM   14019 N  N     . ASP D 2 103 ? 125.537 92.806  149.170 1.00 26.45 ?  82  ASP D N     1 
ATOM   14020 C  CA    . ASP D 2 103 ? 124.077 92.705  149.134 1.00 27.15 ?  82  ASP D CA    1 
ATOM   14021 C  C     . ASP D 2 103 ? 123.473 93.914  148.436 1.00 26.39 ?  82  ASP D C     1 
ATOM   14022 O  O     . ASP D 2 103 ? 123.942 95.047  148.607 1.00 26.40 ?  82  ASP D O     1 
ATOM   14023 C  CB    . ASP D 2 103 ? 123.491 92.590  150.546 1.00 27.72 ?  82  ASP D CB    1 
ATOM   14024 C  CG    . ASP D 2 103 ? 123.944 91.334  151.282 1.00 31.46 ?  82  ASP D CG    1 
ATOM   14025 O  OD1   . ASP D 2 103 ? 124.177 90.275  150.638 1.00 34.26 ?  82  ASP D OD1   1 
ATOM   14026 O  OD2   . ASP D 2 103 ? 124.060 91.403  152.527 1.00 35.52 -1 82  ASP D OD2   1 
ATOM   14027 N  N     . GLY D 2 104 ? 122.417 93.670  147.664 1.00 25.52 ?  83  GLY D N     1 
ATOM   14028 C  CA    . GLY D 2 104 ? 121.707 94.739  146.965 1.00 24.31 ?  83  GLY D CA    1 
ATOM   14029 C  C     . GLY D 2 104 ? 121.681 94.436  145.471 1.00 23.27 ?  83  GLY D C     1 
ATOM   14030 O  O     . GLY D 2 104 ? 122.726 94.241  144.852 1.00 22.38 ?  83  GLY D O     1 
ATOM   14031 N  N     . HIS D 2 105 ? 120.483 94.379  144.896 1.00 22.46 ?  84  HIS D N     1 
ATOM   14032 C  CA    . HIS D 2 105 ? 120.342 94.083  143.469 1.00 22.17 ?  84  HIS D CA    1 
ATOM   14033 C  C     . HIS D 2 105 ? 121.000 95.116  142.570 1.00 21.13 ?  84  HIS D C     1 
ATOM   14034 O  O     . HIS D 2 105 ? 121.605 94.760  141.561 1.00 20.91 ?  84  HIS D O     1 
ATOM   14035 C  CB    . HIS D 2 105 ? 118.862 93.920  143.093 1.00 22.07 ?  84  HIS D CB    1 
ATOM   14036 C  CG    . HIS D 2 105 ? 118.184 92.824  143.851 1.00 23.85 ?  84  HIS D CG    1 
ATOM   14037 N  ND1   . HIS D 2 105 ? 118.699 91.547  143.917 1.00 24.86 ?  84  HIS D ND1   1 
ATOM   14038 C  CD2   . HIS D 2 105 ? 117.059 92.818  144.602 1.00 25.19 ?  84  HIS D CD2   1 
ATOM   14039 C  CE1   . HIS D 2 105 ? 117.907 90.795  144.661 1.00 24.94 ?  84  HIS D CE1   1 
ATOM   14040 N  NE2   . HIS D 2 105 ? 116.909 91.545  145.092 1.00 26.41 ?  84  HIS D NE2   1 
ATOM   14041 N  N     . GLN D 2 106 ? 120.883 96.386  142.930 1.00 20.66 ?  85  GLN D N     1 
ATOM   14042 C  CA    . GLN D 2 106 ? 121.379 97.448  142.060 1.00 20.70 ?  85  GLN D CA    1 
ATOM   14043 C  C     . GLN D 2 106 ? 122.906 97.492  142.101 1.00 20.46 ?  85  GLN D C     1 
ATOM   14044 O  O     . GLN D 2 106 ? 123.548 97.695  141.071 1.00 20.72 ?  85  GLN D O     1 
ATOM   14045 C  CB    . GLN D 2 106 ? 120.713 98.796  142.382 1.00 20.60 ?  85  GLN D CB    1 
ATOM   14046 C  CG    . GLN D 2 106 ? 119.175 98.771  142.173 1.00 20.74 ?  85  GLN D CG    1 
ATOM   14047 C  CD    . GLN D 2 106 ? 118.449 100.027 142.672 1.00 22.11 ?  85  GLN D CD    1 
ATOM   14048 O  OE1   . GLN D 2 106 ? 119.010 101.117 142.696 1.00 22.88 ?  85  GLN D OE1   1 
ATOM   14049 N  NE2   . GLN D 2 106 ? 117.185 99.869  143.058 1.00 21.64 ?  85  GLN D NE2   1 
ATOM   14050 N  N     . ARG D 2 107 ? 123.478 97.246  143.282 1.00 20.17 ?  86  ARG D N     1 
ATOM   14051 C  CA    . ARG D 2 107 ? 124.933 97.176  143.435 1.00 20.29 ?  86  ARG D CA    1 
ATOM   14052 C  C     . ARG D 2 107 ? 125.500 95.998  142.659 1.00 20.07 ?  86  ARG D C     1 
ATOM   14053 O  O     . ARG D 2 107 ? 126.528 96.126  142.008 1.00 19.53 ?  86  ARG D O     1 
ATOM   14054 C  CB    . ARG D 2 107 ? 125.324 97.038  144.904 1.00 20.88 ?  86  ARG D CB    1 
ATOM   14055 C  CG    . ARG D 2 107 ? 124.831 98.167  145.748 1.00 22.56 ?  86  ARG D CG    1 
ATOM   14056 C  CD    . ARG D 2 107 ? 124.947 97.830  147.213 1.00 27.21 ?  86  ARG D CD    1 
ATOM   14057 N  NE    . ARG D 2 107 ? 124.955 99.091  147.930 1.00 31.70 ?  86  ARG D NE    1 
ATOM   14058 C  CZ    . ARG D 2 107 ? 125.419 99.269  149.150 1.00 32.23 ?  86  ARG D CZ    1 
ATOM   14059 N  NH1   . ARG D 2 107 ? 125.923 98.248  149.841 1.00 34.27 1  86  ARG D NH1   1 
ATOM   14060 N  NH2   . ARG D 2 107 ? 125.375 100.484 149.663 1.00 33.79 ?  86  ARG D NH2   1 
ATOM   14061 N  N     . LYS D 2 108 ? 124.833 94.846  142.745 1.00 19.61 ?  87  LYS D N     1 
ATOM   14062 C  CA    . LYS D 2 108 ? 125.269 93.675  141.986 1.00 19.92 ?  87  LYS D CA    1 
ATOM   14063 C  C     . LYS D 2 108 ? 125.260 93.944  140.477 1.00 20.08 ?  87  LYS D C     1 
ATOM   14064 O  O     . LYS D 2 108 ? 126.118 93.436  139.747 1.00 20.38 ?  87  LYS D O     1 
ATOM   14065 C  CB    . LYS D 2 108 ? 124.438 92.435  142.321 1.00 19.54 ?  87  LYS D CB    1 
ATOM   14066 C  CG    . LYS D 2 108 ? 124.623 91.925  143.738 1.00 20.55 ?  87  LYS D CG    1 
ATOM   14067 C  CD    . LYS D 2 108 ? 123.785 90.669  143.993 1.00 21.09 ?  87  LYS D CD    1 
ATOM   14068 C  CE    . LYS D 2 108 ? 123.990 90.118  145.399 1.00 22.98 ?  87  LYS D CE    1 
ATOM   14069 N  NZ    . LYS D 2 108 ? 125.354 89.479  145.538 1.00 22.30 1  87  LYS D NZ    1 
ATOM   14070 N  N     . ALA D 2 109 ? 124.290 94.730  140.013 1.00 19.72 ?  88  ALA D N     1 
ATOM   14071 C  CA    . ALA D 2 109 ? 124.195 95.051  138.594 1.00 19.83 ?  88  ALA D CA    1 
ATOM   14072 C  C     . ALA D 2 109 ? 125.349 95.951  138.148 1.00 19.84 ?  88  ALA D C     1 
ATOM   14073 O  O     . ALA D 2 109 ? 125.977 95.699  137.114 1.00 19.96 ?  88  ALA D O     1 
ATOM   14074 C  CB    . ALA D 2 109 ? 122.832 95.683  138.263 1.00 19.65 ?  88  ALA D CB    1 
ATOM   14075 N  N     . VAL D 2 110 ? 125.643 96.981  138.938 1.00 19.33 ?  89  VAL D N     1 
ATOM   14076 C  CA    . VAL D 2 110 ? 126.759 97.888  138.634 1.00 19.22 ?  89  VAL D CA    1 
ATOM   14077 C  C     . VAL D 2 110 ? 128.074 97.087  138.643 1.00 19.45 ?  89  VAL D C     1 
ATOM   14078 O  O     . VAL D 2 110 ? 128.846 97.121  137.675 1.00 18.97 ?  89  VAL D O     1 
ATOM   14079 C  CB    . VAL D 2 110 ? 126.770 99.109  139.596 1.00 19.01 ?  89  VAL D CB    1 
ATOM   14080 C  CG1   . VAL D 2 110 ? 128.050 99.978  139.419 1.00 19.90 ?  89  VAL D CG1   1 
ATOM   14081 C  CG2   . VAL D 2 110 ? 125.543 99.958  139.348 1.00 19.69 ?  89  VAL D CG2   1 
ATOM   14082 N  N     . LEU D 2 111 ? 128.285 96.309  139.706 1.00 19.27 ?  90  LEU D N     1 
ATOM   14083 C  CA    . LEU D 2 111 ? 129.474 95.458  139.789 1.00 19.96 ?  90  LEU D CA    1 
ATOM   14084 C  C     . LEU D 2 111 ? 129.605 94.476  138.618 1.00 20.30 ?  90  LEU D C     1 
ATOM   14085 O  O     . LEU D 2 111 ? 130.704 94.293  138.087 1.00 19.88 ?  90  LEU D O     1 
ATOM   14086 C  CB    . LEU D 2 111 ? 129.561 94.751  141.148 1.00 19.87 ?  90  LEU D CB    1 
ATOM   14087 C  CG    . LEU D 2 111 ? 129.806 95.712  142.313 1.00 20.24 ?  90  LEU D CG    1 
ATOM   14088 C  CD1   . LEU D 2 111 ? 129.546 95.069  143.685 1.00 21.85 ?  90  LEU D CD1   1 
ATOM   14089 C  CD2   . LEU D 2 111 ? 131.219 96.323  142.240 1.00 20.29 ?  90  LEU D CD2   1 
ATOM   14090 N  N     . ASN D 2 112 ? 128.490 93.869  138.202 1.00 20.92 ?  91  ASN D N     1 
ATOM   14091 C  CA    . ASN D 2 112 ? 128.473 93.028  136.983 1.00 20.70 ?  91  ASN D CA    1 
ATOM   14092 C  C     . ASN D 2 112 ? 128.894 93.782  135.734 1.00 20.57 ?  91  ASN D C     1 
ATOM   14093 O  O     . ASN D 2 112 ? 129.567 93.224  134.851 1.00 20.45 ?  91  ASN D O     1 
ATOM   14094 C  CB    . ASN D 2 112 ? 127.074 92.475  136.707 1.00 21.16 ?  91  ASN D CB    1 
ATOM   14095 C  CG    . ASN D 2 112 ? 126.868 91.077  137.254 1.00 21.98 ?  91  ASN D CG    1 
ATOM   14096 O  OD1   . ASN D 2 112 ? 127.731 90.515  137.937 1.00 25.37 ?  91  ASN D OD1   1 
ATOM   14097 N  ND2   . ASN D 2 112 ? 125.706 90.516  136.976 1.00 21.12 ?  91  ASN D ND2   1 
ATOM   14098 N  N     . PHE D 2 113 ? 128.423 95.021  135.619 1.00 19.70 ?  92  PHE D N     1 
ATOM   14099 C  CA    . PHE D 2 113 ? 128.790 95.851  134.492 1.00 20.02 ?  92  PHE D CA    1 
ATOM   14100 C  C     . PHE D 2 113 ? 130.302 96.120  134.482 1.00 19.97 ?  92  PHE D C     1 
ATOM   14101 O  O     . PHE D 2 113 ? 130.953 96.016  133.437 1.00 19.22 ?  92  PHE D O     1 
ATOM   14102 C  CB    . PHE D 2 113 ? 127.993 97.166  134.455 1.00 20.09 ?  92  PHE D CB    1 
ATOM   14103 C  CG    . PHE D 2 113 ? 128.230 97.951  133.213 1.00 20.54 ?  92  PHE D CG    1 
ATOM   14104 C  CD1   . PHE D 2 113 ? 127.441 97.740  132.081 1.00 20.14 ?  92  PHE D CD1   1 
ATOM   14105 C  CD2   . PHE D 2 113 ? 129.289 98.858  133.147 1.00 20.77 ?  92  PHE D CD2   1 
ATOM   14106 C  CE1   . PHE D 2 113 ? 127.686 98.447  130.907 1.00 20.54 ?  92  PHE D CE1   1 
ATOM   14107 C  CE2   . PHE D 2 113 ? 129.545 99.564  131.972 1.00 21.23 ?  92  PHE D CE2   1 
ATOM   14108 C  CZ    . PHE D 2 113 ? 128.737 99.350  130.848 1.00 20.92 ?  92  PHE D CZ    1 
ATOM   14109 N  N     . MET D 2 114 ? 130.850 96.450  135.648 1.00 19.67 ?  93  MET D N     1 
ATOM   14110 C  CA    . MET D 2 114 ? 132.287 96.662  135.774 1.00 20.55 ?  93  MET D CA    1 
ATOM   14111 C  C     . MET D 2 114 ? 133.091 95.405  135.438 1.00 20.82 ?  93  MET D C     1 
ATOM   14112 O  O     . MET D 2 114 ? 134.094 95.511  134.745 1.00 20.43 ?  93  MET D O     1 
ATOM   14113 C  CB    . MET D 2 114 ? 132.643 97.176  137.165 1.00 20.24 ?  93  MET D CB    1 
ATOM   14114 C  CG    . MET D 2 114 ? 131.908 98.462  137.482 1.00 22.05 ?  93  MET D CG    1 
ATOM   14115 S  SD    . MET D 2 114 ? 132.109 99.032  139.154 1.00 25.85 ?  93  MET D SD    1 
ATOM   14116 C  CE    . MET D 2 114 ? 131.757 100.781 138.914 1.00 27.57 ?  93  MET D CE    1 
ATOM   14117 N  N     . ALA D 2 115 ? 132.647 94.236  135.923 1.00 21.19 ?  94  ALA D N     1 
ATOM   14118 C  CA    . ALA D 2 115 ? 133.305 92.958  135.590 1.00 21.53 ?  94  ALA D CA    1 
ATOM   14119 C  C     . ALA D 2 115 ? 133.276 92.709  134.083 1.00 21.75 ?  94  ALA D C     1 
ATOM   14120 O  O     . ALA D 2 115 ? 134.284 92.303  133.504 1.00 22.18 ?  94  ALA D O     1 
ATOM   14121 C  CB    . ALA D 2 115 ? 132.671 91.786  136.348 1.00 21.32 ?  94  ALA D CB    1 
ATOM   14122 N  N     . MET D 2 116 ? 132.132 92.981  133.452 1.00 21.47 ?  95  MET D N     1 
ATOM   14123 C  CA    . MET D 2 116 ? 132.005 92.883  132.001 1.00 21.83 ?  95  MET D CA    1 
ATOM   14124 C  C     . MET D 2 116 ? 133.059 93.741  131.274 1.00 22.15 ?  95  MET D C     1 
ATOM   14125 O  O     . MET D 2 116 ? 133.707 93.268  130.343 1.00 22.09 ?  95  MET D O     1 
ATOM   14126 C  CB    . MET D 2 116 ? 130.583 93.264  131.555 1.00 21.72 ?  95  MET D CB    1 
ATOM   14127 C  CG    . MET D 2 116 ? 130.364 93.294  130.033 1.00 22.57 ?  95  MET D CG    1 
ATOM   14128 S  SD    . MET D 2 116 ? 130.982 94.786  129.212 1.00 22.75 ?  95  MET D SD    1 
ATOM   14129 C  CE    . MET D 2 116 ? 129.892 96.044  129.874 1.00 22.96 ?  95  MET D CE    1 
ATOM   14130 N  N     . MET D 2 117 ? 133.221 94.994  131.705 1.00 22.04 ?  96  MET D N     1 
ATOM   14131 C  CA    . MET D 2 117 ? 134.199 95.905  131.087 1.00 22.45 ?  96  MET D CA    1 
ATOM   14132 C  C     . MET D 2 117 ? 135.631 95.351  131.179 1.00 22.39 ?  96  MET D C     1 
ATOM   14133 O  O     . MET D 2 117 ? 136.402 95.451  130.223 1.00 21.88 ?  96  MET D O     1 
ATOM   14134 C  CB    . MET D 2 117 ? 134.112 97.318  131.700 1.00 22.00 ?  96  MET D CB    1 
ATOM   14135 C  CG    . MET D 2 117 ? 132.838 98.101  131.288 1.00 23.25 ?  96  MET D CG    1 
ATOM   14136 S  SD    . MET D 2 117 ? 132.661 98.321  129.501 1.00 24.28 ?  96  MET D SD    1 
ATOM   14137 C  CE    . MET D 2 117 ? 133.923 99.544  129.162 1.00 24.59 ?  96  MET D CE    1 
ATOM   14138 N  N     . GLU D 2 118 ? 135.971 94.749  132.318 1.00 22.66 ?  97  GLU D N     1 
ATOM   14139 C  CA    . GLU D 2 118 ? 137.292 94.132  132.490 1.00 23.52 ?  97  GLU D CA    1 
ATOM   14140 C  C     . GLU D 2 118 ? 137.524 93.019  131.482 1.00 24.25 ?  97  GLU D C     1 
ATOM   14141 O  O     . GLU D 2 118 ? 138.548 93.014  130.795 1.00 25.05 ?  97  GLU D O     1 
ATOM   14142 C  CB    . GLU D 2 118 ? 137.505 93.579  133.919 1.00 23.11 ?  97  GLU D CB    1 
ATOM   14143 C  CG    . GLU D 2 118 ? 137.059 94.485  135.074 1.00 23.08 ?  97  GLU D CG    1 
ATOM   14144 C  CD    . GLU D 2 118 ? 137.904 95.735  135.257 1.00 24.08 ?  97  GLU D CD    1 
ATOM   14145 O  OE1   . GLU D 2 118 ? 138.654 96.097  134.338 1.00 26.39 ?  97  GLU D OE1   1 
ATOM   14146 O  OE2   . GLU D 2 118 ? 137.798 96.379  136.322 1.00 27.52 -1 97  GLU D OE2   1 
ATOM   14147 N  N     . ASN D 2 119 ? 136.565 92.103  131.385 1.00 25.47 ?  98  ASN D N     1 
ATOM   14148 C  CA    . ASN D 2 119 ? 136.711 90.855  130.609 1.00 26.32 ?  98  ASN D CA    1 
ATOM   14149 C  C     . ASN D 2 119 ? 136.417 90.979  129.117 1.00 26.22 ?  98  ASN D C     1 
ATOM   14150 O  O     . ASN D 2 119 ? 137.088 90.340  128.280 1.00 26.54 ?  98  ASN D O     1 
ATOM   14151 C  CB    . ASN D 2 119 ? 135.825 89.747  131.207 1.00 26.72 ?  98  ASN D CB    1 
ATOM   14152 C  CG    . ASN D 2 119 ? 136.270 89.337  132.610 1.00 29.12 ?  98  ASN D CG    1 
ATOM   14153 O  OD1   . ASN D 2 119 ? 137.436 88.992  132.831 1.00 32.07 ?  98  ASN D OD1   1 
ATOM   14154 N  ND2   . ASN D 2 119 ? 135.350 89.404  133.566 1.00 29.12 ?  98  ASN D ND2   1 
ATOM   14155 N  N     . ALA D 2 120 ? 135.404 91.775  128.794 1.00 25.46 ?  99  ALA D N     1 
ATOM   14156 C  CA    . ALA D 2 120 ? 134.923 91.898  127.420 1.00 25.77 ?  99  ALA D CA    1 
ATOM   14157 C  C     . ALA D 2 120 ? 135.538 93.072  126.664 1.00 25.51 ?  99  ALA D C     1 
ATOM   14158 O  O     . ALA D 2 120 ? 135.641 93.029  125.436 1.00 26.64 ?  99  ALA D O     1 
ATOM   14159 C  CB    . ALA D 2 120 ? 133.388 91.995  127.390 1.00 25.75 ?  99  ALA D CB    1 
ATOM   14160 N  N     . VAL D 2 121 ? 135.935 94.117  127.383 1.00 24.40 ?  100 VAL D N     1 
ATOM   14161 C  CA    . VAL D 2 121 ? 136.389 95.337  126.726 1.00 24.15 ?  100 VAL D CA    1 
ATOM   14162 C  C     . VAL D 2 121 ? 137.881 95.588  126.961 1.00 23.94 ?  100 VAL D C     1 
ATOM   14163 O  O     . VAL D 2 121 ? 138.663 95.643  126.007 1.00 23.75 ?  100 VAL D O     1 
ATOM   14164 C  CB    . VAL D 2 121 ? 135.527 96.570  127.136 1.00 23.68 ?  100 VAL D CB    1 
ATOM   14165 C  CG1   . VAL D 2 121 ? 135.996 97.827  126.404 1.00 23.76 ?  100 VAL D CG1   1 
ATOM   14166 C  CG2   . VAL D 2 121 ? 134.051 96.305  126.825 1.00 23.99 ?  100 VAL D CG2   1 
ATOM   14167 N  N     . HIS D 2 122 ? 138.267 95.731  128.227 1.00 23.68 ?  101 HIS D N     1 
ATOM   14168 C  CA    . HIS D 2 122 ? 139.663 95.996  128.580 1.00 24.02 ?  101 HIS D CA    1 
ATOM   14169 C  C     . HIS D 2 122 ? 140.609 94.900  128.121 1.00 24.39 ?  101 HIS D C     1 
ATOM   14170 O  O     . HIS D 2 122 ? 141.645 95.197  127.531 1.00 24.71 ?  101 HIS D O     1 
ATOM   14171 C  CB    . HIS D 2 122 ? 139.836 96.249  130.083 1.00 23.20 ?  101 HIS D CB    1 
ATOM   14172 C  CG    . HIS D 2 122 ? 139.128 97.472  130.577 1.00 22.82 ?  101 HIS D CG    1 
ATOM   14173 N  ND1   . HIS D 2 122 ? 139.112 97.833  131.907 1.00 20.48 ?  101 HIS D ND1   1 
ATOM   14174 C  CD2   . HIS D 2 122 ? 138.389 98.403  129.926 1.00 21.03 ?  101 HIS D CD2   1 
ATOM   14175 C  CE1   . HIS D 2 122 ? 138.409 98.941  132.052 1.00 19.88 ?  101 HIS D CE1   1 
ATOM   14176 N  NE2   . HIS D 2 122 ? 137.960 99.310  130.864 1.00 21.62 ?  101 HIS D NE2   1 
ATOM   14177 N  N     . ALA D 2 123 ? 140.258 93.639  128.377 1.00 25.30 ?  102 ALA D N     1 
ATOM   14178 C  CA    . ALA D 2 123 ? 141.154 92.524  128.037 1.00 25.77 ?  102 ALA D CA    1 
ATOM   14179 C  C     . ALA D 2 123 ? 141.387 92.405  126.528 1.00 26.37 ?  102 ALA D C     1 
ATOM   14180 O  O     . ALA D 2 123 ? 142.508 92.132  126.080 1.00 25.87 ?  102 ALA D O     1 
ATOM   14181 C  CB    . ALA D 2 123 ? 140.630 91.203  128.614 1.00 26.43 ?  102 ALA D CB    1 
ATOM   14182 N  N     . LYS D 2 124 ? 140.323 92.614  125.751 1.00 26.51 ?  103 LYS D N     1 
ATOM   14183 C  CA    . LYS D 2 124 ? 140.414 92.588  124.298 1.00 27.22 ?  103 LYS D CA    1 
ATOM   14184 C  C     . LYS D 2 124 ? 141.242 93.776  123.788 1.00 26.63 ?  103 LYS D C     1 
ATOM   14185 O  O     . LYS D 2 124 ? 141.992 93.638  122.821 1.00 26.07 ?  103 LYS D O     1 
ATOM   14186 C  CB    . LYS D 2 124 ? 139.008 92.577  123.665 1.00 27.51 ?  103 LYS D CB    1 
ATOM   14187 C  CG    . LYS D 2 124 ? 138.971 92.639  122.123 1.00 30.58 ?  103 LYS D CG    1 
ATOM   14188 C  CD    . LYS D 2 124 ? 139.533 91.379  121.480 1.00 35.72 ?  103 LYS D CD    1 
ATOM   14189 C  CE    . LYS D 2 124 ? 139.526 91.455  119.951 1.00 37.33 ?  103 LYS D CE    1 
ATOM   14190 N  NZ    . LYS D 2 124 ? 138.132 91.492  119.435 1.00 40.73 1  103 LYS D NZ    1 
ATOM   14191 N  N     . SER D 2 125 ? 141.112 94.924  124.459 1.00 26.02 ?  104 SER D N     1 
ATOM   14192 C  CA    . SER D 2 125 ? 141.832 96.145  124.091 1.00 26.16 ?  104 SER D CA    1 
ATOM   14193 C  C     . SER D 2 125 ? 143.343 96.004  124.274 1.00 26.18 ?  104 SER D C     1 
ATOM   14194 O  O     . SER D 2 125 ? 144.117 96.427  123.407 1.00 26.06 ?  104 SER D O     1 
ATOM   14195 C  CB    . SER D 2 125 ? 141.320 97.348  124.887 1.00 26.10 ?  104 SER D CB    1 
ATOM   14196 O  OG    . SER D 2 125 ? 139.977 97.630  124.540 1.00 26.58 ?  104 SER D OG    1 
ATOM   14197 N  N     . TYR D 2 126 ? 143.751 95.416  125.396 1.00 25.68 ?  105 TYR D N     1 
ATOM   14198 C  CA    . TYR D 2 126 ? 145.171 95.160  125.670 1.00 26.12 ?  105 TYR D CA    1 
ATOM   14199 C  C     . TYR D 2 126 ? 145.748 94.173  124.649 1.00 26.38 ?  105 TYR D C     1 
ATOM   14200 O  O     . TYR D 2 126 ? 146.845 94.375  124.126 1.00 26.83 ?  105 TYR D O     1 
ATOM   14201 C  CB    . TYR D 2 126 ? 145.380 94.618  127.097 1.00 25.35 ?  105 TYR D CB    1 
ATOM   14202 C  CG    . TYR D 2 126 ? 145.334 95.662  128.196 1.00 25.46 ?  105 TYR D CG    1 
ATOM   14203 C  CD1   . TYR D 2 126 ? 146.174 96.776  128.159 1.00 25.41 ?  105 TYR D CD1   1 
ATOM   14204 C  CD2   . TYR D 2 126 ? 144.474 95.521  129.296 1.00 24.77 ?  105 TYR D CD2   1 
ATOM   14205 C  CE1   . TYR D 2 126 ? 146.145 97.740  129.165 1.00 25.89 ?  105 TYR D CE1   1 
ATOM   14206 C  CE2   . TYR D 2 126 ? 144.437 96.487  130.313 1.00 23.11 ?  105 TYR D CE2   1 
ATOM   14207 C  CZ    . TYR D 2 126 ? 145.286 97.583  130.246 1.00 25.38 ?  105 TYR D CZ    1 
ATOM   14208 O  OH    . TYR D 2 126 ? 145.278 98.550  131.228 1.00 23.31 ?  105 TYR D OH    1 
ATOM   14209 N  N     . SER D 2 127 ? 144.992 93.120  124.358 1.00 27.16 ?  106 SER D N     1 
ATOM   14210 C  CA    . SER D 2 127 ? 145.397 92.123  123.361 1.00 27.83 ?  106 SER D CA    1 
ATOM   14211 C  C     . SER D 2 127 ? 145.597 92.768  121.982 1.00 28.21 ?  106 SER D C     1 
ATOM   14212 O  O     . SER D 2 127 ? 146.621 92.532  121.329 1.00 28.30 ?  106 SER D O     1 
ATOM   14213 C  CB    . SER D 2 127 ? 144.373 90.977  123.299 1.00 28.37 ?  106 SER D CB    1 
ATOM   14214 O  OG    . SER D 2 127 ? 144.686 90.052  122.259 1.00 29.33 ?  106 SER D OG    1 
ATOM   14215 N  N     . ASN D 2 128 ? 144.624 93.584  121.561 1.00 28.27 ?  107 ASN D N     1 
ATOM   14216 C  CA    . ASN D 2 128 ? 144.695 94.354  120.309 1.00 28.79 ?  107 ASN D CA    1 
ATOM   14217 C  C     . ASN D 2 128 ? 145.932 95.240  120.198 1.00 28.53 ?  107 ASN D C     1 
ATOM   14218 O  O     . ASN D 2 128 ? 146.578 95.271  119.145 1.00 28.03 ?  107 ASN D O     1 
ATOM   14219 C  CB    . ASN D 2 128 ? 143.437 95.216  120.103 1.00 29.05 ?  107 ASN D CB    1 
ATOM   14220 C  CG    . ASN D 2 128 ? 142.189 94.385  119.789 1.00 30.48 ?  107 ASN D CG    1 
ATOM   14221 O  OD1   . ASN D 2 128 ? 142.274 93.187  119.530 1.00 32.19 ?  107 ASN D OD1   1 
ATOM   14222 N  ND2   . ASN D 2 128 ? 141.026 95.026  119.832 1.00 31.59 ?  107 ASN D ND2   1 
ATOM   14223 N  N     . ILE D 2 129 ? 146.245 95.976  121.266 1.00 28.21 ?  108 ILE D N     1 
ATOM   14224 C  CA    . ILE D 2 129 ? 147.461 96.802  121.285 1.00 28.76 ?  108 ILE D CA    1 
ATOM   14225 C  C     . ILE D 2 129 ? 148.714 95.935  121.072 1.00 29.83 ?  108 ILE D C     1 
ATOM   14226 O  O     . ILE D 2 129 ? 149.567 96.257  120.234 1.00 29.99 ?  108 ILE D O     1 
ATOM   14227 C  CB    . ILE D 2 129 ? 147.587 97.663  122.583 1.00 28.28 ?  108 ILE D CB    1 
ATOM   14228 C  CG1   . ILE D 2 129 ? 146.435 98.674  122.684 1.00 27.94 ?  108 ILE D CG1   1 
ATOM   14229 C  CG2   . ILE D 2 129 ? 148.931 98.405  122.609 1.00 27.52 ?  108 ILE D CG2   1 
ATOM   14230 C  CD1   . ILE D 2 129 ? 146.268 99.294  124.066 1.00 27.98 ?  108 ILE D CD1   1 
ATOM   14231 N  N     . PHE D 2 130 ? 148.820 94.843  121.824 1.00 30.86 ?  109 PHE D N     1 
ATOM   14232 C  CA    . PHE D 2 130 ? 149.946 93.924  121.687 1.00 32.76 ?  109 PHE D CA    1 
ATOM   14233 C  C     . PHE D 2 130 ? 150.111 93.374  120.267 1.00 34.37 ?  109 PHE D C     1 
ATOM   14234 O  O     . PHE D 2 130 ? 151.192 93.467  119.690 1.00 34.61 ?  109 PHE D O     1 
ATOM   14235 C  CB    . PHE D 2 130 ? 149.830 92.767  122.676 1.00 32.81 ?  109 PHE D CB    1 
ATOM   14236 C  CG    . PHE D 2 130 ? 150.600 92.975  123.949 1.00 33.84 ?  109 PHE D CG    1 
ATOM   14237 C  CD1   . PHE D 2 130 ? 151.993 92.988  123.940 1.00 34.61 ?  109 PHE D CD1   1 
ATOM   14238 C  CD2   . PHE D 2 130 ? 149.935 93.124  125.159 1.00 35.74 ?  109 PHE D CD2   1 
ATOM   14239 C  CE1   . PHE D 2 130 ? 152.716 93.169  125.119 1.00 36.99 ?  109 PHE D CE1   1 
ATOM   14240 C  CE2   . PHE D 2 130 ? 150.646 93.306  126.352 1.00 36.96 ?  109 PHE D CE2   1 
ATOM   14241 C  CZ    . PHE D 2 130 ? 152.040 93.328  126.332 1.00 36.91 ?  109 PHE D CZ    1 
ATOM   14242 N  N     . MET D 2 131 ? 149.031 92.821  119.715 1.00 35.90 ?  110 MET D N     1 
ATOM   14243 C  CA    . MET D 2 131 ? 149.039 92.214  118.383 1.00 37.94 ?  110 MET D CA    1 
ATOM   14244 C  C     . MET D 2 131 ? 149.418 93.209  117.294 1.00 38.05 ?  110 MET D C     1 
ATOM   14245 O  O     . MET D 2 131 ? 149.969 92.820  116.271 1.00 38.20 ?  110 MET D O     1 
ATOM   14246 C  CB    . MET D 2 131 ? 147.682 91.570  118.054 1.00 38.63 ?  110 MET D CB    1 
ATOM   14247 C  CG    . MET D 2 131 ? 147.339 90.329  118.895 1.00 42.34 ?  110 MET D CG    1 
ATOM   14248 S  SD    . MET D 2 131 ? 145.734 89.562  118.495 1.00 50.15 ?  110 MET D SD    1 
ATOM   14249 C  CE    . MET D 2 131 ? 144.550 90.777  119.092 1.00 48.14 ?  110 MET D CE    1 
ATOM   14250 N  N     . THR D 2 132 ? 149.120 94.488  117.521 1.00 38.12 ?  111 THR D N     1 
ATOM   14251 C  CA    . THR D 2 132 ? 149.473 95.540  116.569 1.00 38.79 ?  111 THR D CA    1 
ATOM   14252 C  C     . THR D 2 132 ? 150.979 95.859  116.584 1.00 38.81 ?  111 THR D C     1 
ATOM   14253 O  O     . THR D 2 132 ? 151.587 96.029  115.522 1.00 39.26 ?  111 THR D O     1 
ATOM   14254 C  CB    . THR D 2 132 ? 148.648 96.819  116.816 1.00 38.78 ?  111 THR D CB    1 
ATOM   14255 O  OG1   . THR D 2 132 ? 147.252 96.505  116.743 1.00 39.32 ?  111 THR D OG1   1 
ATOM   14256 C  CG2   . THR D 2 132 ? 148.957 97.884  115.769 1.00 39.75 ?  111 THR D CG2   1 
ATOM   14257 N  N     . LEU D 2 133 ? 151.565 95.921  117.780 1.00 38.34 ?  112 LEU D N     1 
ATOM   14258 C  CA    . LEU D 2 133 ? 152.942 96.391  117.968 1.00 38.36 ?  112 LEU D CA    1 
ATOM   14259 C  C     . LEU D 2 133 ? 154.016 95.303  117.917 1.00 38.94 ?  112 LEU D C     1 
ATOM   14260 O  O     . LEU D 2 133 ? 155.144 95.569  117.504 1.00 39.14 ?  112 LEU D O     1 
ATOM   14261 C  CB    . LEU D 2 133 ? 153.071 97.161  119.294 1.00 37.62 ?  112 LEU D CB    1 
ATOM   14262 C  CG    . LEU D 2 133 ? 152.133 98.344  119.546 1.00 36.50 ?  112 LEU D CG    1 
ATOM   14263 C  CD1   . LEU D 2 133 ? 152.245 98.814  121.000 1.00 35.80 ?  112 LEU D CD1   1 
ATOM   14264 C  CD2   . LEU D 2 133 ? 152.381 99.491  118.581 1.00 35.32 ?  112 LEU D CD2   1 
ATOM   14265 N  N     . ALA D 2 134 ? 153.687 94.091  118.342 1.00 39.41 ?  113 ALA D N     1 
ATOM   14266 C  CA    . ALA D 2 134 ? 154.697 93.026  118.380 1.00 40.33 ?  113 ALA D CA    1 
ATOM   14267 C  C     . ALA D 2 134 ? 154.264 91.777  117.619 1.00 41.05 ?  113 ALA D C     1 
ATOM   14268 O  O     . ALA D 2 134 ? 153.074 91.495  117.539 1.00 40.81 ?  113 ALA D O     1 
ATOM   14269 C  CB    . ALA D 2 134 ? 155.041 92.682  119.817 1.00 40.15 ?  113 ALA D CB    1 
ATOM   14270 N  N     . PRO D 2 135 ? 155.231 91.028  117.046 1.00 42.21 ?  114 PRO D N     1 
ATOM   14271 C  CA    . PRO D 2 135 ? 154.874 89.725  116.472 1.00 43.27 ?  114 PRO D CA    1 
ATOM   14272 C  C     . PRO D 2 135 ? 154.576 88.697  117.573 1.00 43.89 ?  114 PRO D C     1 
ATOM   14273 O  O     . PRO D 2 135 ? 154.997 88.880  118.719 1.00 43.31 ?  114 PRO D O     1 
ATOM   14274 C  CB    . PRO D 2 135 ? 156.127 89.327  115.687 1.00 43.69 ?  114 PRO D CB    1 
ATOM   14275 C  CG    . PRO D 2 135 ? 157.236 90.034  116.369 1.00 43.01 ?  114 PRO D CG    1 
ATOM   14276 C  CD    . PRO D 2 135 ? 156.666 91.329  116.879 1.00 42.16 ?  114 PRO D CD    1 
ATOM   14277 N  N     . THR D 2 136 ? 153.866 87.628  117.213 1.00 45.26 ?  115 THR D N     1 
ATOM   14278 C  CA    . THR D 2 136 ? 153.390 86.619  118.173 1.00 46.11 ?  115 THR D CA    1 
ATOM   14279 C  C     . THR D 2 136 ? 154.482 86.115  119.121 1.00 46.35 ?  115 THR D C     1 
ATOM   14280 O  O     . THR D 2 136 ? 154.263 86.040  120.335 1.00 46.25 ?  115 THR D O     1 
ATOM   14281 C  CB    . THR D 2 136 ? 152.692 85.427  117.461 1.00 46.59 ?  115 THR D CB    1 
ATOM   14282 O  OG1   . THR D 2 136 ? 151.664 85.927  116.601 1.00 47.80 ?  115 THR D OG1   1 
ATOM   14283 C  CG2   . THR D 2 136 ? 152.046 84.475  118.466 1.00 46.94 ?  115 THR D CG2   1 
ATOM   14284 N  N     . GLU D 2 137 ? 155.656 85.797  118.575 1.00 46.92 ?  116 GLU D N     1 
ATOM   14285 C  CA    . GLU D 2 137 ? 156.761 85.273  119.376 1.00 47.37 ?  116 GLU D CA    1 
ATOM   14286 C  C     . GLU D 2 137 ? 157.256 86.262  120.435 1.00 46.64 ?  116 GLU D C     1 
ATOM   14287 O  O     . GLU D 2 137 ? 157.587 85.855  121.550 1.00 46.89 ?  116 GLU D O     1 
ATOM   14288 C  CB    . GLU D 2 137 ? 157.921 84.798  118.487 1.00 48.04 ?  116 GLU D CB    1 
ATOM   14289 C  CG    . GLU D 2 137 ? 159.076 84.115  119.242 1.00 49.86 ?  116 GLU D CG    1 
ATOM   14290 C  CD    . GLU D 2 137 ? 158.729 82.726  119.798 1.00 52.40 ?  116 GLU D CD    1 
ATOM   14291 O  OE1   . GLU D 2 137 ? 157.720 82.587  120.526 1.00 52.97 ?  116 GLU D OE1   1 
ATOM   14292 O  OE2   . GLU D 2 137 ? 159.489 81.767  119.524 1.00 54.12 -1 116 GLU D OE2   1 
ATOM   14293 N  N     . THR D 2 138 ? 157.299 87.546  120.082 1.00 46.09 ?  117 THR D N     1 
ATOM   14294 C  CA    . THR D 2 138 ? 157.698 88.610  121.016 1.00 45.30 ?  117 THR D CA    1 
ATOM   14295 C  C     . THR D 2 138 ? 156.687 88.782  122.157 1.00 44.63 ?  117 THR D C     1 
ATOM   14296 O  O     . THR D 2 138 ? 157.074 88.984  123.311 1.00 44.51 ?  117 THR D O     1 
ATOM   14297 C  CB    . THR D 2 138 ? 157.904 89.958  120.284 1.00 45.20 ?  117 THR D CB    1 
ATOM   14298 O  OG1   . THR D 2 138 ? 158.874 89.792  119.244 1.00 45.69 ?  117 THR D OG1   1 
ATOM   14299 C  CG2   . THR D 2 138 ? 158.390 91.045  121.242 1.00 44.67 ?  117 THR D CG2   1 
ATOM   14300 N  N     . ILE D 2 139 ? 155.397 88.693  121.832 1.00 44.24 ?  118 ILE D N     1 
ATOM   14301 C  CA    . ILE D 2 139 ? 154.337 88.780  122.839 1.00 43.65 ?  118 ILE D CA    1 
ATOM   14302 C  C     . ILE D 2 139 ? 154.470 87.645  123.866 1.00 43.87 ?  118 ILE D C     1 
ATOM   14303 O  O     . ILE D 2 139 ? 154.461 87.890  125.075 1.00 43.36 ?  118 ILE D O     1 
ATOM   14304 C  CB    . ILE D 2 139 ? 152.930 88.807  122.187 1.00 43.68 ?  118 ILE D CB    1 
ATOM   14305 C  CG1   . ILE D 2 139 ? 152.740 90.111  121.397 1.00 43.30 ?  118 ILE D CG1   1 
ATOM   14306 C  CG2   . ILE D 2 139 ? 151.822 88.647  123.245 1.00 43.11 ?  118 ILE D CG2   1 
ATOM   14307 C  CD1   . ILE D 2 139 ? 151.590 90.098  120.398 1.00 43.41 ?  118 ILE D CD1   1 
ATOM   14308 N  N     . ASN D 2 140 ? 154.626 86.417  123.375 1.00 44.52 ?  119 ASN D N     1 
ATOM   14309 C  CA    . ASN D 2 140 ? 154.799 85.245  124.240 1.00 45.00 ?  119 ASN D CA    1 
ATOM   14310 C  C     . ASN D 2 140 ? 156.008 85.367  125.192 1.00 44.99 ?  119 ASN D C     1 
ATOM   14311 O  O     . ASN D 2 140 ? 155.917 84.995  126.369 1.00 44.61 ?  119 ASN D O     1 
ATOM   14312 C  CB    . ASN D 2 140 ? 154.879 83.955  123.404 1.00 45.74 ?  119 ASN D CB    1 
ATOM   14313 C  CG    . ASN D 2 140 ? 153.609 83.692  122.586 1.00 46.40 ?  119 ASN D CG    1 
ATOM   14314 O  OD1   . ASN D 2 140 ? 152.553 84.290  122.823 1.00 46.85 ?  119 ASN D OD1   1 
ATOM   14315 N  ND2   . ASN D 2 140 ? 153.712 82.782  121.620 1.00 48.16 ?  119 ASN D ND2   1 
ATOM   14316 N  N     . GLU D 2 141 ? 157.117 85.913  124.689 1.00 45.09 ?  120 GLU D N     1 
ATOM   14317 C  CA    . GLU D 2 141 ? 158.330 86.095  125.492 1.00 45.27 ?  120 GLU D CA    1 
ATOM   14318 C  C     . GLU D 2 141 ? 158.194 87.175  126.576 1.00 44.75 ?  120 GLU D C     1 
ATOM   14319 O  O     . GLU D 2 141 ? 158.648 86.984  127.709 1.00 44.37 ?  120 GLU D O     1 
ATOM   14320 C  CB    . GLU D 2 141 ? 159.538 86.389  124.602 1.00 45.75 ?  120 GLU D CB    1 
ATOM   14321 C  CG    . GLU D 2 141 ? 159.979 85.206  123.740 1.00 48.17 ?  120 GLU D CG    1 
ATOM   14322 C  CD    . GLU D 2 141 ? 161.213 85.500  122.911 1.00 50.15 ?  120 GLU D CD    1 
ATOM   14323 O  OE1   . GLU D 2 141 ? 162.215 85.992  123.472 1.00 50.90 ?  120 GLU D OE1   1 
ATOM   14324 O  OE2   . GLU D 2 141 ? 161.183 85.231  121.692 1.00 52.25 -1 120 GLU D OE2   1 
ATOM   14325 N  N     . VAL D 2 142 ? 157.586 88.305  126.216 1.00 44.31 ?  121 VAL D N     1 
ATOM   14326 C  CA    . VAL D 2 142 ? 157.329 89.388  127.166 1.00 43.91 ?  121 VAL D CA    1 
ATOM   14327 C  C     . VAL D 2 142 ? 156.437 88.901  128.311 1.00 43.71 ?  121 VAL D C     1 
ATOM   14328 O  O     . VAL D 2 142 ? 156.698 89.198  129.476 1.00 43.44 ?  121 VAL D O     1 
ATOM   14329 C  CB    . VAL D 2 142 ? 156.702 90.632  126.476 1.00 43.65 ?  121 VAL D CB    1 
ATOM   14330 C  CG1   . VAL D 2 142 ? 156.325 91.695  127.507 1.00 43.40 ?  121 VAL D CG1   1 
ATOM   14331 C  CG2   . VAL D 2 142 ? 157.672 91.221  125.457 1.00 43.96 ?  121 VAL D CG2   1 
ATOM   14332 N  N     . PHE D 2 143 ? 155.396 88.143  127.976 1.00 44.03 ?  122 PHE D N     1 
ATOM   14333 C  CA    . PHE D 2 143 ? 154.503 87.603  128.995 1.00 44.42 ?  122 PHE D CA    1 
ATOM   14334 C  C     . PHE D 2 143 ? 155.170 86.546  129.869 1.00 45.38 ?  122 PHE D C     1 
ATOM   14335 O  O     . PHE D 2 143 ? 154.902 86.484  131.066 1.00 45.50 ?  122 PHE D O     1 
ATOM   14336 C  CB    . PHE D 2 143 ? 153.189 87.102  128.390 1.00 44.27 ?  122 PHE D CB    1 
ATOM   14337 C  CG    . PHE D 2 143 ? 152.156 88.180  128.262 1.00 43.28 ?  122 PHE D CG    1 
ATOM   14338 C  CD1   . PHE D 2 143 ? 151.375 88.544  129.358 1.00 42.17 ?  122 PHE D CD1   1 
ATOM   14339 C  CD2   . PHE D 2 143 ? 151.986 88.860  127.064 1.00 42.76 ?  122 PHE D CD2   1 
ATOM   14340 C  CE1   . PHE D 2 143 ? 150.428 89.555  129.257 1.00 42.16 ?  122 PHE D CE1   1 
ATOM   14341 C  CE2   . PHE D 2 143 ? 151.042 89.874  126.951 1.00 42.77 ?  122 PHE D CE2   1 
ATOM   14342 C  CZ    . PHE D 2 143 ? 150.259 90.223  128.050 1.00 42.28 ?  122 PHE D CZ    1 
ATOM   14343 N  N     . GLU D 2 144 ? 156.050 85.744  129.277 1.00 46.18 ?  123 GLU D N     1 
ATOM   14344 C  CA    . GLU D 2 144 ? 156.885 84.819  130.042 1.00 47.19 ?  123 GLU D CA    1 
ATOM   14345 C  C     . GLU D 2 144 ? 157.766 85.570  131.053 1.00 46.99 ?  123 GLU D C     1 
ATOM   14346 O  O     . GLU D 2 144 ? 157.856 85.158  132.214 1.00 46.94 ?  123 GLU D O     1 
ATOM   14347 C  CB    . GLU D 2 144 ? 157.746 83.967  129.099 1.00 47.80 ?  123 GLU D CB    1 
ATOM   14348 C  CG    . GLU D 2 144 ? 158.560 82.856  129.771 1.00 49.54 ?  123 GLU D CG    1 
ATOM   14349 C  CD    . GLU D 2 144 ? 159.486 82.121  128.797 1.00 52.37 ?  123 GLU D CD    1 
ATOM   14350 O  OE1   . GLU D 2 144 ? 160.183 82.785  127.996 1.00 52.92 ?  123 GLU D OE1   1 
ATOM   14351 O  OE2   . GLU D 2 144 ? 159.521 80.872  128.837 1.00 53.55 -1 123 GLU D OE2   1 
ATOM   14352 N  N     . TRP D 2 145 ? 158.398 86.661  130.607 1.00 47.02 ?  124 TRP D N     1 
ATOM   14353 C  CA    . TRP D 2 145 ? 159.274 87.491  131.454 1.00 46.93 ?  124 TRP D CA    1 
ATOM   14354 C  C     . TRP D 2 145 ? 158.496 88.151  132.583 1.00 46.55 ?  124 TRP D C     1 
ATOM   14355 O  O     . TRP D 2 145 ? 158.875 88.045  133.746 1.00 46.42 ?  124 TRP D O     1 
ATOM   14356 C  CB    . TRP D 2 145 ? 159.984 88.574  130.627 1.00 47.07 ?  124 TRP D CB    1 
ATOM   14357 C  CG    . TRP D 2 145 ? 161.069 89.357  131.373 1.00 47.82 ?  124 TRP D CG    1 
ATOM   14358 C  CD1   . TRP D 2 145 ? 162.409 89.074  131.402 1.00 48.78 ?  124 TRP D CD1   1 
ATOM   14359 C  CD2   . TRP D 2 145 ? 160.899 90.550  132.165 1.00 47.80 ?  124 TRP D CD2   1 
ATOM   14360 N  NE1   . TRP D 2 145 ? 163.080 90.006  132.164 1.00 49.06 ?  124 TRP D NE1   1 
ATOM   14361 C  CE2   . TRP D 2 145 ? 162.179 90.920  132.646 1.00 48.24 ?  124 TRP D CE2   1 
ATOM   14362 C  CE3   . TRP D 2 145 ? 159.793 91.336  132.519 1.00 47.65 ?  124 TRP D CE3   1 
ATOM   14363 C  CZ2   . TRP D 2 145 ? 162.382 92.043  133.466 1.00 47.74 ?  124 TRP D CZ2   1 
ATOM   14364 C  CZ3   . TRP D 2 145 ? 159.994 92.453  133.334 1.00 46.92 ?  124 TRP D CZ3   1 
ATOM   14365 C  CH2   . TRP D 2 145 ? 161.283 92.794  133.796 1.00 47.88 ?  124 TRP D CH2   1 
ATOM   14366 N  N     . VAL D 2 146 ? 157.409 88.833  132.233 1.00 46.09 ?  125 VAL D N     1 
ATOM   14367 C  CA    . VAL D 2 146 ? 156.620 89.568  133.215 1.00 45.36 ?  125 VAL D CA    1 
ATOM   14368 C  C     . VAL D 2 146 ? 155.934 88.598  134.190 1.00 45.28 ?  125 VAL D C     1 
ATOM   14369 O  O     . VAL D 2 146 ? 155.774 88.911  135.375 1.00 45.29 ?  125 VAL D O     1 
ATOM   14370 C  CB    . VAL D 2 146 ? 155.661 90.587  132.519 1.00 45.33 ?  125 VAL D CB    1 
ATOM   14371 C  CG1   . VAL D 2 146 ? 154.734 91.246  133.506 1.00 44.97 ?  125 VAL D CG1   1 
ATOM   14372 C  CG2   . VAL D 2 146 ? 156.477 91.668  131.805 1.00 44.52 ?  125 VAL D CG2   1 
ATOM   14373 N  N     . LYS D 2 147 ? 155.582 87.408  133.703 1.00 44.98 ?  126 LYS D N     1 
ATOM   14374 C  CA    . LYS D 2 147 ? 155.014 86.353  134.553 1.00 44.65 ?  126 LYS D CA    1 
ATOM   14375 C  C     . LYS D 2 147 ? 155.995 85.857  135.628 1.00 44.06 ?  126 LYS D C     1 
ATOM   14376 O  O     . LYS D 2 147 ? 155.579 85.425  136.704 1.00 44.65 ?  126 LYS D O     1 
ATOM   14377 C  CB    . LYS D 2 147 ? 154.533 85.165  133.715 1.00 45.31 ?  126 LYS D CB    1 
ATOM   14378 C  CG    . LYS D 2 147 ? 153.160 84.650  134.121 1.00 46.54 ?  126 LYS D CG    1 
ATOM   14379 C  CD    . LYS D 2 147 ? 153.085 83.122  134.148 1.00 49.06 ?  126 LYS D CD    1 
ATOM   14380 C  CE    . LYS D 2 147 ? 153.519 82.568  135.512 1.00 50.46 ?  126 LYS D CE    1 
ATOM   14381 N  NZ    . LYS D 2 147 ? 152.905 81.240  135.818 1.00 51.33 1  126 LYS D NZ    1 
ATOM   14382 N  N     . GLN D 2 148 ? 157.290 85.920  135.330 1.00 42.58 ?  127 GLN D N     1 
ATOM   14383 C  CA    . GLN D 2 148 ? 158.330 85.498  136.267 1.00 41.39 ?  127 GLN D CA    1 
ATOM   14384 C  C     . GLN D 2 148 ? 158.874 86.659  137.110 1.00 39.56 ?  127 GLN D C     1 
ATOM   14385 O  O     . GLN D 2 148 ? 159.533 86.432  138.124 1.00 39.77 ?  127 GLN D O     1 
ATOM   14386 C  CB    . GLN D 2 148 ? 159.454 84.771  135.503 1.00 42.11 ?  127 GLN D CB    1 
ATOM   14387 C  CG    . GLN D 2 148 ? 160.873 84.971  136.029 1.00 44.08 ?  127 GLN D CG    1 
ATOM   14388 C  CD    . GLN D 2 148 ? 161.658 86.045  135.275 1.00 46.12 ?  127 GLN D CD    1 
ATOM   14389 O  OE1   . GLN D 2 148 ? 161.130 87.114  134.941 1.00 46.47 ?  127 GLN D OE1   1 
ATOM   14390 N  NE2   . GLN D 2 148 ? 162.937 85.767  135.018 1.00 45.69 ?  127 GLN D NE2   1 
ATOM   14391 N  N     . ASN D 2 149 ? 158.584 87.893  136.689 1.00 36.99 ?  128 ASN D N     1 
ATOM   14392 C  CA    . ASN D 2 149 ? 159.091 89.091  137.358 1.00 34.54 ?  128 ASN D CA    1 
ATOM   14393 C  C     . ASN D 2 149 ? 158.675 89.214  138.826 1.00 33.13 ?  128 ASN D C     1 
ATOM   14394 O  O     . ASN D 2 149 ? 157.492 89.173  139.154 1.00 32.62 ?  128 ASN D O     1 
ATOM   14395 C  CB    . ASN D 2 149 ? 158.678 90.352  136.596 1.00 34.24 ?  128 ASN D CB    1 
ATOM   14396 C  CG    . ASN D 2 149 ? 159.283 91.607  137.192 1.00 33.83 ?  128 ASN D CG    1 
ATOM   14397 O  OD1   . ASN D 2 149 ? 158.622 92.337  137.934 1.00 32.21 ?  128 ASN D OD1   1 
ATOM   14398 N  ND2   . ASN D 2 149 ? 160.558 91.847  136.896 1.00 33.26 ?  128 ASN D ND2   1 
ATOM   14399 N  N     . LYS D 2 150 ? 159.666 89.398  139.695 1.00 31.49 ?  129 LYS D N     1 
ATOM   14400 C  CA    . LYS D 2 150 ? 159.466 89.410  141.142 1.00 30.68 ?  129 LYS D CA    1 
ATOM   14401 C  C     . LYS D 2 150 ? 158.514 90.521  141.649 1.00 28.95 ?  129 LYS D C     1 
ATOM   14402 O  O     . LYS D 2 150 ? 157.683 90.277  142.531 1.00 27.90 ?  129 LYS D O     1 
ATOM   14403 C  CB    . LYS D 2 150 ? 160.842 89.482  141.822 1.00 31.17 ?  129 LYS D CB    1 
ATOM   14404 C  CG    . LYS D 2 150 ? 160.877 89.855  143.290 1.00 33.66 ?  129 LYS D CG    1 
ATOM   14405 C  CD    . LYS D 2 150 ? 162.337 89.901  143.768 1.00 38.08 ?  129 LYS D CD    1 
ATOM   14406 C  CE    . LYS D 2 150 ? 162.524 90.833  144.971 1.00 40.20 ?  129 LYS D CE    1 
ATOM   14407 N  NZ    . LYS D 2 150 ? 162.393 90.119  146.270 1.00 42.60 1  129 LYS D NZ    1 
ATOM   14408 N  N     . TYR D 2 151 ? 158.640 91.727  141.098 1.00 27.36 ?  130 TYR D N     1 
ATOM   14409 C  CA    . TYR D 2 151 ? 157.863 92.878  141.591 1.00 26.56 ?  130 TYR D CA    1 
ATOM   14410 C  C     . TYR D 2 151 ? 156.425 92.859  141.096 1.00 25.66 ?  130 TYR D C     1 
ATOM   14411 O  O     . TYR D 2 151 ? 155.514 93.218  141.848 1.00 25.61 ?  130 TYR D O     1 
ATOM   14412 C  CB    . TYR D 2 151 ? 158.562 94.215  141.272 1.00 26.32 ?  130 TYR D CB    1 
ATOM   14413 C  CG    . TYR D 2 151 ? 160.044 94.167  141.593 1.00 27.20 ?  130 TYR D CG    1 
ATOM   14414 C  CD1   . TYR D 2 151 ? 160.482 94.123  142.917 1.00 27.31 ?  130 TYR D CD1   1 
ATOM   14415 C  CD2   . TYR D 2 151 ? 160.999 94.109  140.579 1.00 27.22 ?  130 TYR D CD2   1 
ATOM   14416 C  CE1   . TYR D 2 151 ? 161.838 94.045  143.225 1.00 29.65 ?  130 TYR D CE1   1 
ATOM   14417 C  CE2   . TYR D 2 151 ? 162.368 94.032  140.879 1.00 28.75 ?  130 TYR D CE2   1 
ATOM   14418 C  CZ    . TYR D 2 151 ? 162.770 94.009  142.217 1.00 29.17 ?  130 TYR D CZ    1 
ATOM   14419 O  OH    . TYR D 2 151 ? 164.101 93.935  142.559 1.00 30.61 ?  130 TYR D OH    1 
ATOM   14420 N  N     . LEU D 2 152 ? 156.227 92.441  139.845 1.00 24.87 ?  131 LEU D N     1 
ATOM   14421 C  CA    . LEU D 2 152 ? 154.880 92.247  139.319 1.00 24.37 ?  131 LEU D CA    1 
ATOM   14422 C  C     . LEU D 2 152 ? 154.161 91.136  140.094 1.00 24.18 ?  131 LEU D C     1 
ATOM   14423 O  O     . LEU D 2 152 ? 153.046 91.340  140.571 1.00 23.16 ?  131 LEU D O     1 
ATOM   14424 C  CB    . LEU D 2 152 ? 154.864 91.950  137.816 1.00 24.45 ?  131 LEU D CB    1 
ATOM   14425 C  CG    . LEU D 2 152 ? 153.380 91.826  137.427 1.00 26.33 ?  131 LEU D CG    1 
ATOM   14426 C  CD1   . LEU D 2 152 ? 152.706 93.205  137.387 1.00 25.00 ?  131 LEU D CD1   1 
ATOM   14427 C  CD2   . LEU D 2 152 ? 153.138 91.049  136.166 1.00 29.15 ?  131 LEU D CD2   1 
ATOM   14428 N  N     . GLN D 2 153 ? 154.816 89.983  140.243 1.00 24.07 ?  132 GLN D N     1 
ATOM   14429 C  CA    . GLN D 2 153 ? 154.238 88.873  141.030 1.00 24.99 ?  132 GLN D CA    1 
ATOM   14430 C  C     . GLN D 2 153 ? 153.917 89.248  142.474 1.00 24.24 ?  132 GLN D C     1 
ATOM   14431 O  O     . GLN D 2 153 ? 152.836 88.913  142.990 1.00 23.75 ?  132 GLN D O     1 
ATOM   14432 C  CB    . GLN D 2 153 ? 155.118 87.613  140.972 1.00 25.84 ?  132 GLN D CB    1 
ATOM   14433 C  CG    . GLN D 2 153 ? 155.105 86.911  139.588 1.00 28.48 ?  132 GLN D CG    1 
ATOM   14434 C  CD    . GLN D 2 153 ? 153.713 86.425  139.153 1.00 30.95 ?  132 GLN D CD    1 
ATOM   14435 O  OE1   . GLN D 2 153 ? 152.916 85.984  139.973 1.00 31.78 ?  132 GLN D OE1   1 
ATOM   14436 N  NE2   . GLN D 2 153 ? 153.431 86.496  137.851 1.00 32.81 ?  132 GLN D NE2   1 
ATOM   14437 N  N     . LYS D 2 154 ? 154.832 89.951  143.138 1.00 24.00 ?  133 LYS D N     1 
ATOM   14438 C  CA    . LYS D 2 154 ? 154.574 90.316  144.530 1.00 24.43 ?  133 LYS D CA    1 
ATOM   14439 C  C     . LYS D 2 154 ? 153.234 91.051  144.676 1.00 23.40 ?  133 LYS D C     1 
ATOM   14440 O  O     . LYS D 2 154 ? 152.383 90.647  145.472 1.00 22.68 ?  133 LYS D O     1 
ATOM   14441 C  CB    . LYS D 2 154 ? 155.698 91.158  145.144 1.00 24.64 ?  133 LYS D CB    1 
ATOM   14442 C  CG    . LYS D 2 154 ? 155.401 91.485  146.618 1.00 28.01 ?  133 LYS D CG    1 
ATOM   14443 C  CD    . LYS D 2 154 ? 156.537 92.163  147.346 1.00 32.56 ?  133 LYS D CD    1 
ATOM   14444 C  CE    . LYS D 2 154 ? 157.693 91.218  147.567 1.00 34.45 ?  133 LYS D CE    1 
ATOM   14445 N  NZ    . LYS D 2 154 ? 158.811 91.912  148.280 1.00 36.11 1  133 LYS D NZ    1 
ATOM   14446 N  N     . LYS D 2 155 ? 153.045 92.122  143.905 1.00 23.07 ?  134 LYS D N     1 
ATOM   14447 C  CA    . LYS D 2 155 ? 151.793 92.870  143.992 1.00 22.70 ?  134 LYS D CA    1 
ATOM   14448 C  C     . LYS D 2 155 ? 150.595 92.066  143.490 1.00 21.96 ?  134 LYS D C     1 
ATOM   14449 O  O     . LYS D 2 155 ? 149.547 92.085  144.128 1.00 22.25 ?  134 LYS D O     1 
ATOM   14450 C  CB    . LYS D 2 155 ? 151.886 94.257  143.330 1.00 22.70 ?  134 LYS D CB    1 
ATOM   14451 C  CG    . LYS D 2 155 ? 152.106 94.282  141.831 1.00 23.62 ?  134 LYS D CG    1 
ATOM   14452 C  CD    . LYS D 2 155 ? 152.092 95.730  141.347 1.00 25.32 ?  134 LYS D CD    1 
ATOM   14453 C  CE    . LYS D 2 155 ? 153.065 95.916  140.187 1.00 27.09 ?  134 LYS D CE    1 
ATOM   14454 N  NZ    . LYS D 2 155 ? 152.999 97.313  139.666 1.00 26.65 1  134 LYS D NZ    1 
ATOM   14455 N  N     . ALA D 2 156 ? 150.737 91.337  142.382 1.00 21.76 ?  135 ALA D N     1 
ATOM   14456 C  CA    . ALA D 2 156 ? 149.600 90.554  141.866 1.00 21.83 ?  135 ALA D CA    1 
ATOM   14457 C  C     . ALA D 2 156 ? 149.101 89.545  142.916 1.00 22.30 ?  135 ALA D C     1 
ATOM   14458 O  O     . ALA D 2 156 ? 147.897 89.449  143.172 1.00 21.92 ?  135 ALA D O     1 
ATOM   14459 C  CB    . ALA D 2 156 ? 149.962 89.836  140.554 1.00 22.30 ?  135 ALA D CB    1 
ATOM   14460 N  N     . GLN D 2 157 ? 150.030 88.819  143.540 1.00 22.15 ?  136 GLN D N     1 
ATOM   14461 C  CA    . GLN D 2 157 ? 149.650 87.803  144.528 1.00 22.38 ?  136 GLN D CA    1 
ATOM   14462 C  C     . GLN D 2 157 ? 149.149 88.386  145.856 1.00 21.59 ?  136 GLN D C     1 
ATOM   14463 O  O     . GLN D 2 157 ? 148.301 87.784  146.514 1.00 21.44 ?  136 GLN D O     1 
ATOM   14464 C  CB    . GLN D 2 157 ? 150.783 86.789  144.767 1.00 22.94 ?  136 GLN D CB    1 
ATOM   14465 C  CG    . GLN D 2 157 ? 151.254 86.035  143.513 1.00 25.31 ?  136 GLN D CG    1 
ATOM   14466 C  CD    . GLN D 2 157 ? 150.112 85.501  142.643 1.00 28.02 ?  136 GLN D CD    1 
ATOM   14467 O  OE1   . GLN D 2 157 ? 149.091 85.019  143.143 1.00 27.14 ?  136 GLN D OE1   1 
ATOM   14468 N  NE2   . GLN D 2 157 ? 150.295 85.582  141.327 1.00 29.47 ?  136 GLN D NE2   1 
ATOM   14469 N  N     . MET D 2 158 ? 149.670 89.541  146.255 1.00 21.52 ?  137 MET D N     1 
ATOM   14470 C  CA    . MET D 2 158 ? 149.157 90.229  147.453 1.00 22.20 ?  137 MET D CA    1 
ATOM   14471 C  C     . MET D 2 158 ? 147.671 90.581  147.316 1.00 21.84 ?  137 MET D C     1 
ATOM   14472 O  O     . MET D 2 158 ? 146.887 90.368  148.244 1.00 21.91 ?  137 MET D O     1 
ATOM   14473 C  CB    . MET D 2 158 ? 149.961 91.493  147.757 1.00 22.52 ?  137 MET D CB    1 
ATOM   14474 C  CG    . MET D 2 158 ? 151.320 91.221  148.418 1.00 25.81 ?  137 MET D CG    1 
ATOM   14475 S  SD    . MET D 2 158 ? 152.268 92.727  148.766 1.00 31.19 ?  137 MET D SD    1 
ATOM   14476 C  CE    . MET D 2 158 ? 151.158 93.475  149.930 1.00 23.91 ?  137 MET D CE    1 
ATOM   14477 N  N     . ILE D 2 159 ? 147.303 91.115  146.154 1.00 21.41 ?  138 ILE D N     1 
ATOM   14478 C  CA    . ILE D 2 159 ? 145.926 91.511  145.875 1.00 21.51 ?  138 ILE D CA    1 
ATOM   14479 C  C     . ILE D 2 159 ? 145.013 90.276  145.817 1.00 21.77 ?  138 ILE D C     1 
ATOM   14480 O  O     . ILE D 2 159 ? 143.958 90.242  146.471 1.00 21.44 ?  138 ILE D O     1 
ATOM   14481 C  CB    . ILE D 2 159 ? 145.853 92.380  144.560 1.00 21.49 ?  138 ILE D CB    1 
ATOM   14482 C  CG1   . ILE D 2 159 ? 146.651 93.685  144.710 1.00 21.16 ?  138 ILE D CG1   1 
ATOM   14483 C  CG2   . ILE D 2 159 ? 144.407 92.669  144.139 1.00 22.34 ?  138 ILE D CG2   1 
ATOM   14484 C  CD1   . ILE D 2 159 ? 146.141 94.640  145.809 1.00 23.85 ?  138 ILE D CD1   1 
ATOM   14485 N  N     . VAL D 2 160 ? 145.438 89.268  145.046 1.00 21.96 ?  139 VAL D N     1 
ATOM   14486 C  CA    . VAL D 2 160 ? 144.689 88.017  144.854 1.00 22.59 ?  139 VAL D CA    1 
ATOM   14487 C  C     . VAL D 2 160 ? 144.501 87.283  146.189 1.00 22.36 ?  139 VAL D C     1 
ATOM   14488 O  O     . VAL D 2 160 ? 143.440 86.700  146.437 1.00 21.64 ?  139 VAL D O     1 
ATOM   14489 C  CB    . VAL D 2 160 ? 145.384 87.096  143.794 1.00 23.08 ?  139 VAL D CB    1 
ATOM   14490 C  CG1   . VAL D 2 160 ? 144.862 85.647  143.843 1.00 24.33 ?  139 VAL D CG1   1 
ATOM   14491 C  CG2   . VAL D 2 160 ? 145.208 87.673  142.380 1.00 22.87 ?  139 VAL D CG2   1 
ATOM   14492 N  N     . GLY D 2 161 ? 145.529 87.325  147.041 1.00 22.21 ?  140 GLY D N     1 
ATOM   14493 C  CA    . GLY D 2 161 ? 145.455 86.732  148.374 1.00 22.50 ?  140 GLY D CA    1 
ATOM   14494 C  C     . GLY D 2 161 ? 144.297 87.291  149.196 1.00 22.88 ?  140 GLY D C     1 
ATOM   14495 O  O     . GLY D 2 161 ? 143.571 86.534  149.855 1.00 23.54 ?  140 GLY D O     1 
ATOM   14496 N  N     . LEU D 2 162 ? 144.111 88.611  149.151 1.00 22.25 ?  141 LEU D N     1 
ATOM   14497 C  CA    . LEU D 2 162 ? 143.005 89.244  149.874 1.00 22.48 ?  141 LEU D CA    1 
ATOM   14498 C  C     . LEU D 2 162 ? 141.630 88.904  149.291 1.00 22.27 ?  141 LEU D C     1 
ATOM   14499 O  O     . LEU D 2 162 ? 140.666 88.762  150.044 1.00 22.31 ?  141 LEU D O     1 
ATOM   14500 C  CB    . LEU D 2 162 ? 143.210 90.765  150.021 1.00 22.07 ?  141 LEU D CB    1 
ATOM   14501 C  CG    . LEU D 2 162 ? 144.276 91.155  151.068 1.00 22.81 ?  141 LEU D CG    1 
ATOM   14502 C  CD1   . LEU D 2 162 ? 144.818 92.564  150.841 1.00 21.65 ?  141 LEU D CD1   1 
ATOM   14503 C  CD2   . LEU D 2 162 ? 143.794 90.961  152.510 1.00 23.35 ?  141 LEU D CD2   1 
ATOM   14504 N  N     . TYR D 2 163 ? 141.534 88.774  147.966 1.00 22.63 ?  142 TYR D N     1 
ATOM   14505 C  CA    . TYR D 2 163 ? 140.282 88.312  147.333 1.00 23.30 ?  142 TYR D CA    1 
ATOM   14506 C  C     . TYR D 2 163 ? 139.936 86.883  147.734 1.00 23.40 ?  142 TYR D C     1 
ATOM   14507 O  O     . TYR D 2 163 ? 138.778 86.569  147.965 1.00 23.75 ?  142 TYR D O     1 
ATOM   14508 C  CB    . TYR D 2 163 ? 140.364 88.342  145.814 1.00 23.22 ?  142 TYR D CB    1 
ATOM   14509 C  CG    . TYR D 2 163 ? 140.588 89.691  145.188 1.00 24.01 ?  142 TYR D CG    1 
ATOM   14510 C  CD1   . TYR D 2 163 ? 140.255 90.861  145.859 1.00 24.47 ?  142 TYR D CD1   1 
ATOM   14511 C  CD2   . TYR D 2 163 ? 141.129 89.789  143.910 1.00 24.62 ?  142 TYR D CD2   1 
ATOM   14512 C  CE1   . TYR D 2 163 ? 140.460 92.096  145.280 1.00 26.33 ?  142 TYR D CE1   1 
ATOM   14513 C  CE2   . TYR D 2 163 ? 141.327 91.024  143.312 1.00 26.07 ?  142 TYR D CE2   1 
ATOM   14514 C  CZ    . TYR D 2 163 ? 140.984 92.174  144.010 1.00 26.65 ?  142 TYR D CZ    1 
ATOM   14515 O  OH    . TYR D 2 163 ? 141.184 93.411  143.442 1.00 31.13 ?  142 TYR D OH    1 
ATOM   14516 N  N     . LYS D 2 164 ? 140.942 86.021  147.804 1.00 23.70 ?  143 LYS D N     1 
ATOM   14517 C  CA    . LYS D 2 164 ? 140.729 84.620  148.201 1.00 24.47 ?  143 LYS D CA    1 
ATOM   14518 C  C     . LYS D 2 164 ? 140.360 84.449  149.684 1.00 24.55 ?  143 LYS D C     1 
ATOM   14519 O  O     . LYS D 2 164 ? 139.842 83.404  150.084 1.00 24.49 ?  143 LYS D O     1 
ATOM   14520 C  CB    . LYS D 2 164 ? 141.972 83.790  147.872 1.00 24.98 ?  143 LYS D CB    1 
ATOM   14521 C  CG    . LYS D 2 164 ? 142.151 83.467  146.381 1.00 27.10 ?  143 LYS D CG    1 
ATOM   14522 C  CD    . LYS D 2 164 ? 143.344 82.541  146.195 1.00 30.75 ?  143 LYS D CD    1 
ATOM   14523 C  CE    . LYS D 2 164 ? 143.524 82.091  144.746 1.00 32.81 ?  143 LYS D CE    1 
ATOM   14524 N  NZ    . LYS D 2 164 ? 144.779 81.257  144.562 1.00 33.68 1  143 LYS D NZ    1 
ATOM   14525 N  N     . ALA D 2 165 ? 140.638 85.467  150.494 1.00 24.18 ?  144 ALA D N     1 
ATOM   14526 C  CA    . ALA D 2 165 ? 140.397 85.395  151.938 1.00 25.04 ?  144 ALA D CA    1 
ATOM   14527 C  C     . ALA D 2 165 ? 139.017 85.901  152.381 1.00 25.00 ?  144 ALA D C     1 
ATOM   14528 O  O     . ALA D 2 165 ? 138.697 85.854  153.578 1.00 25.50 ?  144 ALA D O     1 
ATOM   14529 C  CB    . ALA D 2 165 ? 141.508 86.131  152.707 1.00 25.02 ?  144 ALA D CB    1 
ATOM   14530 N  N     . ILE D 2 166 ? 138.204 86.386  151.439 1.00 24.60 ?  145 ILE D N     1 
ATOM   14531 C  CA    . ILE D 2 166 ? 136.844 86.817  151.764 1.00 24.40 ?  145 ILE D CA    1 
ATOM   14532 C  C     . ILE D 2 166 ? 136.035 85.610  152.259 1.00 25.75 ?  145 ILE D C     1 
ATOM   14533 O  O     . ILE D 2 166 ? 136.064 84.536  151.648 1.00 25.84 ?  145 ILE D O     1 
ATOM   14534 C  CB    . ILE D 2 166 ? 136.101 87.462  150.560 1.00 24.15 ?  145 ILE D CB    1 
ATOM   14535 C  CG1   . ILE D 2 166 ? 136.947 88.555  149.909 1.00 23.15 ?  145 ILE D CG1   1 
ATOM   14536 C  CG2   . ILE D 2 166 ? 134.754 88.030  151.007 1.00 22.72 ?  145 ILE D CG2   1 
ATOM   14537 C  CD1   . ILE D 2 166 ? 136.389 89.063  148.597 1.00 21.70 ?  145 ILE D CD1   1 
ATOM   14538 N  N     . GLN D 2 167 ? 135.349 85.787  153.381 1.00 26.52 ?  146 GLN D N     1 
ATOM   14539 C  CA    . GLN D 2 167 ? 134.493 84.742  153.926 1.00 28.77 ?  146 GLN D CA    1 
ATOM   14540 C  C     . GLN D 2 167 ? 133.029 85.154  153.847 1.00 29.20 ?  146 GLN D C     1 
ATOM   14541 O  O     . GLN D 2 167 ? 132.688 86.324  154.073 1.00 28.89 ?  146 GLN D O     1 
ATOM   14542 C  CB    . GLN D 2 167 ? 134.877 84.443  155.372 1.00 29.04 ?  146 GLN D CB    1 
ATOM   14543 C  CG    . GLN D 2 167 ? 136.268 83.854  155.514 1.00 31.87 ?  146 GLN D CG    1 
ATOM   14544 C  CD    . GLN D 2 167 ? 137.030 84.473  156.655 1.00 35.35 ?  146 GLN D CD    1 
ATOM   14545 O  OE1   . GLN D 2 167 ? 136.694 84.271  157.825 1.00 36.91 ?  146 GLN D OE1   1 
ATOM   14546 N  NE2   . GLN D 2 167 ? 138.070 85.236  156.325 1.00 36.19 ?  146 GLN D NE2   1 
ATOM   14547 N  N     . LYS D 2 168 ? 132.169 84.189  153.530 1.00 30.29 ?  147 LYS D N     1 
ATOM   14548 C  CA    . LYS D 2 168 ? 130.728 84.432  153.482 1.00 31.24 ?  147 LYS D CA    1 
ATOM   14549 C  C     . LYS D 2 168 ? 130.235 85.100  154.765 1.00 31.73 ?  147 LYS D C     1 
ATOM   14550 O  O     . LYS D 2 168 ? 130.634 84.706  155.861 1.00 31.46 ?  147 LYS D O     1 
ATOM   14551 C  CB    . LYS D 2 168 ? 129.972 83.130  153.229 1.00 31.92 ?  147 LYS D CB    1 
ATOM   14552 C  CG    . LYS D 2 168 ? 128.470 83.320  153.081 1.00 33.23 ?  147 LYS D CG    1 
ATOM   14553 C  CD    . LYS D 2 168 ? 127.788 82.050  152.596 1.00 36.06 ?  147 LYS D CD    1 
ATOM   14554 C  CE    . LYS D 2 168 ? 126.286 82.228  152.522 1.00 35.46 ?  147 LYS D CE    1 
ATOM   14555 N  NZ    . LYS D 2 168 ? 125.880 83.129  151.411 1.00 38.24 1  147 LYS D NZ    1 
ATOM   14556 N  N     . ASP D 2 169 ? 129.388 86.121  154.613 1.00 32.28 ?  148 ASP D N     1 
ATOM   14557 C  CA    . ASP D 2 169 ? 128.812 86.873  155.741 1.00 33.45 ?  148 ASP D CA    1 
ATOM   14558 C  C     . ASP D 2 169 ? 129.821 87.501  156.702 1.00 33.30 ?  148 ASP D C     1 
ATOM   14559 O  O     . ASP D 2 169 ? 129.502 87.745  157.868 1.00 34.32 ?  148 ASP D O     1 
ATOM   14560 C  CB    . ASP D 2 169 ? 127.848 85.993  156.554 1.00 34.63 ?  148 ASP D CB    1 
ATOM   14561 C  CG    . ASP D 2 169 ? 126.540 85.727  155.839 1.00 36.09 ?  148 ASP D CG    1 
ATOM   14562 O  OD1   . ASP D 2 169 ? 126.236 86.392  154.827 1.00 37.80 ?  148 ASP D OD1   1 
ATOM   14563 O  OD2   . ASP D 2 169 ? 125.807 84.835  156.314 1.00 40.47 -1 148 ASP D OD2   1 
ATOM   14564 N  N     . ASP D 2 170 ? 131.037 87.745  156.240 1.00 32.58 ?  149 ASP D N     1 
ATOM   14565 C  CA    . ASP D 2 170 ? 132.011 88.454  157.067 1.00 32.01 ?  149 ASP D CA    1 
ATOM   14566 C  C     . ASP D 2 170 ? 132.403 89.748  156.364 1.00 30.59 ?  149 ASP D C     1 
ATOM   14567 O  O     . ASP D 2 170 ? 133.175 89.739  155.404 1.00 29.11 ?  149 ASP D O     1 
ATOM   14568 C  CB    . ASP D 2 170 ? 133.227 87.576  157.374 1.00 32.93 ?  149 ASP D CB    1 
ATOM   14569 C  CG    . ASP D 2 170 ? 134.371 88.348  158.019 1.00 35.05 ?  149 ASP D CG    1 
ATOM   14570 O  OD1   . ASP D 2 170 ? 134.137 89.352  158.727 1.00 39.25 ?  149 ASP D OD1   1 
ATOM   14571 O  OD2   . ASP D 2 170 ? 135.522 87.935  157.830 1.00 39.22 -1 149 ASP D OD2   1 
ATOM   14572 N  N     . GLU D 2 171 ? 131.847 90.852  156.856 1.00 29.34 ?  150 GLU D N     1 
ATOM   14573 C  CA    . GLU D 2 171 ? 132.037 92.161  156.238 1.00 28.51 ?  150 GLU D CA    1 
ATOM   14574 C  C     . GLU D 2 171 ? 133.449 92.730  156.433 1.00 27.27 ?  150 GLU D C     1 
ATOM   14575 O  O     . GLU D 2 171 ? 133.881 93.567  155.657 1.00 26.62 ?  150 GLU D O     1 
ATOM   14576 C  CB    . GLU D 2 171 ? 130.965 93.147  156.721 1.00 29.09 ?  150 GLU D CB    1 
ATOM   14577 C  CG    . GLU D 2 171 ? 131.075 93.572  158.184 1.00 30.68 ?  150 GLU D CG    1 
ATOM   14578 C  CD    . GLU D 2 171 ? 129.885 94.400  158.641 1.00 33.92 ?  150 GLU D CD    1 
ATOM   14579 O  OE1   . GLU D 2 171 ? 128.993 94.680  157.803 1.00 36.31 ?  150 GLU D OE1   1 
ATOM   14580 O  OE2   . GLU D 2 171 ? 129.833 94.782  159.830 1.00 34.02 -1 150 GLU D OE2   1 
ATOM   14581 N  N     . ILE D 2 172 ? 134.168 92.256  157.450 1.00 26.19 ?  151 ILE D N     1 
ATOM   14582 C  CA    . ILE D 2 172 ? 135.547 92.689  157.675 1.00 25.49 ?  151 ILE D CA    1 
ATOM   14583 C  C     . ILE D 2 172 ? 136.459 92.187  156.552 1.00 24.61 ?  151 ILE D C     1 
ATOM   14584 O  O     . ILE D 2 172 ? 137.238 92.960  155.980 1.00 24.09 ?  151 ILE D O     1 
ATOM   14585 C  CB    . ILE D 2 172 ? 136.075 92.260  159.073 1.00 25.98 ?  151 ILE D CB    1 
ATOM   14586 C  CG1   . ILE D 2 172 ? 135.269 92.930  160.188 1.00 26.86 ?  151 ILE D CG1   1 
ATOM   14587 C  CG2   . ILE D 2 172 ? 137.590 92.550  159.245 1.00 26.50 ?  151 ILE D CG2   1 
ATOM   14588 C  CD1   . ILE D 2 172 ? 135.325 94.451  160.177 1.00 27.81 ?  151 ILE D CD1   1 
ATOM   14589 N  N     . SER D 2 173 ? 136.339 90.903  156.227 1.00 23.71 ?  152 SER D N     1 
ATOM   14590 C  CA    . SER D 2 173 ? 137.124 90.307  155.148 1.00 23.38 ?  152 SER D CA    1 
ATOM   14591 C  C     . SER D 2 173 ? 136.729 90.900  153.783 1.00 22.41 ?  152 SER D C     1 
ATOM   14592 O  O     . SER D 2 173 ? 137.571 91.065  152.896 1.00 21.43 ?  152 SER D O     1 
ATOM   14593 C  CB    . SER D 2 173 ? 137.002 88.777  155.155 1.00 23.90 ?  152 SER D CB    1 
ATOM   14594 O  OG    . SER D 2 173 ? 135.714 88.313  154.754 1.00 23.74 ?  152 SER D OG    1 
ATOM   14595 N  N     . LEU D 2 174 ? 135.452 91.237  153.631 1.00 21.63 ?  153 LEU D N     1 
ATOM   14596 C  CA    . LEU D 2 174 ? 134.993 91.893  152.404 1.00 20.75 ?  153 LEU D CA    1 
ATOM   14597 C  C     . LEU D 2 174 ? 135.630 93.276  152.284 1.00 20.96 ?  153 LEU D C     1 
ATOM   14598 O  O     . LEU D 2 174 ? 136.107 93.653  151.214 1.00 20.41 ?  153 LEU D O     1 
ATOM   14599 C  CB    . LEU D 2 174 ? 133.455 91.994  152.362 1.00 20.62 ?  153 LEU D CB    1 
ATOM   14600 C  CG    . LEU D 2 174 ? 132.842 92.703  151.136 1.00 19.55 ?  153 LEU D CG    1 
ATOM   14601 C  CD1   . LEU D 2 174 ? 133.356 92.082  149.831 1.00 20.44 ?  153 LEU D CD1   1 
ATOM   14602 C  CD2   . LEU D 2 174 ? 131.309 92.651  151.210 1.00 20.99 ?  153 LEU D CD2   1 
ATOM   14603 N  N     . PHE D 2 175 ? 135.640 94.026  153.386 1.00 21.07 ?  154 PHE D N     1 
ATOM   14604 C  CA    . PHE D 2 175 ? 136.238 95.359  153.398 1.00 21.32 ?  154 PHE D CA    1 
ATOM   14605 C  C     . PHE D 2 175 ? 137.717 95.315  152.996 1.00 21.08 ?  154 PHE D C     1 
ATOM   14606 O  O     . PHE D 2 175 ? 138.176 96.127  152.191 1.00 20.85 ?  154 PHE D O     1 
ATOM   14607 C  CB    . PHE D 2 175 ? 136.087 96.003  154.781 1.00 21.20 ?  154 PHE D CB    1 
ATOM   14608 C  CG    . PHE D 2 175 ? 136.902 97.249  154.962 1.00 22.46 ?  154 PHE D CG    1 
ATOM   14609 C  CD1   . PHE D 2 175 ? 136.361 98.497  154.656 1.00 21.21 ?  154 PHE D CD1   1 
ATOM   14610 C  CD2   . PHE D 2 175 ? 138.211 97.185  155.447 1.00 22.53 ?  154 PHE D CD2   1 
ATOM   14611 C  CE1   . PHE D 2 175 ? 137.098 99.651  154.830 1.00 22.11 ?  154 PHE D CE1   1 
ATOM   14612 C  CE2   . PHE D 2 175 ? 138.969 98.341  155.608 1.00 23.26 ?  154 PHE D CE2   1 
ATOM   14613 C  CZ    . PHE D 2 175 ? 138.411 99.579  155.305 1.00 22.08 ?  154 PHE D CZ    1 
ATOM   14614 N  N     . LYS D 2 176 ? 138.456 94.371  153.571 1.00 21.14 ?  155 LYS D N     1 
ATOM   14615 C  CA    . LYS D 2 176 ? 139.878 94.205  153.256 1.00 20.93 ?  155 LYS D CA    1 
ATOM   14616 C  C     . LYS D 2 176 ? 140.115 93.947  151.770 1.00 20.61 ?  155 LYS D C     1 
ATOM   14617 O  O     . LYS D 2 176 ? 141.034 94.513  151.168 1.00 20.62 ?  155 LYS D O     1 
ATOM   14618 C  CB    . LYS D 2 176 ? 140.466 93.083  154.097 1.00 21.27 ?  155 LYS D CB    1 
ATOM   14619 C  CG    . LYS D 2 176 ? 140.633 93.486  155.536 1.00 22.04 ?  155 LYS D CG    1 
ATOM   14620 C  CD    . LYS D 2 176 ? 141.121 92.345  156.413 1.00 25.24 ?  155 LYS D CD    1 
ATOM   14621 C  CE    . LYS D 2 176 ? 141.321 92.853  157.818 1.00 25.83 ?  155 LYS D CE    1 
ATOM   14622 N  NZ    . LYS D 2 176 ? 141.819 91.801  158.752 1.00 26.64 1  155 LYS D NZ    1 
ATOM   14623 N  N     . ALA D 2 177 ? 139.264 93.114  151.181 1.00 20.02 ?  156 ALA D N     1 
ATOM   14624 C  CA    . ALA D 2 177 ? 139.311 92.862  149.742 1.00 19.86 ?  156 ALA D CA    1 
ATOM   14625 C  C     . ALA D 2 177 ? 138.961 94.113  148.924 1.00 19.61 ?  156 ALA D C     1 
ATOM   14626 O  O     . ALA D 2 177 ? 139.515 94.339  147.846 1.00 19.69 ?  156 ALA D O     1 
ATOM   14627 C  CB    . ALA D 2 177 ? 138.382 91.743  149.405 1.00 19.99 ?  156 ALA D CB    1 
ATOM   14628 N  N     . MET D 2 178 ? 138.032 94.920  149.432 1.00 19.75 ?  157 MET D N     1 
ATOM   14629 C  CA    . MET D 2 178 ? 137.626 96.156  148.731 1.00 18.89 ?  157 MET D CA    1 
ATOM   14630 C  C     . MET D 2 178 ? 138.767 97.162  148.736 1.00 18.62 ?  157 MET D C     1 
ATOM   14631 O  O     . MET D 2 178 ? 139.005 97.848  147.735 1.00 18.10 ?  157 MET D O     1 
ATOM   14632 C  CB    . MET D 2 178 ? 136.381 96.763  149.370 1.00 18.82 ?  157 MET D CB    1 
ATOM   14633 C  CG    . MET D 2 178 ? 135.107 96.002  149.044 1.00 20.20 ?  157 MET D CG    1 
ATOM   14634 S  SD    . MET D 2 178 ? 133.721 96.693  149.957 1.00 23.78 ?  157 MET D SD    1 
ATOM   14635 C  CE    . MET D 2 178 ? 132.370 95.796  149.198 1.00 22.62 ?  157 MET D CE    1 
ATOM   14636 N  N     . VAL D 2 179 ? 139.481 97.222  149.861 1.00 18.34 ?  158 VAL D N     1 
ATOM   14637 C  CA    . VAL D 2 179 ? 140.673 98.049  149.978 1.00 18.75 ?  158 VAL D CA    1 
ATOM   14638 C  C     . VAL D 2 179 ? 141.712 97.627  148.947 1.00 18.86 ?  158 VAL D C     1 
ATOM   14639 O  O     . VAL D 2 179 ? 142.283 98.487  148.254 1.00 18.79 ?  158 VAL D O     1 
ATOM   14640 C  CB    . VAL D 2 179 ? 141.294 98.008  151.400 1.00 19.02 ?  158 VAL D CB    1 
ATOM   14641 C  CG1   . VAL D 2 179 ? 142.660 98.709  151.401 1.00 19.10 ?  158 VAL D CG1   1 
ATOM   14642 C  CG2   . VAL D 2 179 ? 140.346 98.647  152.427 1.00 18.94 ?  158 VAL D CG2   1 
ATOM   14643 N  N     . ALA D 2 180 ? 141.958 96.314  148.861 1.00 18.96 ?  159 ALA D N     1 
ATOM   14644 C  CA    . ALA D 2 180 ? 142.853 95.755  147.846 1.00 19.05 ?  159 ALA D CA    1 
ATOM   14645 C  C     . ALA D 2 180 ? 142.399 96.143  146.437 1.00 18.67 ?  159 ALA D C     1 
ATOM   14646 O  O     . ALA D 2 180 ? 143.216 96.571  145.612 1.00 17.72 ?  159 ALA D O     1 
ATOM   14647 C  CB    . ALA D 2 180 ? 142.950 94.225  147.983 1.00 19.43 ?  159 ALA D CB    1 
ATOM   14648 N  N     . SER D 2 181 ? 141.092 96.024  146.181 1.00 18.49 ?  160 SER D N     1 
ATOM   14649 C  CA    . SER D 2 181 ? 140.537 96.381  144.875 1.00 18.51 ?  160 SER D CA    1 
ATOM   14650 C  C     . SER D 2 181 ? 140.728 97.860  144.541 1.00 18.23 ?  160 SER D C     1 
ATOM   14651 O  O     . SER D 2 181 ? 141.154 98.201  143.446 1.00 18.18 ?  160 SER D O     1 
ATOM   14652 C  CB    . SER D 2 181 ? 139.052 96.017  144.784 1.00 18.51 ?  160 SER D CB    1 
ATOM   14653 O  OG    . SER D 2 181 ? 138.603 96.219  143.458 1.00 19.42 ?  160 SER D OG    1 
ATOM   14654 N  N     . VAL D 2 182 ? 140.419 98.735  145.496 1.00 18.43 ?  161 VAL D N     1 
ATOM   14655 C  CA    . VAL D 2 182 ? 140.642 100.172 145.304 1.00 18.09 ?  161 VAL D CA    1 
ATOM   14656 C  C     . VAL D 2 182 ? 142.124 100.475 145.058 1.00 18.41 ?  161 VAL D C     1 
ATOM   14657 O  O     . VAL D 2 182 ? 142.460 101.269 144.177 1.00 18.52 ?  161 VAL D O     1 
ATOM   14658 C  CB    . VAL D 2 182 ? 140.090 101.000 146.470 1.00 17.71 ?  161 VAL D CB    1 
ATOM   14659 C  CG1   . VAL D 2 182 ? 140.523 102.481 146.350 1.00 16.02 ?  161 VAL D CG1   1 
ATOM   14660 C  CG2   . VAL D 2 182 ? 138.558 100.893 146.491 1.00 17.78 ?  161 VAL D CG2   1 
ATOM   14661 N  N     . TYR D 2 183 ? 143.007 99.807  145.803 1.00 19.06 ?  162 TYR D N     1 
ATOM   14662 C  CA    . TYR D 2 183 ? 144.438 100.003 145.591 1.00 19.73 ?  162 TYR D CA    1 
ATOM   14663 C  C     . TYR D 2 183 ? 144.859 99.581  144.190 1.00 19.90 ?  162 TYR D C     1 
ATOM   14664 O  O     . TYR D 2 183 ? 145.716 100.216 143.599 1.00 20.73 ?  162 TYR D O     1 
ATOM   14665 C  CB    . TYR D 2 183 ? 145.300 99.307  146.660 1.00 19.84 ?  162 TYR D CB    1 
ATOM   14666 C  CG    . TYR D 2 183 ? 145.276 99.977  148.018 1.00 20.24 ?  162 TYR D CG    1 
ATOM   14667 C  CD1   . TYR D 2 183 ? 144.745 101.254 148.182 1.00 21.51 ?  162 TYR D CD1   1 
ATOM   14668 C  CD2   . TYR D 2 183 ? 145.807 99.337  149.145 1.00 20.45 ?  162 TYR D CD2   1 
ATOM   14669 C  CE1   . TYR D 2 183 ? 144.730 101.876 149.437 1.00 21.68 ?  162 TYR D CE1   1 
ATOM   14670 C  CE2   . TYR D 2 183 ? 145.816 99.960  150.400 1.00 19.97 ?  162 TYR D CE2   1 
ATOM   14671 C  CZ    . TYR D 2 183 ? 145.271 101.225 150.536 1.00 21.83 ?  162 TYR D CZ    1 
ATOM   14672 O  OH    . TYR D 2 183 ? 145.263 101.846 151.770 1.00 21.96 ?  162 TYR D OH    1 
ATOM   14673 N  N     . LEU D 2 184 ? 144.251 98.534  143.649 1.00 20.22 ?  163 LEU D N     1 
ATOM   14674 C  CA    . LEU D 2 184 ? 144.582 98.123  142.288 1.00 20.89 ?  163 LEU D CA    1 
ATOM   14675 C  C     . LEU D 2 184 ? 144.049 99.151  141.279 1.00 20.72 ?  163 LEU D C     1 
ATOM   14676 O  O     . LEU D 2 184 ? 144.810 99.679  140.474 1.00 21.07 ?  163 LEU D O     1 
ATOM   14677 C  CB    . LEU D 2 184 ? 144.097 96.689  141.993 1.00 21.16 ?  163 LEU D CB    1 
ATOM   14678 C  CG    . LEU D 2 184 ? 144.317 96.094  140.587 1.00 22.77 ?  163 LEU D CG    1 
ATOM   14679 C  CD1   . LEU D 2 184 ? 145.782 96.208  140.110 1.00 22.44 ?  163 LEU D CD1   1 
ATOM   14680 C  CD2   . LEU D 2 184 ? 143.857 94.647  140.522 1.00 24.75 ?  163 LEU D CD2   1 
ATOM   14681 N  N     . GLU D 2 185 ? 142.755 99.455  141.362 1.00 20.65 ?  164 GLU D N     1 
ATOM   14682 C  CA    . GLU D 2 185 ? 142.089 100.376 140.430 1.00 20.69 ?  164 GLU D CA    1 
ATOM   14683 C  C     . GLU D 2 185 ? 142.652 101.798 140.431 1.00 20.64 ?  164 GLU D C     1 
ATOM   14684 O  O     . GLU D 2 185 ? 142.769 102.431 139.372 1.00 20.25 ?  164 GLU D O     1 
ATOM   14685 C  CB    . GLU D 2 185 ? 140.587 100.457 140.742 1.00 21.03 ?  164 GLU D CB    1 
ATOM   14686 C  CG    . GLU D 2 185 ? 139.840 99.121  140.673 1.00 22.19 ?  164 GLU D CG    1 
ATOM   14687 C  CD    . GLU D 2 185 ? 139.410 98.724  139.263 1.00 24.19 ?  164 GLU D CD    1 
ATOM   14688 O  OE1   . GLU D 2 185 ? 139.751 99.408  138.281 1.00 27.97 ?  164 GLU D OE1   1 
ATOM   14689 O  OE2   . GLU D 2 185 ? 138.699 97.727  139.129 1.00 25.47 -1 164 GLU D OE2   1 
ATOM   14690 N  N     . SER D 2 186 ? 142.967 102.304 141.619 1.00 20.42 ?  165 SER D N     1 
ATOM   14691 C  CA    . SER D 2 186 ? 143.276 103.723 141.793 1.00 20.70 ?  165 SER D CA    1 
ATOM   14692 C  C     . SER D 2 186 ? 144.749 104.012 142.080 1.00 20.88 ?  165 SER D C     1 
ATOM   14693 O  O     . SER D 2 186 ? 145.127 105.171 142.250 1.00 21.21 ?  165 SER D O     1 
ATOM   14694 C  CB    . SER D 2 186 ? 142.408 104.331 142.909 1.00 21.25 ?  165 SER D CB    1 
ATOM   14695 O  OG    . SER D 2 186 ? 141.026 104.068 142.709 1.00 20.97 ?  165 SER D OG    1 
ATOM   14696 N  N     . PHE D 2 187 ? 145.588 102.977 142.127 1.00 20.94 ?  166 PHE D N     1 
ATOM   14697 C  CA    . PHE D 2 187 ? 146.961 103.176 142.570 1.00 21.19 ?  166 PHE D CA    1 
ATOM   14698 C  C     . PHE D 2 187 ? 147.952 102.292 141.815 1.00 21.22 ?  166 PHE D C     1 
ATOM   14699 O  O     . PHE D 2 187 ? 148.813 102.824 141.105 1.00 21.10 ?  166 PHE D O     1 
ATOM   14700 C  CB    . PHE D 2 187 ? 147.039 103.059 144.118 1.00 21.63 ?  166 PHE D CB    1 
ATOM   14701 C  CG    . PHE D 2 187 ? 148.411 102.767 144.670 1.00 24.05 ?  166 PHE D CG    1 
ATOM   14702 C  CD1   . PHE D 2 187 ? 149.485 103.624 144.431 1.00 25.52 ?  166 PHE D CD1   1 
ATOM   14703 C  CD2   . PHE D 2 187 ? 148.616 101.651 145.477 1.00 27.03 ?  166 PHE D CD2   1 
ATOM   14704 C  CE1   . PHE D 2 187 ? 150.738 103.357 144.965 1.00 26.73 ?  166 PHE D CE1   1 
ATOM   14705 C  CE2   . PHE D 2 187 ? 149.884 101.373 146.009 1.00 27.36 ?  166 PHE D CE2   1 
ATOM   14706 C  CZ    . PHE D 2 187 ? 150.937 102.226 145.748 1.00 27.87 ?  166 PHE D CZ    1 
ATOM   14707 N  N     . LEU D 2 188 ? 147.803 100.974 141.915 1.00 20.78 ?  167 LEU D N     1 
ATOM   14708 C  CA    . LEU D 2 188 ? 148.779 100.035 141.325 1.00 21.78 ?  167 LEU D CA    1 
ATOM   14709 C  C     . LEU D 2 188 ? 148.894 100.093 139.796 1.00 21.91 ?  167 LEU D C     1 
ATOM   14710 O  O     . LEU D 2 188 ? 149.975 99.863  139.254 1.00 22.87 ?  167 LEU D O     1 
ATOM   14711 C  CB    . LEU D 2 188 ? 148.492 98.599  141.761 1.00 22.32 ?  167 LEU D CB    1 
ATOM   14712 C  CG    . LEU D 2 188 ? 148.666 98.187  143.222 1.00 23.33 ?  167 LEU D CG    1 
ATOM   14713 C  CD1   . LEU D 2 188 ? 148.288 96.723  143.362 1.00 22.43 ?  167 LEU D CD1   1 
ATOM   14714 C  CD2   . LEU D 2 188 ? 150.088 98.431  143.743 1.00 25.71 ?  167 LEU D CD2   1 
ATOM   14715 N  N     . PHE D 2 189 ? 147.787 100.375 139.107 1.00 21.56 ?  168 PHE D N     1 
ATOM   14716 C  CA    . PHE D 2 189 ? 147.798 100.528 137.649 1.00 21.86 ?  168 PHE D CA    1 
ATOM   14717 C  C     . PHE D 2 189 ? 148.659 101.720 137.181 1.00 21.87 ?  168 PHE D C     1 
ATOM   14718 O  O     . PHE D 2 189 ? 149.125 101.749 136.039 1.00 21.79 ?  168 PHE D O     1 
ATOM   14719 C  CB    . PHE D 2 189 ? 146.374 100.738 137.103 1.00 21.79 ?  168 PHE D CB    1 
ATOM   14720 C  CG    . PHE D 2 189 ? 145.557 99.474  136.971 1.00 21.88 ?  168 PHE D CG    1 
ATOM   14721 C  CD1   . PHE D 2 189 ? 146.131 98.277  136.539 1.00 21.44 ?  168 PHE D CD1   1 
ATOM   14722 C  CD2   . PHE D 2 189 ? 144.190 99.499  137.251 1.00 22.82 ?  168 PHE D CD2   1 
ATOM   14723 C  CE1   . PHE D 2 189 ? 145.360 97.114  136.414 1.00 22.35 ?  168 PHE D CE1   1 
ATOM   14724 C  CE2   . PHE D 2 189 ? 143.406 98.350  137.129 1.00 22.08 ?  168 PHE D CE2   1 
ATOM   14725 C  CZ    . PHE D 2 189 ? 143.994 97.150  136.721 1.00 22.60 ?  168 PHE D CZ    1 
ATOM   14726 N  N     . TYR D 2 190 ? 148.849 102.710 138.048 1.00 21.91 ?  169 TYR D N     1 
ATOM   14727 C  CA    . TYR D 2 190 ? 149.384 104.000 137.587 1.00 22.52 ?  169 TYR D CA    1 
ATOM   14728 C  C     . TYR D 2 190 ? 150.888 104.046 137.317 1.00 22.75 ?  169 TYR D C     1 
ATOM   14729 O  O     . TYR D 2 190 ? 151.323 104.846 136.500 1.00 21.93 ?  169 TYR D O     1 
ATOM   14730 C  CB    . TYR D 2 190 ? 148.903 105.157 138.468 1.00 22.67 ?  169 TYR D CB    1 
ATOM   14731 C  CG    . TYR D 2 190 ? 147.459 105.496 138.162 1.00 24.77 ?  169 TYR D CG    1 
ATOM   14732 C  CD1   . TYR D 2 190 ? 146.415 104.683 138.616 1.00 25.65 ?  169 TYR D CD1   1 
ATOM   14733 C  CD2   . TYR D 2 190 ? 147.139 106.601 137.377 1.00 25.94 ?  169 TYR D CD2   1 
ATOM   14734 C  CE1   . TYR D 2 190 ? 145.084 104.980 138.304 1.00 26.62 ?  169 TYR D CE1   1 
ATOM   14735 C  CE2   . TYR D 2 190 ? 145.815 106.915 137.075 1.00 26.91 ?  169 TYR D CE2   1 
ATOM   14736 C  CZ    . TYR D 2 190 ? 144.797 106.102 137.536 1.00 27.39 ?  169 TYR D CZ    1 
ATOM   14737 O  OH    . TYR D 2 190 ? 143.491 106.427 137.219 1.00 27.50 ?  169 TYR D OH    1 
ATOM   14738 N  N     . SER D 2 191 ? 151.668 103.174 137.964 1.00 22.74 ?  170 SER D N     1 
ATOM   14739 C  CA    . SER D 2 191 ? 153.078 103.015 137.585 1.00 23.43 ?  170 SER D CA    1 
ATOM   14740 C  C     . SER D 2 191 ? 153.157 102.534 136.136 1.00 23.08 ?  170 SER D C     1 
ATOM   14741 O  O     . SER D 2 191 ? 154.105 102.829 135.430 1.00 23.67 ?  170 SER D O     1 
ATOM   14742 C  CB    . SER D 2 191 ? 153.821 102.044 138.516 1.00 23.39 ?  170 SER D CB    1 
ATOM   14743 O  OG    . SER D 2 191 ? 153.255 100.742 138.471 1.00 24.10 ?  170 SER D OG    1 
ATOM   14744 N  N     . GLY D 2 192 ? 152.125 101.825 135.697 1.00 22.82 ?  171 GLY D N     1 
ATOM   14745 C  CA    . GLY D 2 192 ? 152.021 101.348 134.323 1.00 22.08 ?  171 GLY D CA    1 
ATOM   14746 C  C     . GLY D 2 192 ? 151.437 102.374 133.366 1.00 22.12 ?  171 GLY D C     1 
ATOM   14747 O  O     . GLY D 2 192 ? 152.015 102.631 132.308 1.00 22.86 ?  171 GLY D O     1 
ATOM   14748 N  N     . PHE D 2 193 ? 150.300 102.963 133.731 1.00 21.48 ?  172 PHE D N     1 
ATOM   14749 C  CA    . PHE D 2 193 ? 149.641 103.987 132.898 1.00 21.06 ?  172 PHE D CA    1 
ATOM   14750 C  C     . PHE D 2 193 ? 150.574 105.147 132.552 1.00 21.13 ?  172 PHE D C     1 
ATOM   14751 O  O     . PHE D 2 193 ? 150.416 105.774 131.503 1.00 21.18 ?  172 PHE D O     1 
ATOM   14752 C  CB    . PHE D 2 193 ? 148.407 104.556 133.597 1.00 21.33 ?  172 PHE D CB    1 
ATOM   14753 C  CG    . PHE D 2 193 ? 147.230 103.610 133.666 1.00 20.93 ?  172 PHE D CG    1 
ATOM   14754 C  CD1   . PHE D 2 193 ? 147.011 102.646 132.683 1.00 20.88 ?  172 PHE D CD1   1 
ATOM   14755 C  CD2   . PHE D 2 193 ? 146.310 103.730 134.699 1.00 19.83 ?  172 PHE D CD2   1 
ATOM   14756 C  CE1   . PHE D 2 193 ? 145.902 101.793 132.759 1.00 22.31 ?  172 PHE D CE1   1 
ATOM   14757 C  CE2   . PHE D 2 193 ? 145.193 102.891 134.774 1.00 20.67 ?  172 PHE D CE2   1 
ATOM   14758 C  CZ    . PHE D 2 193 ? 144.990 101.922 133.802 1.00 21.00 ?  172 PHE D CZ    1 
ATOM   14759 N  N     . TYR D 2 194 ? 151.546 105.419 133.425 1.00 20.48 ?  173 TYR D N     1 
ATOM   14760 C  CA    . TYR D 2 194 ? 152.467 106.538 133.236 1.00 20.76 ?  173 TYR D CA    1 
ATOM   14761 C  C     . TYR D 2 194 ? 153.041 106.579 131.816 1.00 20.53 ?  173 TYR D C     1 
ATOM   14762 O  O     . TYR D 2 194 ? 153.010 107.611 131.139 1.00 19.89 ?  173 TYR D O     1 
ATOM   14763 C  CB    . TYR D 2 194 ? 153.614 106.504 134.277 1.00 20.94 ?  173 TYR D CB    1 
ATOM   14764 C  CG    . TYR D 2 194 ? 154.453 107.769 134.259 1.00 21.56 ?  173 TYR D CG    1 
ATOM   14765 C  CD1   . TYR D 2 194 ? 154.244 108.783 135.196 1.00 22.23 ?  173 TYR D CD1   1 
ATOM   14766 C  CD2   . TYR D 2 194 ? 155.443 107.964 133.288 1.00 22.00 ?  173 TYR D CD2   1 
ATOM   14767 C  CE1   . TYR D 2 194 ? 154.996 109.956 135.168 1.00 21.58 ?  173 TYR D CE1   1 
ATOM   14768 C  CE2   . TYR D 2 194 ? 156.199 109.121 133.258 1.00 20.52 ?  173 TYR D CE2   1 
ATOM   14769 C  CZ    . TYR D 2 194 ? 155.971 110.113 134.196 1.00 21.66 ?  173 TYR D CZ    1 
ATOM   14770 O  OH    . TYR D 2 194 ? 156.705 111.274 134.148 1.00 21.37 ?  173 TYR D OH    1 
ATOM   14771 N  N     . TYR D 2 195 ? 153.535 105.443 131.354 1.00 20.77 ?  174 TYR D N     1 
ATOM   14772 C  CA    . TYR D 2 195 ? 154.291 105.428 130.113 1.00 21.12 ?  174 TYR D CA    1 
ATOM   14773 C  C     . TYR D 2 195 ? 153.429 105.716 128.871 1.00 21.49 ?  174 TYR D C     1 
ATOM   14774 O  O     . TYR D 2 195 ? 153.783 106.603 128.089 1.00 21.60 ?  174 TYR D O     1 
ATOM   14775 C  CB    . TYR D 2 195 ? 155.113 104.141 130.005 1.00 21.23 ?  174 TYR D CB    1 
ATOM   14776 C  CG    . TYR D 2 195 ? 156.403 104.271 129.226 1.00 21.77 ?  174 TYR D CG    1 
ATOM   14777 C  CD1   . TYR D 2 195 ? 157.198 105.418 129.319 1.00 23.28 ?  174 TYR D CD1   1 
ATOM   14778 C  CD2   . TYR D 2 195 ? 156.841 103.230 128.409 1.00 22.87 ?  174 TYR D CD2   1 
ATOM   14779 C  CE1   . TYR D 2 195 ? 158.395 105.522 128.595 1.00 23.81 ?  174 TYR D CE1   1 
ATOM   14780 C  CE2   . TYR D 2 195 ? 158.034 103.325 127.696 1.00 24.09 ?  174 TYR D CE2   1 
ATOM   14781 C  CZ    . TYR D 2 195 ? 158.799 104.469 127.788 1.00 23.51 ?  174 TYR D CZ    1 
ATOM   14782 O  OH    . TYR D 2 195 ? 159.975 104.560 127.070 1.00 25.36 ?  174 TYR D OH    1 
ATOM   14783 N  N     . PRO D 2 196 ? 152.296 104.990 128.687 1.00 21.86 ?  175 PRO D N     1 
ATOM   14784 C  CA    . PRO D 2 196 ? 151.393 105.331 127.577 1.00 22.03 ?  175 PRO D CA    1 
ATOM   14785 C  C     . PRO D 2 196 ? 150.916 106.782 127.622 1.00 22.18 ?  175 PRO D C     1 
ATOM   14786 O  O     . PRO D 2 196 ? 150.809 107.413 126.567 1.00 23.00 ?  175 PRO D O     1 
ATOM   14787 C  CB    . PRO D 2 196 ? 150.197 104.389 127.773 1.00 21.50 ?  175 PRO D CB    1 
ATOM   14788 C  CG    . PRO D 2 196 ? 150.691 103.289 128.572 1.00 22.47 ?  175 PRO D CG    1 
ATOM   14789 C  CD    . PRO D 2 196 ? 151.916 103.717 129.325 1.00 20.91 ?  175 PRO D CD    1 
ATOM   14790 N  N     . LEU D 2 197 ? 150.645 107.308 128.818 1.00 21.70 ?  176 LEU D N     1 
ATOM   14791 C  CA    . LEU D 2 197 ? 150.259 108.719 128.966 1.00 22.40 ?  176 LEU D CA    1 
ATOM   14792 C  C     . LEU D 2 197 ? 151.392 109.678 128.596 1.00 22.58 ?  176 LEU D C     1 
ATOM   14793 O  O     . LEU D 2 197 ? 151.149 110.741 128.009 1.00 22.15 ?  176 LEU D O     1 
ATOM   14794 C  CB    . LEU D 2 197 ? 149.801 109.016 130.388 1.00 22.15 ?  176 LEU D CB    1 
ATOM   14795 C  CG    . LEU D 2 197 ? 148.461 108.455 130.880 1.00 23.08 ?  176 LEU D CG    1 
ATOM   14796 C  CD1   . LEU D 2 197 ? 148.417 108.581 132.393 1.00 21.62 ?  176 LEU D CD1   1 
ATOM   14797 C  CD2   . LEU D 2 197 ? 147.273 109.187 130.222 1.00 21.94 ?  176 LEU D CD2   1 
ATOM   14798 N  N     . TYR D 2 198 ? 152.619 109.291 128.955 1.00 22.76 ?  177 TYR D N     1 
ATOM   14799 C  CA    . TYR D 2 198 ? 153.833 110.030 128.606 1.00 23.23 ?  177 TYR D CA    1 
ATOM   14800 C  C     . TYR D 2 198 ? 154.005 110.123 127.090 1.00 23.91 ?  177 TYR D C     1 
ATOM   14801 O  O     . TYR D 2 198 ? 154.265 111.212 126.556 1.00 24.20 ?  177 TYR D O     1 
ATOM   14802 C  CB    . TYR D 2 198 ? 155.057 109.384 129.277 1.00 23.19 ?  177 TYR D CB    1 
ATOM   14803 C  CG    . TYR D 2 198 ? 156.386 110.075 129.034 1.00 23.52 ?  177 TYR D CG    1 
ATOM   14804 C  CD1   . TYR D 2 198 ? 156.639 111.339 129.548 1.00 24.85 ?  177 TYR D CD1   1 
ATOM   14805 C  CD2   . TYR D 2 198 ? 157.409 109.434 128.324 1.00 25.30 ?  177 TYR D CD2   1 
ATOM   14806 C  CE1   . TYR D 2 198 ? 157.868 111.971 129.345 1.00 26.05 ?  177 TYR D CE1   1 
ATOM   14807 C  CE2   . TYR D 2 198 ? 158.651 110.059 128.117 1.00 26.38 ?  177 TYR D CE2   1 
ATOM   14808 C  CZ    . TYR D 2 198 ? 158.864 111.323 128.633 1.00 26.68 ?  177 TYR D CZ    1 
ATOM   14809 O  OH    . TYR D 2 198 ? 160.073 111.957 128.448 1.00 30.01 ?  177 TYR D OH    1 
ATOM   14810 N  N     . PHE D 2 199 ? 153.852 109.000 126.388 1.00 24.84 ?  178 PHE D N     1 
ATOM   14811 C  CA    . PHE D 2 199 ? 153.873 109.036 124.922 1.00 25.81 ?  178 PHE D CA    1 
ATOM   14812 C  C     . PHE D 2 199 ? 152.712 109.823 124.327 1.00 26.23 ?  178 PHE D C     1 
ATOM   14813 O  O     . PHE D 2 199 ? 152.907 110.634 123.421 1.00 26.58 ?  178 PHE D O     1 
ATOM   14814 C  CB    . PHE D 2 199 ? 153.921 107.633 124.330 1.00 26.08 ?  178 PHE D CB    1 
ATOM   14815 C  CG    . PHE D 2 199 ? 155.269 106.985 124.435 1.00 28.71 ?  178 PHE D CG    1 
ATOM   14816 C  CD1   . PHE D 2 199 ? 156.420 107.686 124.097 1.00 32.03 ?  178 PHE D CD1   1 
ATOM   14817 C  CD2   . PHE D 2 199 ? 155.396 105.679 124.876 1.00 31.77 ?  178 PHE D CD2   1 
ATOM   14818 C  CE1   . PHE D 2 199 ? 157.688 107.094 124.203 1.00 32.29 ?  178 PHE D CE1   1 
ATOM   14819 C  CE2   . PHE D 2 199 ? 156.656 105.079 124.976 1.00 32.72 ?  178 PHE D CE2   1 
ATOM   14820 C  CZ    . PHE D 2 199 ? 157.799 105.794 124.636 1.00 31.91 ?  178 PHE D CZ    1 
ATOM   14821 N  N     . TYR D 2 200 ? 151.516 109.568 124.850 1.00 26.46 ?  179 TYR D N     1 
ATOM   14822 C  CA    . TYR D 2 200 ? 150.269 110.211 124.405 1.00 27.43 ?  179 TYR D CA    1 
ATOM   14823 C  C     . TYR D 2 200 ? 150.372 111.729 124.511 1.00 27.68 ?  179 TYR D C     1 
ATOM   14824 O  O     . TYR D 2 200 ? 149.911 112.450 123.627 1.00 28.71 ?  179 TYR D O     1 
ATOM   14825 C  CB    . TYR D 2 200 ? 149.131 109.703 125.282 1.00 27.27 ?  179 TYR D CB    1 
ATOM   14826 C  CG    . TYR D 2 200 ? 147.720 109.904 124.785 1.00 28.90 ?  179 TYR D CG    1 
ATOM   14827 C  CD1   . TYR D 2 200 ? 147.356 109.579 123.485 1.00 29.00 ?  179 TYR D CD1   1 
ATOM   14828 C  CD2   . TYR D 2 200 ? 146.727 110.359 125.658 1.00 30.14 ?  179 TYR D CD2   1 
ATOM   14829 C  CE1   . TYR D 2 200 ? 146.044 109.740 123.047 1.00 31.26 ?  179 TYR D CE1   1 
ATOM   14830 C  CE2   . TYR D 2 200 ? 145.417 110.513 125.238 1.00 31.86 ?  179 TYR D CE2   1 
ATOM   14831 C  CZ    . TYR D 2 200 ? 145.081 110.207 123.930 1.00 32.51 ?  179 TYR D CZ    1 
ATOM   14832 O  OH    . TYR D 2 200 ? 143.781 110.362 123.512 1.00 33.77 ?  179 TYR D OH    1 
ATOM   14833 N  N     . GLY D 2 201 ? 150.983 112.208 125.593 1.00 27.68 ?  180 GLY D N     1 
ATOM   14834 C  CA    . GLY D 2 201 ? 151.206 113.636 125.793 1.00 28.02 ?  180 GLY D CA    1 
ATOM   14835 C  C     . GLY D 2 201 ? 152.245 114.264 124.868 1.00 28.60 ?  180 GLY D C     1 
ATOM   14836 O  O     . GLY D 2 201 ? 152.321 115.482 124.777 1.00 28.44 ?  180 GLY D O     1 
ATOM   14837 N  N     . GLN D 2 202 ? 153.049 113.427 124.206 1.00 29.34 ?  181 GLN D N     1 
ATOM   14838 C  CA    . GLN D 2 202 ? 154.096 113.857 123.262 1.00 30.39 ?  181 GLN D CA    1 
ATOM   14839 C  C     . GLN D 2 202 ? 153.698 113.694 121.795 1.00 30.55 ?  181 GLN D C     1 
ATOM   14840 O  O     . GLN D 2 202 ? 154.482 114.032 120.902 1.00 31.23 ?  181 GLN D O     1 
ATOM   14841 C  CB    . GLN D 2 202 ? 155.347 112.990 123.422 1.00 30.31 ?  181 GLN D CB    1 
ATOM   14842 C  CG    . GLN D 2 202 ? 156.127 113.114 124.675 1.00 32.40 ?  181 GLN D CG    1 
ATOM   14843 C  CD    . GLN D 2 202 ? 157.315 112.175 124.648 1.00 33.85 ?  181 GLN D CD    1 
ATOM   14844 O  OE1   . GLN D 2 202 ? 157.323 111.141 125.312 1.00 33.94 ?  181 GLN D OE1   1 
ATOM   14845 N  NE2   . GLN D 2 202 ? 158.306 112.507 123.839 1.00 34.92 ?  181 GLN D NE2   1 
ATOM   14846 N  N     . GLY D 2 203 ? 152.530 113.116 121.538 1.00 30.57 ?  182 GLY D N     1 
ATOM   14847 C  CA    . GLY D 2 203 ? 152.096 112.855 120.163 1.00 30.83 ?  182 GLY D CA    1 
ATOM   14848 C  C     . GLY D 2 203 ? 152.543 111.509 119.613 1.00 30.80 ?  182 GLY D C     1 
ATOM   14849 O  O     . GLY D 2 203 ? 152.418 111.254 118.412 1.00 30.86 ?  182 GLY D O     1 
ATOM   14850 N  N     . LYS D 2 204 ? 153.057 110.645 120.489 1.00 30.14 ?  183 LYS D N     1 
ATOM   14851 C  CA    . LYS D 2 204 ? 153.492 109.302 120.095 1.00 30.35 ?  183 LYS D CA    1 
ATOM   14852 C  C     . LYS D 2 204 ? 152.493 108.231 120.526 1.00 29.52 ?  183 LYS D C     1 
ATOM   14853 O  O     . LYS D 2 204 ? 151.858 108.362 121.570 1.00 28.60 ?  183 LYS D O     1 
ATOM   14854 C  CB    . LYS D 2 204 ? 154.873 108.998 120.672 1.00 30.76 ?  183 LYS D CB    1 
ATOM   14855 C  CG    . LYS D 2 204 ? 155.984 109.885 120.102 1.00 32.95 ?  183 LYS D CG    1 
ATOM   14856 C  CD    . LYS D 2 204 ? 157.244 109.724 120.918 1.00 36.37 ?  183 LYS D CD    1 
ATOM   14857 C  CE    . LYS D 2 204 ? 158.381 110.582 120.392 1.00 38.47 ?  183 LYS D CE    1 
ATOM   14858 N  NZ    . LYS D 2 204 ? 159.489 110.554 121.393 1.00 40.21 1  183 LYS D NZ    1 
ATOM   14859 N  N     . LEU D 2 205 ? 152.371 107.173 119.721 1.00 29.47 ?  184 LEU D N     1 
ATOM   14860 C  CA    . LEU D 2 205 ? 151.446 106.060 119.990 1.00 29.06 ?  184 LEU D CA    1 
ATOM   14861 C  C     . LEU D 2 205 ? 150.068 106.565 120.468 1.00 28.96 ?  184 LEU D C     1 
ATOM   14862 O  O     . LEU D 2 205 ? 149.566 106.177 121.530 1.00 27.68 ?  184 LEU D O     1 
ATOM   14863 C  CB    . LEU D 2 205 ? 152.056 105.063 120.987 1.00 28.63 ?  184 LEU D CB    1 
ATOM   14864 C  CG    . LEU D 2 205 ? 153.414 104.434 120.637 1.00 29.00 ?  184 LEU D CG    1 
ATOM   14865 C  CD1   . LEU D 2 205 ? 153.893 103.535 121.780 1.00 28.90 ?  184 LEU D CD1   1 
ATOM   14866 C  CD2   . LEU D 2 205 ? 153.345 103.642 119.338 1.00 28.67 ?  184 LEU D CD2   1 
ATOM   14867 N  N     . MET D 2 206 ? 149.483 107.434 119.648 1.00 29.02 ?  185 MET D N     1 
ATOM   14868 C  CA    . MET D 2 206 ? 148.227 108.108 119.940 1.00 29.72 ?  185 MET D CA    1 
ATOM   14869 C  C     . MET D 2 206 ? 146.990 107.215 119.959 1.00 29.54 ?  185 MET D C     1 
ATOM   14870 O  O     . MET D 2 206 ? 146.062 107.480 120.719 1.00 29.47 ?  185 MET D O     1 
ATOM   14871 C  CB    . MET D 2 206 ? 148.017 109.260 118.949 1.00 30.69 ?  185 MET D CB    1 
ATOM   14872 C  CG    . MET D 2 206 ? 149.140 110.285 118.986 1.00 32.03 ?  185 MET D CG    1 
ATOM   14873 S  SD    . MET D 2 206 ? 149.325 110.998 120.630 1.00 36.63 ?  185 MET D SD    1 
ATOM   14874 C  CE    . MET D 2 206 ? 148.101 112.294 120.563 1.00 33.80 ?  185 MET D CE    1 
ATOM   14875 N  N     . GLN D 2 207 ? 146.966 106.187 119.113 1.00 29.56 ?  186 GLN D N     1 
ATOM   14876 C  CA    . GLN D 2 207 ? 145.814 105.283 119.030 1.00 29.17 ?  186 GLN D CA    1 
ATOM   14877 C  C     . GLN D 2 207 ? 145.746 104.385 120.262 1.00 28.26 ?  186 GLN D C     1 
ATOM   14878 O  O     . GLN D 2 207 ? 144.688 104.251 120.871 1.00 27.98 ?  186 GLN D O     1 
ATOM   14879 C  CB    . GLN D 2 207 ? 145.855 104.436 117.748 1.00 29.80 ?  186 GLN D CB    1 
ATOM   14880 C  CG    . GLN D 2 207 ? 145.983 105.241 116.455 1.00 31.75 ?  186 GLN D CG    1 
ATOM   14881 C  CD    . GLN D 2 207 ? 144.942 106.338 116.359 1.00 34.93 ?  186 GLN D CD    1 
ATOM   14882 O  OE1   . GLN D 2 207 ? 143.748 106.073 116.163 1.00 36.91 ?  186 GLN D OE1   1 
ATOM   14883 N  NE2   . GLN D 2 207 ? 145.386 107.580 116.508 1.00 36.09 ?  186 GLN D NE2   1 
ATOM   14884 N  N     . SER D 2 208 ? 146.871 103.775 120.627 0.50 27.75 ?  187 SER D N     1 
ATOM   14885 C  CA    . SER D 2 208 ? 146.922 102.940 121.821 0.50 27.12 ?  187 SER D CA    1 
ATOM   14886 C  C     . SER D 2 208 ? 146.805 103.792 123.082 0.50 26.72 ?  187 SER D C     1 
ATOM   14887 O  O     . SER D 2 208 ? 146.249 103.339 124.081 0.50 26.30 ?  187 SER D O     1 
ATOM   14888 C  CB    . SER D 2 208 ? 148.194 102.093 121.855 0.50 26.88 ?  187 SER D CB    1 
ATOM   14889 O  OG    . SER D 2 208 ? 149.336 102.902 121.668 0.50 26.59 ?  187 SER D OG    1 
ATOM   14890 N  N     . GLY D 2 209 ? 147.326 105.019 123.024 1.00 26.64 ?  188 GLY D N     1 
ATOM   14891 C  CA    . GLY D 2 209 ? 147.194 105.982 124.136 1.00 26.43 ?  188 GLY D CA    1 
ATOM   14892 C  C     . GLY D 2 209 ? 145.751 106.405 124.377 1.00 26.66 ?  188 GLY D C     1 
ATOM   14893 O  O     . GLY D 2 209 ? 145.334 106.612 125.516 1.00 26.57 ?  188 GLY D O     1 
ATOM   14894 N  N     . GLU D 2 210 ? 144.983 106.540 123.299 1.00 27.42 ?  189 GLU D N     1 
ATOM   14895 C  CA    . GLU D 2 210 ? 143.555 106.830 123.411 1.00 27.73 ?  189 GLU D CA    1 
ATOM   14896 C  C     . GLU D 2 210 ? 142.836 105.656 124.092 1.00 27.04 ?  189 GLU D C     1 
ATOM   14897 O  O     . GLU D 2 210 ? 142.036 105.854 125.006 1.00 26.57 ?  189 GLU D O     1 
ATOM   14898 C  CB    . GLU D 2 210 ? 142.940 107.143 122.035 1.00 28.28 ?  189 GLU D CB    1 
ATOM   14899 C  CG    . GLU D 2 210 ? 141.460 107.553 122.105 1.00 30.71 ?  189 GLU D CG    1 
ATOM   14900 C  CD    . GLU D 2 210 ? 140.902 108.119 120.801 1.00 35.43 ?  189 GLU D CD    1 
ATOM   14901 O  OE1   . GLU D 2 210 ? 141.590 108.069 119.751 1.00 36.89 ?  189 GLU D OE1   1 
ATOM   14902 O  OE2   . GLU D 2 210 ? 139.758 108.628 120.835 1.00 37.04 -1 189 GLU D OE2   1 
ATOM   14903 N  N     . ILE D 2 211 ? 143.138 104.439 123.649 1.00 26.80 ?  190 ILE D N     1 
ATOM   14904 C  CA    . ILE D 2 211 ? 142.603 103.240 124.287 1.00 26.92 ?  190 ILE D CA    1 
ATOM   14905 C  C     . ILE D 2 211 ? 142.948 103.205 125.769 1.00 26.45 ?  190 ILE D C     1 
ATOM   14906 O  O     . ILE D 2 211 ? 142.071 102.967 126.596 1.00 26.65 ?  190 ILE D O     1 
ATOM   14907 C  CB    . ILE D 2 211 ? 143.064 101.943 123.573 1.00 27.00 ?  190 ILE D CB    1 
ATOM   14908 C  CG1   . ILE D 2 211 ? 142.380 101.840 122.204 1.00 28.77 ?  190 ILE D CG1   1 
ATOM   14909 C  CG2   . ILE D 2 211 ? 142.738 100.705 124.425 1.00 26.82 ?  190 ILE D CG2   1 
ATOM   14910 C  CD1   . ILE D 2 211 ? 142.861 100.690 121.329 1.00 30.88 ?  190 ILE D CD1   1 
ATOM   14911 N  N     . ILE D 2 212 ? 144.212 103.470 126.112 1.00 26.49 ?  191 ILE D N     1 
ATOM   14912 C  CA    . ILE D 2 212 ? 144.642 103.413 127.510 1.00 25.73 ?  191 ILE D CA    1 
ATOM   14913 C  C     . ILE D 2 212 ? 143.903 104.457 128.349 1.00 25.48 ?  191 ILE D C     1 
ATOM   14914 O  O     . ILE D 2 212 ? 143.508 104.185 129.486 1.00 24.95 ?  191 ILE D O     1 
ATOM   14915 C  CB    . ILE D 2 212 ? 146.186 103.557 127.663 1.00 26.44 ?  191 ILE D CB    1 
ATOM   14916 C  CG1   . ILE D 2 212 ? 146.911 102.362 127.031 1.00 26.71 ?  191 ILE D CG1   1 
ATOM   14917 C  CG2   . ILE D 2 212 ? 146.587 103.724 129.146 1.00 26.01 ?  191 ILE D CG2   1 
ATOM   14918 C  CD1   . ILE D 2 212 ? 146.616 101.006 127.647 1.00 30.50 ?  191 ILE D CD1   1 
ATOM   14919 N  N     . ASN D 2 213 ? 143.698 105.637 127.772 1.00 24.79 ?  192 ASN D N     1 
ATOM   14920 C  CA    . ASN D 2 213 ? 142.971 106.699 128.453 1.00 24.80 ?  192 ASN D CA    1 
ATOM   14921 C  C     . ASN D 2 213 ? 141.509 106.314 128.761 1.00 24.44 ?  192 ASN D C     1 
ATOM   14922 O  O     . ASN D 2 213 ? 140.959 106.705 129.796 1.00 23.25 ?  192 ASN D O     1 
ATOM   14923 C  CB    . ASN D 2 213 ? 143.045 107.993 127.640 1.00 25.68 ?  192 ASN D CB    1 
ATOM   14924 C  CG    . ASN D 2 213 ? 143.172 109.226 128.513 1.00 27.89 ?  192 ASN D CG    1 
ATOM   14925 O  OD1   . ASN D 2 213 ? 143.739 109.181 129.602 1.00 31.05 ?  192 ASN D OD1   1 
ATOM   14926 N  ND2   . ASN D 2 213 ? 142.647 110.344 128.030 1.00 31.70 ?  192 ASN D ND2   1 
ATOM   14927 N  N     . LEU D 2 214 ? 140.894 105.536 127.868 1.00 23.60 ?  193 LEU D N     1 
ATOM   14928 C  CA    . LEU D 2 214 ? 139.521 105.074 128.080 1.00 23.84 ?  193 LEU D CA    1 
ATOM   14929 C  C     . LEU D 2 214 ? 139.486 104.024 129.176 1.00 23.48 ?  193 LEU D C     1 
ATOM   14930 O  O     . LEU D 2 214 ? 138.591 104.038 130.025 1.00 24.12 ?  193 LEU D O     1 
ATOM   14931 C  CB    . LEU D 2 214 ? 138.933 104.511 126.787 1.00 23.71 ?  193 LEU D CB    1 
ATOM   14932 C  CG    . LEU D 2 214 ? 138.563 105.552 125.722 1.00 25.29 ?  193 LEU D CG    1 
ATOM   14933 C  CD1   . LEU D 2 214 ? 138.128 104.862 124.428 1.00 25.41 ?  193 LEU D CD1   1 
ATOM   14934 C  CD2   . LEU D 2 214 ? 137.474 106.493 126.211 1.00 25.80 ?  193 LEU D CD2   1 
ATOM   14935 N  N     . ILE D 2 215 ? 140.470 103.125 129.153 1.00 22.89 ?  194 ILE D N     1 
ATOM   14936 C  CA    . ILE D 2 215 ? 140.611 102.102 130.178 1.00 22.25 ?  194 ILE D CA    1 
ATOM   14937 C  C     . ILE D 2 215 ? 140.804 102.775 131.533 1.00 22.55 ?  194 ILE D C     1 
ATOM   14938 O  O     . ILE D 2 215 ? 140.101 102.463 132.505 1.00 22.53 ?  194 ILE D O     1 
ATOM   14939 C  CB    . ILE D 2 215 ? 141.800 101.162 129.892 1.00 22.37 ?  194 ILE D CB    1 
ATOM   14940 C  CG1   . ILE D 2 215 ? 141.529 100.329 128.632 1.00 21.89 ?  194 ILE D CG1   1 
ATOM   14941 C  CG2   . ILE D 2 215 ? 142.094 100.271 131.116 1.00 20.25 ?  194 ILE D CG2   1 
ATOM   14942 C  CD1   . ILE D 2 215 ? 142.662 99.368  128.251 1.00 20.48 ?  194 ILE D CD1   1 
ATOM   14943 N  N     . LEU D 2 216 ? 141.746 103.712 131.588 1.00 22.35 ?  195 LEU D N     1 
ATOM   14944 C  CA    . LEU D 2 216 ? 142.073 104.404 132.832 1.00 22.51 ?  195 LEU D CA    1 
ATOM   14945 C  C     . LEU D 2 216 ? 140.837 105.113 133.391 1.00 22.30 ?  195 LEU D C     1 
ATOM   14946 O  O     . LEU D 2 216 ? 140.599 105.079 134.605 1.00 21.62 ?  195 LEU D O     1 
ATOM   14947 C  CB    . LEU D 2 216 ? 143.215 105.402 132.581 1.00 23.06 ?  195 LEU D CB    1 
ATOM   14948 C  CG    . LEU D 2 216 ? 143.733 106.387 133.640 1.00 23.98 ?  195 LEU D CG    1 
ATOM   14949 C  CD1   . LEU D 2 216 ? 145.069 106.908 133.181 1.00 24.44 ?  195 LEU D CD1   1 
ATOM   14950 C  CD2   . LEU D 2 216 ? 142.768 107.564 133.866 1.00 25.00 ?  195 LEU D CD2   1 
ATOM   14951 N  N     . ARG D 2 217 ? 140.065 105.754 132.506 1.00 21.64 ?  196 ARG D N     1 
ATOM   14952 C  CA    . ARG D 2 217 ? 138.827 106.432 132.904 1.00 22.49 ?  196 ARG D CA    1 
ATOM   14953 C  C     . ARG D 2 217 ? 137.812 105.447 133.536 1.00 21.56 ?  196 ARG D C     1 
ATOM   14954 O  O     . ARG D 2 217 ? 137.150 105.792 134.505 1.00 21.32 ?  196 ARG D O     1 
ATOM   14955 C  CB    . ARG D 2 217 ? 138.200 107.221 131.737 1.00 23.07 ?  196 ARG D CB    1 
ATOM   14956 C  CG    . ARG D 2 217 ? 136.994 108.096 132.143 1.00 25.64 ?  196 ARG D CG    1 
ATOM   14957 C  CD    . ARG D 2 217 ? 136.251 108.699 130.937 1.00 32.11 ?  196 ARG D CD    1 
ATOM   14958 N  NE    . ARG D 2 217 ? 135.742 107.668 130.022 1.00 35.06 ?  196 ARG D NE    1 
ATOM   14959 C  CZ    . ARG D 2 217 ? 134.889 107.891 129.027 1.00 37.65 ?  196 ARG D CZ    1 
ATOM   14960 N  NH1   . ARG D 2 217 ? 134.409 109.111 128.813 1.00 40.20 1  196 ARG D NH1   1 
ATOM   14961 N  NH2   . ARG D 2 217 ? 134.500 106.886 128.247 1.00 38.20 ?  196 ARG D NH2   1 
ATOM   14962 N  N     . ASP D 2 218 ? 137.702 104.234 132.992 1.00 21.34 ?  197 ASP D N     1 
ATOM   14963 C  CA    . ASP D 2 218 ? 136.903 103.174 133.626 1.00 21.09 ?  197 ASP D CA    1 
ATOM   14964 C  C     . ASP D 2 218 ? 137.469 102.773 135.004 1.00 20.65 ?  197 ASP D C     1 
ATOM   14965 O  O     . ASP D 2 218 ? 136.714 102.668 135.973 1.00 20.16 ?  197 ASP D O     1 
ATOM   14966 C  CB    . ASP D 2 218 ? 136.801 101.931 132.729 1.00 21.58 ?  197 ASP D CB    1 
ATOM   14967 C  CG    . ASP D 2 218 ? 136.001 102.177 131.451 1.00 22.60 ?  197 ASP D CG    1 
ATOM   14968 O  OD1   . ASP D 2 218 ? 135.161 103.105 131.410 1.00 24.72 ?  197 ASP D OD1   1 
ATOM   14969 O  OD2   . ASP D 2 218 ? 136.229 101.430 130.472 1.00 22.64 -1 197 ASP D OD2   1 
ATOM   14970 N  N     . GLU D 2 219 ? 138.781 102.546 135.101 1.00 20.59 ?  198 GLU D N     1 
ATOM   14971 C  CA    . GLU D 2 219 ? 139.366 102.118 136.391 1.00 20.66 ?  198 GLU D CA    1 
ATOM   14972 C  C     . GLU D 2 219 ? 139.176 103.177 137.480 1.00 20.45 ?  198 GLU D C     1 
ATOM   14973 O  O     . GLU D 2 219 ? 138.951 102.839 138.647 1.00 20.59 ?  198 GLU D O     1 
ATOM   14974 C  CB    . GLU D 2 219 ? 140.851 101.739 136.269 1.00 20.55 ?  198 GLU D CB    1 
ATOM   14975 C  CG    . GLU D 2 219 ? 141.249 100.901 135.014 1.00 21.99 ?  198 GLU D CG    1 
ATOM   14976 C  CD    . GLU D 2 219 ? 140.563 99.536  134.888 1.00 24.00 ?  198 GLU D CD    1 
ATOM   14977 O  OE1   . GLU D 2 219 ? 139.462 99.314  135.436 1.00 25.06 ?  198 GLU D OE1   1 
ATOM   14978 O  OE2   . GLU D 2 219 ? 141.121 98.667  134.196 1.00 24.49 -1 198 GLU D OE2   1 
ATOM   14979 N  N     . ALA D 2 220 ? 139.249 104.448 137.094 1.00 20.47 ?  199 ALA D N     1 
ATOM   14980 C  CA    . ALA D 2 220 ? 139.002 105.563 138.032 1.00 21.10 ?  199 ALA D CA    1 
ATOM   14981 C  C     . ALA D 2 220 ? 137.623 105.472 138.681 1.00 21.34 ?  199 ALA D C     1 
ATOM   14982 O  O     . ALA D 2 220 ? 137.519 105.472 139.906 1.00 21.19 ?  199 ALA D O     1 
ATOM   14983 C  CB    . ALA D 2 220 ? 139.200 106.919 137.352 1.00 21.09 ?  199 ALA D CB    1 
ATOM   14984 N  N     . ILE D 2 221 ? 136.573 105.366 137.862 1.00 21.31 ?  200 ILE D N     1 
ATOM   14985 C  CA    . ILE D 2 221 ? 135.226 105.187 138.398 1.00 21.80 ?  200 ILE D CA    1 
ATOM   14986 C  C     . ILE D 2 221 ? 135.036 103.858 139.161 1.00 20.90 ?  200 ILE D C     1 
ATOM   14987 O  O     . ILE D 2 221 ? 134.333 103.827 140.170 1.00 20.54 ?  200 ILE D O     1 
ATOM   14988 C  CB    . ILE D 2 221 ? 134.110 105.440 137.344 1.00 22.75 ?  200 ILE D CB    1 
ATOM   14989 C  CG1   . ILE D 2 221 ? 132.775 105.650 138.049 1.00 24.63 ?  200 ILE D CG1   1 
ATOM   14990 C  CG2   . ILE D 2 221 ? 133.991 104.282 136.356 1.00 23.38 ?  200 ILE D CG2   1 
ATOM   14991 C  CD1   . ILE D 2 221 ? 131.761 106.391 137.228 1.00 26.91 ?  200 ILE D CD1   1 
ATOM   14992 N  N     . HIS D 2 222 ? 135.687 102.780 138.711 1.00 20.31 ?  201 HIS D N     1 
ATOM   14993 C  CA    . HIS D 2 222 ? 135.642 101.518 139.457 1.00 20.25 ?  201 HIS D CA    1 
ATOM   14994 C  C     . HIS D 2 222 ? 136.189 101.718 140.869 1.00 20.51 ?  201 HIS D C     1 
ATOM   14995 O  O     . HIS D 2 222 ? 135.550 101.330 141.854 1.00 20.99 ?  201 HIS D O     1 
ATOM   14996 C  CB    . HIS D 2 222 ? 136.419 100.399 138.754 1.00 19.79 ?  201 HIS D CB    1 
ATOM   14997 C  CG    . HIS D 2 222 ? 135.895 100.030 137.401 1.00 19.25 ?  201 HIS D CG    1 
ATOM   14998 N  ND1   . HIS D 2 222 ? 136.565 99.158  136.569 1.00 18.35 ?  201 HIS D ND1   1 
ATOM   14999 C  CD2   . HIS D 2 222 ? 134.782 100.415 136.727 1.00 17.64 ?  201 HIS D CD2   1 
ATOM   15000 C  CE1   . HIS D 2 222 ? 135.884 99.009  135.446 1.00 18.28 ?  201 HIS D CE1   1 
ATOM   15001 N  NE2   . HIS D 2 222 ? 134.802 99.767  135.513 1.00 20.01 ?  201 HIS D NE2   1 
ATOM   15002 N  N     . GLY D 2 223 ? 137.363 102.345 140.961 1.00 20.33 ?  202 GLY D N     1 
ATOM   15003 C  CA    . GLY D 2 223 ? 137.994 102.650 142.252 1.00 19.94 ?  202 GLY D CA    1 
ATOM   15004 C  C     . GLY D 2 223 ? 137.129 103.508 143.168 1.00 19.80 ?  202 GLY D C     1 
ATOM   15005 O  O     . GLY D 2 223 ? 137.002 103.212 144.355 1.00 19.96 ?  202 GLY D O     1 
ATOM   15006 N  N     . VAL D 2 224 ? 136.508 104.554 142.619 1.00 19.49 ?  203 VAL D N     1 
ATOM   15007 C  CA    . VAL D 2 224 ? 135.619 105.422 143.409 1.00 18.88 ?  203 VAL D CA    1 
ATOM   15008 C  C     . VAL D 2 224 ? 134.401 104.656 143.943 1.00 18.55 ?  203 VAL D C     1 
ATOM   15009 O  O     . VAL D 2 224 ? 134.034 104.784 145.122 1.00 17.65 ?  203 VAL D O     1 
ATOM   15010 C  CB    . VAL D 2 224 ? 135.162 106.696 142.608 1.00 19.22 ?  203 VAL D CB    1 
ATOM   15011 C  CG1   . VAL D 2 224 ? 134.210 107.566 143.453 1.00 18.51 ?  203 VAL D CG1   1 
ATOM   15012 C  CG2   . VAL D 2 224 ? 136.382 107.528 142.160 1.00 19.69 ?  203 VAL D CG2   1 
ATOM   15013 N  N     . TYR D 2 225 ? 133.796 103.841 143.081 1.00 18.17 ?  204 TYR D N     1 
ATOM   15014 C  CA    . TYR D 2 225 ? 132.602 103.073 143.440 1.00 18.76 ?  204 TYR D CA    1 
ATOM   15015 C  C     . TYR D 2 225 ? 132.895 102.028 144.530 1.00 18.93 ?  204 TYR D C     1 
ATOM   15016 O  O     . TYR D 2 225 ? 132.218 101.984 145.566 1.00 18.77 ?  204 TYR D O     1 
ATOM   15017 C  CB    . TYR D 2 225 ? 131.977 102.402 142.200 1.00 18.96 ?  204 TYR D CB    1 
ATOM   15018 C  CG    . TYR D 2 225 ? 130.659 101.712 142.531 1.00 20.06 ?  204 TYR D CG    1 
ATOM   15019 C  CD1   . TYR D 2 225 ? 129.539 102.463 142.915 1.00 21.79 ?  204 TYR D CD1   1 
ATOM   15020 C  CD2   . TYR D 2 225 ? 130.541 100.320 142.495 1.00 19.51 ?  204 TYR D CD2   1 
ATOM   15021 C  CE1   . TYR D 2 225 ? 128.334 101.843 143.249 1.00 20.38 ?  204 TYR D CE1   1 
ATOM   15022 C  CE2   . TYR D 2 225 ? 129.322 99.685  142.826 1.00 19.38 ?  204 TYR D CE2   1 
ATOM   15023 C  CZ    . TYR D 2 225 ? 128.232 100.463 143.204 1.00 20.84 ?  204 TYR D CZ    1 
ATOM   15024 O  OH    . TYR D 2 225 ? 127.033 99.879  143.548 1.00 20.77 ?  204 TYR D OH    1 
ATOM   15025 N  N     . VAL D 2 226 ? 133.909 101.195 144.302 1.00 18.76 ?  205 VAL D N     1 
ATOM   15026 C  CA    . VAL D 2 226 ? 134.287 100.195 145.297 1.00 18.85 ?  205 VAL D CA    1 
ATOM   15027 C  C     . VAL D 2 226 ? 134.687 100.883 146.602 1.00 19.19 ?  205 VAL D C     1 
ATOM   15028 O  O     . VAL D 2 226 ? 134.383 100.376 147.684 1.00 19.87 ?  205 VAL D O     1 
ATOM   15029 C  CB    . VAL D 2 226 ? 135.391 99.262  144.784 1.00 19.28 ?  205 VAL D CB    1 
ATOM   15030 C  CG1   . VAL D 2 226 ? 135.819 98.252  145.882 1.00 18.22 ?  205 VAL D CG1   1 
ATOM   15031 C  CG2   . VAL D 2 226 ? 134.885 98.532  143.529 1.00 18.40 ?  205 VAL D CG2   1 
ATOM   15032 N  N     . GLY D 2 227 ? 135.335 102.043 146.490 1.00 18.53 ?  206 GLY D N     1 
ATOM   15033 C  CA    . GLY D 2 227 ? 135.669 102.871 147.665 1.00 18.74 ?  206 GLY D CA    1 
ATOM   15034 C  C     . GLY D 2 227 ? 134.470 103.259 148.513 1.00 19.17 ?  206 GLY D C     1 
ATOM   15035 O  O     . GLY D 2 227 ? 134.537 103.246 149.750 1.00 18.66 ?  206 GLY D O     1 
ATOM   15036 N  N     . LEU D 2 228 ? 133.374 103.626 147.852 1.00 19.00 ?  207 LEU D N     1 
ATOM   15037 C  CA    . LEU D 2 228 ? 132.146 103.981 148.567 1.00 19.73 ?  207 LEU D CA    1 
ATOM   15038 C  C     . LEU D 2 228 ? 131.542 102.757 149.269 1.00 19.76 ?  207 LEU D C     1 
ATOM   15039 O  O     . LEU D 2 228 ? 131.076 102.862 150.403 1.00 20.07 ?  207 LEU D O     1 
ATOM   15040 C  CB    . LEU D 2 228 ? 131.140 104.649 147.625 1.00 19.36 ?  207 LEU D CB    1 
ATOM   15041 C  CG    . LEU D 2 228 ? 131.529 106.053 147.135 1.00 20.50 ?  207 LEU D CG    1 
ATOM   15042 C  CD1   . LEU D 2 228 ? 130.610 106.501 146.014 1.00 19.87 ?  207 LEU D CD1   1 
ATOM   15043 C  CD2   . LEU D 2 228 ? 131.518 107.088 148.298 1.00 22.38 ?  207 LEU D CD2   1 
ATOM   15044 N  N     . LEU D 2 229 ? 131.592 101.596 148.616 1.00 19.27 ?  208 LEU D N     1 
ATOM   15045 C  CA    . LEU D 2 229 ? 131.145 100.340 149.247 1.00 19.47 ?  208 LEU D CA    1 
ATOM   15046 C  C     . LEU D 2 229 ? 131.987 99.958  150.471 1.00 19.67 ?  208 LEU D C     1 
ATOM   15047 O  O     . LEU D 2 229 ? 131.458 99.429  151.456 1.00 19.82 ?  208 LEU D O     1 
ATOM   15048 C  CB    . LEU D 2 229 ? 131.134 99.178  148.232 1.00 19.51 ?  208 LEU D CB    1 
ATOM   15049 C  CG    . LEU D 2 229 ? 130.232 99.266  146.990 1.00 19.48 ?  208 LEU D CG    1 
ATOM   15050 C  CD1   . LEU D 2 229 ? 130.503 98.077  146.051 1.00 20.14 ?  208 LEU D CD1   1 
ATOM   15051 C  CD2   . LEU D 2 229 ? 128.730 99.365  147.338 1.00 19.95 ?  208 LEU D CD2   1 
ATOM   15052 N  N     . ALA D 2 230 ? 133.295 100.215 150.409 1.00 19.43 ?  209 ALA D N     1 
ATOM   15053 C  CA    . ALA D 2 230 ? 134.186 99.987  151.555 1.00 20.29 ?  209 ALA D CA    1 
ATOM   15054 C  C     . ALA D 2 230 ? 133.889 100.939 152.715 1.00 21.17 ?  209 ALA D C     1 
ATOM   15055 O  O     . ALA D 2 230 ? 133.854 100.518 153.867 1.00 21.73 ?  209 ALA D O     1 
ATOM   15056 C  CB    . ALA D 2 230 ? 135.648 100.097 151.129 1.00 19.99 ?  209 ALA D CB    1 
ATOM   15057 N  N     . GLN D 2 231 ? 133.672 102.218 152.410 1.00 22.26 ?  210 GLN D N     1 
ATOM   15058 C  CA    . GLN D 2 231 ? 133.318 103.215 153.439 1.00 23.33 ?  210 GLN D CA    1 
ATOM   15059 C  C     . GLN D 2 231 ? 132.009 102.863 154.153 1.00 23.85 ?  210 GLN D C     1 
ATOM   15060 O  O     . GLN D 2 231 ? 131.882 103.077 155.356 1.00 24.91 ?  210 GLN D O     1 
ATOM   15061 C  CB    . GLN D 2 231 ? 133.206 104.619 152.838 1.00 23.49 ?  210 GLN D CB    1 
ATOM   15062 C  CG    . GLN D 2 231 ? 134.515 105.212 152.306 1.00 23.05 ?  210 GLN D CG    1 
ATOM   15063 C  CD    . GLN D 2 231 ? 134.308 106.600 151.702 1.00 24.65 ?  210 GLN D CD    1 
ATOM   15064 O  OE1   . GLN D 2 231 ? 133.720 107.474 152.338 1.00 25.85 ?  210 GLN D OE1   1 
ATOM   15065 N  NE2   . GLN D 2 231 ? 134.773 106.800 150.468 1.00 22.30 ?  210 GLN D NE2   1 
ATOM   15066 N  N     . GLU D 2 232 ? 131.038 102.344 153.408 1.00 24.36 ?  211 GLU D N     1 
ATOM   15067 C  CA    . GLU D 2 232 ? 129.794 101.852 153.996 1.00 24.83 ?  211 GLU D CA    1 
ATOM   15068 C  C     . GLU D 2 232 ? 130.049 100.797 155.078 1.00 24.34 ?  211 GLU D C     1 
ATOM   15069 O  O     . GLU D 2 232 ? 129.460 100.866 156.157 1.00 24.20 ?  211 GLU D O     1 
ATOM   15070 C  CB    . GLU D 2 232 ? 128.879 101.282 152.918 1.00 25.15 ?  211 GLU D CB    1 
ATOM   15071 C  CG    . GLU D 2 232 ? 127.479 100.995 153.394 1.00 28.55 ?  211 GLU D CG    1 
ATOM   15072 C  CD    . GLU D 2 232 ? 126.621 100.459 152.280 1.00 33.83 ?  211 GLU D CD    1 
ATOM   15073 O  OE1   . GLU D 2 232 ? 125.959 101.277 151.610 1.00 35.09 ?  211 GLU D OE1   1 
ATOM   15074 O  OE2   . GLU D 2 232 ? 126.644 99.230  152.047 1.00 35.51 -1 211 GLU D OE2   1 
ATOM   15075 N  N     . ILE D 2 233 ? 130.926 99.835  154.795 1.00 23.39 ?  212 ILE D N     1 
ATOM   15076 C  CA    . ILE D 2 233 ? 131.300 98.820  155.794 1.00 23.42 ?  212 ILE D CA    1 
ATOM   15077 C  C     . ILE D 2 233 ? 132.059 99.455  156.960 1.00 23.74 ?  212 ILE D C     1 
ATOM   15078 O  O     . ILE D 2 233 ? 131.731 99.226  158.124 1.00 24.61 ?  212 ILE D O     1 
ATOM   15079 C  CB    . ILE D 2 233 ? 132.111 97.649  155.176 1.00 22.81 ?  212 ILE D CB    1 
ATOM   15080 C  CG1   . ILE D 2 233 ? 131.239 96.854  154.193 1.00 22.94 ?  212 ILE D CG1   1 
ATOM   15081 C  CG2   . ILE D 2 233 ? 132.645 96.713  156.268 1.00 22.45 ?  212 ILE D CG2   1 
ATOM   15082 C  CD1   . ILE D 2 233 ? 132.036 95.903  153.273 1.00 22.21 ?  212 ILE D CD1   1 
ATOM   15083 N  N     . TYR D 2 234 ? 133.063 100.268 156.641 1.00 24.19 ?  213 TYR D N     1 
ATOM   15084 C  CA    . TYR D 2 234 ? 133.874 100.956 157.635 1.00 24.59 ?  213 TYR D CA    1 
ATOM   15085 C  C     . TYR D 2 234 ? 133.011 101.733 158.634 1.00 25.15 ?  213 TYR D C     1 
ATOM   15086 O  O     . TYR D 2 234 ? 133.271 101.693 159.839 1.00 24.94 ?  213 TYR D O     1 
ATOM   15087 C  CB    . TYR D 2 234 ? 134.850 101.906 156.935 1.00 24.41 ?  213 TYR D CB    1 
ATOM   15088 C  CG    . TYR D 2 234 ? 135.750 102.702 157.858 1.00 25.93 ?  213 TYR D CG    1 
ATOM   15089 C  CD1   . TYR D 2 234 ? 136.946 102.167 158.321 1.00 24.70 ?  213 TYR D CD1   1 
ATOM   15090 C  CD2   . TYR D 2 234 ? 135.403 103.999 158.258 1.00 26.11 ?  213 TYR D CD2   1 
ATOM   15091 C  CE1   . TYR D 2 234 ? 137.781 102.895 159.164 1.00 27.90 ?  213 TYR D CE1   1 
ATOM   15092 C  CE2   . TYR D 2 234 ? 136.233 104.734 159.094 1.00 27.70 ?  213 TYR D CE2   1 
ATOM   15093 C  CZ    . TYR D 2 234 ? 137.419 104.179 159.540 1.00 27.89 ?  213 TYR D CZ    1 
ATOM   15094 O  OH    . TYR D 2 234 ? 138.244 104.901 160.371 1.00 32.34 ?  213 TYR D OH    1 
ATOM   15095 N  N     . ASN D 2 235 ? 131.998 102.434 158.122 1.00 25.43 ?  214 ASN D N     1 
ATOM   15096 C  CA    . ASN D 2 235 ? 131.123 103.278 158.952 1.00 26.77 ?  214 ASN D CA    1 
ATOM   15097 C  C     . ASN D 2 235 ? 130.174 102.495 159.858 1.00 27.06 ?  214 ASN D C     1 
ATOM   15098 O  O     . ASN D 2 235 ? 129.557 103.062 160.755 1.00 27.42 ?  214 ASN D O     1 
ATOM   15099 C  CB    . ASN D 2 235 ? 130.300 104.239 158.089 1.00 26.80 ?  214 ASN D CB    1 
ATOM   15100 C  CG    . ASN D 2 235 ? 131.152 105.226 157.338 1.00 28.19 ?  214 ASN D CG    1 
ATOM   15101 O  OD1   . ASN D 2 235 ? 132.192 105.669 157.821 1.00 29.35 ?  214 ASN D OD1   1 
ATOM   15102 N  ND2   . ASN D 2 235 ? 130.708 105.587 156.146 1.00 30.84 ?  214 ASN D ND2   1 
ATOM   15103 N  N     . LYS D 2 236 ? 130.059 101.197 159.617 1.00 26.87 ?  215 LYS D N     1 
ATOM   15104 C  CA    . LYS D 2 236 ? 129.230 100.341 160.455 1.00 27.86 ?  215 LYS D CA    1 
ATOM   15105 C  C     . LYS D 2 236 ? 130.018 99.787  161.651 1.00 28.07 ?  215 LYS D C     1 
ATOM   15106 O  O     . LYS D 2 236 ? 129.462 99.084  162.493 1.00 28.22 ?  215 LYS D O     1 
ATOM   15107 C  CB    . LYS D 2 236 ? 128.636 99.199  159.630 1.00 27.52 ?  215 LYS D CB    1 
ATOM   15108 C  CG    . LYS D 2 236 ? 127.675 99.645  158.555 1.00 29.60 ?  215 LYS D CG    1 
ATOM   15109 C  CD    . LYS D 2 236 ? 126.678 98.555  158.200 1.00 34.24 ?  215 LYS D CD    1 
ATOM   15110 C  CE    . LYS D 2 236 ? 127.046 97.788  156.944 1.00 36.75 ?  215 LYS D CE    1 
ATOM   15111 N  NZ    . LYS D 2 236 ? 128.292 97.012  157.119 1.00 40.41 1  215 LYS D NZ    1 
ATOM   15112 N  N     . GLN D 2 237 ? 131.305 100.116 161.723 1.00 28.33 ?  216 GLN D N     1 
ATOM   15113 C  CA    . GLN D 2 237 ? 132.191 99.538  162.737 1.00 29.60 ?  216 GLN D CA    1 
ATOM   15114 C  C     . GLN D 2 237 ? 132.337 100.426 163.967 1.00 30.69 ?  216 GLN D C     1 
ATOM   15115 O  O     . GLN D 2 237 ? 132.095 101.636 163.903 1.00 30.85 ?  216 GLN D O     1 
ATOM   15116 C  CB    . GLN D 2 237 ? 133.587 99.244  162.149 1.00 29.08 ?  216 GLN D CB    1 
ATOM   15117 C  CG    . GLN D 2 237 ? 133.606 98.402  160.869 1.00 27.78 ?  216 GLN D CG    1 
ATOM   15118 C  CD    . GLN D 2 237 ? 132.771 97.135  160.968 1.00 28.38 ?  216 GLN D CD    1 
ATOM   15119 O  OE1   . GLN D 2 237 ? 132.909 96.357  161.909 1.00 29.30 ?  216 GLN D OE1   1 
ATOM   15120 N  NE2   . GLN D 2 237 ? 131.905 96.918  159.982 1.00 26.88 ?  216 GLN D NE2   1 
ATOM   15121 N  N     . THR D 2 238 ? 132.747 99.815  165.078 1.00 32.02 ?  217 THR D N     1 
ATOM   15122 C  CA    . THR D 2 238 ? 133.097 100.554 166.295 1.00 33.47 ?  217 THR D CA    1 
ATOM   15123 C  C     . THR D 2 238 ? 134.341 101.422 166.076 1.00 34.29 ?  217 THR D C     1 
ATOM   15124 O  O     . THR D 2 238 ? 135.036 101.297 165.054 1.00 33.78 ?  217 THR D O     1 
ATOM   15125 C  CB    . THR D 2 238 ? 133.358 99.592  167.488 1.00 34.00 ?  217 THR D CB    1 
ATOM   15126 O  OG1   . THR D 2 238 ? 134.524 98.797  167.223 1.00 34.33 ?  217 THR D OG1   1 
ATOM   15127 C  CG2   . THR D 2 238 ? 132.152 98.667  167.724 1.00 33.53 ?  217 THR D CG2   1 
ATOM   15128 N  N     . GLU D 2 239 ? 134.634 102.292 167.037 1.00 35.45 ?  218 GLU D N     1 
ATOM   15129 C  CA    . GLU D 2 239 ? 135.809 103.152 166.936 1.00 36.37 ?  218 GLU D CA    1 
ATOM   15130 C  C     . GLU D 2 239 ? 137.117 102.366 166.987 1.00 36.29 ?  218 GLU D C     1 
ATOM   15131 O  O     . GLU D 2 239 ? 138.055 102.677 166.246 1.00 36.18 ?  218 GLU D O     1 
ATOM   15132 C  CB    . GLU D 2 239 ? 135.780 104.261 167.992 1.00 37.27 ?  218 GLU D CB    1 
ATOM   15133 C  CG    . GLU D 2 239 ? 134.689 105.318 167.740 1.00 39.45 ?  218 GLU D CG    1 
ATOM   15134 C  CD    . GLU D 2 239 ? 134.788 105.974 166.364 1.00 41.22 ?  218 GLU D CD    1 
ATOM   15135 O  OE1   . GLU D 2 239 ? 135.902 106.372 165.958 1.00 42.62 ?  218 GLU D OE1   1 
ATOM   15136 O  OE2   . GLU D 2 239 ? 133.746 106.093 165.684 1.00 41.24 -1 218 GLU D OE2   1 
ATOM   15137 N  N     . GLU D 2 240 ? 137.173 101.345 167.839 1.00 36.66 ?  219 GLU D N     1 
ATOM   15138 C  CA    . GLU D 2 240 ? 138.363 100.496 167.934 1.00 37.01 ?  219 GLU D CA    1 
ATOM   15139 C  C     . GLU D 2 240 ? 138.567 99.693  166.650 1.00 35.85 ?  219 GLU D C     1 
ATOM   15140 O  O     . GLU D 2 240 ? 139.698 99.565  166.172 1.00 35.62 ?  219 GLU D O     1 
ATOM   15141 C  CB    . GLU D 2 240 ? 138.295 99.556  169.148 1.00 37.98 ?  219 GLU D CB    1 
ATOM   15142 C  CG    . GLU D 2 240 ? 139.574 98.726  169.339 1.00 40.87 ?  219 GLU D CG    1 
ATOM   15143 C  CD    . GLU D 2 240 ? 139.533 97.771  170.531 1.00 44.58 ?  219 GLU D CD    1 
ATOM   15144 O  OE1   . GLU D 2 240 ? 140.628 97.447  171.054 1.00 45.86 ?  219 GLU D OE1   1 
ATOM   15145 O  OE2   . GLU D 2 240 ? 138.427 97.343  170.941 1.00 45.75 -1 219 GLU D OE2   1 
ATOM   15146 N  N     . LYS D 2 241 ? 137.473 99.157  166.110 1.00 34.54 ?  220 LYS D N     1 
ATOM   15147 C  CA    . LYS D 2 241 ? 137.512 98.390  164.863 1.00 33.65 ?  220 LYS D CA    1 
ATOM   15148 C  C     . LYS D 2 241 ? 137.906 99.283  163.679 1.00 32.67 ?  220 LYS D C     1 
ATOM   15149 O  O     . LYS D 2 241 ? 138.651 98.847  162.807 1.00 32.05 ?  220 LYS D O     1 
ATOM   15150 C  CB    . LYS D 2 241 ? 136.175 97.686  164.607 1.00 33.30 ?  220 LYS D CB    1 
ATOM   15151 C  CG    . LYS D 2 241 ? 136.151 96.723  163.404 1.00 34.50 ?  220 LYS D CG    1 
ATOM   15152 C  CD    . LYS D 2 241 ? 137.152 95.569  163.540 1.00 36.30 ?  220 LYS D CD    1 
ATOM   15153 C  CE    . LYS D 2 241 ? 136.728 94.573  164.613 1.00 38.44 ?  220 LYS D CE    1 
ATOM   15154 N  NZ    . LYS D 2 241 ? 137.894 93.803  165.124 1.00 39.28 1  220 LYS D NZ    1 
ATOM   15155 N  N     . LYS D 2 242 ? 137.405 100.522 163.664 1.00 31.90 ?  221 LYS D N     1 
ATOM   15156 C  CA    . LYS D 2 242 ? 137.787 101.505 162.650 1.00 31.28 ?  221 LYS D CA    1 
ATOM   15157 C  C     . LYS D 2 242 ? 139.293 101.767 162.664 1.00 31.32 ?  221 LYS D C     1 
ATOM   15158 O  O     . LYS D 2 242 ? 139.932 101.711 161.621 1.00 30.72 ?  221 LYS D O     1 
ATOM   15159 C  CB    . LYS D 2 242 ? 137.030 102.828 162.834 1.00 31.38 ?  221 LYS D CB    1 
ATOM   15160 C  CG    . LYS D 2 242 ? 135.624 102.845 162.244 1.00 30.64 ?  221 LYS D CG    1 
ATOM   15161 C  CD    . LYS D 2 242 ? 134.968 104.206 162.474 1.00 32.51 ?  221 LYS D CD    1 
ATOM   15162 C  CE    . LYS D 2 242 ? 133.583 104.254 161.870 1.00 32.66 ?  221 LYS D CE    1 
ATOM   15163 N  NZ    . LYS D 2 242 ? 132.862 105.474 162.297 1.00 35.31 1  221 LYS D NZ    1 
ATOM   15164 N  N     . ALA D 2 243 ? 139.845 102.056 163.846 1.00 31.62 ?  222 ALA D N     1 
ATOM   15165 C  CA    . ALA D 2 243 ? 141.286 102.285 164.004 1.00 31.66 ?  222 ALA D CA    1 
ATOM   15166 C  C     . ALA D 2 243 ? 142.114 101.094 163.504 1.00 31.52 ?  222 ALA D C     1 
ATOM   15167 O  O     . ALA D 2 243 ? 143.192 101.268 162.928 1.00 31.41 ?  222 ALA D O     1 
ATOM   15168 C  CB    . ALA D 2 243 ? 141.620 102.608 165.464 1.00 31.89 ?  222 ALA D CB    1 
ATOM   15169 N  N     . GLU D 2 244 ? 141.580 99.894  163.714 1.00 31.35 ?  223 GLU D N     1 
ATOM   15170 C  CA    . GLU D 2 244 ? 142.199 98.648  163.296 1.00 31.54 ?  223 GLU D CA    1 
ATOM   15171 C  C     . GLU D 2 244 ? 142.158 98.476  161.760 1.00 30.63 ?  223 GLU D C     1 
ATOM   15172 O  O     . GLU D 2 244 ? 143.128 98.015  161.141 1.00 29.47 ?  223 GLU D O     1 
ATOM   15173 C  CB    . GLU D 2 244 ? 141.464 97.514  163.992 1.00 32.45 ?  223 GLU D CB    1 
ATOM   15174 C  CG    . GLU D 2 244 ? 142.110 96.164  163.957 1.00 35.31 ?  223 GLU D CG    1 
ATOM   15175 C  CD    . GLU D 2 244 ? 141.452 95.222  164.945 1.00 38.36 ?  223 GLU D CD    1 
ATOM   15176 O  OE1   . GLU D 2 244 ? 141.597 95.440  166.166 1.00 41.93 ?  223 GLU D OE1   1 
ATOM   15177 O  OE2   . GLU D 2 244 ? 140.778 94.268  164.508 1.00 39.37 -1 223 GLU D OE2   1 
ATOM   15178 N  N     . LEU D 2 245 ? 141.034 98.856  161.161 1.00 29.62 ?  224 LEU D N     1 
ATOM   15179 C  CA    . LEU D 2 245 ? 140.888 98.854  159.708 1.00 29.44 ?  224 LEU D CA    1 
ATOM   15180 C  C     . LEU D 2 245 ? 141.752 99.922  159.033 1.00 28.99 ?  224 LEU D C     1 
ATOM   15181 O  O     . LEU D 2 245 ? 142.265 99.691  157.942 1.00 28.63 ?  224 LEU D O     1 
ATOM   15182 C  CB    . LEU D 2 245 ? 139.417 99.014  159.311 1.00 29.06 ?  224 LEU D CB    1 
ATOM   15183 C  CG    . LEU D 2 245 ? 138.486 97.845  159.653 1.00 29.27 ?  224 LEU D CG    1 
ATOM   15184 C  CD1   . LEU D 2 245 ? 137.081 98.150  159.143 1.00 30.76 ?  224 LEU D CD1   1 
ATOM   15185 C  CD2   . LEU D 2 245 ? 138.982 96.528  159.064 1.00 28.11 ?  224 LEU D CD2   1 
ATOM   15186 N  N     . ARG D 2 246 ? 141.906 101.078 159.680 1.00 29.31 ?  225 ARG D N     1 
ATOM   15187 C  CA    . ARG D 2 246 ? 142.813 102.121 159.190 1.00 29.86 ?  225 ARG D CA    1 
ATOM   15188 C  C     . ARG D 2 246 ? 144.256 101.636 159.190 1.00 29.23 ?  225 ARG D C     1 
ATOM   15189 O  O     . ARG D 2 246 ? 144.984 101.855 158.232 1.00 28.95 ?  225 ARG D O     1 
ATOM   15190 C  CB    . ARG D 2 246 ? 142.730 103.401 160.031 1.00 30.56 ?  225 ARG D CB    1 
ATOM   15191 C  CG    . ARG D 2 246 ? 141.511 104.254 159.764 1.00 33.71 ?  225 ARG D CG    1 
ATOM   15192 C  CD    . ARG D 2 246 ? 141.719 105.721 160.184 1.00 37.42 ?  225 ARG D CD    1 
ATOM   15193 N  NE    . ARG D 2 246 ? 142.118 105.879 161.588 1.00 39.17 ?  225 ARG D NE    1 
ATOM   15194 C  CZ    . ARG D 2 246 ? 141.297 105.809 162.636 1.00 40.68 ?  225 ARG D CZ    1 
ATOM   15195 N  NH1   . ARG D 2 246 ? 139.998 105.568 162.476 1.00 40.28 1  225 ARG D NH1   1 
ATOM   15196 N  NH2   . ARG D 2 246 ? 141.784 105.972 163.862 1.00 41.65 ?  225 ARG D NH2   1 
ATOM   15197 N  N     . GLU D 2 247 ? 144.663 100.993 160.278 1.00 28.89 ?  226 GLU D N     1 
ATOM   15198 C  CA    . GLU D 2 247 ? 146.005 100.427 160.374 1.00 29.27 ?  226 GLU D CA    1 
ATOM   15199 C  C     . GLU D 2 247 ? 146.231 99.382  159.283 1.00 27.84 ?  226 GLU D C     1 
ATOM   15200 O  O     . GLU D 2 247 ? 147.294 99.373  158.657 1.00 27.37 ?  226 GLU D O     1 
ATOM   15201 C  CB    . GLU D 2 247 ? 146.268 99.841  161.772 1.00 30.21 ?  226 GLU D CB    1 
ATOM   15202 C  CG    . GLU D 2 247 ? 147.620 99.115  161.927 1.00 34.46 ?  226 GLU D CG    1 
ATOM   15203 C  CD    . GLU D 2 247 ? 148.819 100.015 161.638 1.00 40.77 ?  226 GLU D CD    1 
ATOM   15204 O  OE1   . GLU D 2 247 ? 149.009 101.009 162.378 1.00 44.03 ?  226 GLU D OE1   1 
ATOM   15205 O  OE2   . GLU D 2 247 ? 149.573 99.735  160.671 1.00 42.98 -1 226 GLU D OE2   1 
ATOM   15206 N  N     . PHE D 2 248 ? 145.235 98.522  159.051 1.00 26.73 ?  227 PHE D N     1 
ATOM   15207 C  CA    . PHE D 2 248 ? 145.289 97.547  157.954 1.00 26.15 ?  227 PHE D CA    1 
ATOM   15208 C  C     . PHE D 2 248 ? 145.540 98.228  156.606 1.00 25.33 ?  227 PHE D C     1 
ATOM   15209 O  O     . PHE D 2 248 ? 146.420 97.809  155.858 1.00 24.70 ?  227 PHE D O     1 
ATOM   15210 C  CB    . PHE D 2 248 ? 144.017 96.684  157.848 1.00 26.02 ?  227 PHE D CB    1 
ATOM   15211 C  CG    . PHE D 2 248 ? 143.894 95.949  156.513 1.00 25.61 ?  227 PHE D CG    1 
ATOM   15212 C  CD1   . PHE D 2 248 ? 144.505 94.713  156.324 1.00 26.51 ?  227 PHE D CD1   1 
ATOM   15213 C  CD2   . PHE D 2 248 ? 143.199 96.519  155.443 1.00 26.21 ?  227 PHE D CD2   1 
ATOM   15214 C  CE1   . PHE D 2 248 ? 144.421 94.045  155.102 1.00 26.16 ?  227 PHE D CE1   1 
ATOM   15215 C  CE2   . PHE D 2 248 ? 143.108 95.861  154.209 1.00 26.07 ?  227 PHE D CE2   1 
ATOM   15216 C  CZ    . PHE D 2 248 ? 143.727 94.619  154.042 1.00 25.82 ?  227 PHE D CZ    1 
ATOM   15217 N  N     . ALA D 2 249 ? 144.749 99.260  156.307 1.00 24.83 ?  228 ALA D N     1 
ATOM   15218 C  CA    . ALA D 2 249 ? 144.815 99.965  155.019 1.00 24.08 ?  228 ALA D CA    1 
ATOM   15219 C  C     . ALA D 2 249 ? 146.174 100.647 154.806 1.00 23.93 ?  228 ALA D C     1 
ATOM   15220 O  O     . ALA D 2 249 ? 146.747 100.573 153.717 1.00 22.51 ?  228 ALA D O     1 
ATOM   15221 C  CB    . ALA D 2 249 ? 143.685 100.998 154.929 1.00 24.18 ?  228 ALA D CB    1 
ATOM   15222 N  N     . ILE D 2 250 ? 146.676 101.309 155.847 1.00 24.20 ?  229 ILE D N     1 
ATOM   15223 C  CA    . ILE D 2 250 ? 147.962 102.004 155.772 1.00 24.86 ?  229 ILE D CA    1 
ATOM   15224 C  C     . ILE D 2 250 ? 149.118 101.004 155.655 1.00 24.68 ?  229 ILE D C     1 
ATOM   15225 O  O     . ILE D 2 250 ? 150.039 101.211 154.873 1.00 24.30 ?  229 ILE D O     1 
ATOM   15226 C  CB    . ILE D 2 250 ? 148.173 102.992 156.973 1.00 25.44 ?  229 ILE D CB    1 
ATOM   15227 C  CG1   . ILE D 2 250 ? 147.061 104.058 157.037 1.00 26.49 ?  229 ILE D CG1   1 
ATOM   15228 C  CG2   . ILE D 2 250 ? 149.555 103.657 156.924 1.00 27.13 ?  229 ILE D CG2   1 
ATOM   15229 C  CD1   . ILE D 2 250 ? 146.830 104.853 155.750 1.00 28.58 ?  229 ILE D CD1   1 
ATOM   15230 N  N     . ASP D 2 251 ? 149.061 99.922  156.432 1.00 24.90 ?  230 ASP D N     1 
ATOM   15231 C  CA    . ASP D 2 251 ? 150.068 98.868  156.376 1.00 25.04 ?  230 ASP D CA    1 
ATOM   15232 C  C     . ASP D 2 251 ? 150.121 98.233  154.974 1.00 24.25 ?  230 ASP D C     1 
ATOM   15233 O  O     . ASP D 2 251 ? 151.201 98.056  154.406 1.00 23.60 ?  230 ASP D O     1 
ATOM   15234 C  CB    . ASP D 2 251 ? 149.776 97.812  157.446 1.00 26.23 ?  230 ASP D CB    1 
ATOM   15235 C  CG    . ASP D 2 251 ? 150.702 96.618  157.367 1.00 28.91 ?  230 ASP D CG    1 
ATOM   15236 O  OD1   . ASP D 2 251 ? 151.910 96.761  157.649 1.00 32.03 ?  230 ASP D OD1   1 
ATOM   15237 O  OD2   . ASP D 2 251 ? 150.209 95.519  157.045 1.00 33.16 -1 230 ASP D OD2   1 
ATOM   15238 N  N     . LEU D 2 252 ? 148.954 97.890  154.434 1.00 23.43 ?  231 LEU D N     1 
ATOM   15239 C  CA    . LEU D 2 252 ? 148.866 97.359  153.077 1.00 22.79 ?  231 LEU D CA    1 
ATOM   15240 C  C     . LEU D 2 252 ? 149.425 98.354  152.055 1.00 22.71 ?  231 LEU D C     1 
ATOM   15241 O  O     . LEU D 2 252 ? 150.196 97.973  151.165 1.00 21.58 ?  231 LEU D O     1 
ATOM   15242 C  CB    . LEU D 2 252 ? 147.421 96.996  152.717 1.00 22.48 ?  231 LEU D CB    1 
ATOM   15243 C  CG    . LEU D 2 252 ? 147.210 96.420  151.304 1.00 21.05 ?  231 LEU D CG    1 
ATOM   15244 C  CD1   . LEU D 2 252 ? 148.053 95.147  151.070 1.00 22.94 ?  231 LEU D CD1   1 
ATOM   15245 C  CD2   . LEU D 2 252 ? 145.740 96.121  151.051 1.00 19.31 ?  231 LEU D CD2   1 
ATOM   15246 N  N     . LEU D 2 253 ? 149.031 99.621  152.185 1.00 22.90 ?  232 LEU D N     1 
ATOM   15247 C  CA    . LEU D 2 253 ? 149.523 100.660 151.269 1.00 23.78 ?  232 LEU D CA    1 
ATOM   15248 C  C     . LEU D 2 253 ? 151.054 100.734 151.292 1.00 23.75 ?  232 LEU D C     1 
ATOM   15249 O  O     . LEU D 2 253 ? 151.691 100.798 150.240 1.00 23.26 ?  232 LEU D O     1 
ATOM   15250 C  CB    . LEU D 2 253 ? 148.940 102.033 151.615 1.00 24.03 ?  232 LEU D CB    1 
ATOM   15251 C  CG    . LEU D 2 253 ? 149.581 103.209 150.856 1.00 26.46 ?  232 LEU D CG    1 
ATOM   15252 C  CD1   . LEU D 2 253 ? 149.149 103.192 149.409 1.00 26.52 ?  232 LEU D CD1   1 
ATOM   15253 C  CD2   . LEU D 2 253 ? 149.232 104.556 151.496 1.00 27.50 ?  232 LEU D CD2   1 
ATOM   15254 N  N     . ASN D 2 254 ? 151.623 100.751 152.499 1.00 24.63 ?  233 ASN D N     1 
ATOM   15255 C  CA    . ASN D 2 254 ? 153.077 100.753 152.678 1.00 25.49 ?  233 ASN D CA    1 
ATOM   15256 C  C     . ASN D 2 254 ? 153.788 99.581  151.986 1.00 24.94 ?  233 ASN D C     1 
ATOM   15257 O  O     . ASN D 2 254 ? 154.814 99.786  151.334 1.00 24.64 ?  233 ASN D O     1 
ATOM   15258 C  CB    . ASN D 2 254 ? 153.443 100.767 154.160 1.00 26.98 ?  233 ASN D CB    1 
ATOM   15259 C  CG    . ASN D 2 254 ? 153.482 102.165 154.736 1.00 29.94 ?  233 ASN D CG    1 
ATOM   15260 O  OD1   . ASN D 2 254 ? 153.959 103.109 154.093 1.00 34.55 ?  233 ASN D OD1   1 
ATOM   15261 N  ND2   . ASN D 2 254 ? 152.993 102.308 155.960 1.00 33.81 ?  233 ASN D ND2   1 
ATOM   15262 N  N     . GLN D 2 255 ? 153.251 98.370  152.142 1.00 24.08 ?  234 GLN D N     1 
ATOM   15263 C  CA    . GLN D 2 255 ? 153.849 97.188  151.515 1.00 24.35 ?  234 GLN D CA    1 
ATOM   15264 C  C     . GLN D 2 255 ? 153.829 97.332  150.005 1.00 23.26 ?  234 GLN D C     1 
ATOM   15265 O  O     . GLN D 2 255 ? 154.851 97.104  149.349 1.00 23.12 ?  234 GLN D O     1 
ATOM   15266 C  CB    . GLN D 2 255 ? 153.115 95.895  151.892 1.00 24.84 ?  234 GLN D CB    1 
ATOM   15267 C  CG    . GLN D 2 255 ? 153.317 95.408  153.309 1.00 27.45 ?  234 GLN D CG    1 
ATOM   15268 C  CD    . GLN D 2 255 ? 154.779 95.207  153.669 1.00 32.02 ?  234 GLN D CD    1 
ATOM   15269 O  OE1   . GLN D 2 255 ? 155.287 95.859  154.578 1.00 35.80 ?  234 GLN D OE1   1 
ATOM   15270 N  NE2   . GLN D 2 255 ? 155.459 94.302  152.963 1.00 32.12 ?  234 GLN D NE2   1 
ATOM   15271 N  N     . LEU D 2 256 ? 152.669 97.713  149.467 1.00 21.77 ?  235 LEU D N     1 
ATOM   15272 C  CA    . LEU D 2 256 ? 152.505 97.877  148.020 1.00 21.68 ?  235 LEU D CA    1 
ATOM   15273 C  C     . LEU D 2 256 ? 153.374 99.015  147.497 1.00 21.49 ?  235 LEU D C     1 
ATOM   15274 O  O     . LEU D 2 256 ? 153.985 98.893  146.440 1.00 20.89 ?  235 LEU D O     1 
ATOM   15275 C  CB    . LEU D 2 256 ? 151.032 98.125  147.638 1.00 20.49 ?  235 LEU D CB    1 
ATOM   15276 C  CG    . LEU D 2 256 ? 150.060 96.954  147.840 1.00 21.52 ?  235 LEU D CG    1 
ATOM   15277 C  CD1   . LEU D 2 256 ? 148.597 97.385  147.641 1.00 20.71 ?  235 LEU D CD1   1 
ATOM   15278 C  CD2   . LEU D 2 256 ? 150.386 95.786  146.920 1.00 20.74 ?  235 LEU D CD2   1 
ATOM   15279 N  N     . TYR D 2 257 ? 153.427 100.115 148.247 1.00 21.42 ?  236 TYR D N     1 
ATOM   15280 C  CA    . TYR D 2 257 ? 154.222 101.270 147.833 1.00 22.02 ?  236 TYR D CA    1 
ATOM   15281 C  C     . TYR D 2 257 ? 155.714 100.953 147.743 1.00 22.61 ?  236 TYR D C     1 
ATOM   15282 O  O     . TYR D 2 257 ? 156.379 101.346 146.783 1.00 22.19 ?  236 TYR D O     1 
ATOM   15283 C  CB    . TYR D 2 257 ? 153.974 102.465 148.748 1.00 22.06 ?  236 TYR D CB    1 
ATOM   15284 C  CG    . TYR D 2 257 ? 154.882 103.644 148.477 1.00 23.44 ?  236 TYR D CG    1 
ATOM   15285 C  CD1   . TYR D 2 257 ? 154.786 104.368 147.282 1.00 24.01 ?  236 TYR D CD1   1 
ATOM   15286 C  CD2   . TYR D 2 257 ? 155.828 104.041 149.418 1.00 25.22 ?  236 TYR D CD2   1 
ATOM   15287 C  CE1   . TYR D 2 257 ? 155.620 105.456 147.036 1.00 25.14 ?  236 TYR D CE1   1 
ATOM   15288 C  CE2   . TYR D 2 257 ? 156.673 105.121 149.179 1.00 26.71 ?  236 TYR D CE2   1 
ATOM   15289 C  CZ    . TYR D 2 257 ? 156.560 105.823 147.992 1.00 25.35 ?  236 TYR D CZ    1 
ATOM   15290 O  OH    . TYR D 2 257 ? 157.390 106.892 147.774 1.00 26.77 ?  236 TYR D OH    1 
ATOM   15291 N  N     . GLU D 2 258 ? 156.241 100.233 148.731 1.00 23.09 ?  237 GLU D N     1 
ATOM   15292 C  CA    . GLU D 2 258 ? 157.668 99.907  148.718 1.00 23.98 ?  237 GLU D CA    1 
ATOM   15293 C  C     . GLU D 2 258 ? 158.024 98.985  147.551 1.00 23.13 ?  237 GLU D C     1 
ATOM   15294 O  O     . GLU D 2 258 ? 159.068 99.150  146.927 1.00 23.02 ?  237 GLU D O     1 
ATOM   15295 C  CB    . GLU D 2 258 ? 158.130 99.336  150.067 1.00 25.20 ?  237 GLU D CB    1 
ATOM   15296 C  CG    . GLU D 2 258 ? 158.055 100.350 151.221 1.00 28.82 ?  237 GLU D CG    1 
ATOM   15297 C  CD    . GLU D 2 258 ? 159.093 101.479 151.138 1.00 34.48 ?  237 GLU D CD    1 
ATOM   15298 O  OE1   . GLU D 2 258 ? 160.199 101.272 150.573 1.00 37.75 ?  237 GLU D OE1   1 
ATOM   15299 O  OE2   . GLU D 2 258 ? 158.806 102.586 151.658 1.00 37.16 -1 237 GLU D OE2   1 
ATOM   15300 N  N     . ASN D 2 259 ? 157.140 98.044  147.244 1.00 22.12 ?  238 ASN D N     1 
ATOM   15301 C  CA    . ASN D 2 259 ? 157.289 97.208  146.052 1.00 22.35 ?  238 ASN D CA    1 
ATOM   15302 C  C     . ASN D 2 259 ? 157.136 97.994  144.722 1.00 22.11 ?  238 ASN D C     1 
ATOM   15303 O  O     . ASN D 2 259 ? 157.839 97.704  143.751 1.00 22.24 ?  238 ASN D O     1 
ATOM   15304 C  CB    . ASN D 2 259 ? 156.320 96.021  146.107 1.00 21.69 ?  238 ASN D CB    1 
ATOM   15305 C  CG    . ASN D 2 259 ? 156.468 95.092  144.916 1.00 23.38 ?  238 ASN D CG    1 
ATOM   15306 O  OD1   . ASN D 2 259 ? 157.452 94.345  144.806 1.00 23.95 ?  238 ASN D OD1   1 
ATOM   15307 N  ND2   . ASN D 2 259 ? 155.500 95.140  144.011 1.00 21.14 ?  238 ASN D ND2   1 
ATOM   15308 N  N     . GLU D 2 260 ? 156.230 98.978  144.690 1.00 21.95 ?  239 GLU D N     1 
ATOM   15309 C  CA    . GLU D 2 260 ? 156.071 99.866  143.519 1.00 22.50 ?  239 GLU D CA    1 
ATOM   15310 C  C     . GLU D 2 260 ? 157.345 100.649 143.207 1.00 22.03 ?  239 GLU D C     1 
ATOM   15311 O  O     . GLU D 2 260 ? 157.664 100.881 142.045 1.00 22.03 ?  239 GLU D O     1 
ATOM   15312 C  CB    . GLU D 2 260 ? 154.935 100.887 143.717 1.00 22.90 ?  239 GLU D CB    1 
ATOM   15313 C  CG    . GLU D 2 260 ? 153.514 100.394 143.398 1.00 25.84 ?  239 GLU D CG    1 
ATOM   15314 C  CD    . GLU D 2 260 ? 153.395 99.674  142.058 1.00 28.59 ?  239 GLU D CD    1 
ATOM   15315 O  OE1   . GLU D 2 260 ? 153.750 98.480  141.994 1.00 28.18 ?  239 GLU D OE1   1 
ATOM   15316 O  OE2   . GLU D 2 260 ? 152.907 100.289 141.081 1.00 30.32 -1 239 GLU D OE2   1 
ATOM   15317 N  N     . LEU D 2 261 ? 158.047 101.085 144.248 1.00 21.50 ?  240 LEU D N     1 
ATOM   15318 C  CA    . LEU D 2 261 ? 159.294 101.818 144.054 1.00 22.03 ?  240 LEU D CA    1 
ATOM   15319 C  C     . LEU D 2 261 ? 160.314 100.927 143.366 1.00 21.52 ?  240 LEU D C     1 
ATOM   15320 O  O     . LEU D 2 261 ? 160.987 101.368 142.433 1.00 21.44 ?  240 LEU D O     1 
ATOM   15321 C  CB    . LEU D 2 261 ? 159.853 102.344 145.374 1.00 21.57 ?  240 LEU D CB    1 
ATOM   15322 C  CG    . LEU D 2 261 ? 159.001 103.333 146.170 1.00 23.22 ?  240 LEU D CG    1 
ATOM   15323 C  CD1   . LEU D 2 261 ? 159.730 103.694 147.451 1.00 23.06 ?  240 LEU D CD1   1 
ATOM   15324 C  CD2   . LEU D 2 261 ? 158.692 104.585 145.350 1.00 23.52 ?  240 LEU D CD2   1 
ATOM   15325 N  N     . GLU D 2 262 ? 160.405 99.675  143.813 1.00 21.69 ?  241 GLU D N     1 
ATOM   15326 C  CA    . GLU D 2 262 ? 161.311 98.698  143.187 1.00 22.31 ?  241 GLU D CA    1 
ATOM   15327 C  C     . GLU D 2 262 ? 160.871 98.346  141.765 1.00 21.69 ?  241 GLU D C     1 
ATOM   15328 O  O     . GLU D 2 262 ? 161.696 98.263  140.852 1.00 21.75 ?  241 GLU D O     1 
ATOM   15329 C  CB    . GLU D 2 262 ? 161.407 97.419  144.025 1.00 22.46 ?  241 GLU D CB    1 
ATOM   15330 C  CG    . GLU D 2 262 ? 161.963 97.590  145.440 1.00 25.63 ?  241 GLU D CG    1 
ATOM   15331 C  CD    . GLU D 2 262 ? 162.106 96.246  146.143 1.00 29.83 ?  241 GLU D CD    1 
ATOM   15332 O  OE1   . GLU D 2 262 ? 161.090 95.714  146.636 1.00 33.22 ?  241 GLU D OE1   1 
ATOM   15333 O  OE2   . GLU D 2 262 ? 163.225 95.704  146.177 1.00 33.36 -1 241 GLU D OE2   1 
ATOM   15334 N  N     . TYR D 2 263 ? 159.571 98.118  141.587 1.00 21.42 ?  242 TYR D N     1 
ATOM   15335 C  CA    . TYR D 2 263 ? 158.982 97.854  140.269 1.00 21.04 ?  242 TYR D CA    1 
ATOM   15336 C  C     . TYR D 2 263 ? 159.322 98.996  139.302 1.00 21.15 ?  242 TYR D C     1 
ATOM   15337 O  O     . TYR D 2 263 ? 159.667 98.767  138.142 1.00 20.32 ?  242 TYR D O     1 
ATOM   15338 C  CB    . TYR D 2 263 ? 157.457 97.715  140.408 1.00 20.95 ?  242 TYR D CB    1 
ATOM   15339 C  CG    . TYR D 2 263 ? 156.690 97.538  139.111 1.00 21.86 ?  242 TYR D CG    1 
ATOM   15340 C  CD1   . TYR D 2 263 ? 156.615 96.292  138.489 1.00 23.53 ?  242 TYR D CD1   1 
ATOM   15341 C  CD2   . TYR D 2 263 ? 156.039 98.618  138.505 1.00 21.20 ?  242 TYR D CD2   1 
ATOM   15342 C  CE1   . TYR D 2 263 ? 155.913 96.123  137.304 1.00 23.34 ?  242 TYR D CE1   1 
ATOM   15343 C  CE2   . TYR D 2 263 ? 155.334 98.456  137.317 1.00 23.11 ?  242 TYR D CE2   1 
ATOM   15344 C  CZ    . TYR D 2 263 ? 155.281 97.207  136.721 1.00 23.27 ?  242 TYR D CZ    1 
ATOM   15345 O  OH    . TYR D 2 263 ? 154.583 97.041  135.544 1.00 27.07 ?  242 TYR D OH    1 
ATOM   15346 N  N     . THR D 2 264 ? 159.200 100.223 139.806 1.00 21.12 ?  243 THR D N     1 
ATOM   15347 C  CA    . THR D 2 264 ? 159.421 101.436 139.025 1.00 21.98 ?  243 THR D CA    1 
ATOM   15348 C  C     . THR D 2 264 ? 160.870 101.542 138.554 1.00 22.32 ?  243 THR D C     1 
ATOM   15349 O  O     . THR D 2 264 ? 161.118 101.730 137.364 1.00 21.78 ?  243 THR D O     1 
ATOM   15350 C  CB    . THR D 2 264 ? 158.992 102.690 139.820 1.00 21.68 ?  243 THR D CB    1 
ATOM   15351 O  OG1   . THR D 2 264 ? 157.576 102.649 140.017 1.00 23.29 ?  243 THR D OG1   1 
ATOM   15352 C  CG2   . THR D 2 264 ? 159.370 103.996 139.094 1.00 23.16 ?  243 THR D CG2   1 
ATOM   15353 N  N     . GLU D 2 265 ? 161.820 101.396 139.477 1.00 22.48 ?  244 GLU D N     1 
ATOM   15354 C  CA    . GLU D 2 265 ? 163.235 101.454 139.102 1.00 23.73 ?  244 GLU D CA    1 
ATOM   15355 C  C     . GLU D 2 265 ? 163.591 100.362 138.104 1.00 23.85 ?  244 GLU D C     1 
ATOM   15356 O  O     . GLU D 2 265 ? 164.322 100.616 137.155 1.00 24.40 ?  244 GLU D O     1 
ATOM   15357 C  CB    . GLU D 2 265 ? 164.132 101.365 140.327 1.00 23.19 ?  244 GLU D CB    1 
ATOM   15358 C  CG    . GLU D 2 265 ? 164.117 102.639 141.128 1.00 25.08 ?  244 GLU D CG    1 
ATOM   15359 C  CD    . GLU D 2 265 ? 164.861 102.523 142.442 1.00 27.30 ?  244 GLU D CD    1 
ATOM   15360 O  OE1   . GLU D 2 265 ? 165.569 101.519 142.656 1.00 27.77 ?  244 GLU D OE1   1 
ATOM   15361 O  OE2   . GLU D 2 265 ? 164.733 103.450 143.263 1.00 28.63 -1 244 GLU D OE2   1 
ATOM   15362 N  N     . ASP D 2 266 ? 163.038 99.167  138.311 1.00 24.13 ?  245 ASP D N     1 
ATOM   15363 C  CA    . ASP D 2 266 ? 163.283 98.010  137.445 1.00 25.22 ?  245 ASP D CA    1 
ATOM   15364 C  C     . ASP D 2 266 ? 162.891 98.273  135.974 1.00 24.84 ?  245 ASP D C     1 
ATOM   15365 O  O     . ASP D 2 266 ? 163.574 97.813  135.055 1.00 25.64 ?  245 ASP D O     1 
ATOM   15366 C  CB    . ASP D 2 266 ? 162.536 96.790  138.006 1.00 25.79 ?  245 ASP D CB    1 
ATOM   15367 C  CG    . ASP D 2 266 ? 162.839 95.502  137.252 1.00 27.71 ?  245 ASP D CG    1 
ATOM   15368 O  OD1   . ASP D 2 266 ? 164.021 95.142  137.143 1.00 31.57 ?  245 ASP D OD1   1 
ATOM   15369 O  OD2   . ASP D 2 266 ? 161.891 94.833  136.788 1.00 30.29 -1 245 ASP D OD2   1 
ATOM   15370 N  N     . LEU D 2 267 ? 161.813 99.023  135.763 1.00 24.07 ?  246 LEU D N     1 
ATOM   15371 C  CA    . LEU D 2 267 ? 161.295 99.291  134.418 1.00 23.98 ?  246 LEU D CA    1 
ATOM   15372 C  C     . LEU D 2 267 ? 161.751 100.618 133.811 1.00 22.83 ?  246 LEU D C     1 
ATOM   15373 O  O     . LEU D 2 267 ? 162.021 100.687 132.606 1.00 23.00 ?  246 LEU D O     1 
ATOM   15374 C  CB    . LEU D 2 267 ? 159.757 99.250  134.410 1.00 23.82 ?  246 LEU D CB    1 
ATOM   15375 C  CG    . LEU D 2 267 ? 159.104 97.876  134.619 1.00 26.05 ?  246 LEU D CG    1 
ATOM   15376 C  CD1   . LEU D 2 267 ? 157.631 97.940  134.326 1.00 26.74 ?  246 LEU D CD1   1 
ATOM   15377 C  CD2   . LEU D 2 267 ? 159.751 96.810  133.755 1.00 28.00 ?  246 LEU D CD2   1 
ATOM   15378 N  N     . TYR D 2 268 ? 161.826 101.658 134.643 1.00 21.68 ?  247 TYR D N     1 
ATOM   15379 C  CA    . TYR D 2 268 ? 161.991 103.030 134.154 1.00 20.95 ?  247 TYR D CA    1 
ATOM   15380 C  C     . TYR D 2 268 ? 163.397 103.637 134.242 1.00 21.43 ?  247 TYR D C     1 
ATOM   15381 O  O     . TYR D 2 268 ? 163.655 104.648 133.590 1.00 20.73 ?  247 TYR D O     1 
ATOM   15382 C  CB    . TYR D 2 268 ? 160.995 103.972 134.838 1.00 20.27 ?  247 TYR D CB    1 
ATOM   15383 C  CG    . TYR D 2 268 ? 159.549 103.779 134.417 1.00 19.54 ?  247 TYR D CG    1 
ATOM   15384 C  CD1   . TYR D 2 268 ? 158.657 103.085 135.227 1.00 18.52 ?  247 TYR D CD1   1 
ATOM   15385 C  CD2   . TYR D 2 268 ? 159.080 104.291 133.197 1.00 20.62 ?  247 TYR D CD2   1 
ATOM   15386 C  CE1   . TYR D 2 268 ? 157.300 102.911 134.845 1.00 18.33 ?  247 TYR D CE1   1 
ATOM   15387 C  CE2   . TYR D 2 268 ? 157.733 104.123 132.804 1.00 20.79 ?  247 TYR D CE2   1 
ATOM   15388 C  CZ    . TYR D 2 268 ? 156.857 103.442 133.639 1.00 20.23 ?  247 TYR D CZ    1 
ATOM   15389 O  OH    . TYR D 2 268 ? 155.544 103.283 133.243 1.00 20.50 ?  247 TYR D OH    1 
ATOM   15390 N  N     . ASP D 2 269 ? 164.296 103.057 135.045 1.00 21.65 ?  248 ASP D N     1 
ATOM   15391 C  CA    . ASP D 2 269 ? 165.678 103.548 135.050 1.00 22.30 ?  248 ASP D CA    1 
ATOM   15392 C  C     . ASP D 2 269 ? 166.320 103.539 133.642 1.00 22.54 ?  248 ASP D C     1 
ATOM   15393 O  O     . ASP D 2 269 ? 167.057 104.465 133.293 1.00 22.49 ?  248 ASP D O     1 
ATOM   15394 C  CB    . ASP D 2 269 ? 166.554 102.783 136.044 1.00 22.83 ?  248 ASP D CB    1 
ATOM   15395 C  CG    . ASP D 2 269 ? 166.392 103.281 137.477 1.00 23.55 ?  248 ASP D CG    1 
ATOM   15396 O  OD1   . ASP D 2 269 ? 165.725 104.314 137.688 1.00 24.95 ?  248 ASP D OD1   1 
ATOM   15397 O  OD2   . ASP D 2 269 ? 166.937 102.633 138.399 1.00 24.47 -1 248 ASP D OD2   1 
ATOM   15398 N  N     . GLN D 2 270 ? 166.032 102.509 132.844 1.00 22.79 ?  249 GLN D N     1 
ATOM   15399 C  CA    . GLN D 2 270 ? 166.619 102.385 131.504 1.00 23.41 ?  249 GLN D CA    1 
ATOM   15400 C  C     . GLN D 2 270 ? 166.151 103.465 130.523 1.00 22.83 ?  249 GLN D C     1 
ATOM   15401 O  O     . GLN D 2 270 ? 166.768 103.656 129.477 1.00 23.75 ?  249 GLN D O     1 
ATOM   15402 C  CB    . GLN D 2 270 ? 166.389 100.991 130.910 1.00 24.02 ?  249 GLN D CB    1 
ATOM   15403 C  CG    . GLN D 2 270 ? 164.931 100.682 130.526 1.00 25.40 ?  249 GLN D CG    1 
ATOM   15404 C  CD    . GLN D 2 270 ? 164.702 99.208  130.242 1.00 29.23 ?  249 GLN D CD    1 
ATOM   15405 O  OE1   . GLN D 2 270 ? 165.358 98.343  130.825 1.00 31.31 ?  249 GLN D OE1   1 
ATOM   15406 N  NE2   . GLN D 2 270 ? 163.758 98.911  129.351 1.00 30.04 ?  249 GLN D NE2   1 
ATOM   15407 N  N     . VAL D 2 271 ? 165.057 104.152 130.852 1.00 21.93 ?  250 VAL D N     1 
ATOM   15408 C  CA    . VAL D 2 271 ? 164.584 105.279 130.042 1.00 21.29 ?  250 VAL D CA    1 
ATOM   15409 C  C     . VAL D 2 271 ? 164.593 106.605 130.825 1.00 21.16 ?  250 VAL D C     1 
ATOM   15410 O  O     . VAL D 2 271 ? 164.028 107.605 130.373 1.00 21.54 ?  250 VAL D O     1 
ATOM   15411 C  CB    . VAL D 2 271 ? 163.184 104.984 129.413 1.00 21.62 ?  250 VAL D CB    1 
ATOM   15412 C  CG1   . VAL D 2 271 ? 163.277 103.821 128.428 1.00 21.36 ?  250 VAL D CG1   1 
ATOM   15413 C  CG2   . VAL D 2 271 ? 162.129 104.698 130.499 1.00 21.17 ?  250 VAL D CG2   1 
ATOM   15414 N  N     . GLY D 2 272 ? 165.216 106.596 132.010 1.00 20.92 ?  251 GLY D N     1 
ATOM   15415 C  CA    . GLY D 2 272 ? 165.477 107.814 132.802 1.00 20.61 ?  251 GLY D CA    1 
ATOM   15416 C  C     . GLY D 2 272 ? 164.286 108.536 133.429 1.00 20.77 ?  251 GLY D C     1 
ATOM   15417 O  O     . GLY D 2 272 ? 164.352 109.746 133.692 1.00 20.28 ?  251 GLY D O     1 
ATOM   15418 N  N     . LEU D 2 273 ? 163.209 107.802 133.695 1.00 19.85 ?  252 LEU D N     1 
ATOM   15419 C  CA    . LEU D 2 273 ? 161.961 108.443 134.115 1.00 20.09 ?  252 LEU D CA    1 
ATOM   15420 C  C     . LEU D 2 273 ? 161.526 108.199 135.563 1.00 19.88 ?  252 LEU D C     1 
ATOM   15421 O  O     . LEU D 2 273 ? 160.541 108.782 136.003 1.00 20.04 ?  252 LEU D O     1 
ATOM   15422 C  CB    . LEU D 2 273 ? 160.823 108.005 133.179 1.00 19.97 ?  252 LEU D CB    1 
ATOM   15423 C  CG    . LEU D 2 273 ? 160.989 108.316 131.699 1.00 20.26 ?  252 LEU D CG    1 
ATOM   15424 C  CD1   . LEU D 2 273 ? 159.719 107.902 130.989 1.00 18.98 ?  252 LEU D CD1   1 
ATOM   15425 C  CD2   . LEU D 2 273 ? 161.299 109.819 131.449 1.00 21.03 ?  252 LEU D CD2   1 
ATOM   15426 N  N     . SER D 2 274 ? 162.266 107.359 136.289 0.50 19.54 ?  253 SER D N     1 
ATOM   15427 C  CA    . SER D 2 274 ? 161.814 106.835 137.587 0.50 19.34 ?  253 SER D CA    1 
ATOM   15428 C  C     . SER D 2 274 ? 161.423 107.897 138.621 0.50 20.05 ?  253 SER D C     1 
ATOM   15429 O  O     . SER D 2 274 ? 160.422 107.736 139.319 0.50 20.31 ?  253 SER D O     1 
ATOM   15430 C  CB    . SER D 2 274 ? 162.843 105.862 138.179 0.50 18.97 ?  253 SER D CB    1 
ATOM   15431 O  OG    . SER D 2 274 ? 163.131 104.807 137.280 0.50 15.35 ?  253 SER D OG    1 
ATOM   15432 N  N     . HIS D 2 275 ? 162.212 108.966 138.723 1.00 20.77 ?  254 HIS D N     1 
ATOM   15433 C  CA    . HIS D 2 275 ? 161.905 110.077 139.646 1.00 21.18 ?  254 HIS D CA    1 
ATOM   15434 C  C     . HIS D 2 275 ? 160.478 110.619 139.450 1.00 21.50 ?  254 HIS D C     1 
ATOM   15435 O  O     . HIS D 2 275 ? 159.711 110.749 140.419 1.00 19.88 ?  254 HIS D O     1 
ATOM   15436 C  CB    . HIS D 2 275 ? 162.931 111.216 139.525 1.00 21.60 ?  254 HIS D CB    1 
ATOM   15437 C  CG    . HIS D 2 275 ? 162.587 112.419 140.351 1.00 22.43 ?  254 HIS D CG    1 
ATOM   15438 N  ND1   . HIS D 2 275 ? 162.987 112.565 141.664 1.00 22.77 ?  254 HIS D ND1   1 
ATOM   15439 C  CD2   . HIS D 2 275 ? 161.865 113.528 140.051 1.00 22.50 ?  254 HIS D CD2   1 
ATOM   15440 C  CE1   . HIS D 2 275 ? 162.529 113.714 142.133 1.00 24.05 ?  254 HIS D CE1   1 
ATOM   15441 N  NE2   . HIS D 2 275 ? 161.840 114.313 141.176 1.00 23.22 ?  254 HIS D NE2   1 
ATOM   15442 N  N     . ASP D 2 276 ? 160.130 110.913 138.196 1.00 22.34 ?  255 ASP D N     1 
ATOM   15443 C  CA    . ASP D 2 276 ? 158.809 111.448 137.876 1.00 23.19 ?  255 ASP D CA    1 
ATOM   15444 C  C     . ASP D 2 276 ? 157.704 110.414 138.043 1.00 22.17 ?  255 ASP D C     1 
ATOM   15445 O  O     . ASP D 2 276 ? 156.598 110.765 138.433 1.00 21.87 ?  255 ASP D O     1 
ATOM   15446 C  CB    . ASP D 2 276 ? 158.763 112.024 136.452 1.00 24.33 ?  255 ASP D CB    1 
ATOM   15447 C  CG    . ASP D 2 276 ? 159.195 113.490 136.383 1.00 27.58 ?  255 ASP D CG    1 
ATOM   15448 O  OD1   . ASP D 2 276 ? 159.099 114.215 137.398 1.00 31.10 ?  255 ASP D OD1   1 
ATOM   15449 O  OD2   . ASP D 2 276 ? 159.639 113.916 135.292 1.00 29.88 -1 255 ASP D OD2   1 
ATOM   15450 N  N     . VAL D 2 277 ? 157.989 109.155 137.714 1.00 21.21 ?  256 VAL D N     1 
ATOM   15451 C  CA    . VAL D 2 277 ? 157.010 108.082 137.916 1.00 20.51 ?  256 VAL D CA    1 
ATOM   15452 C  C     . VAL D 2 277 ? 156.664 107.921 139.401 1.00 20.32 ?  256 VAL D C     1 
ATOM   15453 O  O     . VAL D 2 277 ? 155.501 107.732 139.748 1.00 19.81 ?  256 VAL D O     1 
ATOM   15454 C  CB    . VAL D 2 277 ? 157.479 106.725 137.320 1.00 20.30 ?  256 VAL D CB    1 
ATOM   15455 C  CG1   . VAL D 2 277 ? 156.468 105.631 137.619 1.00 21.16 ?  256 VAL D CG1   1 
ATOM   15456 C  CG2   . VAL D 2 277 ? 157.680 106.846 135.820 1.00 19.06 ?  256 VAL D CG2   1 
ATOM   15457 N  N     . LYS D 2 278 ? 157.677 108.019 140.262 1.00 19.84 ?  257 LYS D N     1 
ATOM   15458 C  CA    . LYS D 2 278 ? 157.476 107.940 141.709 1.00 20.27 ?  257 LYS D CA    1 
ATOM   15459 C  C     . LYS D 2 278 ? 156.529 109.028 142.233 1.00 20.16 ?  257 LYS D C     1 
ATOM   15460 O  O     . LYS D 2 278 ? 155.676 108.737 143.067 1.00 19.88 ?  257 LYS D O     1 
ATOM   15461 C  CB    . LYS D 2 278 ? 158.811 107.952 142.458 1.00 20.20 ?  257 LYS D CB    1 
ATOM   15462 C  CG    . LYS D 2 278 ? 159.581 106.642 142.332 1.00 21.60 ?  257 LYS D CG    1 
ATOM   15463 C  CD    . LYS D 2 278 ? 161.010 106.772 142.847 1.00 21.53 ?  257 LYS D CD    1 
ATOM   15464 C  CE    . LYS D 2 278 ? 161.779 105.507 142.548 1.00 24.52 ?  257 LYS D CE    1 
ATOM   15465 N  NZ    . LYS D 2 278 ? 163.179 105.599 143.080 1.00 26.32 1  257 LYS D NZ    1 
ATOM   15466 N  N     . LYS D 2 279 ? 156.665 110.258 141.724 1.00 19.67 ?  258 LYS D N     1 
ATOM   15467 C  CA    . LYS D 2 279 ? 155.730 111.336 142.080 1.00 20.10 ?  258 LYS D CA    1 
ATOM   15468 C  C     . LYS D 2 279 ? 154.292 110.974 141.689 1.00 19.12 ?  258 LYS D C     1 
ATOM   15469 O  O     . LYS D 2 279 ? 153.359 111.236 142.451 1.00 18.59 ?  258 LYS D O     1 
ATOM   15470 C  CB    . LYS D 2 279 ? 156.131 112.680 141.442 1.00 20.54 ?  258 LYS D CB    1 
ATOM   15471 C  CG    . LYS D 2 279 ? 157.500 113.211 141.863 1.00 22.84 ?  258 LYS D CG    1 
ATOM   15472 C  CD    . LYS D 2 279 ? 157.617 114.743 141.688 1.00 24.16 ?  258 LYS D CD    1 
ATOM   15473 C  CE    . LYS D 2 279 ? 157.572 115.174 140.225 1.00 25.61 ?  258 LYS D CE    1 
ATOM   15474 N  NZ    . LYS D 2 279 ? 157.695 116.675 140.062 1.00 24.70 1  258 LYS D NZ    1 
ATOM   15475 N  N     . PHE D 2 280 ? 154.138 110.355 140.514 1.00 19.04 ?  259 PHE D N     1 
ATOM   15476 C  CA    . PHE D 2 280 ? 152.829 109.939 139.979 1.00 19.31 ?  259 PHE D CA    1 
ATOM   15477 C  C     . PHE D 2 280 ? 152.182 108.810 140.789 1.00 19.25 ?  259 PHE D C     1 
ATOM   15478 O  O     . PHE D 2 280 ? 150.963 108.799 141.001 1.00 19.71 ?  259 PHE D O     1 
ATOM   15479 C  CB    . PHE D 2 280 ? 152.981 109.505 138.521 1.00 19.04 ?  259 PHE D CB    1 
ATOM   15480 C  CG    . PHE D 2 280 ? 151.680 109.428 137.744 1.00 20.15 ?  259 PHE D CG    1 
ATOM   15481 C  CD1   . PHE D 2 280 ? 150.837 110.525 137.651 1.00 21.63 ?  259 PHE D CD1   1 
ATOM   15482 C  CD2   . PHE D 2 280 ? 151.338 108.258 137.063 1.00 19.95 ?  259 PHE D CD2   1 
ATOM   15483 C  CE1   . PHE D 2 280 ? 149.648 110.457 136.892 1.00 22.56 ?  259 PHE D CE1   1 
ATOM   15484 C  CE2   . PHE D 2 280 ? 150.169 108.174 136.309 1.00 20.29 ?  259 PHE D CE2   1 
ATOM   15485 C  CZ    . PHE D 2 280 ? 149.318 109.277 136.225 1.00 21.30 ?  259 PHE D CZ    1 
ATOM   15486 N  N     . ILE D 2 281 ? 152.994 107.853 141.229 1.00 19.36 ?  260 ILE D N     1 
ATOM   15487 C  CA    . ILE D 2 281 ? 152.535 106.809 142.150 1.00 19.45 ?  260 ILE D CA    1 
ATOM   15488 C  C     . ILE D 2 281 ? 151.969 107.390 143.464 1.00 19.61 ?  260 ILE D C     1 
ATOM   15489 O  O     . ILE D 2 281 ? 150.883 106.995 143.892 1.00 19.72 ?  260 ILE D O     1 
ATOM   15490 C  CB    . ILE D 2 281 ? 153.679 105.799 142.425 1.00 19.49 ?  260 ILE D CB    1 
ATOM   15491 C  CG1   . ILE D 2 281 ? 154.019 105.044 141.136 1.00 20.10 ?  260 ILE D CG1   1 
ATOM   15492 C  CG2   . ILE D 2 281 ? 153.355 104.841 143.593 1.00 20.53 ?  260 ILE D CG2   1 
ATOM   15493 C  CD1   . ILE D 2 281 ? 155.347 104.287 141.236 1.00 21.17 ?  260 ILE D CD1   1 
ATOM   15494 N  N     . ARG D 2 282 ? 152.694 108.324 144.085 1.00 19.75 ?  261 ARG D N     1 
ATOM   15495 C  CA    . ARG D 2 282 ? 152.270 108.905 145.374 1.00 20.34 ?  261 ARG D CA    1 
ATOM   15496 C  C     . ARG D 2 282 ? 150.990 109.720 145.236 1.00 21.18 ?  261 ARG D C     1 
ATOM   15497 O  O     . ARG D 2 282 ? 150.098 109.663 146.095 1.00 21.68 ?  261 ARG D O     1 
ATOM   15498 C  CB    . ARG D 2 282 ? 153.386 109.753 145.998 1.00 20.20 ?  261 ARG D CB    1 
ATOM   15499 C  CG    . ARG D 2 282 ? 154.556 108.940 146.523 1.00 20.57 ?  261 ARG D CG    1 
ATOM   15500 C  CD    . ARG D 2 282 ? 155.551 109.821 147.281 1.00 23.15 ?  261 ARG D CD    1 
ATOM   15501 N  NE    . ARG D 2 282 ? 156.361 110.675 146.409 1.00 23.46 ?  261 ARG D NE    1 
ATOM   15502 C  CZ    . ARG D 2 282 ? 157.522 110.315 145.862 1.00 22.84 ?  261 ARG D CZ    1 
ATOM   15503 N  NH1   . ARG D 2 282 ? 158.014 109.099 146.058 1.00 23.37 1  261 ARG D NH1   1 
ATOM   15504 N  NH2   . ARG D 2 282 ? 158.188 111.177 145.106 1.00 22.27 ?  261 ARG D NH2   1 
ATOM   15505 N  N     . TYR D 2 283 ? 150.919 110.493 144.159 1.00 21.46 ?  262 TYR D N     1 
ATOM   15506 C  CA    . TYR D 2 283 ? 149.734 111.283 143.832 1.00 22.97 ?  262 TYR D CA    1 
ATOM   15507 C  C     . TYR D 2 283 ? 148.501 110.364 143.677 1.00 22.12 ?  262 TYR D C     1 
ATOM   15508 O  O     . TYR D 2 283 ? 147.420 110.667 144.188 1.00 22.00 ?  262 TYR D O     1 
ATOM   15509 C  CB    . TYR D 2 283 ? 150.027 112.102 142.570 1.00 23.37 ?  262 TYR D CB    1 
ATOM   15510 C  CG    . TYR D 2 283 ? 148.839 112.717 141.868 1.00 27.31 ?  262 TYR D CG    1 
ATOM   15511 C  CD1   . TYR D 2 283 ? 148.356 113.971 142.243 1.00 30.79 ?  262 TYR D CD1   1 
ATOM   15512 C  CD2   . TYR D 2 283 ? 148.227 112.064 140.799 1.00 30.31 ?  262 TYR D CD2   1 
ATOM   15513 C  CE1   . TYR D 2 283 ? 147.257 114.549 141.587 1.00 33.18 ?  262 TYR D CE1   1 
ATOM   15514 C  CE2   . TYR D 2 283 ? 147.139 112.633 140.129 1.00 33.20 ?  262 TYR D CE2   1 
ATOM   15515 C  CZ    . TYR D 2 283 ? 146.666 113.878 140.527 1.00 34.74 ?  262 TYR D CZ    1 
ATOM   15516 O  OH    . TYR D 2 283 ? 145.596 114.440 139.859 1.00 37.63 ?  262 TYR D OH    1 
ATOM   15517 N  N     . ASN D 2 284 ? 148.679 109.221 143.020 1.00 21.63 ?  263 ASN D N     1 
ATOM   15518 C  CA    . ASN D 2 284 ? 147.573 108.284 142.839 1.00 21.41 ?  263 ASN D CA    1 
ATOM   15519 C  C     . ASN D 2 284 ? 147.259 107.457 144.089 1.00 20.86 ?  263 ASN D C     1 
ATOM   15520 O  O     . ASN D 2 284 ? 146.108 107.100 144.313 1.00 20.92 ?  263 ASN D O     1 
ATOM   15521 C  CB    . ASN D 2 284 ? 147.776 107.416 141.596 1.00 21.15 ?  263 ASN D CB    1 
ATOM   15522 C  CG    . ASN D 2 284 ? 147.517 108.190 140.310 1.00 22.59 ?  263 ASN D CG    1 
ATOM   15523 O  OD1   . ASN D 2 284 ? 146.370 108.508 139.986 1.00 22.35 ?  263 ASN D OD1   1 
ATOM   15524 N  ND2   . ASN D 2 284 ? 148.582 108.510 139.580 1.00 22.93 ?  263 ASN D ND2   1 
ATOM   15525 N  N     . ALA D 2 285 ? 148.277 107.166 144.898 1.00 20.92 ?  264 ALA D N     1 
ATOM   15526 C  CA    . ALA D 2 285 ? 148.067 106.579 146.233 1.00 20.77 ?  264 ALA D CA    1 
ATOM   15527 C  C     . ALA D 2 285 ? 147.147 107.450 147.096 1.00 21.13 ?  264 ALA D C     1 
ATOM   15528 O  O     . ALA D 2 285 ? 146.241 106.935 147.765 1.00 19.92 ?  264 ALA D O     1 
ATOM   15529 C  CB    . ALA D 2 285 ? 149.407 106.336 146.942 1.00 20.68 ?  264 ALA D CB    1 
ATOM   15530 N  N     . ASN D 2 286 ? 147.381 108.767 147.070 1.00 21.38 ?  265 ASN D N     1 
ATOM   15531 C  CA    . ASN D 2 286 ? 146.533 109.731 147.776 1.00 21.94 ?  265 ASN D CA    1 
ATOM   15532 C  C     . ASN D 2 286 ? 145.079 109.714 147.269 1.00 22.13 ?  265 ASN D C     1 
ATOM   15533 O  O     . ASN D 2 286 ? 144.148 109.818 148.058 1.00 21.95 ?  265 ASN D O     1 
ATOM   15534 C  CB    . ASN D 2 286 ? 147.101 111.147 147.661 1.00 22.22 ?  265 ASN D CB    1 
ATOM   15535 C  CG    . ASN D 2 286 ? 148.257 111.415 148.619 1.00 22.80 ?  265 ASN D CG    1 
ATOM   15536 O  OD1   . ASN D 2 286 ? 148.521 110.653 149.556 1.00 22.57 ?  265 ASN D OD1   1 
ATOM   15537 N  ND2   . ASN D 2 286 ? 148.958 112.517 148.375 1.00 23.91 ?  265 ASN D ND2   1 
ATOM   15538 N  N     . LYS D 2 287 ? 144.891 109.576 145.958 1.00 22.51 ?  266 LYS D N     1 
ATOM   15539 C  CA    . LYS D 2 287 ? 143.537 109.466 145.397 1.00 22.91 ?  266 LYS D CA    1 
ATOM   15540 C  C     . LYS D 2 287 ? 142.833 108.194 145.887 1.00 22.33 ?  266 LYS D C     1 
ATOM   15541 O  O     . LYS D 2 287 ? 141.660 108.235 146.235 1.00 22.24 ?  266 LYS D O     1 
ATOM   15542 C  CB    . LYS D 2 287 ? 143.560 109.513 143.863 1.00 23.65 ?  266 LYS D CB    1 
ATOM   15543 C  CG    . LYS D 2 287 ? 143.814 110.908 143.292 1.00 26.50 ?  266 LYS D CG    1 
ATOM   15544 C  CD    . LYS D 2 287 ? 143.808 110.876 141.752 1.00 31.30 ?  266 LYS D CD    1 
ATOM   15545 C  CE    . LYS D 2 287 ? 143.555 112.266 141.196 1.00 35.08 ?  266 LYS D CE    1 
ATOM   15546 N  NZ    . LYS D 2 287 ? 143.498 112.316 139.704 1.00 37.66 1  266 LYS D NZ    1 
ATOM   15547 N  N     . ALA D 2 288 ? 143.567 107.080 145.921 1.00 21.41 ?  267 ALA D N     1 
ATOM   15548 C  CA    . ALA D 2 288 ? 143.059 105.798 146.409 1.00 21.53 ?  267 ALA D CA    1 
ATOM   15549 C  C     . ALA D 2 288 ? 142.622 105.884 147.882 1.00 21.77 ?  267 ALA D C     1 
ATOM   15550 O  O     . ALA D 2 288 ? 141.544 105.396 148.263 1.00 21.59 ?  267 ALA D O     1 
ATOM   15551 C  CB    . ALA D 2 288 ? 144.111 104.697 146.212 1.00 21.33 ?  267 ALA D CB    1 
ATOM   15552 N  N     . LEU D 2 289 ? 143.447 106.525 148.699 1.00 21.71 ?  268 LEU D N     1 
ATOM   15553 C  CA    . LEU D 2 289 ? 143.089 106.764 150.092 1.00 22.36 ?  268 LEU D CA    1 
ATOM   15554 C  C     . LEU D 2 289 ? 141.837 107.625 150.197 1.00 23.01 ?  268 LEU D C     1 
ATOM   15555 O  O     . LEU D 2 289 ? 140.923 107.308 150.962 1.00 23.14 ?  268 LEU D O     1 
ATOM   15556 C  CB    . LEU D 2 289 ? 144.261 107.382 150.864 1.00 22.61 ?  268 LEU D CB    1 
ATOM   15557 C  CG    . LEU D 2 289 ? 145.456 106.439 151.120 1.00 21.22 ?  268 LEU D CG    1 
ATOM   15558 C  CD1   . LEU D 2 289 ? 146.670 107.220 151.601 1.00 20.77 ?  268 LEU D CD1   1 
ATOM   15559 C  CD2   . LEU D 2 289 ? 145.104 105.315 152.120 1.00 21.40 ?  268 LEU D CD2   1 
ATOM   15560 N  N     . MET D 2 290 ? 141.769 108.698 149.416 1.00 23.87 ?  269 MET D N     1 
ATOM   15561 C  CA    . MET D 2 290 ? 140.574 109.536 149.451 1.00 25.26 ?  269 MET D CA    1 
ATOM   15562 C  C     . MET D 2 290 ? 139.317 108.763 149.018 1.00 24.37 ?  269 MET D C     1 
ATOM   15563 O  O     . MET D 2 290 ? 138.261 108.945 149.616 1.00 23.97 ?  269 MET D O     1 
ATOM   15564 C  CB    . MET D 2 290 ? 140.789 110.847 148.701 1.00 25.94 ?  269 MET D CB    1 
ATOM   15565 C  CG    . MET D 2 290 ? 141.586 111.850 149.557 1.00 31.08 ?  269 MET D CG    1 
ATOM   15566 S  SD    . MET D 2 290 ? 141.921 113.429 148.743 1.00 41.28 ?  269 MET D SD    1 
ATOM   15567 C  CE    . MET D 2 290 ? 140.260 113.924 148.217 1.00 38.56 ?  269 MET D CE    1 
ATOM   15568 N  N     . ASN D 2 291 ? 139.445 107.871 148.030 1.00 23.66 ?  270 ASN D N     1 
ATOM   15569 C  CA    . ASN D 2 291 ? 138.339 106.958 147.659 1.00 23.17 ?  270 ASN D CA    1 
ATOM   15570 C  C     . ASN D 2 291 ? 137.817 106.098 148.815 1.00 23.22 ?  270 ASN D C     1 
ATOM   15571 O  O     . ASN D 2 291 ? 136.641 105.739 148.845 1.00 22.68 ?  270 ASN D O     1 
ATOM   15572 C  CB    . ASN D 2 291 ? 138.726 106.043 146.487 1.00 22.41 ?  270 ASN D CB    1 
ATOM   15573 C  CG    . ASN D 2 291 ? 138.864 106.794 145.183 1.00 21.93 ?  270 ASN D CG    1 
ATOM   15574 O  OD1   . ASN D 2 291 ? 138.441 107.948 145.066 1.00 20.94 ?  270 ASN D OD1   1 
ATOM   15575 N  ND2   . ASN D 2 291 ? 139.460 106.143 144.187 1.00 19.20 ?  270 ASN D ND2   1 
ATOM   15576 N  N     . LEU D 2 292 ? 138.709 105.775 149.751 1.00 23.53 ?  271 LEU D N     1 
ATOM   15577 C  CA    . LEU D 2 292 ? 138.369 104.980 150.933 1.00 24.21 ?  271 LEU D CA    1 
ATOM   15578 C  C     . LEU D 2 292 ? 138.006 105.858 152.134 1.00 25.14 ?  271 LEU D C     1 
ATOM   15579 O  O     . LEU D 2 292 ? 137.869 105.365 153.265 1.00 25.14 ?  271 LEU D O     1 
ATOM   15580 C  CB    . LEU D 2 292 ? 139.528 104.022 151.284 1.00 23.71 ?  271 LEU D CB    1 
ATOM   15581 C  CG    . LEU D 2 292 ? 139.883 102.931 150.263 1.00 23.37 ?  271 LEU D CG    1 
ATOM   15582 C  CD1   . LEU D 2 292 ? 141.266 102.341 150.551 1.00 23.28 ?  271 LEU D CD1   1 
ATOM   15583 C  CD2   . LEU D 2 292 ? 138.814 101.822 150.217 1.00 23.06 ?  271 LEU D CD2   1 
ATOM   15584 N  N     . GLY D 2 293 ? 137.839 107.158 151.880 1.00 25.82 ?  272 GLY D N     1 
ATOM   15585 C  CA    . GLY D 2 293 ? 137.480 108.118 152.917 1.00 27.13 ?  272 GLY D CA    1 
ATOM   15586 C  C     . GLY D 2 293 ? 138.588 108.418 153.906 1.00 27.99 ?  272 GLY D C     1 
ATOM   15587 O  O     . GLY D 2 293 ? 138.320 108.917 154.995 1.00 27.97 ?  272 GLY D O     1 
ATOM   15588 N  N     . PHE D 2 294 ? 139.833 108.113 153.530 1.00 28.02 ?  273 PHE D N     1 
ATOM   15589 C  CA    . PHE D 2 294 ? 140.999 108.364 154.387 1.00 28.75 ?  273 PHE D CA    1 
ATOM   15590 C  C     . PHE D 2 294 ? 141.780 109.614 153.962 1.00 29.00 ?  273 PHE D C     1 
ATOM   15591 O  O     . PHE D 2 294 ? 141.664 110.067 152.825 1.00 28.74 ?  273 PHE D O     1 
ATOM   15592 C  CB    . PHE D 2 294 ? 141.941 107.148 154.380 1.00 28.32 ?  273 PHE D CB    1 
ATOM   15593 C  CG    . PHE D 2 294 ? 141.342 105.907 154.982 1.00 28.66 ?  273 PHE D CG    1 
ATOM   15594 C  CD1   . PHE D 2 294 ? 140.578 105.975 156.148 1.00 30.23 ?  273 PHE D CD1   1 
ATOM   15595 C  CD2   . PHE D 2 294 ? 141.555 104.668 154.392 1.00 26.94 ?  273 PHE D CD2   1 
ATOM   15596 C  CE1   . PHE D 2 294 ? 140.022 104.819 156.708 1.00 31.04 ?  273 PHE D CE1   1 
ATOM   15597 C  CE2   . PHE D 2 294 ? 141.015 103.513 154.940 1.00 27.39 ?  273 PHE D CE2   1 
ATOM   15598 C  CZ    . PHE D 2 294 ? 140.250 103.579 156.098 1.00 29.80 ?  273 PHE D CZ    1 
ATOM   15599 N  N     . ASP D 2 295 ? 142.570 110.161 154.883 1.00 29.60 ?  274 ASP D N     1 
ATOM   15600 C  CA    . ASP D 2 295 ? 143.419 111.315 154.597 1.00 30.40 ?  274 ASP D CA    1 
ATOM   15601 C  C     . ASP D 2 295 ? 144.584 110.945 153.659 1.00 29.58 ?  274 ASP D C     1 
ATOM   15602 O  O     . ASP D 2 295 ? 145.034 109.799 153.651 1.00 28.68 ?  274 ASP D O     1 
ATOM   15603 C  CB    . ASP D 2 295 ? 143.975 111.916 155.894 1.00 31.44 ?  274 ASP D CB    1 
ATOM   15604 C  CG    . ASP D 2 295 ? 142.893 112.508 156.790 1.00 34.27 ?  274 ASP D CG    1 
ATOM   15605 O  OD1   . ASP D 2 295 ? 141.842 112.961 156.274 1.00 36.43 ?  274 ASP D OD1   1 
ATOM   15606 O  OD2   . ASP D 2 295 ? 143.105 112.521 158.022 1.00 38.03 -1 274 ASP D OD2   1 
ATOM   15607 N  N     . PRO D 2 296 ? 145.080 111.921 152.875 1.00 29.59 ?  275 PRO D N     1 
ATOM   15608 C  CA    . PRO D 2 296 ? 146.250 111.630 152.041 1.00 29.09 ?  275 PRO D CA    1 
ATOM   15609 C  C     . PRO D 2 296 ? 147.455 111.261 152.904 1.00 29.26 ?  275 PRO D C     1 
ATOM   15610 O  O     . PRO D 2 296 ? 147.620 111.789 154.004 1.00 29.36 ?  275 PRO D O     1 
ATOM   15611 C  CB    . PRO D 2 296 ? 146.504 112.949 151.298 1.00 29.49 ?  275 PRO D CB    1 
ATOM   15612 C  CG    . PRO D 2 296 ? 145.774 114.002 152.085 1.00 30.28 ?  275 PRO D CG    1 
ATOM   15613 C  CD    . PRO D 2 296 ? 144.603 113.308 152.708 1.00 29.63 ?  275 PRO D CD    1 
ATOM   15614 N  N     . TYR D 2 297 ? 148.276 110.344 152.414 1.00 28.97 ?  276 TYR D N     1 
ATOM   15615 C  CA    . TYR D 2 297 ? 149.437 109.871 153.160 1.00 29.63 ?  276 TYR D CA    1 
ATOM   15616 C  C     . TYR D 2 297 ? 150.701 110.666 152.795 1.00 29.55 ?  276 TYR D C     1 
ATOM   15617 O  O     . TYR D 2 297 ? 151.573 110.905 153.640 1.00 30.12 ?  276 TYR D O     1 
ATOM   15618 C  CB    . TYR D 2 297 ? 149.645 108.388 152.853 1.00 29.49 ?  276 TYR D CB    1 
ATOM   15619 C  CG    . TYR D 2 297 ? 150.596 107.667 153.771 1.00 31.19 ?  276 TYR D CG    1 
ATOM   15620 C  CD1   . TYR D 2 297 ? 150.318 107.545 155.136 1.00 31.93 ?  276 TYR D CD1   1 
ATOM   15621 C  CD2   . TYR D 2 297 ? 151.763 107.082 153.276 1.00 31.98 ?  276 TYR D CD2   1 
ATOM   15622 C  CE1   . TYR D 2 297 ? 151.184 106.874 155.989 1.00 33.86 ?  276 TYR D CE1   1 
ATOM   15623 C  CE2   . TYR D 2 297 ? 152.637 106.400 154.123 1.00 33.88 ?  276 TYR D CE2   1 
ATOM   15624 C  CZ    . TYR D 2 297 ? 152.333 106.300 155.476 1.00 34.42 ?  276 TYR D CZ    1 
ATOM   15625 O  OH    . TYR D 2 297 ? 153.183 105.641 156.327 1.00 37.63 ?  276 TYR D OH    1 
ATOM   15626 N  N     . PHE D 2 298 ? 150.779 111.063 151.529 1.00 29.10 ?  277 PHE D N     1 
ATOM   15627 C  CA    . PHE D 2 298 ? 151.960 111.703 150.959 1.00 28.97 ?  277 PHE D CA    1 
ATOM   15628 C  C     . PHE D 2 298 ? 151.725 113.204 150.759 1.00 29.77 ?  277 PHE D C     1 
ATOM   15629 O  O     . PHE D 2 298 ? 150.599 113.633 150.492 1.00 29.07 ?  277 PHE D O     1 
ATOM   15630 C  CB    . PHE D 2 298 ? 152.309 111.056 149.614 1.00 27.99 ?  277 PHE D CB    1 
ATOM   15631 C  CG    . PHE D 2 298 ? 152.636 109.584 149.704 1.00 27.61 ?  277 PHE D CG    1 
ATOM   15632 C  CD1   . PHE D 2 298 ? 151.749 108.630 149.223 1.00 25.91 ?  277 PHE D CD1   1 
ATOM   15633 C  CD2   . PHE D 2 298 ? 153.846 109.157 150.254 1.00 27.32 ?  277 PHE D CD2   1 
ATOM   15634 C  CE1   . PHE D 2 298 ? 152.052 107.282 149.297 1.00 26.65 ?  277 PHE D CE1   1 
ATOM   15635 C  CE2   . PHE D 2 298 ? 154.163 107.813 150.333 1.00 25.38 ?  277 PHE D CE2   1 
ATOM   15636 C  CZ    . PHE D 2 298 ? 153.268 106.870 149.864 1.00 26.20 ?  277 PHE D CZ    1 
ATOM   15637 N  N     . GLU D 2 299 ? 152.792 113.990 150.896 1.00 31.10 ?  278 GLU D N     1 
ATOM   15638 C  CA    . GLU D 2 299 ? 152.748 115.426 150.603 1.00 32.86 ?  278 GLU D CA    1 
ATOM   15639 C  C     . GLU D 2 299 ? 152.389 115.646 149.127 1.00 33.04 ?  278 GLU D C     1 
ATOM   15640 O  O     . GLU D 2 299 ? 152.701 114.811 148.273 1.00 32.23 ?  278 GLU D O     1 
ATOM   15641 C  CB    . GLU D 2 299 ? 154.092 116.094 150.943 1.00 33.45 ?  278 GLU D CB    1 
ATOM   15642 C  CG    . GLU D 2 299 ? 155.273 115.553 150.122 1.00 36.27 ?  278 GLU D CG    1 
ATOM   15643 C  CD    . GLU D 2 299 ? 156.586 116.291 150.340 1.00 40.47 ?  278 GLU D CD    1 
ATOM   15644 O  OE1   . GLU D 2 299 ? 156.910 116.648 151.496 1.00 41.72 ?  278 GLU D OE1   1 
ATOM   15645 O  OE2   . GLU D 2 299 ? 157.309 116.483 149.338 1.00 42.65 -1 278 GLU D OE2   1 
ATOM   15646 N  N     . GLU D 2 300 ? 151.730 116.768 148.849 1.00 34.09 ?  279 GLU D N     1 
ATOM   15647 C  CA    . GLU D 2 300 ? 151.340 117.139 147.495 1.00 35.06 ?  279 GLU D CA    1 
ATOM   15648 C  C     . GLU D 2 300 ? 152.578 117.435 146.648 1.00 34.97 ?  279 GLU D C     1 
ATOM   15649 O  O     . GLU D 2 300 ? 153.502 118.115 147.096 1.00 34.96 ?  279 GLU D O     1 
ATOM   15650 C  CB    . GLU D 2 300 ? 150.397 118.355 147.530 1.00 35.81 ?  279 GLU D CB    1 
ATOM   15651 C  CG    . GLU D 2 300 ? 149.775 118.710 146.178 1.00 38.58 ?  279 GLU D CG    1 
ATOM   15652 C  CD    . GLU D 2 300 ? 148.457 119.471 146.304 1.00 43.09 ?  279 GLU D CD    1 
ATOM   15653 O  OE1   . GLU D 2 300 ? 147.442 118.992 145.748 1.00 44.69 ?  279 GLU D OE1   1 
ATOM   15654 O  OE2   . GLU D 2 300 ? 148.431 120.537 146.961 1.00 44.94 -1 279 GLU D OE2   1 
ATOM   15655 N  N     . GLU D 2 301 ? 152.591 116.892 145.434 1.00 34.73 ?  280 GLU D N     1 
ATOM   15656 C  CA    . GLU D 2 301 ? 153.678 117.104 144.487 1.00 35.16 ?  280 GLU D CA    1 
ATOM   15657 C  C     . GLU D 2 301 ? 153.089 117.459 143.132 1.00 35.23 ?  280 GLU D C     1 
ATOM   15658 O  O     . GLU D 2 301 ? 151.966 117.059 142.811 1.00 34.92 ?  280 GLU D O     1 
ATOM   15659 C  CB    . GLU D 2 301 ? 154.531 115.836 144.354 1.00 35.10 ?  280 GLU D CB    1 
ATOM   15660 C  CG    . GLU D 2 301 ? 155.559 115.632 145.465 1.00 36.62 ?  280 GLU D CG    1 
ATOM   15661 C  CD    . GLU D 2 301 ? 156.189 114.240 145.444 1.00 37.59 ?  280 GLU D CD    1 
ATOM   15662 O  OE1   . GLU D 2 301 ? 155.448 113.238 145.519 1.00 38.10 ?  280 GLU D OE1   1 
ATOM   15663 O  OE2   . GLU D 2 301 ? 157.431 114.145 145.378 1.00 38.93 -1 280 GLU D OE2   1 
ATOM   15664 N  N     . ASP D 2 302 ? 153.842 118.208 142.336 1.00 35.60 ?  281 ASP D N     1 
ATOM   15665 C  CA    . ASP D 2 302 ? 153.418 118.501 140.972 1.00 35.96 ?  281 ASP D CA    1 
ATOM   15666 C  C     . ASP D 2 302 ? 153.739 117.296 140.097 1.00 35.01 ?  281 ASP D C     1 
ATOM   15667 O  O     . ASP D 2 302 ? 154.656 116.533 140.404 1.00 35.52 ?  281 ASP D O     1 
ATOM   15668 C  CB    . ASP D 2 302 ? 154.067 119.794 140.448 1.00 36.82 ?  281 ASP D CB    1 
ATOM   15669 C  CG    . ASP D 2 302 ? 155.601 119.711 140.341 1.00 39.01 ?  281 ASP D CG    1 
ATOM   15670 O  OD1   . ASP D 2 302 ? 156.243 118.861 141.007 1.00 40.83 ?  281 ASP D OD1   1 
ATOM   15671 O  OD2   . ASP D 2 302 ? 156.168 120.531 139.591 1.00 41.13 -1 281 ASP D OD2   1 
ATOM   15672 N  N     . ILE D 2 303 ? 152.969 117.096 139.036 1.00 33.94 ?  282 ILE D N     1 
ATOM   15673 C  CA    . ILE D 2 303 ? 153.190 115.959 138.147 1.00 33.00 ?  282 ILE D CA    1 
ATOM   15674 C  C     . ILE D 2 303 ? 153.823 116.381 136.814 1.00 31.59 ?  282 ILE D C     1 
ATOM   15675 O  O     . ILE D 2 303 ? 153.635 117.513 136.362 1.00 31.14 ?  282 ILE D O     1 
ATOM   15676 C  CB    . ILE D 2 303 ? 151.885 115.120 137.959 1.00 33.44 ?  282 ILE D CB    1 
ATOM   15677 C  CG1   . ILE D 2 303 ? 151.829 114.443 136.584 1.00 34.29 ?  282 ILE D CG1   1 
ATOM   15678 C  CG2   . ILE D 2 303 ? 150.654 115.978 138.205 1.00 35.47 ?  282 ILE D CG2   1 
ATOM   15679 C  CD1   . ILE D 2 303 ? 150.502 113.783 136.269 1.00 36.30 ?  282 ILE D CD1   1 
ATOM   15680 N  N     . ASN D 2 304 ? 154.591 115.474 136.211 1.00 29.53 ?  283 ASN D N     1 
ATOM   15681 C  CA    . ASN D 2 304 ? 155.183 115.707 134.897 1.00 28.49 ?  283 ASN D CA    1 
ATOM   15682 C  C     . ASN D 2 304 ? 154.153 116.293 133.907 1.00 27.87 ?  283 ASN D C     1 
ATOM   15683 O  O     . ASN D 2 304 ? 153.091 115.708 133.704 1.00 27.02 ?  283 ASN D O     1 
ATOM   15684 C  CB    . ASN D 2 304 ? 155.770 114.404 134.350 1.00 28.20 ?  283 ASN D CB    1 
ATOM   15685 C  CG    . ASN D 2 304 ? 156.478 114.599 133.036 1.00 28.17 ?  283 ASN D CG    1 
ATOM   15686 O  OD1   . ASN D 2 304 ? 155.854 114.575 131.980 1.00 29.01 ?  283 ASN D OD1   1 
ATOM   15687 N  ND2   . ASN D 2 304 ? 157.786 114.793 133.089 1.00 27.24 ?  283 ASN D ND2   1 
ATOM   15688 N  N     . PRO D 2 305 ? 154.462 117.459 133.303 1.00 28.00 ?  284 PRO D N     1 
ATOM   15689 C  CA    . PRO D 2 305 ? 153.485 118.142 132.440 1.00 27.58 ?  284 PRO D CA    1 
ATOM   15690 C  C     . PRO D 2 305 ? 153.134 117.390 131.154 1.00 27.01 ?  284 PRO D C     1 
ATOM   15691 O  O     . PRO D 2 305 ? 152.055 117.592 130.607 1.00 26.66 ?  284 PRO D O     1 
ATOM   15692 C  CB    . PRO D 2 305 ? 154.167 119.476 132.109 1.00 28.21 ?  284 PRO D CB    1 
ATOM   15693 C  CG    . PRO D 2 305 ? 155.594 119.269 132.365 1.00 28.80 ?  284 PRO D CG    1 
ATOM   15694 C  CD    . PRO D 2 305 ? 155.667 118.283 133.510 1.00 28.11 ?  284 PRO D CD    1 
ATOM   15695 N  N     . ILE D 2 306 ? 154.033 116.531 130.682 1.00 26.52 ?  285 ILE D N     1 
ATOM   15696 C  CA    . ILE D 2 306 ? 153.758 115.730 129.495 1.00 26.50 ?  285 ILE D CA    1 
ATOM   15697 C  C     . ILE D 2 306 ? 152.687 114.676 129.811 1.00 26.43 ?  285 ILE D C     1 
ATOM   15698 O  O     . ILE D 2 306 ? 151.702 114.522 129.075 1.00 26.00 ?  285 ILE D O     1 
ATOM   15699 C  CB    . ILE D 2 306 ? 155.047 115.100 128.911 1.00 26.88 ?  285 ILE D CB    1 
ATOM   15700 C  CG1   . ILE D 2 306 ? 156.033 116.212 128.509 1.00 26.98 ?  285 ILE D CG1   1 
ATOM   15701 C  CG2   . ILE D 2 306 ? 154.699 114.193 127.732 1.00 24.94 ?  285 ILE D CG2   1 
ATOM   15702 C  CD1   . ILE D 2 306 ? 157.401 115.737 128.102 1.00 26.65 ?  285 ILE D CD1   1 
ATOM   15703 N  N     . VAL D 2 307 ? 152.872 113.982 130.929 1.00 26.36 ?  286 VAL D N     1 
ATOM   15704 C  CA    . VAL D 2 307 ? 151.860 113.067 131.441 1.00 26.71 ?  286 VAL D CA    1 
ATOM   15705 C  C     . VAL D 2 307 ? 150.542 113.790 131.738 1.00 27.68 ?  286 VAL D C     1 
ATOM   15706 O  O     . VAL D 2 307 ? 149.477 113.273 131.399 1.00 27.92 ?  286 VAL D O     1 
ATOM   15707 C  CB    . VAL D 2 307 ? 152.381 112.260 132.661 1.00 26.37 ?  286 VAL D CB    1 
ATOM   15708 C  CG1   . VAL D 2 307 ? 151.248 111.487 133.354 1.00 25.48 ?  286 VAL D CG1   1 
ATOM   15709 C  CG2   . VAL D 2 307 ? 153.435 111.306 132.199 1.00 25.55 ?  286 VAL D CG2   1 
ATOM   15710 N  N     . LEU D 2 308 ? 150.604 114.990 132.323 1.00 28.80 ?  287 LEU D N     1 
ATOM   15711 C  CA    . LEU D 2 308 ? 149.384 115.792 132.519 1.00 30.07 ?  287 LEU D CA    1 
ATOM   15712 C  C     . LEU D 2 308 ? 148.659 116.091 131.203 1.00 30.38 ?  287 LEU D C     1 
ATOM   15713 O  O     . LEU D 2 308 ? 147.428 116.016 131.128 1.00 30.71 ?  287 LEU D O     1 
ATOM   15714 C  CB    . LEU D 2 308 ? 149.680 117.096 133.265 1.00 30.86 ?  287 LEU D CB    1 
ATOM   15715 C  CG    . LEU D 2 308 ? 149.720 116.996 134.794 1.00 32.62 ?  287 LEU D CG    1 
ATOM   15716 C  CD1   . LEU D 2 308 ? 150.221 118.287 135.402 1.00 33.97 ?  287 LEU D CD1   1 
ATOM   15717 C  CD2   . LEU D 2 308 ? 148.344 116.617 135.372 1.00 34.73 ?  287 LEU D CD2   1 
ATOM   15718 N  N     . ASN D 2 309 ? 149.420 116.418 130.165 1.00 30.81 ?  288 ASN D N     1 
ATOM   15719 C  CA    . ASN D 2 309 ? 148.833 116.674 128.854 1.00 31.25 ?  288 ASN D CA    1 
ATOM   15720 C  C     . ASN D 2 309 ? 148.172 115.421 128.277 1.00 31.83 ?  288 ASN D C     1 
ATOM   15721 O  O     . ASN D 2 309 ? 147.151 115.511 127.588 1.00 31.73 ?  288 ASN D O     1 
ATOM   15722 C  CB    . ASN D 2 309 ? 149.863 117.255 127.879 1.00 31.21 ?  288 ASN D CB    1 
ATOM   15723 C  CG    . ASN D 2 309 ? 149.229 117.714 126.576 1.00 31.41 ?  288 ASN D CG    1 
ATOM   15724 O  OD1   . ASN D 2 309 ? 148.175 118.361 126.580 1.00 31.88 ?  288 ASN D OD1   1 
ATOM   15725 N  ND2   . ASN D 2 309 ? 149.859 117.376 125.455 1.00 29.12 ?  288 ASN D ND2   1 
ATOM   15726 N  N     . GLY D 2 310 ? 148.756 114.259 128.570 1.00 32.04 ?  289 GLY D N     1 
ATOM   15727 C  CA    . GLY D 2 310 ? 148.156 112.976 128.221 1.00 33.04 ?  289 GLY D CA    1 
ATOM   15728 C  C     . GLY D 2 310 ? 146.856 112.745 128.981 1.00 33.85 ?  289 GLY D C     1 
ATOM   15729 O  O     . GLY D 2 310 ? 145.846 112.371 128.385 1.00 34.05 ?  289 GLY D O     1 
ATOM   15730 N  N     . LEU D 2 311 ? 146.885 112.973 130.293 1.00 34.33 ?  290 LEU D N     1 
ATOM   15731 C  CA    . LEU D 2 311 ? 145.722 112.774 131.162 1.00 35.77 ?  290 LEU D CA    1 
ATOM   15732 C  C     . LEU D 2 311 ? 144.539 113.667 130.801 1.00 37.01 ?  290 LEU D C     1 
ATOM   15733 O  O     . LEU D 2 311 ? 143.390 113.225 130.831 1.00 37.18 ?  290 LEU D O     1 
ATOM   15734 C  CB    . LEU D 2 311 ? 146.093 113.026 132.629 1.00 35.50 ?  290 LEU D CB    1 
ATOM   15735 C  CG    . LEU D 2 311 ? 146.595 111.904 133.532 1.00 35.45 ?  290 LEU D CG    1 
ATOM   15736 C  CD1   . LEU D 2 311 ? 147.061 112.503 134.869 1.00 35.28 ?  290 LEU D CD1   1 
ATOM   15737 C  CD2   . LEU D 2 311 ? 145.531 110.829 133.769 1.00 34.16 ?  290 LEU D CD2   1 
ATOM   15738 N  N     . LYS D 2 330 ? 117.778 117.744 148.442 1.00 61.72 ?  309 LYS D N     1 
ATOM   15739 C  CA    . LYS D 2 330 ? 116.487 117.069 148.409 1.00 61.83 ?  309 LYS D CA    1 
ATOM   15740 C  C     . LYS D 2 330 ? 116.132 116.507 149.778 1.00 62.21 ?  309 LYS D C     1 
ATOM   15741 O  O     . LYS D 2 330 ? 116.390 115.333 150.048 1.00 61.32 ?  309 LYS D O     1 
ATOM   15742 C  CB    . LYS D 2 330 ? 116.494 115.932 147.383 1.00 59.60 ?  309 LYS D CB    1 
ATOM   15743 C  CG    . LYS D 2 330 ? 117.084 116.285 146.031 1.00 60.95 ?  309 LYS D CG    1 
ATOM   15744 C  CD    . LYS D 2 330 ? 116.078 116.055 144.914 1.00 60.77 ?  309 LYS D CD    1 
ATOM   15745 C  CE    . LYS D 2 330 ? 116.507 116.749 143.632 1.00 61.40 ?  309 LYS D CE    1 
ATOM   15746 N  NZ    . LYS D 2 330 ? 115.686 117.957 143.348 1.00 62.04 1  309 LYS D NZ    1 
ATOM   15747 N  N     . ALA D 2 331 ? 115.553 117.327 150.654 1.00 57.72 ?  310 ALA D N     1 
ATOM   15748 C  CA    . ALA D 2 331 ? 115.157 116.816 151.958 1.00 58.04 ?  310 ALA D CA    1 
ATOM   15749 C  C     . ALA D 2 331 ? 113.809 116.107 151.917 1.00 58.14 ?  310 ALA D C     1 
ATOM   15750 O  O     . ALA D 2 331 ? 113.757 114.881 152.057 1.00 58.87 ?  310 ALA D O     1 
ATOM   15751 C  CB    . ALA D 2 331 ? 115.115 117.959 152.979 1.00 56.57 ?  310 ALA D CB    1 
ATOM   15752 N  N     . THR D 2 332 ? 112.719 116.852 151.722 1.00 46.15 ?  311 THR D N     1 
ATOM   15753 C  CA    . THR D 2 332 ? 111.415 116.296 151.371 1.00 42.78 ?  311 THR D CA    1 
ATOM   15754 C  C     . THR D 2 332 ? 110.456 117.405 150.947 1.00 42.27 ?  311 THR D C     1 
ATOM   15755 O  O     . THR D 2 332 ? 110.112 118.273 151.756 1.00 45.09 ?  311 THR D O     1 
ATOM   15756 C  CB    . THR D 2 332 ? 110.837 115.474 152.530 1.00 46.86 ?  311 THR D CB    1 
ATOM   15757 O  OG1   . THR D 2 332 ? 109.666 114.768 152.097 1.00 46.97 ?  311 THR D OG1   1 
ATOM   15758 C  CG2   . THR D 2 332 ? 110.532 116.346 153.732 1.00 43.65 ?  311 THR D CG2   1 
ATOM   15759 N  N     . VAL D 2 333 ? 110.016 117.388 149.691 1.00 39.49 ?  312 VAL D N     1 
ATOM   15760 C  CA    . VAL D 2 333 ? 109.065 118.382 149.203 1.00 35.97 ?  312 VAL D CA    1 
ATOM   15761 C  C     . VAL D 2 333 ? 107.718 118.170 149.883 1.00 40.19 ?  312 VAL D C     1 
ATOM   15762 O  O     . VAL D 2 333 ? 107.156 117.070 149.839 1.00 43.38 ?  312 VAL D O     1 
ATOM   15763 C  CB    . VAL D 2 333 ? 108.926 118.319 147.671 1.00 38.60 ?  312 VAL D CB    1 
ATOM   15764 C  CG1   . VAL D 2 333 ? 107.595 118.909 147.225 1.00 39.63 ?  312 VAL D CG1   1 
ATOM   15765 C  CG2   . VAL D 2 333 ? 110.084 119.042 147.003 1.00 39.03 ?  312 VAL D CG2   1 
ATOM   15766 N  N     . GLU D 2 334 ? 107.196 119.216 150.521 1.00 39.20 ?  313 GLU D N     1 
ATOM   15767 C  CA    . GLU D 2 334 ? 105.863 119.188 151.114 1.00 36.81 ?  313 GLU D CA    1 
ATOM   15768 C  C     . GLU D 2 334 ? 105.142 120.469 150.718 1.00 37.73 ?  313 GLU D C     1 
ATOM   15769 O  O     . GLU D 2 334 ? 105.718 121.568 150.853 1.00 40.12 ?  313 GLU D O     1 
ATOM   15770 C  CB    . GLU D 2 334 ? 105.918 119.040 152.636 1.00 34.61 ?  313 GLU D CB    1 
ATOM   15771 C  CG    . GLU D 2 334 ? 104.550 118.834 153.268 1.00 37.90 ?  313 GLU D CG    1 
ATOM   15772 C  CD    . GLU D 2 334 ? 104.604 118.662 154.772 1.00 39.43 ?  313 GLU D CD    1 
ATOM   15773 O  OE1   . GLU D 2 334 ? 105.717 118.583 155.324 1.00 37.54 ?  313 GLU D OE1   1 
ATOM   15774 O  OE2   . GLU D 2 334 ? 103.529 118.601 155.402 1.00 39.69 -1 313 GLU D OE2   1 
ATOM   15775 N  N     . PRO D 2 335 ? 103.909 120.391 150.224 1.00 38.18 ?  314 PRO D N     1 
ATOM   15776 C  CA    . PRO D 2 335 ? 103.206 121.606 149.802 1.00 40.62 ?  314 PRO D CA    1 
ATOM   15777 C  C     . PRO D 2 335 ? 102.788 122.467 150.984 1.00 40.02 ?  314 PRO D C     1 
ATOM   15778 O  O     . PRO D 2 335 ? 102.624 121.990 152.108 1.00 41.11 ?  314 PRO D O     1 
ATOM   15779 C  CB    . PRO D 2 335 ? 101.983 121.062 149.057 1.00 37.91 ?  314 PRO D CB    1 
ATOM   15780 C  CG    . PRO D 2 335 ? 101.743 119.729 149.680 1.00 34.58 ?  314 PRO D CG    1 
ATOM   15781 C  CD    . PRO D 2 335 ? 103.108 119.178 149.985 1.00 36.60 ?  314 PRO D CD    1 
ATOM   15782 N  N     . LEU D 2 336 ? 102.627 123.760 150.712 1.00 34.57 ?  315 LEU D N     1 
ATOM   15783 C  CA    . LEU D 2 336 ? 102.054 124.677 151.686 1.00 30.08 ?  315 LEU D CA    1 
ATOM   15784 C  C     . LEU D 2 336 ? 100.540 124.504 151.706 1.00 33.20 ?  315 LEU D C     1 
ATOM   15785 O  O     . LEU D 2 336 ? 99.869  124.730 150.695 1.00 37.22 ?  315 LEU D O     1 
ATOM   15786 C  CB    . LEU D 2 336 ? 102.422 126.120 151.341 1.00 28.04 ?  315 LEU D CB    1 
ATOM   15787 C  CG    . LEU D 2 336 ? 103.831 126.585 151.711 1.00 27.76 ?  315 LEU D CG    1 
ATOM   15788 C  CD1   . LEU D 2 336 ? 104.260 127.741 150.822 1.00 24.11 ?  315 LEU D CD1   1 
ATOM   15789 C  CD2   . LEU D 2 336 ? 103.889 126.984 153.173 1.00 29.08 ?  315 LEU D CD2   1 
ATOM   15790 N  N     . LYS D 2 337 ? 100.004 124.106 152.858 1.00 36.25 ?  316 LYS D N     1 
ATOM   15791 C  CA    . LYS D 2 337 ? 98.600  123.729 152.978 1.00 47.76 ?  316 LYS D CA    1 
ATOM   15792 C  C     . LYS D 2 337 ? 97.782  124.807 153.680 1.00 47.26 ?  316 LYS D C     1 
ATOM   15793 O  O     . LYS D 2 337 ? 96.854  124.495 154.430 1.00 51.37 ?  316 LYS D O     1 
ATOM   15794 C  CB    . LYS D 2 337 ? 98.463  122.397 153.712 1.00 44.37 ?  316 LYS D CB    1 
ATOM   15795 C  CG    . LYS D 2 337 ? 99.411  122.244 154.889 1.00 46.03 ?  316 LYS D CG    1 
ATOM   15796 C  CD    . LYS D 2 337 ? 99.862  120.803 155.057 1.00 46.40 ?  316 LYS D CD    1 
ATOM   15797 C  CE    . LYS D 2 337 ? 100.421 120.247 153.758 1.00 45.29 ?  316 LYS D CE    1 
ATOM   15798 N  NZ    . LYS D 2 337 ? 101.278 119.054 153.988 1.00 42.09 1  316 LYS D NZ    1 
ATOM   15799 N  N     . ASP D 2 338 ? 98.123  126.076 153.444 1.00 29.55 ?  317 ASP D N     1 
ATOM   15800 C  CA    . ASP D 2 338 ? 97.464  127.222 154.065 1.00 32.48 ?  317 ASP D CA    1 
ATOM   15801 C  C     . ASP D 2 338 ? 97.613  127.205 155.582 1.00 37.94 ?  317 ASP D C     1 
ATOM   15802 O  O     . ASP D 2 338 ? 98.074  126.215 156.159 1.00 40.84 ?  317 ASP D O     1 
ATOM   15803 C  CB    . ASP D 2 338 ? 95.985  127.280 153.674 1.00 36.01 ?  317 ASP D CB    1 
ATOM   15804 C  CG    . ASP D 2 338 ? 95.443  128.693 153.672 1.00 38.86 ?  317 ASP D CG    1 
ATOM   15805 O  OD1   . ASP D 2 338 ? 96.229  129.628 153.934 1.00 36.19 ?  317 ASP D OD1   1 
ATOM   15806 O  OD2   . ASP D 2 338 ? 94.235  128.870 153.409 1.00 34.94 -1 317 ASP D OD2   1 
ATOM   15807 N  N     . ASP D 2 339 ? 97.274  128.327 156.224 1.00 32.37 ?  318 ASP D N     1 
ATOM   15808 C  CA    . ASP D 2 339 ? 97.449  128.533 157.661 1.00 28.49 ?  318 ASP D CA    1 
ATOM   15809 C  C     . ASP D 2 339 ? 98.931  128.588 158.015 1.00 28.80 ?  318 ASP D C     1 
ATOM   15810 O  O     . ASP D 2 339 ? 99.293  128.831 159.169 1.00 36.28 ?  318 ASP D O     1 
ATOM   15811 C  CB    . ASP D 2 339 ? 96.735  127.451 158.475 1.00 30.55 ?  318 ASP D CB    1 
ATOM   15812 C  CG    . ASP D 2 339 ? 95.858  128.030 159.569 1.00 37.05 ?  318 ASP D CG    1 
ATOM   15813 O  OD1   . ASP D 2 339 ? 96.212  129.099 160.111 1.00 32.14 ?  318 ASP D OD1   1 
ATOM   15814 O  OD2   . ASP D 2 339 ? 94.817  127.418 159.887 1.00 39.30 -1 318 ASP D OD2   1 
ATOM   15815 N  N     . ASP D 2 340 ? 99.793  128.362 157.023 1.00 24.72 ?  319 ASP D N     1 
ATOM   15816 C  CA    . ASP D 2 340 ? 101.217 128.621 157.140 1.00 24.52 ?  319 ASP D CA    1 
ATOM   15817 C  C     . ASP D 2 340 ? 101.563 130.065 156.818 1.00 21.51 ?  319 ASP D C     1 
ATOM   15818 O  O     . ASP D 2 340 ? 102.694 130.491 157.070 1.00 32.71 ?  319 ASP D O     1 
ATOM   15819 C  CB    . ASP D 2 340 ? 102.001 127.686 156.214 1.00 23.05 ?  319 ASP D CB    1 
ATOM   15820 C  CG    . ASP D 2 340 ? 101.914 126.234 156.641 1.00 28.00 ?  319 ASP D CG    1 
ATOM   15821 O  OD1   . ASP D 2 340 ? 101.797 125.974 157.856 1.00 34.28 ?  319 ASP D OD1   1 
ATOM   15822 O  OD2   . ASP D 2 340 ? 101.961 125.350 155.760 1.00 31.08 -1 319 ASP D OD2   1 
ATOM   15823 N  N     . PHE D 2 341 ? 100.614 130.816 156.264 1.00 10.52 ?  320 PHE D N     1 
ATOM   15824 C  CA    . PHE D 2 341 ? 100.767 132.236 155.997 1.00 15.27 ?  320 PHE D CA    1 
ATOM   15825 C  C     . PHE D 2 341 ? 100.191 133.096 157.109 1.00 12.85 ?  320 PHE D C     1 
ATOM   15826 O  O     . PHE D 2 341 ? 100.223 134.326 157.006 1.00 22.40 ?  320 PHE D O     1 
ATOM   15827 C  CB    . PHE D 2 341 ? 100.093 132.596 154.669 1.00 21.01 ?  320 PHE D CB    1 
ATOM   15828 C  CG    . PHE D 2 341 ? 100.682 131.895 153.476 1.00 15.79 ?  320 PHE D CG    1 
ATOM   15829 C  CD1   . PHE D 2 341 ? 100.266 130.621 153.132 1.00 11.88 ?  320 PHE D CD1   1 
ATOM   15830 C  CD2   . PHE D 2 341 ? 101.643 132.512 152.697 1.00 9.87  ?  320 PHE D CD2   1 
ATOM   15831 C  CE1   . PHE D 2 341 ? 100.803 129.975 152.038 1.00 13.02 ?  320 PHE D CE1   1 
ATOM   15832 C  CE2   . PHE D 2 341 ? 102.183 131.870 151.601 1.00 10.78 ?  320 PHE D CE2   1 
ATOM   15833 C  CZ    . PHE D 2 341 ? 101.763 130.600 151.273 1.00 4.79  ?  320 PHE D CZ    1 
ATOM   15834 N  N     . TYR D 2 342 ? 99.666  132.479 158.163 1.00 12.46 ?  321 TYR D N     1 
ATOM   15835 C  CA    . TYR D 2 342 ? 99.051  133.186 159.275 1.00 17.95 ?  321 TYR D CA    1 
ATOM   15836 C  C     . TYR D 2 342 ? 99.730  132.763 160.566 1.00 22.41 ?  321 TYR D C     1 
ATOM   15837 O  O     . TYR D 2 342 ? 100.059 131.586 160.747 1.00 24.04 ?  321 TYR D O     1 
ATOM   15838 C  CB    . TYR D 2 342 ? 97.549  132.899 159.348 1.00 13.28 ?  321 TYR D CB    1 
ATOM   15839 C  CG    . TYR D 2 342 ? 96.783  133.373 158.136 1.00 11.63 ?  321 TYR D CG    1 
ATOM   15840 C  CD1   . TYR D 2 342 ? 96.354  134.690 158.031 1.00 16.81 ?  321 TYR D CD1   1 
ATOM   15841 C  CD2   . TYR D 2 342 ? 96.494  132.505 157.093 1.00 15.94 ?  321 TYR D CD2   1 
ATOM   15842 C  CE1   . TYR D 2 342 ? 95.656  135.125 156.922 1.00 20.80 ?  321 TYR D CE1   1 
ATOM   15843 C  CE2   . TYR D 2 342 ? 95.796  132.931 155.981 1.00 15.55 ?  321 TYR D CE2   1 
ATOM   15844 C  CZ    . TYR D 2 342 ? 95.380  134.243 155.900 1.00 24.69 ?  321 TYR D CZ    1 
ATOM   15845 O  OH    . TYR D 2 342 ? 94.684  134.674 154.794 1.00 21.45 ?  321 TYR D OH    1 
ATOM   15846 N  N     . PHE D 2 343 ? 99.944  133.724 161.457 1.00 12.93 ?  322 PHE D N     1 
ATOM   15847 C  CA    . PHE D 2 343 ? 100.652 133.463 162.705 1.00 18.66 ?  322 PHE D CA    1 
ATOM   15848 C  C     . PHE D 2 343 ? 99.967  134.152 163.879 1.00 24.79 ?  322 PHE D C     1 
ATOM   15849 O  O     . PHE D 2 343 ? 99.642  135.336 163.815 1.00 23.91 ?  322 PHE D O     1 
ATOM   15850 C  CB    . PHE D 2 343 ? 102.110 133.923 162.597 1.00 13.99 ?  322 PHE D CB    1 
ATOM   15851 C  CG    . PHE D 2 343 ? 102.776 133.526 161.310 1.00 14.21 ?  322 PHE D CG    1 
ATOM   15852 C  CD1   . PHE D 2 343 ? 102.737 134.360 160.205 1.00 13.48 ?  322 PHE D CD1   1 
ATOM   15853 C  CD2   . PHE D 2 343 ? 103.439 132.317 161.204 1.00 16.65 ?  322 PHE D CD2   1 
ATOM   15854 C  CE1   . PHE D 2 343 ? 103.343 133.992 159.022 1.00 9.34  ?  322 PHE D CE1   1 
ATOM   15855 C  CE2   . PHE D 2 343 ? 104.047 131.947 160.023 1.00 9.50  ?  322 PHE D CE2   1 
ATOM   15856 C  CZ    . PHE D 2 343 ? 103.998 132.786 158.932 1.00 5.03  ?  322 PHE D CZ    1 
HETATM 15857 P  PA    . TTP E 3 .   ? 146.150 144.549 134.187 1.00 19.37 ?  801 TTP A PA    1 
HETATM 15858 O  O1A   . TTP E 3 .   ? 144.725 145.022 134.084 1.00 21.91 -1 801 TTP A O1A   1 
HETATM 15859 O  O2A   . TTP E 3 .   ? 147.052 145.368 133.298 1.00 26.56 ?  801 TTP A O2A   1 
HETATM 15860 O  O3A   . TTP E 3 .   ? 146.633 144.532 135.720 1.00 35.02 ?  801 TTP A O3A   1 
HETATM 15861 P  PB    . TTP E 3 .   ? 147.725 145.569 136.279 1.00 29.77 ?  801 TTP A PB    1 
HETATM 15862 O  O1B   . TTP E 3 .   ? 147.362 145.976 137.683 1.00 33.96 -1 801 TTP A O1B   1 
HETATM 15863 O  O2B   . TTP E 3 .   ? 147.883 146.788 135.408 1.00 25.37 ?  801 TTP A O2B   1 
HETATM 15864 O  O3B   . TTP E 3 .   ? 149.039 144.642 136.267 1.00 28.38 ?  801 TTP A O3B   1 
HETATM 15865 P  PG    . TTP E 3 .   ? 150.401 145.099 135.544 1.00 32.16 ?  801 TTP A PG    1 
HETATM 15866 O  O1G   . TTP E 3 .   ? 150.101 145.664 134.178 1.00 33.52 ?  801 TTP A O1G   1 
HETATM 15867 O  O2G   . TTP E 3 .   ? 151.297 143.896 135.399 1.00 23.47 -1 801 TTP A O2G   1 
HETATM 15868 O  O3G   . TTP E 3 .   ? 151.102 146.144 136.376 1.00 34.78 ?  801 TTP A O3G   1 
HETATM 15869 O  "O5'" . TTP E 3 .   ? 146.267 142.998 133.800 1.00 18.77 ?  801 TTP A "O5'" 1 
HETATM 15870 C  "C5'" . TTP E 3 .   ? 147.197 142.620 132.793 1.00 25.04 ?  801 TTP A "C5'" 1 
HETATM 15871 C  "C4'" . TTP E 3 .   ? 146.980 141.168 132.403 1.00 26.93 ?  801 TTP A "C4'" 1 
HETATM 15872 O  "O4'" . TTP E 3 .   ? 146.640 140.401 133.556 1.00 30.38 ?  801 TTP A "O4'" 1 
HETATM 15873 C  "C3'" . TTP E 3 .   ? 145.830 141.038 131.426 1.00 25.75 ?  801 TTP A "C3'" 1 
HETATM 15874 O  "O3'" . TTP E 3 .   ? 146.323 140.742 130.117 1.00 30.86 ?  801 TTP A "O3'" 1 
HETATM 15875 C  "C2'" . TTP E 3 .   ? 144.993 139.885 131.934 1.00 28.56 ?  801 TTP A "C2'" 1 
HETATM 15876 C  "C1'" . TTP E 3 .   ? 145.646 139.429 133.228 1.00 25.58 ?  801 TTP A "C1'" 1 
HETATM 15877 N  N1    . TTP E 3 .   ? 144.648 139.354 134.294 1.00 26.58 ?  801 TTP A N1    1 
HETATM 15878 C  C2    . TTP E 3 .   ? 144.067 138.109 134.617 1.00 30.61 ?  801 TTP A C2    1 
HETATM 15879 O  O2    . TTP E 3 .   ? 144.420 137.089 133.990 1.00 27.38 ?  801 TTP A O2    1 
HETATM 15880 N  N3    . TTP E 3 .   ? 143.151 137.995 135.587 1.00 28.52 ?  801 TTP A N3    1 
HETATM 15881 C  C4    . TTP E 3 .   ? 142.759 139.069 136.274 1.00 31.97 ?  801 TTP A C4    1 
HETATM 15882 O  O4    . TTP E 3 .   ? 141.904 138.965 137.178 1.00 33.14 ?  801 TTP A O4    1 
HETATM 15883 C  C5    . TTP E 3 .   ? 143.352 140.387 135.951 1.00 26.42 ?  801 TTP A C5    1 
HETATM 15884 C  C5M   . TTP E 3 .   ? 142.937 141.620 136.705 1.00 26.94 ?  801 TTP A C5M   1 
HETATM 15885 C  C6    . TTP E 3 .   ? 144.298 140.467 134.943 1.00 25.12 ?  801 TTP A C6    1 
HETATM 15886 MG MG    . MG  F 4 .   ? 148.333 146.934 132.983 1.00 24.14 ?  802 MG  A MG    1 
HETATM 15887 P  PG    . ATP G 5 .   ? 109.475 134.845 77.200  1.00 73.57 ?  803 ATP A PG    1 
HETATM 15888 O  O1G   . ATP G 5 .   ? 109.947 135.779 76.137  1.00 63.77 ?  803 ATP A O1G   1 
HETATM 15889 O  O2G   . ATP G 5 .   ? 108.966 133.505 76.659  1.00 64.13 -1 803 ATP A O2G   1 
HETATM 15890 O  O3G   . ATP G 5 .   ? 110.515 134.582 78.293  1.00 61.47 ?  803 ATP A O3G   1 
HETATM 15891 P  PB    . ATP G 5 .   ? 107.895 136.255 79.320  1.00 71.75 ?  803 ATP A PB    1 
HETATM 15892 O  O1B   . ATP G 5 .   ? 108.692 137.492 79.439  1.00 63.94 -1 803 ATP A O1B   1 
HETATM 15893 O  O2B   . ATP G 5 .   ? 106.379 136.447 79.377  1.00 62.90 ?  803 ATP A O2B   1 
HETATM 15894 O  O3B   . ATP G 5 .   ? 108.223 135.467 77.978  1.00 66.82 ?  803 ATP A O3B   1 
HETATM 15895 P  PA    . ATP G 5 .   ? 107.528 134.072 81.291  1.00 70.68 ?  803 ATP A PA    1 
HETATM 15896 O  O1A   . ATP G 5 .   ? 108.187 132.755 81.174  1.00 64.00 -1 803 ATP A O1A   1 
HETATM 15897 O  O2A   . ATP G 5 .   ? 106.060 134.090 80.868  1.00 62.49 ?  803 ATP A O2A   1 
HETATM 15898 O  O3A   . ATP G 5 .   ? 108.282 135.184 80.433  1.00 63.22 ?  803 ATP A O3A   1 
HETATM 15899 O  "O5'" . ATP G 5 .   ? 107.627 134.642 82.760  1.00 62.47 ?  803 ATP A "O5'" 1 
HETATM 15900 C  "C5'" . ATP G 5 .   ? 106.732 135.677 83.221  1.00 61.67 ?  803 ATP A "C5'" 1 
HETATM 15901 C  "C4'" . ATP G 5 .   ? 107.424 136.480 84.293  1.00 61.88 ?  803 ATP A "C4'" 1 
HETATM 15902 O  "O4'" . ATP G 5 .   ? 107.908 135.594 85.325  1.00 63.84 ?  803 ATP A "O4'" 1 
HETATM 15903 C  "C3'" . ATP G 5 .   ? 108.647 137.262 83.833  1.00 60.84 ?  803 ATP A "C3'" 1 
HETATM 15904 O  "O3'" . ATP G 5 .   ? 108.277 138.541 83.329  1.00 63.01 ?  803 ATP A "O3'" 1 
HETATM 15905 C  "C2'" . ATP G 5 .   ? 109.460 137.381 85.122  1.00 62.28 ?  803 ATP A "C2'" 1 
HETATM 15906 O  "O2'" . ATP G 5 .   ? 109.000 138.454 85.936  1.00 61.13 ?  803 ATP A "O2'" 1 
HETATM 15907 C  "C1'" . ATP G 5 .   ? 109.172 136.035 85.795  1.00 61.93 ?  803 ATP A "C1'" 1 
HETATM 15908 N  N9    . ATP G 5 .   ? 110.158 135.000 85.508  1.00 60.22 ?  803 ATP A N9    1 
HETATM 15909 C  C8    . ATP G 5 .   ? 109.934 133.788 84.908  1.00 60.42 ?  803 ATP A C8    1 
HETATM 15910 N  N7    . ATP G 5 .   ? 111.009 133.050 84.775  1.00 60.85 ?  803 ATP A N7    1 
HETATM 15911 C  C5    . ATP G 5 .   ? 112.012 133.829 85.329  1.00 61.63 ?  803 ATP A C5    1 
HETATM 15912 C  C6    . ATP G 5 .   ? 113.394 133.618 85.502  1.00 58.03 ?  803 ATP A C6    1 
HETATM 15913 N  N6    . ATP G 5 .   ? 114.033 132.510 85.115  1.00 57.72 ?  803 ATP A N6    1 
HETATM 15914 N  N1    . ATP G 5 .   ? 114.109 134.599 86.095  1.00 58.44 ?  803 ATP A N1    1 
HETATM 15915 C  C2    . ATP G 5 .   ? 113.480 135.712 86.479  1.00 58.37 ?  803 ATP A C2    1 
HETATM 15916 N  N3    . ATP G 5 .   ? 112.187 136.020 86.374  1.00 61.94 ?  803 ATP A N3    1 
HETATM 15917 C  C4    . ATP G 5 .   ? 111.502 135.034 85.786  1.00 62.47 ?  803 ATP A C4    1 
HETATM 15918 O  O1B   . DGI H 6 .   ? 105.323 151.767 83.368  1.00 65.79 ?  804 DGI A O1B   1 
HETATM 15919 P  PB    . DGI H 6 .   ? 105.430 153.232 83.728  1.00 74.95 ?  804 DGI A PB    1 
HETATM 15920 O  O2B   . DGI H 6 .   ? 104.093 153.944 83.714  1.00 66.56 -1 804 DGI A O2B   1 
HETATM 15921 O  O3B   . DGI H 6 .   ? 106.491 153.962 82.932  1.00 66.82 ?  804 DGI A O3B   1 
HETATM 15922 O  O3A   . DGI H 6 .   ? 105.932 153.211 85.275  1.00 67.64 ?  804 DGI A O3A   1 
HETATM 15923 P  PA    . DGI H 6 .   ? 105.822 152.346 86.617  1.00 72.66 ?  804 DGI A PA    1 
HETATM 15924 O  O1A   . DGI H 6 .   ? 105.935 153.246 87.783  1.00 65.42 -1 804 DGI A O1A   1 
HETATM 15925 O  O2A   . DGI H 6 .   ? 104.651 151.443 86.511  1.00 66.08 ?  804 DGI A O2A   1 
HETATM 15926 O  "O5'" . DGI H 6 .   ? 107.161 151.481 86.539  1.00 64.30 ?  804 DGI A "O5'" 1 
HETATM 15927 C  "C5'" . DGI H 6 .   ? 108.422 152.132 86.283  1.00 63.95 ?  804 DGI A "C5'" 1 
HETATM 15928 C  "C4'" . DGI H 6 .   ? 109.543 151.162 86.555  1.00 63.55 ?  804 DGI A "C4'" 1 
HETATM 15929 O  "O4'" . DGI H 6 .   ? 109.462 150.698 87.922  1.00 62.06 ?  804 DGI A "O4'" 1 
HETATM 15930 C  "C3'" . DGI H 6 .   ? 109.548 149.913 85.667  1.00 64.87 ?  804 DGI A "C3'" 1 
HETATM 15931 O  "O3'" . DGI H 6 .   ? 110.859 149.672 85.156  1.00 62.86 ?  804 DGI A "O3'" 1 
HETATM 15932 C  "C2'" . DGI H 6 .   ? 109.127 148.797 86.615  1.00 62.93 ?  804 DGI A "C2'" 1 
HETATM 15933 C  "C1'" . DGI H 6 .   ? 109.641 149.298 87.950  1.00 59.66 ?  804 DGI A "C1'" 1 
HETATM 15934 N  N9    . DGI H 6 .   ? 108.915 148.764 89.118  1.00 62.34 ?  804 DGI A N9    1 
HETATM 15935 C  C8    . DGI H 6 .   ? 109.451 148.121 90.201  1.00 63.25 ?  804 DGI A C8    1 
HETATM 15936 N  N7    . DGI H 6 .   ? 108.552 147.745 91.078  1.00 62.94 ?  804 DGI A N7    1 
HETATM 15937 C  C5    . DGI H 6 .   ? 107.349 148.167 90.539  1.00 64.85 ?  804 DGI A C5    1 
HETATM 15938 C  C4    . DGI H 6 .   ? 107.556 148.798 89.331  1.00 64.28 ?  804 DGI A C4    1 
HETATM 15939 N  N3    . DGI H 6 .   ? 106.641 149.345 88.510  1.00 64.32 ?  804 DGI A N3    1 
HETATM 15940 C  C2    . DGI H 6 .   ? 105.401 149.231 88.977  1.00 62.71 ?  804 DGI A C2    1 
HETATM 15941 N  N2    . DGI H 6 .   ? 104.381 149.729 88.273  1.00 63.01 ?  804 DGI A N2    1 
HETATM 15942 N  N1    . DGI H 6 .   ? 105.095 148.622 90.163  1.00 63.42 ?  804 DGI A N1    1 
HETATM 15943 C  C6    . DGI H 6 .   ? 106.012 148.052 91.025  1.00 64.23 ?  804 DGI A C6    1 
HETATM 15944 O  O6    . DGI H 6 .   ? 105.643 147.522 92.073  1.00 64.17 ?  804 DGI A O6    1 
HETATM 15945 P  PA    . TTP I 3 .   ? 119.777 147.315 123.733 1.00 22.87 ?  801 TTP B PA    1 
HETATM 15946 O  O1A   . TTP I 3 .   ? 121.147 146.851 123.313 1.00 21.90 -1 801 TTP B O1A   1 
HETATM 15947 O  O2A   . TTP I 3 .   ? 119.839 148.700 124.324 1.00 27.07 ?  801 TTP B O2A   1 
HETATM 15948 O  O3A   . TTP I 3 .   ? 118.738 147.274 122.506 1.00 36.80 ?  801 TTP B O3A   1 
HETATM 15949 P  PB    . TTP I 3 .   ? 118.706 148.407 121.366 1.00 32.44 ?  801 TTP B PB    1 
HETATM 15950 O  O1B   . TTP I 3 .   ? 119.550 148.004 120.186 1.00 35.04 -1 801 TTP B O1B   1 
HETATM 15951 O  O2B   . TTP I 3 .   ? 119.135 149.753 121.888 1.00 28.12 ?  801 TTP B O2B   1 
HETATM 15952 O  O3B   . TTP I 3 .   ? 117.150 148.423 120.970 1.00 37.21 ?  801 TTP B O3B   1 
HETATM 15953 P  PG    . TTP I 3 .   ? 116.034 148.655 122.106 1.00 30.08 ?  801 TTP B PG    1 
HETATM 15954 O  O1G   . TTP I 3 .   ? 115.563 147.313 122.603 1.00 20.36 ?  801 TTP B O1G   1 
HETATM 15955 O  O2G   . TTP I 3 .   ? 114.855 149.399 121.533 1.00 33.83 -1 801 TTP B O2G   1 
HETATM 15956 O  O3G   . TTP I 3 .   ? 116.625 149.437 123.254 1.00 27.09 ?  801 TTP B O3G   1 
HETATM 15957 O  "O5'" . TTP I 3 .   ? 119.109 146.285 124.768 1.00 24.10 ?  801 TTP B "O5'" 1 
HETATM 15958 C  "C5'" . TTP I 3 .   ? 118.374 145.169 124.276 1.00 22.09 ?  801 TTP B "C5'" 1 
HETATM 15959 C  "C4'" . TTP I 3 .   ? 118.263 144.117 125.366 1.00 23.21 ?  801 TTP B "C4'" 1 
HETATM 15960 O  "O4'" . TTP I 3 .   ? 118.346 142.836 124.746 1.00 35.77 ?  801 TTP B "O4'" 1 
HETATM 15961 C  "C3'" . TTP I 3 .   ? 119.411 144.235 126.349 1.00 25.49 ?  801 TTP B "C3'" 1 
HETATM 15962 O  "O3'" . TTP I 3 .   ? 118.907 144.335 127.681 1.00 27.76 ?  801 TTP B "O3'" 1 
HETATM 15963 C  "C2'" . TTP I 3 .   ? 120.222 142.966 126.208 1.00 25.02 ?  801 TTP B "C2'" 1 
HETATM 15964 C  "C1'" . TTP I 3 .   ? 119.437 142.072 125.261 1.00 28.60 ?  801 TTP B "C1'" 1 
HETATM 15965 N  N1    . TTP I 3 .   ? 120.285 141.639 124.153 1.00 27.06 ?  801 TTP B N1    1 
HETATM 15966 C  C2    . TTP I 3 .   ? 120.428 140.261 123.877 1.00 29.68 ?  801 TTP B C2    1 
HETATM 15967 O  O2    . TTP I 3 .   ? 119.827 139.429 124.588 1.00 27.86 ?  801 TTP B O2    1 
HETATM 15968 N  N3    . TTP I 3 .   ? 121.195 139.829 122.869 1.00 27.67 ?  801 TTP B N3    1 
HETATM 15969 C  C4    . TTP I 3 .   ? 121.849 140.697 122.095 1.00 32.29 ?  801 TTP B C4    1 
HETATM 15970 O  O4    . TTP I 3 .   ? 122.564 140.293 121.155 1.00 35.26 ?  801 TTP B O4    1 
HETATM 15971 C  C5    . TTP I 3 .   ? 121.714 142.148 122.364 1.00 27.29 ?  801 TTP B C5    1 
HETATM 15972 C  C5M   . TTP I 3 .   ? 122.433 143.159 121.514 1.00 27.10 ?  801 TTP B C5M   1 
HETATM 15973 C  C6    . TTP I 3 .   ? 120.912 142.558 123.414 1.00 25.61 ?  801 TTP B C6    1 
HETATM 15974 MG MG    . MG  J 4 .   ? 118.014 150.125 124.677 1.00 27.32 ?  802 MG  B MG    1 
HETATM 15975 P  PG    . ATP K 5 .   ? 154.762 137.777 179.174 1.00 78.28 ?  803 ATP B PG    1 
HETATM 15976 O  O1G   . ATP K 5 .   ? 154.528 138.248 180.569 1.00 64.48 ?  803 ATP B O1G   1 
HETATM 15977 O  O2G   . ATP K 5 .   ? 153.480 137.650 178.345 1.00 66.98 -1 803 ATP B O2G   1 
HETATM 15978 O  O3G   . ATP K 5 .   ? 155.776 138.624 178.399 1.00 64.37 ?  803 ATP B O3G   1 
HETATM 15979 P  PB    . ATP K 5 .   ? 156.742 135.563 179.540 1.00 74.62 ?  803 ATP B PB    1 
HETATM 15980 O  O1B   . ATP K 5 .   ? 157.885 136.093 178.770 1.00 63.94 -1 803 ATP B O1B   1 
HETATM 15981 O  O2B   . ATP K 5 .   ? 156.885 135.608 181.061 1.00 65.48 ?  803 ATP B O2B   1 
HETATM 15982 O  O3B   . ATP K 5 .   ? 155.386 136.307 179.175 1.00 67.90 ?  803 ATP B O3B   1 
HETATM 15983 P  PA    . ATP K 5 .   ? 155.663 133.317 177.947 1.00 74.99 ?  803 ATP B PA    1 
HETATM 15984 O  O1A   . ATP K 5 .   ? 154.312 132.874 178.348 1.00 65.28 -1 803 ATP B O1A   1 
HETATM 15985 O  O2A   . ATP K 5 .   ? 156.594 132.205 177.467 1.00 66.62 ?  803 ATP B O2A   1 
HETATM 15986 O  O3A   . ATP K 5 .   ? 156.403 134.061 179.141 1.00 66.93 ?  803 ATP B O3A   1 
HETATM 15987 O  "O5'" . ATP K 5 .   ? 155.595 134.425 176.826 1.00 63.34 ?  803 ATP B "O5'" 1 
HETATM 15988 C  "C5'" . ATP K 5 .   ? 156.646 134.567 175.848 1.00 62.23 ?  803 ATP B "C5'" 1 
HETATM 15989 C  "C4'" . ATP K 5 .   ? 156.174 135.488 174.753 1.00 64.37 ?  803 ATP B "C4'" 1 
HETATM 15990 O  "O4'" . ATP K 5 .   ? 155.428 134.733 173.774 1.00 66.78 ?  803 ATP B "O4'" 1 
HETATM 15991 C  "C3'" . ATP K 5 .   ? 155.231 136.600 175.200 1.00 61.93 ?  803 ATP B "C3'" 1 
HETATM 15992 O  "O3'" . ATP K 5 .   ? 155.958 137.741 175.636 1.00 65.20 ?  803 ATP B "O3'" 1 
HETATM 15993 C  "C2'" . ATP K 5 .   ? 154.444 136.891 173.922 1.00 61.89 ?  803 ATP B "C2'" 1 
HETATM 15994 O  "O2'" . ATP K 5 .   ? 155.153 137.764 173.052 1.00 64.23 ?  803 ATP B "O2'" 1 
HETATM 15995 C  "C1'" . ATP K 5 .   ? 154.329 135.495 173.301 1.00 63.64 ?  803 ATP B "C1'" 1 
HETATM 15996 N  N9    . ATP K 5 .   ? 153.098 134.788 173.638 1.00 61.39 ?  803 ATP B N9    1 
HETATM 15997 C  C8    . ATP K 5 .   ? 152.978 133.611 174.331 1.00 60.31 ?  803 ATP B C8    1 
HETATM 15998 N  N7    . ATP K 5 .   ? 151.742 133.203 174.485 1.00 61.85 ?  803 ATP B N7    1 
HETATM 15999 C  C5    . ATP K 5 .   ? 150.993 134.179 173.845 1.00 64.90 ?  803 ATP B C5    1 
HETATM 16000 C  C6    . ATP K 5 .   ? 149.608 134.338 173.648 1.00 60.15 ?  803 ATP B C6    1 
HETATM 16001 N  N6    . ATP K 5 .   ? 148.688 133.478 174.096 1.00 59.38 ?  803 ATP B N6    1 
HETATM 16002 N  N1    . ATP K 5 .   ? 149.191 135.426 172.966 1.00 59.56 ?  803 ATP B N1    1 
HETATM 16003 C  C2    . ATP K 5 .   ? 150.103 136.293 172.519 1.00 58.45 ?  803 ATP B C2    1 
HETATM 16004 N  N3    . ATP K 5 .   ? 151.431 136.248 172.641 1.00 61.55 ?  803 ATP B N3    1 
HETATM 16005 C  C4    . ATP K 5 .   ? 151.815 135.162 173.319 1.00 64.32 ?  803 ATP B C4    1 
HETATM 16006 O  O1B   . DGI L 6 .   ? 162.155 153.025 173.651 1.00 62.73 -1 804 DGI B O1B   1 
HETATM 16007 P  PB    . DGI L 6 .   ? 162.402 151.559 173.357 1.00 78.16 ?  804 DGI B PB    1 
HETATM 16008 O  O2B   . DGI L 6 .   ? 163.850 151.252 173.049 1.00 66.34 ?  804 DGI B O2B   1 
HETATM 16009 O  O3B   . DGI L 6 .   ? 161.813 150.643 174.409 1.00 63.38 ?  804 DGI B O3B   1 
HETATM 16010 O  O3A   . DGI L 6 .   ? 161.632 151.223 171.962 1.00 65.58 ?  804 DGI B O3A   1 
HETATM 16011 P  PA    . DGI L 6 .   ? 161.675 150.218 170.719 1.00 72.25 ?  804 DGI B PA    1 
HETATM 16012 O  O1A   . DGI L 6 .   ? 162.541 149.067 171.066 1.00 65.11 ?  804 DGI B O1A   1 
HETATM 16013 O  O2A   . DGI L 6 .   ? 161.955 150.987 169.489 1.00 63.88 -1 804 DGI B O2A   1 
HETATM 16014 O  "O5'" . DGI L 6 .   ? 160.155 149.734 170.654 1.00 64.69 ?  804 DGI B "O5'" 1 
HETATM 16015 C  "C5'" . DGI L 6 .   ? 159.092 150.707 170.706 1.00 61.37 ?  804 DGI B "C5'" 1 
HETATM 16016 C  "C4'" . DGI L 6 .   ? 157.767 150.002 170.552 1.00 62.25 ?  804 DGI B "C4'" 1 
HETATM 16017 O  "O4'" . DGI L 6 .   ? 157.723 149.326 169.275 1.00 62.79 ?  804 DGI B "O4'" 1 
HETATM 16018 C  "C3'" . DGI L 6 .   ? 157.465 148.947 171.621 1.00 63.26 ?  804 DGI B "C3'" 1 
HETATM 16019 O  "O3'" . DGI L 6 .   ? 156.144 149.124 172.135 1.00 62.44 ?  804 DGI B "O3'" 1 
HETATM 16020 C  "C2'" . DGI L 6 .   ? 157.577 147.627 170.865 1.00 58.79 ?  804 DGI B "C2'" 1 
HETATM 16021 C  "C1'" . DGI L 6 .   ? 157.196 148.029 169.454 1.00 58.08 ?  804 DGI B "C1'" 1 
HETATM 16022 N  N9    . DGI L 6 .   ? 157.752 147.157 168.400 1.00 59.64 ?  804 DGI B N9    1 
HETATM 16023 C  C8    . DGI L 6 .   ? 157.061 146.541 167.392 1.00 62.54 ?  804 DGI B C8    1 
HETATM 16024 N  N7    . DGI L 6 .   ? 157.825 145.823 166.603 1.00 61.46 ?  804 DGI B N7    1 
HETATM 16025 C  C5    . DGI L 6 .   ? 159.098 145.976 167.126 1.00 64.08 ?  804 DGI B C5    1 
HETATM 16026 C  C4    . DGI L 6 .   ? 159.069 146.796 168.233 1.00 62.76 ?  804 DGI B C4    1 
HETATM 16027 N  N3    . DGI L 6 .   ? 160.099 147.179 169.011 1.00 63.02 ?  804 DGI B N3    1 
HETATM 16028 C  C2    . DGI L 6 .   ? 161.262 146.668 168.611 1.00 61.32 ?  804 DGI B C2    1 
HETATM 16029 N  N2    . DGI L 6 .   ? 162.376 146.955 169.289 1.00 62.38 ?  804 DGI B N2    1 
HETATM 16030 N  N1    . DGI L 6 .   ? 161.389 145.846 167.525 1.00 60.59 ?  804 DGI B N1    1 
HETATM 16031 C  C6    . DGI L 6 .   ? 160.353 145.437 166.709 1.00 62.82 ?  804 DGI B C6    1 
HETATM 16032 O  O6    . DGI L 6 .   ? 160.563 144.695 165.750 1.00 61.55 ?  804 DGI B O6    1 
HETATM 16033 MN MN    . MN  M 7 .   ? 119.486 85.332  129.420 0.85 25.05 ?  401 MN  C MN    1 
HETATM 16034 MN MN    . MN  N 7 .   ? 117.466 88.283  130.501 0.85 26.37 ?  402 MN  C MN    1 
HETATM 16035 MN MN    . MN  O 7 .   ? 138.592 98.040  136.835 1.00 22.51 ?  401 MN  D MN    1 
HETATM 16036 MN MN    . MN  P 7 .   ? 140.252 96.914  133.477 1.00 24.72 ?  402 MN  D MN    1 
# 
